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Human Metabolome Database Version 2.5

 

Showing metabocard for PI(16:0/16:0) (HMDB09778)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2008-09-12 02:59:36
Update Date 2009-05-05 21:05:43
Accession Number HMDB09778
Secondary Accession Numbers Not Available
Common Name PI(16:0/16:0)
Description PI(16:0/16:0) is a phosphatidylinositol. Phosphatidylinositols are important lipids, both as a key membrane constituent and as a participant in essential metabolic processes, both directly and via a number of metabolites. Phosphatidylinositols are acidic (anionic) phospholipids that consist of a phosphatidic acid backbone, linked via the phosphate group to inositol (hexahydroxycyclohexane). Phosphatidylinositols can have many different combinations of fatty acids of varying lengths and saturation attached at the C-1 and C-2 positions. Fatty acids containing 18 and 20 carbons are the most common. PI(16:0/16:0), in particular, consists of one chain of palmitic acid at the C-1 position and one chain of palmitic acid at the C-2 position. The palmitic acid moiety is derived from fish oils, milk fats, vegetable oils and animal fats, while the palmitic acid moiety is derived from fish oils, milk fats, vegetable oils and animal fats. In most organisms, the stereochemical form of the last is myo-D-inositol (with one axial hydroxyl in position 2 with the remainder equatorial. Phosphatidylinositol is especially abundant in brain tissue, where it can amount to 10% of the phospholipids, but it is present in all tissues and cell types. There is usually less of it than of phosphatidylcholine, phosphatidylethanolamine and phosphatidylserine. In animal tissues, phosphatidylinositol is the primary source of the arachidonic acid required for biosynthesis of eicosanoids, including prostaglandins, via the action of the enzyme phospholipase A2. Phosphatidylinositol can be phosphorylated by a number of different kinases that place the phosphate moiety on positions 4 and 5 of the inositol ring, although position 3 can also be phosphorylated by a specific kinase. Seven different isomers are known, but the most important in both quantitative and biological terms are phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate. Phosphatidylinositol and the phosphatidylinositol phosphates are the main source of diacylglycerols that serve as signaling molecules, via the action of phospholipase C enzymes. While most phospholipids have a saturated fatty acid on C-1 and an unsaturated fatty acid on C-2 of the glycerol backbone, the fatty acid distribution at the C-1 and C-2 positions of glycerol within phospholipids is continually in flux, owing to phospholipid degradation and the continuous phospholipid remodeling that occurs while these molecules are in membranes. PIs contain almost exclusively stearic acid at carbon 1 and arachidonic acid at carbon 2. PIs composed exclusively of non-phosphorylated inositol exhibit a net charge of -1 at physiological pH. Molecules with phosphorylated inositol (such as PIP, PIP2, PIP3, etc.) are termed polyphosphoinositides. The polyphosphoinositides are important intracellular transducers of signals emanating from the plasma membrane. The synthesis of PI involves CDP-activated 1,2-diacylglycerol condensation with myo-inositol.
Synonyms
  1. Phosphatidylinositol(32:0)
  2. PIno(16:0/16:0)
  3. PIno(32:0)
  4. 1,2-dipalmitoyl-rac-glycero-3-phosphoinositol
  5. Phosphatidylinositol(16:0/16:0)
  6. PI(32:0)
  7. 1,2-dihexadecanoyl-rac-glycero-3-phospho-(1'-myo-inositol)
  8. PI(16:0/16:0)
Chemical IUPAC Name 1,2-dihexadecanoyl-rac-glycero-3-phosphoinositol
Chemical Formula C41H79O13P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Lipids
Class
  • Phospholipids
Sub Class
  • Phosphatidylinositols
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • carboxylic acid ester
  • phosphoric acid ester
Biofunction
  • Membrane component
  • Energy source
  • Cell signaling
Application
—
Source
  • Endogenous
Average Molecular Weight 811.032
Monoisotopic Molecular Weight 810.525818
Isomeric SMILES CCCCCCCCCCCCCCCC(=O)OC[C@H](COP(O)(=O)O[C@H]1C(O)C(O)C(O)[C@@H](O)C1O)OC(=O)CCCCCCCCCCCCCCC
Canonical SMILES CCCCCCCCCCCCCCCC(=O)OCC(COP(O)(=O)OC1C(O)C(O)C(O)C(O)C1O)OC(=O)CCCCCCCCCCCCCCC
KEGG Compound ID C00626 Link Image
BioCyc ID Phosphatidylinositols Link Image
BiGG ID Not Available
Wikipedia Link Lecithin Link Image
NuGOwiki Link HMDB09778 Link Image
Metagene Link HMDB09778 Link Image
METLIN ID Not Available
PubChem Compound Not Available
PubChem Substance Not Available
ChEBI ID Not Available
CAS Registry Number Not Available
InChI Identifier InChI=1/C41H79O13P/c1-3-5-7-9-11-13-15-17-19-21-23-25-27-29-34(42)51-31-33(32-52-55(49,50)54-41-39(47)37(45)36(44)38(46)40(41)48)53-35(43)30-28-26-24-22-20-18-16-14-12-10-8-6-4-2/h33,36-41,44-48H,3-32H2,1-2H3,(H,49,50)/t33-,36?,37-,38?,39-,40?,41-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.40e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 6.79 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Not Available
Not Available
Predicted 13C NMR Spectrum Not Available
Not Available
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane
Biofluid Location Not Available
Tissue Location
Tissue References
All Tissues —
Brain —
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Phospholipid Biosynthesis SMP00025 Link Image map00564 Link Image
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 1
  2. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 4
  3. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 2
  4. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 3
  5. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma 2
  6. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma 1
  7. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta 1
  8. N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
  9. Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
  10. Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
  11. Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
  12. Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
  13. Probable phospholipid-transporting ATPase IG
  14. Probable phospholipid-transporting ATPase IH
  15. Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta isoform
  16. Probable phospholipid-transporting ATPase VA
  17. Probable phospholipid-transporting ATPase IC
  18. Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform
  19. Probable phospholipid-transporting ATPase IIA
  20. Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
  21. Probable phospholipid-transporting ATPase VD
  22. Probable phospholipid-transporting ATPase IB
  23. Probable phospholipid-transporting ATPase IA
  24. Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
  25. Probable phospholipid-transporting ATPase IM
  26. Probable phospholipid-transporting ATPase IF
  27. Probable phospholipid-transporting ATPase IK
  28. Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual- specificity protein phosphatase PTEN
  29. Phosphatidylinositol transfer protein beta isoform
  30. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta 2
  31. Phospholipid scramblase 1
  32. Phosphatidylserine synthase 1
  33. Phosphatidylserine decarboxylase proenzyme
  34. Phosphatidylinositol transfer protein alpha isoform
  35. Phospholipid transfer protein precursor
  36. GPI mannosyltransferase 1
  37. Phosphatidylserine synthase 2
  38. Phosphatidylinositol-glycan biosynthesis class W protein
  39. Phosphatidylinositol-glycan biosynthesis class X protein precursor
  40. GPI mannosyltransferase 4
  41. Inositol polyphosphate 5-phosphatase
  42. Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1
  43. Phosphatidylinositol 3-kinase catalytic subunit type 3
  44. Phosphatidylinositol-specific phospholipase C X domain-containing protein 2
  45. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
  46. Phospholipase C eta 1
  47. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1
  48. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
  49. Phospholipid scramblase 2
  50. Phospholipid scramblase 3
  51. Phospholipid scramblase 4
  52. Phospholipid scramblase family memmber 5
  53. Probable phospholipid-transporting ATPase VB
  54. Probable phospholipid-transporting ATPase ID
  55. Phospholipase A1 member A precursor
  56. Serum deprivation-response protein
  57. GPI mannosyltransferase 3
  58. Phosphatidylinositol-glycan biosynthesis class F protein
  59. GPI ethanolamine phosphate transferase 2
  60. GPI ethanolamine phosphate transferase 1
  61. GPI ethanolamine phosphate transferase 3
  62. GPI transamidase component PIG-S
  63. GPI transamidase component PIG-T precursor
  64. Phosphatidylinositol glycan anchor biosynthesis class U protein
  65. GPI mannosyltransferase 2
  66. Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
  67. Cytoplasmic phosphatidylinositol transfer protein 1
  68. Membrane-associated phosphatidylinositol transfer protein 1
  69. Membrane-associated phosphatidylinositol transfer protein 2
  70. Membrane-associated phosphatidylinositol transfer protein 3
  71. Pleckstrin homology domain-containing family A member 8
  72. Phosphatidylinositol-specific phospholipase C X domain-containing protein 1
  73. Phosphatidylinositol-specific phospholipase C X domain-containing protein 3
  74. Phospholipase C zeta 1
  75. Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
  76. Transmembrane protein 55A
  77. Transmembrane protein 55B
  78. Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase TPTE2
  79. Centaurin-beta-1
  80. 130 kDa phosphatidylinositol 4,5-biphosphate-dependent ARF1 GTPase-activating protein
Enzyme 1 [top]
Enzyme 1 ID 5454
Enzyme 1 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 1
Enzyme 1 Synonyms
  1. Phosphoinositide phospholipase C
  2. Phospholipase C- beta-1
  3. PLC-beta-1
  4. PLC-I
  5. PLC-154
Enzyme 1 Gene Name PLCB1
Enzyme 1 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 1 
MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKE
TELLDLSLVKDARCGRHAKAPKDPKLRELLDVGNIGRLEQRMITVVYGPDLVNISHLNLV
AFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSA
DRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYL
TVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLARKGQISVDGFMRYLS
GEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCV
ELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQ
QAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKK
KLSEQASNTYSDSSSMFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEM
SNLVNYIQPVKFESFEISKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPK
GTRVDSSNYMPQLFWNAGCQMVALNFQTMDLAMQINMGMYEYNGKSGYRLKPEFMRRPDK
HFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQG
NAVNPVWEEEPIVFKKVVLPTLACLRIAVYEEGGKFIGHRILPVQAIRPGYHYICLRNER
NQPLTLPAVFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKK
EADPGETPSEAPSEARTTPAENGVNHTTTLTPKPPSQALHSQPAPGSVKAPAKTEDLIQS
VLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTTKYNEIQNDYL
RRRAALEKSAKKDSKKKSEPSSPDHGSSTIEQDLAALDAEMTQKLIDLKDKQQQQLLNLR
QEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKI
TEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHKEIRQQILDEKP
KLQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPLSLSSDPGKVNHKTPSS
EELGGDIPGKEFDTPL
Enzyme 1 Number of Residues 1216
Enzyme 1 Molecular Weight 138568
Enzyme 1 Theoretical pI 6.12
Enzyme 1 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 1 General Function Cell cycle control, cell division, chromosome partitioning
Enzyme 1 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 9368448 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9NQ66 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PLCB1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >3651 bp 
ATGGCCGGGGCTCAACCCGGAGTGCACGCCTTGCAACTCAAGCCCGTGTGCGTGTCCGAC
AGCCTCAAGAAGGGCACCAAATTCGTCAAGTGGGATGATGATTCAACTATTGTTACTCCA
ATTATTTTGAGGACTGACCCTCAGGGATTTTTCTTTTACTGGACAGATCAAAACAAGGAG
ACAGAGCTACTGGATCTCAGCCTTGTCAAAGATGCCAGATGTGGGAGACACGCCAAAGCT
CCCAAGGACCCCAAATTACGTGAACTTTTGGATGTGGGGAACATCGGGCGCCTGGAGCAG
CGCATGATCACAGTGGTGTATGGGCCTGACCTCGTGAACATCTCCCATTTGAATCTCGTG
GCTTTCCAAGAAGAAGTGGCCAAGGAATGGACAAATGAGGTTTTCAGTTTGGCAACAAAC
CTGCTGGCCCAAAACATGTCCAGGGATGCATTTCTGGAAAAAGCCTATACTAAACTTAAG
CTGCAAGTCACTCCAGAAGGGCGTATTCCTCTCAAAAACATATATCGCTTGTTTTCAGCA
GATCGGAAGCGAGTTGAAACTGCTTTAGAGGCTTGTAGTCTTCCATCTTCAAGGAATGAT
TCAATACCTCAAGAAGATTTCACTCCAGAAGTGTACAGAGTTTTCCTCAACAACCTTTGC
CCTCGACCTGAAATTGATAACATCTTTTCAGAATTTGGTGCAAAAAGCAAACCATATCTT
ACCGTTGATCAGATGATGGATTTTATCAACCTTAAGCAGCGAGATCCTCGGCTTAATGAA
ATACTTTATCCACCTCTAAAACAAGAGCAAGTCCAAGTATTGATTGAGAAGTATGAACCC
AACAACAGCCTCGCCAGAAAAGGACAAATATCAGTGGATGGGTTCATGCGCTATCTGAGT
GGAGAAGAAAACGGAGTCGTTTCACCTGAGAAACTGGATTTGAATGAAGACATGTCTCAG
CCCCTTTCTCACTATTTCATTAATTCCTCGCACAACACCTACCTCACAGCTGGCCAACTG
GCTGGAAACTCCTCTGTTGAGATGTATCGCCAAGTGCTCCTGTCTGGTTGTCGCTGTGTG
GAGCTGGACTGCTGGAAGGGACGGACTGCAGAAGAGGAACCTGTCATCACCCATGGCTTC
ACCATGACAACTGAAATATCTTTCAAGGAAGTGATAGAAGCAATTGCGGAGTGTGCATTT
AAGACTTCACCTTTTCCAATTCTCCTTTCGTTTGAGAACCATGTGGATTCCCCAAAGCAG
CAAGCCAAGATGGCGGAGTACTGCCGACTGATCTTTGGGGATGCCCTTCTCATGGAGCCC
CTGGAAAAATATCCACTGGAATCTGGAGTTCCTCTTCCAAGCCCTATGGATTTAATGTAT
AAAATTTTGGTGAAAAATAAGAAGAAATCACACAAGTCATCAGAAGGAAGCGGCAAAAAG
AAGCTCTCAGAACAAGCCTCCAACACCTACAGTGACTCCTCCAGCATGTTCGAGCCCTCA
TCCCCAGGAGCCGGAGAAGCTGATACGGAAAGTGACGACGACGATGATGATGATGACTGT
AAAAAATCTTCAATGGATGAGGGGACTGCTGGAAGTGAGGCTATGGCCACAGAAGAAATG
TCTAATCTGGTGAACTATATTCAGCCAGTCAAGTTTGAGTCATTTGAAATTTCAAAAAAA
AGAAATAAAAGTTTTGAAATGTCTTCCTTCGTGGAAACCAAAGGACTTGAACAACTCACC
AAGTCTCCAGTGGAATTTGTAGAATATAACAAAATGCAGCTTAGCAGGATATATCCAAAA
GGAACACGTGTGGATTCATCCAACTATATGCCTCAGCTCTTCTGGAATGCAGGTTGTCAG
ATGGTGGCACTTAATTTCCAGACAATGGACCTGGCTATGCAAATAAATATGGGGATGTAT
GAATACAACGGGAAGAGTGGCTACAGATTGAAGCCAGAGTTCATGAGGAGGCCTGACAAG
CATTTTGATCCATTTACTGAAGGCATCGTAGATGGGATAGTGGCAAACACTTTGTCTGTT
AAGATTATTTCAGGTCAGTTTCTTTCTGATAAGAAAGTTGGGACTTACGTGGAAGTAGAT
ATGTTTGGTTTGCCTGTGGATACAAGGAGGAAGGCATTTAAGACCAAAACATCCCAAGGA
AATGCTGTGAATCCTGTCTGGGAAGAAGAACCTATTGTGTTCAAAAAGGTGGTTCTTCCT
ACTCTGGCCTGTTTGAGAATAGCAGTTTATGAAGAAGGAGGTAAATTCATTGGCCACCGT
ATCTTGCCAGTGCAAGCCATTCGGCCAGGCTATCACTATATCTGTCTAAGGAATGAAAGG
AACCAGCCTCTGACGCTGCCTGCTGTCTTTGTCTACATAGAAGTGAAAGACTATGTGCCA
GACACATATGCAGATGTCATCGAAGCTTTATCAAACCCAATCCGATATGTGAACCTGATG
GAACAGAGAGCTAAGCAATTGGCTGCTTTGACACTGGAAGATGAAGAAGAAGTAAAGAAA
GAGGCTGATCCTGGAGAAACACCATCAGAGGCTCCAAGTGAAGCGAGAACGACTCCAGCA
GAAAATGGGGTGAATCACACTACAACCCTGACACCCAAGCCACCCTCCCAGGCTCTCCAC
AGCCAGCCAGCTCCAGGTTCTGTAAAGGCACCTGCCAAAACAGAAGATCTTATTCAGAGT
GTCTTAACAGAAGTGGAAGCACAGACCATCGAAGAACTAAAGCAACAGAAATCGTTTGTG
AAACTTCAAAAGAAACACTACAAAGAAATGAAAGACCTGGTTAAGAGACACCACAAGAAA
ACCACTGACCTTATCAAAGAACACACTACCAAGTATAATGAAATTCAGAATGACTACTTG
AGAAGGAGAGCCGCTTTGGAAAAGTCCGCCAAAAAGGACAGTAAGAAAAAATCGGAACCC
AGCAGCCCTGATCATGGTTCATCAACGATTGAGCAAGACCTCGCTGCTCTGGATGCTGAA
ATGACCCAAAAGTTAATAGACTTGAAGGACAAACAACAGCAGCAGCTGCTTAATCTTCGG
CAAGAACAGTATTATAGTGAAAAATACCAGAAGCGAGAACATATTAAACTGCTTATTCAA
AAGTTGACGGATGTCGCAGAAGAGTGTCAGAACAATCAGTTAAAGAAGCTCAAAGAAATC
TGTGAGAAAGAAAAGAAAGAATTAAAGAAGAAAATGGATAAAAAGAGGCAGGAGAAGATA
ACAGAAGCTAAATCCAAAGACAAAAGTCAGATGGAAGAGGAGAAGACAGAGATGATCCGG
TCATATATCCAGGAAGTGGTGCAGTATATCAAGAGGCTAGAAGAAGCGCAAAGTAAACGG
CAAGAAAAACTCGTAGAGAAACACAAGGAAATACGTCAGCAGATCCTGGATGAAAAGCCC
AAGCTGCAGGTGGAGCTGGAGCAAGAATACCAAGACAAATTCAAAAGACTGCCCCTCGAG
ATTTTGGAATTCGTGCAGGAAGCCATGAAAGGAAAGATCAGTGAAGACAGCAATCACGGT
TCTGCCCCTCTCTCCCTGTCCTCAGACCCTGGAAAAGTGAACCACAAGACTCCCTCCAGT
GAGGAGCTGGGAGGAGACATCCCAGGAAAAGAATTTGATACTCCTCTGTGA
Enzyme 1 GenBank Gene ID AJ278313 Link Image
Enzyme 1 GeneCard ID PLCB1 Link Image
Enzyme 1 GenAtlas ID PLCB1 Link Image
Enzyme 1 HGNC ID HGNC:15917 Link Image
Enzyme 1 Chromosome Location 20
Enzyme 1 Locus 20p12
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Peruzzi D, Calabrese G, Faenza I, Manzoli L, Matteucci A, Gianfrancesco F, Billi AM, Stuppia L, Palka G, Cocco L: Identification and chromosomal localisation by fluorescence in situ hybridisation of human gene of phosphoinositide-specific phospholipase C beta(1). Biochim Biophys Acta. 2000 Apr 12;1484(2-3):175-82. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  3. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5455
Enzyme 2 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 4
Enzyme 2 Synonyms
  1. Phosphoinositide phospholipase C
  2. Phospholipase C- beta-4
  3. PLC-beta-4
Enzyme 2 Gene Name PLCB4
Enzyme 2 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 4 
MAKPYEFNWQKEVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWRSEGKEGQVL
ECSLINSIRSGAIPKDPKILAALEAVGKSENDLEGRIVCVCSGTDLVNISFTYMVAENPE
VTKQWVEGLRSIIHNFRANNVSPMTCLKKHWMKLAFMTNTNGKIPVRSITRTFASGKTEK
VIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVD
QLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE
NAPVFLDRLELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELD
CWDGKGEDQEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKM
SKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRLKPEVEKKQLEALRSM
MEAGESASPANILEDDNEEEIESADQEEEAHPEFKFGNELSADDLGHKEAVANSVKKGLV
TVEDEQAWMASYKYVGATTNIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVG
LGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQL
NQGKFEYNGSCGYLLKPDFMRRPDRTFDPFSETPVDGVIAATCSVQVISGQFLSDKKIGT
YVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNK
LIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNIVLKTYVPDGFGDIVDALSDPKK
FLSITEKRADQMRAMGIETSDIADVPSDTSKNDKKGKANTAKANVTPQSSSELRPTTTAA
LASGVEAKKGIELIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHCTQ
VDKIVAQYDKEKSTHEKILEKAMKKKGGSNCLEMKKETEIKIQTLTSDHKSKVKEIVAQH
TKEWSEMINTHSAEEQEIRDLHLSQQCELLKKLLINAHEQQTQQLKLSHDRESKEMRAHQ
AKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQ
LEHLEFLEKQNEQAKEMQQMVKLEAEMDRRPATVV
Enzyme 2 Number of Residues 1175
Enzyme 2 Molecular Weight 134465
Enzyme 2 Theoretical pI 6.90
Enzyme 2 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 2 General Function Replication, recombination and repair
Enzyme 2 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This form has a role in retina signal transduction
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 762826 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q15147 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PLCB4_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >3069 bp 
ATGAACAATAACTGGAATGTGTGTTTCTTTCTTTTCTGCCCTAGTATTACTAGAACATTT
GCATCGGGAAAAACAGAAAAGGTGATCTTTCAAGCACTCAAGGAGTTAGGTCTTCCCAGT
GGAAAGAATGATGAAATTGAGCCCACAGCATTTTCTTATGAAAAGTTCTATGAACTGACA
CAAAAGATTTGTCCTCGGACAGATATAGAAGATCTTTTCAAAAAAATCAATGGAGACAAA
ACTGATTATTTAACGGTAGACCAATTAGTGAGCTTTCTAAATGAACATCAACGAGATCCT
CGATTGAATGAAATTTTATTTCCATTTTATGATGCCAAAAGGGCAATGCAGATCATTGAG
ATGTATGAACCTGATGAAGATTTGAAGAAAAAAGGCCTTATATCAAGTGATGGGTTTTGC
AGATATCTGATGTCAGATGAAAACGCCCCAGTCTTCCTAGATCGTTTAGAACTTTACCAA
GAAATGGACCATCCTCTGGCTCACTACTTCATCAGTTCTTCCCATAACACTTATCTCACT
GGCAGACAGTTCGGCGGGAAGTCTTCGGTAGAAATGTACAGACAGGTTCTCCTGGCTGGT
TGCAGATGTGTTGAACTTGACTGCTGGGATGGAAAAGGTGAGGACCAAGAACCAATAATA
ACTCATGGAAAAGCAATGTGTACAGATATCCTTTTTAAGGATGTAATTCAAGCCATCAAG
GAAACTGCATTTGTCACATCAGAATATCCTGTAATTCTCTCCTTTGAAAATCACTGCAGC
AAATATCAACAGTACAAGATGTCCAAATATTGCGAAGATCTATTTGGGGATCTCCTGTTG
AAACAAGCACTTGAATCACATCCACTGGAACCAGGCAGACCTTTGCCATCCCCCAATGAC
CTCAAAAGAAAAATACTCATAAAAAACAAGCGGCTGAAACCTGAAGTTGAAAAAAAACAG
CTGGAAGCTTTGAGAAGCATGATGGAAGCTGGAGAATCTGCCTCCCCAGCAAACATCTTA
GAGGACGATAATGAAGAGGAGATCGAAAGTGCTGACCAAGAGGAGGAAGCTCACCCCGAA
TTCAAATTTGGAAATGAACTTTCTGCTGATGACTTGGGTCACAAGGAAGCTGTTGCAAAT
AGCGTCAAGAAGGGCCTGGTCACTGTAGAAGATGAGCAGGCGTGGATGGCATCTTATAAA
TATGTAGGTGCTACCACTAATATCCATCCATATTTGTCCACAATGATCAACTATGCCCAG
CCTGTAAAGTTTCAAGGTTTCCATGTGGCAGAAGAACGCAATATTCATTATAACATGTCT
TCTTTTAATGAATCAGTCGGTCTTGGCTACTTGAAGACACATGCAATTGAATTTGTCAAT
TATAACAAACGGCAAATGAGTCGCATTTACCCCAAGGGAGGCCGAGTCGATTCCAGTAAT
TACATGCCTCAGATTTTCTGGAACGCTGGCTGCCAGATGGTTTCACTGAACTATCAAACC
CCAGATTTAGCGATGCAATTGAATCAGGGAAAATTTGAGTATAATGGATCGTGCGGGTAC
CTTCTCAAACCAGATTTCATGAGGCGGCCTGATCGAACATTTGACCCCTTCTCTGAAACG
CCTGTTGATGGGGTTATTGCAGCCACTTGCTCAGTGCAGGTTATATCAGGTCAATTCTTA
TCAGATAAGAAAATTGGCACCTACGTAGAGGTGGATATGTATGGGTTGCCCACTGACACC
ATACGTAAGGAATTCCGAACTCGCATGGTTATGAATAATGGACTCAATCCAGTTTACAAT
GAAGAGTCACTTGTATTTCGGAAGGTGATCCTGCCGGACCTGGCTGTCTTGAGAATAGCT
GTGTATGATGATAACAACAAGCTGATTGGCCAGAGGATTCCTCCGCTTGATGGCCTCCAA
GCCGGATATCGACACATTTCCCTTCGAAATGAGGGAAATAAACCATTATCACTACCAACA
ATTTTCTGCAATATTGTTCTTAAAACATATGTGCCTGATGGATTTGGAGATATCGTGGAT
GCTTTATCAGATCCAAAGACATTTCTCTCAATTACAGAAAAGAGAGCAGACCAAATGAGA
GCTATGGGCATTGAGACTAGTGACATAGCCGACGTGCCCAGTGACACTTCCAAAAATGAC
AAGAAAGGAAAGGCCAACACCGCCAAAGCAAATGTGACCCCTCAGAGTAGCTCTGAGCTC
AGACCAACCACCACGGCTGCCCTGCCGTCTGGTGTGGAAGCCAAGAAAGGTATTGAACTT
ATCCCTCAAGTAAGGATAGAAGACTTAAAGCAGATGAAGGCTTACTTGAAGCATTTAAAG
AAACAGCAGAAGGAGCTAAATTCTTTAAAGAAGAAACATGCAAAGGAACACAGTACCATG
CAGAAGTTACACTGCACGCAAGTTGACAAAATTGTGGCACAGTATGACAAAGAGAAGTCG
ACTCATGAGAAAATCCTAGAGAAGGCAATGAAGAAGAAAGGGGGAAGTAATTGTCTTGAA
ATGAAGAAAGAAACAGAAATTAAAATTCAGACGCTGACATCAGATCACAAATCTAAGGTC
AAGGAGATTGTAGCACAGCACACAAAGGAATGGTCAGAAATGATCAATACTCACAGTGCT
GAGGAGCAAGAAATCCGAGACCTGCACCTCAGCCAGCAGTGTGAGCTGCTGAAAAAGCTA
CTCATCAATGCCCACGAGCAGCAAACCCAGCAGCTGAAACTGTCCCATGACAGGGAAAGC
AAGGAAATGCGAGCACACCAGGCTAAGATTTCTATGGAAAATAGCAAAGCCATCAGCCAA
GATAAATCTATCAAGAATAAAGCAGAACGGGAAAGGCGAGTCAGGGAGTTAAACAGCAGC
AACACTAAAAAGTTTCTGGAAGAAAGAAAGAGACTTGCCATGAAGCAGTCCAAAGAAATG
GATCAGTTGAAAAAAGTCCAGCTTGAACATCTAGAATTCCTAGAGAAACAGAATGAGCAG
GCGAAGGAGATGCAGCAGATGGTGAAATTGGAAGCCGAGATGGACCGCAGACCAGCAACA
GTAGTATGA
Enzyme 2 GenBank Gene ID L41349 Link Image
Enzyme 2 GeneCard ID PLCB4 Link Image
Enzyme 2 GenAtlas ID PLCB4 Link Image
Enzyme 2 HGNC ID HGNC:9059 Link Image
Enzyme 2 Chromosome Location 20
Enzyme 2 Locus 20p12
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Alvarez RA, Ghalayini AJ, Xu P, Hardcastle A, Bhattacharya S, Rao PN, Pettenati MJ, Anderson RE, Baehr W: cDNA sequence and gene locus of the human retinal phosphoinositide-specific phospholipase-C beta 4 (PLCB4). Genomics. 1995 Sep 1;29(1):53-61. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5456
Enzyme 3 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 2
Enzyme 3 Synonyms
  1. Phosphoinositide phospholipase C
  2. Phospholipase C- beta-2
  3. PLC-beta-2
Enzyme 3 Gene Name PLCB2
Enzyme 3 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 2 
MSLLNPVLLPPKVKAYLSQGERFIKWDDETTVASPVILRVDPKGYYLYWTYQSKEMEFLD
ITSIRDTRFGKFAKMPKSQKLRDVFNMDFPDNSFLLKTLTVVSGPDMVDLTFHNFVSYKE
NVGKAWAEDVLALVKHPLTANASRSTFLDKILVKLKMQLNSEGKIPVKNFFQMFPADRKR
VEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSYHAKAKPYMTKEH
LTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPEN
SVLAQDKLLLHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDC
WKGKPPDEEPIITHGFTMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVDSPRQQAKM
AEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKNQFSGPTSSSKDTGGE
AEGSSPPSAPAVWAGEEGTELEEEEVEEEEEEESGNLDEEEIKKMQSDEGTAGLEVTAYE
EMSSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIY
PKGTRMDSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFMRRP
DKQFNPFSVDRIDVVVATTLSITVISGQFLSERSVRTYVEVELFGLPGDPKRRYRTKLSP
STNSINPVWKEEPFVFEKILMPELASLRVAVMEEGNKFLGHRIIPINALNSGYHHLCLHS
ESNMPLTMPALFIFLEMKDYIPGAWADLTVALANPIKFFSAHDTKSVKLKEAMGGLPEKP
FPLASPVASQVNGALAPTSNGSPAARAGAREEAMKEAAEPRTASLEELRELKGVVKLQRR
HEKELRELERRGARRWEELLQRGAAQLAELGPPGVGGVGACKLGPGKGSRKKRSLPREES
AGAAPGEGPEGVDGRVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREK
QAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVV
QVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAEVKESVRA
CLRTCFPSEAKDKPERACECPPELCEQDPLIAKADAQESRL
Enzyme 3 Number of Residues 1181
Enzyme 3 Molecular Weight 133681
Enzyme 3 Theoretical pI 6.28
Enzyme 3 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 3 General Function Replication, recombination and repair
Enzyme 3 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes
Enzyme 3 Pathways
Enzyme 3 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 190040 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q00722 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PLCB2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >3546 bp 
ATGTCTCTGCTCAACCCTGTCCTGCTGCCCCCCAAGGTGAAGGCCTATCTGAGCCAAGGG
GAGCGCTTCATCAAATGGGATGATGAAACTACAGTTGCCTCTCCAGTTATCCTCCGTGTG
GATCCTAAGGGCTACTACTTATACTGGACGTATCAAAGTAAGGAGATGGAGTTTCTGGAT
ATCACCAGCATCCGGGATACTCGCTTTGGGAAGTTTGCCAAGATGCCCAAGAGCCAGAAG
CTCCGGGACGTCTTCAACATGGACTTTCCTGATAACAGTTTCCTGCTGAAGACACTCACG
GTGGTGTCCGGCCCGGACATGGTGGACCTCACCTTCCACAACTTCGTCTCCTACAAGGAG
AACGTGGGCAAGGCCTGGGCTGAGGACGTACTGGCCCTAGTCAAACATCCGCTGACGGCC
AACGCCTCCCGCAGCACCTTCCTGGACAAGATCCTTGTGAAGCTCAAGATGCAGCTCAAC
TCTGAAGGGAAGATTCCGGTGAAGAACTTTTTCCAGATGTTTCCTGCTGACCGCAAGCGG
GTGGAAGCTGCTCTCAGTGCCTGCCACCTCCCCAAAGGCAAAAATGACGCCATCAATCCT
GAGGACTTCCCAGAACCTGTCTACAAGAGTTTCCTCATGAGCCTCTGTCCTCGGCCAGAA
ATAGATGAGATCTTCACTTCTTACCATGCTAAGGCCAAACCCTACATGACGAAGGAGCAC
CTGACCAAATTCATCAACCAGAAACAGCGGGACTCCCGGCTTAACTCCCTGCTGTTCCCG
CCAGCACGGCCTGACCAGGTGCAGGGCCTCATCGACAAGTATGAGCCCAGTGGCATCAAT
GCACAGAGGGGCCAGCTGTCACCTGAAGGCATGGTCTGGTTTCTCTGTGGGCCAGAGAAC
AGCGTGCTGGCCCAGGACAAGCTGCTGCTCCACCACGACATGACGCAGCCACTCAATCAT
TACTTCATCAACTCGTCCCACAACACCTACCTGACAGCCGGCCAGTTCTCAGGCCTCTCC
TCGGCTGAGATGTACCGCCAGGTGCTGCTCTCTGGCTGCCGTTGCGTGGAGCTAGACTGC
TGGAAGGGGAAACCCCCTGACGAGGAGCCCATTATCACCCATGGCTTCACCATGACCACA
GACATCTTCTTCAAAGAAGCAATTGAGGCTATTGCAGAAAGTGCCTTTAAGACCTCCCCC
TATCCCATCATCCTGTCGTTTGAGAACCATGTGGACTCACCCCGCCAGCAGGCTAAGATG
GCTGAGTATTGCCGGACGATCTTTGGGGATATGCTGCTCACAGAGCCCCTGGAAAAGTTC
CCACTAAAACCAGGTGTCCCCCTGCCCAGCCCTGAGGATCTCAGGGGCAAGATCCTCATC
AAGAACAAGAAGAACCAGTTTTCTGGCCCCACCTCCTCCAGTAAGGATACCGGTGGGGAG
GCTGAGGGCAGCAGCCCACCCAGTGCCCCTGCAGTGTGGGCTGGCGAGGAAGGGACTGAG
CTGGAGGAGGAGGAGGTGGAAGAGGAAGAGGAGGAGGAGTCAGGAAACCTGGATGAAGAA
GAGATTAAGAAGATGCAGTCGGATGAGGGCACAGCGGGCCTGGAAGTGACGGCTTATGAG
GAGATGTCCAGCCTAGTCAATTACATCCAGCCCACCAAGTTCGTCTCCTTTGAGTTCTCT
GCCCAAAAGAACCGAAGTTATGTCATCTCGTCCTTCACAGAGCTCAAGGCATATGACCTG
CTCTCCAAGGCCTCGGTGCAGTTTGTGGACTACAACAAGCGCCAGATGAGCCGCATTTAC
CCCAAGGGAACCCGCATGGACTCCTCCAACTACATGCCCCAGATGTTCTGGAATGCTGGA
TGCCAGATGGTTGCCCTCAACTTCCAGACGATGGACTTGCCCATGCAGCAGAACATGGCA
GTATTTGAGTTCAACGGGCAGAGCGGCTACCTCCTCAAGCATGAGTTCATGCGCCGGCCG
GACAAGCAGTTCAACCCCTTCTCAGTGGACCGCATCGACGTGGTGGTGGCCACCACCCTT
TCCATTACGGTGATCTCTGGGCAGTTCCTGTCAGAACGCAGCGTGCGCACCTATGTAGAA
GTGGAGCTGTTTGGCCTTCCTGGGGACCCCAAGAGGCGCTATCGAACTAAGCTGTCACCC
AGTACTAACTCCATCAATCCTGTCTGGAAGGAGGAGCCCTTTGTCTTTGAGAAGATCTTG
ATGCCTGAGCTGGCCTCCCTCAGAGTGGCTGTGATGGAGGAAGGCAACAAGTTTCTTGGA
CACCGCATCATCCCCATCAATGCCCTAAATTCTGGGTACCACCACCTGTGCCTGCACAGT
GAGAGCAACATGCCCCTCACCATGCCTGCGCTCTTCATCTTCCTGGAGATGAAGGACTAC
ATACCTGGTGCTTGGGCAGATCTCACTGTGGCCCTCGCCAACCCCATTAAGTTCTTCAGT
GCCCATGACACGAAGTCTGTGAAGCTCAAGGAGGCCATGGGAGGTCTGCCTGAGAAGCCC
TTCCCACTGGCGAGTCCAGTTGCCAGCCAGGTCAATGGGGCGTTGGCCCCAACGAGCAAT
GGGTCACCAGCAGCCAGGGCCGGGGCCAGGGAAGAGGCTATGAAAGAAGCTGCGGAGCCG
CGGACCGCCAGCCTGGAGGAGCTCCGGGAGCTAAAGGGCGTGGTGAAGCTGCAGCGGCGG
CACGAGAAGGAGCTGCGAGAGTTGGAGCGGCGCGGAGCGCGGCGCTGGGAGGAGCTGCTG
CAGCGGGGCGCGGCGCAGCTGGCGGAGCTCGGGCCACCGGGCGTGGGGGGCGTCGGGGCC
TGCAAGCTCGGTCCCGGCAAGGGCTCTCGCAAGAAGAGGAGCCTGCCCCGCGAGGAGAGC
GCCGGAGCCGCGCCGGGCGAGGGCCCTGAGGGCGTGGACGGGCGCGTGCGGGAGCTGAAA
GACAGGCTGGAGCTGGAGCTGCTGCGGCAGGGCGAGGAGCAGTACGAGTGCGTTCTGAAG
CGCAAGGAGCAGCACGTGGCCGAGCAAATCTCCAAAATGATGGAGCTGGCCAGAGAGAAA
CAGGCGGCAGAGCTGAAGGCCCTGAAGGAGACGTCGGAGAACGACACCAAAGAGATGAAG
AAAAAGCTGGAGACAAAGAGACTGGAGCGGATCCAGGGCATGACCAAAGTCACCACAGAC
AAGATGGCCCAGGAGAGGTTGAAGAGAGAGATTAACAACTCCCACATCCAGGAAGTAGTG
CAGGTGATCAAGCAGATGACGGAGAACTTGGAGAGGCACCAGGAGAAGCTGGAGGAGAAG
CAGGCGGCTTGCCTGGAACAGATACGGGAGATGGAAAAGCAGTTCCAGAAGGAGGCGCTG
GCAGAGTACGAGGCCAGGATGAAGGGTCTGGAGGCAGAGGTGAAGGAGTCGGTGAGGGCC
TGCCTCAGGACCTGCTTTCCCTCCGAGGCCAAGGACAAGCCTGAGAGGGCCTGCGAGTGC
CCCCCAGAGCTGTGTGAGCAGGACCCACTCATAGCAAAGGCAGATGCCCAGGAGAGCCGC
CTCTGA
Enzyme 3 GenBank Gene ID M95678 Link Image
Enzyme 3 GeneCard ID PLCB2 Link Image
Enzyme 3 GenAtlas ID PLCB2 Link Image
Enzyme 3 HGNC ID HGNC:9055 Link Image
Enzyme 3 Chromosome Location 15
Enzyme 3 Locus 15q15
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Park D, Jhon DY, Kriz R, Knopf J, Rhee SG: Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2. J Biol Chem. 1992 Aug 15;267(23):16048-55. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5460
Enzyme 4 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 3
Enzyme 4 Synonyms
  1. Phosphoinositide phospholipase C
  2. Phospholipase C- beta-3
  3. PLC-beta-3
Enzyme 4 Gene Name PLCB3
Enzyme 4 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 3 
MAGAQPGVHALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNME
VDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNF
MAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFS
ADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPY
LTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYL
GGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRC
VELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAK
QQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPDS
AGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGD
EGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPV
KFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYM
PQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIV
DGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEP
FDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLI
YTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQL
GSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRGH
KALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVED
TKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQF
KRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLE
EAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGLG
DGPLVACASNGHAPGSSGHLSGADSESQEENTQL
Enzyme 4 Number of Residues 1234
Enzyme 4 Molecular Weight 138801
Enzyme 4 Theoretical pI 5.66
Enzyme 4 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes
Enzyme 4 Pathways
Enzyme 4 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 836665 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q01970 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PLCB3_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >3705 bp 
ATGGCGGGCGCCCAGCCCGGCGTCCACGCGCTGCAGTTGGAGCCGCCCACCGTGGTGGAG
ACCCTGCGGCGCGGGAGTAAGTTCATCAAATGGGACGAGGAGACCTCCAGTCGGAACCTG
GTGACCCTGCGTGTGGACCCCAATGGCTTCTTCTTGTACTGGACGGGCCCCAACATGGAG
GTGGACACACTGGACATCAGTTCCATCAGGGACACACGGACAGGCCGGTACGCCCGCCTG
CCCAAGGACCCCAAGATCCGGGAAGTTCTGGGCTTTGGGGGTCCCGATGCCCGGCTGGAG
GAGAAGCTGATGACGGTGGTGTCTGGGCCAGACCCGGTGAACACAGTGTTCTTGAACTTC
ATGGCCGTGCAGGATGACACAGCCAAGGTCTGGTCTGAGGAGCTATTCAAGCTGGCTATG
AACATCCTGGCTCAGAACGCCTCCCGGAACACCTTCCTGCGCAAAGCATACACGAAGCTG
AAGCTGCAGGTGAACCAGGATGGTCGGATCCCCGTCAAGAACATCCTGAAGATGTTCTCA
GCAGACAAGAAGCGGGTGGAGACTGCGCTGGAATCCTGTGGCCTCAAATTCAACCGGAGT
GAGTCCATCCGGCCTGATGAGTTTTCCTTGGAAATCTTTGAGCGGTTCCTGAACAAGCTG
TGTCTGCGGCCGGACATTGACAAGATCCTGCTGGAGATAGGCGCCAAGGGCAAGCCATAC
CTGACGCTGGAGCAGCTCATGGACTTCATCAACCAGAAGCAACGCGACCCGAGACTCAAC
GAAGTGCTGTACCCGCCCCTGCGGCCCTCCCAGGCCCGGCTGCTCATCGAAAAGTATGAG
CCCAACCAGCAGTTTCTGGAGCGAGACCAGATGTCCATGGAGGGCTTTAGCCGCTACCTG
GGAGGCGAGGAGAATGGCATCCTGCCCCTGGAAGCCCTGGATCTGAGCACGGACATGACC
CAGCCACTGAGTGCCTACTTCATCAACTCCTCGCATAACACCTATCTCACTGCGGGGCAG
CTGGCTGGGACCTCGTCGGTGGAGATGTACCGCCAGGCACTACTATGGGGCTGCCGCTGC
GTGGAGCTGGACGTGTGGAAGGGACGGCCGCCTGAGGAGGAACCCTTCATTACCCACGGC
TTCACCATGACCACAGAGGTGCCTCTGCGCGACGTGCTGGAGGCCATTGCCGAGACTGCC
TTCAAGACCTCGCCCTACCCCGTCATCCTCTCCTTCGAGAACCATGTGGACTCGGCAAAG
CAACAGGCAAAGATGGCTGAGTACTGCCGCTCCATCTTTGGAGACGCGCTACTCATCGAG
CCTCTGGACAAGTACCCGCTGGCCCCAGGCGTTCCCCTGCCCAGCCCCCAGGACCTGATG
GGCCGTATCCTGGTGAAGAACAAGAAGCGGCACCGACCCAGCGCAGGTGGCCCAGACAGC
GCCGGGCGCAAGCGGCCCCTGGAGCAGAGCAATTCTGCCCTGAGCGAGAGCTCCGCGGCC
ACCGAGCCCTCCTCCCCGCAGCTGGGGTCTCCCAGCTCTGACAGCTGCCCAGGCCTGAGC
AATGGGGAGGAGGTAGGGCTTGAGAAGCCCAGCCTGGAGCCTCAGAAGTCTCTGGGTGAC
GAGGGCCTGAACCGAGGCCCCTATGTTCTTGGACCTGCTGACCGTGAGGATGAGGAGGAA
GATGAGGAAGAGGAGGAACAGACAGACCCCAAAAAGCCAACTACAGATGAGGGCACAGCC
AGCAGCGAGGTGAATGCCACTGAGGAGATGTCCACGCTTGTCAACTACATCGAACCTGTC
AAGTTCAAGTCCTTTGAGGCTGCTCGAAAGAGGAACAAATGCTTCGAGATGTCGTCCTTT
GTGGAGACCAAGGCCATGGAGCAACTGACCAAGAGCCCCATGGAGTTTGTGGAATACAAC
AAGCAGCAGCTCAGCCGCATCTACCCCAAGGGCACCCGCGTGGACTCCTCCAACTACATG
CCCCAGCTCTTCTGGAACGTAGGGTGCCAGCTTGTTGCGCTCAACTTCCAGACCCTCGAT
GTGGCGATGCAGCTCAACGCGGGCGTTTTTGAGTACAACGGGCGCAGCGGGTACCTGCTC
AAGCCGGAGTTCATGCGGCGGCCGGACAAGTCCTTCGACCCCTTCACTGAGGTCATCGTG
GATGGCATCGTGGCCAATGCCTTGCGGGTCAAGGTGATCTCAGGGCAGTTCCTGTCCGAC
AGGAAGGTGGGCATCTACGTGGAGGTGGACATGTTTGGCCTCCCTGTTGATACGCGGCGC
AAGTACCGCACCCGGACCTCTCAGGGGAACTCGTTCAACCCCGTGTGGGACGAAGAGCCC
TTCGACTTCCCCAAGGTGGTGCTGCCCACGCTGGCTTCACTTCGCATTGCAGCCTTTGAG
GAGGGGGGTAAATTCGTAGGGCACCGGATCCTGCCTGTCTCTGCCATCCGCTCCGGATAC
CACTACGTCTGCCTGCGGAACGAGGCCAACCAACCGCTGTGCCTGCCGGCCCTGCTCATC
TACACCGAAGCCTCGGACTACATTCCTGACGACCACCAGGACTATGCGGAGGCCCTGATC
AACCCCATTAAGCACGTCAGCCTGATGGACCAGAGGGCCCGGCAGCTGGCCGCCCTCATT
GGGGAGAGTGAGGCTCAGGCTGGCCAAGAGACGTGCCAGGACACCCAGTCTCAGCAGCTG
GGGTCTCAGCCGTCCTCAAACCCCACCCCCAGCCCACTGGATGCCTCCCCCCGCCGGCCC
CCTGGCCCCACCACCTCCCCTGCCAGCACCTCCCTCAGCAGCCCAGGGCAGCGTGATGAT
CTCATCGCCAGCATCCTCTCAGAGGTGGCCCCCACCCCGCTGGATGAGCTCCGAGGTCAC
AAGGCTCTGGTCAAGCTCCGGAGCCGGCAAGAGCGAGACCTGCGGGAGCTGCGCAAGAAG
CATCAGCGGAAGGCAGTCACCCTCACCCGCCGCCTGCTGGATGGCCTGGCTCAGGCACAG
GCTGAGGGCAGGTGCCGGCTGCGGCCAGGTGCCCTAGGTGGGGCCGCTGATGTGGAGGAC
ACGAAGGAGGGGGAGGACGAGGCAAAGCGGTATCAGGAGTTCCAGAACAGACAGGTGCAG
AGCCTGCTGGAGCTGCGGGAGGCCCAGGTGGACGCAGAGGCCCAGCGGAGGCTGGAACAC
CTGAGACAGGCTCTGCAGCGGCTCAGGGAGGTCGTCCTTGATGCAAACACAACTCAGTTC
AAGAGGCTGAAAGAGATGAACGAGAGGGAGAAGAAGGAGCTGCAGAAGATCCTGGACAGA
AAGCGCCATAACAGCATCTCGGAGGCCAAGATGAGGGACAAGCATAAGAAGGAGGCGGAA
CTGACGGAGATTAACCGTCGGCACATCACTGAGTCAGTCAACTCCATCCGTCGGCTGGAG
GAGGCCCAGAAGCAGCGGCATGACCGTCTTGTGGCTGGGCAGCAGCAGGTCCTGCAACAG
CTGGCAGAAGAGGAGCCCAAGCTGCTGGCCCAGCTGGCCCAGGAGTGTCAGGAGCAGCGG
GCGAGGCTCCCCCAGGAGATCCGCCGGAGCCTGCTGGGCGAGATGCCGGAGGGGCTGGGG
GACGGGCCTCTGGTGGCCTGTGCCAGCAACGGTCACGCACCCGGGAGCAGCGGGCACCTG
TCGGGCGCTGACTCGGAGAGCCAGGAGGAGAACACGCAGCTCTGA
Enzyme 4 GenBank Gene ID U26425 Link Image
Enzyme 4 GeneCard ID PLCB3 Link Image
Enzyme 4 GenAtlas ID PLCB3 Link Image
Enzyme 4 HGNC ID HGNC:9056 Link Image
Enzyme 4 Chromosome Location 11
Enzyme 4 Locus 11q13
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Mazuruk K, Schoen TJ, Chader GJ, Rodriguez IR: Structural organization and expression of the human phosphatidylinositol-specific phospholipase C beta-3 gene. Biochem Biophys Res Commun. 1995 Jul 6;212(1):190-5. [PubMed Link Image]
  2. Lagercrantz J, Carson E, Phelan C, Grimmond S, Rosen A, Dare E, Nordenskjold M, Hayward NK, Larsson C, Weber G: Genomic organization and complete cDNA sequence of the human phosphoinositide-specific phospholipase C beta 3 gene (PLCB3). Genomics. 1995 Apr 10;26(3):467-72. [PubMed Link Image]
  3. Carozzi AJ, Kriz RW, Webster C, Parker PJ: Identification, purification and characterization of a novel phosphatidylinositol-specific phospholipase C, a third member of the beta subfamily. Eur J Biochem. 1992 Dec 1;210(2):521-9. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5462
Enzyme 5 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma 2
Enzyme 5 Synonyms
  1. Phosphoinositide phospholipase C
  2. PLC-gamma-2
  3. Phospholipase C-gamma-2
  4. PLC-IV
Enzyme 5 Gene Name PLCG2
Enzyme 5 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma 2 
MSTTVNVDSLAEYEKSQIKRALELGTVMTVFSFRKSTPERRTVQVIMETRQVAWSKTADK
IEGFLDIMEIKEIRPGKNSKDFERAKAVRQKEDCCFTILYGTQFVLSTLSLAADSKEDAV
NWLSGLKILHQEAMNASTPTIIESWLRKQIYSVDQTRRNSISLRELKTILPLINFKVSSA
KFLKDKFVEIGAHKDELSFEQFHLFYKKLMFEQQKSILDEFKKDSSVFILGNTDRPDASA
VYLHDFQRFLIHEQQEHWAQDLNKVRERMTKFIDDTMRETAEPFLFVDEFLTYLFSRENS
IWDEKYDAVDMQDMNNPLSHYWISSSHNTYLTGDQLRSESSPEAYIRCLRMGCRCIELDC
WDGPDGKPVIYHGWTRTTKIKFDDVVQAIKDHAFVTSSFPVILSIEEHCSVEQQRHMAKA
FKEVFGDLLLTKPTEASADQLPSPSQLREKIIIKHKKLGPRGDVDVNMEDKKDEHKQQGE
LYMWDSIDQKWTRHYCAIADAKLSFSDDIEQTMEEEVPQDIPPTELHFGEKWFHKKVEKR
TSAEKLLQEYCMETGGKDGTFLVRESETFPNDYTLSFWRSGRVQHCRIRSTMEGGTLKYY
LTDNLTFSSIYALIQHYRETHLRCAEFELRLTDPVPNPNPHESKPWYYDSLSRGEAEDML
MRIPRDGAFLIRKREGSDSYAITFRARGKVKHCRINRDGRHFVLGTSAYFESLVELVSYY
EKHSLYRKMRLRYPVTPELLERYNMERDINSLYDVSRMYVDPSEINPSMPQRTVKALYDY
KAKRSDELSFCRGALIHNVSKEPGGWWKGDYGTRIQQYFPSNYVEDISTADFEELEKQII
EDNPLGSLCRGILDLNTYNVVKAPQGKNQKSFVFILEPKQQGYPPVEFATDRVEELFEWF
QSIREITWKIDTKENNMKYWEKNQSIAIELSDLVVYCKPTSKTKDNLENPDFREIRSFVE
TKADSIIRQKPVDLLKYNQKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTADKY
MQMNHALFSLNGRTGYVLQPESMRTEKYDPMPPESQRKILMTLTVKVLGARHLPKLGRSI
ACPFVEVEICGAEYDNNKFKTTVVNDNGLSPIWAPTQEKVTFEIYDPNLAFLRFVVYEED
MFSDPNFLAHATYPIKAVKSGFRSVPLKNGYSEDIELASLLVFCEMRPVLESEEELYSSC
RQLRRRQEELNNQLFLYDTHQNLRNANRDALVKEFSVNENQLQLYQEKCNKRLREKRVSN
SKFYS
Enzyme 5 Number of Residues 1265
Enzyme 5 Molecular Weight 147919
Enzyme 5 Theoretical pI 6.66
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling
Enzyme 5 Pathways
Enzyme 5 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 5 Pfam Domain Function Not Available
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 35514 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P16885 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PLCG2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >3759 bp 
ATGTCCACCACGGTCAATGTAGATTCCCTTGCGGAATATGAGAAGAGCCAGATCAAGAGA
GCCCTGGAGCTGGGGACGGTGATGACTGTGTTCAGCTTCCGCAAGTCCACCCCCGAGCGG
AGAACCGTCCAGGTGATCATGGAGACGCGGCAGGTGGCCTGGAGCAAGACCGCCGACAAG
ATCGAGGGCTTCTTGGATATCATGGAAATAAAAGAAATCCGCCCAGGGAAGAACTCCAAA
GATTTCGAGCGAGCAAAAGCAGTTCGCCAGAAAGAAGACTGCTGCTTCACCATCCTATAT
GGCACTCAGTTCGTCCTCAGCACGCTCAGCTTGGCAGCTGACTCTAAAGAGGATGCAGTT
AACTGGCTCTCTGGCTTGAAAATCTTACACCAGGAAGCGATGAATGCGTCCACGCCCACC
ATTATCGAGAGTTGGCTGAGAAAGCAGATATATTCTGTGGATCAAACCAGAAGAAACAGC
ATCAGTCTCCGAGAGTTGAAGACCATCTTGCCCCTGATCAACTTTAAAGTGAGCAGTGCC
AAGTTCCTTAAAGATAAGTTTGTGGAAATAGGAGCACACAAAGATGAGCTCAGCTTTGAA
CAGTTCCATCTCTTCTATAAAAAACTTATGTTTGAACAGCAAAAATCGATTCTCGATGAA
TTCAAAAAGGATTCGTCCGTGTTCATCCTGGGGAACACTGACAGGCCGGATGCCTCTGCT
GTTTACCTGCATGACTTCCAGAGGTTTCTCATACATGAACAGCAGGAGCATTGGGCTCAG
GATCTGAACAAAGTCCGTGAGCGGATGACAAAGTTCATTGATGACACCATGCGTGAAACT
GCTGAGCCTTTCTTGTTTGTGGATGAGTTCCTCACGTACCTGTTTTCACGAGAAAACAGC
ATCTGGGATGAGAAGTATGACGCGGTGGACATGCAGGACATGAACAACCCCCTGTCTCAT
TACTGGATCTCCTCGTCACATAACACGTACCTTACAGGTGACCAGCTGCGGAGCGAGTCG
TCCCCAGAAGCTTACATCCGCTGCCTGCGCATGGGCTGTCGCTGCATTGAACTGGACTGC
TGGGACGGGCCCGATGGGAAGCCGGTCATCTACCATGGCTGGACGCGGACTACCAAGATC
AAGTTTGATGACGTCGTGCAGGCCATCAAAGACCACGCCTTTGTTACCTCGAGCTTCCCA
GTGATCCTGTCCATCGAGGAGCACTGCAGCGTGGAGCAACAGCGTCACATGGCCAAGGCC
TTCAAGGAAGTATTTGGCGACCTGCTGTTGACGAAGCCCACGGAGGCCAGTGCTGACCAG
CTGCCCTCGCCCAGCCAGCTGCGGGAGAAGATCATCATCAAGCATAAGAAGCTGGGCCCC
CGAGGCGATGTGGATGTCAACATGGAGGACAAGAAGGACGAACACAAGCAACAGGGGGAG
CTGTACATGTGGGATTCCATTGACCAGAAATGGACTCGGCACTACTGCGCCATTGCTGAT
GCCAAGCTGTCCTTCAGTGATGACATTGAACAGACTATGGAGGAGGAAGTGCCCCAGGAT
ATACCCCCTACAGAACTACATTTTGGGGAGAAATGGTTCCACAAGAAGGTGGAGAAGAGG
ACGAGTGCCGAGAAGTTGCTGCAGGAATACTGCATGGAGACGGGGGGCAAGGATGGCACC
TTCCTGGTTCGGGAGAGCGAGACCTTCCCCAATGACTACACCCTGTCCTTCTGGCGGTCA
GGCCGGGTCCAGCACTGCCGGATCCGCTCCACCATGGAGGGCGGGACCCTGAAATACTAC
TTGACTGACAACCTGAGGTTCAGGAGGATGTATGCCCTCATCCAGCACTACCGCGAGACG
CACCTGCCGTGCGCCGAGTTCGAGCTGCGGCTCACGGACCCTGTGCCCAACCCCAACCCC
CACGAGTCCAAGCCGTGGTACTATGACAGCCTGAGCCGCGGAGAGGCAGAGGACATGCTG
ATGAGGATTCCCCGGGACGGGGCCTTCCTGATCCGGAAGCGAGAGGGGAGCGACTCCTAT
GCCATCACCTTCAGGGCTAGGGGCAAGGTAAAGCATTGTCGCATCAACCGGGACGGCCGG
CACTTTGTGCTGGGGACCTCCGCCTATTTTGAGAGTCTGGTGGAGCTCGTCAGTTACTAC
GAGAAGCATTCACTCTACCGAAAGATGAGACTGCGCTACCCCGTGACCCCCGAGCTCCTG
GAGCGCTACAATACGGAAAGAGATATAAACTCCCTCTACGACGTCAGCAGAATGTATGTG
GATCCCAGTGAAATCAATCCGTCCATGCCTCAGAGAACCGTGAAAGCTCTGTATGACTAC
AAAGCCAAGCGAAGCGATGAGCTGAGCTTCTGCCGTGGTGCCCTCATCCACAATGTCTCC
AAGGAGCCCGGGGGCTGGTGGAAAGGAGACTATGGAACCAGGATCCAGCAGTACTTCCCA
TCCAACTACGTCGAGGACATCTCAACTGCAGACTTCGAGGAGCTAGAAAAGCAGATTATT
GAAGACAATCCCTTAGGGTCTCTTTGCAGAGGAATATTGGACCTCAATACCTATAACGTC
GTGAAAGCCCCTCAGGGAAAAAACCAGAAGTCCTTTGTCTTCATCCTGGAGCCCAAGGAG
CAGGGCGATCCTCCGGTGGAGTTTGCCACAGACAGGGTGGAGGAGCTCTTTGAGTGGTTT
CAGAGCATCCGAGAGATCACGTGGAAGATTGACAGCAAGGAGAACAACATGAAGTACTGG
GAGAAGAACCAGTCCATCGCCATCGAGCTCTCTGACCTGGTTGTCTACTGCAAACCAACC
AGCAAAACCAAGGACAACTTAGAAAATCCTGACTTCCGAGAAATCCGCTCCTTTGTGGAG
ACGAAGGCTGACAGCATCATCAGACAGAAGCCCGTCGACCTCCTGAAGTACAATCAAAAG
GGCCTGACCCGCGTCTACCCAAAGGGACAAAGAGTTGACTCTTCAAACTACGACCCCTTC
CGCCTCTGGCTGTGCGGTTCTCAGATGGTGGCACTCAATTTCCAGACGGCAGATAAGTAC
ATGCAGATGAATCACGCATTGTTTTCTCTCAACGGGCGCACGGGCTACGTTCTGCAGCCT
GAGAGCATGAGGACAGAGAAATATGACCCGATGCCACCCGAGTCCCAGAGGAAGATCCTG
ATGACGCTGACAGTCAAGGTTCTCGGTGCTCGCCATCTCCCCAAACTTGGACGAAGTATT
GCCTGTCCCTTTGTAGAAGTGGAGATCTGTGGAGCCGAGTATGGCAACAACAAGTTCAAG
ACGACGGTTGTGAATGATAATGGCCTCAGCCCTATCTGGGCTCCAACACAGGAGAAGGTG
ACATTTGAAATTTATGACCCAAACCTGGCATTTCTGCGCTTTGTGGTTTATGAAGAAGAT
ATGTTCAGCGATCCCAACTTTCTTGCTCATGCCACTTACCCCATTAAAGCAGTCAAATCA
GGATTCAGGTCCGTTCCTCTGAAGAATGGGTACAGCGAGGACATAGAGCTGGCTTCCCTC
CTGGTTTTCTGTGAGATGCGGCCAGTCCTGGAGAGCGAAGAGGAACTTTACTCCTCCTGT
CGCCAGCTGAGGAGGCGGCAAGAAGAACTGAACAACCAGCTCTTTCTGTATGACACACAC
CAGAACTTGCGCAATGCCAACCGGGATGCCCTGGTTAAAGAGTTCAGTGTTAATGAGAAC
CACTCCAGCTGTACCAGGAGAAATGCAACAAGAGGTTAA
Enzyme 5 GenBank Gene ID X14034 Link Image
Enzyme 5 GeneCard ID PLCG2 Link Image
Enzyme 5 GenAtlas ID PLCG2 Link Image
Enzyme 5 HGNC ID HGNC:9066 Link Image
Enzyme 5 Chromosome Location 16
Enzyme 5 Locus 16q24.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Ohta S, Matsui A, Nazawa Y, Kagawa Y: Complete cDNA encoding a putative phospholipase C from transformed human lymphocytes. FEBS Lett. 1988 Dec 19;242(1):31-5. [PubMed Link Image]
  2. Ozdener F, Dangelmaier C, Ashby B, Kunapuli SP, Daniel JL: Activation of phospholipase Cgamma2 by tyrosine phosphorylation. Mol Pharmacol. 2002 Sep;62(3):672-9. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5476
Enzyme 6 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma 1
Enzyme 6 Synonyms
  1. Phosphoinositide phospholipase C
  2. PLC-gamma-1
  3. Phospholipase C-gamma-1
  4. PLC-II
  5. PLC-148
Enzyme 6 Gene Name PLCG1
Enzyme 6 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma 1 
MAGAASPCANGCGPGAPSDAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQI
TWSRGADKIEGAIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTL
SLQATSEDEVNMWIKGLTWLMEDTLQAPTPLQIERWLRKQFYSVDRNREDRISAKDLKNM
LSQVNYRVPNMRFLRERLTDLEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLEASTLRA
GERPELCRVSLPEFQQFLLDYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDEFVT
FLFSKENSVWNSQLDAVCPDTMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMG
CRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIA
QQRNMAQYFKKVLGDTLLTKPVEISADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSMM
YSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEVSS
STELHSNEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFW
RNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQT
NAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQE
GQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNP
GFYVEANPMPTFKCAVKALFDYKAQREDELTFIKSAIIQNVEKQEGGWWRGDYGGKKQLW
FPSNYVEEMVNPVALEPEREHLDENSPLGDLLRGVLDVPACQIAIRPEGKNNRLFVFSIS
MASVAHWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKIMERRKKIALELSELVVYC
RPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDS
SNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMTGRHCGYVLQPSTMRDEAFDPFDKS
SLRGLEPCAISIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVW
PAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDL
ELASLLIKIDIFPAKENGDLSPFSGTSLRERGSDASGQLFHGRAREGSFESRYQQPFEDF
RISQEHLADHFDSRERRAPRRTRVNGDNRL
Enzyme 6 Number of Residues 1290
Enzyme 6 Molecular Weight 148534
Enzyme 6 Theoretical pI 5.91
Enzyme 6 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function PLC-gamma is a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase
Enzyme 6 Pathways
Enzyme 6 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 190038 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P19174 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PLCG1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >3873 bp 
ATGGCGGGCGCCGCGTCCCCTTGCGCCAACGGCTGCGGGCCCGGCGCGCCCTCGGACGCC
GAGGTGCTGCACCTCTGCCGCAGCCTCGAGGTGGGCACCGTCATGACTTTGTTCTACTCC
AAGAAGTCGCAGCGACCCGAGCGGAAGACCTTCCAGGTCAAGCTGGAGACGCGCCAGATC
ACGTGGAGCCGGGGCGCCGACAAGATCGAGGGGGCCATTGACATTCGTGAAATTAAGGAG
ATCCGCCCAGGGAAGACCTCACGGGACTTTGATCGCTATCAAGAGGACCCAGCTTTCCGG
CCGGACCAGTCACATTGCTTTGTCATTCTCTATGGAATGGAATTTCGCCTGAAAACGCTG
AGCCTGCAAGCCACATCTGAGGATGAAGTGAACATGTGGATCAAGGGCTTAACTTGGCTG
ATGGAGGATACATTGCAGGCACCCACACCCCTGCAGATTGAGAGGTGGCTCCGGAAGCAG
TTTTACTCAGTGGATCGGAATCGTGAGGATCGTATATCAGCCAAGGACCTGAAGAACATG
CTGTCCCAGGTCAACTACCGGGTCCCCAACATGCGCTTCCTCCGAGAGCGGCTGACGGAC
CTGGAGCAGCGCAGCGGGGACATCACCTACGGGCAGTTTGCTCAGCTGTACCGCAGCCTC
ATGTACAGCGCCCAGAAGACGATGGACCTCCCCTTCTTGGAAGCCAGTACTCTGAGGGCT
GGGGAGCGGCCGGAGCTTTGCCGAGTGTCCCTTCCTGAGTTCCAGCAGTTCCTTCTTGAC
TACCAGGGGGAGCTGTGGGCTGTTGATCGCCTCCAGGTGCAGGAGTTCATGCTCAGCTTC
CTCCGAGACCCCTTACGAGAGATCGAGGAGCCATACTTCTTCCTGGATGAGTTTGTCACC
TTCCTGTTCTCCAAAGAGAACAGTGTGTGGAACTCGCAGCTGGATGCAGTATGCCCGGAC
ACCATGAACAACCCTCTTTCCCACTACTGGATCTCCTCCTCGCACAACACGTACCTGACC
GGGGACCAGTTCTCCAGTGAGTCCTCCTTGGAAGCCTATGCTCGCTGCCTGCGGATGGGC
TGTCGCTGCATTGAGTTGGACTGCTGGGACGGCCCGGATGGGATGCCAGTTATTTACCAT
GGGCACACCCTTACCACCAAGATCAAGTTCTCAGATGTCCTGCACACCATCAAGGAGCAT
GCCTTTGTGGCCTCAGAGTACCCAGTCATCCTGTCCATTGAGGACCACTGCAGCATTGCC
CAGCAGAGAAACATGGCCCAATACTTCAAGAAGGTGCTGGGGGACACACTCCTCACCAAG
CCCGTGGAGATCTCTGCCGACGGGCTCCCCTCACCCAACCAGCTTAAGAGGAAGATCCTC
ATCAAGCACAAGAAGCTGGCTGAGGGCAGTGCCTACGAGGAGGTGCCTACATCCATGATG
TACTCTGAGAACGACATCAGCAACTCTATCAAGAATGGCATCCTCTACCTGGAGGACCCT
GTGAACCACGAATGGTATCCCCACTACTTTGTTCTGACCAGCAGCAAGATCTACTACTCT
GAGGAGACCAGCAGTGACCAGGGCAACGAGGATGAGGAGGAGCCCAAGGAGGTCAGCAGC
AGCACAGAGCTGCACTCCAATGAGAAGTGGTTCCATGGGAAGCTAGGGGCAGGGCGTGAC
GGGCGTCACATCGCTGAGCGCCTGCTTACTGAGTACTGCATCGAGACCGGAGCCCCTGAC
GGCTCCTTCCTCGTGCGAGAGAGTGAGACCTTCGTGGGCGACTACACGCTCTCTTTCTGG
CGGAACGGGAAAGTCCAGCACTGCCGTATCCACTCCCGGCAAGATGCTGGGACCCCCAAG
TTCTTCTTGACAGACAACCTCGTCTTTGACTCCCTCTATGACCTCATCACGCACTACCAG
CAGGTGCCCCTGCGCTGTAATGAGTTTGAGATGCGACTTTCAGAGCCTGTCCCACAGACC
AACGCCCACGAGAGCAAAGAGTGGTACCACGCGAGCCTGACCAGAGCACAGGCTGAGCAC
ATGCTAATGCGCGTCCCTCGTGATGGGGCCTTCCTGGTGCGGAAGCGGAATGAACCCAAC
TCATATGCCATCTCTTTCCGGGCTGAGGGCAAGATCAAGCATTGCCGTGTCCAGCAAGAG
GGCCAGACAGTGATGCTAGGGAACTCGGAGTTCGACAGCCTTGTTGACCTCATCAGCTAC
TATGAGAAACACCCGCTATACCGCAAGATGAAGCTGCGCTATCCCATCAACGAGGAGGCA
CTGGAGAAGATTGGCACAGCTGAGCCTGACTACGGGGCCCTGTATGAGGGACGCAACCCT
GGCTTCTATGTAGAGGCAAACCCTATGCCAACTTTCAAGTGTGCAGTCAAAGCCCTCTTT
GACTACAAGGCCCAGAGGGAGGACGAGCTGACCTTCATCAAGAGCGCCATCATCCAGAAT
GTGGAGAAGCAAGAGGGAGGCTGGTGGCGAGGGGACTACGGAGGGAAGAAGCAGCTGTGG
TTCCCATCAAACTACGTGGAAGAGATGGTCAACCCCGTGGCCCTGGAGCCGGAGAGGGAG
CACTTGGACGAGAACAGCCCCCTAGGGGACTTGCTGCGGGGGGTCTTGGATGTGCCGGCT
TGTCAGATTGCCATCCGTCCTGAGGGCAAGAACAACCGGCTCTTCGTCTTCTCCATCAGC
ATGGCGTCGGTGGCCCACTGGTCCCTGGATGTTGCTGCCGACTCACAGGAGGAGCTGCAG
GACTGGGTGAAAAAGATCCGTGAAGTGGCCCAGACAGCAGACGCCAGGCTCACTGAAGGG
AAGATAATGGAACGGAGGAAGAAGATTGCCCTGGAGCTCTCTGAACTTGTCGTCTACTGC
CGGCCTGTTCCCTTTGATGAAGAGAAGATTGGCACAGAACGTGCTTGCTACCGGGACATG
TCATCCTTCCCGGAAACCAAGGCTGAGAAATACGTGAACAAGGCCAAAGGCAAGAAGTTC
CTTCAGTACAATCGACTGCAGCTCTCCCGCATCTACCCCAAGGGCCAGCGACTGGATTCC
TCCAACTACGATCCTTTGCCCATGTGGATCTGTGGCAGTCAGCTTGTGGCCCTCAACTTC
CAGACCCCTGACAAGCCTATGCAGATGAACCAGGCCCTCTTCATGACGGGCAGGCACTGT
GGCTACGTGCTGCAGCCAAGCACCATGCGGGATGAGGCCTTCGACCCCTTTGACAAGAGC
AGCCTCCGCGGGCTGGAGCCATGTGCCATCTCTATTGAGGTGCTGGGGGCCCGACATCTG
CCAAAGAATGGCCGAGGCATTGTGTGTCCTTTTGTGGAGATTGAGGTGGCTGGAGCTGAG
TATGACAGCACCAAGCAGAAGACAGAGTTTGTGGTGGACAATGGACTCAACCCTGTATGG
CCAGCCAAGCCCTTCCACTTCCAGATCAGTAACCCTGAATTTGCCTTTCTGCGCTTCGTG
GTGTATGAGGAAGACATGTTTAGTGACCAGAATTTCCTGGCTCAGGCTACTTTCCCAGTA
AAAGGCCTGAAGACAGGATACAGAGCAGTGCCTTTGAAGAACAACTACAGTGAGGACCTG
GAGTTGGCCTCCCTGCTGATCAAGATTGACATTTTCCCTGCCAAGGAGAATGGTGACCTC
AGTCCCTTCAGTGGTACGTCCCTGCGGGAGCGGGGCTCAGATGCCTCAGGCCAGCTGTTT
CATGGCCGAGCCCGGGAAGGCTCCTTTGAATCCCGCTACCAGCAGCCGTTTGAGGACTTC
CGCATCTCCCAGGAGCATCTCGCAGACCATTTTGACAGTCGAGAACGAAGGGCCCCAAGA
AGGACTCGGGTCAATGGAGACAACCGCCTCTAG
Enzyme 6 GenBank Gene ID M34667 Link Image
Enzyme 6 GeneCard ID PLCG1 Link Image
Enzyme 6 GenAtlas ID PLCG1 Link Image
Enzyme 6 HGNC ID HGNC:9065 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Burgess WH, Dionne CA, Kaplow J, Mudd R, Friesel R, Zilberstein A, Schlessinger J, Jaye M: Characterization and cDNA cloning of phospholipase C-gamma, a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase. Mol Cell Biol. 1990 Sep;10(9):4770-7. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. Zhang W, Sloan-Lancaster J, Kitchen J, Trible RP, Samelson LE: LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell. 1998 Jan 9;92(1):83-92. [PubMed Link Image]
  4. Felschow DM, Civin CI, Hoehn GT: Characterization of the tyrosine kinase Tnk1 and its binding with phospholipase C-gamma1. Biochem Biophys Res Commun. 2000 Jun 24;273(1):294-301. [PubMed Link Image]
  5. Kohda D, Hatanaka H, Odaka M, Mandiyan V, Ullrich A, Schlessinger J, Inagaki F: Solution structure of the SH3 domain of phospholipase C-gamma. Cell. 1993 Mar 26;72(6):953-60. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5479
Enzyme 7 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta 1
Enzyme 7 Synonyms
  1. Phosphoinositide phospholipase C
  2. PLC-delta-1
  3. Phospholipase C-delta-1
  4. PLC-III
Enzyme 7 Gene Name PLCD1
Enzyme 7 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta 1 
MDSGRDFLTLHGLQDDEDLQALLKGSQLLKVKSSSWRRERFYKLQEDCKTIWQESRKVMR
TPESQLFSIEDIQEVRMGHRTEGLEKFARDVPEDRCFSIVFKDQRNTLDLIAPSPADAQH
WVLGLHKIIHHSGSMDQRQKLQHWIHSCLRKADKNKDNKMSFKELQNFLKELNIQVDDSY
ARKIFRECDHSQTDSLEDEEIEAFYKMLTQRVEIDRTFAEAAGPGETLSVDQLVTFLQHQ
QREEAAGPALALSLIERYEPSETTKAQRQMTKDGFLMYLLSADGSAFSLAHRRVYQDMGQ
PLSHYLVSSSHNTYLLEDQLAGPSSTEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTF
TSKILFCDVLRAIRDYAFKASPYPVILSLENHCTLEQQRVMARHLHAILGPMLLNRPLDG
VTNSLPSPEQLKGKILLKGKKLGGLLPPGGEGGPEATVVSDEDEAAEMEDEAVRSRVQHK
PKEDKLRLAQELSDMVIYCKSVHFGGFSSPGTPGQAFYEMASFSENRALRLLQESGNGFV
RHNVGHLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYQDRFQDNGACG
YVLKPAFLRDPNGTFNPRALAQGPWWARKRLNIRVISGQQLPKVNKNKNSIVDPKVTVEI
HGVSRDVASRQTAVITNNGFNPWWDTEFAFEVVVPDLALIRFLVEDYDASSKNDFIGQST
IPLNSLKQGYRHVHLMSKNGDQHPSATLFVKISLQD
Enzyme 7 Number of Residues 756
Enzyme 7 Molecular Weight 85764
Enzyme 7 Theoretical pI 6.61
Enzyme 7 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes
Enzyme 7 Pathways
Enzyme 7 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 483920 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P51178 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PLCD1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2271 bp 
ATGGACTCGGGCCGGGACTTCCTGACCCTGCACGGCCTACAGGATGATGAGGATCTACAG
GCGCTGCTGAAGGGCAGCCAGCTCCTGAAGGTGAAGTCCAGCTCATGGAGGAGAGAGCGG
TTCTACAAGTTGCAGGAGGACTGCAAGACCATCTGGCAGGAGTCCCGCAAGGTCATGCGG
ACCCCGGAGTCCCAGCTGTTCTCCATCGAGGACATTCAGGAGGTGCGAATGGGGCACCGC
ACGGAGGGTCTGGAGAAGTTCGCCCGTGATGTGCCCGAGGACCGCTGCTTCTCCATTGTC
TTCAAGGACCAGCGCAATACACTAGACCTCATCGCCCCATCGCCAGCTGATGCCCAGCAC
TGGGTGCTGGGGCTGCACAAGATCATCCACCACTCAGGCTCCATGGACCAGCGTCAGAAG
CTACAGCACTGGATTCACTCCTGCTTGCGAAAAGCTGACAAAAACAAGGACAACAAGATG
AGCTTCAAGGAGCTGCAGAACTTCCTGAAGGAGCTCAACATCCAGGTGGACGACAGCTAT
GCCCGGAAGATCTTCAGGGAGTGTGACCACTCCCAGACAGACTCCCTGGAGGACGAGGAG
ATTGAGGCCTTCTACAAGATGCTGACCCAGCGGGTGGAGATCGACCGCACCTTCGCCGAG
GCCGCGGGCCCAGGGGAGACTCTGTCGGTGGATCAGTTAGTGACGTTCCTGCAGCACCAG
CAGCGGGAGGAGGCGGCAGGGCCTGCGCTGGCCCTCTCCCTCATTGAGCGCTACGAGCCC
AGCGAGACTACCAAGGCGCAGCGGCAGATGACCAAGGACGGCTTCCTCATGTACTTACTG
TCGGCTGACGGCAGCGCCTTCAGCCTGGCACACCGCCGTGTCTACCAGGACATGGGCCAG
CCACTTAGCCACTACCTGGTGTCCTCTTCACACAACACCTACCTGCTGGAGGACCAGCTA
GCCGGGCCCAGCAGCACTGAAGCCTACATCCGGGCACTGTGCAAAGGCTGCCGATGCCTG
GAGCTTGACTGCTGGGACGGGCCCAACCAGGAACCAATCATCTACCACGGCTATACTTTC
ACTTCCAAGATCCTCTTCTGCGATGTGCTCAGGGCCATCCGGGACTATGCCTTCAAGGCG
TCCCCCTACCCTGTCATCCTATCCCTGGAGAACCACTGCACACTGGAGCAGCAGCGCGTG
ATGGCGCGGCACCTGCATGCCATCCTGGGCCCCATGCTGTTGAACCGACCACTGGATGGG
GTCACCAACAGCCTGCCCTCCCCTGAGCAACTGAAGGGGAAGATCCTGCTGAAGGGGAAG
AAGCTCGGGGGGCTCCTCCCCCCTGGAGGGGAGGGTGGCCCTGAGGCCACTGTGGTGTCA
GACGAAGACGAGGCTGCTGAGATGGAGGATGAGGCAGTGAGGAGCCGTGTGCAGCACAAG
CCCAAGGAGGACAAGCTCAGGCTAGCACAGGAGCTCTCTGACATGGTCATTTACTGCAAG
AGTGTCCACTTTGGGGGCTTCTCCAGTCCTGGCACCCCTGGACAGGCCTTCTACGAGATG
GCGTCCTTCTCTGAGAACCGTGCCCTTCGACTGCTCCAAGAATCAGGAAACGGCTTTGTC
CGCCACAACGTGGGGCACCTGAGCAGAATATACCCGGCTGGATGGAGAACAGACTCCTCC
AACTACAGCCCCGTGGAGATGTGGAATGGGGGCTGCCAGATCGTGGCCCTGAATTTCCAG
ACACCTGGGCCAGAGATGGACGTGTACCAGGACCGCTTCCAGGACAACGGGGCCTGTGGG
TACGTGCTGAAGCCCGCCTTCCTGCGAGACCCCAACGGCACCTTTAACCCCCGCGCCCTG
GCTCAGGGGCCCTGGTGGGCACGGAAGCGGCTCAACATCAGGGTCATTTCGGGGCAGCAG
CTGCCAAAAGTCAACAAGAATAAGAATTCAATTGTGGACCCCAAAGTGACAGTGGAGATC
CATGGCGTGAGCCGGGACGTGGCCAGCCGCCAGACTGCTGTCATCACCAACAATGGTTTC
AACCCATGGTGGGACACGGAGTTTGCGTTTGAGGTAGTTGTGCCTGACCTTGCCCTCATC
CGCTTCTTGGTGGAAGATTATGATGCCTCCTCCAAGAATGACTTCATTGGCCAGAGTACC
ATCCCCTTGAACAGCCTCAAGCAAGGATACCGCCATGTCCACCTCATGTCTAAGAACGGG
GACCAGCATCCATCAGCCACCCTCTTTGTGAAGATCTCCCTCCAGGACTAG
Enzyme 7 GenBank Gene ID U09117 Link Image
Enzyme 7 GeneCard ID PLCD1 Link Image
Enzyme 7 GenAtlas ID PLCD1 Link Image
Enzyme 7 HGNC ID HGNC:9060 Link Image
Enzyme 7 Chromosome Location 3
Enzyme 7 Locus 3p22-p21.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Cheng HF, Jiang MJ, Chen CL, Liu SM, Wong LP, Lomasney JW, King K: Cloning and identification of amino acid residues of human phospholipase C delta 1 essential for catalysis. J Biol Chem. 1995 Mar 10;270(10):5495-505. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5829
Enzyme 8 Name N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
Enzyme 8 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class L protein
  2. PIG-L
Enzyme 8 Gene Name PIGL
Enzyme 8 Protein Sequence >N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase 
MEAMWLLCVALAVLAWGFLWVWDSSERMKSREQGGRLGAESRTLLVIAHPDDEAMFFAPT
VLGLARLRHWVYLLCFSAGNYYNQGETRKKELLQSCDVLGIPLSSVMIIDNRDFPDDPGM
QWDTEHVARVLLQHIEVNGINLVVTFDAGGVSGHSNHIALYAAVRALHSEGKLPKGCSVL
TLQSVNVLRKYISLLDLPLSLLHTQDVLFVLNSKEVAQAKKAMSCHRSQLLWFRRLYIIF
SRYMRINSLSFL
Enzyme 8 Number of Residues 252
Enzyme 8 Molecular Weight 28532
Enzyme 8 Theoretical pI 8.23
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Involved in the second step of GPI biosynthesis. De-N- acetylation of N-acetylglucosaminyl-phosphatidylinositol
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • 6-(N-acetyl-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-17
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 4239986 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9Y2B2 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PIGL_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >759 bp 
ATGGAAGCAATGTGGCTCCTGTGTGTGGCGTTGGCGGTCTTGGCATGGGGCTTCCTCTGG
GTTTGGGACTCCTCAGAACGAATGAAGAGTCGGGAGCAGGGAGGACGGCTGGGAGCCGAA
AGCCGGACCCTGCTGGTCATAGCGCACCCTGACGATGAAGCCATGTTTTTTGCTCCCACA
GTGCTAGGCTTGGCCCGCCTAAGGCACTGGGTGTACCTGCTTTGCTTCTCTGCAGGAAAT
TACTACAATCAAGGAGAGACTCGTAAGAAAGAACTTTTGCAGAGCTGTGATGTTTTGGGG
ATTCCACTCTCCAGTGTAATGATTATTGACAACAGGGATTTCCCAGATGACCCAGGCATG
CAGTGGGACACAGAGCACGTGGCCAGAGTCCTCCTTCAGCACATAGAAGTGAATGGCATC
AATCTGGTGGTGACTTTCGATGCAGGGGGAGTAAGTGGCCACAGCAATCACATTGCTCTG
TATGCAGCTGTGAGGGCCCTGCACTCAGAAGGGAAGTTACCTAAAGGGTGCTCTGTGCTC
ACGCTTCAGTCTGTGAATGTGCTGCGCAAGTACATCTCCCTTCTGGATCTGCCCTTGTCT
CTGCTTCATACGCAGGATGTCCTCTTCGTGCTCAACAGCAAAGAAGTGGCACAGGCCAAG
AAAGCCATGTCCTGCCACCGCAGCCAGCTCCTCTGGTTCCGCCGCCTCTACATTATCTTC
TCCCGGTACATGAGAATCAACTCACTGAGCTTCCTCTGA
Enzyme 8 GenBank Gene ID AB017165 Link Image
Enzyme 8 GeneCard ID PIGL Link Image
Enzyme 8 GenAtlas ID PIGL Link Image
Enzyme 8 HGNC ID HGNC:8966 Link Image
Enzyme 8 Chromosome Location 17
Enzyme 8 Locus 17p12-p11.2
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Watanabe R, Ohishi K, Maeda Y, Nakamura N, Kinoshita T: Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis. Biochem J. 1999 Apr 1;339 ( Pt 1):185-92. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6228
Enzyme 9 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
Enzyme 9 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class Q protein
  2. PIG-Q
  3. N-acetylglucosamyl transferase component GPI1
Enzyme 9 Gene Name PIGQ
Enzyme 9 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q 
MVLKAFFPTCCVSTDSGLLVGRWVPEQSSAVVLAVLHFPFIPIQVKQLLAQVRQASQVGV
AVLGTWCHCRQEPEESLGRFLESLGAVFPHEPWLRLCRERGGTFWSCEATHRQAPTAPGA
PGEDQVMLIFYDQRQVLLSQLHLPTVLPDRQAGATTASTGGLAAVFDTVARSEVLFRSDR
FDEGPVRLSHWQSEGVEASILAELARRASGPICLLLASLLSLVSAVSACRVFKLWPLSFL
GSKLSTCEQLRHRLEHLTLIFSTRKAENPAQLMRKANTVASVLLDVALGLMLLSWLHGRS
RIGHLADALVPVADHVAEELQHLLQWLMGAPAGLKMNRALDQVLGRFFLYHIHLWISYIH
LMSPFVEHILWHVGLSACLGLTVALSLLSDIIALLTFHIYCFYVYGARLYCLKIHGLSSL
WRLFRGKKWNVLRQRVDSCSYDLDQLFIGTLLFTILLFLLPTTALYYLVFTLLRLLVVAV
QGLIHLLVDLINSLPLYSLGLRLCRPYRLADKPTALQPRGAHLPPPQLWLPPQALLGRPV
PQAVPWGAHLPLEAERGQAGLRELLARLAPPHGHSQPSALPGWHQLSWRMSCALWTLLCA
PEHGRPCYHTLGLEVIGSEQMWGWPARLAALHHWHCLPWDPLPTCCGHHGGEHSNPRCPE
HCPMPTLCTQVQRVRPPQQPQVEGWSPWGLPSGSALAVGVEGPCQDEPPSPRHPLAPSAE
QHPASGGLKQSLTPVPSGPGPSLPEPHGVYLRMFPGEVAL
Enzyme 9 Number of Residues 760
Enzyme 9 Molecular Weight 84083
Enzyme 9 Theoretical pI 8.08
Enzyme 9 GO Classification
Function
  • UDP-glycosyltransferase activity
  • acetylglucosaminyltransferase activity
  • catalytic activity
  • phosphatidylinositol N-acetylglucosaminyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • GPI anchor biosynthesis
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein modification
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • 278-298 349-371 378-400 446-468 475-497
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 2623158 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9BRB3 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PIGQ_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1746 bp 
ATGGTGCTCAAGGCCTTCTTCCCCACGTGCTGCGTCTCGGCGGACAGCGGGCTGCTGGTG
GGACGGTGGGTGCCGGAGCAGAGCAGCGCCGTGGTCCTGGCGGTCCTGCACTTTCCCTTC
ATCCCCATCCAGGTCAAGCAGCTCCTGGCCCAGGTGCGGCAGGCCAGCCAGGTGGGCGTG
GCCGTGCTGGGCACCTGGTGCCACTGCCGGCAGGAGCCCGAGGAGAGCCTGGGCCGCTTC
CTGGAGAGCCTGGGTGCTGTCTTCCCCCATGAGCCCTGGCTGCGGCTGTGCCGGGAGAGA
GGCGGCACGTTCTGGAGCTGCGAGGCCACCCACCGGCAAGCGCCCACTGCCCCCGGTGCC
CCTGGTGAGGACCAGGTCATGCTCATCTTCTATGACCAGCGCCAGGTGTTGCTGTCACAG
CTACACCTGCCCACCGTCCTGCCCGACCGCCAGGCTGGAGCCACCACTGCCAGCACGGGG
GGCCTGGCTGCCGTCTTCGACACGGTAGCACGCAGTGAGGTGCTCTTCCGCAGTGACCGC
TTTGATGAGGGCCCCGTGCGGCTGAGCCACTGGCAGTCGGAGGGCGTGGAGGCCAGCATC
CTCGCGGAGCTGGCCAGGCGAGCCTCGGGACCCATTTGTCTGCTGTTGGCCAGCCTGCTG
TCGCTGGTCTCAGCTGTCAGTGCCTGCCGAGTGTTCAAGCTCTGGCCCCTGTCCTTCCTC
GGGAGCAAACTCTCCACGTGCGAACAGCTCCGGCACCGGCTGGAGCACCTCACGCTAATC
TTCAGTACACGGAAGGCGGAGAACCCTGCCCAGCTGATGAGGAAGGCCAACACGGTGGCC
TCTGTGCTGCTGGACGTGGCCCTGGGCCTCATGCTGCTGTCCTGGCTCCACGGGAGAAGC
CGCATCGGGCATCTGGCCGACGCCCTCGTTCCTGTGGCTGACCACGTGGCCGAGGAGCTC
CAGCATCTGCTGCAGTGGCTGATGGGTGCTCCCGCCGGGCTCAAGATGAACCGTGCACTG
GACCAGGTGCTGGGCCGCTTCTTCCTCTACCACATCCACCTGTGGATCAGCTACATCCAC
CTCATGTCCCCCTTCGTGGAGCACATCCTTTGGCACGTGGGCCTCTCGGCCTGCCTGGGC
CTGACGGTGGCCCTGTCCCTCCTCTCGGACATTATCGCCCTCCTCACCTTCCACATCTAC
TGCTTTTACGTCTATGGAGCCAGGCTGTACTGCCTGAAGATCCATGGCCTGTCCTCACTG
TGGCGTCTGTTCCGGGGGAAGAAGTGGAACGTTCTGCGCCAGCGCGTGGACTCCTGTTCC
TATGACCTGGACCAGCTGTTCATCGGGACTCTGCTCTTCACCATCCTGCTCTTCCTCCTG
CCTACCACAGCCCTGTACTACCTGGTGTTCACCCTGCTCCGGCTCCTGGTGGTCGCCGTG
CAGGGCCTGATCCATCTGCTGGTGGACCTCATCAACTCCCTGCCGCTGTACTCACTGGGT
CTTCGGCTCTGCCGGCCCTACAGGCTGGCGGCTGGCGTGAAGTTCCGTGTCCTCCGGCAC
GAGGCCAGCAGGCCCCTCCGCCTCCTGATGCAGATAAACCCACTGCCCTACAGCCGCGTG
GTGCACACCTACCGCCTCCCCAGCTGTGGCTGCCACCCCAAGCACTCCTGGGGCGCCCTG
TGCCGCAAGCTGTTCCTTGGGGAGCTCATCTACCCCTGGAGGCAGAGAGGGGACAAGCAG
GACTGA
Enzyme 9 GenBank Gene ID AF030177 Link Image
Enzyme 9 GeneCard ID PIGQ Link Image
Enzyme 9 GenAtlas ID PIGQ Link Image
Enzyme 9 HGNC ID HGNC:14135 Link Image
Enzyme 9 Chromosome Location 16
Enzyme 9 Locus 16p13.3
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Tiede A, Schubert J, Nischan C, Jensen I, Westfall B, Taron CH, Orlean P, Schmidt RE: Human and mouse Gpi1p homologues restore glycosylphosphatidylinositol membrane anchor biosynthesis in yeast mutants. Biochem J. 1998 Sep 15;334 ( Pt 3):609-16. [PubMed Link Image]
  2. Watanabe R, Inoue N, Westfall B, Taron CH, Orlean P, Takeda J, Kinoshita T: The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1. EMBO J. 1998 Feb 16;17(4):877-85. [PubMed Link Image]
  3. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  4. Watanabe R, Murakami Y, Marmor MD, Inoue N, Maeda Y, Hino J, Kangawa K, Julius M, Kinoshita T: Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2. EMBO J. 2000 Aug 15;19(16):4402-11. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6229
Enzyme 10 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
Enzyme 10 Synonyms
  1. GlcNAc-PI synthesis protein
  2. Phosphatidylinositol- glycan biosynthesis class A protein
  3. PIG-A
Enzyme 10 Gene Name PIGA
Enzyme 10 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit A 
MACRGGAGNGHRASATLSRVSPGSLYTCRTRTHNICMVSDFFYPNMGGVESHIYQLSQCL
IERGHKVIIVTHAYGNRKGIRYLTSGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRE
RVTIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNH
IICVSYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPFRRHDSITIVVVSRLVYRKGI
DLLSGIIPELCQKYPDLNFIIGGEGPKRIILEEVRERYQLHDRVRLLGALEHKDVRNVLV
QGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEPSVKSLCEGLE
KAIFQLKSGTLPAPENIHNIVKTFYTWRNVAERTEKVYDRVSVEAVLPMDKRLDRLISHC
GPVTGYIFALLAVFNFLFLIFLRWMTPDSIIDVAIDATGPRGAWTNNYSHSKRGGENNEI
SETR
Enzyme 10 Number of Residues 484
Enzyme 10 Molecular Weight 54127
Enzyme 10 Theoretical pI 8.41
Enzyme 10 GO Classification
Function
—
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
—
Enzyme 10 General Function Cell wall/membrane/envelope biogenesis
Enzyme 10 Specific Function Necessary for the synthesis of N-acetylglucosaminyl- phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • 422-442
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 219994 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P37287 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PIGA_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1455 bp 
ATGGCCTGTAGAGGAGGAGCTGGGAATGGCCACCGTGCCTCAGCTACACTCTCTCGGGTT
AGCCCTGGAAGTCTTTACACATGTAGAACCCGTACCCATAATATATGCATGGTATCTGAC
TTTTTCTACCCAAATATGGGAGGCGTGGAAAGCCACATTTACCAGCTCTCTCAGTGCCTG
ATTGAAAGAGGGCATAAGGTTATAATTGTCACCCATGCTTATGGAAATCGAAAAGGCATC
CGTTACCTCACCAGTGGCCTCAAAGTCTATTACTTGCCTCTGAAAGTCATGTACAACCAG
TCTACAGCCACGACCCTCTTTCACAGTCTGCCATTGCTCAGGTACATATTTGTTCGGGAG
AGAGTCACGATAATCCATTCACATAGTTCTTTTTCTGCTATGGCCCATGATGCTCTCTTC
CACGCCAAGACAATGGGGCTTCAGACAGTCTTCACGGACCATTCCCTTTTTGGATTTGCT
GATGTCAGCTCGGTGCTTACAAACAAGCTTCTAACCGTGTCTCTTTGTGATACAAACCAC
ATCATTTGTGTGTCTTATACTAGTAAGGAAAATACTGTACTAAGAGCAGCACTGAATCCT
GAAATAGTGTCCGTCATTCCTAATGCTGTAGATCCTACTGACTTCACTCCAGACCCATTT
AGAAGGCATGATAGTATAACTATTGTTGTTGTCAGCAGACTTGTTTACAGAAAAGGGATC
GATTTGCTTAGTGGTATAATACCTGAACTCTGTCAGAAATATCCAGATTTAAATTTCATA
ATTGGAGGAGAGGGACCAAAGAGAATCATTTTGGAAGAAGTTCGGGAAAGATACCAGCTG
CATGACAGGGTGCGTCTTTTGGGAGCTTTAGAACACAAGGATGTTAGAAATGTCTTAGTT
CAAGGACATATTTTTCTGAATACCTCCCTTACTGAAGCATTCTGCATGGCGATCGTGGAA
GCAGCCAGTTGTGGTTTACAGGTTGTAAGTACCAGAGTTGGTGGAATTCCTGAGGTGCTT
CCAGAAAACCTTATTATTTTATGTGAGCCTTCAGTAAAATCTTTGTGTGAAGGATTGGAA
AAGGCTATTTTCCAACTGAAGTCAGGGACATTGCCAGCTCCAGAAAACATCCATAACATA
GTAAAGACTTTCTACACCTGGAGGAATGTTGCAGAAAGAACTGAAAAGGTATATGACCGG
GTATCAGTGGAAGCTGTGTTGCCAATGGACAAACGACTGGACAGACTTATTTCTCACTGC
GGCCCAGTAACAGGCTACATCTTTGCTTTGTTGGCAGTTTTCAACTTCCTCTTCCTCATT
TTCTTGAGATGGATGACTCCAGATTCTATCATTGATGTTGCAATAGATGCCACTGGGCCA
CGGGGTGCCTGGACTAATAACTATTCTCACAGTAAAAGAGGGGGTGAGAATAATGAGATA
TCTGAAACCAGGTAG
Enzyme 10 GenBank Gene ID D11466 Link Image
Enzyme 10 GeneCard ID PIGA Link Image
Enzyme 10 GenAtlas ID PIGA Link Image
Enzyme 10 HGNC ID HGNC:8957 Link Image
Enzyme 10 Chromosome Location X
Enzyme 10 Locus Xp22.1
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Miyata T, Takeda J, Iida Y, Yamada N, Inoue N, Takahashi M, Maeda K, Kitani T, Kinoshita T: The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis. Science. 1993 Feb 26;259(5099):1318-20. [PubMed Link Image]
  2. Bessler M, Hillmen P, Longo L, Luzzatto L, Mason PJ: Genomic organization of the X-linked gene (PIG-A) that is mutated in paroxysmal nocturnal haemoglobinuria and of a related autosomal pseudogene mapped to 12q21. Hum Mol Genet. 1994 May;3(5):751-7. [PubMed Link Image]
  3. Iida Y, Takeda J, Miyata T, Inoue N, Nishimura J, Kitani T, Maeda K, Kinoshita T: Characterization of genomic PIG-A gene: a gene for glycosylphosphatidylinositol-anchor biosynthesis and paroxysmal nocturnal hemoglobinuria. Blood. 1994 Jun 1;83(11):3126-31. [PubMed Link Image]
  4. Yu J, Nagarajan S, Ueda E, Knez JJ, Petersen RB, Medof ME: Characterization of alternatively spliced PIG-A transcripts in normal and paroxysmal nocturnal hemoglobinuria cells. Braz J Med Biol Res. 1994 Feb;27(2):195-201. [PubMed Link Image]
  5. Takeda J, Miyata T, Kawagoe K, Iida Y, Endo Y, Fujita T, Takahashi M, Kitani T, Kinoshita T: Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria. Cell. 1993 May 21;73(4):703-11. [PubMed Link Image]
  6. Bessler M, Mason PJ, Hillmen P, Miyata T, Yamada N, Takeda J, Luzzatto L, Kinoshita T: Paroxysmal nocturnal haemoglobinuria (PNH) is caused by somatic mutations in the PIG-A gene. EMBO J. 1994 Jan 1;13(1):110-7. [PubMed Link Image]
  7. Ware RE, Rosse WF, Howard TA: Mutations within the Piga gene in patients with paroxysmal nocturnal hemoglobinuria. Blood. 1994 May 1;83(9):2418-22. [PubMed Link Image]
  8. Nafa K, Bessler M, Castro-Malaspina H, Jhanwar S, Luzzatto L: The spectrum of somatic mutations in the PIG-A gene in paroxysmal nocturnal hemoglobinuria includes large deletions and small duplications. Blood Cells Mol Dis. 1998 Sep;24(3):370-84. [PubMed Link Image]
  9. Yoon JH, Cho HI, Park SS, Chang YH, Kim BK: Mutation analysis of the PIG-A gene in Korean patients with paroxysmal nocturnal haemoglobinuria. J Clin Pathol. 2002 Jun;55(6):410-3. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6230
Enzyme 11 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
Enzyme 11 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class H protein
  2. PIG-H
Enzyme 11 Gene Name PIGH
Enzyme 11 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit H 
MEDERSFSDICGGRLALQRRYYSPSCREFCLSCPRLSLRSLTAVTCTVWLAAYGLFTLCE
NSMILSAAIFITLLGLLGYLHFVKIDQETLLIIDSLGIQMTSSYASGKESTTFIEMGKVK
DIVINEAIYMQKVIYYLCILLKDPVEPHGISQVVPVFQSAKPRLDCLIEVYRSCQEILAH
QKATSTSP
Enzyme 11 Number of Residues 188
Enzyme 11 Molecular Weight 21081
Enzyme 11 Theoretical pI 6.72
Enzyme 11 GO Classification Not Available
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
Enzyme 11 Pfam Domain Function Not Available
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • 36-58
  • 63-83
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 404726 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q14442 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name PIGH_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >567 bp 
ATGGAGGATGAGCGGAGCTTTTCGGATATCTGCGGCGGCCGCCTGGCGCTGCAGCGCCGC
TACTACTCCCCGTCCTGCCGGGAATTCTGCCTCAGCTGCCCTCGGCTCTCGCTGCGTTCG
CTCACCGCTGTCACCTGCACGGTGTGGCTGGCGGCCTACGGACTCTTCACCCTCTGCGAG
AACAGCATGATCCTCTCTGCTGCCATCTTCATCACCCTCTTAGGTCTGCTTGGTTATCTC
CATTTTGTGAAGATTGATCAGGAGACTCTGTTAATCATTGATTCCCTTGGCATTCAGATG
ACTTCATCTTATGCTTCAGGCAAAGAAAGCACTACCTTCATAGAAATGGGCAAGGTCAAG
GATATTGTCATCAATGAGGCCATTTACATGCAGAAGGTGATTTACTACCTCTGCATCTTA
TTGAAAGATCCAGTGGAACCACATGGGATATCCCAAGTAGTACCCGTCTTCCAGAGTGCC
AAGCCCCGGCTGGACTGCTTGATTGAAGTATACAGGAGCTGCCAGGAGATCCTGGCACAC
CAGAAAGCCACATCAACAAGCCCATGA
Enzyme 11 GenBank Gene ID L19783 Link Image
Enzyme 11 GeneCard ID PIGH Link Image
Enzyme 11 GenAtlas ID PIGH Link Image
Enzyme 11 HGNC ID HGNC:8964 Link Image
Enzyme 11 Chromosome Location 14
Enzyme 11 Locus 14q11-q24
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Kamitani T, Chang HM, Rollins C, Waneck GL, Yeh ET: Correction of the class H defect in glycosylphosphatidylinositol anchor biosynthesis in Ltk- cells by a human cDNA clone. J Biol Chem. 1993 Oct 5;268(28):20733-6. [PubMed Link Image]
  2. Watanabe R, Inoue N, Westfall B, Taron CH, Orlean P, Takeda J, Kinoshita T: The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1. EMBO J. 1998 Feb 16;17(4):877-85. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6232
Enzyme 12 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
Enzyme 12 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class C protein
  2. PIG-C
Enzyme 12 Gene Name PIGC
Enzyme 12 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit C 
MYAQPVTNTKEVKWQKVLYERQPFPDNYVDRRFLEELRKNIHARKYQYWAVVFESSVVIQ
QLCSVCVFVVIWWYMDEGLLAPHWLLGTGLASSLIGYVLFDLIDGGEGRKKSGQTRWADL
KSALVFITFTYGFSPVLKTLTESVSTDTIYAMSVFMLLGHLIFFDYGANAAIVSSTLSLN
MAIFASVCLASRLPRSLHAFIMVTFAIQIFALWPMLQKKLKACTPRSYVGVTLLFAFSAV
GGLLSISAVGAVLFALLLMSISCLCPFYLIRLQLFKENIHGPWDEAEIKEDLSRFLS
Enzyme 12 Number of Residues 297
Enzyme 12 Molecular Weight 33583
Enzyme 12 Theoretical pI 8.55
Enzyme 12 GO Classification
Function
  • UDP-glycosyltransferase activity
  • acetylglucosaminyltransferase activity
  • catalytic activity
  • phosphatidylinositol N-acetylglucosaminyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • GPI anchor biosynthesis
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein modification
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 51-71 80-100 154-174 239-259
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 1620890 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q92535 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name PIGC_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >894 bp 
ATGTATGCTCAACCTGTGACTAACACCAAGGAGGTCAAGTGGCAGAAGGTCTTGTATGAG
CGACAGCCCTTTCCTGATAACTATGTGGACCGGCGATTCCTGGAAGAGCTCCGGAAAAAC
ATCCATGCTCGGAAATACCAATATTGGGCTGTGGTATTTGAGTCCAGTGTGGTGATCCAG
CAGCTGTGCAGTGTTTGTGTTTTTGTGGTTATCTGGTGGTATATGGATGAGGGTCTTCTG
GCCCCCCATTGGCTTTTAGGGACTGGCCTGGCTTCTTCACTGATTGGGTATGTTTTGTTT
GATCTCATTGATGGAGGTGAAGGGCGGAAGAAGAGTGGGCAGACCCGGTGGGCTGACCTG
AAGAGTGCCCTAGTCTTCATTACTTTCACTTATGGGTTTTCACCAGTGCTGAAGACCCTT
ACAGAGTCTGTCAGCACTGACACCATCTATGCCATGTCAGTCTTCATGCTGTTAGGCCAT
CTCATCTTTTTTGACTATGGTGCCAATGCTGCCATTGTATCCAGCACACTATCCTTGAAC
ATGGCCATCTTTGCTTCTGTATGCTTGGCATCACGTCTTCCCCGGTCCCTGCATGCCTTC
ATCATGGTGACATTTGCCATTCAGATTTTTGCCCTGTGGCCCATGTTGCAGAAGAAACTA
AAGGCATGTACTCCCCGGAGCTATGTGGGGGTCACACTGCTTTTTGCATTTTCAGCCGTG
GGAGGCCTACTGTCCATTAGTGCTGTGGGAGCCGTACTCTTTGCCCTTCTGCTGATGTCT
ATCTCATGTCTGTGTCCATTCTACCTCATTCGCTTGCAGCTTTTTAAAGAAAACATTCAT
GGGCCTTGGGATGAAGCTGAAATCAAGGAAGACTTGTCCAGGTTCCTCAGTTAA
Enzyme 12 GenBank Gene ID D85418 Link Image
Enzyme 12 GeneCard ID PIGC Link Image
Enzyme 12 GenAtlas ID PIGC Link Image
Enzyme 12 HGNC ID HGNC:8960 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 1q23-q25
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Inoue N, Watanabe R, Takeda J, Kinoshita T: PIG-C, one of the three human genes involved in the first step of glycosylphosphatidylinositol biosynthesis is a homologue of Saccharomyces cerevisiae GPI2. Biochem Biophys Res Commun. 1996 Sep 4;226(1):193-9. [PubMed Link Image]
  2. Hong Y, Ohishi K, Inoue N, Endo Y, Fujita T, Takeda J, Kinoshita T: Structures and chromosomal localizations of the glycosylphosphatidylinositol synthesis gene PIGC and its pseudogene PIGCP1. Genomics. 1997 Sep 15;44(3):347-9. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6427
Enzyme 13 Name Probable phospholipid-transporting ATPase IG
Enzyme 13 Synonyms
  1. ATPase class I type 11C
  2. ATPase IG
  3. ATPase IQ
  4. ATPase class VI type 11C
Enzyme 13 Gene Name ATP11C
Enzyme 13 Protein Sequence >Probable phospholipid-transporting ATPase IG 
MQMVPSLPPASECAGEEKRVGTRTVFVGNHPVSETEAYIAQRFCDNRIVSSKYTLWNFLP
KNLFEQFRRIANFYFLIIFLVQVTVDTPTSPVTSGLPLFFVITVTAIKQGYEDCLRHRAD
NEVNKSTVYIIENAKRVRKESEKIKVGDVVEVQADETFPCDLILLSSCTTDGTCYVTTAS
LDGESNCKTHYAVRDTIALCTAESIDTLRAAIECEQPQPDLYKFVGRINIYSNSLEAVAR
SLGPENLLLKGATLKNTEKIYGVAVYTGMETKMALNYQGKSQKRSAVEKSINAFLIVYLF
ILLTKAAVCTTLKYVWQSTPYNDEPWYNQKTQKERETLKVLKMFTDFLSFMVLFNFIIPV
SMYVTVEMQKFLGSFFISWDKDFYDEEINEGALVNTSDLNEELGQVDYVFTDKTGTLTEN
SMEFIECCIDGHKYKGVTQEVDGLSQTDGTLTYFDKVDKNREELFLRALCLCHTVEIKTN
DAVDGATESAELTYISSSPDEIALVKGAKRYGFTFLGNRNGYMRVENQRKEIEEYELLHT
LNFDAVRRRMSVIVKTQEGDILLFCKGADSAVFPRVQNHEIELTKVHVERNAMDGYRTLC
VAFKEIAPDDYERINRQLIEAKMALQDREEKMEKVFDDIETNMNLIGATAVEDKLQDQAA
ETIEALHAAGLKVWVLTGDKMETAKSTCYACRLFQTNTELLELTTKTIEESERKEDRLHE
LLIEYRKKLLHEFPKSTRSFKKAWTEHQEYGLIIDGSTLSLILNSSQDSSSNNYKSIFLQ
ICMKCTAVLCCRMAPLQKAQIVRMVKNLKGSPITLSIGDGANDVSMILESHVGIGIKGKE
GRQAARNSDYSVPKFKHLKKLLLAHGHLYYVRIAHLVQYFFYKNLCFILPQFLYQFFCGF
SQQPLYDAAYLTMYNICFTSLPILAYSLLEQHINIDTLTSDPRLYMKISGNAMLQLGPFL
YWTFLAAFEGTVFFFGTYFLFQTASLEENGKVYGNWTFGTIVFTVLVFTVTLKLALDTRF
WTWINHFVIWGSLAFYVFFSFFWGGIIWPFLKQQRMYFVFAQMLSSVSTWLAIILLIFIS
LFPEILLIVLKNVRRRSARRNLSCRRASDSLSARPSVRPLLLRTFSDESNVL
Enzyme 13 Number of Residues 1132
Enzyme 13 Molecular Weight 129479
Enzyme 13 Theoretical pI 6.63
Enzyme 13 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion transporter activity
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • transporter activity
Process
  • cation transport
  • cellular physiological process
  • ion transport
  • metabolism
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 13 General Function Inorganic ion transport and metabolism
Enzyme 13 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • 67-85 87-107 291-311 347-367 880-900 909-929 956-976 996-1016 1027-1047 1070-1090
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 39573513 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q8NB49 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name AT11C_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >3399 bp 
ATGCAGATGGTCCCATCTCTCCCTCCAGCCTCTGAGTGTGCTGGAGAAGAGAAACGAGTT
GGCACACGCACAGTGTTTGTTGGCAATCATCCAGTTTCGGAAACAGAAGCTTACATTGCA
CAAAGATTTTGTGATAATAGAATAGTCTCATCTAAGTATACACTTTGGAATTTTCTCCCA
AAGAATCTGTTTGAACAGTTTAGAAGAATTGCAAATTTTTATTTTCTCATAATCTTCCTT
GTACAGGTCACAGTAGACACACCAACTAGCCCAGTTACCAGTGGACTTCCACTTTTCTTT
GTTATAACTGTTACAGCCATCAAGCAGGGATATGAGGATTGGCTGAGACACAGAGCTGAC
AATGAAGTCAACAAAAGCACTGTTTACATTATTGAAAATGCAAAGCGAGTGAGAAAAGAA
AGTGAAAAAATCAAGGTTGGTGATGTAGTAGAAGTACAGGCAGATGAAACCTTTCCCTGT
GATCTTATTCTTCTATCATCTTGCACCACTGATGGAACCTGTTATGTCACTACAGCCAGT
CTTGATGGGGAATCCAATTGCAAGACACATTATGCAGTACGTGATACCATTGCACTGTGT
ACAGCAGAATCCATCGATACCCTCCGAGCAGCAATTGAATGTGAACAGCCTCAACCTGAC
CTCTACAAATTTGTTGGGCGAATCAATATCTACAGTAATAGTCTTGAGGCTGTTGCCAGG
TCTTTGGGACCTGAAAATCTCTTGCTGAAAGGAGCTACGCTAAAAAATACCGAGAAGATA
TATGGAGTTGCTGTTTACACTGGAATGGAAACCAAAATGGCTTTGAACTACCAAGGGAAA
TCTCAGAAACGTTCTGCTGTTGAAAAATCTATTAATGCTTTCCTGATTGTATATTTATTT
ATCTTACTGACCAAAGCTGCAGTATGCACTACTCTAAAGTATGTTTGGCAAAGTACCCCA
TACAATGATGAACCTTGGTATAACCAAAAGACTCAGAAAGAGCGAGAGACCTTGAAGGTT
TTAAAAATGTTCACCGACTTCCTATCATTTATGGTTCTATTCAACTTTATCATTCCTGTC
TCCATGTACGTCACAGTAGAAATGCAGAAATTCTTGGGCTCCTTCTTCATCTCATGGGAT
AAGGACTTTTATGATGAAGAAATTAATGAAGGAGCCCTGGTTAACACATCAGACCTTAAT
GAAGAACTTGGTCAGGTGGATTATGTATTTACAGATAAGACTGGAACACTCACTGAAAAC
AGCATGGAATTCATTGAATGCTGCATAGATGGCCACAAATATAAAGGTGTAACTCAAGAG
GTTGATGGATTATCTCAAACTGATGGAACTTTAACATATTTTGACAAAGTAGATAAGAAT
CGAGAAGAGCTGTTTCTACGTGCCTTGTGTTTATGTCATACTGTAGAAATCAAAACAAAC
GATGCTGTTGATGGAGCTACAGAATCAGCTGAATTAACCTATATCTCCTCTTCACCAGAT
GAAATAGCTTTGGTGAAAGGAGCTAAAAGGTACGGGTTCACATTTTTAGGAAATCGAAAT
GGATATATGAGAGTAGAGAACCAAAGAAAAGAAATAGAAGAATATGAACTTCTTCACACC
TTAAACTTTGATGCTGTCCGGCGACGTATGAGTGTAATTGTGAAGACTCAAGAAGGAGAC
ATACTTCTCTTTTGTAAAGGAGCAGACTCGGCAGTTTTTCCCAGAGTGCAAAATCATGAA
ATTGAGTTAACTAAAGTCCATGTGGAACGTAATGCAATGGATGGGTATCGGACACTCTGT
GTAGCCTTCAAAGAAATTGCTCCAGATGATTATGAAAGAATTAACAGACAGCTCATAGAG
GCAAAAATGGCCTTACAAGACAGAGAAGAAAAAATGGAAAAAGTTTTCGATGATATTGAG
ACAAACATGAATTTAATTGGAGCCACTGCAGTTGAAGACAAGCTACAAGATCAAGCTGCA
GAGACCATTGAAGCTCTGCATGCAGCAGGCCTGAAAGTCTGGGTGCTCACTGGGGACAAG
ATGGAGACAGCTAAATCCACATGCTATGCCTGCCGCCTTTTCCAGACCAACACTGAGCTC
TTAGAACTAACCACAAAAACCATTGAAGAAAGTGAAAGGAAAGAAGATCGATTACATGAA
TTATTGATAGAATATCGCAAGAAATTGCTGCATGAGTTTCCTAAAAGTACTAGAAGCTTT
AAAAAAGCATGGACAGAACATCAGGAATATGGATTAATCATAGATGGCTCCACATTGTCA
CTCATACTAAATTCTAGTCAAGACTCTAGTTCAAACAATTACAAAAGCATTTTCCTACAA
ATATGTATGAAGTGTACTGCAGTGCTCTGCTGTCGGATGGCACCATTACAGAAAGCCCAG
ATTGTCAGAATGGTGAAGAATTTAAAAGGCAGCCCAATAACTCTGTCGATAGGTGATGGT
GCCAATGATGTTAGTATGATCTTGGAATCCCATGTGGGAATAGGTATTAAAGGCAAAGAA
GGTCGCCAAGCAGCTAGGAATAGCGATTATTCTGTTCCAAAGTTTAAACACTTAAAGAAA
CTGCTGTTGGCTCATGGACATCTATATTATGTGAGAATAGCACACCTTGTACAGTACTTC
TTCTATAAGAACCTTTGTTTCATTTTGCCACAGTTTTTGTACCAGTTCTTCTGTGGATTC
TCACAACAGCCACTGTATGATGCTGCTTACCTTACAATGTACAATATCTGCTTCACATCC
TTGCCCATCCTGGCCTATAGTCTACTGGAACAGCACATCAACATTGACACTCTGACCTCA
GATCCCCGATTGTATATGAAAATTTCTGGCAATGCCATGCTACAGTTGGGCCCCTTCTTA
TATTGGACATTTCTGGCTGCCTTTGAAGGGACAGTGTTCTTCTTTGGGACTTACTTTCTT
TTTCAGACTGCATCCCTAGAAGAAAATGGAAAGGTATACGGAAACTGGACTTTTGGAACC
ATTGTTTTTACAGTCTTAGTATTCACTGTAACCCTGAAGCTTGCCTTGGATACCCGATTC
TGGACGTGGATAAATCACTTTGTGATTTGGGGTTCTTTAGCCTTCTATGTATTTTTCTCA
TTCTTCTGGGGAGGAATTATTTGGCCTTTTCTCAAGCAACAGAGAATGTATTTTGTATTT
GCCCAAATGCTGTCTTCTGTATCCACATGGTTGGCTATAATTCTTCTAATATTTATCAGC
CTGTTCCCTGAGATTCTTCTGATAGTATTAAAGAATGTAAGAAGAAGAAGTGCCAGGAGA
AATCTGAGCTGTAGAAGGGCATCTGACTCATTATCCGCCAGACCTTCAGTCAGACCTCTT
CTTTTACGAACATTCTCAGACGAATCTAATGTATTGTAA
Enzyme 13 GenBank Gene ID AJ580093 Link Image
Enzyme 13 GeneCard ID ATP11C Link Image
Enzyme 13 GenAtlas ID ATP11C Link Image
Enzyme 13 HGNC ID HGNC:13554 Link Image
Enzyme 13 Chromosome Location X
Enzyme 13 Locus Xq27.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 6428
Enzyme 14 Name Probable phospholipid-transporting ATPase IH
Enzyme 14 Synonyms
  1. ATPase class I type 11A
  2. ATPase IS
Enzyme 14 Gene Name ATP11A
Enzyme 14 Protein Sequence >Probable phospholipid-transporting ATPase IH 
MDCSLVRTLVHRYCAGEENWVDSRTIYVGHREPPPGAEAYIPQRYPDNRIVSSKYTFWNF
IPKNLFEQFRRVANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHK
ADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTT
ASLDGESSHKTHYAVQDTKGFHTEEDIGGLHATIECEQPQPDLYKFVGRINVYSDLNDPV
VRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNAFLIVY
LCILISKALINTVLKYMWQSEPFRDEPWYNQKTESERQRNLFLKAFTDFLAFMVLFNYII
PVSMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLT
ENNMEFKECCIEGHVYVPHVICNGQVLPESSGIDMIDSSPSVNGREREELFFRALCLCHT
VQVKDDDSVDGPRKSPDGGKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEILNREN
HIERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPRVIEGKVDQIRARVER
NAVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATA
VEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLLELTTKRIEE
QSLHDVLFELSKTVLRHSGSLTRDNLSGLSADMQDYGLIIDGAALSLIMKPREDGSSGNY
RELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEHPITLAIGDGANDVSMILEAHVGI
GVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLY
QFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALL
RWRVFIYWTLLGLFDALVFFFGAYFVFENTTVTSNGQIFGNWTFGTLVFTVMVFTVTLKL
ALDTHYWTWINHFVIWGSLLFYVVFSLLWGGVIWPFLNYQRMYYVFIQMLSSGPAWLAIV
LLVTISLLPDVLKKVLCRQLWPTATERVQTKSQCLSVEQSTIFMLSQTSSSLSF
Enzyme 14 Number of Residues 1134
Enzyme 14 Molecular Weight 129757
Enzyme 14 Theoretical pI 6.58
Enzyme 14 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion transporter activity
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • transporter activity
Process
  • cation transport
  • cellular physiological process
  • ion transport
  • metabolism
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 14 General Function Inorganic ion transport and metabolism
Enzyme 14 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • 62-82 89-110 297-318 350-372 882-902 915-934 965-986 1001-1023 1030-1050 1069-1093
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 55664449 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P98196 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name AT11A_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >414 bp 
ATATTTGGAAACTGGACGTTTGGAACGCTGGTATTCACCGTGATGGTGTTCACAGTTACA
CTAAAGCTTGCATTGGACACACACTACTGGACTTGGATCAACCATTTTGTCATCTGGGGG
TCGCTGCTGTTCTACGTTGTCTTTTCGCTTCTCTGGGGAGGAGTGATCTGGCCGTTCCTC
AACTACCAGAGGATGTACTACGTGTTCATCCAGATGCTGTCCAGCGGGCCCGCCTGGCTG
GCCATCGTGCTGCTGGTGACCATCAGCCTCCTTCCCGACGTCCTCAAGAAAGTCCTGTGC
CGGCAGCTGTGGCCAACAGCAACAGAGAGAGTCCAGACTAAGAGCCAGTGCCTTTCTGTC
GAGCAGTCAACCATCTTTATGCTTTCTCAGACTTCCAGCAGCCTGAGTTTCTGA
Enzyme 14 GenBank Gene ID AL356740 Link Image
Enzyme 14 GeneCard ID ATP11A Link Image
Enzyme 14 GenAtlas ID ATP11A Link Image
Enzyme 14 HGNC ID HGNC:13552 Link Image
Enzyme 14 Chromosome Location 13
Enzyme 14 Locus 13q34
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 6439
Enzyme 15 Name Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta isoform
Enzyme 15 Synonyms
  1. PI3-kinase p110 subunit delta
  2. PtdIns-3- kinase p110
  3. PI3K
  4. p110delta
Enzyme 15 Gene Name PIK3CD
Enzyme 15 Protein Sequence >Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta isoform 
MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFH
MLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLL
IGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGP
GTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYT
LQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPR
AKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSS
SEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAW
ANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAP
HPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQE
HFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSL
RKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSV
ALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMR
QEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKN
GDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLN
KSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIM
IRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYC
ERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFN
EALRESWKTKVNWLAHNVSKDNRQ
Enzyme 15 Number of Residues 1044
Enzyme 15 Molecular Weight 119481
Enzyme 15 Theoretical pI 7.18
Enzyme 15 GO Classification
Function
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • kinase activity
  • lipid kinase activity
  • phosphatidylinositol 3-kinase activity
  • phosphoinositide 3-kinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cell communication
  • cellular process
  • signal transduction
Component
  • phosphoinositide 3-kinase complex
  • protein complex
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function ATP + 1-phosphatidyl-1D-myo-inositol 4,5- bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5- trisphosphate
Enzyme 15 Pathways
Enzyme 15 Reactions
  • ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 37496959 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID O00329 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name PK3CD_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >3135 bp 
ATGCCCCCTGGGGTGGACTGCCCCATGGAATTCTGGACCAAGGAGGAGAATCAGAGCGTT
GTGGTTGACTTCCTGCTGCCCACAGGGGTCTACCTGAACTTCCCTGTGTCCCGCAATGCC
AACCTCAGCACCATCAAGCAGCTGCTGTGGCACCGCGCCCAGTATGAGCCGCTCTTCCAC
ATGCTCAGTGGCCCCGAGGCCTATGTGTTCACCTGCATCAACCAGACAGCGGAGCAGCAA
GAGCTGGAGGACGAGCAACGGCGTCTGTGTGACGTGCAGCCCTTCCTGCCCGTCCTGCGC
CTGGTGGCCCGTGAGGGCGACCGCGTGAAGAAGCTCATCAACTCACAGATCAGCCTCCTC
ATCGGCAAAGGCCTCCACGAGTTTGACTCCTTGTGCGACCCAGAAGTGAACGACTTTCGC
GCCAAGATGTGCCAATTCTGCGAGGAGGCGGCCGCCCGCCGGCAGCAGCTGGGCTGGGAG
GCCTGGCTGCAGTACAGTTTCCCCCTGCAGCTGGAGCCCTCGGCTCAAACCTGGGGGCCT
GGTACCCTGCGGCTCCCGAACCGGGCCCTTCTGGTCAACGTTAAGTTTGAGGGCAGCGAG
GAGAGCTTCACCTTCCAGGTGTCCACCAAGGACGTGCCGCTGGCGCTGATGGCCTGTGCC
CTGCGGAAGAAGGCCACAGTGTTCCGGCAGCCGCTGGTGGAGCAGCCGGAAGACTACACG
CTGCAGGTGAACGGCAGGCATGAGTACCTGTATGGCAGCTACCCGCTCTGCCAGTTCCAG
TACATCTGCAGCTGCCTGCACAGTGGGTTGACCCCTCACCTGACCATGGTCCATTCCTCC
TCCATCCTCGCCATGCGGGATGAGCAGAGCAACCCTGCCCCCCAGGTCCAGAAACCGCGT
GCCAAACCACCTCCCATTCCTGCGAAGAAGCCTTCCTCTGTGTCCCTGTGGTCCCTGGAG
CAGCCGTTCCGCATCGAGCTCATCCAGGGCAGCAAAGTGAACGCCGACGAGCGGATGAAG
CTGGTGGTGCAGGCCGGGCTTTTCCACGGCAACGAGATGCTGTGCAAGACGGTGTCCAGC
TCGGAGGTGAGCGTGTGCTCGGAGCCCGTGTGGAAGCAGCGGCTGGAGTTCGACATCAAC
ATCTGCGACCTGCCCCGCATGGCCCGTCTCTGCTTTGCGCTGTACGCCGTGATCGAGAAA
GCCAAGAAGGCTCGCTCCACCAAGAAGAAGTCCAAGAAGGCGGACTGCCCCATTGCCTGG
GCCAACCTCATGCTGTTTGACTACAAGGACCAGCTTAAGACCGGGGAACGCTGCCTCTAC
ATGTGGCCCTCCGTCCCAGATGAGAAGGGCGAGCTGCTGAACCCCACGGGCACTGTGCGC
AGTAACCCCAACACGGATAGCGCCGCTGCCCTGCTCATCTGCCTGCCCGAGGTGGCCCCG
CACCCCGTGTACTACCCCGCCCTGGAGAAGATCTTGGAGCTGGGGCGACACAGCGAGTGT
GTGCATGTCACCGAGGAGGAGCAGCTGCAGCTGCGGGAAATCCTGGAGCGGCGGGGGTCT
GGGGAGCTGTATGAGCACGAGAAGGACCTGGTGTGGAAGCTGCGGCATGAAGTCCAGGAG
CACTTCCCGGAGGCGCTAGCCCGGCTGCTGCTGGTCACCAAGTGGAACAAGCATGAGGAT
GTGGCCCAGATGCTCTACCTGCTGTGCTCCTGGCCGGAGCTGCCCGTCCTGAGCGCCCTG
GAGCTGCTAGACTTCAGCTTCCCCGATTGCCACGTAGGCTCCTTCGCCATCAAGTCGCTG
CGGAAACTGACGGACGATGAGCTGTTCCAGTACCTGCTGCAGCTGGTGCAGGTGCTCAAG
TACGAGTCCTACCTGGACTGCGAGCTGACCAAATTCCTGCTGGACCGGGCCCTGGCCAAC
CGCAAGATCGGCCACTTCCTTTTCTGGCACCTCCGCTCCGAGATGCACGTGCCGTCGGTG
GCCCTGCGCTTCGGCCTCATCCTGGAGGCCTACTGCAGGGGCAGCACCCACCACATGAAG
GTGCTGATGAAGCAGGGGGAAGCACTGAGCAAACTGAAGGCCCTGAATGACTTCGTCAAG
CTGAGCTCTCAGAAGACCCCCAAGCCCCAGACCAAGGAGCTGATGCACTTGTGCATGCGG
CAGGAGGCCTACCTAGAGGCCCTCTCCCACCTGCAGTCCCCACTCGACCCCAGCACCCTG
CTGGCTGAAGTCTGCGTGGAGCAGTGCACCTTCATGGACTCCAAGATGAAGCCCCTGTGG
ATCATGTACAGCAACGAGGAGGCAGGCAGCGGCGGCAGCGTGGGCATCATCTTTAAGAAC
GGGGATGACCTCCGGCAGGACATGCTGACCCTGCAGATGATCCAGCTCATGGACGTCCTG
TGGAAGCAGGAGGGGCTGGACCTGAGGATGACCCCCTATGGCTGCCTCCCCACCGGGGAC
CGCACAGGCCTCATTGAGGTGGTACTCCGTTCAGACACCATCGCCAACATCCAACTCAAC
AAGAGCAACATGGCAGCCACAGCCGCCTTCAACAAGGATGCCCTGCTCAACTGGCTGAAG
TCCAAGAACCCGGGGGAGGCCCTGGATCGAGCCATTGAGGAGTTCACCCTCTCCTGTGCT
GGCTATTGTGTGGCCACATATGTGCTGGGCATTGGCGATCGGCACAGCGACAACATCATG
ATCCGAGAGAGTGGGCAGCTGTTCCACATTGATTTTGGCCACTTTCTGGGGAATTTCAAG
ACCAAGTTTGGAATCAACCGCGAGCGTGTCCCATTCATCCTCACCTACGACTTTGTCCAT
GTGATTCAGCAGGGGAAGACTAATAATAGTGAGAAATTTGAACGGTTCCGGGGCTACTGT
GAAAGGGCCTACACCATCCTGCGGCGCCACGGGCTTCTCTTCCTCCACCTCTTTGCCCTG
ATGCGGGCGGCAGGCCTGCCTGAGCTCAGCTGCTCCAAAGACATCCAGTATCTCAAGGAC
TCCCTGGCACTGGGGAAAACAGAGGAGGAGGCACTGAAGCACTTCCGAGTGAAGTTTAAC
GAAGCCCTCCGTGAGAGCTGGAAAACCAAAGTGAACTGGCTGGCCCACAACGTGTCCAAA
GACAACAGGCAGTAG
Enzyme 15 GenBank Gene ID Y10055 Link Image
Enzyme 15 GeneCard ID PIK3CD Link Image
Enzyme 15 GenAtlas ID PIK3CD Link Image
Enzyme 15 HGNC ID HGNC:8977 Link Image
Enzyme 15 Chromosome Location 1
Enzyme 15 Locus 1p36.2
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Vanhaesebroeck B, Welham MJ, Kotani K, Stein R, Warne PH, Zvelebil MJ, Higashi K, Volinia S, Downward J, Waterfield MD: P110delta, a novel phosphoinositide 3-kinase in leukocytes. Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4330-5. [PubMed Link Image]
  2. Chantry D, Vojtek A, Kashishian A, Holtzman DA, Wood C, Gray PW, Cooper JA, Hoekstra MF: p110delta, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes. J Biol Chem. 1997 Aug 1;272(31):19236-41. [PubMed Link Image]
  3. Vanhaesebroeck B, Higashi K, Raven C, Welham M, Anderson S, Brennan P, Ward SG, Waterfield MD: Autophosphorylation of p110delta phosphoinositide 3-kinase: a new paradigm for the regulation of lipid kinases in vitro and in vivo. EMBO J. 1999 Mar 1;18(5):1292-302. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 6465
Enzyme 16 Name Probable phospholipid-transporting ATPase VA
Enzyme 16 Synonyms
  1. ATPVA
  2. Aminophospholipid translocase VA
Enzyme 16 Gene Name ATP10A
Enzyme 16 Protein Sequence >Probable phospholipid-transporting ATPase VA 
MEREPAGTEEPGPPGRRRRREGRTRTVRSNLLPPPGAEDPAAGAAKGERRRRRGCAQHLA
DNRLKTTKYTLLSFLPKNLFEQFHRPANVYFVFIALLNFVPAVNAFQPGLALAPVLFILA
ITAFRDLWEDYSRHRSDHKINHLGCLVFSREEKKYVNRFWKEIHVGDFVRLRCNEIFPAD
ILLLSSSDPDGLCHIETANLDGETNLKRRQVVRGFSELVSEFNPLTFTSVIECEKPNNDL
SRFRGCIIHDNGKKAGLYKENLLLRGCTLRNTDAVVGIVIYAGHETKALLNNSGPRYKRS
KLERQMNCDVLWCVLLLVCMSLFSAVGHGLWIWRYQEKKSLFYVPKSDGSSLSPVTAAVY
SFLTMIIVLQVLIPISLYVSIEIVKACQVYFINQDMQLYDEETDSQLQCRALNITEDLGQ
IQYIFSDKTGTLTENKMVFRRCTVSGVEYSHDANAQRLARYQEADSEEEEVVPRGGSVSQ
RGSIGSHQSVRVVHRTQSTKSHRRTGSRAEAKRASMLSKHTAFSSPMEKDITPDPKLLEK
VSECDKSLAVARHQEHLLAHLSPELSDVFDFFIALTICNTVVVTSPDQPRTKVRVRFELK
SPVKTIEDFLRRFTPSCLTSGCSSIGSLAANKSSHKLGSSFPSTPSSDGMLLRLEERLGQ
PTSAIASNGYSSQADNWASELAQEQESERELRYEAESPDEAALVYAARAYNCVLVERLHD
QVSVELPHLGRLTFELLHTLGFDSVRKRMSVVIRHPLTDEINVYTKGADSVVMDLLQPCS
SVDARGRHQKKIRSKTQNYLNVYAAEGLRTLCIAKRVLSKEEYACWLQSHLEAESSLENS
EELLFQSAIRLETNLHLLGATGIEDRLQDGVPETISKLRQAGLQIWVLTGDKQETAVNIA
YACKLLDHDEEVITLNATSQEACAALLDQCLCYVQSRGLQRAPEKTKGKVSMRFSSLCPP
STSTASGRRPSLVIDGRSLAYALEKNLEDKFLFLAKQCRSVLCCRSTPLQKSMVVKLVRS
KLKAMTLAIGDGANDVSMIQVADVGVGISGQEGMQAVMASDFAVPKFRYLERLLILHGHW
CYSRLANMVLYFFYKNTMFVGLLFWFQFFCGFSASTMIDQWYLIFFNLLFSSLPPLVTGV
LDRDVPANVLLTNPQLYKSGQNMEEYRPRTFWFNMADAAFQSLVCFSIPYLAYYDSNVDL
FTWGTPIVTIALLTFLLHLGIETKTWTWLNWITCGFSVLLFFTVALIYNASCATCYPPSN
PYWTMQALLGDPVFYLTCLMTPVAALLPRLFFRSLQGRVFPTQLQLARQLTRKSPRRCSA
PKETFAQGRLPKDSGTEHSSGRTVKTSVPLSQPSWHTQQPVCSLEASGEPSTVDMSMPVR
EHTLLEGLSAPAPMSSAPGEAVLRSPGGCPEESKVRAASTGRVTPLSSLFSLPTFSLLNW
ISSWSLVSRLGSVLQFSRTEQLADGQAGRGLPVQPHSGRSGLQGPDHRLLIGASSRRSQ
Enzyme 16 Number of Residues 1499
Enzyme 16 Molecular Weight 167690
Enzyme 16 Theoretical pI 8.43
Enzyme 16 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion transporter activity
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • transporter activity
Process
  • cation transport
  • cellular physiological process
  • ion transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 16 General Function Inorganic ion transport and metabolism
Enzyme 16 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • 87-106 111-128 310-332 363-384 1088-1108 1120-1140 1171-1192 1200-1222 1229-1249 1268-1292
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 14009443 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID O60312 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name AT10A_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >4500 bp 
ATGGAGCGGGAGCCGGCGGGGACCGAGGAGCCCGGGCCTCCGGGACGGCGGAGGCGCCGA
GAGGGCAGGACGCGCACGGTGCGCTCCAACCTGCTGCCGCCCCCGGGCGCCGAGGACCCT
GCGGCTGGCGCGGCCAAGGGCGAGCGGCGACGGCGGCGCGGGTGTGCCCAGCACCTGGCC
GACAACCGGCTCAAGACTACCAAGTACACGCTGCTGTCCTTCCTGCCCAAGAACCTGTTC
GAGCAGTTCCACCGCCCGGCCAACGTGTACTTTGTCTTCATCGCGCTGCTCAACTTCGTG
CCGGCGGTGAACGCCTTCCAGCCCGGCCTGGCACTGGCGCCGGTGCTCTTCATCCTGGCC
ATCACGGCCTTCAGGGACCTGTGGGAGGACTACAGCCGCCACCGCTCCGACCACAAGATC
AACCACCTGGGCTGCCTGGTCTTCAGCAGGGAAGAAAAGAAATACGTGAACCGATTCTGG
AAAGAAATCCACGTGGGAGACTTTGTGCGTCTTCGCTGCAACGAAATCTTCCCTGCGGAC
ATTCTGCTGCTCTCCTCCAGTGACCCCGACGGGCTATGCCACATCGAGACCGCCAACCTG
GATGGAGAGACCAACCTGAAGCGGCGGCAGGTGGTCCGCGGCTTCTCGGAGCTTGTCTCC
GAATTCAATCCTTTGACGTTCACCAGCGTGATCGAATGCGAGAAGCCAAACAACGACCTG
AGTAGGTTTCGCGGCTGCATCATACATGACAACGGGAAAAAGGCCGGGCTGTATAAAGAA
AACCTGCTGCTGAGGGGCTGCACCCTTAGGAACACGGACGCAGTCGTCGGCATTGTCATC
TACGCAGGACATGAAACCAAGGCTCTGCTGAACAACAGTGGGCCCCGCTACAAGCGCAGC
AAGCTGGAGAGGCAGATGAACTGCGACGTGCTCTGGTGTGTCCTGCTCCTTGTTTGCATG
TCTCTGTTTTCAGCAGTCGGACATGGACTGTGGATATGGCGGTATCAAGAGAAGAAGTCA
TTATTTTATGTCCCCAAGTCTGATGGAAGCTCCTTATCCCCAGTCACAGCTGCAGTTTAC
TCATTTTTAACAATGATAATAGTTCTGCAGGTTTTGATCCCAATTTCCTTATACGTTTCC
ATTGAAATTGTTAAAGCATGCCAAGTGTACTTCATTAACCAGGACATGCAGTTGTATGAC
GAAGAAACAGACTCGCAGCTGCAGTGCCGAGCTCTGAACATCACGGAAGACTTAGGACAG
ATACAGTACATTTTCTCAGATAAAACTGGCACTTTGACAGAGAATAAGATGGTTTTCCGA
AGATGCACTGTGTCTGGTGTAGAATATTCTCATGATGCAAATGCGCAGCGTCTGGCCAGG
TACCAAGAGGCAGACTCGGAGGAGGAGGAGGTGGTGCCCAGAGGGGGCTCGGTGTCCCAG
CGCGGCAGCATCGGCAGCCACCAGAGTGTCCGGGTGGTGCACAGAACCCAGAGCACCAAG
TCCCACCGGCGCACGGGCAGCCGGGCCGAGGCCAAGAGGGCCAGCATGCTGTCCAAGCAC
ACGGCCTTCAGCAGCCCCATGGAGAAGGATATCACGCCCGACCCAAAGCTGCTGGAGAAG
GTGAGTGAGTGTGACAAGAGCCTAGCCGTGGCGAGGCATCAGGAGCACCTGCTGGCCCAC
CTCTCGCCCGAGCTGTCTGACGTCTTTGATTTCTTCATCGCACTCACCATCTGCAACACA
GTCGTCGTCACGTCCCCGGATCAGCCACGAACAAAGGTGAGGGTGAGGTTTGAGCTGAAG
TCCCCGGTGAAGACGATAGAAGACTTCCTGCGGAGGTTCACACCCAGCTGCCTGACCTCA
GGCTGCAGCAGCATCGGGAGCCTGGCCGCCAACAAGTCCAGCCACAAGTTGGGCTCCAGC
TTCCCGTCCACCCCGTCCAGCGACGGCATGCTTCTCAGGCTGGAGGAGAGGCTGGGCCAG
CCCACCTCGGCCATCGCCAGCAACGGCTACAGCAGCCAGGCGGACAACTGGGCCTCGGAG
CTTGCTCAGGAGCAGGAGTCAGAGCGCGAGCTGCGGTACGAGGCGGAGAGCCCGGATGAG
GCCGCACTGGTGTATGCGGCCAGAGCCTACAACTGCGTGCTTGTGGAGCGGCTGCACGAC
CAAGTGTCAGTGGAGCTGCCCCACCTGGGCAGGCTCACCTTCGAGCTCCTGCACACACTG
GGTTTCGATTCCGTCCGCAAGAGGATGTCAGTGGTGATCCGGCACCCGCTTACCGATGAG
ATCAACGTCTACACCAAGGGGGCCGACTCAGTGGTCATGGATCTCCTGCAGCCCTGCTCT
TCAGTTGACGCCAGAGGGAGGCATCAAAAAAAGATTCGGAGCAAAACTCAGAATTACCTC
AACGTGTATGCGGCGGAAGGCCTGCGCACCTTGTGCATCGCCAAGAGAGTTCTGAGTAAA
GAAGAGTATGCCTGCTGGTTGCAAAGCCACCTAGAAGCCGAATCCTCCCTGGAAAACAGC
GAGGAGCTCCTCTTCCAGTCTGCCATTCGCCTGGAGACCAACCTGCACTTGTTAGGTGCC
ACTGGGATTGAAGACCGCCTGCAGGACGGAGTCCCTGAAACTATTTCTAAATTGCGTCAA
GCGGGCCTGCAGATTTGGGTTCTCACTGGTGACAAACAAGAAACAGCTGTCAACATTGCA
TATGCCTGCAAACTGCTGGACCACGACGAGGAGGTCATCACCCTGAATGCCACCTCCCAG
GAGGCGTGTGCAGCCCTGCTAGACCAGTGCCTATGCTACGTGCAGTCCAGAGGCCTCCAG
AGAGCCCCTGAGAAGACCAAGGGCAAAGTGAGCATGAGGTTCTCCTCTCTCTGCCCACCC
TCCACGTCCACTGCCTCTGGCCGCAGACCCAGCCTCGTGATCGATGGGAGAAGCCTGGCC
TACGCTCTCGAGAAAAACCTGGAGGACAAATTCCTCTTCCTTGCCAAGCAGTGCCGCTCC
GTCCTCTGCTGTCGGTCGACGCCTCTGCAGAAGAGCATGGTGGTGAAGCTGGTGCGGAGC
AAGCTCAAGGCCATGACCCTGGCCATAGGTGATGGAGCCAATGATGTCAGCATGATCCAG
GTGGCAGATGTGGGTGTGGGAATCTCCGGCCAGGAGGGTATGCAGGCAGTGATGGCCAGC
GACTTTGCAGTGCCGAAATTCCGATACCTGGAGAGGCTCTTGATTCTTCACGGGCATTGG
TGCTACTCCCGACTTGCCAACATGGTGCTGTACTTCTTCTACAAAAACACAATGTTCGTG
GGCCTCCTGTTTTGGTTCCAGTTTTTCTGTGGCTTCTCTGCATCTACCATGATTGACCAG
TGGTATCTAATCTTCTTTAATCTGCTCTTCTCGTCACTTCCCCCGCTCGTGACTGGGGTG
CTGGACAGGGATGTGCCAGCCAATGTGCTGCTGACCAACCCGCAGCTCTACAAGAGTGGC
CAGAACATGGAGGAATACCGGCCACGAACGTTCTGGTTTAACATGGCCGACGCCGCCTTC
CAGAGCCTGGTTTGCTTTTCCATTCCTTACCTGGCCTACTATGACTCGAACGTGGACCTG
TTTACCTGGGGGACCCCTATTGTGACAATCGCGCTGCTCACTTTCCTGCTCCACCTGGGC
ATTGAAACCAAAACCTGGACCTGGCTCAACTGGATAACGTGTGGCTTCAGTGTCCTTTTG
TTTTTCACCGTGGCTTTGATTTACAATGCGTCTTGTGCCACGTGCTATCCTCCGTCCAAC
CCTTACTGGACTATGCAAGCCTTACTGGGTGACCCAGTGTTTTACTTGACTTGCCTGATG
ACGCCTGTCGCTGCACTGCTGCCCAGATTGTTTTTCAGATCCCTCCAGGGGAGGGTTTTC
CCCACACAACTTCAGCTGGCACGTCAGTTGACCAGGAAGTCCCCCAGGAGATGCAGTGCT
CCCAAAGAGACCTTTGCTCAGGGACGCCTCCCGAAGGACTCGGGAACCGAGCACTCATCA
GGGAGGACAGTCAAGACCTCTGTGCCCCTGTCCCAGCCTTCTTGGCACACACAGCAGCCG
GTCTGCTCCCTGGAGGCCAGCGGGGAGCCCAGCACAGTGGACATGAGCATGCCAGTGAGG
GAGCACACCCTGCTGGAGGGGCTGAGCGCACCGGCCCCCATGTCCTCTGCGCCAGGGGAG
GCTGTCCTGAGGAGTCCAGGAGGGTGTCCTGAGGAGTCCAAGGTGAGAGCTGCCAGCACC
GGCAGGGTGACCCCCCTGTCTTCCCTCTTCAGCCTGCCTACCTTCAGCTTACTCAACTGG
ATTTCCTCCTGGTCGCTGGTCAGCAGGCTGGGGAGTGTCTTACAGTTCTCCCGGACGGAG
CAGCTTGCAGATGGACAAGCGGGACGTGGACTTCCTGTCCAGCCCCACTCAGGCCGATCA
GGACTTCAAGGGCCAGACCACAGACTACTTATAGGAGCATCTTCAAGGCGGTCACAGTGA
Enzyme 16 GenBank Gene ID AB051358 Link Image
Enzyme 16 GeneCard ID ATP10A Link Image
Enzyme 16 GenAtlas ID ATP10A Link Image
Enzyme 16 HGNC ID HGNC:13542 Link Image
Enzyme 16 Chromosome Location 15
Enzyme 16 Locus 15q11.2
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Meguro M, Kashiwagi A, Mitsuya K, Nakao M, Kondo I, Saitoh S, Oshimura M: A novel maternally expressed gene, ATP10C, encodes a putative aminophospholipid translocase associated with Angelman syndrome. Nat Genet. 2001 May;28(1):19-20. [PubMed Link Image]
  2. Herzing LB, Kim SJ, Cook EH Jr, Ledbetter DH: The human aminophospholipid-transporting ATPase gene ATP10C maps adjacent to UBE3A and exhibits similar imprinted expression. Am J Hum Genet. 2001 Jun;68(6):1501-5. Epub 2001 May 11. [PubMed Link Image]
  3. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 6488
Enzyme 17 Name Probable phospholipid-transporting ATPase IC
Enzyme 17 Synonyms
  1. Familial intrahepatic cholestasis type 1
  2. ATPase class I type 8B member 1
Enzyme 17 Gene Name ATP8B1
Enzyme 17 Protein Sequence >Probable phospholipid-transporting ATPase IC 
MSTERDSETTFDEDSQPNDEVVPYSDDETEDELDDQGSAVEPEQNRVNREAEENREPFRK
ECTWQVKANDRKYHEQPHFMNTKFLCIKESKYANNAIKTYKYNAFTFIPMNLFEQFKRAA
NLYFLALLILQAVPQISTLAWYTTLVPLLVVLGVTAIKDLVDDVARHKMDKEINNRTCEV
IKDGRFKVAKWKEIQVGDVIRLKKNDFVPADILLLSSSEPNSLCYVETAELDGETNLKFK
MSLEITDQYLQREDTLATFDGFIECEEPNNRLDKFTGTLFWRNTSFPLDADKILLRGCVI
RNTDFCHGLVIFAGADTKIMKNSGKTRFKRTKIDYLMNYMVYTIFVVLILLSAGLAIGHA
YWEAQVGNSSWYLYDGEDDTPSYRGFLIFWGYIIVLNTMVPISLYVSVEVIRLGQSHFIN
WDLQMYYAEKDTPAKARTTTLNEQLGQIHYIFSDKTGTLTQNIMTFKKCCINGQIYGDHR
DASQHNHNKIEQVDFSWNTYADGKLAFYDHYLIEQIQSGKEPEVRQFFFLLAVCHTVMVD
RTDGQLNYQAASPDEGALVNAARNFGFAFLARTQNTITISELGTERTYNVLAILDFNSDR
KRMSIIVRTPEGNIKLYCKGADTVIYERLHRMNPTKQETQDALDIFANETLRTLCLCYKE
IEEKEFTEWNKKFMAASVASTNRDEALDKVYEEIEKDLILLGATAIEDKLQDGVPETISK
LAKADIKIWVLTGDKKETAENIGFACELLTEDTTICYGEDINSLLHARMENQRNRGGVYA
KFAPPVQESFFPPGGNRALIITGSWLNEILLEKKTKRNKILKLKFPRTEEERRMRTQSKR
RLEAKKEQRQKNFVDLACECSAVICCRVTPKQKAMVVDLVKRYKKAITLAIGDGANDVNM
IKTAHIGVGISGQEGMQAVMSSDYSFAQFRYLQRLLLVHGRWSYIRMCKFLRYFFYKNFA
FTLVHFWYSFFNGYSAQTAYEDWFITLYNVLYTSLPVLLMGLLDQDVSDKLSLRFPGLYI
VGQRDLLFNYKRFFVSLLHGVLTSMILFFIPLGAYLQTVGQDGEAPSDYQSFAVTIASAL
VITVNFQIGLDTSYWTFVNAFSIFGSIALYFGIMFDFHSAGIHVLFPSAFQFTGTASNAL
RQPYIWLTIILTVAVCLLPVVAIRFLSMTIWPSESDKIQKHRKRLKAEEQWQRRQQVFRR
GVSTRRSAYAFSHQRGYADLISSGRSIRKKRSPLDAIVADGTAEYRRTGDS
Enzyme 17 Number of Residues 1251
Enzyme 17 Molecular Weight 143727
Enzyme 17 Theoretical pI 7.16
Enzyme 17 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion transporter activity
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • transporter activity
Process
  • cation transport
  • cellular physiological process
  • ion transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 17 General Function Inorganic ion transport and metabolism
Enzyme 17 Specific Function May play a role in the transport of aminophospholipids from the outer to the inner leaflet of various membranes and the maintenance of asymmetric distribution of phospholipids in the canicular membrane. May have a role in transport of bile acids into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 17 Pfam Domain Function Not Available
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • 109-130 137-156 341-362 390-411 950-970 983-1002 1033-1054 1069-1091 1098-1118 1139-1163
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 3628757 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID O43520 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name AT8B1_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >3756 bp 
ATGAGTACAGAAAGAGACTCAGAAACGACATTTGACGAGGATTCTCAGCCTAATGACGAA
GTGGTTCCCTACAGTGATGATGAAACAGAAGATGAACTTGATGACCAGGGGTCTGCTGTT
GAACCAGAACAAAACCGAGTCAACAGGGAAGCAGAGGAGAACCGGGAGCCATTCAGAAAA
GAATGTACATGGCAAGTCAAAGCAAACGATCGCAAGTACCACGAACAACCTCACTTTATG
AACACAAAATTCTTGTGTATTAAGGAGAGTAAATATGCGAATAATGCAATTAAAACATAC
AAGTACAACGCATTTACCTTTATACCAATGAATCTGTTTGAGCAGTTTAAGAGAGCAGCC
AATTTATATTTCCTGGCTCTTCTTATCTTACAGGCAGTTCCTCAAATCTCTACCCTGGCT
TGGTACACCACACTAGTGCCCCTGCTTGTGGTGCTGGGCGTCACTGCAATCAAAGACCTG
GTGGACGATGTGGCTCGCCATAAAATGGATAAGGAAATCAACAATAGGACGTGTGAAGTC
ATTAAGGATGGCAGGTTCAAAGTTGCTAAGTGGAAAGAAATTCAAGTTGGAGACGTCATT
CGTCTGAAAAAAAATGATTTTGTTCCAGCTGACATTCTCCTGCTGTCTAGCTCTGAGCCT
AACAGCCTCTGCTATGTGGAAACAGCAGAACTGGACGGAGAAACCAATTTAAAATTTAAG
ATGTCACTTGAAATCACAGACCAGTACCTCCAAAGAGAAGATACATTGGCTACATTTGAT
GGTTTTATTGAATGTGAAGAACCCAATAACCGACTAGATAAGTTTACAGGAACACTATTT
TGGAGAAACACAAGTTTTCCTTTGGATGCTGATAAAATTTTGTTACGTGGCTGTGTAATT
AGGAACACCGATTTCTGCCACGGCTTAGTCATTTTTGCAGGTGCTGACACTAAAATAATG
AAGAATAGTGGGAAAACCAGATTTAAAAGAACTAAAATTGATTACTTGATGAACTACATG
GTTTACACGATCTTTGTTGTTCTTATTCTGCTTTCTGCTGGTCTTGCCATCGGCCATGCT
TATTGGGAAGCACAGGTGGGCAATTCCTCTTGGTACCTCTATGATGGAGAAGACGATACA
CCCTCCTACCGTGGATTCCTCATTTTCTGGGGCTATATCATTGTTCTCAACACCATGGTA
CCCATCTCTCTCTATGTCAGCGTGGAAGTGATTCGTCTTGGACAGAGTCACTTCATCAAC
TGGGACCTGCAAATGTACTATGCTGAGAAGGACACACCCGCAAAAGCTAGAACCACCACA
CTCAATGAACAGCTCGGGCAGATCCATTATATCTTCTCTGATAAGACGGGGACACTCACA
CAAAATATCATGACCTTTAAAAAGTGCTGTATCAACGGGCAGATATATGGGGACCATCGG
GATGCCTCTCAACACAACCACAACAAAATAGAGCAAGTTGATTTTAGCTGGAATACATAT
GCTGATGGGAAGCTTGCATTTTATGACCACTATCTTATTGAGCAAATCCAGTCAGGGAAA
GAGCCAGAAGTACGACAGTTCTTCTTCTTGCTCGCAGTTTGCCACACAGTCATGGTGGAT
AGGACTGATGGTCAGCTCAACTACCAGGCAGCCTCTCCCGATGAAGGTGCCCTGGTAAAC
GCTGCCAGGAACTTTGGCTTTGCCTTCCTCGCCAGGACCCAGAACACCATCACCATCAGT
GAACTGGGCACTGAAAGGACTTACAATGTTCTTGCCATTTTGGACTTCAACAGTGACCGG
AAGCGAATGTCTATCATTGTAAGAACCCCAGAAGGCAATATCAAGCTTTACTGTAAAGGT
GCTGACACTGTTATTTATGAACGGTTACATCGAATGAATCCTACTAAGCAAGAAACACAG
GATGCCCTGGATATCTTTGCAAATGAAACTCTTAGAACCCTATGCCTTTGCTACAAGGAA
ATTGAAGAAAAAGAATTTACAGAATGGAATAAAAAGTTTATGGCTGCCAGTGTGGCCTCC
ACCAACCGGGACGAAGCTCTGGATAAAGTATATGAGGAGATTGAAAAAGACTTAATTCTC
CTGGGAGCTACAGCTATTGAAGACAAGCTACAGGATGGAGTTCCAGAAACCATTTCAAAA
CTTGCAAAAGCTGACATTAAGATCTGGGTGCTTACTGGAGACAAAAAGGAAACTGCTGAA
AATATAGGATTTGCTTGTGAACTTCTGACTGAAGACACCACCATCTGCTATGGGGAGGAT
ATTAATTCTCTTCTTCATGCAAGGATGGAAAACCAGAGGAATAGAGGTGGCGTCTACGCA
AAGTTTGCACCTCCTGTGCAGGAATCTTTTTTTCCACCCGGTGGAAACCGTGCCTTAATC
ATCACTGGTTCTTGGTTGAATGAAATTCTTCTCGAGAAAAAGACCAAGAGAAATAAGATT
CTGAAGCTGAAGTTCCCAAGAACAGAAGAAGAAAGACGGATGCGGACCCAAAGTAAAAGG
AGGCTAGAAGCTAAGAAAGAGCAGCGGCAGAAAAACTTTGTGGACCTGGCCTGCGAGTGC
AGCGCAGTCATCTGCTGCCGCGTCACCCCCAAGCAGAAGGCCATGGTGGTGGACCTGGTG
AAGAGGTACAAGAAAGCCATCACGCTGGCCATCGGAGATGGGGCCAATGACGTGAACATG
ATCAAAACTGCCCACATTGGCGTTGGAATAAGTGGACAAGAAGGAATGCAAGCTGTCATG
TCGAGTGACTATTCCTTTGCTCAGTTCCGATATCTGCAGAGGCTACTGCTGGTGCATGGC
CGATGGTCTTACATAAGGATGTGCAAGTTCCTACGATACTTCTTTTACAAAAACTTTGCC
TTTACTTTGGTTCATTTCTGGTACTCCTTCTTCAATGGCTACTCTGCGCAGACTGCATAC
GAGGATTGGTTCATCACCCTCTACAACGTGCTGTACACCAGCCTGCCCGTGCTCCTCATG
GGGCTGCTCGACCAGGATGTGAGTGACAAACTGAGCCTCCGATTCCCTGGGTTATACATA
GTGGGACAAAGAGACTTACTATTCAACTATAAGAGATTCTTTGTAAGCTTGTTGCATGGG
GTCCTAACATCGATGATCCTCTTCTTCATACCTCTTGGAGCTTATCTGCAAACCGTAGGG
CAGGATGGAGAGGCACCTTCCGACTACCAGTCTTTTGCCGTCACCATTGCCTCTGCTCTT
GTAATAACAGTCAATTTCCAGATTGGCTTGGATACTTCTTATTGGACTTTTGTGAATGCT
TTTTCAATTTTTGGAAGCATTGCACTTTATTTTGGCATCATGTTTGACTTTCATAGTGCT
GGAATACATGTTCTCTTTCCATCTGCATTTCAATTTACAGGCACAGCTTCAAACGCTCTG
AGACAGCCATACATTTGGTTAACTATCATCCTGACTGTTGCTGTGTGCTTACTACCCGTC
GTTGCCATTCGATTCCTGTCAATGACCATCTGGCCATCAGAAAGTGATAAGATCCAGAAG
CATCGCAAGCGGTTGAAGGCGGAGGAGCAGTGGCAGCGACGGCAGCAGGTGTTCCGCCGG
GGCGTGTCAACGCGGCGCTCGGCCTACGCCTTCTCGCACCAGCGGGGCTACGCGGACCTC
ATCTCCTCCGGGCGCAGCATCCGCAAGAAGCGCTCGCCGCTTGATGCCATCGTGGCGGAT
GGCACCGCGGAGTACAGGCGCACCGGGGACAGCTGA
Enzyme 17 GenBank Gene ID AF038007 Link Image
Enzyme 17 GeneCard ID ATP8B1 Link Image
Enzyme 17 GenAtlas ID ATP8B1 Link Image
Enzyme 17 HGNC ID HGNC:3706 Link Image
Enzyme 17 Chromosome Location 18
Enzyme 17 Locus 18q21-q22|18q21.31
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Bull LN, van Eijk MJ, Pawlikowska L, DeYoung JA, Juijn JA, Liao M, Klomp LW, Lomri N, Berger R, Scharschmidt BF, Knisely AS, Houwen RH, Freimer NB: A gene encoding a P-type ATPase mutated in two forms of hereditary cholestasis. Nat Genet. 1998 Mar;18(3):219-24. [PubMed Link Image]
  2. Halleck MS, Pradhan D, Blackman C, Berkes C, Williamson P, Schlegel RA: Multiple members of a third subfamily of P-type ATPases identified by genomic sequences and ESTs. Genome Res. 1998 Apr;8(4):354-61. [PubMed Link Image]
  3. Tygstrup N, Steig BA, Juijn JA, Bull LN, Houwen RH: Recurrent familial intrahepatic cholestasis in the Faeroe Islands. Phenotypic heterogeneity but genetic homogeneity. Hepatology. 1999 Feb;29(2):506-8. [PubMed Link Image]
  4. Klomp LW, Bull LN, Knisely AS, van Der Doelen MA, Juijn JA, Berger R, Forget S, Nielsen IM, Eiberg H, Houwen RH: A missense mutation in FIC1 is associated with greenland familial cholestasis. Hepatology. 2000 Dec;32(6):1337-41. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6504
Enzyme 18 Name Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform
Enzyme 18 Synonyms
  1. PI3-kinase p110 subunit beta
  2. PtdIns-3-kinase p110
  3. PI3K
  4. PI3Kbeta
Enzyme 18 Gene Name PIK3CB
Enzyme 18 Protein Sequence >Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform 
MCFSFIMPPAMADILDIWAVDSQIASDGSIPVDFLLPTGIYIQLEVPREATISYIKQMLW
KQVHNYPMFNLLMDIDSYMFACVNQTAVYEELEDETRRLCDVRPFLPVLKLVTRSCDPGE
KLDSKIGVLIGKGLHEFDSLKDPEVNEFRRKMRKFSEEKILSLVGLSWMDWLKQTYPPEH
EPSIPENLEDKLYGGKLIVAVHFENCQDVFSFQVSPNMNPIKVNELAIQKRLTIHGKEDE
VSPYDYVLQVSGRVEYVFGDHPLIQFQYIRNCVMNRALPHFILVECCKIKKMYEQEMIAI
EAAINRNSSNLPLPLPPKKTRIISHVWENNNPFQIVLVKGNKLNTEETVKVHVRAGLFHG
TELLCKTIVSSEVSGKNDHIWNEPLEFDINICDLPRMARLCFAVYAVLDKVKTKKSTKTI
NPSKYQTIRKAGKVHYPVAWVNTMVFDFKGQLRTGDIILHSWSSFPDELEEMLNPMGTVQ
TNPYTENATALHVKFPENKKQPYYYPPFDKIIEKAAEIASSDSANVSSRGGKKFLPVLKE
ILDRDPLSQLCENEMDLIWTLRQDCREIFPQSLPKLLLSIKWNKLEDVAQLQALLQIWPK
LPPREALELLDFNYPDQYVREYAVGCLRQMSDEELSQYLLQLVQVLKYEPFLDCALSRFL
LERALGNRRIGQFLFWHLRSEVHIPAVSVQFGVILEAYCRGSVGHMKVLSKQVEALNKLK
TLNSLIKLNAVKLNRAKGKEAMHTCLKQSAYREALSDLQSPLNPCVILSELYVEKCKYMD
SKMKPLWLVYNNKVFGEDSVGVIFKNGDDLRQDMLTLQMLRLMDLLWKEAGLDLRMLPYG
CLATGDRSGLIEVVSTSETIADIQLNSSNVAAAAAFNKDALLNWLKEYNSGDDLDRAIEE
FTLSCAGYCVASYVLGIGDRHSDNIMVKKTGQLFHIDFGHILGNFKSKFGIKRERVPFIL
TYDFIHVIQQGKTGNTEKFGRFRQCCEDAYLILRRHGNLFITLFALMLTAGLPELTSVKD
IQYLKDSLALGKSEEEALKQFKQKFDEALRESWTTKVNWMAHTVRKDYRS
Enzyme 18 Number of Residues 1070
Enzyme 18 Molecular Weight 122764
Enzyme 18 Theoretical pI 7.09
Enzyme 18 GO Classification
Function
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • kinase activity
  • lipid kinase activity
  • phosphatidylinositol 3-kinase activity
  • phosphoinositide 3-kinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cell communication
  • cellular process
  • signal transduction
Component
  • phosphoinositide 3-kinase complex
  • protein complex
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2 with a preference for PtdIns(4,5)P2
Enzyme 18 Pathways
Enzyme 18 Reactions
  • ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-12
Enzyme 18 Transmembrane Regions Not Available
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 455760 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID P42338 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PK3CB_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >3213 bp 
ATGTGCTTCAGTTTCATAATGCCTCCTGCTATGGCAGACATCCTTGACATCTGGGCGGTG
GATTCACAGATAGCATCTGATGGCTCCATACCTGTGGATTTCCTTTTGCCCACTGGGATT
TATATCCAGTTGGAGGTACCTCGGGAAGCTACCATTTCTTATATTAAGCAGATGTTATGG
AAGCAAGTTCACAATTACCCAATGTTCAACCTCCTTATGGATATTGACTCCTATATGTTT
GCATGTGTGAATCAGACTGCTGTATATGAGGAGCTTGAAGATGAAACACGAAGACTCTGT
GATGTCAGACCTTTTCTTCCAGTTCTCAAATTAGTGACAAGAAGTTGTGACCCAGGGGAA
AAATTAGACTCAAAAATTGGAGTCCTTATAGGAAAAGGTCTGCATGAATTTGATTCCTTG
AAGGATCCTGAAGTAAATGAATTTCGAAGAAAAATGCGCAAATTCAGCGAGGAAAAAATC
CTGTCACTTGTGGGATTGTCTTGGATGGACTGGCTAAAACAAACATATCCACCAGAGCAT
GAACCATCCATCCCTGAAAACTTAGAAGATAAACTTTATGGGGGAAAGCTCATCGTAGCT
GTTCATTTTGAAAACTGCCAGGACGTGTTTAGCTTTCAAGTGTCTCCTAATATGAATCCT
ATCAAAGTAAATGAATTGGCAATCCAAAAACGTTTGACTATTCATGGGAAGGAAGATGAA
GTTAGCCCCTATGATTATGTGTTGCAAGTCAGCGGGAGAGTAGAATATGTTTTTGGTGAT
CATCCACTAATTCAGTTCCAGTATATCCGGAACTGTGTGATGAACAGAGCCCTGCCCCAT
TTTATACTTGTGGAATGCTGCAAGATCAAGAAAATGTATGAACAAGAAATGATTGCCATA
GAGGCTGCCATAAATCGAAATTCATCTAATCTTCCTCTTCCATTACCACCAAAGAAAACA
CGAATTATTTCTCATGTTTGGGAAAATAACAACCCTTTCCAAATTGTCTTGGTTAAGGGA
AATAAACTTAACACAGAGGAAACTGTAAAAGTTCATGTCAGGGCTGGTCTTTTTCATGGT
ACTGAGCTCCTGTGTAAAACCATCGTAAGCTCAGAGGTATCAGGGAAAAATGATCATATT
TGGAATGAACCACTGGAATTTGATATTAATATTTGTGACTTACCAAGAATGGCTCGATTA
TGTTTTGCTGTTTATGCAGTTTTGGATAAAGTAAAAACGAAGAAATCAACGAAAACTATT
AATCCCTCTAAATATCAGACCATCAGGAAAGCTGGAAAAGTGCATTATCCTGTAGCGTGG
GTAAATACGATGGTTTTTGACTTTAAAGGACAATTGAGAACTGGAGACATAATATTACAC
AGCTGGTCTTCATTTCCTGATGAACTCGAAGAAATGTTGAATCCAATGGGAACTGTTCAA
ACAAATCCATATACTGAAAATGCAACAGCTTTGCATGTTAAATTTCCAGAGAATAAAAAA
CAACCTTATTATTACCCTCCCTTCGATAAGATTATTGAAAAGGCAGCTGAGATTGCAAGC
AGTGATAGTGCTAATGTGTCAAGTCGAGGTGGAAAAAAGTTTCTTCCTGTATTGAAAGAA
ATCTTGGACAGGGATCCCTTGTCTCAACTGTGTGAAAATGAAATGGATCTTATTTGGACT
TTGCGACAAGACTGCCGAGAGATTTTCCCACAATCACTGCCAAAATTACTGCTGTCAATC
AAGTGGAATAAACTTGAGGATGTTGCTCAGCTTCAGGCGCTGCTTCAGATTTGGCCTAAA
CTGCCCCCCCGGGAGGCCCTAGAGCTTCTGGATTTCAACTATCCAGACCAGTACGTTCGA
GAATATGCTGTAGGCTGCCTGCGACAGATGAGTGATGAAGAACTTTCTCAATATCTTTTA
CAACTGGTGCAAGTGTTAAAATATGAGCCTTTTCTTGATTGTGCCCTCTCTAGATTCCTA
TTAGAAAGAGCACTTGGTAATCGGAGGATAGGGCAGTTTCTATTTTGGCATCTTAGGTCA
GAAGTGCACATTCCTGCTGTCTCAGTACAATTTGGTGTCATCCTTGAAGCATACTGCCGG
GGAAGTGTGGGGCACATGAAAGTGCTTTCTAAGCAGGTTGAAGCACTCAATAAGTTAAAA
ACTTTAAATAGTTTAATCAAACTGAATGCCGTGAAGTTAAACAGAGCCAAAGGGAAGGAG
GCCATGCATACCTGTTTAAAACAGAGTGCTTACCGGGAAGCCCTCTCTGACCTGCAGTCA
CCCCTGAACCCATGTGTTATCCTCTCAGAACTCTATGTTGAAAAGTGCAAATACATGGAT
TCCAAAATGAAGCCTTTGTGGCTGGTATACAATAACAAGGTATTTGGTGAGGATTCAGTT
GGAGTGATTTTTAAAAATGGTGATGATTTACGACAGGATATGTTGACACTCCAAATGTTG
CGCTTGATGGATTTACTCTGGAAAGAAGCTGGTTTGGATCTTCGGATGTTGCCTTATGGC
TGTTTAGCAACAGGAGATCGCTCTGGCCTCATTGAAGTTGTGAGCACCTCTGAAACAATT
GCTGACATTCAGCTGAACAGTAGCAATGTGGCTGCTGCAGCAGCCTTCAACAAAGATGCC
CTTCTGAACTGGCTTAAAGAATACAACTCTGGGGATGACCTGGACCGAGCCATTGAGGAA
TTTACACTGTCCTGTGCTGGCTACTGTGTAGCTTCTTATGTCCTTGGGATTGGTGACAGA
CATAGTGACAACATCATGGTCAAAAAAACTGGCCAGCTCTTCCACATTGACTTTGGACAT
ATTCTTGGAAATTTCAAATCTAAGTTTGGCATTAAAAGGGAGCGAGTGCCTTTTATTCTT
ACCTATGATTTCATCCATGTCATTCAACAAGGAAAAACAGGAAATACAGAAAAGTTTGGC
CGGTTCCGCCAGTGTTGTGAGGATGCATATCTGATTTTACGACGGCATGGGAATCTCTTC
ATCACTCTCTTTGCGCTGATGTTGACTGCAGGGCTTCCTGAACTCACATCAGTCAAAGAT
ATACAGTATCTTAAGGACTCTCTTGCATTAGGGAAGAGTGAAGAAGAAGCACTCAAACAG
TTTAAGCAAAAATTTGATGAGGCGCTCAGGGAAAGCTGGACTACTAAAGTGAACTGGATG
GCCCACACAGTTCGGAAAGACTACAGATCTTAA
Enzyme 18 GenBank Gene ID S67334 Link Image
Enzyme 18 GeneCard ID PIK3CB Link Image
Enzyme 18 GenAtlas ID PIK3CB Link Image
Enzyme 18 HGNC ID HGNC:8976 Link Image
Enzyme 18 Chromosome Location 3
Enzyme 18 Locus 3q22.3
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Hu P, Mondino A, Skolnik EY, Schlessinger J: Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85. Mol Cell Biol. 1993 Dec;13(12):7677-88. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 6516
Enzyme 19 Name Probable phospholipid-transporting ATPase IIA
Enzyme 19 Synonyms
  1. ATPase class II type 9A
  2. ATPase IIA
Enzyme 19 Gene Name ATP9A
Enzyme 19 Protein Sequence >Probable phospholipid-transporting ATPase IIA 
MTDNIPLQPVRQKKRMDSRPRAGCCEWLRCCGGGEARPRTVWLGHPEKRDQRYPRNVINN
QKYNFFTFLPGVLFNQFKYFFNLYFLLLACSQFVPEMRLGALYTYWVPLGFVLAVTVIRE
AVEEIRCYVRDKEVNSQVYSRLTARGTVKVKSSNIQVGDLIIVEKNQRVPADMIFLRTSE
KNGSCFLRTDQLDGETDWKLRLPVACTQRLPTAADLLQIRSYVYAEEPNIDIHNFVGTFT
REDSDPPISESLSIENTLWAGTVVASGTVVGVVLYTGRELRSVMNTSNPRSKIGLFDLEV
NCLTKILFGALVVVSLVMVALQHFAGRWYLQIIRFLLLFSNIIPISLRVNLDMGKIVYSW
VIRRDSKIPGTVVRSSTIPEQLGRISYLLTDKTGTLTQNEMIFKRLHLGTVAYGLDSMDE
VQSHIFSIYTQQSQDPPAQKGPTLTTKVRRTMSSRVHEAVKAIALCHNVTPVYESNGVTD
QAEAEKQYEDSCRVYQASSPDEVALVQWTESVGLTLVGRDQSSMQLRTPGDQILNFTILQ
IFPFTYESKRMGIIVRDESTGEITFYMKGADVVMAGIVQYNDWLEEECGNMAREGLRVLV
VAKKSLAEEQYQDFEARYVQAKLSVHDRSLKVATVIESLEMEMELLCLTGVEDQLQADVR
PTLETLRNAGIKVWMLTGDKLETATCTAKNAHLVTRNQDIHVFRLVTNRGEAHLELNAFR
RKHDCALVISGDSLEVCLKYYEYEFMELACQCPAVVCCRCAPTQKAQIVRLLQERTGKLT
CAVGDGGNDVSMIQESDCGVGVEGKEGKQASLAADFSITQFKHLGRLLMVHGRNSYKRSA
ALSQFVIHRSLCISTMQAVFSSVFYFASVPLYQGFLIIGYSTIYTMFPVFSLVLDKDVKS
EVAMLYPELYKDLLKGRPLSYKTFLIWVLISIYQGSTIMYGALLLFESEFVHIVAISFTS
LILTELLMVALTIQTWHWLMTVAELLSLACYIASLVFLHEFIDVYFIATLSFLWKVSVIT
LVSCLPLYVLKYLRRRFSPPSYSKLTS
Enzyme 19 Number of Residues 1047
Enzyme 19 Molecular Weight 118584
Enzyme 19 Theoretical pI 7.81
Enzyme 19 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion transporter activity
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • transporter activity
Process
  • cation transport
  • cellular physiological process
  • ion transport
  • metabolism
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 19 General Function Inorganic ion transport and metabolism
Enzyme 19 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • 70-91 97-119 304-325 333-354 842-862 875-893 924-942 950-972 979-999 1007-1030
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 56205769 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID O75110 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name ATP9A_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >68 bp 
ATGACGGACAACATCCCGCTGCAGCCGGTGCGCCAGAAGAAGCGGATGGACAGCAGGCCC
CGCGCCGG
Enzyme 19 GenBank Gene ID AL353799 Link Image
Enzyme 19 GeneCard ID ATP9A Link Image
Enzyme 19 GenAtlas ID ATP9A Link Image
Enzyme 19 HGNC ID HGNC:13540 Link Image
Enzyme 19 Chromosome Location 20
Enzyme 19 Locus 20q13.2
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  2. Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Jun 30;5(3):169-76. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 6532
Enzyme 20 Name Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
Enzyme 20 Synonyms
  1. PI3-kinase p110 subunit alpha
  2. PtdIns-3- kinase p110
  3. PI3K
Enzyme 20 Gene Name PIK3CA
Enzyme 20 Protein Sequence >Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha isoform 
MPPRPSSGELWGIHLMPPRILVECLLPNGMIVTLECLREATLITIKHELFKEARKYPLHQ
LLQDESSYIFVSVTQEAEREEFFDETRRLCDLRLFQPFLKVIEPVGNREEKILNREIGFA
IGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKH
IYNKLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLK
LCVLEYQGKYILKVCGCDEYFLEKYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPMD
CFTMPSYSRRISTATPYMNGETSTKSLWVINSALRIKILCATYVNVNIRDIDKIYVRTGI
YHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHC
PLAWGNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNPNKETPCLELEFDWF
SSVVKFPDMSVIEEHANWSVSREAGFSYSHAGLSNRLARDNELRENDKEQLKAISTRDPL
SEITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMYCLVKDWPPIKPEQAME
LLDCNYPDPMVRGFAVRCLEKYLTDDKLSQYLIQLVQVLKYEQYLDNLLVRFLLKKALTN
QRIGHFFFWHLKSEMHNKTVSQRFGLLLESYCRACGMYLKHLNRQVEAMEKLINLTDILK
QEKKDETQKVQMKFLVEQMRRPDFMDALQGFLSPLNPAHQLGNLRLEECRIMSSAKRPLW
LNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLS
IGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRS
CAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDF
LIVISKGAQECTKTREFERFQEMCYKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIA
YIRKTLALDKTEQEALEYFMKQMNDAHHGGWTTKMDWIFHTIKQHALN
Enzyme 20 Number of Residues 1068
Enzyme 20 Molecular Weight 124286
Enzyme 20 Theoretical pI 7.23
Enzyme 20 GO Classification
Function
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • kinase activity
  • lipid kinase activity
  • phosphatidylinositol 3-kinase activity
  • phosphoinositide 3-kinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cell communication
  • cellular process
  • signal transduction
Component
  • phosphoinositide 3-kinase complex
  • protein complex
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2 with a preference for PtdIns(4,5)P2
Enzyme 20 Pathways
Enzyme 20 Reactions
  • ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 472991 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P42336 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name PK3CA_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >3207 bp 
ATGCCTCCAAGACCATCATCAGGTGAACTGTGGGGCATCCACTTGATGCCCCCAAGAATC
CTAGTGGAATGTTTACTACCAAATGGAATGATAGTGACTTTAGAATGCCTCCGTGAGGCT
ACATTAGTAACTATAAAGCATGAACTATTTAAAGAAGCAAGAAAATACCCTCTCCATCAA
CTTCTTCAAGATGAATCTTCTTACATTTTCGTAAGTGTTACCCAAGAAGCAGAAAGGGAA
GAATTTTTTGATGAAACAAGACGACTTTGTGATCTTCGGCTTTTTCAACCATTTTTAAAA
GTAATTGAACCAGTAGGCAACCGTGAAGAAAAGATCCTCAATCGAGAAATTGGTTTTGCT
ATCGGCATGCCAGTGTGCGAATTTGATATGGTTAAAGATCCTGAAGTACAGGACTTCCGA
AGAAATATTCTTAATGTTTGTAAAGAAGCTGTGGATCTTAGGGATCTTAATTCACCTCAT
AGTAGAGCAATGTATGTCTATCCGCCACATGTAGAATCTTCACCAGAGCTGCCAAAGCAC
ATATATAATAAATTGGATAGAGGCCAAATAATAGTGGTGATTTGGGTAATAGTTTCTCCA
AATAATGACAAGCAGAAGTATACTCTGAAAATCAACCATGACTGTGTGCCAGAACAAGTA
ATTGCTGAAGCAATCAGGAAAAAAACTAGAAGTATGTTGCTATCATCTGAACAATTAAAA
CTCTGTGTTTTAGAATATCAGGGCAAGTACATTTTAAAAGTGTGTGGATGTGATGAATAC
TTCCTAGAAAAATATCCTCTGAGTCAGTATAAGTATATAAGAAGCTGTATAATGCTTGGG
AGGATGCCCAATTTGAAGATGATGGCTAAAGAAAGCCTTTATTCTCAACTGCCAATGGAC
TGTTTTACAATGCCATCTTATTCCAGACGCATTTCCACAGCTACACCATATATGAATGGA
GAAACATCTACAAAATCCCTTTGGGTTATAAATAGAGCACTCAGAATAAAAATTCTTTGT
GCAACCTACGTGAATCTAAATATTCGAGACATTGACAAGATTTATGTTCGAACAGGTATC
TACCATGGAGGAGAACCCTTATGTGACAATGTGAACACTCAAAGAGTACCTTGTTCCAAT
CCCAGGTGGAATGAATGGCTGAATTATGATATATACATTCCTGATCTTCCTCGTGCTGCT
CGACTTTGCCTTTCCATTTGCTCTGTTAAAGGCCGAAAGGGTGCTAAAGAGGAACACTGT
CCATTGGCATGGGGAAATATAAACTTGTTTGATTACACAGACACTCTAGTATCTGGAAAA
ATGGCTTTGAATCTTTGGCCAGTACCTCATGGATTAGAAGATTTGCTGAACCCTATTGGT
GTTACTGGATCAAATCCAAATAAAGAAACTCCATGCTTAGAGTTGGAGTTTGACTGGTTC
AGCAGTGTGGTAAAGTTCCCAGATATGTCAGTGATTGAAGAGCATGCCAATTGGTCTGTA
TCCCGAGAAGCAGGATTTAGCTATTCCCACGCAGGACTGAGTAACAGACTAGCTAGAGAC
AATGAATTAAGGGAAAATGACAAAGAACAGCTCAAAGCAATTTCTACACGAGATCCTCTC
TCTGAAATCACTGAGCAGGAGAAAGATTTTCTATGGAGTCACAGACACTATTGTGTAACT
ATCCCCGAAATTCTACCCAAATTGCTTCTGTCTGTTAAATGGAATTCTAGAGATGAAGTA
GCCCAGATGTATTGCTTGGTAAAAGATTGGCCTCCAATCAAACCTGAACAGGCTATGGAA
CTTCTGGACTGTAATTACCCAGATCCTATGGTTCGAGGTTTTGCTGTTCGGTGCTTGGAA
AAATATTTAACAGATGACAAACTTTCTCAGTATTTAATTCAGCTAGTACAGGTCCTAAAA
TATGAACAATATTTGGATAACTTGCTTGTGAGATTTTTACTGAAGAAAGCATTGACTAAT
CAAAGGATTGGGCACTTTTTCTTTTGGCATTTAAAATCTGAGATGCACAATAAAACAGTT
AGCCAGAGGTTTGGCCTGCTTTTGGAGTCCTATTGTCGTGCATGTGGGATGTATTTGAAG
CACCTGAATAGGCAAGTCGAGGCAATGGAAAAGCTCATTAACTTAACTGACATTCTCAAA
CAGGAGAGGAAGGATGAAACACAAAAGGTACAGATGAAGTTTTTAGTTGAGCAAATGAGG
CGACCAGATTTCATGGATGCCCTACAGGGCTTGCTGTCTCCTCTAAACCCTGCTCATCAA
CTAGGAAACCTCAGGCTTAAAGAGTGTCGAATTATGTCTTCTGCAAAAAGGCCACTGTGG
TTGAATTGGGAGAACCCAGACATCATGTCAGAGTTACTGTTTCAGAACAATGAGATCATC
TTTAAAAATGGGGATGATTTACGGCAAGATATGCTAACACTTCAAATTATTCGTATTATG
GAAAATATCTGGCAAAATCAAGGTCTTGATCTTCGAATGTTACCTTATGGTTGTCTGTCA
ATCGGTGACTGTGTGGGACTTATTGAGGTGGTGCGAAATTCTCACACTATTATGCAAATT
CAGTGCAAAGGCGGCTTGAAAGGTGCACTGCAGTTCAACAGCCACACACTACATCAGTGG
CTCAAAGACAAGAACAAAGGAGAAATATATGATGCAGCCATTGACCTGTTTACACGTTCA
TGTGCTGGATACTGTGTAGCTACCTTCATTTTGGGAATTGGAGATCGTCACAATAGTAAC
ATCATGGTGAAAGACGATGGACAACTGTTTCATATAGATTTTGGACACTTTTTGGATCAC
AAGAAGAAAAAATTTGGTTATAAACGAGAACGTGTGCCATTTGTTTTGACACAGGATTTC
TTAATAGTGATTAGTAAAGGAGCCCAAGAATGCACAAAGACAAGAGAATTTGAGAGGTTT
CAGGAGATGTGTTACAAGGCTTATCTAGCTATTCGACAGCATGCCAATCTCTTCATAAAT
CTTTTCTCAATGATGCTTGGCTCTGGAATGCCAGAACTACAATCTTTTGATGACATTGCA
TACATTCGAAAGACCCTAGCCTTAGATAAAACTGAGCAAGAGGCTTTGGAGTATTTCATG
AAACAAATGAATGATGCACATCATGGTGGCTGGACAACAAAAATGGATTGGATCTTCCAC
ACAATTAAACAGCATGCATTGAACTGA
Enzyme 20 GenBank Gene ID Z29090 Link Image
Enzyme 20 GeneCard ID PIK3CA Link Image
Enzyme 20 GenAtlas ID PIK3CA Link Image
Enzyme 20 HGNC ID HGNC:8975 Link Image
Enzyme 20 Chromosome Location 3
Enzyme 20 Locus 3q26.3
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Volinia S, Hiles I, Ormondroyd E, Nizetic D, Antonacci R, Rocchi M, Waterfield MD: Molecular cloning, cDNA sequence, and chromosomal localization of the human phosphatidylinositol 3-kinase p110 alpha (PIK3CA) gene. Genomics. 1994 Dec;24(3):472-7. [PubMed Link Image]
  2. Stirdivant SM, Ahern J, Conroy RR, Barnett SF, Ledder LM, Oliff A, Heimbrook DC: Cloning and mutagenesis of the p110 alpha subunit of human phosphoinositide 3'-hydroxykinase. Bioorg Med Chem. 1997 Jan;5(1):65-74. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 6535
Enzyme 21 Name Probable phospholipid-transporting ATPase VD
Enzyme 21 Synonyms
  1. ATPVD
Enzyme 21 Gene Name ATP10D
Enzyme 21 Protein Sequence >Probable phospholipid-transporting ATPase VD 
MTEALQWARYHWRRLIRGATRDDDSGPYNYSSLLACGRKSSQTPKLSGRHRIVVPHIQPF
KDEYEKFSGAYVNNRIRTTKYTLLNFVPRNLFEQFHRAANLYFLFLVVLNWVPLVEAFQK
EITMLPLVVVLTIIAIKDGLEGYRKYKIDKQINNLITKVYSRKEKKYIDRCWKDVTVGDF
IRLSCNEVIPADMVLLFSTDPDGICHIETSGLDGESNLKQRQVVRGYAEQDSEVDPEKFS
SRIECESPNNDLSRFRGFLEHSNKERVGLSKENLLLRGCTIRNTEAVVGIVVYAGHETKA
MLNNSGPRYKRSKLERRANTDVLWCVMLLVIMCLTGAVGHGIWLSRYEKMHFFNVPEPDG
HIISPLLAGFYMFWTMIILLQVLIPISLYVSIEIVKLGQIYFIQSDVDFYNEKMDSIVQC
RALNIAEDLGQIQYLFSDKTGTLTENKMVFRRCSVAGFDYCHEENARRLESYQEAVSEDE
DFIDTVSGSLSNMAKPRAPSCRTVHNGPLGNKPSNHLAGSSFTLGSGEGASEVPHSRQAA
FSSPIETDVVPDTRLLDKFSQITPRLFMPLDETIQNPPMETLYIIDFFIALAICNTVVVS
APNQPRQKIRHPSLGGLPIKSLEEIKSLFQRWSVRRSSSPSLNSGKEPSSGVPNAFVSRL
PLFSRMKPASPVEEEVSQVCESPQCSSSSACCTETEKQHGDAGLLNGKAESLPGQPLACN
LCYEAESPDEAALVYAARAYQCTLRSRTPEQVMVDFAALGPLTFQLLHILPFDSVRKRMS
VVVRHPLSNQVVVYTKGADSVIMELLSVASPDGASLEKQQMIVREKTQKHLDDYAKQGLR
TLCIAKKVMSDTEYAEWLRNHFLAETSIDNREELLLESAMRLENKLTLLGATGIEDRLQE
GVPESIEALHKAGIKIWMLTGDKQETAVNIAYACKLLEPDDKLFILNTQSKDACGMLMST
ILKELQKKTQALPEQVSLSEDLLQPPVPRDSGLRAGLIITGRTLEFALQESLQKQFLELT
SWCQAVVCCRATPLQKSEVVKLVRSHLQVMTLAIGDGANDVSMIQVADIGIGVSGQEGMQ
AVMASDFAVYQFKHLSKLLLVHGHWCYTRLSNMILYFFYKNVAYVNLLFWYQFFCGFSGT
SMTDYWVLIFFNLLFTSAPPVIYGVLEKDVSAETLMQLPELYRSGQKSEAYLPHTFWITL
LDAFYQSLVCFFVPYFTYQGSDTDIFAFGNPLNTAALFIVLLHLVIESKSLTWIHLLVII
GSILSYFLFAIVFGAMCVTCNPPSNPYWIMQEHMLDPVFYLVCILTTSIALLPRFVYRVL
QGSLFPSPILRAKHFDRLTPEERTKALKKWRGAGKMNQVTSKYANQSAGKSGRRPMPGPS
AVFAMKSASSCAIEQGNLSLCETALDQGYSETKAFEMAGPSKGKES
Enzyme 21 Number of Residues 1426
Enzyme 21 Molecular Weight 160322
Enzyme 21 Theoretical pI 7.23
Enzyme 21 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion transporter activity
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • transporter activity
Process
  • cation transport
  • cellular physiological process
  • ion transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 21 General Function Inorganic ion transport and metabolism
Enzyme 21 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 98-118 122-142 322-342 366-386 1114-1134 1146-1166 1196-1216 1225-1245 1253-1273 1293-1313
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 28193030 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q9P241 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name AT10D_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >4281 bp 
ATGACTGAGGCTCTCCAATGGGCCAGATATCACTGGCGACGGCTGATCAGAGGTGCAACC
AGGGATGATGATTCAGGGCCATACAACTATTCCTCGTTGCTCGCCTGTGGGCGCAAGTCC
TCTCAGACCCCTAAACTGTCAGGAAGGCACCGGATTGTTGTTCCCCACATCCAGCCCTTC
AAGGATGAGTATGAGAAGTTCTCCGGAGCCTATGTGAACAATCGAATACGAACAACAAAG
TACACACTTCTGAATTTTGTGCCAAGAAATTTATTTGAACAATTTCACAGAGCTGCCAAT
TTATATTTCCTGTTCCTAGTTGTCCTGAACTGGGTACCTTTGGTAGAAGCCTTCCAAAAG
GAAATCACCATGTTGCCTCTGGTGGTGGTCCTTACAATTATCGCAATTAAAGATGGCCTG
GAAGGTTATCGGAAATACAAAATTGACAAACAGATCAATAATTTAATAACTAAAGTTTAT
AGTAGGAAAGAGAAAAAATACATTGACCGATGCTGGAAAGACGTTACTGTTGGGGACTTT
ATTCGCCTCTCCTGCAACGAGGTCATCCCTGCAGACATGGTACTACTCTTTTCCACTGAT
CCAGATGGAATCTGTCACATTGAGACTTCTGGTCTTGATGGAGAGAGCAATTTAAAACAG
AGGCAGGTGGTTCGGGGATATGCAGAACAGGACTCTGAAGTTGATCCTGAGAAGTTTTCC
AGTAGGATAGAATGTGAAAGCCCAAACAATGACCTCAGCAGATTCCGAGGCTTCCTAGAA
CATTCCAACAAAGAACGCGTGGGTCTCAGTAAAGAAAATTTGTTGCTTAGAGGATGCACC
ATTAGAAACACAGAGGCTGTTGTGGGCATTGTGGTTTATGCAGGCCATGAAACCAAAGCA
ATGCTGAACAACAGTGGGCCACGGTATAAGCGCAGCAAATTAGAAAGAAGAGCAAACACA
GATGTCCTCTGGTGTGTCATGCTTCTGGTCATAATGTGCTTAACTGGCGCAGTAGGTCAT
GGAATCTGGCTGAGCAGGTATGAAAAGATGCATTTTTTCAATGTTCCCGAGCCTGATGGA
CATATCATATCACCACTGTTGGCAGGATTTTATATGTTTTGGACCATGATCATTTTGTTA
CAGGTCTTGATTCCTATTTCTCTCTATGTTTCCATCGAAATTGTGAAGCTTGGACAAATA
TATTTCATTCAAAGTGATGTGGATTTCTACAATGAAAAAATGGATTCTATTGTTCAGTGC
CGAGCCCTGAACATCGCCGAGGATCTGGGACAGATTCAGTACCTCTTTTCCGATAAGACA
GGAACCCTCACTGAGAATAAGATGGTTTTTCGAAGATGTAGTGTGGCAGGATTTGATTAC
TGCCATGAAGAAAATGCCAGGAGGTTGGAGTCCTATCAGGAAGCTGTCTCTGAAGATGAA
GATTTTATAGACACAGTCAGTGGTTCCCTCAGCAATATGGCAAAACCGAGAGCCCCCAGC
TGCAGGACAGTTCATAATGGGCCTTTGGGAAATAAGCCCTCAAATCATCTTGCTGGGAGC
TCTTTTACTCTAGGAAGTGGAGAAGGAGCCAGTGAAGTGCCTCATTCCAGACAGGCTGCT
TTCAGTAGCCCCATTGAAACAGACGTGGTACCAGACACCAGGCTTTTAGACAAATTTAGT
CAGATTACACCTCGGCTCTTTATGCCACTAGATGAGACCATCCAAAATCCACCAATGGAA
ACTTTGTACATTATCGACTTTTTCATTGCATTGGCAATTTGCAACACAGTAGTGGTTTCT
GCTCCTAACCAACCCCGACAAAAGATCAGACACCCTTCACTGGGGGGGTTGCCCATTAAG
TCTTTGGAAGAGATTAAAAGTCTTTTCCAGAGATGGTCTGTCCGAAGATCAAGTTCTCCA
TCGCTTAACAGTGGGAAAGAGCCATCTTCTGGAGTTCCAAACGCCTTTGTGAGCAGACTC
CCTCTCTTTAGTCGAATGAAACCAGCTTCACCTGTGGAGGAAGAGGTCTCCCAGGTGTGT
GAGAGCCCCCAGTGCTCCAGTAGCTCAGCTTGCTGCACAGAAACAGAGAAACAACACGGT
GATGCAGGCCTCCTGAATGGCAAGGCAGAGTCCCTCCCTGGACAGCCATTGGCCTGCAAC
CTGTGTTATGAGGCCGAGAGCCCAGACGAAGCGGCCTTAGTGTATGCCGCCAGGGCTTAC
CAATGCACTTTACGGTCTCGGACACCAGAGCAGGTCATGGTGGACTTTGCTGCTTTGGGA
CCATTAACATTTCAACTCCTACACATCCTGCCCTTTGACTCAGTAAGAAAAAGAATGTCT
GTTGTGGTCCGACACCCTCTTTCCAATCAAGTTGTGGTGTATACGAAAGGCGCTGATTCT
GTGATCATGGAGTTACTGTCGGTGGCTTCCCCAGATGGAGCAAGTCTGGAGAAACAACAG
ATGATAGTAAGGGAGAAAACCCAGAAGCACTTGGATGACTATGCCAAACAAGGCCTTCGT
ACTTTATGTATAGCAAAGAAGGTCATGAGTGACACTGAATATGCAGAGTGGCTGAGGAAT
CATTTTTTAGCTGAAACCAGCATTGACAACAGGGAAGAATTACTACTTGAATCTGCCATG
AGGTTGGAGAACAAACTTACATTACTTGGTGCTACTGGCATTGAAGACCGTCTGCAGGAG
GGAGTCCCTGAATCTATAGAAGCTCTTCACAAAGCGGGCATCAAGATCTGGATGCTGACA
GGGGACAAGCAGGAGACAGCTGTCAACATAGCTTATGCATGCAAACTACTGGAGCCAGAT
GACAAGCTTTTTATCCTCAATACCCAAAGTAAAGATGCCTGTGGGATGCTGATGAGCACA
ATTTTGAAAGAACTTCAGAAGAAAACTCAAGCCCTGCCAGAGCAAGTGTCATTAAGTGAA
GATTTACTTCAGCCTCCTGTCCCCCGGGACTCAGGGTTACGAGCTGGACTCATTATCACT
GGGAGGACCCTGGAGTTTGCCCTGCAAGAAAGTCTGCAAAAGCAGTTCCTGGAACTGACA
TCTTGGTGTCAAGCTGTGGTCTGCTGCCGAGCCACACCGCTGCAGAAAAGTGAAGTGGTG
AAATTGGTCCGCAGCCATCTCCAGGTGATGACCCTTGCTATTGGTGATGGTGCCAATGAT
GTTAGCATGATACAAGTGGCAGACATTGGGATAGGGGTCTCAGGTCAAGAAGGCATGCAG
GCTGTGATGGCCAGTGACTTTGCCGTTTATCAGTTCAAACATCTCAGCAAGCTCCTTCTT
GTCCATGGACACTGGTGTTATACACGGCTTTCCAACATGATTCTCTATTTTTTCTATAAG
AATGTGGCCTATGTGAACCTCCTTTTCTGGTACCAGTTCTTTTGTGGATTTTCAGGGACA
TCCATGACTGATTACTGGGTTTTGATCTTCTTCAACCTCCTCTTCACATCTGCCCCTCCT
GTCATTTATGGTGTTTTGGAGAAAGATGTGTCTGCAGAGACCCTCATGCAACTGCCTGAA
CTTTACAGAAGTGGTCAGAAATCAGAGGCATACTTACCCCATACCTTCTGGATCACCTTA
TTGGATGCTTTTTATCAAAGCCTGGTCTGCTTCTTTGTGCCTTATTTTACCTACCAGGGC
TCAGATACTGACATCTTTGCATTTGGAAACCCCCTGAACACAGCCGCTCTGTTCATCGTT
CTCCTCCATCTGGTCATTGAAAGCAAGAGTTTGACTTGGATTCACTTGCTGGTCATCATT
GGTAGCATCTTGTCTTATTTTTTATTTGCCATAGTTTTTGGAGCCATGTGTGTAACTTGC
AACCCACCATCCAACCCTTACTGGATTATGCAGGAGCACATGCTGGATCCAGTATTCTAC
TTAGTTTGTATCCTCACGACGTCCATTGCTCTTCTGCCCAGGTTTGTATACAGAGTTCTT
CAGGGATCCCTGTTTCCATCTCCAATTCTGAGAGCTAAGCACTTTGACAGACTAACTCCA
GAGGAGAGGACTAAAGCTCTCAAGAAGTGGAGAGGGGCTGGAAAGATGAATCAAGTGACA
TCAAAGTATGCTAACCAATCAGCTGGCAAGTCAGGAAGAAGACCCATGCCTGGCCCTTCT
GCTGTATTTGCAATGAAGTCAGCAAGTTCCTGTGCTATTGAGCAAGGAAACTTATCTCTG
TGTGAGACTGCTTTAGATCAAGGCTACTCTGAAACTAAGGCCTTTGAGATGGCTGGACCC
TCCAAAGGTAAAGAAAGCTAG
Enzyme 21 GenBank Gene ID AJ441078 Link Image
Enzyme 21 GeneCard ID ATP10D Link Image
Enzyme 21 GenAtlas ID ATP10D Link Image
Enzyme 21 HGNC ID HGNC:13549 Link Image
Enzyme 21 Chromosome Location 4
Enzyme 21 Locus 4p12
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Flamant S, Pescher P, Lemercier B, Clement-Ziza M, Kepes F, Fellous M, Milon G, Marchal G, Besmond C: Characterization of a putative type IV aminophospholipid transporter P-type ATPase. Mamm Genome. 2003 Jan;14(1):21-30. [PubMed Link Image]
  2. Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 6543
Enzyme 22 Name Probable phospholipid-transporting ATPase IB
Enzyme 22 Synonyms
  1. ATPase class I type 8A member 2
  2. ML-1
Enzyme 22 Gene Name ATP8A2
Enzyme 22 Protein Sequence >Probable phospholipid-transporting ATPase IB 
MSRATSVGDQLEAPARTIYLNQPHLNKFRDNQISTAKYSVLTFLPRFLYEQIRRAANAFF
LFIALLQQIPDVSPTGRYTTLVPLIIILTIAGIKEIVEDFKRHKADNAVNKKKTIVLRNG
MWHTIMWKEVAVGDIVKVVNGQYLPADVVLLSSSEPQAMCYVETANLDGETNLKIRQGLS
HTADMQTREVLMKLSGTIECEGPNRHLYDFTGNLNLDGKSLVALGPDQILLRGTQLRNTQ
WVFGIVVYTGHDTKLMQNSTKAPLKRSNVEKVTNVQILVLFGILLVMALVSSAGALYWNR
SHGEKNWYIKKMDTTSDNFGYNLLTFIILYNNLIPISLLVTLEVVKYTQALFINWDTDMY
YIGNDTPAMARTSNLNEELGQVKYLFSDKTGTLTCNIMNFKKCSIAGVTYGHFPELAREP
SSDDFCRMPPPCSDSCDFDDPRLLKNIEDRHPTAPCIQEFLTLLAVCHTVVPEKDGDNII
YQASSPDEAALVKGAKKLGFVFTARTPFSVIIEAMGQEQTFGILNVLEFSSDRKRMSVIV
RTPSGRLRLYCKGADNVIFERLSKDSKYMEETLCHLEYFATEGLRTLCVAYADLSENEYE
EWLKVYQEASTILKDRAQRLEECYEIIEKNLLLLGATAIEDRLQAGVPETIATLLKAEIK
IWVLTGDKQETAINIGYSCRLVSQNMALILLKEDSLDATRAAITQHCTDLGNLLGKENDV
ALIIDGHTLKYALSFEVRRSFLDLALSCKAVICCRVSPLQKSEIVDVVKKRVKAITLAIG
DGANDVGMIQTAHVGVGISGNEGMQATNNSDYAIAQFSYLEKLLLVHGAWSYNRVTKCIL
YCFYKNVVLYIIELWFAFVNGFSGQILFERWCIGLYNVIFTALPPFTLGIFERSCTQESM
LRFPQLYKITQNGEGFNTKVFWGHCINALVHSLILFWFPMKALEHDTVLTSGHATDYLFV
GNIVYTYVVVTVCLKAGLETTAWTKFSHLAVWGSMLTWLVFFGIYSTIWPTIPIAPDMRG
QATMVLSSAHFWLGLFLVPTACLIEDVAWRAAKHTCKKTLLEEVQELETKSRVLGKAVLR
DSNGKRLNERDRLIKRLGRKTPPTLFRGSSLQQGVPHGYAFSQEEHGAVSQEEVIRAYDT
TKKKSRKK
Enzyme 22 Number of Residues 1148
Enzyme 22 Molecular Weight 129243
Enzyme 22 Theoretical pI 7.84
Enzyme 22 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion transporter activity
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • transporter activity
Process
  • cation transport
  • cellular physiological process
  • ion transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 22 General Function Inorganic ion transport and metabolism
Enzyme 22 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 45-66 72-94 277-298 324-345 838-858 871-890 921-942 957-979 986-1006 1025-1049
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 27820152 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q9NTI2 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name AT8A2_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >2985 bp 
ATGTCCCGGGCCACGTCTGTTGGAGACCAGCTGGAGGCACCCGCCCGCACCATTTACCTC
AACCAACCGCATCTCAACAAATTCCGCGACAACCAGATCAGTACGGCCAAGTACAGCGTG
TTGACATTTCTACCTCGATTCTTGTATGAGCAGATTAGAAGAGCTGCTAATGCCTTCTTT
CTCTTCATTGCCTTATTACAGCAAATTCCAGATGTATCTCCAACAGGAAGATATACCACC
CTGGTGCCATTGATCATTATTTTAACAATTGCAGGCATCAAAGAGATTGTAGAAGATTTT
AAGCGACACAAGGCAGACAATGCAGTTAACAAAAAGAAAACAATAGTGTTAAGAAATGGT
ATGTGGCATACCATTATGTGGAAAGAGGTGGCAGTGGGAGACATTGTGAAGGTCGTCAAT
GGGCAGTATCTTCCAGCAGATGTGGTCCTGCTGTCATCCAGTGAACCTCAGGCAATGTGT
TATGTTGAAACAGCTAATCTGGATGGGGAGACGAACCTTAAAATACGTCAGGGTTTGAGT
CACACTGCTGACATGCAAACACGTGAAGTTCTGATGAAGTTATCTGGAACTATAGAGTGT
GAAGGGCCCAACCGCCACCTCTATGACTTCACTGGAAACTTGAACTTAGATGGGAAAAGC
CTTGTTGCCCTTGGGCCTGACCAGATCTTATTAAGAGGTACACAGCTTAGAAATACTCAG
TGGGTCTTTGGCATAGTTGTTTATACTGGACACGACACCAAACTCATGCAGAATTCAACC
AAAGCGCCTCTCAAGAGATCAAATGTTGAGAAGGTGACTAACGTGCAGATCCTGGTGTTG
TTTGGCATCCTCTTGGTCATGGCCTTGGTGAGCTCGGCGGGGGCCCTGTACTGGAACAGG
TCTCATGGTGAAAAGAACTGGTACATCAAGAAGATGGACACCACCTCAGATAATTTTGGA
TACAACCTACTGACGTTCATCATCTTATACAACAATCTTATTCCCATCAGTCTGTTGGTG
ACTCTTGAGGTTGTGAAGTATACTCAAGCCCTTTTCATAAACTGGGACACAGATATGTAT
TATATAGGAAATGACACTCCTGCCATGGCCAGGACATCAAACCTTAATGAAGAGCTTGGG
CAGGTGAAATATCTCTTTTCTGACAAGACTGGAACGCTTACATGCAATATCATGAACTTT
AAGAAGTGCAGCATTGCCGGAGTAACCTATGGTCACTTCCCAGAATTGGCAAGAGAGCCG
TCTTCAGATGACTTCTGTCGGATGCCTCCTCCCTGTAGTGATTCCTGTGACTTTGATGAC
CCCAGGCTGTTGAAGAACATTGAGGATCGCCATCCCACAGCCCCTTGCATTCAGGAGTTC
CTCACCCTTCTGGCCGTGTGCCACACGGTTGTTCCTGAGAAGGATGGAGATAACATCATC
TACCAGGCCTCTTCCCCAGATGAAGCTGCTTTGGTGAAAGGAGCTAAAAAGCTGGGCTTT
GTCTTCACAGCCAGAACACCATTCTCAGTCATCATAGAAGCGGTGAGTAACATGCGTGTG
CATTTCAGATCACCTGCTTTTGTGAAGATTGTGTGTGTGAAATGGCATGTCTATTGTAAA
TATGATCAGGCCACAAGGGCAGCCATTACTCAGCACTGCACTGACCTTGGGAATTTGCTG
GGCAAGGAAAATGACGTGGCCCTCATCATCGATGGCCACACCCTGAAGTACGCGCTCTCC
TTCGAAGTCCGGAGGAGTTTCCTGGATTTGGCACTCTCGTGCAAAGCGGTCATATGCTGC
AGAGTGTCTCCTCTGCAGAAGTCTGAGATAGTGGATGTGGTGAAGAAGCGGGTGAAGGCC
ATCACCCTCGCCATCGGAGACGGCGCCAACGATGTCGGGATGATCCAGACAGCCCACGTG
GGTGTGGGAATCAGTGGGAATGAAGGCATGCAGGCCACCAACAACTCGGATTACGCCATC
GCACAGTTTTCCTACTTAGAGAAGCTTCTGTTGGTTCATGGAGCCTGGAGCTACAACCGG
GTGACCAAGTGCATCTTGTACTGCTTCTATAAGAACGTGGTCCTGTATATTATTGAGCTT
TGGTTCGCCTTTGTTAATGGATTTTCTGGGCAGATTTTATTTGAACGTTGGTGCATCGGC
CTGTACAATGTGATTTTCACCGCTTTGCCGCCCTTCACTCTGGGAATCTTTGAGAGGTCT
TGCACTCAGGAGAGCATGCTCAGGTTTCCCCAGCTCTACAAAATCACCCAGAATGGCGAA
GGCTTCAACACAAAGGTTTTCTGGGGTCACTGCATCAACGCCTTGGTCCACTCCCTCATC
CTCTTCTGGTTTCCCATGAAAGCTCTGGAGCATGATACTGTGTTTGACAGTGGTCATGCT
ACCGACTATTTATTTGTTGGAAATATTGTTTACACATATGTTGTTGTTACTGTTTGTCTG
AAAGCTGGTTTGGAGACCACAGCTTGGACTAAATTCAGTCATCTGGCTGTCTGGGGAAGC
ATGCTGACCTGGCTGGTGTTTTTTGGCATCTACTCGACCATCTGGCCCACCATTCCCATT
GCTCCAGATATGAGAGGACAGGCAACTATGGTCCTGAGCTCCGCACACTTCTGGTTGGGA
TTATTTCTGGTTCCTACTGCCTGTTTGATTGAAGATGTGGCATGGAGAGCAGCCAAGCAC
ACCTGCAAAAAGACATTGCTGGAGGAGGTGCAGGAGCTGGAAACCAAGTCTCGAGTCCTG
GGAAAAGCGGTGCTGCGGGATAGCAATGGAAAGAGGCTGAACGAGCGCGACCGCCTGATC
AAGAGGCTGGGCCGGAAGACGCCCCCGACGCTGTTCCGGGGCAGCTCCCTGCAGCAGGGC
GTCCCGCATGGGTATGCTTTTTCTCAAGAAGAACACGGAGCTGTTAGTCAGGAAGAAGTC
ATCCGTGCTTATGACACCACCAAAAAGAAATCCAGGAAGAAATAA
Enzyme 22 GenBank Gene ID AF236871 Link Image
Enzyme 22 GeneCard ID ATP8A2 Link Image
Enzyme 22 GenAtlas ID ATP8A2 Link Image
Enzyme 22 HGNC ID HGNC:13533 Link Image
Enzyme 22 Chromosome Location 13
Enzyme 22 Locus 13q12-13
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Sun XL, Li D, Fang J, Noyes I, Casto B, Theil K, Shuler C, Milo GE: Changes in levels of normal ML-1 gene transcripts associated with the conversion of human nontumorigenic to tumorigenic phenotypes. Gene Expr. 1999;8(2):129-39. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 6655
Enzyme 23 Name Probable phospholipid-transporting ATPase IA
Enzyme 23 Synonyms
  1. Chromaffin granule ATPase II
  2. ATPase class I type 8A member 1
Enzyme 23 Gene Name ATP8A1
Enzyme 23 Protein Sequence >Probable phospholipid-transporting ATPase IA 
MPTMRRTVSEIRSRAEGYEKTDDVSEKTSLADQEEVRTIFINQPQLTKFCNNHVSTAKYN
IITFLPRFLYSQFRRAANSFFLFIALLQQIPDVSPTGRYTTLVPLLFILAVAAIKEIIED
IKRHKADNAVNKKQTQVLRNGAWEIVHWEKVAVGEIVKVTNGEHLPADLISLSSSEPQAM
CYIETSNLDGETNLKIRQGLPATSDIKDVDSLMRISGRIECESPNRHLYDFVGNIRLDGH
GTVPLGADQILLRGAQLRNTQWVHGIVVYTGHDTKLMQNSTSPPLKLSNVERITNVQILI
LFCILIAMSLVCSVGSAIWNRRHSGKDWYLNLNYGGASNFGLNFLTFIILFNNLIPISLL
VTLEVVKFTQAYFINWDLDMHYEPTDTAAMARTSNLNEELGQVKYIFSDKTGTLTCNVMQ
FKKCTIAGVAYGHVPEPEDYGCSPDEWQNSQFGDEKTFSDSSLLENLQNNHPTAPIICEF
LTMMAVCHTAVPEREGDKIIYQAASPDEGALVRAAKQLNFVFTGRTPDSVIIDSLGQEER
YELLNVLEFTSARKRMSVIVRTPSGKLRLYCKGADTVIYDRLAETSKYKEITLKHLEQFA
TEGLRTLCFAVAEISESDFQEWRAVYQRASTSVQNRLLKLEESYELIEKNLQLLGATAIE
DKLQDQVPETIETLMKADIKIWILTGDKQETAINIGHSCKLLKKNMGMIVINEGSLDGTR
ETLSRHCTTLGDALRKENDFALIIDGKTLKYALTFGVRQYFLDLALSCKAVICCRVSPLQ
KSEVVEMVKKQVKVVTLAIGDGANDVSMIQTAHVGVGISGNEGLQAANSSDYSIAQFKYL
KNLLMIHGAWNYNRVSKCILYCFYKNIVLYIIEIWFAFVNGFSGQILFERWCIGLYNVMF
TAMPPLTLGIFERSCRKENMLKYPELYKTSQNALDFNTKVFWVHCLNGLFHSVILFWFPL
KALQYGTAFGNGKTSDYLLLGNFVYTFVVITVCLKAGLETSYWTWFSHIAIWGSIALWVV
FFGIYSSLWPAIPMAPDMSGEAAMLFSSGVFWMGLLFIPVASLLLDVVYKVIKRTAFKTL
VDEVQELEAKSQDPGAVVLGKSLTERAQLLKNVFKKNHVNLYRSESLQQNLLHGYAFSQD
ENGIVSQSEVIRAYDTTKQRPDEW
Enzyme 23 Number of Residues 1164
Enzyme 23 Molecular Weight 131371
Enzyme 23 Theoretical pI 6.83
Enzyme 23 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion transporter activity
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • transporter activity
Process
  • cation transport
  • cellular physiological process
  • ion transport
  • metabolism
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 23 General Function Inorganic ion transport and metabolism
Enzyme 23 Specific Function May play a role in the transport of aminophospholipids from the outer to the inner leaflet of various membranes and the maintenance of asymmetric distribution of phospholipids, mainly in secretory vesicles
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 66-86 93-115 298-319 345-366 858-878 891-910 941-962 977-999 1006-1026 1045-1070
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 4972583 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q9Y2Q0 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name AT8A1_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >3492 bp 
ATGCCCACCATGCGGAGGACCGTGTCGGAGATCCGCTCGCGCGCCGAAGGTTATGAGAAG
ACAGATGATGTTTCAGAGAAGACCTCACTGGCTGACCAGGAGGAAGTAAGGACTATTTTC
ATCAACCAGCCCCAGCTGACAAAATTCTGCAATAACCATGTCAGCACTGCAAAATACAAC
ATAATCACATTCCTTCCAAGATTTCTCTACTCTCAGTTCAGAAGAGCTGCTAATTCATTT
TTTCTCTTTATTGCACTGCTGCAGCAAATACCTGATGTGTCACCAACAGGTCGTTATACA
ACACTGGTTCCTCTCTTATTTATTTTAGCTGTGGCAGCTATCAAAGAGATAATAGAAGAT
ATTAAACGACATAAAGCTGATAATGCAGTGAACAAGAAACAAACGCAAGTTTTGAGAAAT
GGTGCTTGGGAAATTGTCCACTGGGAAAAGGTGGCAGTAGGGGAGATAGTGAAAGTGACC
AATGGGGAACATCTCCCAGCAGATCTCATCAGTCTGTCCTCAAGTGAGCCCCAAGCCATG
TGCTACATTGAAACATCCAACTTAGATGGTGAAACAAACTTGAAAATTAGACAGGGCTTA
CCAGCAACATCAGATATCAAAGACGTTGACAGTTTGATGAGGATTTCTGGCAGAATTGAG
TGTGAAAGTCCAAACAGACATCTCTACGATTTTGTTGGAAACATAAGGCTTGATGGACAT
GGCACCGTTCCACTGGGAGCAGATCAGATTCTTCTTCGAGGAGCTCAGTTGAGAAATACA
CAGTGGGTTCATGGAATAGTTGTCTACACTGGACATGACACCAAGCTGATGCAGAATTCA
ACAAGTCCACCACTTAAGCTCTCAAATGTGGAACGGATTACAAATGTACAAATTTTGATT
TTATTTTGTATCTTAATTGCCATGTCTCTTGTCTGTTCTGTGGGCTCAGCCATTTGGAAT
CGAAGGCATTCTGGAAAAGACTGGTATCTCAATCTAAACTATGGTGGCGCTAGTAATTTT
GGACTGAATTTCTTGACCTTCATCATCCTTTTCAACAATCTCATTCCTATCAGCTTATTG
GTTACATTAGAAGTTGTGAAATTTACCCAGGCATACTTCATAAATTGGGATCTTGACATG
CACTATGAACCCACAGACACTGCTGCTATGGCTCGAACATCTAATCTGAATGAGGAACTT
GGCCAGGTTAAATACATATTTTCTGACAAAACTGGTACTCTGACATGCAATGTAATGCAG
TTTAAGAAGTGCACCATAGCGGGAGTTGCTTATGGCCATGTCCCTGAACCTGAGGATTAT
GGCTGCTCTCCTGATGAATGGCAGAACTCACAGTTTGGAGATGAAAAAACATTTAGTGAT
TCATCATTGCTGGAAAATCTCCAAAATAATCATCCAACTGCACCTATAATATGTGAATTT
CTTACAATGATGGCAGTCTGTCACACAGCAGTGCCAGAGCGAGAAGGTGACAAGATTATT
TATCAAGCAGCATCTCCAGATGAGGGAGCATTGGTCAGAGCAGCCAAGCAATTGAATTTT
GTTTTCACTGGAAGAACACCCGACTCGGTGATTATAGATTCACTGGGGCAGGAAGAAAGA
TATGAATTGCTCAATGTCTTGGAGTTTACCAGTGCTAGGAAAAGAATGTCAGTGATTGTT
CGCACTCCATCTGGAAAGTTACGACTCTACTGCAAAGGAGCTGACACTGTAATTTATGAT
CGACTGGCAGAGACGTCAAAATACAAAGAAATTACCCTAAAACATTTAGAGCAGTTTGCT
ACAGAAGGGTTAAGAACTTTATGTTTTGCTGTGGCTGAGATTTCAGAGAGCGACTTTCAG
GAGTGGCGAGCAGTCTATCAGCGAGCATCTACATCTGTGCAGAACAGGCTACTCAAACTC
GAAGAGAGTTATGAGTTGATTGAAAAGAATCTTCAGCTACTTGGAGCAACAGCCATTGAG
GATAAATTACAAGATCAAGTGCCTGAAACCATAGAAACGCTAATGAAAGCAGACATCAAA
ATCTGGATCCTTACAGGGGACAAGCAAGAAACTGCCATTAACATCGGACACTCCTGCAAA
CTGTTGAAGAAGAACATGGGAATGATTGTTATAAATGAAGGCTCTCTTGATGGAACAAGG
GAAACTCTCAGTCGTCACTGTACTACCCTTGGTGATGCTCTCCGGAAAGAGAATGATTTT
GCTCTTATAATTGATGGGAAAACCCTCAAATATGCCTTAACCTTTGGAGTACGACAGTAT
TTCCTGGACTTAGCTTTGTCATGCAAAGCTGTCATTTGCTGTCGGGTTTCTCCTCTTCAA
AAATCTGAAGTTGTTGAGATGGTTAAGAAACAAGTCAAAGTCGTAACGCTTGCAATCGGT
GATGGAGCAAATGATGTCAGCATGATACAGACAGCGCACGTTGGTGTTGGTATCAGTGGC
AATGAAGGCCTGCAGGCAGCTAATTCCTCTGACTACTCCATAGCTCAGTTCAAATATTTG
AAGAATTTACTGATGATTCATGGTGCCTGGAACTATAACAGAGTCTCCAAGTGCATCTTA
TACTGCTTCTACAAGAATATAGTGCTCTATATTATCGAGATCTGGTTTGCCTTTGTTAAT
GGCTTTTCTGGACAGATCCTCTTTGAAAGATGGTGTATAGGTCTCTATAACGTGATGTTT
ACAGCAATGCCTCCTTTAACTCTTGGAATATTTGAGAGATCATGCAGAAAAGAGAACATG
TTGAAGTACCCTGAATTATACAAAACATCTCAGAATGCCCTGGACTTCAACACCAAGGTT
TTCTGGGTTCATTGTTTAAATGGCCTCTTCCACTCAGTTATTCTGTTTTGGTTTCCACTA
AAAGCCCTTCAGTATGGTACTGCATTTGGAAATGGGAAAACCTCGGATTATCTGCTACTG
GGAAACTTTGTGTACACTTTTGTGGTGATAACTGTGTGTTTGAAAGCTGGATTGGAGACA
TCATATTGGACATGGTTCAGCCACATAGCGATATGGGGGAGCATCGCACTCTGGGTGGTG
TTTTTTGGAATCTACTCATCTCTGTGGCCTGCCATTCCGATGGCCCCTGATATGTCAGGA
GAGGCAGCCATGTTGTTCAGTTCTGGAGTCTTTTGGATGGGCTTGTTATTCATCCCTGTG
GCATCTCTGCTCCTTGATGTGGTGTACAAGGTTATCAAGAGGACTGCTTTTAAAACATTG
GTCGATGAAGTTCAGGAGCTGGAGGCAAAATCTCAAGACCCAGGAGCAGTTGTACTTGGA
AAAAGCCTGACCGAGAGGGCGCAACTGCTCAAGAACGTCTTTAAGAAGAACCACGTGAAC
TTGTACCGCTCTGAATCCTTGCAACAAAATCTGCTCCATGGGTATGCGTTCTCTCAAGAT
GAAAATGGAATCGTTTCACAGTCTGAAGTGATAAGAGCATATGATACCACGAAACAGAGG
CCCGACGAATGG
Enzyme 23 GenBank Gene ID AF067820 Link Image
Enzyme 23 GeneCard ID ATP8A1 Link Image
Enzyme 23 GenAtlas ID ATP8A1 Link Image
Enzyme 23 HGNC ID HGNC:13531 Link Image
Enzyme 23 Chromosome Location 4
Enzyme 23 Locus 4p14-p12
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Mouro I, Halleck MS, Schlegel RA, Mattei MG, Williamson P, Zachowski A, Devaux P, Cartron JP, Colin Y: Cloning, expression, and chromosomal mapping of a human ATPase II gene, member of the third subfamily of P-type ATPases and orthologous to the presumed bovine and murine aminophospholipid translocase. Biochem Biophys Res Commun. 1999 Apr 13;257(2):333-9. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 6688
Enzyme 24 Name Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
Enzyme 24 Synonyms
  1. PI3-kinase p110 subunit gamma
  2. PtdIns-3- kinase subunit p110
  3. PI3K
  4. PI3Kgamma
  5. p120-PI3K
Enzyme 24 Gene Name PIK3CG
Enzyme 24 Protein Sequence >Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform 
MELENYKQPVVLREDNCRRRRRMKPRSAAASLSSMELIPIEFVLPTSQRKCKSPETALLH
VAGHGNVEQMKAQVWLRALETSVAADFYHRLGPHHFLLLYQKKGQWYEIYDKYQVVQTLD
CLRYWKATHRSPGQIHLVQRHPPSEESQAFQRQLTALIGYDVTDVSNVHDDELEFTRRGL
VTPRMAEVASRDPKLYAMHPWVTSKPLPEYLWKKIANNCIFIVIHRSTTSQTIKVSPDDT
PGAILQSFFTKMAKKKSLMDIPESQSEQDFVLRVCGRDEYLVGETPIKNFQWVRHCLKNG
EEIHVVLDTPPDPALDEVRKEEWPLVDDCTGVTGYHEQLTIHGKDHESVFTVSLWDCDRK
FRVKIRGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNVWLEFSIKI
KDLPKGALLNLQIYCGKAPALSSKASAESPSSESKGKVQLLYYVNLLLIDHRFLLRRGEY
VLHMWQISGKGEDQGSFNADKLTSATNPDKENSMSISILLDNYCHPIALPKHQPTPDPEG
DRVRAEMPNQLRKQLEAIIATDPLNPLTAEDKELLWHFRYESLKHPKAYPKLFSSVKWGQ
QEIVAKTYQLLARREVWDQSALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYL
LQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLRSEIAQSRHYQQRFAVILEAY
LRGCGTAMLHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLP
ESFRVPYDPGLKAGALAIEKCKVMASKKKPLWLEFKCADPTALSNETIGIIFKHGDDLRQ
DMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTVGNTG
AFKDEVLNHWLKEKSPTEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNL
FHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSPHFQKFQDICVKAYLAL
RHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKNEEDAKKYFLDQIEVCRDKGW
TVQFNWFLHLVLGIKQGEKHSA
Enzyme 24 Number of Residues 1102
Enzyme 24 Molecular Weight 126455
Enzyme 24 Theoretical pI 7.53
Enzyme 24 GO Classification
Function
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • kinase activity
  • lipid kinase activity
  • phosphatidylinositol 3-kinase activity
  • phosphoinositide 3-kinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
—
Component
  • phosphoinositide 3-kinase complex
  • protein complex
Enzyme 24 General Function Not Available
Enzyme 24 Specific Function 3-phosphorylates the cellular phosphoinositide PtdIns- 4,5-biphosphate (PtdIns(4,5)P2) to produce PtdIns-3, 4,5- triiphosphate (PtdIns(3,4,5)P3). Links G-protein coupled receptor activation to the secondary messenger PtdIns(3,4,5)P3 production
Enzyme 24 Pathways
Enzyme 24 Reactions
  • ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 1507822 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P48736 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PK3CG_HUMAN Link Image
Enzyme 24 PDB ID 1E8Z Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >3306 bp 
ATGGAGCTGGAGAACTATAAACAGCCCGTGGTGCTGAGAGAGGACAACTGCCGAAGGCGC
CGGAGGATGAAGCCGCGCAGTGCTGCCAGCCTGTCCTCCATGGAGCTCATCCCCATCGAG
TTCGTGCTGCCCACCAGCCAGCGCAAATGCAAGAGCCCCGAAACGGCGCTGCTGCACGTG
GCCGGCCACGGCAACGTGGAGCAGATGAAGGCCCAGGTGTGGCTGCGAGCGCTGGAGACC
AGCGTGGCGGCGGACTTCTACCACCGGCTGGGACCGCATCACTTCCTCCTGCTCTATCAG
AAGAAGGGGCAGTGGTACGAGATCTACGACAAGTACCAGGTGGTGCAGACTCTGGACTGC
CTGCGCTACTGGAAGGCCACGCACCGGAGCCCGGGCCAGATCCACCTGGTGCAGCGGCAC
CCGCCCTCCGAGGAGTCCCAAGCCTTCCAGCGGCAGCTCACGGCGCTGATTGGCTATGAC
GTCACTGACGTCAGCAACGTGCACGACGATGAGCTGGAGTTCACGCGCCGTGGCTTGGTG
ACCCCGCGCATGGCGGAGGTGGCCAGCCGCGACCCCAAGCTCTACGCCATGCACCCGTGG
GTGACGTCCAAGCCCCTCCCGGAGTACCTGTGGAAGAAGATTGCCAACAACTGCATCTTC
ATCGTCATTCACCGCAGCACCACCAGCCAGACCATTAAGGTCTCACCCGACGACACCCCC
GGCGCCATCCTGCAGAGCTTCTTCACCAAGATGGCCAAGAAGAAATCTCTGATGGATATT
CCCGAAAGCCAAAGCGAACAGGATTTTGTGCTGCGCGTCTGTGGCCGGGATGAGTACCTG
GTGGGCGAAACGCCCATCAAAAACTTCCAGTGGGTGAGGCACTGCCTCAAGAACGGAGAA
GAGATTCACGTGGTACTGGACACGCCTCCAGACCCGGCCCTAGACGAGGTGAGGAAGGAA
GAGTGGCCGCTGGTGGACGACTGCACGGGAGTCACCGGCTACCATGAGCAGCTTACCATC
CACGGCAAGGACCACGAGAGTGTGTTCACCGTGTCCCTGTGGGACTGCGACCGCAAGTTC
AGGGTCAAGATCAGAGGCATTGATATCCCCGTCCTGCCTCGGAACACCGACCTCACAGTT
TTTGTAGAGGCAAACATCCAGCATGGGCAACAAGTCCTTTGCCAAAGGAGAACCAGCCCC
AAACCCTTCACAGAGGAGGTGCTGTGGAATGTGTGGCTTGAGTTCAGTATCAAAATCAAA
GACTTGCCCAAAGGGGCTCTACTGAACCTCCAGATCTACTGCGGTAAAGCTCCAGCACTG
TCCAGCAAGGCCTCTGCAGAGTCCCCCAGTTCTGAGTCCAAGGGCAAAGTTCGGCTTCTC
TATTATGTGAACCTGCTGCTGATAGACCACCGTTTCCTCCTGCGCCGTGGAGAATACGTC
CTCCACATGTGGCAGATATCTGGGAAGGGAGAAGACCAAGGAAGCTTCAATGCTGACAAA
CTCACGTCTGCAACTAACCCAGACAAGGAGAACTCAATGTCCATCTCCATTCTTCTGGAC
AATTACTGCCACCCGATAGCCCTGCCTAAGCATCAGCCCACCCCTGACCCGGAAGGGGAC
CGGGTTCGAGCAGAAATGCCCAACCAGCTTCGCAAGCAATTGGAGGCGATCATAGCCACT
GATCCACTTAACCCTCTCACAGCAGAGGACAAAGAATTGCTCTGGCATTTTAGATACGAA
AGCCTTAAGCACCCAAAAGCATATCCTAAGCTATTTAGTTCAGTGAAATGGGGACAGCAA
GAAATTGTGGCCAAAACATACCAATTGTTGGCCAGAAGGGAAGTCTGGGATCAAAGTGCT
TTGGATGTTGGGTTAACAATGCAGCTCCTGGACTGCAACTTCTCAGATGAAAATGTAAGA
GCCATTGCAGTTCAGAAACTGGAGAGCTTGGAGGACGATGATGTTCTGCATTACCTTCTA
CAATTGGTCCAGGCTGTGAAATTTGAACCATACCATGATAGCGCCCTTGCCAGATTTCTG
CTGAAGCGTGGTTTAAGAAACAAAAGAATTGGTCACTTTTTGTTTTGGTTCTTGAGAAGT
GAGATAGCCCAGTCCAGACACTATCAGCAGAGGTTCGCTGTGATTCTGGAAGCCTATCTG
AGGGGCTGTGGCACAGCCATGCTGCACGACTTTACCCAACAAGTCCAAGTAATCGAGATG
TTACAAAAAGTCACCCTTGATATTAAATCGCTCTCTGCTGAAAAGTATGACGTCAGTTCC
CAAGTTATTTCACAACTTAAACAAAAGCTTGAAAACCTGCAGAATTCTCAACTCCCCGAA
AGCTTTAGAGTTCCATATGATCCTGGACTGAAAGCAGGAGCGCTGGCAATTGAAAAATGT
AAAGTAATGGCCTCCAAGAAAAAACCACTATGGCTTGAGTTTAAATGTGCCGATCCTACA
GCCCTATCAAATGAAACAATTGGAATTATCTTTAAACATGGTGATGATCTGCGCCAAGAC
ATGCTTATTTTACAGATTCTACGAATCATGGAGTCTATTTGGGAGACTGAATCTTTGGAT
CTATGCCTCCTGCCATATGGTTGCATTTCAACTGGTGACAAAATAGGAATGATCGAGATT
GTGAAAGACGCCACGACAATTGCCAAAATTCAGCAAAGCACAGTGGGCAACACGGGAGCA
TTTAAAGATGAAGTCCTGAATCACTGGCTCAAAGAAAAATCCCCTACTGAAGAAAAGTTT
CAGGCAGCAGTGGAGAGATTTGTTTATTCCTGTGCAGGCTACTGTGTGGCAACCTTTGTT
CTTGGAATAGGCGACAGACACAATGACAATATTATGATCACCGAGACAGGAAACCTATTT
CATATTGACTTCGGGCACATTCTTGGGAATTACAAAAGTTTCCTGGGCATTAATAAAGAG
AGAGTGCCATTTGTGCTAACCCCTGACTTCCTCTTTGTGATGGGAACTTCTGGAAAGAAG
ACAAGCCCACACTTCCAGAAATTTCAGGACATCTGTGTTAAGGCTTATCTAGCCCTTCGT
CATCACACAAACCTACTGATCATCCTGTTCTCCATGATGCTGATGACAGGAATGCCCCAG
TTAACAAGCAAAGAAGACATTGAATATATCCGGGATGCCCTCACAGTGGGGAAAAATGAG
GAGGATGCTAAAAAGTATTTTCTTGATCAGATCGAAGTTTGCAGAGACAAAGGATGGACT
GTGCAGTTTAATTGGTTTCTACATCTTGTTCTTGGCATCAAACAAGGAGAGAAACATTCA
GCCTAA
Enzyme 24 GenBank Gene ID X83368 Link Image
Enzyme 24 GeneCard ID PIK3CG Link Image
Enzyme 24 GenAtlas ID PIK3CG Link Image
Enzyme 24 HGNC ID HGNC:8978 Link Image
Enzyme 24 Chromosome Location 7
Enzyme 24 Locus 7q22.3
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Stoyanov B, Volinia S, Hanck T, Rubio I, Loubtchenkov M, Malek D, Stoyanova S, Vanhaesebroeck B, Dhand R, Nurnberg B, et al.: Cloning and characterization of a G protein-activated human phosphoinositide-3 kinase. Science. 1995 Aug 4;269(5224):690-3. [PubMed Link Image]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 6759
Enzyme 25 Name Probable phospholipid-transporting ATPase IM
Enzyme 25 Synonyms
  1. ATPase class I type 8B member 4
Enzyme 25 Gene Name ATP8B4
Enzyme 25 Protein Sequence >Probable phospholipid-transporting ATPase IM 
MFCSEKKLREVERIVKANDREYNEKFQYADNRIHTSKYNILTFLPINLFEQFQRVANAYF
LCLLILQLIPEISSLTWFTTIVPLVLVITMTAVKDATDDYFRHKSDNQVNNRQSEVLINS
KLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRHALS
VTSELGADISRLAGFDGIVVCEVPNNKLDKFMGILSWKDSKHSLNNEKIILRGCILRNTS
WCFGMVIFAGPDTKLMQNSGKTKFKRTSIDRLMNTLVLWIFGFLICLGIILAIGNSIWES
QTGDQFRTFLFWNEGEKSSVFSGFLTFWSYIIILNTVVPISLYVSVEVIRLGHSYFINWD
RKMYYSRKAIPAVARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKRCSINGRIYGEVHDD
LDQKTEITQEKEPVDFSVKSQADREFQFFDHHLMESIKMGDPKVHEFLRLLALCHTVMSE
ENSAGELIYQVQSPDEGALVTAARNFGFIFKSRTPETITIEELGTLVTYQLLAFLDFNNT
RKRMSVIVRNPEGQIKLYSKGADTILFEKLHPSNEVLLSLTSDHLSEFAGEGLRTLAIAY
RDLDDKYFKEWHKMLEDANAATEERDERIAELYEEIERDLMLLGATAVEDKLQEGVIETV
TSLSLANIKIWVLTGDKQETAINIGYACNMLTDDMNDVFVIAGNNAVEVREELRKAKQNL
FGQNRNFSNGHVVCEKKQQLELDSIVEETITGDYALIINGHSLAHALESDVKNDLLELAC
MCKTVICCRVTPLQKAQVVELVKKYRNAVTLAIGDGANDVSMIKSAHIGVGISGQEGLQA
VLASDYSFAQFRYLQRLLLVHGRWSYFRMCKFLCYFFYKNFAFTLVHFWFGFFCGFSAQT
VYDQWFITLFNIVYTSLPVLAMGIFDQDVSDQNSVDCPQLYKPGQLNLLFNKRKFFICVL
HGIYTSLVLFFIPYGAFYNVAGEDGQHIADYQSFAVTMATSLVIVVSVQIALDTSYWTFI
NHVFIWGSIAIYFSILFTMHSNGIFGIFPNQFPFVGNARHSLTQKCIWLVILLTTVASVM
PVVAFRFLKVDLYPTLSDQIRRWQKAQKKARPPSSRRPRTRRSSSRRSGYAFAHQEGYGE
LITSGKNMRAKNPPPTSGLEKTHYNSTSWIENLCKKTTDTVSSFSQDKTVKL
Enzyme 25 Number of Residues 1192
Enzyme 25 Molecular Weight 135942
Enzyme 25 Theoretical pI 6.92
Enzyme 25 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion transporter activity
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • transporter activity
Process
  • cation transport
  • cellular physiological process
  • ion transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 25 General Function Inorganic ion transport and metabolism
Enzyme 25 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • 45-66 73-92 277-298 328-349 872-892 905-924 955-976 991-1013 1020-1040 1061-1085
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 18916718 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q8TF62 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name AT8B4_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >3249 bp 
GGAAGAAGATTTATCCTGGTCCTGAGAAAAATACTGCAGAATGAAAAATGGATGAATGTC
AAAGTGGGAGACATCATTAAATTAGAAAATAACCAATTTGTTGCTGCTGATTTACTTCTC
CTATCAAGTAGTGAGCCACATGGTCTCTGTTATGTTGAAACTGCTGAGCTTGATGGGGAA
ACGAACCTAAAAGTCCGCCATGCACTATCAGTTACTTCAGAACTTGGAGCAGATATCAGC
AGACTTGCAGGGTTTGATGGGATTGTTGTCTGTGAGGTGCCTAACAACAAGTTAGATAAA
TTCATGGGAATCCTTTCTTGGAAAGACAGCAAGCATTCCCTCAACAATGAGAAGATAATC
CTGAGAGGCTGCATCCTGAGAAATACCAGCTGGTGTTTTGGAATGGTTATTTTTGCAGGT
CCTGACACTAAACTAATGCAGAATAGTGGTAAGACAAAGTTTAAAAGGACAAGCATTGAT
AGATTGATGAATACTCTAGTACTATGGATTTTTGGGTTTCTGATATGCTTGGGAATTATT
CTTGCAATAGGAAATTCAATCTGGGAGAGTCAAACTGGGGACCAATTCAGAACTTTCCTC
TTTTGGAATGAAGGAGAGAAGAGCTCTGTGTTCTCCGGATTCTTAACATTCTGGTCATAT
ATTATTATTCTCAATACAGTTGTACCCATTTCCTTATATGTGAGTGTGGAAGTAATTCGT
CTAGGACACAGTTATTTTATAAACTGGGACCGGAAGATGTATTATTCTCGAAAAGCAATA
CCTGCAGTGGCTCGAACGACCACGCTCAATGAGGAACTGGGGCAGATTGAGTACATTTTC
TCCGACAAAACGGGTACCCTCACTCAAAACATCATGACCTTTAAAAGATGTTCCATTAAT
GGGAGAATCTATGGTGAAGTACATGATGACCTGGATCAGAAGACAGAAATAACTCAGGAA
AAAGAGCCTGTGGATTTCTCAGTCAAATCTCAAGCGGATAGAGAATTTCAGTTCTTTGAC
CACCATCTGATGGAATCCATTAAAATGGGTGATCCCAAAGTTCATGAATTCCTTAGGTTA
CTTGCTCTCTGCCACACTGTAATGTCAGAAGAGAATAGCGCAGGAGAGCTGATTTACCAA
GTTCAGTCACCTGATGAAGGGGCTCTAGTGACTGCCGCTAGAAATTTTGGGTTCATTTTT
AAATCCCGGACCCCAGAGACCATAACAATAGAAGAATTGGGAACACTAGTTACTTATCAA
TTACTTGCCTTTTTGGATTTCAACAACACCAGAAAAAGGATGTCTGTCATAGTTCGAAAC
CCAGAAGGACAGATAAAGCTTTATTCCAAAGGAGCAGATACTATTCTGTTTGAAAAACTT
CATCCTTCCAATGAAGTCCTTTTGTCTTTGACGTCAGACCACCTCAGTGAATTTGCAGGG
GAAGGCCTTCGGACCTTGGCCATCGCATACAGAGACCTGGATGACAAGTACTTTAAAGAG
TGGCATAAGATGCTTGAAGATGCGAATGCTGCCACAGAAGAGAGGGATGAACGAATAGCT
GAGCTATATGAAGAAATTGAAAGAGATTTGATGCTACTAGGTGCCACTGCTGTAGAAGAT
AAGTTACAGGAGGGTGTTATTGAAACAGTTACAAGTTTATCACTAGCCAATATTAAGATC
TGGGTCCTAACAGGAGACAAACAAGAAACTGCCATCAACATCGGTTATGCCTGCAACATG
CTGACTGACGACATGAATGATGTGTTTGTGATAGCAGGGAATAATGCTGTGGAAGTGAGA
GAAGAACTCAGGAAAGCAAAACAAAATTTGTTTGGACAAAACAGAAATTTTTCCAATGGC
CATGTAGTTTGTGAAAAAAAGCAGCAGCTGGAGTTGGATTCTATTGTAGAAGAAACCATA
ACAGGAGATTATGCCTTAATCATAAATGGCCACAGTTTGGCTCATGCCCTAGAAAGTGAT
GTCAAGAATGATCTCCTAGAACTTGCTTGCATGTGTAAGACTGTAATTTGCTGCAGGGTC
ACTCCACTCCAGAAAGCCCAAGTGGTAGAGCTGGTGAAGAAGTACAGAAATGCTGTTACT
TTGGCCATTGGTGATGGAGCCAATGATGTCAGCATGATTAAAAGTGCTCACATTGGTGTT
GGCATCAGCGGCCAGGAAGGATTGCAAGCAGTCTTAGCCAGCGACTATTCATTTGCACAG
TTTAGATATCTCCAAAGGCTTCTCCTTGTTCATGGAAGGTGGTCTTATTTCCGAATGTGC
AAATTCTTATGCTATTTCTTCTATAAGAATTTTGCATTTACACTTGTGCATTTCTGGTTT
GGTTTCTTCTGTGGTTTCTCAGCCCAGACTGTTTATGACCAGTGGTTCATCACCCTTTTT
AACATTGTTTACACATCACTGCCTGTTTTAGCCATGGGGATTTTTGACCAGGATGTGAGT
GACCAGAACAGCGTGGACTGTCCCCAGCTCTACAAACCAGGACAGCTGAATCTGCTTTTT
AACAAGCGTAAATTTTTCATTTGCGTGTTGCATGGAATCTACACCTCATTAGTCCTTTTC
TTCATCCCCTATGGGGCCTTTTACAACGTGGCTGGAGAAGATGGGCAACATATTGCTGAC
TACCAGTCCTTTGCAGTTACCATGGCCACATCTTTGGTCATTGTGGTCAGTGTGCAGATA
GCCTTGGATACCAGTTACTGGACTTTCATTAATCACGTCTTCATCTGGGGGAGCATTGCC
ATTTATTTCTCCATTTTATTTACAATGCACAGTAATGGCATCTTTGGCATCTTCCCAAAC
CAGTTTCCATTTGTTGGTAATGCACGACATTCCCTGACCCAGAAGTGCATCTGGCTTGTA
ATTCTCTTAACAACAGTGGCTTCAGTTATGCCAGTGGTGGCATTCAGATTTTTGAAGGTG
GATTTATACCCAACCCTGAGTGATCAGATCCGCCGGTGGCAGAAGGCTCAAAAGAAGGCA
AGGCCTCCAAGTAGCCGAAGGCCTCGGACCCGCAGGTCAAGCTCAAGAAGGTCTGGATAT
GCTTTTGCTCACCAAGAAGGCTATGGAGAGCTTATCACATCTGGAAAAAATATGCGAGCT
AAAAATCCACCCCCAACATCAGGGCTGGAAAAGACACATTATAATAGCACTAGCTGGATT
GAAAATTTATGTAAGAAAACCACAGACACCGTGAGCAGCTTTAGCCAGGATAAAACAGTG
AAACTGTGA
Enzyme 25 GenBank Gene ID AB075819 Link Image
Enzyme 25 GeneCard ID ATP8B4 Link Image
Enzyme 25 GenAtlas ID ATP8B4 Link Image
Enzyme 25 HGNC ID HGNC:13536 Link Image
Enzyme 25 Chromosome Location 15
Enzyme 25 Locus 15q21.2
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 6781
Enzyme 26 Name Probable phospholipid-transporting ATPase IF
Enzyme 26 Synonyms
  1. ATPase class I type 11B
  2. ATPase IR
Enzyme 26 Gene Name ATP11B
Enzyme 26 Protein Sequence >Probable phospholipid-transporting ATPase IF 
MWRWIRQQLGFDPPHQSDTRTIYVANRFPQNGLYTPQKFIDNRIISSKYTVWNFVPKNLF
EQFRRVANFYFLIIFLVQLMIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHNSDNEVN
GAPVYVVRSGGLVKTRSKNIRVGDIVRIAKDEIFPADLVLLSSDRLDGSCHVTTASLDGE
TNLKTHVAVPETALLQTVANLDTLVAVIECQQPEADLYRFMGRMIITQQMEEIVRPLGPE
SLLLRGARLKNTKEIFGVAVYTGMETKMALNYKSKSQKRSAVEKSMNTFLIIYLVILISE
AVISTILKYTWQAEEKWDEPWYNQKTEHQRNSSKILRFISDFLAFLVLYNFIIPISLYVT
VEMQKFLGSFFIGWDLDLYHEESDQKAQVNTSDLNEELGQVEYVFTDKTGTLTENEMQFR
ECSINGMKYQEINGRLVPEGPTPDSSEGNLSYLSSLSHLNNLSHLTTSSSFRTSPENETE
LIKEHDLFFKAVSLCHTVQISNVQTDCTGDGPWQSNLAPSQLEYYASSPDEKALVEAAAR
IGIVFIGNSEETMEVKTLGKLERYKLLHILEFDSDRRRMSVIVQAPSGEKLLFAKGAESS
ILPKCIGGEIEKTRIHVDEFALKGLRTLCIAYRKFTSKEYEEIDKRIFEARTALQQREEK
LAAVFQFIEKDLILLGATAVEDRLQDKVRETIEALRMAGIKVWVLTGDKHETAVSVSLSC
GHFHRTMNILELINQKSDSECAEQLRQLARRITEDHVIQHGLVVDGTSLSLALREHEKLF
MEVCRNCSAVLCCRMAPLQKAKVIRLIKISPEKPITLAVGDGANDVSMIQEAHVGIGIMG
KEGRQAARNSDYAIARFKFLSKLLFVHGHFYYIRIATLVQYFFYKNVCFITPQFLYQFYC
LFSQQTLYDSVYLTLYNICFTSLPILIYSLLEQHVDPHVLQNKPTLYRDISKNRLLSIKT
FLYWTILGFSHAFIFFFGSYLLIGKDTSLLGNGQMFGNWTFGTLVFTVMVITVTVKMALE
THFWTWINHLVTWGSIIFYFVFSLFYGGILWPFLGSQNMYFVFIQLLSSGSAWFAIILMV
VTCLFLDIIKKVFDRHLHPTSTEKAQLTETNAGIKCLDSMCCFPEGEAACASVGRMLERV
IGRCSPTHISRSWSASDPFYTNDRSILTLSTMDSSTC
Enzyme 26 Number of Residues 1177
Enzyme 26 Molecular Weight 134191
Enzyme 26 Theoretical pI 6.95
Enzyme 26 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion transporter activity
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • transporter activity
Process
  • cation transport
  • cellular physiological process
  • ion transport
  • metabolism
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 26 General Function Inorganic ion transport and metabolism
Enzyme 26 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • 56-77 83-104 290-311 342-359 877-898 911-930 961-982 998-1020 1026-1047 1066-1090
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 6457268 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q9Y2G3 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name AT11B_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >744 bp 
ATGTGGCGCTGGATCCGGCAGCAGCTGGGTTTTGACCCACCACATCAGAGTGACACAAGA
ACCATCTACGTAGCCAACAGGTTTCCTCAGAATGGCCTTTACACACCTCAGAAATTTATA
GATAACAGGATCATTTCATCTAAGTACACTGTGTGGAATTTTGTTCCAAAAAATTTATTT
GAACAGTTCAGAAGAGTGGCAAACTTTTATTTTCTTATTATATTTTTGGTTCAGCTTATG
ATTGATACACCTACCAGTCCAGTTACCAGTGGACTTCCATTATTCTTTGTGATAACAGTA
ACTGCCATAAAGCAGGGATATGAAGATTGGTTACGGCATAANTCAGATAATGAAGTAAAT
GGAGCTCCTGTTTATGTTGTTCGAAGTGGTGGCCTTGTAAAAACTAGATCAAAAAACATT
CGGGTGGGTGATATTGTTCGAATAGCCAAAGATGAAATTTTTCCTGCAGACTTGGTGCTT
CTGTCCTCAGATCGACTGGATGGTTCCTGTCACGTTACAACTGCTAGTTTGGACGGAGAA
ACTAACCTGAAGACACATGTGGCAGTTCCAGAAACAGCATTATTACAAACAGTTGCCAAT
TTGGACACTCTAGTAGCTGTAATAGAATGCCAGCAACCAGAAGCAGACTTATACAGATTC
ATGGGACGAATGATCATAACCCAACAAATGGAAGAAATTGTAAGACCTCTGGGGCCGGAG
AGTCTCCTGCTTCGTGGAGCCAGA
Enzyme 26 GenBank Gene ID AF156548 Link Image
Enzyme 26 GeneCard ID ATP11B Link Image
Enzyme 26 GenAtlas ID ATP11B Link Image
Enzyme 26 HGNC ID HGNC:13553 Link Image
Enzyme 26 Chromosome Location 3
Enzyme 26 Locus 3q27
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Halleck MS, Lawler JF JR, Blackshaw S, Gao L, Nagarajan P, Hacker C, Pyle S, Newman JT, Nakanishi Y, Ando H, Weinstock D, Williamson P, Schlegel RA: Differential expression of putative transbilayer amphipath transporters. Physiol Genomics. 1999 Nov 11;1(3):139-50. [PubMed Link Image]
  2. Halleck MS, Schlegel RA, Williamson PL: Reanalysis of ATP11B, a type IV P-type ATPase. J Biol Chem. 2002 Mar 22;277(12):9736-40. Epub 2002 Jan 14. [PubMed Link Image]
  3. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Feb 26;6(1):63-70. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 6785
Enzyme 27 Name Probable phospholipid-transporting ATPase IK
Enzyme 27 Synonyms
  1. ATPase class I type 8B member 3
Enzyme 27 Gene Name ATP8B3
Enzyme 27 Protein Sequence >Probable phospholipid-transporting ATPase IK 
MGTGPAQTPRSTRAGPEPSPAPPGPGDTGDSDVTQEGSGPAGIRGGETVIRAGMGDSPGR
GAPERRHKAQPGRARKYEWRPEGPTSMGSLGQREDLQDEDRNSAFTWKVQANNRAYNGQF
KEKVILCWQRKKYKTNVIRTAKYNFYSFLPLNLYEQFHRVSNLFFLIIIILQSIPDISTL
PWFSLSTPMVCLLFIRATRDLVDDMGRHKSDRAINNRPCQILMGKSFKQKKWQDLCVGDV
VCLRKDNIVPADMLLLASTEPSSLCYVETVDIDGETNLKFRQALMVTHKELATIKKMASF
QGTVTCEAPNSRMHHFVGCLEWNDKKYSLDIGNLLLRGCRIRNTDTCYGLVIYAGFDTKI
MKNCGKIHLKRTKLDLLMNKLVVVIFISVVLVCLVLAFGFGFSVKEFKDHHYYLSGVHGS
SVAAESFFVFWSFLILLSVTIPMSMFILSEFIYLGNSVFIDWDVQMYYKPQDVPAKARST
SLNDHLGQVEYIFSDKTGTLTQNILTFNKCCISGRVYGPDSEATTRPKENPYLWNKFADG
KLLFHNAALLHLVRTNGDEAVREFWRLLAICHTVMVRESPRERPDQLLYQAASPDEGALV
TAARNFGYVFLSRTQDTVTIMELGEERVYQVLAIMDFNSTRKRMSVLVRKPEGAICLYTK
GADTVIFERLHRRGAMEFATEEALAAFAQETLRTLCLAYREVAEDIYEDWQQRHQEASLL
LQNRAQALQQVYNEMEQDLRLLGATAIEDRLQDGVPETIKCLKKSNIKIWVLTGDKQETA
VNIGFACELLSENMLILEEKEISRILETYWENSNNLLTRESLSQVKLALVINGDFLDKLL
VSLRKEPRALAQNVNMDEAWQELGQSRRDFLYARRLSLLCRRFGLPLAAPPAQDSRARRS
SEVLQERAFVDLASKCQAVICCRVTPKQKALIVALVKKYHQVVTLAIGDGANDINMIKTA
DVGVGLAGQEGMQAVQNSDFVLGQFCFLQRLLLVHGRWSYVRICKFLRYFFYKSMASMMV
QVWFACYNGFTGQPLYEGWFLALFNLLYSTLPVLYIGLFEQDVSAEQSLEKPELYVVGQK
DELFNYWVFVQAIAHGVTTSLVNFFMTLWISRDTAGPASFSDHQSFAVVVALSCLLSITM
EVILIIKYWTALCVATILLSLGFYAIMTTTTQSFWLFRVSPTTFPFLYADLSVMSSPSIL
LVVLLSVSINTFPVLALRVIFPALKELRAKEEKVEEGPSEEIFTMEPLPHVHRESRARRS
SYAFSHREGYANLITQGTILRRGPGVSSDIASESLDPSDEEAASSPKESQ
Enzyme 27 Number of Residues 1310
Enzyme 27 Molecular Weight 148032
Enzyme 27 Theoretical pI 7.80
Enzyme 27 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion transporter activity
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • transporter activity
Process
  • cation transport
  • cellular physiological process
  • ion transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 27 General Function Inorganic ion transport and metabolism
Enzyme 27 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • 150-171 178-197 382-403 431-452 1006-1026 1039-1058 1089-1110 1123-1145 1152-1172 1193-1217
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein Not Available
Enzyme 27 UniProtKB/Swiss-Prot ID O60423 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name AT8B3_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence Not Available
Enzyme 27 GenBank Gene ID AC004755 Link Image
Enzyme 27 GeneCard ID ATP8B3 Link Image
Enzyme 27 GenAtlas ID ATP8B3 Link Image
Enzyme 27 HGNC ID HGNC:13535 Link Image
Enzyme 27 Chromosome Location 19
Enzyme 27 Locus 19p13.3
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References Not Available
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 6866
Enzyme 28 Name Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual- specificity protein phosphatase PTEN
Enzyme 28 Synonyms
  1. Phosphatase and tensin homolog
  2. Mutated in multiple advanced cancers 1
Enzyme 28 Gene Name PTEN
Enzyme 28 Protein Sequence >Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual- specificity protein phosphatase PTEN 
MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSK
HKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVA
AIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSY
LLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMY
FEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEI
DSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEAS
SSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV
Enzyme 28 Number of Residues 403
Enzyme 28 Molecular Weight 47167
Enzyme 28 Theoretical pI 6.33
Enzyme 28 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoprotein phosphatase activity
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
  • protein tyrosine phosphatase activity
  • protein tyrosine/serine/threonine phosphatase activity
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid dephosphorylation
  • protein modification
Component
—
Enzyme 28 General Function Signal transduction mechanisms
Enzyme 28 Specific Function Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine- phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3- phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K- AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue
Enzyme 28 Pathways
Enzyme 28 Reactions
  • phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 2039370 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID P60484 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name PTEN_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1212 bp 
ATGACAGCCATCATCAAAGAGATCGTTAGCAGAAACAAAAGGAGATATCAAGAGGATGGA
TTCGACTTAGACTTGACCTATATTTATCCAAACATTATTGCTATGGGATTTCCTGCAGAA
AGACTTGAAGGCGTATACAGGAACAATATTGATGATGTAGTAAGGTTTTTGGATTCAAAG
CATAAAAACCATTACAAGATATACAATCTTTGTGCTGAAAGACATTATGACACCGCCAAA
TTTAATTGCAGAGTTGCACAATATCCTTTTGAAGACCATAACCCACCACAGCTAGAACTT
ATCAAACCCTTTTGTGAAGATCTTGACCAATGGCTAAGTGAAGATGACAATCATGTTGCA
GCAATTCACTGTAAAGCTGGAAAGGGACGAACTGGTGTAATGATATGTGCATATTTATTA
CATCGGGGCAAATTTTTAAAGGCACAAGAGGCCCTAGATTTCTATGGGGAAGTAAGGACC
AGAGACAAAAAGGGAGTAACTATTCCCAGTCAGAGGCGCTATGTGTATTATTATAGCTAC
CTGTTAAAGAATCATCTGGATTATAGACCAGTGGCACTGTTGTTTCACAAGATGATGTTT
GAAACTATTCCAATGTTCAGTGGCGGAACTTGCAATCCTCAGTTTGTGGTCTGCCAGCTA
AAGGTGAAGATATATTCCTCCAATTCAGGACCCACACGACGGGAAGACAAGTTCATGTAC
TTTGAGTTCCCTCAGCCGTTACCTGTGTGTGGTGATATCAAAGTAGAGTTCTTCCACAAA
CAGAACAAGATGCTAAAAAAGGACAAAATGTTTCACTTTTGGGTAAATACATTCTTCATA
CCAGGACCAGAGGAAACCTCAGAAAAAGTAGAAAATGGAAGTCTATGTGATCAAGAAATC
GATAGCATTTGCAGTATAGAGCGTGCAGATAATGACAAGGAATATCTAGTACTTACTTTA
ACAAAAAATGATCTTGACAAAGCAAATAAAGACAAAGCCAACCGATACTTTTCTCCAAAT
TTTAAGGTGAAGCTGTACTTCACAAAAACAGTAGAGGAGCCGTCAAATCCAGAGGCTAGC
AGTTCAACTTCTGTAACACCAGATGTTAGTGACAATGAACCTGATCATTATAGATATTCT
GACACCACTGACTCTGATCCAGAGAATGAACCTTTTGATGAAGATCAGCATACACAAATT
ACAAAAGTCTGA
Enzyme 28 GenBank Gene ID U96180 Link Image
Enzyme 28 GeneCard ID PTEN Link Image
Enzyme 28 GenAtlas ID PTEN Link Image
Enzyme 28 HGNC ID HGNC:9588 Link Image
Enzyme 28 Chromosome Location 10
Enzyme 28 Locus 10q23.3
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Li DM, Sun H: TEP1, encoded by a candidate tumor suppressor locus, is a novel protein tyrosine phosphatase regulated by transforming growth factor beta. Cancer Res. 1997 Jun 1;57(11):2124-9. [PubMed Link Image]
  2. Steck PA, Pershouse MA, Jasser SA, Yung WK, Lin H, Ligon AH, Langford LA, Baumgard ML, Hattier T, Davis T, Frye C, Hu R, Swedlund B, Teng DH, Tavtigian SV: Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers. Nat Genet. 1997 Apr;15(4):356-62. [PubMed Link Image]
  3. Li J, Yen C, Liaw D, Podsypanina K, Bose S, Wang SI, Puc J, Miliaresis C, Rodgers L, McCombie R, Bigner SH, Giovanella BC, Ittmann M, Tycko B, Hibshoosh H, Wigler MH, Parsons R: PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science. 1997 Mar 28;275(5308):1943-7. [PubMed Link Image]
  4. Myers MP, Stolarov JP, Eng C, Li J, Wang SI, Wigler MH, Parsons R, Tonks NK: P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase. Proc Natl Acad Sci U S A. 1997 Aug 19;94(17):9052-7. [PubMed Link Image]
  5. Maehama T, Dixon JE: The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem. 1998 May 29;273(22):13375-8. [PubMed Link Image]
  6. Wu X, Hepner K, Castelino-Prabhu S, Do D, Kaye MB, Yuan XJ, Wood J, Ross C, Sawyers CL, Whang YE: Evidence for regulation of the PTEN tumor suppressor by a membrane-localized multi-PDZ domain containing scaffold protein MAGI-2. Proc Natl Acad Sci U S A. 2000 Apr 11;97(8):4233-8. [PubMed Link Image]
  7. Vazquez F, Grossman SR, Takahashi Y, Rokas MV, Nakamura N, Sellers WR: Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex. J Biol Chem. 2001 Dec 28;276(52):48627-30. Epub 2001 Nov 13. [PubMed Link Image]
  8. Miller SJ, Lou DY, Seldin DC, Lane WS, Neel BG: Direct identification of PTEN phosphorylation sites. FEBS Lett. 2002 Sep 25;528(1-3):145-53. [PubMed Link Image]
  9. Lee JO, Yang H, Georgescu MM, Di Cristofano A, Maehama T, Shi Y, Dixon JE, Pandolfi P, Pavletich NP: Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Cell. 1999 Oct 29;99(3):323-34. [PubMed Link Image]
  10. Tsou HC, Teng DH, Ping XL, Brancolini V, Davis T, Hu R, Xie XX, Gruener AC, Schrager CA, Christiano AM, Eng C, Steck P, Ott J, Tavtigian SV, Peacocke M: The role of MMAC1 mutations in early-onset breast cancer: causative in association with Cowden syndrome and excluded in BRCA1-negative cases. Am J Hum Genet. 1997 Nov;61(5):1036-43. [PubMed Link Image]
  11. Lynch ED, Ostermeyer EA, Lee MK, Arena JF, Ji H, Dann J, Swisshelm K, Suchard D, MacLeod PM, Kvinnsland S, Gjertsen BT, Heimdal K, Lubs H, Moller P, King MC: Inherited mutations in PTEN that are associated with breast cancer, cowden disease, and juvenile polyposis. Am J Hum Genet. 1997 Dec;61(6):1254-60. [PubMed Link Image]
  12. Nelen MR, van Staveren WC, Peeters EA, Hassel MB, Gorlin RJ, Hamm H, Lindboe CF, Fryns JP, Sijmons RH, Woods DG, Mariman EC, Padberg GW, Kremer H: Germline mutations in the PTEN/MMAC1 gene in patients with Cowden disease. Hum Mol Genet. 1997 Aug;6(8):1383-7. [PubMed Link Image]
  13. Liaw D, Marsh DJ, Li J, Dahia PL, Wang SI, Zheng Z, Bose S, Call KM, Tsou HC, Peacocke M, Eng C, Parsons R: Germline mutations of the PTEN gene in Cowden disease, an inherited breast and thyroid cancer syndrome. Nat Genet. 1997 May;16(1):64-7. [PubMed Link Image]
  14. Marsh DJ, Dahia PL, Zheng Z, Liaw D, Parsons R, Gorlin RJ, Eng C: Germline mutations in PTEN are present in Bannayan-Zonana syndrome. Nat Genet. 1997 Aug;16(4):333-4. [PubMed Link Image]
  15. Chi SG, Kim HJ, Park BJ, Min HJ, Park JH, Kim YW, Dong SH, Kim BH, Lee JI, Chang YW, Chang R, Kim WK, Yang MH: Mutational abrogation of the PTEN/MMAC1 gene in gastrointestinal polyps in patients with Cowden disease. Gastroenterology. 1998 Nov;115(5):1084-9. [PubMed Link Image]
  16. Tsou HC, Ping XL, Xie XX, Gruener AC, Zhang H, Nini R, Swisshelm K, Sybert V, Diamond TM, Sutphen R, Peacocke M: The genetic basis of Cowden's syndrome: three novel mutations in PTEN/MMAC1/TEP1. Hum Genet. 1998 Apr;102(4):467-73. [PubMed Link Image]
  17. Marsh DJ, Coulon V, Lunetta KL, Rocca-Serra P, Dahia PL, Zheng Z, Liaw D, Caron S, Duboue B, Lin AY, Richardson AL, Bonnetblanc JM, Bressieux JM, Cabarrot-Moreau A, Chompret A, Demange L, Eeles RA, Yahanda AM, Fearon ER, Fricker JP, Gorlin RJ, Hodgson SV, Huson S, Lacombe D, Eng C, et al.: Mutation spectrum and genotype-phenotype analyses in Cowden disease and Bannayan-Zonana syndrome, two hamartoma syndromes with germline PTEN mutation. Hum Mol Genet. 1998 Mar;7(3):507-15. [PubMed Link Image]
  18. Scala S, Bruni P, Lo Muzio L, Mignogna M, Viglietto G, Fusco A: Novel mutation of the PTEN gene in an Italian Cowden's disease kindred. Int J Oncol. 1998 Oct;13(4):665-8. [PubMed Link Image]
  19. Olschwang S, Serova-Sinilnikova OM, Lenoir GM, Thomas G: PTEN germ-line mutations in juvenile polyposis coli. Nat Genet. 1998 Jan;18(1):12-4. [PubMed Link Image]
  20. Kurose K, Araki T, Matsunaka T, Takada Y, Emi M: Variant manifestation of Cowden disease in Japan: hamartomatous polyposis of the digestive tract with mutation of the PTEN gene. Am J Hum Genet. 1999 Jan;64(1):308-10. [PubMed Link Image]
  21. Sutphen R, Diamond TM, Minton SE, Peacocke M, Tsou HC, Root AW: Severe Lhermitte-Duclos disease with unique germline mutation of PTEN. Am J Med Genet. 1999 Feb 12;82(4):290-3. [PubMed Link Image]
  22. Nelen MR, Kremer H, Konings IB, Schoute F, van Essen AJ, Koch R, Woods CG, Fryns JP, Hamel B, Hoefsloot LH, Peeters EA, Padberg GW: Novel PTEN mutations in patients with Cowden disease: absence of clear genotype-phenotype correlations. Eur J Hum Genet. 1999 Apr;7(3):267-73. [PubMed Link Image]
  23. Marsh DJ, Kum JB, Lunetta KL, Bennett MJ, Gorlin RJ, Ahmed SF, Bodurtha J, Crowe C, Curtis MA, Dasouki M, Dunn T, Feit H, Geraghty MT, Graham JM Jr, Hodgson SV, Hunter A, Korf BR, Manchester D, Miesfeldt S, Murday VA, Nathanson KL, Parisi M, Pober B, Romano C, Eng C, et al.: PTEN mutation spectrum and genotype-phenotype correlations in Bannayan-Riley-Ruvalcaba syndrome suggest a single entity with Cowden syndrome. Hum Mol Genet. 1999 Aug;8(8):1461-72. [PubMed Link Image]
  24. De Vivo I, Gertig DM, Nagase S, Hankinson SE, O'Brien R, Speizer FE, Parsons R, Hunter DJ: Novel germline mutations in the PTEN tumour suppressor gene found in women with multiple cancers. J Med Genet. 2000 May;37(5):336-41. [PubMed Link Image]
  25. Marsh DJ, Theodosopoulos G, Howell V, Richardson AL, Benn DE, Proos AL, Eng C, Robinson BG: Rapid mutation scanning of genes associated with familial cancer syndromes using denaturing high-performance liquid chromatography. Neoplasia. 2001 May-Jun;3(3):236-44. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 7009
Enzyme 29 Name Phosphatidylinositol transfer protein beta isoform
Enzyme 29 Synonyms
  1. PtdIns transfer protein beta
  2. PtdInsTP
  3. PI-TP-beta
Enzyme 29 Gene Name PITPNB
Enzyme 29 Protein Sequence >Phosphatidylinositol transfer protein beta isoform 
MVLIKEFRVVLPCSVQEYQVGQLYSVAEASKNETGGGEGIEVLKNEPYEKDGEKGQYTHK
IYHLKSKVPAFVRMIAPEGSLVFHEKAWNAYPYCRTIVTNEYMKDDFFIKIETWHKPDLG
TLENVHGLDPNTWKTVEIVHIDIADRSQVEPADYKADEDPALFQSVKTKRGPLGPNWKKE
LANSPDCPQMCAYKLVTIKFKWWGLQSKVENFIQKQEKRIFTNFHRQLFCWIDKWIDLTM
EDIRRMEDETQKELETMRKRGSVRGTSAADV
Enzyme 29 Number of Residues 271
Enzyme 29 Molecular Weight 31540
Enzyme 29 Theoretical pI 6.87
Enzyme 29 GO Classification
Function
—
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • intracellular
Enzyme 29 General Function Not Available
Enzyme 29 Specific Function Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 1060905 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P48739 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name PIPNB_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >816 bp 
ATGGTGCTGATCAAGGAATTCCGTGTGGTTTTGCCATGTTCTGTTCAGGAGTATCAGGTT
GGGCAGCTTTACTCTGTTGCAGAAGCTAGTAAGAATGAGACTGGTGGTGGAGAAGGAATT
GAAGTCTTAAAGAATGAACCTTATGAGAAGGATGGAGAAAAGGGACAGTATACGCACAAA
ATTTATCACCTAAAGAGCAAAGTGCCTGCATTCGTGAGGATGATTGCTCCCGAGGGCTCC
TTGGTGTTTCATGAGAAAGCCTGGAATGCGTACCCCTACTGTAGAACAATTGTAACGAAT
GAATATATGAAAGATGATTTCTTCATTAAAATCGAAACATGGCACAAACCAGACTTGGGA
ACATTAGAAAATGTACATGGTTTAGATCCAAACACATGGAAAACTGTTGAAATTGTCCAT
ATAGATATTGCAGATAGAAGTCAAGTTGAACCAGCAGACTACAAAGCTGATGAAGACCCA
GCATTATTCCAGTCAGTCAAGACCAAGAGAGGCCCTTTGGGACCCAACTGGAAGAAGGAG
CTGGCAAACAGCCCTGACTGTCCCCAGATGTGTGCCTATAAGCTGGTGACCATCAAATTC
AAGTGGTGGGGACTGCAAAGCAAAGTAGAAAACTTCATTCAAAAGCAAGAAAAACGGATA
TTTACAAACTTCCATCGCCAGCTTTTTTGTTGGATTGACAAGTGGATCGATCTCACGATG
GAAGACATTAGGAGAATGGAAGACGAGACTCAGAAAGAACTAGAAACAATGCGTAAGAGG
GGTTCCGTTCGAGGCACGTCGGCTGCTGATGTCTAG
Enzyme 29 GenBank Gene ID D30037 Link Image
Enzyme 29 GeneCard ID PITPNB Link Image
Enzyme 29 GenAtlas ID PITPNB Link Image
Enzyme 29 HGNC ID HGNC:9002 Link Image
Enzyme 29 Chromosome Location 22
Enzyme 29 Locus 22q12.1
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Tanaka S, Yamashita S, Hosaka K: Cloning and expression of human cDNA encoding phosphatidylinositol transfer protein beta. Biochim Biophys Acta. 1995 Dec 7;1259(3):199-202. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 7222
Enzyme 30 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta 2
Enzyme 30 Synonyms
  1. Phosphoinositide phospholipase C
  2. Phospholipase C-eta- 2
  3. PLC-eta-2
  4. Phosphoinositide phospholipase C-like 4
  5. Phospholipase C-like 4
Enzyme 30 Gene Name PLCH2
Enzyme 30 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta 2 
RAGAAGQRVGLRSAWALRAGCPCSGWGSGDAGGQHRARCPSGRAGNWDWHPPAMEEPGPP
GGLSQDQVERCMGAMQEGMQMVKLRGGSKGLVRFYYLDEHRSCIRWRPSRKNEKAKISID
SIQEVSEGRQSEVFQRYPDGSFDPNCCFSIYHGSHRESLDLVSTSSEVARTWVTGLRYLM
AGISDEDSLARRQRTRDQWLKQTFDEADKNGDGSLSIGEVLQLLHKLNVNLPRQRVKQMF
READTDDHQGTLGFEEFCAFYKMMSTRRDLYLLMLTYSNHKDHLDAASLQRFLQVEQKMA
GVTLESCQDIIEQFEPCPENKSKGLLGIDGFTNYTRSPAGDIFNPEHHHVHQDMTQPLSH
YFITSSHNTYLVGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDGPDGEPIVHHGYTLTSKI
LFKDVIETINKYAFIKNEYPVILSIENHCSVIQQKKMAQYLTDILGDKLDLSSVSSEDAT
TLPSPQMLKGKILVKGKKLPANISEDAEEGEVSDEDSADEIDDDCKLLNGDASTNRKRVE
NTAKRKLDSLIKESKIRDCEDPNNFSVSTLSPSGKLGRKSKAEEDVESGEDAGASRRNGR
LVVGSFSRRKKKGSKLKKAASVEEGDEGQDSPGGQSRGATRQKKTMKLSRALSDLVKYTK
SVATHDIEMEAASSWQVSSFSETKAHQILQQKPAQYLRFNQQQLSRIYPSSYRVDSSNYN
PQPFWNAGCQMVALNYQSEGRMLQLNRAKFSANGGCGYVLKPGCMCQGVFNPNSEDPLPG
QLKKQLVLRIISGQQLPKPRDSMLGDRGEIIDPFVEVEIIGLPVDCSREQTRVVDDNGFN
PTWEETLVFMVHMPEIALVRFLVWDHDPIGRDFIGQRTLAFSSMMPGYRHVYLEGMEEAS
IFVHVAVSDISGKVKQALGLKGLFLRGPKPGSLDSHAAGRPPARPSVSQRILRRTASAPT
KSQKPGRRGFPELVLGTRDTGSKGVADDVVPPGPGPAPEAPAQEGPGSGSPRGKAPAAVA
EKSPVRVRPPRVLDGPGPAGMAATCMKCVVGSCAGVNTGGLQRERPPSPGPASRQAAIRQ
QPRARADSLGAPCCGLDPHAIPGRSREAPKGPGAWRQGPGGSGSMSSDSSSPDSPGIPER
SPRWPEGACRQPGALQGEMSALFAQKLEEIRSKSPMFSAVRN
Enzyme 30 Number of Residues 1182
Enzyme 30 Molecular Weight 129727
Enzyme 30 Theoretical pI 8.18
Enzyme 30 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 30 General Function Not Available
Enzyme 30 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes
Enzyme 30 Pathways
Enzyme 30 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • 1-16
Enzyme 30 Transmembrane Regions Not Available
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 58257652 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID O75038 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name PLCH2_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >3551 bp 
CACGGGCGGGCGCGGCAGGGCAGCGTGTGGGGCTGCGATCGGCATGGGCTCTGCGCGCGG
GGTGCCCCTGCTCGGGCTGGGGCTCAGGGGACGCCGGGGGCCAGCACAGGGCCCGGTGTC
CCTCGGGCCGTGCCGGTAACTGGGATTGGCACCCGCCGGCCATGGAAGAGCCTGGGCCCC
CAGGTGGGCTCAGCCAAGACCAAGTGGAGCGGTGCATGGGTGCCATGCAAGAGGGGATGC
AGATGGTGAAGCTGCGTGGCGGCTCCAAGGGCCTGGTCCGCTTCTACTACCTGGACGAGC
ACCGCTCCTGCATCCGCTGGAGGCCCTCACGCAAGAACGAGAAGGCCAAGATCTCCATCG
ACTCCATCCAGGAGGTGAGTGAGGGGCGGCAGTCGGAGGTCTTCCAGCGCTACCCTGACG
GCAGCTTCGACCCCAACTGCTGCTTCAGCATCTACCACGGCAGCCACCGCGAGTCGCTGG
ACCTGGTCTCCACCAGCAGCGAGGTGGCGCGCACCTGGGTCACTGGCCTGCGCTACCTCA
TGGCCGGCATCAGCGACGAGGACAGCCTGGCTCGCCGCCAGCGCACCAGGGACCAGTGGC
TGAAGCAGACGTTTGACGAGGCCGACAAGAACGGGGATGGCAGCCTGAGCATTGGCGAGG
TCCTGCAGCTGCTGCACAAGCTCAACGTGAACCTGCCCCGGCAGAGGGTGAAGCAGATGT
TCAGGGAAGCGGACACGGATGACCACCAAGGGACGCTGGGTTTTGAAGAGTTCTGTGCCT
TCTACAAGATGATGTCCACCCGCCGGGACCTCTACCTGCTCATGCTGACCTACAGCAACC
ACAAGGACCACCTGGATGCCGCCAGCCTGCAGCGCTTCCTGCAGGTGGAGCAGAAGATGG
CGGGTGTGACCCTCGAGAGCTGCCAGGACATCATCGAGCAGTTTGAGCCATGCCCAGAAA
ACAAGAGTAAGGGGCTGCTGGGCATTGATGGCTTCACCAACTACACCAGGAGCCCTGCTG
GTGACATCTTCAACCCTGAGCACCACCATGTGCACCAGGACATGACGCAGCCGCTGAGCC
ACTACTTCATCACCTCGTCCCACAACACCTACCTCGTGGGTGACCAGCTCATGTCCCAGT
CACGGGTGGACATGTATGCTTGGGTCCTGCAGGCTGGCTGCCGCTGCGTGGAGGTGGACT
GCTGGGATGGGCCCGACGGGGAGCCCATTGTGCACCATGGCTACACTCTGACTTCCAAGA
TCCTCTTCAAAGACGTCATTGAAACCATCAACAAATATGCCTTCATCAAGAATGAGTACC
CAGTGATCCTGTCCATCGAAAACCACTGCAGTGTCATCCAGCAGAAGAAAATGGCCCAGT
ATCTGACTGACATCCTTGGGGACAAGCTGGACCTGTCATCAGTGAGCAGTGAAGATGCCA
CCACACTCCCCTCTCCACAGATGCTCAAGGGCAAGATCCTCGTGAAGGGGAAGAAGCTCC
CAGCCAACATCAGCGAGGATGCGGAGGAAGGCGAGGTGTCTGATGAGGACAGTGCTGATG
AGATTGACGATGACTGCAAGCTCCTCAATGGGGATGCATCCACCAATCGAAAGCGTGTAG
AAAACACTGCTAAGAGGAAACTGGATTCCCTCATCAAAGAGTCGAAGATTCGGGACTGTG
AGGACCCCAACAACTTCTCCGTCTCCACACTGTCCCCATCTGGAAAGCTCGGACGCAAGA
GCAAGGCTGAAGAGGACGTGGAGTCTGGGGAGGATGCCGGGGCCAGCAGACGCAATGGCC
GCCTCGTCGTGGGAAGCTTCTCCAGGCGCAAGAAGAAGGGCAGCAAGCTGAAGAAGGCGG
CCAGCGTGGAGGAGGGAGATGAGGGTCAGGACTCCCCGGGAGGCCAGAGCCGAGGGGCGA
CCCGGCAGAAGAAGACCATGAAGCTGTCCCGGGCCCTCTCTGACCTGGTGAAGTACACCA
AGTCCGTGGCCACCCACGACATAGAGATGGAGGCGGCGTCCAGCTGGCAGGTGTCGTCCT
TCAGCGAGACCAAGGCCCACCAGATTCTGCAGCAGAAGCCGGCGCAGTACCTACGCTTCA
ACCAGCAGCAGCTCTCCCGCATCTACCCCTCCTCCTACCGTGTGGACTCCAGCAACTACA
ACCCGCAGCCCTTCTGGAACGCCGGCTGCCAAATGGTTGCCCTGAACTACCAGTCAGAGG
GGCGGATGCTGCAGCTGAACCGAGCCAAGTTCAGCGCCAACGGTGGCTGCGGCTACGTAC
TCAAGCCTGGGTGCATGTGCCAGGGCGTGTTCAACCCCAACTCGGAGGACCCCCTGCCCG
GGCAGCTCAAGAAGCAGCTGGTGCTCCGGATCATCAGTGGCCAGCAGCTTCCCAAGCCGC
GCGACTCCATGCTGGGGGACCGTGGGGAGATCATCGACCCCTTTGTGGAGGTGGAGATCA
TTGGGCTCCCTGTGGACTGCAGCAGGGAGCAGACCCGCGTGGTGGACGACAACGGGTTCA
ACCCCACCTGGGAGGAGACCCTGGTTTTCATGGTGCACATGCCGGAGATCGCGCTGGTCC
GCTTCCTCGTCTGGGACCACGATCCCATCGGGCGTGACTTCATTGGCCAGAGGACGCTGG
CCTTCAGCAGCATGATGCCAGGCTACAGACACGTGTACCTAGAAGGGATGGAAGAGGCCT
CCATCTTCGTGCATGTGGCTGTCAGTGACATCAGCGGTAAGGTCAAGCAGGCTCTGGGCC
TAAAAGGCCTCTTCCTCCGAGGCCCAAAGCCCGGCTCGCTGGACAGTCATGCTGCTGGGC
GGCCCCCGGCCCGGCCCTCCGTTAGCCAGCGGATCCTGCGGCGCACGGCCAGCGCCCCGA
CCAAGAGCCAGAAGCCGGGCCGCAGGGGCTTCCCGGAGCTGGTCCTGGGTACACGGGACA
CAGGCTCCAAGGGGGTGGCAGACGATGTGGTGCCCCCCGGGCCCGGACCTGCTCCGGAAG
CCCCAGCCCAGGAGGGGCCCGGCAGCGGCAGCCCCCGAGGTAAGGCGCCAGCTGCGGTGG
CAGAGAAGAGCCCTGTGCGAGTGCGGCCCCCGCGTGTCCTGGACGGCCCCGGGCCTGCTG
GGATGGCCGCCACATGCATGAAGTGTGTGGTGGGATCCTGCGCCGGCGTGAACACCGGGG
GCCTGCAGAGGGAGCGGCCACCCAGCCCGGGGCCTGCAAGCAGGCAGGCAGCCATTCGCC
AGCAGCCCCGGGCCCGGGCTGACTCACTGGGGGCCCCCTGCTGTGGCCTGGACCCTCACG
CTATCCCGGGGAGAAGCAGAGAGGCCCCCAAGGGTCCTGGGGCCTGGAGGCAGGGTCCAG
GCGGTAGCGGCTCCATGTCCTCGGACTCCAGCAGCCCAGACAGCCCGGGCATCCCCGAAA
GGTCCCCCCGCTGGCCTGAGGGTGCCTGCAGGCAACCGGGGGCCCTGCAGGGAGAGATGA
GTGCCTTGTTTGCTCAAAAGCTGGAGGAGATCAGGAGTAAATCCCCCATGTTCTCCGCCG
TTAGGAACTGA
Enzyme 30 GenBank Gene ID AB007919 Link Image
Enzyme 30 GeneCard ID PLCH2 Link Image
Enzyme 30 GenAtlas ID PLCH2 Link Image
Enzyme 30 HGNC ID HGNC:29037 Link Image
Enzyme 30 Chromosome Location 1
Enzyme 30 Locus 1p36.32
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Seki N, Ohira M, Nagase T, Ishikawa K, Miyajima N, Nakajima D, Nomura N, Ohara O: Characterization of cDNA clones in size-fractionated cDNA libraries from human brain. DNA Res. 1997 Oct 31;4(5):345-9. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 7395
Enzyme 31 Name Phospholipid scramblase 1
Enzyme 31 Synonyms
  1. PL scramblase 1
  2. Ca(2+-dependent phospholipid scramblase 1
  3. Erythrocyte phospholipid scramblase
  4. MmTRA1b
Enzyme 31 Gene Name PLSCR1
Enzyme 31 Protein Sequence >Phospholipid scramblase 1 
MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAG
FPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVL
TGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLR
CSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCC
GDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLI
DFMFFESTGSQEQKSGVW
Enzyme 31 Number of Residues 318
Enzyme 31 Molecular Weight 35049
Enzyme 31 Theoretical pI 4.57
Enzyme 31 GO Classification Not Available
Enzyme 31 General Function Not Available
Enzyme 31 Specific Function May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes. May contribute to cytokine-regulated cell proliferation and differentiation
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • 289-305
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 4092081 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID O15162 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name PLS1_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >957 bp 
ATGGACAAACAAAACTCACAGATGAATGCTTCTCACCCGGAAACAAACTTGCCAGTTGGG
TATCCTCCTCAGTATCCACCGACAGCATTCCAAGGACCTCCAGGATATAGTGGCTACCCT
GGGCCCCAGGTCAGCTACCCACCCCCACCAGCCGGCCATTCAGGTCCTGGCCCAGCTGGC
TTTCCTGTCCCAAATCAGCCAGTGTATAATCAGCCAGTATATAATCAGCCAGTTGGAGCT
GCAGGGGTACCATGGATGCCAGCGCCACAGCCTCCATTAAACTGTCCACCTGGATTAGAA
TATTTAAGTCAGATAGATCAGATACTGATTCATCAGCAAATTGAACTTCTGGAAGTTTTA
ACAGGTTTTGAAACTAATAACAAATATGAAATTAAGAACAGCTTTGGACAGAGGGTTTAC
TTTGCAGCGGAAGATACTGATTGCTGTACCCGAAATTGCTGTGGGCCATCTAGACCTTTT
ACCTTGAGGATTATTGATAATATGGGTCAAGAAGTCATAACTCTGGAGAGACCACTAAGA
TGTAGCAGCTGTTGTTGTCCCTGCTGCCTTCAGGAGATAGAAATCCAAGCTCCTCCTGGT
GTACCAATAGGTTATGTTATTCAGACTTGGCACCCATGTCTACCAAAGTTTACAATTCAA
AATGAGAAAAGAGAGGATGTACTAAAAATAAGTGGTCCATGTGTTGTGTGCAGCTGTTGT
GGAGATGTTGATTTTGAGATTAAATCTCTTGATGAACAGTGTGTGGTTGGCAAAATTTCC
AAGCACTGGACTGGAATTTTGAGAGAGGCATTTACAGACGCTGATAACTTTGGAATCCAG
TTCCCTTTAGACCTTGATGTTAAAATGAAAGCTGTAATGATTGGTGCCTGTTTCCTCATT
GACTTCATGTTTTTTGAAAGCACTGGCAGCCAGGAACAAAAATCAGGAGTGTGGTAG
Enzyme 31 GenBank Gene ID AF098642 Link Image
Enzyme 31 GeneCard ID PLSCR1 Link Image
Enzyme 31 GenAtlas ID PLSCR1 Link Image
Enzyme 31 HGNC ID HGNC:9092 Link Image
Enzyme 31 Chromosome Location 3
Enzyme 31 Locus 3q23
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Zhou Q, Zhao J, Stout JG, Luhm RA, Wiedmer T, Sims PJ: Molecular cloning of human plasma membrane phospholipid scramblase. A protein mediating transbilayer movement of plasma membrane phospholipids. J Biol Chem. 1997 Jul 18;272(29):18240-4. [PubMed Link Image]
  2. Kasukabe T, Kobayashi H, Kaneko Y, Okabe-Kado J, Honma Y: Identity of human normal counterpart (MmTRA1b) of mouse leukemogenesis-associated gene (MmTRA1a) product as plasma membrane phospholipid scramblase and chromosome mapping of the human MmTRA1b/phospholipid scramblase gene. Biochem Biophys Res Commun. 1998 Aug 19;249(2):449-55. [PubMed Link Image]
  3. Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed Link Image]
  4. Basse F, Stout JG, Sims PJ, Wiedmer T: Isolation of an erythrocyte membrane protein that mediates Ca2+-dependent transbilayer movement of phospholipid. J Biol Chem. 1996 Jul 19;271(29):17205-10. [PubMed Link Image]
  5. Frasch SC, Henson PM, Kailey JM, Richter DA, Janes MS, Fadok VA, Bratton DL: Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cdelta. J Biol Chem. 2000 Jul 28;275(30):23065-73. [PubMed Link Image]
  6. Sun J, Zhao J, Schwartz MA, Wang JY, Wiedmer T, Sims PJ: c-Abl tyrosine kinase binds and phosphorylates phospholipid scramblase 1. J Biol Chem. 2001 Aug 3;276(31):28984-90. Epub 2001 Jun 4. [PubMed Link Image]
  7. Zhao J, Zhou Q, Wiedmer T, Sims PJ: Palmitoylation of phospholipid scramblase is required for normal function in promoting Ca2+-activated transbilayer movement of membrane phospholipids. Biochemistry. 1998 May 5;37(18):6361-6. [PubMed Link Image]
  8. Zhou Q, Sims PJ, Wiedmer T: Identity of a conserved motif in phospholipid scramblase that is required for Ca2+-accelerated transbilayer movement of membrane phospholipids. Biochemistry. 1998 Feb 24;37(8):2356-60. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 7675
Enzyme 32 Name Phosphatidylserine synthase 1
Enzyme 32 Synonyms
  1. PtdSer synthase 1
  2. PSS-1
  3. Serine-exchange enzyme I
Enzyme 32 Gene Name PTDSS1
Enzyme 32 Protein Sequence >Phosphatidylserine synthase 1 
MASCVGSRTLSKDDVNYKMHFRMINEQQVEDITIDFFYRPHTITLLSFTIVSLMYFAFTR
DDSVPEDNIWRGILSVIFFFLIISVLAFPNGPFTRPHPALWRMVFGLSVLYFLFLVFLLF
LNFEQVKSLMYWLDPNLRYATREADVMEYAVNCHVITWERIISHFDIFAFGHFWGWAMKA
LLIRSYGLCWTISITWELTELFFMHLLPNFAECWWDQVILDILLCNGGGIWLGMVVCRFL
EMRTYHWASFKDIHTTTGKIKRAVLQFTPASWTYVRWFDPKSSFQRVAGVYLFMIIWQLT
ELNTFFLKHIFVFQASHPLSWGRILFIGGITAPTVRQYYAYLTDTQCKRVGTQCWVFGVI
GFLEAIVCIKFGQDLFSKTQILYVVLWLLCVAFTTFLCLYGMIWYAEHYGHREKTYSECE
DGTYSPEISWHHRKGTKGSEDSPPKHAGNNESHSSRRRNRHSKSKVTNGVGKK
Enzyme 32 Number of Residues 473
Enzyme 32 Molecular Weight 55528
Enzyme 32 Theoretical pI 8.52
Enzyme 32 GO Classification
Function
—
Process
  • cellular lipid metabolism
  • glycerophospholipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phosphatidylserine biosynthesis
  • phosphatidylserine metabolism
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 32 General Function Not Available
Enzyme 32 Specific Function Catalyzes a base-exchange reaction in which the polar head group of phosphatidylcholine is replaced by L-serine
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • 36-56 73-93 103-123 161-181 187-207 217-237 287-307 310-330 356-376 384-404
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 603802 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID P48651 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name PTSS1_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >1422 bp 
ATGGCGTCCTGCGTGGGGAGCCGGACCCTAAGCAAGGATGATGTGAACTACAAAATGCAT
TTCCGGATGATCAACGAGCAGCAAGTGGAGGACATCACCATTGACTTCTTCTACCGGCCG
CATACCATCACCCTGCTCAGCTTCACCATCGTCAGCCTCATGTACTTCGCCTTTACCAGG
GATGACTCTGTTCCAGAAGACAACATCTGGAGAGGCATCCTCTCTGTTATTTTCTTCTTT
CTTATCATCAGTGTGTTAGCTTTCCCCAATGGTCCGTTCACTCGACCTCATCCAGCCTTA
TGGCGAATGGTTTTTGGACTCAGTGTGCTCTACTTCCTGTTCCTGGTATTCCTACTCTTC
CTGAATTTCGAGCAGGTTAAATCTCTAATGTATTGGCTAGATCCAAATCTTCGATACGCC
ACAAGGGAAGCAGATGTCATGGAGTATGCTGTGAACTGCCATGTGATCACCTGGGAGAGG
ATTATCAGCCACTTTGATATTTTTGCATTTGGACATTTCTGGGGCTGGGCCATGAAGGCC
TTGCTGATCCGTAGTTACGGTCTCTGCTGGACAATCAGTATTACCTGGGAGCTGACTGAG
CTCTTCTTCATGCATCTCCTCCCCAATTTTGCCGAGTGCTGGTGGGATCAAGTCATTCTG
GACATCCTGTTGTGCAATGGCGGTGGCATTTGGCTGGGCATGGTCGTTTGCCGGTTTTTA
GAGATGAGGACTTACCACTGGGCAAGCTTCAAGGACATTCATACCACCACCGGGAAGATC
AAGAGAGCTGTTCTGCAGTTCACTCCTGCTAGCTGGACCTATGTTCGATGGTTTGACCCC
AAATCTTCTTTTCAGAGAGTAGCTGGAGTGTACCTTTTCATGATCATCTGGCAGCTGACT
GAGTTGAATACCTTCTTCTTGAAGCATATCTTTGTGTTCCAAGCCAGTCATCCATTAAGT
TGGGGTAGAATTCTCTTTATTGGTGGCATCACAGCTCCCACAGTGAGACAGTACTACGCT
TACCTCACCGACACACAGTGCAAGCGCGTAGGAACACAATGCTGGGTGTTTGGGGTCATT
GGTTTCCTGGAGGCCATTGTTTGCATAAAATTTGGACAAGATCTCTTCTCTAAGACCCAA
ATACTCTATGTTGTGCTTTGGCTTCTTTGCGTGGCTTTCACCACTTTCCTCTGTCTGTAC
GGCATGATTTGGTATGCAGAACACTATGGTCACCGAGAAAAGACCTACTCGGAGTGTGAA
GATGGCACCTACAGTCCAGAGATCTCCTGGCATCACAGGAAAGGGACAAAAGGTTCTGAA
GACAGCCCACCCAAGCATGCAGGCAACAACGAAAGCCATTCTTCCAGGAGAAGGAATCGG
CATTCCAAGTCAAAAGTCACCAATGGCGTTGGAAAGAAATGA
Enzyme 32 GenBank Gene ID D14694 Link Image
Enzyme 32 GeneCard ID PTDSS1 Link Image
Enzyme 32 GenAtlas ID PTDSS1 Link Image
Enzyme 32 HGNC ID HGNC:9587 Link Image
Enzyme 32 Chromosome Location 8
Enzyme 32 Locus 8q22
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 7740
Enzyme 33 Name Phosphatidylserine decarboxylase proenzyme
Enzyme 33 Synonyms Not Available
Enzyme 33 Gene Name PISD
Enzyme 33 Protein Sequence >Phosphatidylserine decarboxylase proenzyme 
MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARKIHTAPART
MFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWEVALYKSVPTRLLS
RAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPV
CGLHSISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKN
QLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCH
NERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNRE
GVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL
Enzyme 33 Number of Residues 408
Enzyme 33 Molecular Weight 46573
Enzyme 33 Theoretical pI 9.80
Enzyme 33 GO Classification
Function
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
  • phosphatidylserine decarboxylase activity
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid biosynthesis
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 33 General Function Lipid transport and metabolism
Enzyme 33 Specific Function Phosphatidyl-L-serine = phosphatidylethanolamine + CO(2)
Enzyme 33 Pathways
Enzyme 33 Reactions
  • phosphatidyl-L-serine = phosphatidylethanolamine + CO2
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 57997016 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q9UG56 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name PISD_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >1227 bp 
ATGGCGACGTCCGTGGGGCACCGATGTCTGGGATTACTGCACGGGGTCGCGCCGTGGCGG
AGCAGCCTCCATCCCTGTGAGATCACTGCCCTGAGCCAATCCCTACAGCCCTTACGGAAG
CTGCCTTTTAGAGCCTTTCGCACAGATGCCAGAAAAATCCACACTGCCCCTGCCCGAACC
ATGTTCCTGCTGCGTCCCCTGCCCATTCTGTTGGTGACAGGCGGCGGGTATGCAGGGTAC
CGGCAGTATGAGAAGTACAGGGAGCGAGAGCTGGAGAAGCTGGGATTGGAGATTCCACCC
AAACTTGCTGGTCACTGGGAGGTGGCTTTGTACAAGTCAGTGCCAACGCGCTTGCTGTCA
CGGGCCTGGGGTCGCCTCAATCAGGTGGAGCTGCCACACTGGCTGCGCAGGCCCGTCTAC
AGCCTGTACATCTGGACGTTTGGGGTGAACATGAAAGAGGCCGCTGTGGAGGACCTGCAT
CACTACCGCAACCTCAGCGAGTTCTTCCGGCGCAAGCTGAAGCCGCAGGCCCGGCCTGTC
TGTGGCCTGCACAGCATTAGCCCATCGGATGGAAGGATCCTCAACTTTGGGCAGGTGAAG
AACTGTGAGGTGGAGCAGGTAAAGGGGGTCACCTACTCCCTGGAGTCGTTCCTGGGCCCG
CGTATGTGCACAGAGGACCTGCCCTTCCCACCAGCCGCGTCGTGTGACTCCTTCAAGAAC
CAGCTGGTCACCCGGGAAGGGAATGAGCTCTATCACTGTGTCATCTACCTGGCCCCTGGG
GACTACCACTGCTTCCACTCCCCCACCGACTGGACTGTGTCCCACCGGCGCCACTTCCCA
GGCTCCCTGATGTCAGTGAACCCTGGCATGGCTCGCTGGATCAAAGAGCTCTTCTGCCAT
AACGAGCGGGTGGTCCTGACGGGGGACTGGAAACATGGCTTCTTCTCACTGACAGCTGTG
GGGGCCACCAACGTGGGCTCCATTCGCATCTACTTTGACCGGGACCTGCACACAAACAGC
CCAAGGCACAGCAAGGGCTCCTACAATGACTTCAGCTTCGTGACGCACACCAATAGAGAG
GGCGTCCCCATGCGTAAGGGCGAGCACCTGGGCGAGTTCAACCTGGGCTCCACCATCGTG
CTCATCTTCGAGGCCCCCAAGGACTTCAATTTCCAGCTGAAAACAGGACAGAAAATCCGC
TTTGGGGAAGCCCTGGGCTCGCTCTAG
Enzyme 33 GenBank Gene ID AL050371 Link Image
Enzyme 33 GeneCard ID PISD Link Image
Enzyme 33 GenAtlas ID PISD Link Image
Enzyme 33 HGNC ID HGNC:8999 Link Image
Enzyme 33 Chromosome Location 22
Enzyme 33 Locus 22q12.2
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 8021
Enzyme 34 Name Phosphatidylinositol transfer protein alpha isoform
Enzyme 34 Synonyms
  1. PtdIns transfer protein alpha
  2. PtdInsTP
  3. PI-TP-alpha
Enzyme 34 Gene Name PITPNA
Enzyme 34 Protein Sequence >Phosphatidylinositol transfer protein alpha isoform 
MVLLKEYRVILPVSVDEYQVGQLYSVAEASKNETGGGEGVEVLVNEPYEKDGEKGQYTHK
IYHLQSKVPTFVRMLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLG
TQENVHKLEPEAWKHVEAVYIDIADRSQVLSKDYKAEEDPAKFKSIKTGRGPLGPNWKQE
LVNQKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQERRLFTNFHRQLFCWLDKWVDLTM
DDIRRMEEETKRQLDEMRQKDPVKGMTADD
Enzyme 34 Number of Residues 270
Enzyme 34 Molecular Weight 31807
Enzyme 34 Theoretical pI 6.52
Enzyme 34 GO Classification
Function
—
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • intracellular
Enzyme 34 General Function Not Available
Enzyme 34 Specific Function Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions Not Available
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 189939 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q00169 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name PIPNA_HUMAN Link Image
Enzyme 34 PDB ID 1T27 Link Image
Enzyme 34 PDB File Show
Enzyme 34 3D Structure
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >813 bp 
ATGGTGCTGCTCAAGGAGTATCGAGTAATCCTGCCTGTGTCTGTAGATGAGTATCAAGTG
GGGCAGCTGTATTCTGTGGCTGAGGCCAGTAAAAATGAAACGGGTGGTGGCGAAGGCGTG
GAGGTCCTGGTGAATGAGCCCTACGAGAAGGACGGTGAGAAAGGCCAGTACACACACAAG
ATCTACCACCTGCAGAGCAAAGTACCCACGTTTGTTCGAATGCTGGCCCCAGAGGGAGCC
CTGAATATACACGAGAAAGCCTGGAATGCTTACCCCTACTGCAGAACCGTTATTACAAAT
GAGTACATGAAAGAAGACTTTCTGATTAAAATTGAAACCTGGCACAAACCAGATCTTGGC
ACGCAGGAGAATGTGCATAAGCTGGAGCCTGAGGCGTGGAAACACGTGGAAGCCGTATAT
ATAGACATTGCAGATCGAAGCCAAGTGCTCAGCAAGGATTACAAGGCAGAGGAAGACCCA
GCAAAATTTAAATCTATCAAAACAGGCCGAGGACCCTTGGGCCCCAATTGGAAGCAAGAG
CTTGTAAACCAGAAGGACTGCCCATATATGTGTGCATACAAACTGGTGACCGTCAAGTTC
AAGTGGTGGGGCCTGCAGAACAAAGTGGAGAACTTCATCCATAAGCAAGAGAGGCGTCTG
TTTACAAACTTCCACAGGCAGCTGTTCTGTTGGCTCGATAAGTGGGTTGACCTGACCATG
GACGACATTCGAAGGATGGAAGAAGAGACGAAGAGACAGCTGGATGAAATGAGACAAAAG
GACCCAGTGAAAGGAATGACAGCAGATGACTAA
Enzyme 34 GenBank Gene ID M73704 Link Image
Enzyme 34 GeneCard ID PITPNA Link Image
Enzyme 34 GenAtlas ID PITPNA Link Image
Enzyme 34 HGNC ID HGNC:9001 Link Image
Enzyme 34 Chromosome Location 17
Enzyme 34 Locus 17p13.3
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Dickeson SK, Helmkamp GM Jr, Yarbrough LR: Sequence of a human cDNA encoding phosphatidylinositol transfer protein and occurrence of a related sequence in widely divergent eukaryotes. Gene. 1994 May 16;142(2):301-5. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 8048
Enzyme 35 Name Phospholipid transfer protein precursor
Enzyme 35 Synonyms
  1. Lipid transfer protein II
Enzyme 35 Gene Name PLTP
Enzyme 35 Protein Sequence >Phospholipid transfer protein precursor 
MALFGALFLALLAGAHAEFPGCKIRVTSKALELVKQEGLRFLEQELETITIPDLRGKEGH
FYYNISEVKVTELQLTSSELDFQPQQELMLQITNASLGLRFRRQLLYWFFYDGGYINASA
EGVSIRTGLELSRDPAGRMKVSNVSCQASVSRMHAAFGGTFKKVYDFLSTFITSGMRFLL
NQQICPVLYHAGTVLLNSLLDTVPVRSSVDELVGIDYSLMKDPVASTSNLDMDFRGAFFP
LTERNWSLPNRAVEPQLQEEERMVYVAFSEFFFDSAMESYFRAGALQLLLVGDKVPHDLD
MLLRATYFGSIVLLSPAVIDSPLKLELRVLAPPRCTIKPSGTTISVTASVTIALVPPDQP
EVQLSSMTMDARLSAKMALRGKALRTQLDLRRFRIYSNHSALESLALIPLQAPLKTMLQI
GVMPMLNERTWRGVQIPLPEGINFVHEVVTNHAGFLTIGADLHFAKGLREVIEKNRPADV
RASTAPTPSTAAV
Enzyme 35 Number of Residues 493
Enzyme 35 Molecular Weight 54740
Enzyme 35 Theoretical pI 7.01
Enzyme 35 GO Classification
Function
  • binding
  • lipid binding
Process
—
Component
—
Enzyme 35 General Function Not Available
Enzyme 35 Specific Function Converts HDL into larger and smaller particles. May play a key role in extracellular phospholipid transport and modulation of hdl particles
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • 1-17
Enzyme 35 Transmembrane Regions Not Available
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 468326 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID P55058 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name PLTP_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >1482 bp 
ATGGCCCTCTTCGGGGCCCTCTTCCTAGCGCTGCTGGCAGGCGCACATGCAGAGTTCCCA
GGCTGCAAGATCCGCGTCACCTCCAAGGCGCTGGAGCTGGTGAAGCAGGAGGGGCTGCGC
TTTCTGGAGCAAGAGCTGGAGACTATCACCATTCCGGACCTGCGGGGCAAAGAAGGCCAC
TTCTACTACAACATCTCTGAGGTGAAGGTCACAGAGCTGCAACTGACATCTTCCGAGCTC
GATTTCCAGCCACAGCAGGAGCTGATGCTTCAAATCACCAATGCCTCCTTGGGGCTGCGC
TTCCGGAGACAGCTGCTCTACTGGTTCTTCTATGATGGGGGCTACATCAACGCCTCAGCT
GAGGGTGTGTCCATCCGCACTGGTCTGGAGCTCTCCCGGGATCCCGCTGGACGGATGAAA
GTGTCCAATGTCTCCTGCCAGGCCTCTGTCTCCAGAATGCACGCGGCCTTCGGGGGAACC
TTCAAGAAGGTGTATGATTTTCTCTCCACGTTCATCACCTCAGGGATGCGCTTCCTCCTC
AACCAGCAGATCTGCCCTGTCCTCTACCACGCAGGGACGGTCCTGCTCAACTCCCTCCTG
GACACCGTGCCTGTGCGCAGTTCTGTGGACGAGCTTGTTGGCATTGACTATTCCCTCATG
AAGGATCCTGTGGCTTCCACCAGCAACCTGGACATGGACTTCCGGGGGGCCTTCTTCCCC
CTGACTGAGAGGAACTGGAGCCTCCCCAACCGGGCAGTGGAGCCCCAGCTGCAGGAGGAA
GAGCGGATGGTGTATGTGGCCTTCTCTGAGTTCTTCTTCGACTCTGCCATGGAGAGCTAC
TTCCGGGCGGGGGCCCTGCAGCTGTTGCTGGTGGGGGACAAGGTGCCCCACGACCTGGAC
ATGCTGCTGAGGGCCACCTACTTTGGGAGCATTGTCCTGCTGAGCCCAGCAGTGATTGAC
TCCCCATTGAAGCTGGAGCTGCGGGTCCTGGCCCCACCGCGCTGCACCATCAAGCCCTCT
GGCACCACCATCTCTGTCACTGCTAGCGTCACCATTGCCCTGGTCCCACCAGACCAGCCT
GAGGTCCAGCTGTCCAGCATGACTATGGACGCCCGTCTCAGCGCCAAGATGGCTCTCCGG
GGGAAGGCCCTGCGCACGCAGCTGGACCTGCGCAGGTTCCGAATCTATTCCAACCATTCT
GCACTGGAGTCGCTGGCTCTGATCCCATTACAGGCCCCTCTGAAGACCATGCTGCAGATT
GGGGTGATGCCCATGCTCAATGAGCGGACCTGGCGTGGGGTGCAGATCCCACTACCTGAG
GGCATCAACTTTGTGCATGAGGTGGTGACGAACCATGCGGGATTCCTCACCATCGGGGCT
GATCTCCACTTTGCCAAAGGGCTGCGAGAGGTGATTGAGAAGAACCGGCCTGCTGATGTC
AGGGCGTCCACTGCCCCCACACCGTCCACAGCAGCTGTCTGA
Enzyme 35 GenBank Gene ID L26232 Link Image
Enzyme 35 GeneCard ID PLTP Link Image
Enzyme 35 GenAtlas ID PLTP Link Image
Enzyme 35 HGNC ID HGNC:9093 Link Image
Enzyme 35 Chromosome Location 20
Enzyme 35 Locus 20q12-q13.1
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Day JR, Albers JJ, Lofton-Day CE, Gilbert TL, Ching AF, Grant FJ, O'Hara PJ, Marcovina SM, Adolphson JL: Complete cDNA encoding human phospholipid transfer protein from human endothelial cells. J Biol Chem. 1994 Mar 25;269(12):9388-91. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. Qu SJ, Fan HZ, Kilinc C, Pownall HJ: Role of cysteine residues in human plasma phospholipid transfer protein. J Protein Chem. 1999 Feb;18(2):193-8. [PubMed Link Image]
  4. Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 8469
Enzyme 36 Name GPI mannosyltransferase 1
Enzyme 36 Synonyms
  1. GPI mannosyltransferase I
  2. GPI-MT-I
  3. Phosphatidylinositol-glycan biosynthesis class M protein
  4. PIG-M
Enzyme 36 Gene Name PIGM
Enzyme 36 Protein Sequence >GPI mannosyltransferase 1 
MGSTKHWGEWLLNLKVAPAGVFGVAFLARVALVFYGVFQDRTLHVRYTDIDYQVFTDAAR
FVTEGRSPYLRATYRYTPLLGWLLTPNIYLSELFGKFLFISCDLLTAFLLYRLLLLKGLG
RRQACGYCVFWLLNPLPMAVSSRGNADSIVASLVLMVLYLIKKRLVACAAVFYGFAVHMK
IYPVTYILPITLHLLPDRDNDKSLRQFRYTFQACLYELLKRLCNRAVLLFVAVAGLTFFA
LSFGFYYEYGWEFLEHTYFYHLTRRDIRHNFSPYFYMLYLTAESKWSFSLGIAAFLPQLI
LLSAVSFAYYRDLVFCCFLHTSIFVTFNKVCTSQYFLWYLCLLPLVMPLVRMPWKRAVVL
LMLWFIGQAMWLAPAYVLEFQGKNTFLFIWLAGLFFLLINCSILIQIISHYKEEPLTERI
KYD
Enzyme 36 Number of Residues 423
Enzyme 36 Molecular Weight 49460
Enzyme 36 Theoretical pI 9.31
Enzyme 36 GO Classification Not Available
Enzyme 36 General Function Not Available
Enzyme 36 Specific Function Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • 1-369
Enzyme 36 Transmembrane Regions
  • 18-38 80-100 139-161 170-190 226-246 288-308 315-337 339-350 358-378 385-405
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 11414879 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q9H3S5 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name PIGM_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >1272 bp 
ATGGGCTCCACCAAGCACTGGGGCGAATGGCTCCTGAACTTGAAGGTGGCTCCAGCCGGC
GTCTTTGGTGTGGCCTTTCTAGCCAGAGTCGCCCTGGTTTTCTATGGCGTCTTCCAGGAC
CGGACCCTGCACGTGAGGTATACGGACATCGACTACCAGGTCTTCACCGACGCCGCGCGC
TTCGTCACGGAGGGGCGCTCGCCTTACCTGAGAGCCACGTACCGTTACACCCCGCTGCTG
GGTTGGCTCCTCACTCCCAACATCTACCTCAGCGAGCTCTTTGGAAAGTTTCTCTTCATC
AGCTGCGACCTCCTCACCGCTTTCCTCTTATACCGCCTGCTGCTGCTGAAGGGGCTGGGG
CGCCGCCAGGCTTGTGGCTACTGTGTCTTTTGGCTTCTTAACCCCCTGCCTATGGCAGTA
TCCAGCCGCGGTAATGCGGACTCTATTGTCGCCTCCCTGGTCCTGATGGTCCTCTACTTG
ATAAAGAAAAGACTCGTCGCGTGTGCAGCTGTATTCTATGGTTTCGCGGTGCATATGAAG
ATATATCCAGTGACTTACATCCTTCCCATAACCCTCCACCTGCTTCCAGATCGCGACAAT
GACAAAAGCCTCCGTCAATTCCGGTACACTTTCCAGGCTTGTTTGTACGAGCTCCTGAAA
AGGCTGTGTAATCGGGCTGTGCTGCTGTTTGTAGCAGTTGCTGGACTCACGTTTTTTGCC
CTGAGCTTTGGTTTTTACTATGAGTACGGCTGGGAATTTTTGGAACACACCTACTTTTAT
CACCTGACTAGGCGGGATATCCGTCACAACTTTTCTCCGTACTTCTACATGCTGTATTTG
ACTGCAGAGAGCAAGTGGAGTTTTTCCCTGGGAATTGCTGCATTCCTGCCACAGCTCATC
TTGCTTTCAGCTGTGTCTTTCGCCTATTACAGAGACCTCGTTTTTTGTTGTTTTCTTCAT
ACGTCCATTTTTGTGACTTTTAACAAAGTCTGCACCTCCCAGTACTTTCTTTGGTACCTC
TGCTTACTGCCTCTTGTGATGCCACTAGTCAGAATGCCTTGGAAAAGAGCTGTAGTTCTC
CTAATGTTATGGTTTATAGGGCAGGCCATGTGGCTGGCTCCTGCCTATGTTCTAGAGTTT
CAAGGAAAGAACACCTTTCTGTTTATTTGGTTAGCTGGTTTGTTCTTTCTTCTTATCAAT
TGTTCCATCCTGATTCAAATTATTTCCCATTACAAAGAAGAACCCCTGACAGAGAGAATC
AAATATGACTAG
Enzyme 36 GenBank Gene ID AB028127 Link Image
Enzyme 36 GeneCard ID PIGM Link Image
Enzyme 36 GenAtlas ID PIGM Link Image
Enzyme 36 HGNC ID HGNC:18858 Link Image
Enzyme 36 Chromosome Location 1
Enzyme 36 Locus 1q23.2
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Maeda Y, Watanabe R, Harris CL, Hong Y, Ohishi K, Kinoshita K, Kinoshita T: PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER. EMBO J. 2001 Jan 15;20(1-2):250-61. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 8475
Enzyme 37 Name Phosphatidylserine synthase 2
Enzyme 37 Synonyms
  1. PtdSer synthase 2
  2. PSS-2
  3. Serine-exchange enzyme II
Enzyme 37 Gene Name PTDSS2
Enzyme 37 Protein Sequence >Phosphatidylserine synthase 2 
MRRGERRDAGGPRPESPVPAGRASLEEPPDGPSAGQATGPGEGRRSTESEVYDDGTNTFF
WRAHTLTVLFILTCTLGYVTLLEETPQDTAYNTKRGIVASILVFLCFGVTQAKDGPFSRP
HPAYWRFWLCVSVVYELFLIFILFQTVQDGRQFLKYVDPKLGVPLPERDYGGNCLIYDPD
NETDPFHNIWDKLDGFVPAHFLGWYLKTLMIRDWWMCMIISVMFEFLEYSLEHQLPNFSE
CWWDHWIMDVLVCNGLGIYCGMKTLEWLSLKTYKWQGLWNIPTYKGKMKRIAFQFTPYSW
VRFEWKPASSLRRWLAVCGIILVFLLAELNTFYLKFVLWMPPEHYLVLLRLVFFVNVGGV
AMREIYDFMDDPKPHKKLGPQAWLVAAITATELLIVVKYDPHTLTLSLPFYISQCWTLGS
VLALTWTVWRFFLRDITLRYKETRWQKWQNKDDQGSTVGNGDQHPLGLDEDLLGPGVAEG
EGAPTPN
Enzyme 37 Number of Residues 487
Enzyme 37 Molecular Weight 56253
Enzyme 37 Theoretical pI 6.19
Enzyme 37 GO Classification
Function
—
Process
  • cellular lipid metabolism
  • glycerophospholipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phosphatidylserine biosynthesis
  • phosphatidylserine metabolism
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 37 General Function Not Available
Enzyme 37 Specific Function Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine is replaced by L-serine
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions Not Available
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals Not Available
Enzyme 37 Transmembrane Regions
  • 63-83 97-117 127-147 242-262 314-334 336-356 377-397 404-424
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 21740008 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q9BVG9 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name PTSS2_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >1464 bp 
ATGCGGAGGGGCGAGCGCAGGGACGCCGGAGGTCCGCGGCCCGAGTCCCCGGTGCCCGCG
GGCAGGGCCTCGCTGGAGGAGCCGCCTGACGGGCCGTCTGCCGGCCAAGCCACCGGGCCG
GGCGAGGGCCGCCGCAGCACCGAGTCCGAGGTCTACGACGACGGCACCAACACCTTCTTC
TGGCGAGCCCACACCTTAACCGTGCTCTTCATCCTCACCTGTACGCTTGGCTATGTGACG
CTGCTGGAGGAAACACCTCAGGACACGGCCTACAACACCAAGAGAGGTATTGTGGCCAGT
ATTTTGGTTTTCTTATGTTTTGGAGTCACACAAGCTAAAGACGGGCCATTTTCCAGACCT
CATCCAGCTTACTGGAGGTTTTGGCTCTGCGTGAGTGTGGTCTACGAGCTGTTTCTCATC
TTTATACTCTTCCAGACTGTCCAGGACGGCCGGCAGTTTCTAAAGTATGTTGACCCCAAG
CTGGGAGTCCCACTGCCAGAGAGAGACTACGGGGGAAACTGCCTCATCTACGACCCAGAC
AATGAGACTGACCCCTTTCACAACATCTGGGACAAGTTGGATGGCTTTGTTCCCGCGCAC
TTTCTTGGCTGGTACCTGAAGACCCTGATGATCCGAGACTGGTGGATGTGCATGATCATC
AGCGTGATGTTCGAGTTCCTGGAGTACAGCCTGGAGCACCAGCTGCCCAACTTCAGCGAG
TGCTGGTGGGATCACTGGATCATGGACGTGCTCGTCTGCAACGGGCTGGGCATCTACTGC
GGCATGAAGACCCTTGAGTGGCTGTCCCTGAAGACGTACAAGTGGCAGGGCCTCTGGAAC
ATTCCGACCTACAAGGGCAAGATGAAGAGGATCGCCTTCCAGTTCACGCCGTACAGCTGG
GTTCGCTTCGAGTGGAAGCCGGCCTCCAGCCTGCGTCGCTGGCTGGCCGTGTGCGGCATC
ATCCTGGTGTTCCTGTTGGCAGAACTGAACACGTTCTACCTGAAGTTTGTGCTGTGGATG
CCCCCGGAGCACTACCTGGTCCTCCTGCGGCTCGTCTTCTTCGTGAACGTGGGTGGCGTG
GCCATGCGTGAGATCTACGACTTCATGGATGACCCGAAGCCCCACAAGAAGCTGGGCCCG
CAGGCCTGGCTGGTGGCGGCCATCACGGCCACGGAGCTGCTCATCGTGGTGAAGTACGAC
CCCCACACGCTCACCCTGTCCCTGCCCTTCTACATCTCCCAGTGCTGGACCCTCGGCTCC
GTCCTGGCGCTCACCTGGACCGTCTGGCGCTTCTTCCTGCGGGACATCACATTGAGGTAC
AAGGAGACCCGGTGGCAGAAGTGGCAGAACAAGGATGACCAGGGCAGCACCGTCGGCAAC
GGGGACCAGCACCCACTGGGGCTGGACGAAGACCTGCTGGGGCCTGGGGTGGCCGAGGGC
GAGGGAGCACCAACTCCAAACTGA
Enzyme 37 GenBank Gene ID AL834357 Link Image
Enzyme 37 GeneCard ID PTDSS2 Link Image
Enzyme 37 GenAtlas ID PTDSS2 Link Image
Enzyme 37 HGNC ID HGNC:15463 Link Image
Enzyme 37 Chromosome Location 11
Enzyme 37 Locus 11p15
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References Not Available
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 8495
Enzyme 38 Name Phosphatidylinositol-glycan biosynthesis class W protein
Enzyme 38 Synonyms
  1. PIG-W
Enzyme 38 Gene Name PIGW
Enzyme 38 Protein Sequence >Phosphatidylinositol-glycan biosynthesis class W protein 
MSEKQMKEAFVSNLNGTTVLEITQGLCFPAFCILCRGFLIIFSQYLCSFSPTWKTRFLTD
FVVLIVPMVATLTIWASFILLELLGVIIFGAGLLYQIYRRRTCYARLPFLKILEKFLNIS
LESEYNPAISCFRVITSAFTAIAILAVDFPLFPRRFAKTELYGTGAMDFGVGGFVFGSAM
VCLEVRRRKYMEGSKLHYFTNSLYSVWPLVFLGIGRLAIIKSIGYQEHLTEYGVHWNFFF
TIIVVKLITPLLLIIFPLNKSWIIALGITVLYQLALDFTSLKRLILYGTDGSGTRVGLLN
ANREGIISTLGYVAIHMAGVQTGLYMHKNRSHIKDLIKVACFLLLAAISLFISLYVVQVN
VEAVSRRMANLAFCIWIVASSLILLSSLLLGDIILSFAKFLIKGALVPCSWKLIQSPVTN
KKHSESLVPEAERMEPSLCLITALNRKQLIFFLLSNITTGLINLMVDTLHSSTLWALFVV
NLYMFSNCLIVYVLYLQDKTVQFW
Enzyme 38 Number of Residues 504
Enzyme 38 Molecular Weight 56883
Enzyme 38 Theoretical pI 9.44
Enzyme 38 GO Classification
Function
  • acetyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • GPI anchor biosynthesis
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein modification
Component
  • cell
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • organelle membrane
Enzyme 38 General Function Not Available
Enzyme 38 Specific Function Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI- anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually removed soon after the attachment of GPIs to proteins
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions Not Available
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • 1-43
Enzyme 38 Transmembrane Regions
  • 22-42 74-94 132-152 163-183 203-223 238-258 261-281 306-326 339-359 371-391 449-469 474-494
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein Not Available
Enzyme 38 UniProtKB/Swiss-Prot ID Q7Z7B1 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name PIGW_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence Not Available
Enzyme 38 GenBank Gene ID AB097818 Link Image
Enzyme 38 GeneCard ID PIGW Link Image
Enzyme 38 GenAtlas ID PIGW Link Image
Enzyme 38 HGNC ID HGNC:23213 Link Image
Enzyme 38 Chromosome Location 17
Enzyme 38 Locus 17q12
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References Not Available
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 8621
Enzyme 39 Name Phosphatidylinositol-glycan biosynthesis class X protein precursor
Enzyme 39 Synonyms
  1. PIG-X
Enzyme 39 Gene Name PIGX
Enzyme 39 Protein Sequence >Phosphatidylinositol-glycan biosynthesis class X protein precursor 
MAARVAAVRAAAWLLLGAATGLTRGPATAFTAARSDAGIRAMCSEIILRQEVLKDGFHRD
LLIKVKFGESIEDLHTCRLLIKQDIPAGLYVDPYELASLRERNITEAVMVSENFDIEAPN
YLSKESEVLIYARRDSQCIDCFQAFLPVHCRYHRPHSEDGEASIVVNNPDLLMFCDQEFP
ILKCWAHSEVAAPCALDNEDICQWNKMKYKSVYKNVILQVPVGLTVHTSLVCSVTLLITI
LCSTLILVAVFKYGHFSL
Enzyme 39 Number of Residues 258
Enzyme 39 Molecular Weight 28805
Enzyme 39 Theoretical pI 6.30
Enzyme 39 GO Classification Not Available
Enzyme 39 General Function Not Available
Enzyme 39 Specific Function Essential component of glycosylphosphatidylinositol- mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the mannosyltransferase PIGM
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions Not Available
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • 1-21
Enzyme 39 Transmembrane Regions
  • 231-251
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 18490317 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q8TBF5 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name PIGX_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >654 bp 
ATGTGTTCTGAAATTATTTTGAGGCAAGAAGTTTTGAAAGATGGTTTCCACAGAGACCTT
TTAATCAAAGTGAAGTTTGGGGAAAGCATTGAGGACTTGCACACGTGCCGTCTCTTAATT
AAACAGGACATTCCTGCAGGACTTTATGTGGATCCGTATGAGTTGGCTTCATTACGAGAG
AGAAACATAACAGAGGCAGTGATGGTTTCAGAAAATTTTGATATAGAGGCCCCTAACTAT
TTGTCCAAGGAGTCTGAAGTTCTCATTTATGCCAGACGAGATTCACAGTGCATTGACTGT
TTTCAAGCCTTTTTGCCTGTGCACTGCCGCTATCATCGGCCGCACAGTGAAGATGGAGAA
GCCTCGATTGTGGTCAATAACCCAGATTTGTTGATGTTTTGTGACCAAGAGTTCCCGATT
TTGAAATGCTGGGCTCACTCAGAAGTGGCAGCCCCTTGTGCTTTGGATAATGAGGATATA
TGCCAATGGAACAAGATGAAGTATAAATCAGTATATAAGAATGTGATTCTACAAGTTCCA
GTGGGACTGACTGTACATACCTCTCTAGTATGTTCTGTGACTCTGCTCATTACAATCCTG
TGCTCTACATTGATCCTTGTAGCAGTTTTCAAATATGGCCATTTTTCCCTATAA
Enzyme 39 GenBank Gene ID BC022542 Link Image
Enzyme 39 GeneCard ID PIGX Link Image
Enzyme 39 GenAtlas ID PIGX Link Image
Enzyme 39 HGNC ID HGNC:26046 Link Image
Enzyme 39 Chromosome Location 3
Enzyme 39 Locus 3q29
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References Not Available
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 8625
Enzyme 40 Name GPI mannosyltransferase 4
Enzyme 40 Synonyms
  1. GPI mannosyltransferase IV
  2. GPI-MT-IV
  3. Phosphatidylinositol-glycan biosynthesis class Z protein
  4. PIG-Z
  5. hSMP3
Enzyme 40 Gene Name PIGZ
Enzyme 40 Protein Sequence >GPI mannosyltransferase 4 
MAVRVLWGGLSLLRVLWCLLPQTGYVHPDEFFQSPEVMAEDILGVQAARPWEFYPSSSCR
SVLFPLLISGSTFWLLRLWEELGPWPGLVSGYALLVGPRLLLTALSFALDGAVYHLAPPM
GADRWNALALLSGSYVTLVFYTRTFSNTIEGLLFTWLLVLVSSHVTWGPTRKEPAPGPRW
RSWLLGGIVAAGFFNRPTFLAFAVVPLYLWGTRGATNPGLKSLTREALVLLPGATLTAAV
FVATDSWYFSSPATSRNLVLTPVNFLHYNLNPQNLARHGTHARLTHLAVNGFLLFGVLHA
QALQAAWQQLQVGLQASAQMGLLRALGARSLLSSPRSYLLLLYFMPLALLSAFSHQEARF
LIPLLVPLVLLCSPQTQPVPWKGTVVLFNALGALLFGCLHQGGLVPGLEYLEQVVHAPVL
PSTPTHYTLLFTHTYMPPRHLLHLPGLGAPVEVVDIGGTEDWALCQTLKSFTRQPACQVA
GGPWLCRLFVVTPGTTRRAVEKCSFPFKNETLLFPHLTLEDPPALSSLLSGAWRDHLSLH
IVELGEET
Enzyme 40 Number of Residues 548
Enzyme 40 Molecular Weight 60249
Enzyme 40 Theoretical pI 8.40
Enzyme 40 GO Classification Not Available
Enzyme 40 General Function Not Available
Enzyme 40 Specific Function Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to some trimannosyl-GPIs during GPI precursor assembly. The presence of a fourth mannose in GPI is facultative and only scarcely detected, suggesting that it only exists in some tissues
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • 1-28
Enzyme 40 Transmembrane Regions
  • 100-120 125-142 149-169 185-205 227-247 338-358
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein Not Available
Enzyme 40 UniProtKB/Swiss-Prot ID Q86VD9 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name PIGZ_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence Not Available
Enzyme 40 GenBank Gene ID AK022830 Link Image
Enzyme 40 GeneCard ID PIGZ Link Image
Enzyme 40 GenAtlas ID PIGZ Link Image
Enzyme 40 HGNC ID HGNC:30596 Link Image
Enzyme 40 Chromosome Location 3
Enzyme 40 Locus 3q29
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References Not Available
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 8839
Enzyme 41 Name Inositol polyphosphate 5-phosphatase
Enzyme 41 Synonyms Not Available
Enzyme 41 Gene Name INPPL1
Enzyme 41 Protein Sequence >Inositol polyphosphate 5-phosphatase 
MASACGAPGPGGALGSQAPSWYHRDLSRAAAEELLARAGRDGSFLVRDSESVAGAFALCV
LYQKHVHTYRILPDGEDFLAVQTSQGVPVRRFQTLGELIGLYAQPNQGLVCALLLPVEGE
REPDPPDDRDASDGEDEKPPLPPRSGSTSISAPTGPSSPLPAPETPTAPAAESAPNGLST
VSHDYLKGSYGLDLEAVRGGASHLPHLTRTLATSCRRLHSEVDKVLSGLEILSKVFDQQS
SPMVTRLLQQQNLPQTGEQELESLVLKLSVLKDFLSGIQKKALKALQDMSSTAPPAPQPS
TRKAKTIPVQAFEVKLDVTLGDLTKIGKSQKFTLSVDVEGGRLVLLRRQRDSQEDWTTFT
HDRIRQLIKSQRVQNKLGVVFEKEKDRTQRKDFIFVSARKREAFCQLLQLMKNKHSKQDE
PDMISVFIGTWNMGSVPPPKNVTSWFTSKGLGKTLDEVTVTIPHDIYVFGTQENSVGDRE
WLDLLRGGLKELTDLDYRPIAMQSLWNIKVAVLVKPEHENRISHVSTSSVKTGIANTLGN
KGAVGVSFMFNGTSFGFVNCHLTSGNEKTARRNQNYLDILRLLSLGDRQLNAFDISLRFT
HLFWFGDLNYRLDMDIQEILNYISRKEFEPLLRVDQLNLEREKHKVFLRFSEEEISFPPT
YRYERGSRDTYAWHKQKPTGVRTNVPSWCDRILWKSYPETHIICNSYGCTDDIVTSDHSP
VFGTFEVGVTSQFISKKGLSKTSDQAYIEFESIEAIVKTASRTKFFIEFYSTCLEEYKKS
FENDAQSSDNINFLKVQWSSRQLPTLKPILADIEYLQDQHLLLTVKSMDGYESYGECVVA
LKSMIGSTAQQFLTFLSHRGEETGNIRGSMKVRVPTERLGTRERLYEWISIDKDEAGAKS
KAPSVSRGSQEPRSGSRKPAFTEASCPLSRLFEEPEKPPPTGRPPAPPRAAPREEPLTPR
LKPEGAPEPEGVAAPPPKNSFNNPAYYVLEGVPHQLLPPEPPSPARAPVPSATKNKVAIT
VPAPQLGHHRHPRVGEGSSSDEESGGTLPPPDFPPPPLPDSAIFLPPSLDPLPGPVVRGR
GGAEARGPPPPKAHPRPPLPPGPSPASTFLGEVGSGDDRSCSVLQMAKTLSEVDYAPAGP
ARSALLPGPLELQPPRGLPSDYGRPLSFPPPRIRESIQEDLAEEAPCLQGGRASGLGEAG
MSAWLRAIGLERYEEGLVHNGWDDLEFLSDITEEDLEEAGVQDPAHKRLLLDTLQLSK
Enzyme 41 Number of Residues 1258
Enzyme 41 Molecular Weight 138586
Enzyme 41 Theoretical pI 6.49
Enzyme 41 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • signal transduction
Component
—
Enzyme 41 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 41 Specific Function Not Available
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions Not Available
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals Not Available
Enzyme 41 Transmembrane Regions Not Available
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 2653424 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID O15357 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name O15357_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >3777 bp 
ATGGCCTCGGCCTGCGGGGCGCCGGGCCCGGGGGGCGCCCTGGGCAGCCAGGCCCCCTCC
TGGTACCACCGCGACCTGAGCCGGGCGGCCGCGGAGGAGCTGCTGGCCCGGGCGGGCCGC
GATGGCAGCTTCCTGGTCCGAGACAGCGAGAGCGTGGCGGGGGCCTTCGCGCTCTGCGTC
CTGTATCAGAAGCATGTGCACACGTATCGCATTCTGCCTGATGGAGAAGATTTCTTGGCT
GTGCAGACCTCGCAGGGTGTGCCTGTGCGCCGCTTCCAGACCCTGGGTGAGCTCATCGGC
CTGTACGCCCAGCCCAACCAGGGCCTTGTGTGCGCCCTGCTTCTTCCTGTAGAGGGTGAG
CGAGAGCCGGACCCACCGGATGACCGGGATGCCTCAGATGGGGAGGATGAGAAGCCCCCG
CTGCCCCCGCGCTCTGGCTCCACCAGCATTTCTGCCCCCACTGGGCCCAGCAGTCCCCTG
CCAGCTCCTGAGACTCCCACAGCTCCAGCTGCTGAGAGTGCTCCCAATGGGCTGAGCACC
GTCTCGCACGACTACCTGAAAGGCAGCTATGGGCTGGACCTGGAAGCTGTGAGGGGTGGA
GCCAGCCACCTGCCCCACCTCACCCGTACCCTCGCTACCTCATGCCGGAGGCTGCACAGT
GAGGTGGACAAGGTCCTGTCAGGCCTGGAGATCCTGTCCAAGGTGTTTGACCAGCAGAGC
TCGCCCATGGTGACCCGCCTTTTGCAGCAGCAGAACCTGCCACAGACAGGGGAGCAGGAA
CTAGAGAGCCTGGTGCTGAAGCTGTCAGTGCTAAAGGACTTCCTGTCAGGCATCCAGAAG
AAGGCCCTGAAGGCCCTACAGGACATGAGCTCCACAGCACCCCCAGCTCCGCAGCCATCC
ACACGTAAGGCCAAGACCATCCCCGTGCAGGCCTTTGAGGTGAAGCTAGATGTGACCCTG
GGTGACCTGACCAAGATTGGGAAGTCACAGAAGTTCACGCTGAGCGTGGATGTGGAGGGT
GGGCGGCTGGTGCTGCTGCGGAGACAGCGGGACTCCCAGGAGGACTGGACCACCTTCACG
CACGACCGCATCCGCCAGCTCATTAAGTCCCAGCGTGTCCAGAACAAGCTGGGTGTTGTG
TTTGAGAAGGAGAAGGACCGGACTCAGCGCAAGGACTTCATCTTTGTCAGTGCCCGGAAG
CGGGAGGCCTTCTGCCAGCTGTTGCAGCTCATGAAGAACAAGCACTCCAAGCAGGACGAG
CCCGACATGATCTCAGTCTTCATAGGCACCTGGAACATGGGAAGTGTACCACCTCCAAAA
AACGTGACATCCTGGTTCACATCGAAGGGTCTGGGGAAGACCCTGGACGAGGTCACAGTG
ACCATACCCCATGACATCTATGTCTTTGGGACCCAGGAGAACTCAGTGGGCGACCGCGAG
TGGCTGGACCTACTGCGCGGGGGCCTCAAGGAGCTTACGGATCTGGATTACCGCCCGATT
GCCATGCAATCACTGTGGAATATCAAGGTGGCAGTGCTGGTCAAGCCAGAGCACGAGAAC
CGTATCAGCCATGTCAGTACGTCCAGTGTGAAGACTGGCATCGCCAACACCCTGGGGAAC
AAGGGGGCTGTGGGCGTCTCCTTCATGTTTAATGGCACCTCATTTGGCTTTGTGAATTGT
CACCTCACCTCGGGAAATGAGAAGACGGCTCGGAGGAACCAAAACTACTTGGACATCCTG
CGGCTGCTCTCGCTGGGCGACCGGCAGCTCAATGCCTTTGACATCTCTCTGCGTTTCACA
CACCTCTTCTGGTTTGGGGACCTCAACTACCGCCTGGACATGGATATCCAGGAGATCCTG
AACTACATCAGCAGGAAAGAGTTTGAGCCCCTCCTCAGGGTGGACCAGCTCAACCTGGAG
CGGGAGAAGCACAAGGTCTTCCTTCGATTCAGTGAGGAGGAGATCTCCTTCCCACCCACC
TACCGCTATGAGCGGGGTTCCCGGGACACATATGCCTGGCACAAGCAGAAGCCAACTGGG
GTCCGGACCAATGTGCCCTCATGGTGTGACCGGATTCTGTGGAAATCCTACCCTGAAACT
CACATCATCTGCAATTCTTATGGTTGCACTGATGACATCGTCACCAGCGACCATTCCCCC
GTGTTTGGGACATTTGAGGTTGGAGTTACCTCCCAGTTCATCTCCAAGAAAGGGCTCTCA
AAGACTTCAGACCAGGCCTACATTGAGTTTGAGAGCATCGAGGCCATTGTGAAGACAGCC
AGCCGCACCAAGTTCTTCATCGAGTTCTACTCTACCTGCCTGGAGGAATACAAGAAGAGC
TTTGAGAATGATGCCCAGAGCAGTGACAACATCAACTTCCTCAAAGTGCAGTGGTCTTCA
CGCCAGCTGCCCACGCTCAAACCAATTCTGGCTGATATCGAGTACCTGCAGGACCAGCAC
CTCCTGCTCACAGTCAAGTCCATGGATGGCTATGAATCCTATGGGGAGTGTGTGGTTGCA
CTCAAATCCATGATCGGCAGCACGGCCCAACAGTTCCTGACCTTCCTATCCCACCGTGGC
GAGGAGACAGGCAATATCAGAGGCTCCATGAAGGTGCGGGTGCCCACGGAGCGCCTGGGC
ACCCGTGAGCGGCTCTACGAGTGGATCAGCATTGATAAGGATGAGGCAGGAGCAAAGAGC
AAAGCCCCCTCTGTGTCCCGAGGGAGCCAGGAGCCCAGGTCAGGGAGCCGCAAGCCAGCC
TTCACAGAGGCCTCCTGCCCGCTCTCCAGGTTATTTGAAGAACCAGAGAAACCGCCACCA
ACGGGGAGGCCCCCAGCCCCACCCCGAGCAGCTCCCCGGGAGGAGCCCTTGACCCCCAGG
TTGAAGCCAGAGGGAGCTCCTGAACCAGAAGGGGTGGCGGCCCCCCCACCCAAGAACAGC
TTCAATAACCCTGCCTACTACGTCCTTGAAGGGGTCCCGCACCAGCTGCTGCCCCCGGAG
CCACCCTCGCCTGCCAGGGCCCCTGTCCCATCTGCCACCAAGAACAAAGTGGCCATTACA
GTGCCTGCTCCACAGCTTGGGCACCACCGGCACCCTCGTGTGGGAGAGGGGAGTTCTTCA
GATGAGGAGTCTGGAGGCACACTGCCCCCTCCAGACTTTCCACCTCCACCACTGCCGGAC
TCAGCCATCTTCCTGCCCCCCAGCCTGGATCCTTTACCAGGGCCAGTGGTCCGGGGCCGT
GGTGGGGCTGAGGCCCGTGGCCCACCACCTCCCAAGGCCCATCCAAGGCCTCCACTGCCC
CCAGGCCCCTCACCAGCCAGCACTTTCCTGGGGGAAGTGGGCAGTGGGGATGACCGGTCC
TGCTCGGTGCTGCAGATGGCCAAGACGCTGAGCGAGGTGGACTATGCCCCTGCTGGGCCT
GCACGCTCAGCGCTCCTCCCAGGCCCCCTGGAGCTGCAGCCCCCCCGGGGACTGCCCTCG
GACTATGGCCGGCCCCTCAGCTTCCCTCCACCCCGCATCCGGGAGAGCATCCAGGAAGAC
CTGGCAGAGGAGGCTCCGTGCCTGCAGGGCGGGCGGGCCAGCGGGCTGGGCGAGGCAGGC
ATGAGTGCCTGGCTGCGGGCCATCGGCTTGGAGCGCTATGAGGAGGGCCTGGTGCATAAT
GGCTGGGACGACCTGGAGTTTCTCAGTGACATCACCGAGGAGGACTTGGAGGAGGCTGGG
GTGCAGGACCCGGCTCACAAGCGCCTCCTTCTGGACACCCTGCAGCTCAGCAAGTGA
Enzyme 41 GenBank Gene ID Y14385 Link Image
Enzyme 41 GeneCard ID INPPL1 Link Image
Enzyme 41 GenAtlas ID INPPL1 Link Image
Enzyme 41 HGNC ID HGNC:6080 Link Image
Enzyme 41 Chromosome Location 11
Enzyme 41 Locus 11q23
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Pesesse X, Deleu S, De Smedt F, Drayer L, Erneux C: Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP. Biochem Biophys Res Commun. 1997 Oct 29;239(3):697-700. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 9375
Enzyme 42 Name Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1
Enzyme 42 Synonyms
  1. SH2 domain-containing inositol-5'-phosphatase 1
  2. SH2 domain- containing inositol phosphatase 1
  3. SHIP-1
  4. Inositol polyphosphate-5- phosphatase of 145 kDa
  5. SIP-145
  6. p150Ship
  7. hp51CN
Enzyme 42 Gene Name INPP5D
Enzyme 42 Protein Sequence >Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 
MVPCWNHGNITRSKAEELLSRTGKDGSFLVRASESISRAYALCVLYRNCVYTYRILPNED
DKFTVQASEGVSMRFFTKLDQLIEFYKKENMGLVTHLQYPVPLEEEDTGDDPEEDTVESV
VSPPELPPRNIPLTASSCEAKEVPFSNENPRATETSRPSLSETLFQRLQSMDTSGLPEEH
LKAIQDYLSTQLAQDSEFVKTGSSSLPHLKKLTTLLCKELYGEVIRTLPSLESLQRLFDQ
QLSPGLRPRPQVPGEANPINMVSKLSQLTSLLSSIEDKVKALLHEGPESPHRPSLIPPVT
FEVKAESLGIPQKMQLKVDVESGKLIIKKSKDGSEDKFYSHKKILQLIKSQKFLNKLVIL
VETEKEKILRKEYVFADSKKREGFCQLLQQMKNKHSEQPEPDMITIFIGTWNMGNAPPPK
KITSWFLSKGQGKTRDDSADYIPHDIYVIGTQEDPLSEKEWLEILKHSLQEITSVTFKTV
AIHTLWNIRIVVLAKPEHENRISHICTDNVKTGIANTLGNKGAVGVSFMFNGTSLGFVNS
HLTSGSEKKLRRNQNYMNILRFLALGDKKLSPFNITHRFTHLFWFGDLNYRVDLPTWEAE
TIIQKIKQQQYADLLSHDQLLTERREQKVFLHFEEEEITFAPTYRFERLTRDKYAYTKQK
ATGMKYNLPSWCDRVLWKSYPLVHVVCQSYGSTSDIMTSDHSPVFATFEAGVTSQFVSKN
GPGTVDSQGQIEFLRCYATLKTKSQTKFYLEFHSSCLESFVKSQEGENEEGSEGELVVKF
GETLPKLKPIISDPEYLLDQHILISIKSSDSDESYGEGCIALRLEATETQLPIYTPLTHH
GELTGHFQGEIKLQTSQGKTREKLYDFVKTERDESSGPKTLKSLTSHDPMKQWEVTSRAP
PCSGSSITEIINPNYMGVGPFGPPMPLHVKQTLSPDQQPTAWSYDQPPKDSPLGPCRGES
PPTPPGQPPISPKKFLPSTANRGLPPRTQESRPSDLGKNAGDTLPQEDLPLTKPEMFENP
LYGSLSSFPKPAPRKDQESPKMPRKEPPPCPEPGILSPSIVLTKAQEADRGEGPGKQVPA
PRLRSFTCSSSAEGRAAGGDKSQGKPKTPVSSQAPVPAKRPIKPSRSEINQQTPPTPTPR
PPLPVKSPAVLHLQHSKGRDYRDNTELPHHGKHRPEEGPPGPLGRTAMQ
Enzyme 42 Number of Residues 1189
Enzyme 42 Molecular Weight 133294
Enzyme 42 Theoretical pI Not Available
Enzyme 42 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • signal transduction
Component
—
Enzyme 42 General Function Cell cycle control, cell division, chromosome partitioning
Enzyme 42 Specific Function Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol- 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity. Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions
  • H2O + 1D-myo-Inositol 1,3,4,5-tetrakisphosphate --> 1D-myo-Inositol 1,3,4-trisphosphate + Phosphate
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 1495456 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q92835 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name SHIP1_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence Not Available
Enzyme 42 GenBank Gene ID X98429 Link Image
Enzyme 42 GeneCard ID Not Available
Enzyme 42 GenAtlas ID INPP5D Link Image
Enzyme 42 HGNC ID HGNC:6079 Link Image
Enzyme 42 Chromosome Location Not Available
Enzyme 42 Locus Not Available
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Drayer AL, Pesesse X, De Smedt F, Woscholski R, Parker P, Erneux C: Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase. Biochem Biophys Res Commun. 1996 Aug 5;225(1):243-9. [PubMed Link Image]
  2. Ware MD, Rosten P, Damen JE, Liu L, Humphries RK, Krystal G: Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation. Blood. 1996 Oct 15;88(8):2833-40. [PubMed Link Image]
  3. Kavanaugh WM, Pot DA, Chin SM, Deuter-Reinhard M, Jefferson AB, Norris FA, Masiarz FR, Cousens LS, Majerus PW, Williams LT: Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2. Curr Biol. 1996 Apr 1;6(4):438-45. [PubMed Link Image]
  4. Geier SJ, Algate PA, Carlberg K, Flowers D, Friedman C, Trask B, Rohrschneider LR: The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood. Blood. 1997 Mar 15;89(6):1876-85. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 9581
Enzyme 43 Name Phosphatidylinositol 3-kinase catalytic subunit type 3
Enzyme 43 Synonyms
  1. PtdIns-3-kinase type 3
  2. PI3-kinase type 3
  3. PI3K type 3
  4. Phosphoinositide-3-kinase class 3
  5. Phosphatidylinositol 3-kinase p100 subunit
Enzyme 43 Gene Name PIK3C3
Enzyme 43 Protein Sequence >Phosphatidylinositol 3-kinase catalytic subunit type 3 
MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVT
CQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAV
PVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTK
AHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDG
DESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIV
SYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDV
EDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKK
DSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLI
SRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRS
LLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVK
IRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRK
ENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAE
VMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLN
KEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVK
KVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK
Enzyme 43 Number of Residues 887
Enzyme 43 Molecular Weight 101551
Enzyme 43 Theoretical pI Not Available
Enzyme 43 GO Classification
Function
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • kinase activity
  • lipid kinase activity
  • phosphatidylinositol 3-kinase activity
  • phosphoinositide 3-kinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
—
Component
  • phosphoinositide 3-kinase complex
  • protein complex
Enzyme 43 General Function Not Available
Enzyme 43 Specific Function Catalytic subunit of the PI3K complex. Involved in the transport of lysosomal enzyme precursors to lysosomes
Enzyme 43 Pathways
Enzyme 43 Reactions
  • ATP + phosphatidylinositol (homo sapiens) --> ADP + H+ + 1-Phosphatidyl-1D-myo-inositol 3-phosphate (Homo sapiens)
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 987948 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID Q8NEB9 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name PK3C3_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence Not Available
Enzyme 43 GenBank Gene ID Z46973 Link Image
Enzyme 43 GeneCard ID Not Available
Enzyme 43 GenAtlas ID PIK3C3 Link Image
Enzyme 43 HGNC ID HGNC:8974 Link Image
Enzyme 43 Chromosome Location Not Available
Enzyme 43 Locus Not Available
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Volinia S, Dhand R, Vanhaesebroeck B, MacDougall LK, Stein R, Zvelebil MJ, Domin J, Panaretou C, Waterfield MD: A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system. EMBO J. 1995 Jul 17;14(14):3339-48. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 10045
Enzyme 44 Name Phosphatidylinositol-specific phospholipase C X domain-containing protein 2
Enzyme 44 Synonyms
  1. PI-PLC X domain-containing protein 2
Enzyme 44 Gene Name PLCXD2
Enzyme 44 Protein Sequence >Phosphatidylinositol-specific phospholipase C X domain-containing protein 2 
MLAVRKARRKLRMGTICSPNPSGTKTSSEVCNADWMASLPPHLHNLPLSNLAIPGSHDSF
SYWVDEKSPVGPDQTQAIKRLARISLVKKLMKKWSVTQNLTFREQLEAGIRYFDLRVSSK
PGDADQEIYFIHGLFGIKVWDGLMEIDSFLTQHPQEIIFLDFNHFYAMDETHHKCLVLRI
QEAFGNKLCPACSVESLTLRTLWEKNCQVLIFYHCPFYKQYPFLWPGKKIPAPWANTTSV
RKLILFLETTLSERASRGSFHVSQAILTPRVKTIARGLVGGLKNTLVHSNRWNSHGPSLL
SQERS
Enzyme 44 Number of Residues 305
Enzyme 44 Molecular Weight 34778
Enzyme 44 Theoretical pI Not Available
Enzyme 44 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase C activity
  • phospholipase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • signal transduction
Component
—
Enzyme 44 General Function Not Available
Enzyme 44 Specific Function Not Available
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions
  • H2O + 1-Phosphatidyl-1D-myo-inositol 4-phosphate (Homo sapiens) --> diacylglycerol (homo sapiens) + H+ + 1D-myo-Inositol 1,4-bisphosphate
Enzyme 44 Pfam Domain Function Not Available
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 16551464 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID Q0VAA5 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name PLCX2_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence Not Available
Enzyme 44 GenBank Gene ID AK056141 Link Image
Enzyme 44 GeneCard ID Not Available
Enzyme 44 GenAtlas ID PLCXD2 Link Image
Enzyme 44 HGNC ID HGNC:26462 Link Image
Enzyme 44 Chromosome Location Not Available
Enzyme 44 Locus Not Available
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References Not Available
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 10047
Enzyme 45 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
Enzyme 45 Synonyms
  1. Phosphoinositide phospholipase C delta-4
  2. PLC-delta-4
  3. Phospholipase C-delta-4
  4. hPLCD4
Enzyme 45 Gene Name PLCD4
Enzyme 45 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4 
MASLLQDQLTTDQDLLLMQEGMPMRKVRSKSWKKLRYFRLQNDGMTVWHARQARGSAKPS
FSISDVETIRNGHDSELLRSLAEELPLEQGFTIVFHGRRSNLDLMANSVEEAQIWMRGLQ
LLVDLVTSMDHQERLDQWLSDWFQRGDKNQDGKMSFQEVQRLLHLMNVEMDQEYAFSLFQ
AADTSQSGTLEGEEFVQFYKALTKRAEVQELFESFSADGQKLTLLEFLDFLQEEQKERDC
TSELALELIDRYEPSDSGKLRHVLSMDGFLSYLCSKDGDIFNPACLPIYQDMTQPLNHYF
ICSSHNTYLVGDQLCGQSSVEGYIRALKRGCRCVEVDVWDGPSGEPVVYHGHTLTSRILF
KDVVATVAQYAFQTSDYPVILSLETHCSWEQQQTMARHLTEILGEQLLSTTLDGVLPTQL
PSPEELRRKILVKGKKLTLEEDLEYEEEEAEPELEESELALESQFETEPEPQEQNLQNKD
KKKKSKPILCPALSSLVIYLKSVSFRSFTHSKEHYHFYEISSFSETKAKRLIKEAGNEFV
QHNTWQLSRVYPSGLRTDSSNYNPQELWNAGCQMVAMNMQTAGLEMDICDGHFRQNGGCG
YVLKPDFLRDIQSSFHPEKPISPFKAQTLLIQVISGQQLPKVDKTKEGSIVDPLVKVQIF
GVRLDTARQETNYVENNGFNPYWGQTLCFRVLVPELAMLRFVVMDYDWKSRNDFIGQYTL
PWTCMQQGYRHIHLLSKDGISLRPASIFVYICIQEGLEGDES
Enzyme 45 Number of Residues 762
Enzyme 45 Molecular Weight 87586
Enzyme 45 Theoretical pI Not Available
Enzyme 45 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 45 General Function Not Available
Enzyme 45 Specific Function Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Required for acrosome reaction in sperm during fertilization, probably by acting as an important enzyme for intracellular Ca(2+) mobilization in the zona pellucida- induced acrosome reaction. May play a role in cell growth. Modulates the liver regeneration in cooperation with nuclear PKC. Overexpression upregulates the Erk signaling pathway and proliferation
Enzyme 45 Pathways
Enzyme 45 Reactions
  • H2O + 1-Phosphatidyl-1D-myo-inositol 4-phosphate (Homo sapiens) --> diacylglycerol (homo sapiens) + H+ + 1D-myo-Inositol 1,4-bisphosphate
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 46198236 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID Q9BRC7 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name PLCD4_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence Not Available
Enzyme 45 GenBank Gene ID AY512961 Link Image
Enzyme 45 GeneCard ID Not Available
Enzyme 45 GenAtlas ID PLCD4 Link Image
Enzyme 45 HGNC ID HGNC:9062 Link Image
Enzyme 45 Chromosome Location Not Available
Enzyme 45 Locus Not Available
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References Not Available
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 10048
Enzyme 46 Name Phospholipase C eta 1
Enzyme 46 Synonyms
  1. Phospholipase C-eta1
Enzyme 46 Gene Name Not Available
Enzyme 46 Protein Sequence >Phospholipase C eta 1 
MADLEVYKNLSPEKVERCMSVMQSGTQMIKLKRGTKGLVRLFYLDEHRTRLRWRPSRKSE
KAKILIDSIYKVTEGRQSEIFHRQAEGNFDPSCCFTIYHGNHMESLDLITSNPEEARTWI
TGLKYLMAGISDEDSLAKRQRTHDQWVKQTFEEADKNGDGLLNIEEIHQLMHKLNVNLPR
RKVRQMFQEADTDENQGTLTFEEFCVFYKMMSLRRDLYLLLLSYSDKKDHLTVEELAQFL
KVEQKMNNVTTDYCLDIIKKFEVSEENKVKNVLGIEGFTNFMRSPACDIFNPLHHEVYQD
MDQPLCNYYIASSHNTYLTGDQLLSQSKVDMYARVLQEGCRCVEVDCWDGPDGEPVVHHG
YTLTSKILFRDVVETINKHAFVKNEFPVILSIENHCSIQQQRKIAQYLKGIFGDKLDLSS
VDTGECKQLPSPQSLKGKILVKGKKLPYHLGDDAEEGEVSDEDSADEIEDECKFKLHYSN
GTTEHQVESFIRKKLESLLKESQIRDKEDPDSFTVRALLKATHEGLNAHLKQSPDVKESG
KKSHGRSLMTNFGKHKKTTKSRSKSYSTDDEEDTQQSTGKEGGQLYRLGRRRKTMKLCRE
LSDLVVYTNSVAAQDIVDDGTTGNVLSFSETRAHQVVQQKSEQFMIYNQKQLTRIYPSAY
RIDSSNFNPLPYWNAGCQLVALNYQSEGRMMQLNRAKFKANGNCGYVLKPQQMCKGTFNP
FSGDPLPANPKKQLILKVISGQQLPKPPDSMFGDRGEIIDPFVEVEIIGLPVDCCKDQTR
VVDDNGFNPVWEETLTFTVHMPEIALVRFLVWDHDPIGRDFVGQRTVTFSSLVPGYRHVY
LEGLTEASIFVHITINEIYGKWSPLILNPSYTILHFLGATKNRQLQGLKGLFNKNPRHSS
SENNSHYVRKRSIGDRILRRTASAPAKGRKKSKMGFQEMVEIKDSVSEATRDQDGVLRRT
TRSLQARPVSMPVDRNLLGALSLPVSETAKDIEGKENSLAEDKDGRRKGKASIKDPHFLN
FNKKLSSSSSALLHKDTSQGDTIVSTAHMSVTGEQLGMSSPRGGRTTSNATSNCQENPCP
SKSLSPKQHLAPDPVVNPTQDLHGVKIKEKGNPEDFVEGKSILSGSVLSHSNLEIKNLEG
NRGKGRAATSFSLSDVSMLCSDIPDLHSTAILQESVISHLIDNVTLTNENEPGSSISALI
GQFDETNNQALTVVSHLHNTSVMSGHCPLPSLGLKMPIKHGFCKGKSKSSFLCSSPELIA
LSSSETTKHATNTVYETTCTPISKTKPDDDLSSKAKTAALESNLPGSPNTSRGWLPKSPT
KGEDWETLKSCSPASSPDLTLEDVIADPTLCFNSGESSLVEIDGESENLSLTTCEYRREG
TSQLASPLKLKYNQGVVEHFQRGLRNGYCKETLRPSVPEIFNNIQDVKTQSISYLAYQGA
GFVHNHFSDSDAKMFQTCVPQQSSAQDMHVPVPKQLAHLPLPALKLPSPCKSKSLGDLTS
EDIACNFESKYQCISKSFVTTGIRDKKGVTVKTKSLEPIDALTEQLRKLVSFDQEDNCQV
LYSKQDANQLPRALVRKLSSRSQSRVRNIASRAKEKQEANKQKVPNPSNGAGVVLRNKPS
APTPAVNRHSTGSYIAGYLKNTKGGGLEGRGIPEGACTALHYGHVDQFCSDNSVLQTEPS
SDDKPEIYFLLRL
Enzyme 46 Number of Residues 1693
Enzyme 46 Molecular Weight 189225
Enzyme 46 Theoretical pI Not Available
Enzyme 46 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 46 General Function Not Available
Enzyme 46 Specific Function Not Available
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions
  • H2O + 1-Phosphatidyl-1D-myo-inositol 4-phosphate (Homo sapiens) --> diacylglycerol (homo sapiens) + H+ + 1D-myo-Inositol 1,4-bisphosphate
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 56693592 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID Q4KWH8 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name Q4KWH8_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence Not Available
Enzyme 46 GenBank Gene ID AY691171 Link Image
Enzyme 46 GeneCard ID Not Available
Enzyme 46 GenAtlas ID PLCH1 Link Image
Enzyme 46 HGNC ID HGNC:29185 Link Image
Enzyme 46 Chromosome Location Not Available
Enzyme 46 Locus Not Available
Enzyme 46 SNPs Not Available
Enzyme 46 General References Not Available
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 10049
Enzyme 47 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1
Enzyme 47 Synonyms
  1. Phospholipase C-epsilon-1
  2. PLC-epsilon-1
  3. Phosphoinositide-specific phospholipase C epsilon-1
  4. Pancreas- enriched phospholipase C
Enzyme 47 Gene Name PLCE1
Enzyme 47 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1 
MTSEEMTASVLIPVTQRKVVSAQSAADESSEKVSDINISKAHTVRRSGETSHTISQLNKL
KEEPSGSNLPKILSIAREKIVSDENSNEKCWEKIMPDSAKNLNINCNNILRNHQHGLPQR
QFYEMYNSVAEEDLCLETGIPSPLERKVFPGIQLELDRPSMGISPLGNQSVIIETGRAHP
DSRRAVFHFHYEVDRRMSDTFCTLSENLILDDCGNCVPLPGGEEKQKKNYVAYTCKLMEL
AKNCDNKNEQLQCDHCDTLNDKYFCFEGSCEKVDMVYSGDSFCRKDFTDSQAAKTFLSHF
EDFPDNCDDVEEDAFKSKKERSTLLVRRFCKNDREVKKSVYTGTRAIVRTLPSGHIGLTA
WSYIDQKRNGPLLPCGRVMEPPSTVEIRQDGSQRLSEAQWYPIYNAVRREETENTVGSLL
HFLTKLPASETAHGRISVGPCLKQCVRDTVCEYRATLQRTSISQYITGSLLEATTSLGAR
SGLLSTFGGSTGRMMLKERQPGPSVANSNALPSSSAGISKELIDLQPLIQFPEEVASILM
EQEQTIYRRVLPVDYLCFLTRDLGTPECQSSLPCLKASISASILTTQNGEHNALEDLVMR
FNEVSSWVTWLILTAGSMEEKREVFSYLVHVAKCCWNMGNYNAVMEFLAGLRSRKVLKMW
QFMDQSDIETMRSLKDAMAQHESSCEYRKVVTRALHIPGCKVVPFCGVFLKELCEVLDGA
SGLMKLCPRYNSQEETLEFVADYSGQDNFLQRVGQNGLKNSEKESTVNSIFQVIRSCNRS
LETDEEDSPSEGNSSRKSSLKDKSRWQFIIGDLLDSDNDIFEQSKEYDSHGSEDSQKAFD
HGTELIPWYVLSIQADVHQFLLQGATVIHYDQDTHLSARCFLQLQPDNSTLTWVKPTTAS
PASSKAKLGVLNNTAEPGKFPLLGNAGLSSLTEGVLDLFAVKAVYMGHPGIDIHTVCVQN
KLGSMFLSETGVTLLYGLQTTDNRLLHFVAPKHTAKMLFSGLLELTRAVRKMRKFPDQRQ
QWLRKQYVSLYQEDGRYEGPTLAHAVELFGGRRWSARNPSPGTSAKNAEKPNMQRNNTLG
ISTTKKKKKILMRGESGEVTDDEMATRKAKMHKECRSRSGSDPQDINEQEESEVNAIANP
PNPLPSRRAHSLTTAGSPNLAAGTSSPIRPVSSPVLSSSNKSPSSAWSSSSWHGRIKGGM
KGFQSFMVSDSNMSFVEFVELFKSFSVRSRKDLKDLFDVYAVPCNRSGSESAPLYTNLTI
DENTSDLQPDLDLLTRNVSDLGLFIKSKQQLSDNQRQISDAIAAASIVTNGTGIESTSLG
IFGVGILQLNDFLVNCQGEHCTYDEILSIIQKFEPSISMCHQGLMSFEGFARFLMDKENF
ASKNDESQENIKELQLPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLQGCRSVELDC
WDGDDGMPIIYHGHTLTTKIPFKEVVEAIDRSAFINSDLPIIISIENHCSLPQQRKMAEI
FKTVFGEKLVTKFLFETDFSDDPMLPSPDQLRKKVLLKNKKLKAHQTPVDILKQKAHQLA
SMQVQAYNGGNANPRPANNEEEEDEEDEYDYDYESLSDDNILEDRPENKSCNDKLQFEYN
EEIPKRIKKADNSACNKGKVYDMELGEEFYLDQNKKESRQIAPELSDLVIYCQAVKFPGL
STLNASGSSRGKERKSRKSIFGNNPGRMSPGETASFNKTSGKSSCEGIRQTWEESSSPLN
PTTSLSAIIRTPKCYHISSLNENAAKRLCRRYSQKLTQHTACQLLRTYPAATRIDSSNPN
PLMFWLHGIQLVALNYQTDDLPLHLNAAMFEANGGCGYVLKPPVLWDKNCPMYQKFSPLE
RDLDSMDPAVYSLTIVSGQNVCPSNSMGSPCIEVDVLGMPLDSCHFRTKPIHRNTLNPMW
NEQFLFHVHFEDLVFLRFAVVENNSSAVTAQRIIPLKALKRGYRHLQLRNLHNEVLEISS
LFINSRRMEENSSGNTMSASSMFNTEERKCLQTHRVTVHGVPGPEPFTVFTINGGTKAKQ
LLQQILTNEQDIKPVTTDYFLMEEKYFISKEKNECRKQPFQRAIGPEEEIMQILSSWFPE
EGYMGRIVLKTQQENLEEKNIVQDDKEVILSSEEESFFVQVHDVSPEQPRTVIKAPRVST
AQDVIQQTLCKAKYSYSILSNPNPSDYVLLEEVVKDTTNKKTTTPKSSQRVLLDQECVFQ
AQSKWKGAGKFILKLKEQVQASREDKKKGISFASELKKLTKSTKQPRGLTSPSQLLTSES
IQTKEEKPVGGLSSSDTMDYRQ
Enzyme 47 Number of Residues 2302
Enzyme 47 Molecular Weight 258717
Enzyme 47 Theoretical pI Not Available
Enzyme 47 GO Classification
Function
  • GTPase regulator activity
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • small GTPase regulator activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 47 General Function Not Available
Enzyme 47 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. PLCE1 is a bifunctional enzyme which also regulates small GTPases of the Ras superfamily through its Ras guanine- exchange factor (RasGEF) activity. As an effector of heterotrimeric and small G-protein, it may play a role in cell survival, cell growth, actin organization and T-cell activation
Enzyme 47 Pathways
Enzyme 47 Reactions
  • H2O + 1-Phosphatidyl-1D-myo-inositol 4-phosphate (Homo sapiens) --> diacylglycerol (homo sapiens) + H+ + 1D-myo-Inositol 1,4-bisphosphate
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 10518469 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID Q9P212 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name PLCE1_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence Not Available
Enzyme 47 GenBank Gene ID AF190642 Link Image
Enzyme 47 GeneCard ID Not Available
Enzyme 47 GenAtlas ID PLCE1 Link Image
Enzyme 47 HGNC ID HGNC:17175 Link Image
Enzyme 47 Chromosome Location Not Available
Enzyme 47 Locus Not Available
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. Song C, Hu CD, Masago M, Kariyai K, Yamawaki-Kataoka Y, Shibatohge M, Wu D, Satoh T, Kataoka T: Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras. J Biol Chem. 2001 Jan 26;276(4):2752-7. Epub 2000 Oct 5. [PubMed Link Image]
  2. Lopez I, Mak EC, Ding J, Hamm HE, Lomasney JW: A novel bifunctional phospholipase c that is regulated by Galpha 12 and stimulates the Ras/mitogen-activated protein kinase pathway. J Biol Chem. 2001 Jan 26;276(4):2758-65. Epub 2000 Oct 5. [PubMed Link Image]
  3. Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 10050
Enzyme 48 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
Enzyme 48 Synonyms
  1. Phosphoinositide phospholipase C delta-3
  2. PLC-delta-3
  3. Phospholipase C-delta-3
Enzyme 48 Gene Name PLCD3
Enzyme 48 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3 
MLCGRWRRCRRPPEEPPVAAQVAAQVAAPVALPSPPTPSDGGTKRPGLRALKKMGLTEDE
DVRAMLRGSRLRKIRSRTWHKERLYRLQEDGLSVWFQRRIPRAPSQHIFFVQHIEAVREG
HQSEGLRRFGGAFAPARCLTIAFKGRRKNLDLAAPTAEEAQRWVRGLTKLRARLDAMSQR
ERLDHWIHSYLHRADSNQDSKMSFKEIKSLLRMVNVDMNDMYAYLLFKECDHSNNDRLEG
AEIEEFLRRLLKRPELEEIFHQYSGEDRVLSAPELLEFLEDQGEEGATLARAQQLIQTYE
LNETAKQHELMTLDGFMMYLLSPEGAALDNTHTCVFQDMNQPLAHYFISSSHNTYLTDSQ
IGGPSSTEAYVRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVVQAVRDHAFT
LSPYPVILSLENHCGLEQQAAMARHLCTILGDMLVTQALDSPNPEELPSPEQLKGRVLVK
GKKLPAARSEDGRALSDREEEEEDDEEEEEEVEAAAQRRLAKQISPELSALAVYCHATRL
RTLHPAPNAPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQ
EMWNSGCQLVALNFQTPGYEMDLNAGRFLVNGQCGYVLKPACLRQPDSTFDPEYPGPPRT
TLSIQVLTAQQLPKLNAEKPHSIVDPLVRIEIHGVPADCARQETDYVLNNGFNPRWGQTL
QFQLRAPELALVRFVVEDYDATSPNDFVGQFTLPLSSLKQGYRHIHLLSKDGASLSPATL
FIQIRIQRS
Enzyme 48 Number of Residues 789
Enzyme 48 Molecular Weight 89259
Enzyme 48 Theoretical pI Not Available
Enzyme 48 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 48 General Function Not Available
Enzyme 48 Specific Function Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow
Enzyme 48 Pathways
Enzyme 48 Reactions
  • H2O + 1-Phosphatidyl-1D-myo-inositol 4-phosphate (Homo sapiens) --> diacylglycerol (homo sapiens) + H+ + 1D-myo-Inositol 1,4-bisphosphate
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 18676791 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID Q8N3E9 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name PLCD3_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence Not Available
Enzyme 48 GenBank Gene ID AK074240 Link Image
Enzyme 48 GeneCard ID Not Available
Enzyme 48 GenAtlas ID PLCD3 Link Image
Enzyme 48 HGNC ID HGNC:9061 Link Image
Enzyme 48 Chromosome Location Not Available
Enzyme 48 Locus Not Available
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 12915
Enzyme 49 Name Phospholipid scramblase 2
Enzyme 49 Synonyms
  1. PL scramblase 2
  2. Ca(2+-dependent phospholipid scramblase 2
Enzyme 49 Gene Name PLSCR2
Enzyme 49 Protein Sequence >Phospholipid scramblase 2 
MPAPPPPLNCPPGLEYLSQIDMILIHQQIELLEVLFSFESSNMYEIKNSFGQRIYFAAED
TNFCIRNCCGRSRPFTLRITDNVGREVITLERPLRCNCCCCPCCLQEIEIQAPPGVPVGY
VTQTWHPCLTKFTIKNQKREDVLKISGPCIVCSCIAGVDFEITSLDEQIVVGRISKHWSG
FLREAFTDADNFGIQFPRDLDVKMKAVMIGACFLIDYMFFERTR
Enzyme 49 Number of Residues 224
Enzyme 49 Molecular Weight 25523
Enzyme 49 Theoretical pI 5.34
Enzyme 49 GO Classification Not Available
Enzyme 49 General Function Not Available
Enzyme 49 Specific Function May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions Not Available
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • 204-220
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 9651165 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q9NRY7 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name PLS2_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence Not Available
Enzyme 49 GenBank Gene ID AF159441 Link Image
Enzyme 49 GeneCard ID Q9NRY7 Link Image
Enzyme 49 GenAtlas ID PLSCR2 Link Image
Enzyme 49 HGNC ID HGNC:16494 Link Image
Enzyme 49 Chromosome Location Not Available
Enzyme 49 Locus Not Available
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 12916
Enzyme 50 Name Phospholipid scramblase 3
Enzyme 50 Synonyms
  1. PL scramblase 3
  2. Ca(2+-dependent phospholipid scramblase 3
Enzyme 50 Gene Name PLSCR3
Enzyme 50 Protein Sequence >Phospholipid scramblase 3 
MAGYLPPKGYAPSPPPPYPVTPGYPEPALHPGPGQAPVPAQVPAPAPGFALFPSPGPVAL
GSAAPFLPLPGVPSGLEFLVQIDQILIHQKAERVETFLGWETCNRYELRSGAGQPLGQAA
EESNCCARLCCGARRPLRVRLADPGDREVLRLLRPLHCGCSCCPCGLQEMEVQAPPGTTI
GHVLQTWHPFLPKFSIQDADRQTVLRVVGPCWTCGCGTDTNFEVKTRDESRSVGRISKQW
GGLVREALTDADDFGLQFPLDLDVRVKAVLLGATFLIDYMFFEKRGGAGPSAITS
Enzyme 50 Number of Residues 295
Enzyme 50 Molecular Weight 31663
Enzyme 50 Theoretical pI 6.63
Enzyme 50 GO Classification Not Available
Enzyme 50 General Function Not Available
Enzyme 50 Specific Function May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • 266-282
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 9651167 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID Q9NRY6 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name PLS3_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence Not Available
Enzyme 50 GenBank Gene ID AF159442 Link Image
Enzyme 50 GeneCard ID Q9NRY6 Link Image
Enzyme 50 GenAtlas ID PLSCR3 Link Image
Enzyme 50 HGNC ID HGNC:16495 Link Image
Enzyme 50 Chromosome Location Not Available
Enzyme 50 Locus Not Available
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References
  1. Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed Link Image]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 12917
Enzyme 51 Name Phospholipid scramblase 4
Enzyme 51 Synonyms
  1. PL scramblase 4
  2. Ca(2+-dependent phospholipid scramblase 4
  3. TRA1
  4. Cell growth-inhibiting gene 43 protein
Enzyme 51 Gene Name PLSCR4
Enzyme 51 Protein Sequence >Phospholipid scramblase 4 
MSGVVPTAPEQPAGEMENQTKPPDPRPDAPPEYSSHFLPGPPGTAVPPPTGYPGGLPMGY
YSPQQPSTFPLYQPVGGIHPVRYQPGKYPMPNQSVPITWMPGPTPMANCPPGLEYLVQLD
NIHVLQHFEPLEMMTCFETNNRYDIKNNSDQMVYVVTEDTDDFTRNAYRTLRPFVLRVTD
CMGREIMTMQRPFRCTCCCFCCPSARQELEVQCPPGVTIGFVAEHWNLCRAVYSIQNEKK
ENVMRVRGPCSTYGCGSDSVFEVKSLDGISNIGSIIRKWNGLLSAMADADHFDIHFPLDL
DVKMKAMIFGACFLIDFMYFERSPPQRSR
Enzyme 51 Number of Residues 329
Enzyme 51 Molecular Weight 36965
Enzyme 51 Theoretical pI 5.62
Enzyme 51 GO Classification Not Available
Enzyme 51 General Function Not Available
Enzyme 51 Specific Function May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions Not Available
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • 304-320
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 9622872 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID Q9NRQ2 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name PLS4_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence Not Available
Enzyme 51 GenBank Gene ID