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Human Metabolome Database Version 2.5

 

Showing metabocard for PA(16:0/16:0) (HMDB00674)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-26 12:13:39
Accession Number HMDB00674
Secondary Accession Numbers HMDB07857
Common Name PA(16:0/16:0)
Description PA(16:0/16:0) is a phosphatidic acid. It is a glycerophospholipid in which a phosphate moiety occupies a glycerol substitution site. As is the case with diacylglycerols, phosphatidic acids 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 16, 18 and 20 carbons are the most common. PA(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. Phosphatidic acids are quite rare but are extremely important as intermediates in the biosynthesis of triacylglycerols and phospholipids. Indeed, the concentration of phosphatidic acids is often over-estimated in tissues and biofluids as it can arise by inadvertent enzymatic hydrolysis during inappropriate storage or extraction conditions during analysis. The main biosynthetic route of phosphatidic acid in animal tissues involves sequential acylation of alpha-glycerophosphate by acyl-coA derivatives of fatty acids. PAs are biologically active lipids that can stimulate a large range of responses in many different cell types, such as platelet aggregation, smooth muscle contraction, in vivo vasoactive effects, chemotaxis, expression of adhesion molecules, increased tight junction permeability of endothelial cells, induction of stress fibres, modulation of cardiac contractility, and many others. Diacylglycerols (DAGs) can be converted to PAs by DAG kinases and indirect evidence supports the notion that PAs alter the excitability of neurons. Phospholipase Ds (PLDs), which catalyze the conversion of glycerolphospholipids, particularly phosphatidylcholine, to PAs and the conversion of N-arachidonoyl-phosphatidylethanolamine (NAPE) to anandamide and PAs are activated by several inflammatory mediators including bradykinin, ATP and glutamate. PAs activate downstream signaling pathways such as PKCs and mitogen-activated protein kinases (MAPKs), which are linked to an increase in sensitivity of sensory neurons either during inflammation or in chronic pain models. Circumstantial evidence that PAs are converted to DAGs. (PMID: 12618218, 16185776).
Synonyms
  1. Dipalmitoylphosphatidic acid
  2. 1,2-Di-O-palmitoyl-3-sn-glyceryl-O-phosphorate
  3. 1,2-Di-O-palmitoyl-3-sn-glyceryl-O-phosphoric acid
  4. 1,2-Dipalmitoyl-3-sn-phosphatidate
  5. 1,2-Dipalmitoyl-3-sn-phosphatidic acid
  6. 1,2-Dipalmitoyl-sn-glycerol 3-phosphate
  7. 1,2-Dipalmitoyl-sn-glycerol-3-phosphorate
  8. 1,2-Dipalmitoyl-sn-glycerol-3-phosphoric acid
  9. Dipalmitoyl-L-a-phosphatidate
  10. Dipalmitoyl-L-a-phosphatidic acid
  11. Dipalmitoylphosphatidate
  12. L-a-Dipalmitoyl-phosphatidate
  13. L-a-Dipalmitoyl-phosphatidic acid
  14. L-a-Dipalmitoylphosphatidate
  15. L-a-Dipalmitoylphosphatidic acid
  16. Dipalmitoyl-L-alpha-phosphatidate
  17. Dipalmitoyl-L-alpha-phosphatidic acid
  18. L-alpha-Dipalmitoyl-phosphatidate
  19. L-alpha-Dipalmitoyl-phosphatidic acid
  20. L-alpha-Dipalmitoylphosphatidate
  21. L-alpha-Dipalmitoylphosphatidic acid
  22. PA(32:0)
  23. Phosphatidic acid(16:0/16:0)
  24. Phosphatidic acid(32:0)
  25. 1,2-dihexadecanoyl-rac-phosphatidic acid
Chemical IUPAC Name 1,2-dihexadecanoyl-rac-glycero-3-phosphate
Chemical Formula C35H69O8P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Lipids
Class
  • Phospholipids
Sub Class
  • Phosphatidic Acids
Family
  • Mammalian Metabolite
Species
  • carboxylic acid ester
  • phosphoric acid ester
Biofunction
  • Membrane component
Application
—
Source
  • Endogenous
Average Molecular Weight 648.891
Monoisotopic Molecular Weight 648.473022
Isomeric SMILES CCCCCCCCCCCCCCCC(=O)OC[C@H](COP(O)(O)=O)OC(=O)CCCCCCCCCCCCCCC
Canonical SMILES CCCCCCCCCCCCCCCC(=O)OCC(COP(O)(O)=O)OC(=O)CCCCCCCCCCCCCCC
KEGG Compound ID C00416 Link Image
BioCyc ID L-PHOSPHATIDATE Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB00674 Link Image
Metagene Link HMDB00674 Link Image
METLIN ID 5644 Link Image
PubChem Compound 446066 Link Image
PubChem Substance 10299820 Link Image
ChEBI ID Not Available
CAS Registry Number 7091-44-3
InChI Identifier InChI=1/C35H69O8P/c1-3-5-7-9-11-13-15-17-19-21-23-25-27-29-34(36)41-31-33(32-42-44(38,39)40)43-35(37)30-28-26-24-22-20-18-16-14-12-10-8-6-4-2/h33H,3-32H2,1-2H3,(H2,38,39,40)/t33-/m1/s1
Synthesis Reference Ando, Yoshihiro; Oda, Hiroshi; Matsuyoshi, Shigeru; Maekawa, Naoya. Manufacture of phosphatidic acid alkali metal or ammonium salts using phospholipase D. Jpn. Kokai Tokkyo Koho (2001), 8 pp.
Melting Point (Experimental) 161-165 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.18e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 8.66 [Predicted by ALOGPS]; 10.9 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Glycerolipid Metabolism SMP00039 Link Image map00561 Link Image
Phospholipid Biosynthesis SMP00025 Link Image map00564 Link Image
General References Not Available
Metabolic Enzymes
  1. Phospholipase D2
  2. Diacylglycerol kinase gamma
  3. Lipid phosphate phosphohydrolase 2
  4. Diacylglycerol kinase alpha
  5. Diacylglycerol kinase delta
  6. Lipid phosphate phosphohydrolase 1
  7. Diacylglycerol kinase iota
  8. Lipid phosphate phosphohydrolase 3
  9. Diacylglycerol kinase zeta
  10. Probable phospholipase DDHD1
  11. cAMP-specific 3',5'-cyclic phosphodiesterase 4D
  12. Probable phospholipid-transporting ATPase IG
  13. Probable phospholipid-transporting ATPase IH
  14. Probable phospholipid-transporting ATPase VA
  15. Probable phospholipid-transporting ATPase IC
  16. Probable phospholipid-transporting ATPase IIA
  17. Probable phospholipid-transporting ATPase VD
  18. Probable phospholipid-transporting ATPase IB
  19. Probable phospholipid-transporting ATPase IA
  20. Probable phospholipid-transporting ATPase IM
  21. Probable phospholipid-transporting ATPase IF
  22. Probable phospholipid-transporting ATPase IK
  23. 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
  24. 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
  25. 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
  26. Phosphatidylinositol-glycan-specific phospholipase D precursor
  27. Centaurin-gamma 1
  28. Phospholipid transfer protein precursor
  29. 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
  30. 2-acylglycerol O-acyltransferase 2
  31. Diacylglycerol kinase eta
  32. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
  33. 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
  34. Diacylglycerol kinase kappa
  35. Probable phospholipid-transporting ATPase VB
  36. Probable phospholipid-transporting ATPase ID
  37. N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
  38. Lysocardiolipin acyltransferase
  39. Lipase member H precursor
  40. Lipase member I precursor
  41. Plasticity related gene 1
  42. PAP2 protein
  43. Presqualene diphosphate phosphatase
  44. Probable lipid phosphate phosphatase PPAPDC3
  45. Phosphatidic acid phosphatase type 2 domain-containing protein 1A
  46. Phosphatidic acid phosphatase type 2 domain-containing protein 1B
  47. Centaurin-beta-1
  48. Rab11 family-interacting protein 2
  49. Acylglycerol kinase, mitochondrial precursor
  50. Phospholipase D1 variant (Fragment)
  51. 1-acylglycerol-3-phosphate O-acyltransferase 1 (Lysophosphatidic acid acyltransferase, alpha) (1-acylglycerol-3-phosphate O-acyltransferase 1 (Lysophosphatidic acid acyltransferase, alpha), isoform CRA_b)
  52. Testis spermatogenesis apoptosis-related protein 7 (1-acylglycerol-3- phosphate O-acyltransferase 6 (Lysophosphatidic acid acyltransferase, zeta), isoform CRA_b)
  53. Lysocardiolipin acyltransferase (Uncharacterized protein LYCAT)
  54. Diacylglycerol kinase, beta 90kDa (Diacylglycerol kinase, beta 90kDa, isoform CRA_b)
  55. Diacylglycerol kinase, theta 110kDa
  56. Diacylglycerol kinase, epsilon 64kDa (cDNA FLJ75840, highly similar to Homo sapiens diacylglycerol kinase, epsilon 64kDa (DGKE), mRNA)
  57. cDNA, FLJ94990, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 1 (CDS1), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 1, isoform CRA_a)
  58. cDNA, FLJ96552, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 2 (CDS2), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 2, isoform CRA_a)
  59. cDNA, FLJ92787, highly similar to Homo sapiens phosphatidic acid phosphatase type 2B (PPAP2B), mRNA (Phosphatidic acid phosphatase type 2B, isoform CRA_a)
  60. Centaurin-gamma-2
  61. Phospholipase DDHD2
  62. Oxysterol-binding protein-related protein 2
  63. Oxysterol-binding protein-related protein 1
  64. Centaurin-beta-2
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Enzyme 1 [top]
Enzyme 1 ID 5309
Enzyme 1 Name Phospholipase D2
Enzyme 1 Synonyms
  1. PLD 2
  2. Choline phosphatase 2
  3. Phosphatidylcholine-hydrolyzing phospholipase D2
  4. PLD1C
  5. hPLD2
Enzyme 1 Gene Name PLD2
Enzyme 1 Protein Sequence >Phospholipase D2 
MTATPESLFPTGDELDSSQLQMESDEVDTLKEGEDPADRMHPFLAIYELQSLKVHPLVFA
PGVPVTAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVL
MSLLPLARFAVAYSPARDAGNREMPSLPRAGPEGSTRHAASKQKYLENYLNRLLTMSFYR
NYHAMTEFLEVSQLSFIPDLGRKGLEGMIRKRSGGHRVPGLTCCGRDQVCYRWSKRWLVV
KDSFLLYMCLETGAISFVQLFDPGFEVQVGKRSTEARHGVRIDTSHRSLILKCSSYRQAR
WWAQEITELAQGPGRDFLQLHRHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIF
ITDWWLSPEVYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRAL
MLLHPNIKVMRHPDQVTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDLGDSSE
SAASQPPTPRPDSPATPDLSHNQFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPW
RDVGVVVHGLPARDLARHFIQRWNFTKTTKAKYKTPTYPYLLPKSTSTANQLPFTLPGGQ
CTTVQVLRSVDRWSAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDE
IVDRILKAHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHR
LKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSANINDRSLL
GKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILGANTRPDLDLRDPICD
DFFQLWQDMAESNANIYEQIFRCLPSNATRSLRTLREYVAVEPLATVSPPLARSELTQVQ
GHLVHFPLKFLEDESLLPPLGSKEGMIPLEVWT
Enzyme 1 Number of Residues 933
Enzyme 1 Molecular Weight 105988
Enzyme 1 Theoretical pI 7.68
Enzyme 1 GO Classification
Function
  • catalytic activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • metabolism
  • physiological process
  • signal transduction
Component
—
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 Specific Function May have a role in signal-induced cytoskeletal regulation and/or endocytosis
Enzyme 1 Pathways
Enzyme 1 Reactions
  • A phosphatidylcholine + H2O = choline + a phosphatidate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 2645858 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O14939 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PLD2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2802 bp 
ATGACGGCGACCCCTGAGAGCCTCTTCCCCACTGGGGACGAACTGGACTCCAGCCAGCTC
CAGATGGAGTCCGATGAGGTGGACACCCTGAAGGAGGGAGAGGACCCAGCCGACCGGATG
CACCCGTTTCTGGCCATCTATGAGCTTCAGTCTCTGAAAGTGCACCCCTTGGTGTTCGCA
CCTGGGGTCCCTGTCACAGCCCAGGTGGTGGGCACCGAAAGATATACCAGCGGATCCAAG
GTGGGAACCTGCACTCTGTATTCTGTCCGCTTGACTCACGGCGACTTTTCCTGGACAACC
AAGAAGAAATACCGTCATTTTCAGGAGCTGCATCGGGACCTCCTGAGACACAAAGTCTTG
ATGAGTCTGCTCCCTCTGGCTCGATTTGCCGTTGCCTATTCTCCAGCCCGAGATGCAGGC
AACAGAGAGATGCCCTCTCTACCCCGGGCAGGTCCTGAGGGCTCCACCAGACATGCAGCC
AGCAAACAGAAATACCTGGAGAATTACCTCAACTGTCTCTTGACCATGTCTTTCTATCGC
AACTACCATGCCATGACAGAGTTCCTGGAAGTCAGTCAGCTGTCCTTTATCCCGGACTTG
GGCCGCAAAGGACTGGAGGGGATGATCCGGAAGCGCTCAGGTGGCCACCGTGTTCCTGGC
CTCACCTGCTGTGGCCGAGACCAAGTTTGTTATCGCTGGTCCAAGAGGTGGCTGGTGGTG
AAGGACTCCTTCCTGCTGTACATGTGCCTCGAGACAGGTGCCATCTCATTTGTTCAGCTC
TTTGACCCTGGCTTTGAGGTGCAAGTGGGGAAAAGGAGCACGGAGGCACGGCACGGCGTG
CGGATCGATACCTCCCACAGGTCCTTGATTCTCAAGTGCAGCAGCTACCGGCAGGCACGG
TGGTGGGCCCAAGAGATCACTGAGCTGGCACAGGGCCCAGGCAGAGACTTCCTACAGCTG
CACCGGCATGACAGCTACGCCCCACCCCGGCCTGGGACCTTGGCCCGGTGGTTTGTGAAT
GGGGCAGGTTACTTTGCTGCTGTGGCAGATGCCATCCTTCGAGCTCAAGAGGAGATTTTC
ATCACAGACTGGTGGTTGAGTCCTGAGGTTTACCTGAAGCGTCCGGCCCATTCAGATGAC
TGGAGACTGGACATTATGCTCAAGAGGAAGGCGGAGGAAGGTGTCCGTGTGTCTATTCTG
CTGTTTAAAGAAGTGGAATTGGCCTTGGGCATCAACAGTGGCTATAGCAAGAGGGCGCTG
ATGCTGCTGCACCCCAACATAAAGGTGATGCGTCACCCAGACCAAGTGACGTTGTGGGCC
CATCATGAGAAGCTCCTGGTGGTGGACCAAGTGGTAGCATTCCTGGGGGGACTGGACCTT
GCCTATGGCCGCTGGGATGACCTGCACTACCGACTGACTGACCTTGGAGACTCCTCTGAA
TCAGCTGCCTCCCAGCCTCCCACCCCGCGCCCAGACTCACCAGCCACCCCAGACCTCTCT
CACAACCAATTCTTCTGGCTGGGCAAGGACTACAGCAATCTTATCACCAAGGACTGGGTG
CAGCTGGACCGGCCTTTCGAAGATTTCATTGACAGGGAGACGACCCCTCGGATGCCATGG
CGGGACGTTGGGGTGGTCGTCCATGGCCTACCGGCCCGGGACCTTGCCCGGCACTTCATC
CAGCGCTGGAACTTCACCAAGACCACCAAGGCCAAGTACAAGACTCCCACATACCCCTAC
CTGCTTCCCAAGTCTACCAGCACGGCCAATCAGCTCCCCTTCACACTTCCAGGAGGGCAG
TGCACCACCGTACAGGTCTTGCGATCAGTGGACCGCTGGTCAGCAGGGACTCTGGAGAAC
TCCATCCTCAATGCCTACCTGCACACCATCAGGGAGAGCCAGCACTTCCTCTACATTGAG
AATCAGTTCTTCATTAGCTGCTCAGATGGGCGGACGGTTCTGAACAAGGTGGGCGATGAG
ATTGTGGACAGAATCCTGAAGGCCCACAAACAGGGGTGGTGTTACCGAGTCTACGTGCTT
TTGCCCTTACTCCCTGGCTTCGAGGGTGACATCTCCACGGGCGGTGGCAACTCCATCCAG
GCCATTCTGCACTTTACTTACAGGACCCTGTGTCGTGGGGAGTATTCAATCCTGCATCGC
CTTAAAGCAGCCATGGGGACAGCATGGCGGGACTATATTTCCATCTGCGGGCTTCGTACA
CACGGAGAGCTGGGCGGGCACCCCGTCTCGGAGCTCATCTACATCCACAGCAAGGTGCTC
ATCGCAGATGACCGGACAGTCATCATTGGTTCTGCAAACATCAATGACCGGAGCTTGCTG
GGGAAGCGGGACAGTGAGCTGGCCGTGCTGATCGAGGACACAGAGACGGAACCATCCCTC
ATGAATGGGGCAGAGTATCAGGCGGGCAGGTTTGCCTTGAGTCTGCGGAAGCACTGCTTC
GGTGTGATTCTTGGAGCAAATACCCGGCCAGACTTGGATCTCCGAGACCCCATCTGTGAT
GACTTCTTCCAGTTGTGGCAAGACATGGCTGAGAGCAACGCCAATATCTATGAGCAGATC
TTCCGCTGCCTGCCATCCAATGCCACGCGTTCCCTGCGGACTCTCCGGGAGTACGTGGCC
GTGGAGCCCTTGGCCACGGTCAGTCCCCCCTTGGCTCGGTCTGAGCTCACCCAGGTCCAG
GGCCACCTGGTCCACTTCCCCCTCAAGTTCCTAGAGGATGAGTCTTTGCTGCCCCCGCTG
GGTAGCAAGGAGGGCATGATCCCCCTAGAAGTGTGGACATAG
Enzyme 1 GenBank Gene ID AF033850 Link Image
Enzyme 1 GeneCard ID PLD2 Link Image
Enzyme 1 GenAtlas ID PLD2 Link Image
Enzyme 1 HGNC ID HGNC:9068 Link Image
Enzyme 1 Chromosome Location 17
Enzyme 1 Locus 17p13.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Steed PM, Clark KL, Boyar WC, Lasala DJ: Characterization of human PLD2 and the analysis of PLD isoform splice variants. FASEB J. 1998 Oct;12(13):1309-17. [PubMed Link Image]
  2. Lopez I, Arnold RS, Lambeth JD: Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2. J Biol Chem. 1998 May 22;273(21):12846-52. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5457
Enzyme 2 Name Diacylglycerol kinase gamma
Enzyme 2 Synonyms
  1. Diglyceride kinase gamma
  2. DGK-gamma
  3. DAG kinase gamma
Enzyme 2 Gene Name DGKG
Enzyme 2 Protein Sequence >Diacylglycerol kinase gamma 
MGEERWVSLTPEEFDQLQKYSEYSSKKIKDALTEFNEGGSLKQYDPHEPISYDVFKLFMR
AYLEVDLPQPLSTHLFLAFSQKPRHETSDHPTEGASNSEANSADTNIQNADNATKADEAC
APDTESNMAEKQAPAEDQVAATPLEPPVPRSSSSESPVVYLKDVVCYLSLLETGRPQDKL
EFMFRLYDSDENGLLDQAEMDCIVNQMLHIAQYLEWDPTELRPILKEMLQGMDYDRDGFV
SLQEWVHGGMTTIPLLVLLGMDDSGSKGDGGHAWTMKHFKKPTYCNFCHIMLMGVRKQGL
CCTYCKYTVHERCVSKNIPGCVKTYSKAKRSGEVMQHAWVEGNSSVKCDRCHKSIKCYQS
VTARHCVWCRMTFHRKCELSTLCDGGELRDHILLPTSICPITRDRPGEKSDGCVSAKGEL
VMQYKIIPTPGTHPLLVLVNPKSGGRQGERILRKFHYLLNPKQVFNLDNGGPTPGLNFFR
DTPDFRVLACGGDGTVGWILDCIDKANFAKHPPVAVLPLGTGNDLARCLRWGGGYEGGSL
TKILKDIEQSPLVMLDRWHLEVIPREEVENGDQVPYSIMNNYFSIGVDASIAHRFHVMRE
KHPEKFNSRMKNKLWYFEFGTSETFAATCKKLHDHIELECDGVGVDLSNIFLEGIAILNI
PSMYGGTNLWGENKKNRAVIRESRKGVTDPKELKFCVQDLSDQLLEVVGLEGAMEMGQIY
TGLKSAGRRLAQCASVTIRTNKLLPMQVDGEPWMQPCCTIKITHKNQAPMMMGPPQKSSF
FSLRRKSRSKD
Enzyme 2 Number of Residues 791
Enzyme 2 Molecular Weight 88998
Enzyme 2 Theoretical pI 6.73
Enzyme 2 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • diacylglycerol kinase activity
  • ion binding
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 2 General Function Lipid transport and metabolism
Enzyme 2 Specific Function Reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 516758 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P49619 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name DGKG_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2376 bp 
ATGGGTGAAGAACGGTGGGTCTCCCTCACTCCAGAAGAATTTGACCAACTCCAGAAATAT
TCAGAATATTCCTCCAAGAAGATAAAAGATGCCTTGACTGAATTTAATGAGGGTGGGAGC
CTCAAACAATATGACCCACATGAGCCGATTAGCTATGATGTCTTCAAGCTGTTCATGAGG
GCGTACCTGGAGGTGGACCTTCCCCAGCCACTGAGCACTCACCTCTTCCTGGCCTTCAGC
CAGAAGCCCAGACACGAGACCTCTGACCACCCGACGGAGGGAGCCAGCAACAGTGAGGCC
AACAGCGCAGATACTAATATACAGAATGCAGATAATGCCACCAAAGCAGACGAGGCCTGT
GCCCCTGATACTGAATCAAATATGGCTGAGAAGCAAGCACCAGCTGAAGACCAAGTGGCT
GCGACCCCCCTGGAACCCCCCGTCCCTCGGTCTTCAAGCTCGGAATCCCCAGTGGTGTAC
CTGAAGGATGTTGTGTGCTACCTGTCCCTGCTGGAGACGGGGAGGCCTCAGGATAAGCTG
GAGTTCATGTTTCGCCTCTATGATTCAGATGAGAACGGTCTCCTGGACCAAGCGGAGATG
GATTGCATTGTCAACCAAATGCTGCATATTGCCCAGTACCTGGAGTGGGATCCCACAGAG
CTGAGGCCTATATTGAAGGAGATGCTGCAAGGGATGGACTACGACCGGGACGGCTTTGTG
TCTCTACAGGAATGGGTCCATGGAGGGATGACCACCATCCCATTGCTGGTGCTCCTGGGG
ATGGATGACTCTGGCTCCAAGGGGGATGGGGGGCACGCCTGGACCATGAAGCACTTCAAG
AAACCAACCTACTGCAACTTCTGCCATATCATGCTCATGGGCGTCCGCAAGCAAGGCCTG
TGCTGCACTTACTGTAAATACACTGTCCACGAACGCTGTGTGTCCAAAAACATTCCTGGT
TGTGTCAAAACGTACTCAAAAGCCAAAAGGAGTGGTGAGGTGATGCAGCACGCATGGGTG
GAAGGGAACTCCTCCGTCAAGTGTGACCGGTGCCACAAAAGTATCAAGTGCTACCAGAGT
GTCACCGCGCGGCACTGCGTGTGGTGCCGGATGACGTTTCACCGCAAATGTGAATTATCA
ACGTTGTGTGACGGTGGGGAACTCAGAGACCACATCTTACTGCCCACCTCCATATGCCCC
ATCACCCGGGACAGGCCAGGTGAGAAGTCTGATGGCTGCGTGTCCGCCAAGGGCGAACTT
GTCATGCAGTATAAGATCATCCCCACCCCGGGTACCCACCCCCTGCTGGTCTTGGTGAAC
CCCAAGAGTGGAGGGAGACAAGGAGAAAGAATTCTTCGGAAATTCCACTATCTGCTCAAC
CCCAAACAAGTTTTCAACCTGGACAATGGGGGGCCTACTCCAGGGTTGAACTTTTTCCGT
GATACTCCAGACTTCCGTGTTTTGGCCTGTGGTGGAGATGGGACAGTTGGCTGGATTTTG
GATTGCATTGATAAGGCCAACTTTGCAAAGCATCCACCAGTGGCTGTCCTGCCTCTTGGA
ACAGGAAATGACCTTGCCCGTTGTCTCCGCTGGGGAGGAGGTTATGAAGGGGGCAGCTTG
ACAAAAATCCTGAAAGACATTGAGCAGAGCCCCTTGGTGATGCTGGACCGCTGGCATCTG
GAAGTCATCCCCAGAGAGGAAGTGGAAAACGGGGACCAGGTCCCATACAGCATCATGAAC
AACTATTTCTCCATTGGTGTGGACGCTTCCATTGCACACAGATTCCATGTGATGAGAGAG
AAACATCCTGAAAAATTCAACAGCAGGATGAAGAACAAGCTGTGGTACTTTGAATTTGGC
ACCTCGGAGACTTTTGCAGCGACCTGCAAGAAACTCCACGACCACATTGAGTTGGAGTGT
GATGGGGTTGGGGTGGACCTGAGCAACATCTTCCTGGAAGGCATTGCCATTCTCAACATT
CCCAGCATGTACGGAGGCACCAATCTCTGGGGAGAAAACAAGAAGAACCGGGCTGTGATC
CGGGAAAGCAGGAAGGGTGTCACTGACCCCAAAGAACTGAAATTCTGCGTTCAAGACCTC
AGTGACCAGCTCCTTGAAGTGGTGGGGCTAGAAGGAGCCATGGAGATGGGGCAGATCTAC
ACCGGCCTGAAGAGTGCAGGCAGGAGGCTGGCCCAGTGCGCCTCTGTCACCATCAGGACA
AACAAGCTGCTGCCAATGCAAGTGGATGGAGAACCCTGGATGCAGCCATGTTGCACGATT
AAAATTACTCACAAGAACCAAGCGCCCATGATGATGGGGCCTCCCCAGAAGAGCAGCTTC
TTCTCGTTGAGAAGGAAGAGCCGTTCAAAAGACTAA
Enzyme 2 GenBank Gene ID D26135 Link Image
Enzyme 2 GeneCard ID DGKG Link Image
Enzyme 2 GenAtlas ID DGKG Link Image
Enzyme 2 HGNC ID HGNC:2853 Link Image
Enzyme 2 Chromosome Location 3
Enzyme 2 Locus 3q27.2-q27.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Kai M, Sakane F, Imai S, Wada I, Kanoh H: Molecular cloning of a diacylglycerol kinase isozyme predominantly expressed in human retina with a truncated and inactive enzyme expression in most other human cells. J Biol Chem. 1994 Jul 15;269(28):18492-8. [PubMed Link Image]
  2. Stohr H, Klein J, Gehrig A, Koehler MR, Jurklies B, Kellner U, Leo-Kottler B, Schmid M, Weber BH: Mapping and genomic characterization of the gene encoding diacylglycerol kinase gamma (DAGK3): assessment of its role in dominant optic atrophy (OPA1). Hum Genet. 1999 Jan;104(1):99-105. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5463
Enzyme 3 Name Lipid phosphate phosphohydrolase 2
Enzyme 3 Synonyms
  1. Phosphatidic acid phosphatase 2c
  2. Phosphatidate phosphohydrolase type 2c
  3. PAP2c
  4. PAP- 2c
  5. PAP2-gamma
  6. PAP2-G
Enzyme 3 Gene Name PPAP2C
Enzyme 3 Protein Sequence >Lipid phosphate phosphohydrolase 2 
MQRRWVFVLLDVLCLLVASLPFAILTLVNAPYKRGFYCGDDSIRYPYRPDTITHGLMAGV
TITATVILVSAGEAYLVYTDRLYSRSDFNNYVAAVYKVLGTFLFGAAVSQSLTDLAKYMI
GRLRPNFLAVCDPDWSRVNCSVYVQLEKVCRGNPADVTEARLSFYSGHSSFGMYCMVFLA
LYVQARLCWKWARLLRPTVQFFLVAFALYVGYTRVSDYKHHWSDVLVGLLQGALVAALTV
CYISDFFKARPPQHCLKEEELERKPSLSLTLTLGEADHNHYGYPHSSS
Enzyme 3 Number of Residues 288
Enzyme 3 Molecular Weight 32574
Enzyme 3 Theoretical pI 8.44
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1- phosphate (S-1-P). The relative catalytic efficiency is PA > C-1-P > LPA > S-1-P
Enzyme 3 Pathways
Enzyme 3 Reactions
  • A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-30
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 3123896 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O43688 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name LPP2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >867 bp 
ATGCAGCGGAGGTGGGTCTTCGTGCTGCTCGACGTGCTGTGCTTACTGGTCGCCTCCCTG
CCCTTCGCTATCCTGACGCTGGTGAACGCCCCGTACAAGCGAGGATTTTACTGCGGGGAT
GACTCCATCCGGTACCCCTACCGTCCAGATACCATCACCCACGGGCTCATGGCTGGGGTC
ACCATCACGGCCACCGTCATCCTTGTCTCGGCCGGGGAAGCCTACCTGGTGTACACAGAC
CGGCTCTATTCTCGCTCGGACTTCAACAACTACGTGGCTGCTGTATACAAGGTGCTGGGG
ACCTTCCTGTTTGGGGCTGCCGTGAGCCAGTCTCTGACAGACCTGGCCAAGTACATGATT
GGGCGTCTGAGGCCCAACTTCCTAGCCGTCTGCGACCCCGACTGGAGCCGGGTCAACTGC
TCGGTCTATGTGCAGCTGGAGAAGGTGTGCAGGGGAAACCCTGCTGATGTCACCGAGGCC
AGGTTGTCTTTCTACTCGGGACACTCTTCCTTTGGGATGTACTGCATGGTGTTCTTGGCG
CTGTATGTGCAGGCACGACTCTGTTGGAAGTGGGCACGGCTGCTGCGACCCACAGTCCAG
TTCTTCCTGGTGGCCTTTGCCCTCTACGTGGGCTACACCCGCGTGTCTGATTACAAACAC
CACTGGAGCGATGTCCTTGTTGGCCTCCTGCAGGGGGCACTGGTGGCTGCCCTCACTGTC
TGCTACATCTCAGACTTCTTCAAAGCCCGACCCCCACAGCACTGTCTGAAGGAGGAGGAG
CTGGAACGGAAGCCCAGCCTGTCACTGACGTTGACCCTGGGCGAGGCTGACCACAACCAC
TATGGATACCCGCACTCCTCCTCCTGA
Enzyme 3 GenBank Gene ID AF035959 Link Image
Enzyme 3 GeneCard ID PPAP2C Link Image
Enzyme 3 GenAtlas ID PPAP2C Link Image
Enzyme 3 HGNC ID HGNC:9230 Link Image
Enzyme 3 Chromosome Location 19
Enzyme 3 Locus 19p13
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Leung DW, Tompkins CK, White T: Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. DNA Cell Biol. 1998 Apr;17(4):377-85. [PubMed Link Image]
  2. Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5465
Enzyme 4 Name Diacylglycerol kinase alpha
Enzyme 4 Synonyms
  1. Diglyceride kinase alpha
  2. DGK-alpha
  3. DAG kinase alpha
  4. 80 kDa diacylglycerol kinase
Enzyme 4 Gene Name DGKA
Enzyme 4 Protein Sequence >Diacylglycerol kinase alpha 
MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIY
LEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFK
LYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEW
VRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKY
TVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHC
VWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNL
STSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRL
FKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQ
NLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIM
REKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVL
NIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLE
GAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDVEPWMQTPCTIKITHKNQMPML
MGPPPRSTNFFGFLS
Enzyme 4 Number of Residues 735
Enzyme 4 Molecular Weight 82673
Enzyme 4 Theoretical pI 6.71
Enzyme 4 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • diacylglycerol kinase activity
  • ion binding
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 30823 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P23743 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name DGKA_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2208 bp 
ATGGCCAAGGAGAGGGGCCTAATAAGCCCCAGTGATTTTGCCCAGCTGCAAAAATACATG
GAATACTCCACCAAAAAGGTCAGTGATGTCCTAAAGCTCTTCGAGGATGGCGAGATGGCT
AAATATGTCCAAGGAGATGCCATTGGGTACGAGGGATTCCAGCAATTCCTGAAAATCTAT
CTCGAAGTGGATAATGTTCCCAGACACCTAAGCCTGGCACTGTTTCAATCCTTTGAGACT
GGTCACTGCTTAAATGAGACAAATGTGACAAAAGATGTGGTGTGTCTCAATGATGTTTCC
TGCTACTTTTCCCTTCTGGAGGGTGGTCGGCCAGAAGACAAGTTAGAATTCACCTTCAAG
CTGTACGACACGGACAGAAATGGGATCCTGGACAGCTCAGAAGTGGACAAAATTATCCTA
CAGATGATGCGAGTGGCTGAATACCTGGATTGGGATGTGTCTGAGCTGAGGCCGATTCTT
CAGGAGATGATGAAAGAGATTGACTATGATGGCAGTGGCTCTGTCTCTCAAGCTGAGTGG
GTCCGGGCTGGGGCCACCACCGTGCCACTGCTAGTGCTGCTGGGTCTGGAGATGACTCTG
AAGGACGACGGACAGCACATGTGGAGGCCCAAGAGGTTCCCCAGACCAGTCTACTGCAAT
CTGTGCGAGTCAAGCATTGGTCTTGGCAAACAGGGACTGAGCTGTAACCTCTGTAAGTAC
ACTGTTCACGACCAGTGTGCCATGAAAGCCCTGCCTTGTGAAGTCAGCACCTATGCCAAG
TCTCGGAAGGACATTGGTGTCCAATCACATGTGTGGGTGCGAGGAGGCTGTGAGTCCGGG
CGCTGCGACCGCTGTCAGAAAAAGATCCGGATCTACCACAGTCTGACCGGGCTGCATTGT
GTATGGTGCCACCTAGAGATCCACGATGACTGCCTGCAAGCGGTGGGCCATGAGTGTGAC
TGTGGGCTGCTCCGGGATCACATCCTGCCTCCATCTTCCATCTATCCCAGTGTCCTGGCC
TCTGGACCGGATCGTAAAAATAGCAAAACAAGCCAGAAGACCATGGATGATTTAAATTTG
AGCACCTCTGAGGCTCTGCGGATTGACCCTGTTCCTAACACCCACCCACTTCTCGTCTTT
GTCAATCCTAAGAGTGGCGGGAAGCAGGGGCAGAGGGTGCTCTGGAAGTTCCAGTATATA
TTAAACCCTCGACAGGTGTTCAACCTCCTAAAGGATGGTCCTGAGATAGGGCTCCGATTA
TTCAAGGATGTTCCTGATAGCCGGATTTTGGTGTGTGGTGGAGACGGCACAGTAGGCTGG
ATTCTAGAGACCATTGACAAAGCTAACTTGCCAGTTTTGCCTCCTGTTGCTGTGTTGCCC
CTGGGTACTGGAAATGATCTGGCTCGATGCCTAAGATGGGGAGGAGGTTATGAAGGACAG
AATCTGGCAAAGATCCTCAAGGATTTAGAGATGAGTAAAGTGGTACATATGGATCGATGG
TCTGTGGAGGTGATACCTCAACAAACTGAAGAAAAAAGTGACCCAGTCCCCTTTCAAATC
ATCAATAACTACTTCTCTATTGGCGTGGATGCCTCTATTGCTCATCGATTCCACATCATG
CGAGAGAAATATCCGGAGAAGTTCAACAGCAGAATGAAGAACAAGCTATGGTACTTCGAA
TTTGCCACATCTGAATCCATCTTCTCAACATGCAAAAAGCTGGAGGAGTCTTTGACAGTT
GAGATCTGTGGGAAACCGCTGGATCTGAGCAACCTGTCCCTAGAAGGCATCGCAGTGCTA
AACATCCCTAGCATGCATGGTGGCTCCAACCTCTGGGGTGATACCAGGAGACCCCATGGG
GATATCTATGGGATCAACCAGGCCTTAGGTGCTACAGCTAAAGTCATCACCGACCCTGAT
ATCCTGAAAACCTGTGTACCAGACCTAAGTGACAAGAGACTGGAAGTGGTTGGGCTGGAG
GGTGCAATTGAGATGGGCCAAATCTATACCAAGCTCAAGAATGCTGGACGTCGGCTGGCC
AAGTGCTCTGAGATCACCTTCCACACCACAAAAACCCTTCCCATGCAAATTGACGTAGAA
CCCTGGATGCAGACGCCCTGTACAATCAAGATCACCCACAAGAACCAGATGCCCATGCTC
ATGGGCCCACCCCCCCGCTCCACCAATTTCTTTGGCTTCTTGAGCTAA
Enzyme 4 GenBank Gene ID X62535 Link Image
Enzyme 4 GeneCard ID DGKA Link Image
Enzyme 4 GenAtlas ID DGKA Link Image
Enzyme 4 HGNC ID HGNC:2849 Link Image
Enzyme 4 Chromosome Location 12
Enzyme 4 Locus 12q13.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Schaap D, de Widt J, van der Wal J, Vandekerckhove J, van Damme J, Gussow D, Ploegh HL, van Blitterswijk WJ, van der Bend RL: Purification, cDNA-cloning and expression of human diacylglycerol kinase. FEBS Lett. 1990 Nov 26;275(1-2):151-8. [PubMed Link Image]
  2. Hart TC, Champagne C, Zhou J, Van Dyke TE: Assignment of the gene for diacylglycerol kinase (DAGK) to human chromosome 12. Mamm Genome. 1994 Feb;5(2):123-4. [PubMed Link Image]
  3. Hart TC, Zhou J, Champagne C, Van Dyke TE, Rao PN, Pettenati MJ: Assignment of the human diacylglycerol kinase gene (DAGK) to 12q13.3 using fluorescence in situ hybridization analysis. Genomics. 1994 Jul 1;22(1):246-7. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5466
Enzyme 5 Name Diacylglycerol kinase delta
Enzyme 5 Synonyms
  1. Diglyceride kinase delta
  2. DGK-delta
  3. DAG kinase delta
  4. 130 kDa diacylglycerol kinase
Enzyme 5 Gene Name DGKD
Enzyme 5 Protein Sequence >Diacylglycerol kinase delta 
MAAAAGAPPPGPPQPPPPPPPEESSDSEPEAEPGSPQKLIRKVSTSGQIRQKTIIKEGML
TKQNNSFQRSKRRYFKLRGRTLYYAKTAKSIIFDEVDLTDASVAESSTKNVNNSFTVITP
CRKLILCADNRKEMEDWIAALKTVQNREHFEPTQYSMDHFSGMHNWYACSHARPTYCNVC
REALSGVTSHGLSCEVCKFKAHKRCAVRATNNCKWTTLASIGKDIIEDADGIAMPHQWLE
GNLPVSAKCTVCDKTCGSVLRLQDWRCLWCKAMVHTSCKESLLTKCPLGLCKVSVIPPTA
LNSIDSDGFWKASCPPSCTSPLLVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPH
LGLRLFQKFDTFRILVCGGDGSVGWVLSEIDSLNLHKQCQLGVLPLGTGNDLARVLGWGS
ACDDDTQLPQILEKLERASTKMLDRWSVMAYEAKLPRQASSSTVTEDFSEDSEVQQILFY
EDSVAAHLSKILTSDQHSVVISSAKVLCETVKDFVARVGKAYEKTTESSEESEVMAKKCS
VLKEKLDSLLKTLDDESQASSSLPNPPPTIAEEAEDGDGSGSICGSTGDRLVASACPARP
QIFRPREQLMLRANSLKKAIRQIIEHTEKAVDEQNAQTQEQEGFVLGLSESEEKMDHRVC
PPLSHSESFGVPKGRSQRKVSKSPCEKLISKGSLSLGSSASLPPQPGSRDGLPALNTKIL
YPNVRAGMSGSLPGGSVISRLLINADPFNSEPETLEYYTEKCVMNNYFGIGLDAKISLDF
NNKRDEHPEKCRSRTKNMMWYGVLGTKELLHRTYKNLEQKVLLECDGRPIPLPSLQGIAV
LNIPSYAGGTNFWGGTKEDDTFAAPSFDDKILEVVAVFGSMQMAVSRVIRLQHHRIAQCR
TVKISILGDEGVPVQVDGEAWVQPPGYIRIVHKNRAQTLTRDRAFESTLKSWEDKQKCEL
PRPPSCSLHPEMLSEEEATQMDQFGQAAGVLIHSIREIAQSHRDMEQELAHAVNASSKSM
DRVYGKPRTTEGLNCSFVLEMVNNFRALRSETELLLSGKMALQLDPPQKEQLGSALAEMD
RQLRRLADTPWLCQSAEPGDEESVMLDLAKRSRSGKFRLVTKFKKEKNNKNKEAHSSLGA
PVHLWGTEEVAAWLEHLSLCEYKDIFTRHDIRGSELLHLERRDLKDLGVTKVGHMKRILC
GIKELSRSAPAVEA
Enzyme 5 Number of Residues 1214
Enzyme 5 Molecular Weight 134527
Enzyme 5 Theoretical pI 7.58
Enzyme 5 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function May function as signaling molecule. Isoform 2 may be involved in cell growth and tumorigenesis
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 22773821 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q16760 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name DGKD_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >3645 bp 
ATGGCGGCGGCGGCGGGCGCCCCTCCGCCGGGTCCCCCGCAACCGCCTCCGCCGCCGCCG
CCCGAGGAGTCGTCCGACAGCGAGCCCGAGGCGGAGCCCGGCTCCCCACAGAAGCTCATC
CGCAAGGTGTCCACGTCGGGTCAGATCCGACAGAAGACCATCATCAAAGAGGGGATGCTG
ACCAAACAGAACAATTCATTCCAGCGATCAAAAAGGAGATACTTTAAGCTTCGAGGGCGA
ACGCTTTACTATGCCAAAACGGCAAAGTCAATCATATTTGATGAGGTGGATCTGACAGAT
GCCAGCGTAGCTGAATCCAGTACCAAAAACGTCAACAACAGTTTTACGGTCATAACTCCA
TGCAGGAAGCTCATCTTGTGTGCTGATAACAGAAAAGAAATGGAAGATTGGATTGCAGCA
TTAAAGACTGTGCAGAACAGGGAGCACTTTGAGCCCACCCAGTACAGCATGGACCACTTC
TCAGGGATGCACAATTGGTACGCCTGTTCCCACGCGAGGCCGACCTACTGCAATGTGTGC
CGTGAGGCTCTGTCTGGGGTCACGTCGCACGGGCTGTCCTGCGAGGTGTGCAAATTTAAG
GCCCACAAGCGCTGTGCTGTGCGTGCAACCAATAACTGCAAGTGGACCACACTGGCCTCG
ATCGGGAAGGACATCATTGAAGATGCAGATGGGATTGCAATGCCCCACCAGTGGTTGGAA
GGAAACCTACCTGTGAGCGCCAAGTGCACTGTGTGCGACAAGACCTGTGGCAGTGTGCTG
CGCCTGCAGGACTGGCGCTGCCTCTGGTGCAAGGCCATGGTTCACACATCGTGTAAAGAA
TCCTTGCTGACCAAGTGCCCACTTGGCCTGTGCAAAGTGTCAGTCATCCCACCCACGGCT
CTCAACAGCATCGACTCCGATGGGTTCTGGAAGGCCAGCTGTCCTCCTTCTTGCACAAGC
CCACTGTTGGTCTTCGTCAATTCAAAAAGTGGGGACAACCAGGGTGTGAAGTTCCTCAGA
AGATTCAAACAGCTACTAAACCCCGCCCAGGTCTTCGACCTCATGAACGGAGGCCCACAC
CTCGGCTTACGGTTATTCCAGAAGTTTGACACATTCCGGATTCTGGTTTGTGGCGGGGAT
GGAAGTGTTGGCTGGGTCCTCTCCGAAATCGACAGCCTCAACCTTCATAAACAGTGTCAG
CTGGGAGTGCTGCCGCTCGGCACAGGGAACGACTTGGCCCGAGTACTGGGCTGGGGCTCA
GCCTGCGATGACGACACCCAGCTCCCCCAGATCTTGGAGAAGTTGGAGAGAGCCAGCACC
AAGATGCTGGACAGGTGGAGCGTCATGGCATACGAGGCCAAGCTCCCCCGGCAGGCCTCC
TCCTCTACCGTCACCGAAGACTTCAGCGAGGATTCCGAGGTACAGCAGATTCTCTTCTAT
GAAGACTCGGTTGCAGCCCACCTTTCTAAAATCCTCACCTCGGACCAGCACTCGGTGGTC
ATCTCCTCGGCCAAAGTGCTCTGTGAGACGGTGAAGGACTTCGTGGCACGGGTGGGGAAG
GCCTATGAGAAGACGACCGAGAGCTCGGAGGAGTCAGAGGTCATGGCCAAGAAGTGCTCT
GTCCTGAAAGAGAAGCTGGATTCCCTTCTCAAGACCTTGGACGATGAGTCCCAGGCCTCG
TCCTCTCTGCCCAACCCGCCCCCCACCATTGCCGAGGAGGCTGAAGATGGAGATGGGTCG
GGCAGCATCTGCGGTTCCACCGGAGACCGCTTGGTGGCATCAGCTTGCCCGGCCCGGCCG
CAGATATTCCGGCCTCGAGAACAGCTCATGCTGAGAGCCAACAGCCTGAAGAAAGCAATT
CGTCAGATCATAGAACACACAGAAAAAGCTGTCGATGAGCAGAATGCCCAGACCCAGGAG
CAGGAGGGCTTCGTCCTGGGCCTCTCTGAGTCAGAGGAGAAGATGGACCACAGAGTGTGC
CCACCACTGTCCCACAGCGAGAGCTTCGGGGTCCCCAAGGGGAGGAGCCAGCGCAAAGTG
TCGAAATCTCCGTGTGAAAAGCTGATCAGCAAAGGGAGTCTGTCCCTAGGCAGTTCTGCT
TCCCTTCCGCCCCAGCCGGGAAGCCGGGACGGCCTGCCTGCGCTCAACACCAAGATCCTG
TACCCAAATGTCCGGGCTGGAATGTCTGGTTCCTTACCCGGTGGCTCAGTCATCAGTCGC
CTGTTAATTAATGCTGATCCCTTCAACTCTGAACCAGAAACCCTAGAGTATTACACGGAG
AAATGTGTCATGAACAACTATTTTGGCATTGGCCTGGATGCGAAGATATCCCTGGACTTT
AACAACAAGCGCGATGAGCACCCAGAGAAGTGCAGGAGCCGAACCAAGAACATGATGTGG
TATGGAGTTCTTGGAACCAAAGAGTTGCTGCACAGAACCTACAAGAACCTGGAGCAAAAG
GTCTTGCTGGAGTGTGACGGGCGACCCATCCCACTCCCCAGTCTTCAGGGAATTGCTGTC
CTTAACATTCCCAGCTATGCCGGAGGAACCAACTTCTGGGGGGGTACCAAGGAAGATGAT
ACTTTCGCAGCTCCATCATTCGATGACAAGATTCTGGAGGTGGTCGCCGTGTTCGGCAGC
ATGCAGATGGCCGTCTCTCGAGTCATCAGGCTACAGCATCATCGGATCGCCCAGTGTCGC
ACGGTGAAGATCTCCATCCTTGGGGATGAGGGCGTGCCTGTGCAGGTGGACGGAGAGGCC
TGGGTCCAGCCGCCAGGGTACATTCGGATTGTCCACAAGAACCGGGCACAGACACTGACC
AGAGACAGGGCATTTGAGAGCACCCTGAAGTCCTGGGAAGACAAGCAGAAGTGCGAGGTG
CCCCGCCCTCCATCCTGTTCCCTGCACCCGGAGATGCTGTCCGAGGAGGAGGCCACCCAG
ATGGACCAGTTTGGGCAGGCAGCAGGGGTCCTCATTCACAGTATCCGAGAAATAGCTCAG
TCTCACCGGGACATGGAGCAGGAACTGGCCCACGCCGTCAATGCCAGCTCCAAGTCCATG
GACCGTGTGTATGGCAAGCCCAGAACCACAGAGGGGCTCAACTGCAGCTTCGTCCTGGAA
ATGGTGAATAACTTCAGAGCTCTGCGCAGTGAGACGGAGCTGCTGCTGTCTGGGAAGATG
GCCCTGCAGCTGGATCCGCCTCAGAAGGAGCAGCTGGGGAGTGCTCTTGCCGAGATGGAC
CGACAGCTCAGGAGGCTGGCAGACACCCCGTGGCTCTGCCAGTCCGCAGAGCCCGGCGAC
GAAGAGAGTGTGATGCTGGATCTTGCCAAGCGCAGTCGCAGTGGTAAATTCCGCCTCGTG
ACCAAGTTTAAAAAGGAGAAAAACAACAAGAACAAAGAAGCTCACAGTAGCCTGGGAGCC
CCGGTTCACCTCTGGGGGACAGAGGAGGTTGCTGCCTGGCTGGAGCACCTCAGTCTCTGT
GAGTATAAGGACATCTTCACACGGCACGACATCCGGGGCTCTGAGCTCCTGCACCTGGAG
CGGAGGGACCTCAAGGACCTGGGCGTGACCAAGGTGGGCCACATGAAGAGGATCCTGTGT
GGCATCAAGGAGCTGAGCCGCAGCGCCCCCGCCGTCGAGGCCTAG
Enzyme 5 GenBank Gene ID AB078966 Link Image
Enzyme 5 GeneCard ID DGKD Link Image
Enzyme 5 GenAtlas ID DGKD Link Image
Enzyme 5 HGNC ID HGNC:2851 Link Image
Enzyme 5 Chromosome Location 2
Enzyme 5 Locus 2q37.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Sakane F, Imai S, Yamada K, Murakami T, Tsushima S, Kanoh H: Alternative splicing of the human diacylglycerol kinase delta gene generates two isoforms differing in their expression patterns and in regulatory functions. J Biol Chem. 2002 Nov 8;277(45):43519-26. Epub 2002 Aug 27. [PubMed Link Image]
  2. Nagase T, Seki N, Tanaka A, Ishikawa K, Nomura N: Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995 Aug 31;2(4):167-74, 199-210. [PubMed Link Image]
  3. Sakane F, Imai S, Kai M, Wada I, Kanoh H: Molecular cloning of a novel diacylglycerol kinase isozyme with a pleckstrin homology domain and a C-terminal tail similar to those of the EPH family of protein-tyrosine kinases. J Biol Chem. 1996 Apr 5;271(14):8394-401. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5469
Enzyme 6 Name Lipid phosphate phosphohydrolase 1
Enzyme 6 Synonyms
  1. Phosphatidic acid phosphatase 2a
  2. Phosphatidate phosphohydrolase type 2a
  3. PAP2a
  4. PAP- 2a
  5. PAP2-alpha
Enzyme 6 Gene Name PPAP2A
Enzyme 6 Protein Sequence >Lipid phosphate phosphohydrolase 1 
MFDKTRLPYVALDVLCVLLAGLPFAILTSRHTPFQRGVFCNDESIKYPYKEDTIPYALLG
GIIIPFSIIVIILGETLSVYCNLLHSNSFIRNNYIATIYKAIGTFLFGAAASQSLTDIAK
YSIGRLRPHFLDVCDPDWSKINCSDGYIEYYICRGNAERVKEGRLSFYSGHSSFSMYCML
FVALYLQARMKGDWARLLRPTLQFGLVAVSIYVGLSRVSDYKHHWSDVLTGLIQGALVAI
LVAVYVSDFFKERTSFKERKEEDSHTTLHETPTTGNHYPSNHQP
Enzyme 6 Number of Residues 284
Enzyme 6 Molecular Weight 32156
Enzyme 6 Theoretical pI 8.06
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Lipid transport and metabolism
Enzyme 6 Specific Function Broad-specificity phosphohydrolase that dephosphorylates exogenous bioactive glycerolipids and sphingolipids. Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). Pivotal regulator of lysophosphatidic acid (LPA) signaling in the cardiovascular system. Major enzyme responsible of dephosphorylating LPA in platelets, which terminates signaling actions of LPA. May control circulating, and possibly also regulate localized, LPA levels resulting from platelet activation. It has little activity towards ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA > PA > S-1-P > C-1-P. It's down-regulation may contribute to the development of colon adenocarcinoma
Enzyme 6 Pathways
Enzyme 6 Reactions
  • A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-27
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 2467298 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID O14494 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name LPP1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >855 bp 
ATGTTCGACAAGACGCGGCTGCCGTACGTGGCCCTCGATGTGCTCTGCGTGTTGCTGGCT
GGATTGCCTTTTGCAATTCTTACTTCAAGGCATACCCCCTTCCAACGAGGAGTATTCTGT
AATGATGAGTCCATCAAGTACCCTTACAAAGAAGACACCATACCTTATGCGTTATTAGGT
GGAATAATCATTCCATTCAGTATTATCGTTATTATTCTTGGAGAAACCCTGTCTGTTTAC
TGTAACCTTTTGCACTCAAATTCCTTTATCAGGAATAACTACATAGCCACTATTTACAAA
GCCATTGGAACCTTTTTATTTGGTGCAGCTGCTAGTCAGTCCCTGACTGACATTGCCAAG
TATTCAATAGGCAGACTGCGGCCTCACTTCTTGGATGTTTGTGATCCAGATTGGTCAAAA
ATCAACTGCAGCGATGGTTACATTGAATACTACATATGTCGAGGGAATGCAGAAAGAGTT
AAGGAAGGCAGGTTGTCCTTCTATTCAGGCCACTCTTCGTTTTCCATGTACTGCATGCTG
TTTGTGGCACTTTATCTTCAAGCCAGGATGAAGGGAGACTGGGCAAGACTCTTACGCCCC
ACACTGCAATTTGGTCTTGTTGCCGTATCCATTTATGTGGGCCTTTCTCGAGTTTCTGAT
TATAAACACCACTGGAGCGATGTGTTGACTGGACTCATTCAGGGAGCTCTGGTTGCAATA
TTAGTTGCTGTATATGTATCGGATTTCTTCAAAGAAAGAACTTCTTTTAAAGAAAGAAAA
GAGGAGGACTCTCATACAACTCTGCATGAAACACCAACAACTGGGAATCACTATCCGAGC
AATCACCAGCCTTGA
Enzyme 6 GenBank Gene ID AB000888 Link Image
Enzyme 6 GeneCard ID PPAP2A Link Image
Enzyme 6 GenAtlas ID PPAP2A Link Image
Enzyme 6 HGNC ID HGNC:9228 Link Image
Enzyme 6 Chromosome Location 5
Enzyme 6 Locus 5q11
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Kai M, Wada I, Imai S, Sakane F, Kanoh H: Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. J Biol Chem. 1997 Sep 26;272(39):24572-8. [PubMed Link Image]
  2. Leung DW, Tompkins CK, White T: Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. DNA Cell Biol. 1998 Apr;17(4):377-85. [PubMed Link Image]
  3. Ulrix W, Swinnen JV, Heyns W, Verhoeven G: Identification of the phosphatidic acid phosphatase type 2a isozyme as an androgen-regulated gene in the human prostatic adenocarcinoma cell line LNCaP. J Biol Chem. 1998 Feb 20;273(8):4660-5. [PubMed Link Image]
  4. Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5472
Enzyme 7 Name Diacylglycerol kinase iota
Enzyme 7 Synonyms
  1. Diglyceride kinase iota
  2. DGK-iota
  3. DAG kinase iota
Enzyme 7 Gene Name DGKI
Enzyme 7 Protein Sequence >Diacylglycerol kinase iota 
MDAAGRGCHLLPLPAARGPARAPAAAAAAAASPPGPCSGAACAPSAAAGAGAMNPSSSAG
EEKGATGGSSSSGSGAGSCCLGAEGGADPRGAGSAAAAGAAALDEPAAAGQKEKDEALEE
KLRNLTFRKQVSYRKAISRAGLQHLAPAHPLSLPVANGPAKEPRATLDWSENAVNGEHLW
LETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG
SRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCF
MLHHIEEPCSLGAHAAVIVPPTWIIKVKKPQNSLKASNRKKKRTSFKRKASKRGMEQENK
GRPFVIKPISSPLMKPLLVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEL
YRKVPNLRILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLARTLNWGGGYTDE
PVSKILCQVEDGTVVQLDRWNLHVERNPDLPPEELEDGVCKLPLNVFNNYFSLGFDAHVT
LEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIQEL
KFQCIVFLNIPRYCAGTMPWGNPGDHHDFEPQRHDDGYIEVIGFTMASLAALQVGGHGER
LHQCREVMLLTYKSIPMQVDGEPCRLAPAMIRISLRNQANMVQKSKRRTSMPLLNDPQSV
PDRLRIRVNKISLQDYEGFHYDKEKLREASISDWLRTIAGELVQSFGAIPLGILVVRGDC
DLETCRMYIDRLQEDLQSVSSGSQRVHYQDHETSFPRALSAQRLSPRWCFLDDRSQEHLH
FVMEISQDEIFILDPDMVVSQPAGTPPGMPDLVVEQASGISDWWNPALRKRMLSDSGLGM
IAPYYEDSDLKDLSHSRVLQSPVSSEDHAILQAVIAGDLMKLIESYKNGGSLLIQGPDHC
SLLHYAAKTGNGEIVKYILDHGPSELLDMADSETGETALHKAACQRNRAVCQLLVDAGAS
LRKTDSKGKTPQERAQQAGDPDLAAYLESRQNYKVIGHEDLETAV
Enzyme 7 Number of Residues 1065
Enzyme 7 Molecular Weight 116998
Enzyme 7 Theoretical pI 7.81
Enzyme 7 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl- sn-glycerol 3-phosphate
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 3676530 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID O75912 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name DGKI_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >3198 bp 
ATGGATGCTGCGGGAAGGGGCTGCCATTTGCTGCCCCTGCCAGCGGCGCGCGGACCTGCC
CGCGCTCCTGCAGCCGCCGCCGCCGCCGCCGCCAGCCCGCCCGGCCCCTGCAGCGGCGCC
GCCTGCGCTCCCTCCGCGGCCGCCGGAGCGGGCGCCATGAACCCCAGCTCCTCGGCGGGA
GAGGAGAAAGGGGCGACGGGCGGCAGCAGCAGCAGCGGAAGCGGCGCCGGGAGCTGCTGC
CTGGGCGCCGAGGGCGGCGCGGACCCGCGGGGCGCAGGGTCAGCCGCGGCGGCGGGGGCC
GCTGCCCTGGACGAGCCCGCGGCCGCCGGCCAGAAGGAGAAGGACGAAGCGCTGGAGGAG
AAGCTGAGGAACTTAACTTTCCGGAAGCAGGTCTCGTACAGGAAAGCAATCTCCCGGGCA
GGCCTCCAGCATCTGGCTCCTGCACATCCCCTCAGCCTTCCTGTGGCAAATGGTCCAGCC
AAGGAGCCCAGAGCGACTTTGGACTGGAGTGAGAATGCCGTGAATGGAGAACACCTGTGG
CTGGAGACCAACGTCTCGGGAGACCTCTGCTACCTTGGAGAGGAGAACTGCCAAGTCAGA
TTTGCAAAATCAGCTCTCAGGAGGAAGTGTGCAGTCTGTAAAATCGTCGTCCACACCGCC
TGCATTGAGCAGCTAGAAAAGATTAATTTCAGATGTAAACCAACATTTCGAGAAGGAGGC
TCAAGGTCACCAAGAGAAAATTTTGTACGTCATCACTGGGTGCACAGGCGTCGGCAGGAG
GGGAAATGTAAGCAGTGTGGTAAGGGCTTCCAGCAAAAGTTCTCCTTCCACAGTAAAGAG
ATTGTGGCTATCAGCTGTTCCTGGTGCAAGCAGGCGTTTCACAATAAGGTGACCTGCTTC
ATGCTGCATCACATTGAAGAACCCTGCTCCCTGGGGGCTCATGCTGCTGTTATTGTCCCG
CCCACTTGGATCATTAAGGTGAAGAAACCTCAGAACTCCCTGAAGGCTTCAAATCGGAAG
AAGAAGAGAACAAGCTTTAAAAGAAAAGCCAGTAAAAGAGGGATGGAACAGGAAAACAAA
GGTCGTCCTTTTGTGATAAAACCCATCTCTTCTCCTCTCATGAAACCCTTGCTTGTATTT
GTGAATCCCAAGAGTGGAGGCAACCAGGGAACCAAAGTCCTGCAGATGTTCATGTGGTAC
CTGAATCCACGGCAAGTCTTTGATCTTTCTCAGGAAGGGCCAAAAGATGCGCTTGAATTG
TATAGGAAAGTACCAAATCTGCGAATTCTGGCCTGTGGTGGGGATGGAACGGTGGGCTGG
ATCCTTTCCATCCTGGATGAACTGCAGCTGAGCCCTCAGCCTCCTGTGGGGGTCCTTCCT
CTGGGGACTGGGAATGACCTGGCTCGAACTCTCAACTGGGGAGGGGGCTACACTGATGAA
CCTGTTTCTAAGATCCTGTGTCAAGTGGAAGATGGGACAGTTGTACAGCTAGATCGCTGG
AACCTCCATGTGGAAAGAAACCCCGACTTGCCTCCAGAAGAACTTGAAGATGGCGTATGT
AAGCTCCCTCTGAATGTTTTCAATAACTACTTCAGCCTTGGATTTGATGCCCATGTCACA
CTGGAGTTCCATGAATCCAGAGAAGCAAATCCAGAGAAATTCAACAGTCGTTTTCGAAAT
AAAATGTTCTATGCAGGGGCAGCTTTTTCTGACTTCCTACAGAGAAGTTCTAGAGATCTA
TCCAAACATGTTAAAGTTGTTTGTGATGGAACAGATCTCACCCCAAAGATTCAGGAACTG
AAGTTCCAGTGTATAGTATTTTTAAATATACCCAGATATTGTGCTGGCACAATGCCCTGG
GGAAACCCAGGTGATCACCATGATTTCGAACCTCAGCGTCATGATGATGGTTATATTGAA
GTCATTGGATTTACCATGGCCTCTTTGGCAGCCCTGCAAGTTGGGGGCCATGGAGAGAGG
CTACACCAGTGTCGAGAAGTCATGCTTCTAACTTACAAATCCATCCCCATGCAAGTGGAT
GGGGAGCCCTGTAGGTTGGCCCCAGCTATGATTCGGATCTCCCTGAGGAATCAGGCCAAC
ATGGTACAGAAGAGCAAGAGGAGAACATCCATGCCTTTACTCAATGATCCCCAGTCTGTC
CCAGATCGTCTGAGGATCCGGGTGAACAAAATCAGTTTACAAGACTATGAAGGATTCCAC
TATGACAAGGAGAAACTCCGAGAAGCTTCTATTTCAGACTGGTTAAGAACCATTGCTGGG
GAACTAGTGCAGTCATTTGGAGCGATACCTCTGGGTATTCTAGTTGTGCGTGGAGACTGT
GATTTGGAGACTTGCCGTATGTACATAGACCGCCTACAGGAGGACCTACAGTCAGTTTCT
TCTGGCTCCCAGAGAGTTCATTACCAGGACCATGAAACCTCCTTCCCCAGGGCTCTCTCA
GCACAGAGGCTCTCTCCTCGGTGGTGCTTCCTAGATGACAGATCTCAGGAACATTTGCAC
TTTGTGATGGAGATTTCCCAAGATGAGATTTTTATTCTGGACCCAGATATGGTGGTGTCA
CAGCCGGCGGGGACACCTCCGGGCATGCCTGACCTGGTGGTGGAACAAGCCTCGGGGATC
TCAGACTGGTGGAATCCTGCCCTGCGGAAACGCATGCTGAGTGACAGTGGGCTGGGGATG
ATAGCTCCCTATTATGAGGACTCAGATCTGAAAGATCTCAGCCACTCCCGCGTGCTACAG
TCACCAGTCTCTTCAGAAGATCATGCAATTTTGCAGGCAGTAATAGCTGGTGATCTTATG
AAGCTAATAGAAAGCTATAAAAATGGAGGCAGTCTGCTAATTCAGGGACCAGACCACTGT
TCACTCCTTCACTACGCAGCTAAAACCGGCAACGGGGAGATTGTGAAATATATCCTTGAC
CACGGACCTTCCGAGTTATTGGATATGGCAGACAGTGAAACGGGTGAGACTGCACTGCAC
AAGGCTGCCTGCCAGCGGAACCGGGCTGTGTGCCAGCTTCTGGTGGATGCAGGAGCATCT
CTGAGAAAGACGGACTCCAAGGGTAAGACACCTCAAGAAAGAGCACAGCAGGCTGGGGAC
CCAGACTTGGCTGCTTACCTAGAAAGCCGTCAGAACTATAAGGTCATTGGCCATGAGGAC
CTGGAAACTGCTGTTTGA
Enzyme 7 GenBank Gene ID AF061936 Link Image
Enzyme 7 GeneCard ID DGKI Link Image
Enzyme 7 GenAtlas ID DGKI Link Image
Enzyme 7 HGNC ID HGNC:2855 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Ding L, Traer E, McIntyre TM, Zimmerman GA, Prescott SM: The cloning and characterization of a novel human diacylglycerol kinase, DGKiota. J Biol Chem. 1998 Dec 4;273(49):32746-52. [PubMed Link Image]
  2. Bowne SJ, Sullivan LS, Ding L, Traer E, Prescott SM, Birch DG, Kennan A, Humphries P, Daiger SP: Evaluation of human diacylglycerol kinase(iota), DGKI, a homolog of Drosophila rdgA, in inherited retinopathy mapping to 7q. Mol Vis. 2000 Feb 22;6:6-9. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5474
Enzyme 8 Name Lipid phosphate phosphohydrolase 3
Enzyme 8 Synonyms
  1. Phosphatidic acid phosphatase 2b
  2. Phosphatidate phosphohydrolase type 2b
  3. PAP2b
  4. PAP- 2b
  5. PAP2-beta
  6. Vascular endothelial growth factor and type I collagen-inducible protein
  7. VCIP
Enzyme 8 Gene Name PPAP2B
Enzyme 8 Protein Sequence >Lipid phosphate phosphohydrolase 3 
MQNYKYDKAIVPESKNGGSPALNNNPRRSGSKRVLLICLDLFCLFMAGLPFLIIETSTIK
PYHRGFYCNDESIKYPLKTGETINDAVLCAVGIVIAILAIITGEFYRIYYLKKSRSTIQN
PYVAALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLSVCNPDFSQINCSEGYIQNYR
CRGDDSKVQEARKSFFSGHASFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFY
TGLSRVSDHKHHPSDVLAGFAQGALVACCIVFFVSDLFKTKTTLSLPAPAIRKEILSPVD
IIDRNNHHNMM
Enzyme 8 Number of Residues 311
Enzyme 8 Molecular Weight 35116
Enzyme 8 Theoretical pI 9.40
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Lipid transport and metabolism
Enzyme 8 Specific Function Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1- phosphate (S-1-P). The relative catalytic efficiency is LPA = PA > C-1-P > S-1-P. May be involved in cell adhesion and in cell-cell interactions
Enzyme 8 Pathways
Enzyme 8 Reactions
  • A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 34-54 86-106 123-143 194-214 228-248 258-278
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 2467300 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O14495 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name LPP3_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >936 bp 
ATGCAAAACTACAAGTACGACAAAGCGATCGTCCCGGAGAGCAAGAACGGCGGCAGCCCG
GCGCTCAACAACAACCCGAGGAGGAGCGGCAGCAAGCGGGTGCTGCTCATCTGCCTCGAC
CTCTTCTGCCTCTTCATGGCGGGCCTCCCCTTCCTCATCATCGAGACAAGCACCATCAAG
CCTTACCACCGAGGGTTTTACTGCAATGATGAGAGCATCAAGTACCCACTGAAAACTGGT
GAGACAATAAATGACGCTGTGCTCTGTGCCGTGGGGATCGTCATTGCCATCCTCGCGATC
ATCACGGGGGAATTCTACCGGATCTATTACCTGAAGAAGTCGCGGTCGACGATTCAGAAC
CCCTACGTGGCAGCACTCTATAAGCAAGTGGGCTGCTTCCTCTTTGGCTGTGCCATCAGC
CAGTCTTTCACAGACATTGCCAAAGTGTCCATAGGGCGCCTGCGTCCTCACTTCTTGAGT
GTCTGCAACCCTGATTTCAGCCAGATCAACTGCTCTGAAGGCTACATTCAGAACTACAGA
TGCAGAGGTGATGACAGCAAAGTCCAGGAAGCCAGGAAGTCCTTCTTCTCTGGCCATGCC
TCCTTCTCCATGTACACTATGCTGTATTTGGTGCTATACCTGCAGGCCCGCTTCACTTGG
CGAGGAGCCCGCCTGCTCCGGCCCCTCCTGCAGTTCACCTTGATCATGATGGCCTTCTAC
ACGGGACTGTCTCGCGTATCAGACCACAAGCACCATCCCAGTGATGTTCTGGCAGGATTT
GCTCAAGGAGCCCTGGTGGCCTGCTGCATAGTTTTCTTCGTGTCTGACCTCTTCAAGACT
AAGACGACGCTCTCCCTGCCTGCCCCTGCTATCCGGAAGGAAATCCTTTCACCTGTGGAC
ATTATTGACAGGAACAATCACCACAACATGATGTAG
Enzyme 8 GenBank Gene ID AB000889 Link Image
Enzyme 8 GeneCard ID PPAP2B Link Image
Enzyme 8 GenAtlas ID PPAP2B Link Image
Enzyme 8 HGNC ID HGNC:9229 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1pter-p22.1
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Kai M, Wada I, Imai S, Sakane F, Kanoh H: Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. J Biol Chem. 1997 Sep 26;272(39):24572-8. [PubMed Link Image]
  2. Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed Link Image]
  3. Humtsoe JO, Feng S, Thakker GD, Yang J, Hong J, Wary KK: Regulation of cell-cell interactions by phosphatidic acid phosphatase 2b/VCIP. EMBO J. 2003 Apr 1;22(7):1539-54. [PubMed Link Image]
  4. Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5478
Enzyme 9 Name Diacylglycerol kinase zeta
Enzyme 9 Synonyms
  1. Diglyceride kinase zeta
  2. DGK-zeta
  3. DAG kinase zeta
Enzyme 9 Gene Name DGKZ
Enzyme 9 Protein Sequence >Diacylglycerol kinase zeta 
METFFRRHFRGKVPGPGEGQRRPSSVGLPTGKARRRSPAGQASSSLAQRRRSSAQLQGCL
LSCGVRAQGSSRRRSSTVPPSCNPRFIVDKVLTPQPTTVGAQLLGAPLLLTGLVGMNEEE
GVQEDVVAEASSAIQPGTKTPGPPPPRGAQPLLPLPRYVRRASSHCCPADAVYDHALWGL
HGYYRRLSQRRPSGQHPGPGGRRASGTTAGTMLPTRVRPLSRRRQVALRRKAAGPQAWSA
LLAKAITKSGLQHLAPPPPTPGAPCSESERQIRSTVDWSESATYGEHIWFETNVSGDFCY
VGEQYCVARMLKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESGSRNVREPTFVR
HHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCS
LGVHAAVVIPPTWILRARRPQNTLKASKKKKRASFKRKSSKKGPEEGRWRPFIIRPTPSP
LMKPLLVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHNLRILAC
GGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEG
NVVQLDRWDLHAEPNPEAGPEDRDEGATDRLPLDVFNNYFSLGFDAHVTLEFHESREANP
EKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIQDLKPQCVVFLNIP
RYCAGTMPWGHPGEHHDFEPQRHDDGYLEVIGFTMTSLAALQVGGHGERLTQCREVVLTT
SKAIPVQVDGEPCKLAASRIRIALRNQATMVQKAKRRSAAPLHSDQQPVPEQLRIQVSRV
SMHDYEALHYDKEQLKEASVPLGTVVVPGDSDLELCRAHIERLQQEPDGAGAKSPTCQKL
SPKWCFLDATTASRFYRIDRAQEHLNYVTEIAQDEIYILDPELLGASARPDLPTPTSPLP
TSPCSPTPRSLQGDAAPPQGEELIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAV
STGSKDVVRYLLDHAPPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQG
DTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETAV
Enzyme 9 Number of Residues 1117
Enzyme 9 Molecular Weight 124124
Enzyme 9 Theoretical pI 9.27
Enzyme 9 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols
Enzyme 9 Pathways
Enzyme 9 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 1293079 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q13574 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name DGKZ_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >2787 bp 
ATGGAGCCGCGGGACGGTAGCCCCGAGGCCCGGAGCAGCGACTCCGAGTCGGCTTCCGCC
TCGTCCAGCGGCTCCGAGCGCGACGCCGGTCCCGAGCCGGACAAGGCGCCGCGGCGACTC
AACAAGCGGCGCTTCCCGGGGCTGCGGCTCTTCGGGCACAGGAAAGCCATCACCAAGTCG
GGCCTCCAGCACCTGGCCCCCCCTCCGCCCACCCCTGGGGCCCCGTGCAGCGAGTCAGAG
CGGCAGATCCGGAGTACAGTGGACTGGAGCGAGTCAGCGACATATGGGGAGCACATCTGG
TTCGAGACCAACGTGTCCGGGGACTTCTGCTACGTTGGGGAGCAGTACTGTGTAGCCAGG
ATGCTGAAGTCAGTGTCTCGAAGAAAGTGCGCAGCCTGCAAGATTGTGGTGCACACGCCC
TGCATCGAGCAGCTGGAGAAGATAAATTTCCGCTGTAAGCCGTCCTTCCGTGAATCAGGC
TCCAGGAATGTCCGCGAGCCAACCTTTGTACGGCACCACTGGGTACACAGACGACGCCAG
GACGGCAAGTGTCGGCACTGTGGGAAGGGATTCCAGCAGAAGTTCACCTTCCACAGCAAG
GAGATTGTGGCCATCAGCTGCTCGTGGTGCAAGCAGGCATACCACAGCAAGGTGTCCTGC
TTCATGCTGCAGCAGATCGAGGAGCCGTGCTCGCTGGGGGTCCACGCAGCCGTGGTCATC
CCGCCCACCTGGATCCTCCGCGCCCGGAGGCCCCAGAATACTCTGAAAGCAAGCAAGAAG
AAGAAGAGGGCATCCTTCAAGAGGAAGTCCAGCAAGAAAGGGCCTGAGGAGGGCCGCTGG
AGACCCTTCATCATCAGGCCCACCCCCTCCCCGCTCATGAAGCCCCTGCTGGTGTTTGTG
AACCCCAAGAGTGGGGGCAACCAGGGTGCAAAGATCATCCAGTCTTTCCTCTGGTATCTC
AATCCCCGACAAGTCTTCGACCTGAGCCAGGGAGGGCCCAAGGAGGCGCTGGAGATGTAC
CGCAAAGTGCACAACCTGCGGATCCTGGCGTGCGGGGGCGACGGCACGGTGGGCTGGATC
CTCTCCACCCTGGACCAGCTACGCCTGAAGCCGCCACCCCCTGTTGCCATCCTGCCCCTG
GGTACTGGCAACGACTTGGCCCGAACCCTCAACTGGGGTGGGGGCTACACAGATGAGCCT
GTGTCCAAGATCCTCTCCCACGTGGAGGAGGGGAACGTGGTACAGCTGGACCGCTGGGAC
CTCCACGCTGAGCCCAACCCCGAGGCAGGGCCTGAGGACCGAGATGAAGGCGCCACCGAC
CGGTTGCCCCTGGATGTCTTCAACAACTACTTCAGCCTGGGCTTTGACGCCCACGTCACC
CTGGAGTTCCACGAGTCTCGAGAGGCCAACCCAGAGAAATTCAACAGCCGCTTTCGGAAT
AAGATGTTCTACGCCGGGACAGCTTTCTCTGACTTCCTGATGGGCAGCTCCAAGGACCTG
GCCAAGCACATCCGAGTGGTGTGTGATGGAATGGACTTGACTCCCAAGATCCAGGACCTG
AAACCCCAGTGTGTTGTTTTCCTGAACATCCCCAGGTACTGTGCGGGCACCATGCCCTGG
GGCCACCCTGGGGAGCACCACGACTTTGAGCCCCAGCGGCATGACGACGGCTACCTCGAG
GTCATTGGCTTCACCATGACGTCGTTGGCCGCGCTGCAGGTGGGCGGACACGGCGAGCGG
CTGACGCAGTGTCGCGAGGTGGTGCTCACCACATCCAAGGCCATCCCGGTGCAGGTGGAT
GGCGAGCCCTGCAAGCTTGCAGCCTCACGCATCCGCATCGCCCTGCGCAACCAGGCCACC
ATGGTGCAGAAGGCCAAGCGGCGGAGCGCCGCCCCCCTGCACAGCGACCAGCAGCCGGTG
CCAGAGCAGTTGCGCATCCAGGTGAGTCGCGTCAGCATGCACGACTATGAGGCCCTGCAC
TACGACAAGGAGCAGCTCAAGGAGGCCTCTGTGCCGCTGGGCACTGTGGTGGTCCCAGGA
GACAGTGACCTAGAGCTCTGCCGTGCCCACATTGAGAGACTCCAGCAGGAGCCCGATGGT
GCTGGAGCCAAGTCCCCGACATGCCAGAAACTGTCCCCCAAGTGGTGCTTCCTGGACGCC
ACCACTGCCAGCCGCTTCTACAGGATCGACCGAGCCCAGGAGCACCTCAACTATGTGACT
GAGATCGCACAGGATGAGATTTATATCCTGGACCCTGAGCTGCTGGGGGCATCGGCCCGG
CCTGACCTCCCAACCCCCACTTCCCCTCTCCCCACCTCACCCTGCTCACCCACGCCCCGG
TCACTGCAAGGGGATGCTGCACCCCCTCAAGGTGAAGAGCTGATTGAGGCTGCCAAGAGG
AACGACTTCTGTAAGCTCCAGGAGCTGCACCGAGCTGGGGGCGACCTCATGCACCGAGAC
GAGCAGAGTCGCACGCTCCTGCACCACGCAGTCAGCACTGGCAGCAAGGATGTGGTCCGC
TACCTGCTGGACCACGCCCCCCCAGAGATCCTTGATGCGGTGGAGGAAAACGGGGAGACC
TGTTTGCACCAAGCAGCGGCCCTGGGCCAGCGCACCATCTGCCACTACATCGTGGAGGCC
GGGGCCTCGCTCATGAAGACAGACCAGCAGGGCGACACTCCCCGGCAGCGGGCTGAGAAG
GCTCAGGACACCGAGCTGGCCGCCTACCTGGAGAACCGGCAGCACTACCAGATGATCCAG
CGGGAGGACCAGGAGACGGCTGTGTAG
Enzyme 9 GenBank Gene ID U51477 Link Image
Enzyme 9 GeneCard ID DGKZ Link Image
Enzyme 9 GenAtlas ID DGKZ Link Image
Enzyme 9 HGNC ID HGNC:2857 Link Image
Enzyme 9 Chromosome Location 11
Enzyme 9 Locus 11p11.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Bunting M, Tang W, Zimmerman GA, McIntyre TM, Prescott SM: Molecular cloning and characterization of a novel human diacylglycerol kinase zeta. J Biol Chem. 1996 Apr 26;271(17):10230-6. [PubMed Link Image]
  2. Ding L, Bunting M, Topham MK, McIntyre TM, Zimmerman GA, Prescott SM: Alternative splicing of the human diacylglycerol kinase zeta gene in muscle. Proc Natl Acad Sci U S A. 1997 May 27;94(11):5519-24. [PubMed Link Image]
  3. Topham MK, Bunting M, Zimmerman GA, McIntyre TM, Blackshear PJ, Prescott SM: Protein kinase C regulates the nuclear localization of diacylglycerol kinase-zeta. Nature. 1998 Aug 13;394(6694):697-700. [PubMed Link Image]
  4. Hogan A, Shepherd L, Chabot J, Quenneville S, Prescott SM, Topham MK, Gee SH: Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta. Regulation of nuclear localization by PDZ interactions. J Biol Chem. 2001 Jul 13;276(28):26526-33. Epub 2001 May 14. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5776
Enzyme 10 Name Probable phospholipase DDHD1
Enzyme 10 Synonyms
  1. DDHD domain protein 1
  2. Phosphatidic acid-preferring phospholipase A1 homolog
  3. PA-PLA1
Enzyme 10 Gene Name DDHD1
Enzyme 10 Protein Sequence >Probable phospholipase DDHD1 
MNYPGRGSPRSPEHNGRGGGGGAWELGSDARPAFGGGVCCFEHLPGGDPDDGDVPLALLR
GEPGLHLAPGTDDHNHHLALDPCLSDENYDFSSAESGSSLRYYSEGESGGGGSSLSLHPP
QQPPLVPTNSGGGGATGGSPGERKRTRLGGPAARHRYEVVTELGPEEVRWFYKEDKKTWK
PFIGYDSLRIELAFRTLLQTTGARPQGGDRDGDHVCSPTGPASSSGEDDDEDRACGFCQS
TTGHEPEMVELVNIEPVCVRGGLYEVDVTQGECYPVYWNQADKIPVMRGQWFIDGTWQPL
EEEESNLIEQEHLNCFRGQQMQENFDIEVSKSIDGKDAVHSFKLSRNHVDWHSVDEVYLY
SDATTSKIARTVTQKLGFSKASSSGTRLHRGYVEEATLEDKPSQTTHIVFVVHGIGQKMD
QGRIIKNTAMMREAARKIEERHFSNHATHVEFLPVEWRSKLTLDGDTVDSITPDKVRGLR
DMLNSSAMDIMYYTSPLYRDELVKGLQQELNRLYSLFCSRNPDFEEKGGKVSIVSHSLGC
VITYDIMTGWNPVRLYEQLLQKEEELPDERWMSYEERHLLDELYITKRRLKEIEERLHGL
KASSMTQTPALKFKVENFFCMGSPLAVFLALRGIRPGNTGSQDHILPREICNRLLNIFHP
TDPVAYRLEPLILKHYSNISPVQIHWYNTSNPLPYEHMKPSFLNPAKEPTSVSENEGIST
IPSPVTSPVLSRRHYGESITNIGKASILGAASIGKGLGGMLFSRFGRSSTTQSSETSKDS
MEDEKKPVASPSATTVGTQTLPHSSSGFLDSAYFRLQESFFNLPQLLFPENVMQNKDNAL
VELDHRIDFELREGLVESRYWSAVTSHTAYWSSLDVALFLLTFMYKHEHDDDAKPNLDPI
Enzyme 10 Number of Residues 900
Enzyme 10 Molecular Weight 100436
Enzyme 10 Theoretical pI 5.44
Enzyme 10 GO Classification
Function
  • binding
  • ion binding
  • metal ion binding
Process
—
Component
—
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Probable phospholipase that hydrolyzes phosphatidic acid. The different isoforms may change the substrate specificity
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 12697955 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q8NEL9 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name DDHD1_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1497 bp 
AATTATAATTTTTCTACAGCATCAAGTAGTGGTACCAGACTTCATAGAGGTTATGTAGAA
GAAGCCACATTAGAAGACAAGCCATCACAGACTACCCATATTGTATTTGTTGTGCATGGC
ATTGGGCAGAAAATGGACCAAGGAAGAATTATCAAAAATACAGCTATGATGAGAGAAGCT
GCAAGAAAAATAGAAGAAAGGCATTTTTCCAACCATGCAACACATGTTGAATTTCTGCCT
GTTGAGTGGCGGTCAAAACTTACTCTTGATGGAGACACTGTTGATTCCATTACTCCTGAC
AAAGTACGAGGTTTAAGGGATATGCTGAACAGCAGTGCAATGGACATAATGTATTATACT
AGTCCACTTTATAGAGATGAACTAGTTAAAGGCCTTCAGCAAGAGCTGAATCGATTGTAT
TCCCTTTTCTGTTCTCGGAATCCAGACTTTGAAGAAAAAGGGGGTAAAGTCTCAATAGTA
TCACATTCCTTGGGATGTGTAATTACTTATGACATAATGACTGGCTGGAATCCAGTTCGG
CTGTATGAACAGTTGCTGCAAAAGGAAGAAGAGTTGCCTGATGAACGATGGATGAGCTAT
GAAGAACGACATCTTCTTGATGAACTCTATATAACAAAACGACGGCTGAAGGAAATAGAA
GAACGGCTTCACGGATTGAAAGCATCATCTATGACACAAACACCTGCCTTAAAATTTAAG
GTTGAGAATTTCTTCTGTATGGGATCCCCATTAGCAGTTTTCTTGGCGTTGCGTGGCATC
CGCCCAGGAAATACTGGAAGTCAAGACCATATTTTGCCTAGAGAGATTTGTAACCGGTTA
CTAAATATTTTTCATCCTACAGATCCAGTGGCTTATAGATTAGAACCATTAATACTGAAA
CACTACAGCAACATTTCACCTGTCCAGATCCACTGGTACAATACTTCAAATCCTTTACCT
TATGAACATATGAAGCCAAGCTTTCTCAACCCAGCTAAAGAACCTACCTCAGTTTCAGAG
AATGAAGGCATTTCAACCATACCAAGCCCTGTGACCTCACCAGTTTTGTCCCGCCGACAC
TATGGAGAATCTATAACAAATATAGGCAAAGCAAGCATATTAGGGGCTGCTAGCATTGGA
AAGGGACTTGGAGGAATGTTGTTCTCAAGATTTGGACGTTCATCTACAACACAGTCATCT
GAAACATCAAAAGACTCAATGGAAGATGAGAAGAAGCCAGTTGCCTCACCTTCTGCTACC
ACCGTAGGGACACAGACCCTTCCACATAGCAGTTCTGGCTTCCTCGATTCTGCATTGGAG
TTGGATCACAGGATTGATTTTGAACTCAGAGAAGGCCTTGTGGAGAGCCGCTATTGGTCA
GCTGTCACGTCGCATACTGCCTATTGGTCATCCTTGGATGTTGCCCTTTTTCTTTTAACC
TTCATGTATAAACATGAGCACGATGATGATGCAAAACCCAATTTAGATCCAATCTGA
Enzyme 10 GenBank Gene ID AB051492 Link Image
Enzyme 10 GeneCard ID DDHD1 Link Image
Enzyme 10 GenAtlas ID DDHD1 Link Image
Enzyme 10 HGNC ID HGNC:19714 Link Image
Enzyme 10 Chromosome Location 14
Enzyme 10 Locus 14q21
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Nagase T, Kikuno R, Hattori A, Kondo Y, Okumura K, Ohara O: Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Dec 31;7(6):347-55. [PubMed Link Image]
  2. Higgs HN, Han MH, Johnson GE, Glomset JA: Cloning of a phosphatidic acid-preferring phospholipase A1 from bovine testis. J Biol Chem. 1998 Mar 6;273(10):5468-77. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5908
Enzyme 11 Name cAMP-specific 3',5'-cyclic phosphodiesterase 4D
Enzyme 11 Synonyms
  1. DPDE3
  2. PDE43
Enzyme 11 Gene Name PDE4D
Enzyme 11 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 4D 
MEAEGSSAPARAGSGEGSDSAGGATLKAPKHLWRHEQHHQYPLRQPQFRLLHPHHHLPPP
PPPSPQPQPQCPLQPPPPPPLPPPPPPPGAARGRYASSGATGRVRHRGYSDTERYLYCRA
MDRTSYAVETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTSAGRSPLDPMTSPGSGLILQA
NFVHSQRRESFLYRSDSDYDLSPKSMSRNSSIASDIHGDDLIVTPFAQVLASLRTVRNNF
AALTNLQDRAPSKRSPMCNQPSINKATITEEAYQKLASETLEELDWCLDQLETLQTRHSV
SEMASNKFKRMLNRELTHLSEMSRSGNQVSEFISNTFLDKQHEVEIPSPTQKEKEKKKRP
MSQISGVKKLMHSSSLTNSSIPRFGVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPL
TVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLST
PALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGF
KLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVL
LLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMC
DKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQSPSPAP
DDPEEGRQGQTEKFQFELTLEEDGESDTEKDSGSQVEEDTSCSDSKTLCTQDSESTEIPL
DEQVEEEAVGEEEESQPEACVIDDRSPDT
Enzyme 11 Number of Residues 809
Enzyme 11 Molecular Weight 91116
Enzyme 11 Theoretical pI 5.25
Enzyme 11 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
—
Enzyme 11 General Function Cell wall/membrane/envelope biogenesis
Enzyme 11 Specific Function Regulates the levels of cAMP in the cell
Enzyme 11 Pathways
Enzyme 11 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 347130 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q08499 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name PDE4D_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >2024 bp 
ACATGATGCACGTGAATAATTTTCCCTTTAGAAGGCATTCCTGGATATGTTTTGATGTGG
ACAATGGCACATCTGCGGGACGGAGTCCCTTGGATCCCATGACCAGCCCAGGATCCGGGC
TAATTCTCCAAGCAAATTTTGTCCACAGTCAACGACGGGAGTCCTTCCTGTATCGATCCG
ACAGCGATTATGACCTCTCTCCAAAGTCTATGTCCCGGAACTCCTCCATTGCCAGTGATA
TACACGGAGATGACTTGATTGTGACTCCATTTGCTCAGGTCTTGGCCAGTCTGCGAACTG
TACGAAACAACTTTGCTGCATTAACTAATTTGCAAGATCGAGCACCTAGCAAAAGATCAC
CCATGTGCAACCAACCATCCATCAACAAAGCCACCATAACAGAGGAGGCCTACCAGAAAC
TGGCCAGCGAGACCCTGGAGGAGCTGGACTGGTGTCTGGACCAGCTAGAGACCCTACAGA
CCAGGCACTCCGTCAGTGAGATGGCCTCCAACAAGTTTAAAAGGATGCTTAATCGGGAGC
TCACCCATCTCTCTGAAATGAGTCGGTCTGGAAATCAAGTGTCAGAGTTTATATCAAACA
CATTCTTAGATAAGCAACATGAAGTGGAAATTCCTTCTCCAACTCAGAAGGAAAAGGAGA
AAAAGAAAAGACCAATGTCTCAGATCAGTGGAGTCAAGAAATTGATGCACAGCTCTAGTC
TGACTAATTCAAGTATCCCAAGGTTTGGAGTTAAAACTGAACAAGAAGATGTCCTTGCCA
AGGAACTAGAAGATGTGAACAAATGGGGTCTTCATGTTTTCAGAATAGCAGAGTTGTCTG
GTAACCGGCCCTTGACTGTTATCATGCACACCATTTTTCAGGAACGGGATTTATTAAAAA
CATTTAAAATTCCAGTAGATACTTTAATTACATATCTTATGACTCTCGAAGACCATTACC
ATGCTGATGTGGCCTATCACAACAATATCCATGCTGCAGATGTTGTCCAGTCTACTCATG
TGCTATTATCTACACCTGCTTTGGAGGCTGTGTTTACAGATTTGGAGATTCTTGCAGCAA
TTTTTGCCAGTGCAATACATGATGTAGATCATCCTGGTGTGTCCAATCAATTTCTGATCA
ATACAAACTCTGAACTTGCCTTGATGTACAATGATTCCTCAGTCTTAGAGAACCATCATT
TGGCTGTGGGCTTTAAATTGCTTCAGGAAGAAAACTGTGACATTTTCCAGAATTTGACCA
AAAAACAAAGACAATCTTTAAGGAAAATGGTCATTGACATCGTACTTGCAACAGATATGT
CAAAACACATGAATCTACTGGCTGATTTGAAGACTATGGTTGAAACTAAGAAAGTGACAA
GCTCTGGAGTTCTTCTTCTTGATAATTATTCCGATAGGATTCAGGTTCTTCAGAATATGG
TGCACTGTGCAGATCTGAGCAACCCAACAAAGCCTCTCCAGCTGTACCGCCAGTGGACGG
ACCGGATAATGGAGGAGTTCTTCCGCCAAGGAGACCGAGAGAGGGAACGTGGCATGGAGA
TAAGCCCCATGTGTGACAAGCACAATGCTTCCGTGGAAAAATCACAGGTGGGCTTCATAG
ACTATATTGTTCATCCCCTCTGGGAGACATGGGCAGACCTCGTCCACCCTGACGCCCAGG
ATATTTTGGACACTTTGGAGGACAATCGTGAATGGTACCAGAGCACAATCCCTCAGAGCC
CCTCTCCTGCACCTGATGACCCAGAGGAGGGCCGGCAGGGTCAAACTGAGAAATTCCAGT
TTGAACTAACTTTAGAGGAAGATGGTGAGTCAGACACGGAAAAGGACAGTGGCAGTCAAG
TGGAAGAAGACACTAGCTGCAGTGACTCCAAGACTCTTTGTACTCAAGACTCAGAGTCTA
CTGAAATTCCCCTTGATGAACAGGTTGAAGAGGAGGCAGTAGGGGAAGAAGAGGAAAGCC
AGCCTGAAGCCTGTGTCATAGATGATCGTTCTCCTGACACGTAA
Enzyme 11 GenBank Gene ID L20970 Link Image
Enzyme 11 GeneCard ID PDE4D Link Image
Enzyme 11 GenAtlas ID PDE4D Link Image
Enzyme 11 HGNC ID HGNC:8783 Link Image
Enzyme 11 Chromosome Location 5
Enzyme 11 Locus 5q12
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed Link Image]
  2. Nemoz G, Zhang R, Sette C, Conti M: Identification of cyclic AMP-phosphodiesterase variants from the PDE4D gene expressed in human peripheral mononuclear cells. FEBS Lett. 1996 Apr 8;384(1):97-102. [PubMed Link Image]
  3. Baecker PA, Obernolte R, Bach C, Yee C, Shelton ER: Isolation of a cDNA encoding a human rolipram-sensitive cyclic AMP phosphodiesterase (PDE IVD). Gene. 1994 Jan 28;138(1-2):253-6. [PubMed Link Image]
  4. Bolger GB, Erdogan S, Jones RE, Loughney K, Scotland G, Hoffmann R, Wilkinson I, Farrell C, Houslay MD: Characterization of five different proteins produced by alternatively spliced mRNAs from the human cAMP-specific phosphodiesterase PDE4D gene. Biochem J. 1997 Dec 1;328 ( Pt 2):539-48. [PubMed Link Image]
  5. Miro X, Casacuberta JM, Gutierrez-Lopez MD, de Landazuri MO, Puigdomenech P: Phosphodiesterases 4D and 7A splice variants in the response of HUVEC cells to TNF-alpha(1). Biochem Biophys Res Commun. 2000 Aug 2;274(2):415-21. [PubMed Link Image]
  6. Wang D, Deng C, Bugaj-Gaweda B, Kwan M, Gunwaldsen C, Leonard C, Xin X, Hu Y, Unterbeck A, De Vivo M: Cloning and characterization of novel PDE4D isoforms PDE4D6 and PDE4D7. Cell Signal. 2003 Sep;15(9):883-91. [PubMed Link Image]
  7. Gretarsdottir S, Thorleifsson G, Reynisdottir ST, Manolescu A, Jonsdottir S, Jonsdottir T, Gudmundsdottir T, Bjarnadottir SM, Einarsson OB, Gudjonsdottir HM, Hawkins M, Gudmundsson G, Gudmundsdottir H, Andrason H, Gudmundsdottir AS, Sigurdardottir M, Chou TT, Nahmias J, Goss S, Sveinbjornsdottir S, Valdimarsson EM, Jakobsson F, Agnarsson U, Gudnason V, Thorgeirsson G, Fingerle J, Gurney M, Gudbjartsson D, Frigge ML, Kong A, Stefansson K, Gulcher JR: The gene encoding phosphodiesterase 4D confers risk of ischemic stroke. Nat Genet. 2003 Oct;35(2):131-8. Epub 2003 Sep 21. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6427
Enzyme 12 Name Probable phospholipid-transporting ATPase IG
Enzyme 12 Synonyms
  1. ATPase class I type 11C
  2. ATPase IG
  3. ATPase IQ
  4. ATPase class VI type 11C
Enzyme 12 Gene Name ATP11C
Enzyme 12 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 12 Number of Residues 1132
Enzyme 12 Molecular Weight 129479
Enzyme 12 Theoretical pI 6.63
Enzyme 12 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 12 General Function Inorganic ion transport and metabolism
Enzyme 12 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 67-85 87-107 291-311 347-367 880-900 909-929 956-976 996-1016 1027-1047 1070-1090
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 39573513 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q8NB49 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name AT11C_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 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 12 GenBank Gene ID AJ580093 Link Image
Enzyme 12 GeneCard ID ATP11C Link Image
Enzyme 12 GenAtlas ID ATP11C Link Image
Enzyme 12 HGNC ID HGNC:13554 Link Image
Enzyme 12 Chromosome Location X
Enzyme 12 Locus Xq27.1
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6428
Enzyme 13 Name Probable phospholipid-transporting ATPase IH
Enzyme 13 Synonyms
  1. ATPase class I type 11A
  2. ATPase IS
Enzyme 13 Gene Name ATP11A
Enzyme 13 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 13 Number of Residues 1134
Enzyme 13 Molecular Weight 129757
Enzyme 13 Theoretical pI 6.58
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
  • 62-82 89-110 297-318 350-372 882-902 915-934 965-986 1001-1023 1030-1050 1069-1093
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 55664449 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P98196 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name AT11A_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >414 bp 
ATATTTGGAAACTGGACGTTTGGAACGCTGGTATTCACCGTGATGGTGTTCACAGTTACA
CTAAAGCTTGCATTGGACACACACTACTGGACTTGGATCAACCATTTTGTCATCTGGGGG
TCGCTGCTGTTCTACGTTGTCTTTTCGCTTCTCTGGGGAGGAGTGATCTGGCCGTTCCTC
AACTACCAGAGGATGTACTACGTGTTCATCCAGATGCTGTCCAGCGGGCCCGCCTGGCTG
GCCATCGTGCTGCTGGTGACCATCAGCCTCCTTCCCGACGTCCTCAAGAAAGTCCTGTGC
CGGCAGCTGTGGCCAACAGCAACAGAGAGAGTCCAGACTAAGAGCCAGTGCCTTTCTGTC
GAGCAGTCAACCATCTTTATGCTTTCTCAGACTTCCAGCAGCCTGAGTTTCTGA
Enzyme 13 GenBank Gene ID AL356740 Link Image
Enzyme 13 GeneCard ID ATP11A Link Image
Enzyme 13 GenAtlas ID ATP11A Link Image
Enzyme 13 HGNC ID HGNC:13552 Link Image
Enzyme 13 Chromosome Location 13
Enzyme 13 Locus 13q34
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 6465
Enzyme 14 Name Probable phospholipid-transporting ATPase VA
Enzyme 14 Synonyms
  1. ATPVA
  2. Aminophospholipid translocase VA
Enzyme 14 Gene Name ATP10A
Enzyme 14 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 14 Number of Residues 1499
Enzyme 14 Molecular Weight 167690
Enzyme 14 Theoretical pI 8.43
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
  • 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
  • 87-106 111-128 310-332 363-384 1088-1108 1120-1140 1171-1192 1200-1222 1229-1249 1268-1292
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 14009443 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID O60312 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name AT10A_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 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 14 GenBank Gene ID AB051358 Link Image
Enzyme 14 GeneCard ID ATP10A Link Image
Enzyme 14 GenAtlas ID ATP10A Link Image
Enzyme 14 HGNC ID HGNC:13542 Link Image
Enzyme 14 Chromosome Location 15
Enzyme 14 Locus 15q11.2
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 6488
Enzyme 15 Name Probable phospholipid-transporting ATPase IC
Enzyme 15 Synonyms
  1. Familial intrahepatic cholestasis type 1
  2. ATPase class I type 8B member 1
Enzyme 15 Gene Name ATP8B1
Enzyme 15 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 15 Number of Residues 1251
Enzyme 15 Molecular Weight 143727
Enzyme 15 Theoretical pI 7.16
Enzyme 15 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 15 General Function Inorganic ion transport and metabolism
Enzyme 15 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 15 Pathways Not Available
Enzyme 15 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 15 Pfam Domain Function Not Available
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • 109-130 137-156 341-362 390-411 950-970 983-1002 1033-1054 1069-1091 1098-1118 1139-1163
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 3628757 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID O43520 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name AT8B1_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 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 15 GenBank Gene ID AF038007 Link Image
Enzyme 15 GeneCard ID ATP8B1 Link Image
Enzyme 15 GenAtlas ID ATP8B1 Link Image
Enzyme 15 HGNC ID HGNC:3706 Link Image
Enzyme 15 Chromosome Location 18
Enzyme 15 Locus 18q21-q22|18q21.31
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 6516
Enzyme 16 Name Probable phospholipid-transporting ATPase IIA
Enzyme 16 Synonyms
  1. ATPase class II type 9A
  2. ATPase IIA
Enzyme 16 Gene Name ATP9A
Enzyme 16 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 16 Number of Residues 1047
Enzyme 16 Molecular Weight 118584
Enzyme 16 Theoretical pI 7.81
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
  • metabolism
  • 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
  • 70-91 97-119 304-325 333-354 842-862 875-893 924-942 950-972 979-999 1007-1030
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 56205769 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID O75110 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name ATP9A_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >68 bp 
ATGACGGACAACATCCCGCTGCAGCCGGTGCGCCAGAAGAAGCGGATGGACAGCAGGCCC
CGCGCCGG
Enzyme 16 GenBank Gene ID AL353799 Link Image
Enzyme 16 GeneCard ID ATP9A Link Image
Enzyme 16 GenAtlas ID ATP9A Link Image
Enzyme 16 HGNC ID HGNC:13540 Link Image
Enzyme 16 Chromosome Location 20
Enzyme 16 Locus 20q13.2
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 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 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 6535
Enzyme 17 Name Probable phospholipid-transporting ATPase VD
Enzyme 17 Synonyms
  1. ATPVD
Enzyme 17 Gene Name ATP10D
Enzyme 17 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 17 Number of Residues 1426
Enzyme 17 Molecular Weight 160322
Enzyme 17 Theoretical pI 7.23
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 ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • 98-118 122-142 322-342 366-386 1114-1134 1146-1166 1196-1216 1225-1245 1253-1273 1293-1313
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 28193030 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q9P241 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name AT10D_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 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 17 GenBank Gene ID AJ441078 Link Image
Enzyme 17 GeneCard ID ATP10D Link Image
Enzyme 17 GenAtlas ID ATP10D Link Image
Enzyme 17 HGNC ID HGNC:13549 Link Image
Enzyme 17 Chromosome Location 4
Enzyme 17 Locus 4p12
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 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 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6543
Enzyme 18 Name Probable phospholipid-transporting ATPase IB
Enzyme 18 Synonyms
  1. ATPase class I type 8A member 2
  2. ML-1
Enzyme 18 Gene Name ATP8A2
Enzyme 18 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 18 Number of Residues 1148
Enzyme 18 Molecular Weight 129243
Enzyme 18 Theoretical pI 7.84
Enzyme 18 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 18 General Function Inorganic ion transport and metabolism
Enzyme 18 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • 45-66 72-94 277-298 324-345 838-858 871-890 921-942 957-979 986-1006 1025-1049
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 27820152 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9NTI2 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name AT8A2_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 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 18 GenBank Gene ID AF236871 Link Image
Enzyme 18 GeneCard ID ATP8A2 Link Image
Enzyme 18 GenAtlas ID ATP8A2 Link Image
Enzyme 18 HGNC ID HGNC:13533 Link Image
Enzyme 18 Chromosome Location 13
Enzyme 18 Locus 13q12-13
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 6655
Enzyme 19 Name Probable phospholipid-transporting ATPase IA
Enzyme 19 Synonyms
  1. Chromaffin granule ATPase II
  2. ATPase class I type 8A member 1
Enzyme 19 Gene Name ATP8A1
Enzyme 19 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 19 Number of Residues 1164
Enzyme 19 Molecular Weight 131371
Enzyme 19 Theoretical pI 6.83
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, 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 19 General Function Inorganic ion transport and metabolism
Enzyme 19 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 19 Pathways Not Available
Enzyme 19 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • 66-86 93-115 298-319 345-366 858-878 891-910 941-962 977-999 1006-1026 1045-1070
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 4972583 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9Y2Q0 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name AT8A1_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 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 19 GenBank Gene ID AF067820 Link Image
Enzyme 19 GeneCard ID ATP8A1 Link Image
Enzyme 19 GenAtlas ID ATP8A1 Link Image
Enzyme 19 HGNC ID HGNC:13531 Link Image
Enzyme 19 Chromosome Location 4
Enzyme 19 Locus 4p14-p12
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 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 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 6759
Enzyme 20 Name Probable phospholipid-transporting ATPase IM
Enzyme 20 Synonyms
  1. ATPase class I type 8B member 4
Enzyme 20 Gene Name ATP8B4
Enzyme 20 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 20 Number of Residues 1192
Enzyme 20 Molecular Weight 135942
Enzyme 20 Theoretical pI 6.92
Enzyme 20 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 20 General Function Inorganic ion transport and metabolism
Enzyme 20 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 45-66 73-92 277-298 328-349 872-892 905-924 955-976 991-1013 1020-1040 1061-1085
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 18916718 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q8TF62 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name AT8B4_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 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 20 GenBank Gene ID AB075819 Link Image
Enzyme 20 GeneCard ID ATP8B4 Link Image
Enzyme 20 GenAtlas ID ATP8B4 Link Image
Enzyme 20 HGNC ID HGNC:13536 Link Image
Enzyme 20 Chromosome Location 15
Enzyme 20 Locus 15q21.2
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 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 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 6781
Enzyme 21 Name Probable phospholipid-transporting ATPase IF
Enzyme 21 Synonyms
  1. ATPase class I type 11B
  2. ATPase IR
Enzyme 21 Gene Name ATP11B
Enzyme 21 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 21 Number of Residues 1177
Enzyme 21 Molecular Weight 134191
Enzyme 21 Theoretical pI 6.95
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
  • metabolism
  • 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
  • 56-77 83-104 290-311 342-359 877-898 911-930 961-982 998-1020 1026-1047 1066-1090
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 6457268 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q9Y2G3 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name AT11B_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >744 bp 
ATGTGGCGCTGGATCCGGCAGCAGCTGGGTTTTGACCCACCACATCAGAGTGACACAAGA
ACCATCTACGTAGCCAACAGGTTTCCTCAGAATGGCCTTTACACACCTCAGAAATTTATA
GATAACAGGATCATTTCATCTAAGTACACTGTGTGGAATTTTGTTCCAAAAAATTTATTT
GAACAGTTCAGAAGAGTGGCAAACTTTTATTTTCTTATTATATTTTTGGTTCAGCTTATG
ATTGATACACCTACCAGTCCAGTTACCAGTGGACTTCCATTATTCTTTGTGATAACAGTA
ACTGCCATAAAGCAGGGATATGAAGATTGGTTACGGCATAANTCAGATAATGAAGTAAAT
GGAGCTCCTGTTTATGTTGTTCGAAGTGGTGGCCTTGTAAAAACTAGATCAAAAAACATT
CGGGTGGGTGATATTGTTCGAATAGCCAAAGATGAAATTTTTCCTGCAGACTTGGTGCTT
CTGTCCTCAGATCGACTGGATGGTTCCTGTCACGTTACAACTGCTAGTTTGGACGGAGAA
ACTAACCTGAAGACACATGTGGCAGTTCCAGAAACAGCATTATTACAAACAGTTGCCAAT
TTGGACACTCTAGTAGCTGTAATAGAATGCCAGCAACCAGAAGCAGACTTATACAGATTC
ATGGGACGAATGATCATAACCCAACAAATGGAAGAAATTGTAAGACCTCTGGGGCCGGAG
AGTCTCCTGCTTCGTGGAGCCAGA
Enzyme 21 GenBank Gene ID AF156548 Link Image
Enzyme 21 GeneCard ID ATP11B Link Image
Enzyme 21 GenAtlas ID ATP11B Link Image
Enzyme 21 HGNC ID HGNC:13553 Link Image
Enzyme 21 Chromosome Location 3
Enzyme 21 Locus 3q27
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 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 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 6785
Enzyme 22 Name Probable phospholipid-transporting ATPase IK
Enzyme 22 Synonyms
  1. ATPase class I type 8B member 3
Enzyme 22 Gene Name ATP8B3
Enzyme 22 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 22 Number of Residues 1310
Enzyme 22 Molecular Weight 148032
Enzyme 22 Theoretical pI 7.80
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, 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
  • 150-171 178-197 382-403 431-452 1006-1026 1039-1058 1089-1110 1123-1145 1152-1172 1193-1217
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein Not Available
Enzyme 22 UniProtKB/Swiss-Prot ID O60423 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name AT8B3_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence Not Available
Enzyme 22 GenBank Gene ID AC004755 Link Image
Enzyme 22 GeneCard ID ATP8B3 Link Image
Enzyme 22 GenAtlas ID ATP8B3 Link Image
Enzyme 22 HGNC ID HGNC:13535 Link Image
Enzyme 22 Chromosome Location 19
Enzyme 22 Locus 19p13.3
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References Not Available
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 6873
Enzyme 23 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
Enzyme 23 Synonyms
  1. 1- AGP acyltransferase 3
  2. 1-AGPAT 3
  3. Lysophosphatidic acid acyltransferase gamma
  4. LPAAT-gamma
  5. 1-acylglycerol-3-phosphate O- acyltransferase 3
Enzyme 23 Gene Name AGPAT3
Enzyme 23 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase gamma 
MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQ
LVMLLEWWSCTECTLFTDQATVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKV
LAKKELLYVPLIGWTWYFLEIVFCKRKWEEDRDTVVEGLRRLSDYPEYMWFLLYCEGTRF
TETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSL
LGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFK
PARRPWTLLNFLSWATILLSPLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTE
IEKGSSYGNQEFKKKE
Enzyme 23 Number of Residues 376
Enzyme 23 Molecular Weight 43381
Enzyme 23 Theoretical pI 8.91
Enzyme 23 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 23 General Function Lipid transport and metabolism
Enzyme 23 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 23 Pathways
Enzyme 23 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-25
Enzyme 23 Transmembrane Regions Not Available
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 8886001 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q9NRZ7 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name PLCC_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1131 bp 
ATGGGCCTGCTGGCCTTCCTGAAGACCCAGTTCGTGCTGCACCTGCTGGTCGGCTTTGTC
TTCGTGGTGAGTGGTCTGGTCATCAACTTCGTCCAGCTGTGCACGCTGGCGCTCTGGCCG
GTCAGCAAGCAGCTCTACCGCCGCCTCAACTGCCGCCTCGCATACTCACTCTGGAGCCAA
CTGGTCATGCTGCTGGAGTGGTGGTCCTGCACGGAGTGTACACTGTTCACGGACCAGGCC
ACGGTAGAGCGCTTTGGGAAGGAGCACGCAGTCATCATCCTCAACCACAACTTCGAGATC
GACTTCCTCTGTGGGTGGACCATGTGTGAGCGCTTCGGAGTGCTGGGGAGCTCCAAGGTC
CTCGCTAAGAAGGAGCTGCTCTACGTGCCCCTCATCGGCTGGACGTGGTACTTTCTGGAG
ATTGTGTTCTGCAAGCGGAAGTGGGAGGAGGACCGGGACACCGTGGTCGAAGGGCTGAGG
CGCCTGTCGGACTACCCCGAGTACATGTGGTTTCTCCTGTACTGCGAGGGGACGCGCTTC
ACGGAGACCAAGCACCGCGTTAGCATGGAGGTGGCGGCTGCTAAGGGGCTTCCTGTCCTC
AAGTACCACCTGCTGCCGCGGACCAAGGGCTTCACCACCGCAGTCAAGTGCCTCCGGGGG
ACAGTCGCAGCTGTCTATGATGTAACCCTGAACTTCAGAGGAAACAAGAACCCGTCCCTG
CTGGGGATCCTCTACGGGAAGAAGTACGAGGCGGACATGTGCGTGAGGAGATTTCCTCTG
GAAGACATCCCGCTGGATGAAAAGGAAGCAGCTCAGTGGCTTCATAAACTGTACCAGGAG
AAGGACGCGCTCCAGGAGATATATAATCAGAAGGGCATGTTTCCAGGGGAGCAGTTTAAG
CCTGCCCGGAGGCCGTGGACCCTCCTGAACTTCCTGTCCTGGGCCACCATTCTCCTGTCT
CCCCTCTTCAGTTTTGTCTTGGGCGTCTTTGCCAGCGGATCACCTCTCCTGATCCTGACT
TTCTTGGGGTTTGTGGGAGCAGCTTCCTTTGGAGTTCGCAGACTGATAGGAGTAACTGAG
ATAGAAAAAGGCTCCAGCTACGGAAACCAAGAGTTTAAGAAAAAGGAATAA
Enzyme 23 GenBank Gene ID AF156774 Link Image
Enzyme 23 GeneCard ID AGPAT3 Link Image
Enzyme 23 GenAtlas ID AGPAT3 Link Image
Enzyme 23 HGNC ID HGNC:326 Link Image
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 6875
Enzyme 24 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
Enzyme 24 Synonyms
  1. 1- AGP acyltransferase 2
  2. 1-AGPAT 2
  3. Lysophosphatidic acid acyltransferase beta
  4. LPAAT-beta
  5. 1-acylglycerol-3-phosphate O- acyltransferase 2
Enzyme 24 Gene Name AGPAT2
Enzyme 24 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase beta 
MELWPCLAAALLLLLLLVQLSRAAEFYAKVALYCALCFTVSAVASLVCLLRHGGRTVENM
SIIGWFVRSFKYFYGLRFEVRDPRRLQEARPCVIVSNHQSILDMMGLMEVLPERCVQIAK
RELLFLGPVGLIMYLGGVFFINRQRSSTAMTVMADLGERMVRENLKVWIYPEGTRNDNGD
LLPFKKGAFYLAVQAQVPIVPVVYSSFSSFYNTKKKFFTSGTVTVQVLEAIPTSGLTAAD
VPALVDTCHRAMRTTFLHISKTPQENGATAGSGVQPAQ
Enzyme 24 Number of Residues 278
Enzyme 24 Molecular Weight 30915
Enzyme 24 Theoretical pI 9.22
Enzyme 24 GO Classification
Function
  • 1-acylglycerol-3-phosphate O-acyltransferase activity
  • O-acyltransferase activity
  • acylglycerol O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid biosynthesis
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
  • cell
  • membrane
Enzyme 24 General Function Lipid transport and metabolism
Enzyme 24 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 24 Pathways
Enzyme 24 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • 1-23
Enzyme 24 Transmembrane Regions Not Available
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 2282590 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID O15120 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PLCB_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >837 bp 
ATGGAGCTGTGGCCGTGTCTGGCCGCGGCGCTGCTGTTGCTGCTGCTGCTGGTGCAGCTG
AGCCGCGCGGCCGAGTTCTACGCCAAGGTCGCCCTGTACTGCGCGCTGTGCTTCACGGTG
TCCGCCGTGGCCTCGCTCGTCTGCCTGCTGCGCCACGGCGGCCGGACGGTGGAGAACATG
AGCATCATCGGCTGGTTCGTGCGAAGCTTCAAGTACTTTTACGGGCTCCGCTTCGAGGTG
CGGGACCCGCGCAGGCTGCAGGAGGCCCGTCCCTGTGTCATCGTCTCCAACCACCAGAGC
ATCCTGGACATGATGGGCCTCATGGAGGTCCTTCCGGAGCGCTGCGTGCAGATCGCCAAG
CGGGAGCTGCTCTTCCTGGGGCCCGTGGGCCTCATCATGTACCTCGGGGGCGTCTTCTTC
ATCAACCGGCAGCGCTCTAGCACTGCCATGACAGTGATGGCCGACCTGGGCGAGCGCATG
GTCAGGGAGAACCTCAAAGTGTGGATCTATCCCGAGGGTACTCGCAACGACAATGGGGAC
CTGCTGCCTTTTAAGAAGGGCGCCTTCTACCTGGCAGTCCAGGCACAGGTGCCCATCGTC
CCCGTGGTGTACTCTTCCTTCTCCTCCTTCTACAACACCAAGAAGAAGTTCTTCACTTCA
GGAACAGTCACAGTGCAGGTGCTGGAAGCCATCCCCACCAGCGGCCTCACTGCGGCGGAC
GTCCCTGCGCTCGTGGACACCTGCCACCGGGCCATGAGGACCACCTTCCTCCACATCTCC
AAGACCCCCCAGGAGAACGGGGCCACTGCGGGGTCTGGCGTGCAGCCGGCCCAGTAG
Enzyme 24 GenBank Gene ID AF000237 Link Image
Enzyme 24 GeneCard ID AGPAT2 Link Image
Enzyme 24 GenAtlas ID AGPAT2 Link Image
Enzyme 24 HGNC ID HGNC:325 Link Image
Enzyme 24 Chromosome Location 9
Enzyme 24 Locus 9q34.3
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Eberhardt C, Gray PW, Tjoelker LW: Human lysophosphatidic acid acyltransferase. cDNA cloning, expression, and localization to chromosome 9q34.3. J Biol Chem. 1997 Aug 8;272(32):20299-305. [PubMed Link Image]
  2. Stamps AC, Elmore MA, Hill ME, Kelly K, Makda AA, Finnen MJ: A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases. Biochem J. 1997 Sep 1;326 ( Pt 2):455-61. [PubMed Link Image]
  3. West J, Tompkins CK, Balantac N, Nudelman E, Meengs B, White T, Bursten S, Coleman J, Kumar A, Singer JW, Leung DW: Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells. DNA Cell Biol. 1997 Jun;16(6):691-701. [PubMed Link Image]
  4. Agarwal AK, Arioglu E, De Almeida S, Akkoc N, Taylor SI, Bowcock AM, Barnes RI, Garg A: AGPAT2 is mutated in congenital generalized lipodystrophy linked to chromosome 9q34. Nat Genet. 2002 May;31(1):21-3. Epub 2002 Apr 22. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 6877
Enzyme 25 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
Enzyme 25 Synonyms
  1. 1- AGP acyltransferase 1
  2. 1-AGPAT 1
  3. Lysophosphatidic acid acyltransferase alpha
  4. LPAAT-alpha
  5. 1-acylglycerol-3-phosphate O- acyltransferase 1
  6. Protein G15
Enzyme 25 Gene Name AGPAT1
Enzyme 25 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase alpha 
MDLWPGAWMLLLLLFLLLLFLLPTLWFCSPSAKYFFKMAFYNGWILFLAVLAIPVCAVRG
RNVENMKILRLMLLHIKYLYGIRVEVRGAHHFPPSQPYVVVSNHQSSLDLLGMMEVLPGR
CVPIAKRELLWAGSAGLACWLAGVIFIDRKRTGDAISVMSEVAQTLLTQDVRVWVFPEGT
RNHNGSMLPFKRGAFHLAVQAQVPIVPIVMSSYQDFYCKKERRFTSGQCQVRVLPPVPTE
GLTPDDVPALADRVRHSMLTVFREISTDGRGGGDYLKKPGGGG
Enzyme 25 Number of Residues 283
Enzyme 25 Molecular Weight 31717
Enzyme 25 Theoretical pI 9.75
Enzyme 25 GO Classification
Function
  • 1-acylglycerol-3-phosphate O-acyltransferase activity
  • O-acyltransferase activity
  • acylglycerol O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid biosynthesis
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
  • cell
  • membrane
Enzyme 25 General Function Lipid transport and metabolism
Enzyme 25 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 25 Pathways
Enzyme 25 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • 1-26
Enzyme 25 Transmembrane Regions Not Available
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 2155238 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q99943 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name PLCA_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >852 bp 
ATGGATTTGTGGCCAGGGGCATGGATGCTGCTGCTGCTGCTCTTCCTGCTGCTGCTCTTC
CTGCTGCCCACCCTGTGGTTCTGCAGCCCCAGTGCCAAGTACTTCTTCAAGATGGCCTTC
TACAATGGCTGGATCCTCTTCCTGGCTGTGCTCGCCATCCCTGTGTGTGCCGTGCGAGGA
CGCAACGTCGAGAACATGAAGATCTTGCGTCTAATGCTGCTCCACATCAAATACCTGTAC
GGGATCCGAGTGGAGGTGCGAGGGGCTCACCACTTCCCTCCCTCGCAGCCCTATGTTGTT
GTCTCCAACCACCAGAGCTCTCTCGATCTGCTTGGGATGATGGAGGTACTGCCAGGCCGC
TGTGTGCCCATTGCCAAGCGCGAGCTACTGTGGGCTGGCTCTGCCGGGCTGGCCTGCTGG
CTGGCAGGAGTCATCTTCATCGACCGGAAGCGCACGGGGGATGCCATCAGTGTCATGTCT
GAGGTCGCCCAGACCCTGCTCACCCAGGACGTGAGGGTCTGGGTGTTTCCTGAGGGAACG
AGAAACCACAATGGCTCCATGCTGCCCTTCAAACGTGGCGCCTTCCATCTTGCAGTGCAG
GCCCAGGTTCCCATTGTCCCCATAGTCATGTCCTCCTACCAAGACTTCTACTGCAAGAAG
GAGCGTCGCTTCACCTCGGGACAATGTCAGGTGCGGGTGCTGCCCCCAGTGCCCACGGAA
GGGCTGACACCAGATGACGTCCCAGCTCTGGCTGACAGAGTCCGGCACTCCATGCTCACT
GTTTTCCGGGAAATCTCCACTGATGGCCGGGGTGGTGGTGACTATCTGAAGAAGCCTGGG
GGCGGTGGGTGA
Enzyme 25 GenBank Gene ID U56417 Link Image
Enzyme 25 GeneCard ID AGPAT1 Link Image
Enzyme 25 GenAtlas ID AGPAT1 Link Image
Enzyme 25 HGNC ID HGNC:324 Link Image
Enzyme 25 Chromosome Location 6
Enzyme 25 Locus 6p21.3
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. West J, Tompkins CK, Balantac N, Nudelman E, Meengs B, White T, Bursten S, Coleman J, Kumar A, Singer JW, Leung DW: Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells. DNA Cell Biol. 1997 Jun;16(6):691-701. [PubMed Link Image]
  2. Stamps AC, Elmore MA, Hill ME, Kelly K, Makda AA, Finnen MJ: A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases. Biochem J. 1997 Sep 1;326 ( Pt 2):455-61. [PubMed Link Image]
  3. Aguado B, Campbell RD: Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene located in the class III region of the human major histocompatibility complex. J Biol Chem. 1998 Feb 13;273(7):4096-105. [PubMed Link Image]
  4. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 6881
Enzyme 26 Name Phosphatidylinositol-glycan-specific phospholipase D precursor
Enzyme 26 Synonyms
  1. PI-G PLD
  2. Glycoprotein phospholipase D
  3. Glycosyl- phosphatidylinositol-specific phospholipase D
Enzyme 26 Gene Name GPLD1
Enzyme 26 Protein Sequence >Phosphatidylinositol-glycan-specific phospholipase D precursor 
MSAFRLWPGLLIMLGSLCHRGSPCGLSTHVEIGHRALEFLQLHNGRVNYRELLLEHQDAY
QAGIVFPDCFYPSICKGGKFHDVSESTHWTPFLNASVHYIRENYPLPWEKDTEKLVAFLF
GITSHMAADVSWHSLGLEQGFLRTMGAIDFHGSYSEAHSAGDFGGDVLSQFEFNFNYLAR
RWYVPVKDLLGIYEKLYGRKVITENVIVDCSHIQFLEMYGEMLAVSKLYPTYSTKSPFLV
EQFQEYFLGGLDDMAFWSTNIYHLTSFMLENGTSDCNLPENPLFIACGGQQNHTQGSKMQ
KNDFHRNLTTSLTESVDRNINYTERGVFFSVNSWTPDSMSFIYKALERNIRTMFIGGSQL
SQKHVSSPLASYFLSFPYARLGWAMTSADLNQDGHGDLVVGAPGYSRPGHIHIGRVYLIY
GNDLGLPPVDLDLDKEAHRILEGFQPSGRFGSALAVLDFNVDGVPDLAVGAPSVGSEQLT
YKGAVYVYFGSKQGGMSSSPNITISCQDIYCNLGWTLLAADVNGDSEPDLVIGSPFAPGG
GKQKGIVAAFYSGPSLSDKEKLNVEAANWTVRGEEDFSWFGYSLHGVTVDNRTLLLVGSP
TWKNASRLGHLLHIRDEKKSLGRVYGYFPPNGQSWFTISGDKAMGKLGTSLSSGHVLMNG
TLKQVLLVGAPTYDDVSKVAFLTVTLHQGGATRMYALTSDAQPLLLSTFSGDRRFSRFGG
VLHLSDLDDDGLDEIIMAAPLRIADVTSGLIGGEDGRVYVYNGKETTLGDMTGKCKSWIT
PCPEEKAQYVLISPEASSRFGSSLITVRSKAKNQVVIAAGRSSLGARLSGALHVYSLGSD
Enzyme 26 Number of Residues 840
Enzyme 26 Molecular Weight 92337
Enzyme 26 Theoretical pI 6.33
Enzyme 26 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • glycosylphosphatidylinositol phospholipase D activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase D activity
  • phospholipase activity
Process
—
Component
  • extracellular region
Enzyme 26 General Function Not Available
Enzyme 26 Specific Function This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions
  • 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + phosphatidate
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • 1-23
Enzyme 26 Transmembrane Regions Not Available
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 388763 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P80108 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name PHLD_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >2526 bp 
ATGTCTGCTTTCAGGTTGTGGCCCGGCCTGCTGATGATCGTGATGGCTTCTCTCTGCCAT
AGAGGTTCATCGTGTGGCCTTTCAACGCACATAGAAATCGGACACAGAGCTCTGGAGTTT
CTTCATCTTCACAATGGGCATGTTAACTACAAAGAGCTGTTACTAGAACACCAGGATGCA
TATCAGGCTGGAACCGTGTTTCCTGATTGTTTTTACCCTAGCCTCTGCAAAGGAGGAAAA
TTCCATGATGTGTCTGAGAGCACTCACTGGACTCCGTTTCTTAACGCAAGCGTTCATTAT
ATCCGAGAGAACTATCCCCTTCCCTGGGAGAAGGACACAGAGAAACTGGTAGCTTTCTTG
TTTGGAATTACTTCTCATATGGTAGCAGATGTCAGCTGGCATAGTCTGGGCATTGAACAA
GGATTCCTTAGGACCATGGGAGCTATTGATTTTCACGGCTCCTATTCTGAGGCTCATTCA
GCTGGTGATTTTGGAGGAGATGTGTTGAGCCAGTTTGAATTTAATTTTAATTACCTTGCA
CGACGCTGGTATGTGCCAGTCAAAGATCTGCTGGGAATTTATGAGAAACTCTATGGTCGA
GAAGTCATCACTGAAAATGTAATTGTTGATTGTTCACATATCCAGTTCTTAGAAATGTAT
GGTGAGATGCTAGCTGTTTCCAAGTTATATCCCTCTTACTCTACAAAGTCCCCGTTTTTG
GTGGAACAATTCCAAGAGTATTTTCTTGGAGGACTGGATGATATGGCGTTTTGGTCCACT
AATATTTACCATCTAACGAGCTTCATGTTGGAGAATGGGACCAGTGACTGCAGCCTACCT
GAGAACCCTCTGTTCATTGCATGTGGTGGCCAGCAAAACCACACCCAGGGCTCGAAAATG
CAGAAAAATGATTTTCACAGAAATTTGACTTCATCCCTAACTGAAAACATTGACAGGAAT
ATAAACTATACCGAAAGAGGAGTGTTCTTCAGTGTAAATTCCTGGACCCCGGATTCCATG
TCCTTTATCTACAAGGCTTTGGAAAGGAACGTAAGGACAATGTTCATAGGTGGCTCTCAG
TTGTCACAGAAGCACATCTCTAGCCCCTTAGCATCTTACTTCTTGTCATTTCCTTATGCA
AGGCTTGGCTGGGCAATGACCTCAGCTGACCTCAACCAGGATGGGTACGGCGACCTCGTG
GTGGGCGCACCAGGCTACAGCCGCCCTGGCCGCATCCACATCGGGCGCGTGTACCTCATC
TACGGCAATGAACTGGGTCTGCCGCCCGTTGACCTGGACCTGGACAAGGAGGCCCACGGG
ATCCTTGAAGGTTTCCAGCCCTCAGGTCGGTTTGGCTCGGCCTTGGCTATGTTGGACTTT
AACATGGATGGCGTGCCTGACCTGGCCGTGGGAGCTCCCTCGGTGGGCTCTGAGCAGCTC
ACCTACAAAGGTGCTGTGTATGTCTACTTTGGTTCCAAACAAGGAAGAATGTCTTCTTCC
CCTAACATCACCATCTCTTGCCAGGACATCTACTGTAACTTGGGCTGGACTCTCTTGGCT
GCAGATGTGAATGGAGACAGTGAGCCCGATCTGGTCATTGGCTCCCCTTTTGCACCAGGT
GGAGGGAAGCAGAAGGGAATTGTGGCTGCGTTTTATTCTGGCCCCAGCCTGAGCAACAAA
GAGAAACTGAACGTGGAGGCGGCCAACTGGACGGTGAGAGGCGAGGAAGACTTTGCCTGG
TTTGGATACTCCCTTCACGGTGTCACTGTGGACAACAGAACCTTGCTGCTGGTTGGGAGC
CCGACCTGGAAGAATGCCAGCAGGCTGGGCCGTTTGTTACACATCCGAGATGAGAAAAAG
AGCCTTGGGAGGGTGTATGGCTACTTCCCACCAAACAGCCAAAGCTGGTTTACCATTGTT
GGAGACAAGGCAATGGGGAAACTGGGTACTTCCCTGTCCAGTGGCCACGTGCTGATGAAT
GGAACTCTGACCCAGGTGCTGCTGGTGGGAGCCCCGACACGTGATGATGTGTCTAAGATG
GCATTCCTGACCATGACCCTGCACCAAGGCGGAGCCACTCGGATGTACGCGCTCACATCC
GACCTGCAGCCACCGCTGCTCAGCACCTTCAGCGGAGACCGCCGCTTCTCTCGATTTGGT
GGCGTTCTGCACTTGAGTGACCTGGATGATGATGGCGTAGATGAAATCATCGTGGCAGCC
CCCCTGAGGATAGCAGATGTAACCTCTGGGCTGATTGGGGGAGAAGATGGCCGAGTTTAT
GTATATAATGGCAAAGAGACCACCCTTGGTGACATGACTGGCAAATGCAAATCGTGGATG
ACTCCATGTCCAGAAGAAAAGGCCCAATATGTATTGATTTCTCCTGAAGCCAGCTCAAGG
TTTGGGAGCTCCCTGATCACCGTGAGGTCCAAGGCAAAGAATCAAGTCGTCATTGCCGCT
GGAAGGAGCTCTTTGGGAGCCCGACTCTCCGGGGCACTTCACGTCTATAGCTTTGGCTCA
GATTGA
Enzyme 26 GenBank Gene ID L11701 Link Image
Enzyme 26 GeneCard ID GPLD1 Link Image
Enzyme 26 GenAtlas ID GPLD1 Link Image
Enzyme 26 HGNC ID HGNC:4459 Link Image
Enzyme 26 Chromosome Location 6
Enzyme 26 Locus 6p22.3-p22.2
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Schofield JN, Rademacher TW: Structure and expression of the human glycosylphosphatidylinositol phospholipase D1 (GPLD1) gene. Biochim Biophys Acta. 2000 Nov 15;1494(1-2):189-94. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  3. Hoener MC, Brodbeck U: Phosphatidylinositol-glycan-specific phospholipase D is an amphiphilic glycoprotein that in serum is associated with high-density lipoproteins. Eur J Biochem. 1992 Jun 15;206(3):747-57. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 6926
Enzyme 27 Name Centaurin-gamma 1
Enzyme 27 Synonyms
  1. ARF-GAP with GTP-binding protein-like, ankyrin repeat and pleckstrin homology domains 2
  2. AGAP-2
  3. Phosphatidylinositol-3-kinase enhancer
  4. PIKE
  5. GTP-binding and GTPase-activating protein 2
  6. GGAP2
Enzyme 27 Gene Name CENTG1
Enzyme 27 Protein Sequence >Centaurin-gamma 1 
MSRGAGALQRRTTTYLISLTLVKLESVPPPPPSPSAAAVGAPGARGSEPRDPGSPRGAEE
PGKKRHERLFHRQDALWISTSSAGAGGAEPPALSPAPASPARPVSPAPGRRLSLWAAPPG
PPLSGGLSPDSKPGGAPSSSRRPLLSSPSWGGPEPEGRTGGGVPGSSSPHPGTGSRRLKV
APPPPAPKPCKTVTTSGAKAGGGKGAGSRLSWPESEGKPRVKGSKSSAGTGASVSAAATA
AAAGGGGSTASTSGGVGAGAGARGKLSPRKGKSKTLDNSDLHPGPPAGSPPPLTLPPTPS
PATAVTAASAQPPGPAPPITLEPPAPGLKRGREGGRASTRDRKMLKFISGIFTKSTGGPP
GSGPLPGPPSLSSGSGSRELLGAELRASPKAVINSQEWTLSRSIPELRLGVLGDARSGKS
SLIHRFLTGSYQVLEKTESEQYKKEMLVDGQTHLVLIREEAGAPDAKFSGWADAVIFVFS
LEDENSFQAVSRLHGQLSSLRGEGRGGLALALVGTQDRISASSPRVVGDARARALCADMK
RCSYYETCATYGLNVDRVFQEVAQKVVTLRKQQQLLAACKSLPSSPSHSAASTPVAGQAS
NGGHTSDYSSSLPSSPNVGHRELRAEAAAVAGLSTPGSLHRAAKRRTSLFANRRGSDSEK
RSLDSRGETTGSGRAIPIKQSFLLKRSGNSLNKEWKKKYVTLSSNGFLLYHPSINDYIHS
THGKEMDLLRTTVKVPGKRPPRAISAFGPSASINGLVKDMSTVQMGEGLEATTPMPSPSP
SPSSLQPPPDQTSKHLLKPDRNLARALSTDCTPSGDLSPLSREPPPSPMVKKQRRKKLTT
PSKTEGSAGQAEAKRKMWKLKSFGSLRNIYKAEENFEFLIVSSTGQTWHFEAASFEERDA
WVQAIESQILASLQCCESSKVKLRTDSQSEAVAIQAIRNAKGNSICVDCGAPNPTWASLN
LGALICIECSGIHRNLGTHLSRVRSLDLDDWPRELTLVLTAIGNDTANRVWESDTRGRAK
PSRDSSREERESWIRAKYEQLLFLAPLSTSEEPLGRQLWAAVQAQDVATVLLLLAHARHG
PLDTSVEDPQLRSPLHLAAELAHVVITQLLLWYGADVAARDAQGRTALFYARQAGSQLCA
DILLQHGCPGEGGSAATTPSAATTPSITATPSPRRRSSAASVGRADAPVALV
Enzyme 27 Number of Residues 1192
Enzyme 27 Molecular Weight 124675
Enzyme 27 Theoretical pI 10.54
Enzyme 27 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • regulation of GTPase activity
  • regulation of biological process
  • regulation of enzyme activity
  • regulation of hydrolase activity
  • signal transduction
  • small GTPase mediated signal transduction
Component
—
Enzyme 27 General Function Translation, ribosomal structure and biogenesis
Enzyme 27 Specific Function GTPase-activating protein (GAP) for ARF1 and ARF5, which also shows strong GTPase activity. Isoform 1 participates in the prevention of neuronal apoptosis by enhancing PI3 kinase activity. It aids the coupling of metabotropic glutamate receptor 1 (GRM1) to cytoplasmic PI3 kinase by interacting with Homer scaffolding proteins, and also seems to mediate anti-apoptotic effects of NGF by activating nuclear PI3 kinase. Isoform 2 does not stimulate PI3 kinase but may protect cells from apoptosis by stimulating Akt. It also regulates the adapter protein 1 (AP-1)-dependent trafficking of proteins in the endosomal system
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • 1-26
Enzyme 27 Transmembrane Regions Not Available
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein Not Available
Enzyme 27 UniProtKB/Swiss-Prot ID Q99490 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name CENG1_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 U81031 Link Image
Enzyme 27 GeneCard ID CENTG1 Link Image
Enzyme 27 GenAtlas ID CENTG1 Link Image
Enzyme 27 HGNC ID HGNC:16921 Link Image
Enzyme 27 Chromosome Location 12
Enzyme 27 Locus 12q14.1
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Elkahloun AG, Krizman DB, Wang Z, Hofmann TA, Roe B, Meltzer PS: Transcript mapping in a 46-kb sequenced region at the core of 12q13.3 amplification in human cancers. Genomics. 1997 Jun 1;42(2):295-301. [PubMed Link Image]
  2. Xia C, Ma W, Stafford LJ, Liu C, Gong L, Martin JF, Liu M: GGAPs, a new family of bifunctional GTP-binding and GTPase-activating proteins. Mol Cell Biol. 2003 Apr;23(7):2476-88. [PubMed Link Image]
  3. Rong R, Ahn JY, Huang H, Nagata E, Kalman D, Kapp JA, Tu J, Worley PF, Snyder SH, Ye K: PI3 kinase enhancer-Homer complex couples mGluRI to PI3 kinase, preventing neuronal apoptosis. Nat Neurosci. 2003 Nov;6(11):1153-61. Epub 2003 Oct 5. [PubMed Link Image]
  4. Nagase T, Seki N, Ishikawa K, Tanaka A, Nomura N: Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1996 Feb 29;3(1):17-24. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 8048
Enzyme 28 Name Phospholipid transfer protein precursor
Enzyme 28 Synonyms
  1. Lipid transfer protein II
Enzyme 28 Gene Name PLTP
Enzyme 28 Protein Sequence >Phospholipid transfer protein precursor 
MALFGALFLALLAGAHAEFPGCKIRVTSKALELVKQEGLRFLEQELETITIPDLRGKEGH
FYYNISEVKVTELQLTSSELDFQPQQELMLQITNASLGLRFRRQLLYWFFYDGGYINASA
EGVSIRTGLELSRDPAGRMKVSNVSCQASVSRMHAAFGGTFKKVYDFLSTFITSGMRFLL
NQQICPVLYHAGTVLLNSLLDTVPVRSSVDELVGIDYSLMKDPVASTSNLDMDFRGAFFP
LTERNWSLPNRAVEPQLQEEERMVYVAFSEFFFDSAMESYFRAGALQLLLVGDKVPHDLD
MLLRATYFGSIVLLSPAVIDSPLKLELRVLAPPRCTIKPSGTTISVTASVTIALVPPDQP
EVQLSSMTMDARLSAKMALRGKALRTQLDLRRFRIYSNHSALESLALIPLQAPLKTMLQI
GVMPMLNERTWRGVQIPLPEGINFVHEVVTNHAGFLTIGADLHFAKGLREVIEKNRPADV
RASTAPTPSTAAV
Enzyme 28 Number of Residues 493
Enzyme 28 Molecular Weight 54740
Enzyme 28 Theoretical pI 7.01
Enzyme 28 GO Classification
Function
  • binding
  • lipid binding
Process
—
Component
—
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function Converts HDL into larger and smaller particles. May play a key role in extracellular phospholipid transport and modulation of hdl particles
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • 1-17
Enzyme 28 Transmembrane Regions Not Available
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 468326 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID P55058 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name PLTP_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 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 28 GenBank Gene ID L26232 Link Image
Enzyme 28 GeneCard ID PLTP Link Image
Enzyme 28 GenAtlas ID PLTP Link Image
Enzyme 28 HGNC ID HGNC:9093 Link Image
Enzyme 28 Chromosome Location 20
Enzyme 28 Locus 20q12-q13.1
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 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 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 8524
Enzyme 29 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
Enzyme 29 Synonyms
  1. 1-AGP acyltransferase 5
  2. 1-AGPAT 5
  3. Lysophosphatidic acid acyltransferase epsilon
  4. LPAAT-epsilon
  5. 1-acylglycerol-3-phosphate O-acyltransferase 5
Enzyme 29 Gene Name AGPAT5
Enzyme 29 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon 
MLLSLVLHTYSMRYLLPSVVLLGTAPTYVLAWGVWRLLSAFLPARFYQALDDRLYCVYQS
MVLFFFENYTGVQILLYGDLPKNKENIIYLANHQSTVDWIVADILAIRQNALGHVRYVLK
EGLKWLPLYGCYFAQHGGIYVKRSAKFNEKEMRNKLQSYVDAGTPMYLVIFPEGTRYNPE
QTKVLSASQAFAAQRGLAVLKHVLTPRIKATHVAFDCMKNYLDAIYDVTVVYEGKDDGGQ
RRESPTMTEFLCKECPKIHIHIDRIDKKDVPEEQEHMRRWLHERFEIKDKMLIEFYESPD
PERRKRFPGKSVNSKLSIKKTLPSMLILSGLTAGMLMTDAGRKLYVNTWIYGTLLGCLWV
TIKA
Enzyme 29 Number of Residues 364
Enzyme 29 Molecular Weight 42073
Enzyme 29 Theoretical pI 9.41
Enzyme 29 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 29 General Function Lipid transport and metabolism
Enzyme 29 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 29 Pathways
Enzyme 29 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • 1-31
Enzyme 29 Transmembrane Regions
  • 15-35 61-81 344-364
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 14161585 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q9NUQ2 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name PLCE_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >1095 bp 
ATGCTGCTGTCCCTGGTGCTCCACACGTACTCCATGCGCTACCTGCTGCCCAGCGTCGTG
CTCCTGGGCACGGCGCCCACCTACGTGTTGGCCTGGGGGGTCTGGCGGCTGCTCTCCGCC
TTCCTGCCCGCCCGCTTCTACCAAGCGCTGGACGACCGGCTCTACTGCGTCTACCAGAGC
ATGGTGCTCTTCTTCTTCGAGAATTACACCGGGGTCCAGATATTGCTATATGGAGATTTG
CCAAAAAATAAAGAAAATATAATATATTTAGCAAATCATCAAAGCACAGTTGACTGGATT
GTTGCTGACATCTTGGCCATCAGGCAGAATGCGCTAGGACATGTGCGCTACGTGCTGAAA
GAAGGGTTAAAATGGCTGCCATTGTATGGGTGTTACTTTGCTCAGCATGGAGGAATCTAT
GTAAAGCGCAGTGCCAAATTTAACGAGAAAGAGATGCGAAACAAGTTGCAGAGCTACGTG
GACGCAGGAACTCCAATGTATCTTGTGATTTTTCCAGAAGGTACAAGGTATAATCCAGAG
CAAACAAAAGTCCTTTCAGCTAGTCAGGCATTTGCTGCCCAACGTGGCCTTGCAGTATTA
AAACATGTGCTAACACCACGAATAAAGGCAACTCACGTTGCTTTTGATTGCATGAAGAAT
TATTTAGATGCAATTTATGATGTTACGGTGGTTTATGAAGGGAAAGACGATGGAGGGCAG
CGAAGAGAGTCACCGACCATGACGGAATTTCTCTGCAAAGAATGTCCAAAAATTCATATT
CACATTGATCGTATCGACAAAAAAGATGTCCCAGAAGAACAAGAACATATGAGAAGATGG
CTGCATGAACGTTTCGAAATCAAAGATAAGATGCTTATAGAATTTTATGAGTCACCAGAT
CCAGAAAGAAGAAAAAGATTTCCTGGGAAAAGTGTTAATTCCAAATTAAGTATCAAGAAG
ACTTTACCATCAATGTTGATCTTAAGTGGTTTGACTGCAGGCATGCTTATGACCGATGCT
GGAAGGAAGCTGTATGTGAACACCTGGATATATGGAACCCTACTTGGCTGCCTGTGGGTT
ACTATTAAAGCATAG
Enzyme 29 GenBank Gene ID AF375789 Link Image
Enzyme 29 GeneCard ID AGPAT5 Link Image
Enzyme 29 GenAtlas ID AGPAT5 Link Image
Enzyme 29 HGNC ID HGNC:20886 Link Image
Enzyme 29 Chromosome Location 8
Enzyme 29 Locus 8p23.1
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 8626
Enzyme 30 Name 2-acylglycerol O-acyltransferase 2
Enzyme 30 Synonyms
  1. Monoacylglycerol O- acyltransferase 2
  2. Acyl CoA:monoacylglycerol acyltransferase 2
  3. MGAT2
  4. hMGAT2
  5. Diacylglycerol acyltransferase 2-like protein 5
  6. Diacylglycerol O-acyltransferase candidate 5
  7. hDC5
Enzyme 30 Gene Name MOGAT2
Enzyme 30 Protein Sequence >2-acylglycerol O-acyltransferase 2 
MVEFAPLFMPWERRLQTLAVLQFVFSFLALAEICTVGFIALLFTRFWLLTVLYAAWWYLD
RDKPRQGGRHIQAIRCWTIWKYMKDYFPISLVKTAELDPSRNYIAGFHPHGVLAVGAFAN
LCTESTGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKESAAHILNRKGGGNL
LGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSG
SWLRYIQNRLQKIMGISLPLFHGRGVFQYSFGLIPYRRPITTVVGKPIEVQKTLHPSEEE
VNQLHQRYIKELCNLFEAHKLKFNIPADQHLEFC
Enzyme 30 Number of Residues 334
Enzyme 30 Molecular Weight 38196
Enzyme 30 Theoretical pI 9.77
Enzyme 30 GO Classification Not Available
Enzyme 30 General Function Lipid transport and metabolism
Enzyme 30 Specific Function Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity
Enzyme 30 Pathways
Enzyme 30 Reactions
  • acyl-CoA + 2-acylglycerol = CoA + diacylglycerol
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • 1-31
Enzyme 30 Transmembrane Regions
  • 23-37 38-59 103-123
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 28881910 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q3SYC2 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name MOGT2_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >1005 bp 
ATGGTAGAGTTCGCGCCCTTGTTTATGCCGTGGGAGCGCAGGCTGCAGACACTTGCTGTC
CTACAGTTTGTCTTCTCCTTCTTGGCACTGGCCGAGATCTGCACTGTGGGCTTCATAGCC
CTCCTGTTTACAAGATTCTGGCTCCTCACTGTCCTGTATGCGGCCTGGTGGTATCTGGAC
CGAGACAAGCCACGGCAGGGGGGCCGGCACATCCAGGCCATCAGGTGCTGGACTATATGG
AAGTACATGAAGGACTATTTCCCCATCTCGCTGGTCAAGACTGCTGAGCTGGACCCCTCT
CGGAACTACATTGCGGGCTTCCACCCCCATGGAGTCCTGGCAGTCGGAGCCTTTGCCAAC
CTGTGCACTGAGAGCACAGGCTTCTCTTCGATCTTCCCCGGTATCCGCCCCCATCTGATG
ATGCTGACCTTGTGGTTCCGGGCCCCCTTCTTCAGAGATTACATCATGTCTGCAGGGTTG
GTCACATCAGAAAAGGAGAGTGCTGCTCACATTCTGAACAGGAAGGGTGGCGGAAACTTG
CTGGGCATCATTGTAGGGGGTGCCCAGGAGGCCCTGGATGCCAGGCCTGGATCCTTCACG
CTGTTACTGCGGAACCGAAAGGGCTTCGTCAGGCTCGCCCTGACACACGGGGCACCCCTG
GTGCCAATCTTCTCCTTCGGGGAGAATGACCTATTTGACCAGATTCCCAACTCTTCTGGC
TCCTGGTTACGCTATATCCAGAATCGGTTGCAGAAGATCATGGGCATCTCCCTCCCACTC
TTTCATGGCCGTGGTGTCTTCCAGTACAGCTTTGGTTTAATACCCTACCGCCGGCCCATC
ACCACTGTGGTGGGGAAGCCCATCGAGGTACAGAAGACGCTGCATCCCTCGGAGGAGGAG
GTGAACCAGCTGCACCAGCGTTATATCAAAGAGCTGTGCAACCTCTTCGAGGCCCACAAA
CTTAAGTTCAACATCCCTGCTGACCAGCACTTGGAGTTCTGCTGA
Enzyme 30 GenBank Gene ID AY157608 Link Image
Enzyme 30 GeneCard ID MOGAT2 Link Image
Enzyme 30 GenAtlas ID MOGAT2 Link Image
Enzyme 30 HGNC ID HGNC:23248 Link Image
Enzyme 30 Chromosome Location 11
Enzyme 30 Locus 11q13.5
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Yen CL, Farese RV Jr: MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine. J Biol Chem. 2003 May 16;278(20):18532-7. Epub 2003 Mar 5. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 9821
Enzyme 31 Name Diacylglycerol kinase eta
Enzyme 31 Synonyms
  1. Diglyceride kinase eta
  2. DGK-eta
  3. DAG kinase eta
Enzyme 31 Gene Name DGKH
Enzyme 31 Protein Sequence >Diacylglycerol kinase eta 
MAGAGGQHHPPGAAGGAAAGAGAAVTSAAASAGPGEDSSDSEAEQEGPQKLIRKVSTSGQ
IRTKTSIKEGQLLKQTSSFQRWKKRYFKLRGRTLYYAKDSKSLIFDEVDLSDASVAEAST
KNANNSFTIITPFRRLMLCAENRKEMEDWISSLKSVQTREPYEVAQFNVEHFSGMHNWYA
CSHARPTFCNVCRESLSGVTSHGLSCEVCKFKAHKRCAVRATNNCKWTTLASIGKDIIED
EDGVAMPHQWLEGNLPVSAKCAVCDKTCGSVLRLQDWKCLWCKTMVHTACKDLYHPICPL
GQCKVSIIPPIALNSTDSDGFCRATFSFCVSPLLVFVNSKSGDNQGVKFLRRFKQLLNPA
QVFDLMNGGPHLGLRLFQKFDNFRILVCGGDGSVGWVLSEIDKLNLNKQCQLGVLPLGTG
NDLARVLGWGGSYDDDTQLPQILEKLERASTKMLDRWSIMTYELKLPPKASLLPGPPEAS
EEFYMTIYEDSVATHLTKILNSDEHAVVISSAKTLCETVKDFVAKVEKTYDKTLENAVVA
DAVASKCSVLNEKLEQLLQALHTDSQAAPVLPGLSPLIVEEDAVESSSEESLGESKEQLG
DDVTKPSSQKAVKPREIMLRANSLKKAVRQVIEEAGKVMDDPTVHPCEPANQSSDYDSTE
TDESKEEAKDDGAKESITVKTAPRSPDARASYGHSQTDSVPGPAVAASKENLPVLNTRII
CPGLRAGLAASIAGSSIINKMLLANIDPFGATPFIDPDLDSVDGYSEKCVMNNYFGIGLD
AKISLEFNNKREEHPEKCRSRTKNLMWYGVLGTRELLQRSYKNLEQRVQLECDGQYIPLP
SLQGIAVLNIPSYAGGTNFWGGTKEDDIFAAPSFDDKILEVVAIFDSMQMAVSRVIKLQH
HRIAQCRTVKITIFGDEGVPVQVDGEAWVQPPGIIKIVHKNRAQMLTRDRAFESTLKSWE
DKQKCDSGKPVLRTHLYIHHAIDLATEEVSQMQLCSQAAEELITRICDAATIHCLLEQEL
AHAVNACSHALNKANPRCPESLTRDTATEIAINVKALYNETESLLVGRVPLQLESPHEER
VSNALHSVEVELQKLTEIPWLYYILHPNEDEEPPMDCTKRNNRSTVFRIVPKFKKEKVQK
QKTSSQPVQKWGTEEVAAWLDLLNLGEYKDIFIRHDIRGAELLHLERRDLKDLGIPKVGH
VKRILQGIKELGRSTPQSEV
Enzyme 31 Number of Residues 1220
Enzyme 31 Molecular Weight 134867
Enzyme 31 Theoretical pI Not Available
Enzyme 31 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 31 General Function Not Available
Enzyme 31 Specific Function Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA)
Enzyme 31 Pathways
Enzyme 31 Reactions
  • ATP + diacylglycerol (homo sapiens) <==> ADP + H+ + phosphatidic acid (homo sapiens)
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 29467042 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q86XP1 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name DGKH_HUMAN Link Image
Enzyme 31 PDB ID 1R79 Link Image
Enzyme 31 PDB File Show
Enzyme 31 3D Structure
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence Not Available
Enzyme 31 GenBank Gene ID AB078967 Link Image
Enzyme 31 GeneCard ID Not Available
Enzyme 31 GenAtlas ID DGKH Link Image
Enzyme 31 HGNC ID HGNC:2854 Link Image
Enzyme 31 Chromosome Location Not Available
Enzyme 31 Locus Not Available
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Murakami T, Sakane F, Imai S, Houkin K, Kanoh H: Identification and characterization of two splice variants of human diacylglycerol kinase eta. J Biol Chem. 2003 Sep 5;278(36):34364-72. Epub 2003 Jun 16. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 10050
Enzyme 32 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
Enzyme 32 Synonyms
  1. Phosphoinositide phospholipase C delta-3
  2. PLC-delta-3
  3. Phospholipase C-delta-3
Enzyme 32 Gene Name PLCD3
Enzyme 32 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 32 Number of Residues 789
Enzyme 32 Molecular Weight 89259
Enzyme 32 Theoretical pI Not Available
Enzyme 32 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 32 General Function Not Available
Enzyme 32 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 32 Pathways
Enzyme 32 Reactions
  • H2O + 1-Phosphatidyl-1D-myo-inositol 4-phosphate (Homo sapiens) --> diacylglycerol (homo sapiens) + H+ + 1D-myo-Inositol 1,4-bisphosphate
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 18676791 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q8N3E9 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name PLCD3_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence Not Available
Enzyme 32 GenBank Gene ID AK074240 Link Image
Enzyme 32 GeneCard ID Not Available
Enzyme 32 GenAtlas ID PLCD3 Link Image
Enzyme 32 HGNC ID HGNC:9061 Link Image
Enzyme 32 Chromosome Location Not Available
Enzyme 32 Locus Not Available
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 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 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 10119
Enzyme 33 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
Enzyme 33 Synonyms
  1. 1- AGP acyltransferase 4
  2. 1-AGPAT 4
  3. Lysophosphatidic acid acyltransferase delta
  4. LPAAT-delta
  5. 1-acylglycerol-3-phosphate O- acyltransferase 4
Enzyme 33 Gene Name AGPAT4
Enzyme 33 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase delta 
MDLAGLLKSQFLCHLVFCYVFIASGLIINTIQLFTLLLWPINKQLFRKINCRLSYCISSQ
LVMLLEWWSGTECTIFTDPRAYLKYGKENAIVVLNHKFEIDFLCGWSLSERFGLLGGSKV
LAKKELAYVPIIGWMWYFTEMVFCSRKWEQDRKTVATSLQHLRDYPEKYFFLIHCEGTRF
TEKKHEISMQVARAKGLPRLKHHLLPRTKGFAITVRSLRNVVSAVYDCTLNFRNNENPTL
LGVLNGKKYHADLYVRRIPLEDIPEDDDECSAWLHKLYQEKDAFQEEYYRTGTFPETPMV
PPRRPWTLVNWLFWASLVLYPFFQFLVSMIRSGSSLTLASFILVFFVASVGVRWMIGVTE
IDKGSAYGNSDSKQKLND
Enzyme 33 Number of Residues 378
Enzyme 33 Molecular Weight 44022
Enzyme 33 Theoretical pI Not Available
Enzyme 33 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 33 General Function Lipid transport and metabolism
Enzyme 33 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 33 Pathways
Enzyme 33 Reactions
  • R total 2 coenzyme A + lysophosphatidic acid (homo sapiens) --> Coenzyme A + phosphatidic acid (homo sapiens)
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • 11-31 125-145 307-327 338-358
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 8886005 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q9NRZ5 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name PLCD_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence Not Available
Enzyme 33 GenBank Gene ID AF156776 Link Image
Enzyme 33 GeneCard ID Not Available
Enzyme 33 GenAtlas ID AGPAT4 Link Image
Enzyme 33 HGNC ID HGNC:20885 Link Image
Enzyme 33 Chromosome Location Not Available
Enzyme 33 Locus Not Available
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 12904
Enzyme 34 Name Diacylglycerol kinase kappa
Enzyme 34 Synonyms
  1. Diglyceride kinase kappa
  2. DGK-kappa
  3. DAG kinase kappa
  4. 142 kDa diacylglycerol kinase
Enzyme 34 Gene Name DGKK
Enzyme 34 Protein Sequence >Diacylglycerol kinase kappa 
MDRGAAAAQGTAPPQDGEQPAESPEPPPPWPPPPPPPAPPPAPPLLSEASPEPIPEPCPE
LAPGPCPEATSESATELYTEPTPEPATEPASEPAPEPATEPAPEPATEPAPEPAPEPATE
SAPEPTPEPALESVPEPAPELTPEVAPELAPEPTPEPVTELAPEFCPEAAPEFRPSPAPC
LLQCPVDTRERGLKTSPSPSPSPSPRTPMSWSRIKKILKEGPMLKNCNSFKRWKLRYFLV
QGQKLYFAHHPAFAHFETIDLSQATVAESSCRNLCHSFCVITPQRKITLAAPNRKDMEEW
INIIKTIQQGEIYKIPAAENNPFLVGMHCWYSSYSHRTQHCNVCRESIPALSRDAIICEV
CKVKSHRLCALRASKDCKWNTLSITDDLLLPADEVNMPHQWVEGNMPVSSQCAVCHESCG
SYQRLQDFRCLWCNSTVHDDCRRRFSKECCFRSHRSSVIPPTALSDPKGDGQLVVSSDFW
NLDWSSACSCPLLIFINSKSGDHQGIVFLRKFKQYLNPSQVFDLLKGGPEAGLSMFKNFA
RFRILVCGGDGSVSWVLSLIDAFGLHEKCQLAVIPLGTGNDLARVLGWGAFWNKSKSPLD
ILNRVEQASVRILDRWSVMIRETPRQTPLLKGQVEMDVPRFEAAAIQHLESAATELNKIL
KAKYPTEMIIATRFLCSAVEDFVVDIVKAWGQIKQNNTAIVSVILKSDLMYDRLSVLIDV
LAEEAAATSAEKSATEYADSSKADRKPFIPQIDHIAKCKLELATKAQSLQKSLKLIIFQV
EQALDEESRQTISVKNFSSTFFLEDDPEDINQTSPRRRSRRGTLSSISSLKSEDLDNLNL
DHLHFTPESIRFKEKCVMNNYFGIGLDAKISLDFNTRRDEHPGQYNSRLKNKMWYGLLGT
KELLQRSYRKLEERVHLECDGETISLPNLQGIVVLNITSYAGGINFWGSNTATTEYEAPA
IDDGKLEVVAIFGSVQMAMSRIINLHHHRIAQCHEVMITIDGEEGIPVQVDGEAWIQRPG
LIKIRYKNAAQMLTRDRDFENSMKMWEYKHTEIQAAPQPQLDFQDSQESLSDEEYAQMQH
LARLAENLISKLNDLSKIHQHVSVLMGSVNASANILNDIFYGQDSGNEMGAASCIPIETL
SRNDAVDVTFSLKGLYDDTTAFLDEKLLRSAEDETALQSALDAMNKEFKKLSEIDWMNPI
FVPEEKSSDTDSRSLRLKIKFPKLGKKKVEEERKPKSGQSVQSFIGNLWHRRHREDEAEG
DDPLTPSRSQL
Enzyme 34 Number of Residues 1271
Enzyme 34 Molecular Weight 141830
Enzyme 34 Theoretical pI 5.23
Enzyme 34 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 34 General Function Not Available
Enzyme 34 Specific Function Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA)
Enzyme 34 Pathways
Enzyme 34 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240] ALL_REAC R02240
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 57753888 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q5KSL6 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name DGKK_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence Not Available
Enzyme 34 GenBank Gene ID AB183864 Link Image
Enzyme 34 GeneCard ID Q5KSL6 Link Image
Enzyme 34 GenAtlas ID DGKK Link Image
Enzyme 34 HGNC ID HGNC:32395 Link Image
Enzyme 34 Chromosome Location Not Available
Enzyme 34 Locus Not Available
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References Not Available
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 12919
Enzyme 35 Name Probable phospholipid-transporting ATPase VB
Enzyme 35 Synonyms Not Available
Enzyme 35 Gene Name ATP10B
Enzyme 35 Protein Sequence >Probable phospholipid-transporting ATPase VB 
MALSVDSSWHRWQWRVRDGFPHCPSETTPLLSPEKGRQSYNLTQQRVVFPNNSIFHQDWE
EVSRRYPGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITML
PLAIVLFVIMIKDGMEDFKRHRFDKAINCSNIRIYERKEQTYVQKCWKDVRVGDFIQMKC
NEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEVQFEPELFHNTIVC
EKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNS
GPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSFLPS
ALGGFYMFLTMIILLQVLIPISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNI
AEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQENAKRLETPKELDSDGEEWTQY
QCLSFSARWAQDPATMRSQKGAQPLRRSQSARVPIQGHYRQRSMGHRESSQPPVAFSSSI
EKDVTPDKNLLTKVRDAALWLETLSDSRPAKASLSTTSSIADFFLALTICNSVMVSTTTE
PRQRVTIKPSSKALGTSLEKIQQLFQKLKLLSLSQSFSSTAPSDTDLGESLGANVATTDS
DERDDASVCSGGDSTDDGGYRSSMWDQGDILESGSGTSLEEALEAPATDLARPEFCYEAE
SPDEAALVHAAHAYSFTLVSRTPEQVTVRLPQGTCLTFSLLCTLGFDSVRKRMSVVVRHP
LTGEIVVYTKGADSVIMDLLEDPACVPDINMEKKLRKIRARTQKHLDLYARDGLRTLCIA
KKVVSEEDFRRWASFRREAEASLDNRDELLMETAQHLENQLTLLGATGIEDRLQEGVPDT
IATLREAGIQLWVLTGDKQETAVNIAHSCRLLNQTDTVYTINTENQETCESILNCALEEL
KQFRELQKPDRKLFGFRLPSKTPSITSEAVVPEAGLVIDGKTLNAIFQGKLEKKFLELTQ
YCRSVLCCRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAADIGIGISGQEGMQA
VMSSDFAITRFKHLKKLLLVHGHWCYSRLARMVVYYLYKNVCYVNLLFWYQFFCGFSSST
MIDYWQMIFFNLFFTSLPPLVFGVLDKDISAETLLALPELYKSGQNSECYNLSTFWISMV
DAFYQSLICFFIPYLAYKGSDIDVFTFGTPINTISLTTILLHQAMEMKTWTIFHGVVLLG
SFLMYFLVSLLYNATCVICNSPTNPYWVMEGQLSNPTFYLVCFLTPVVALLPRYFFLSLQ
GTCGKSLISKAQKIDKLPPDKRNLEIQSWRSRQRPAPVPEVARPTHHPVSSITGQDFSAS
TPKSSNPPKRKHVEESVLHEQRCGTECMRDDSCSGDSSAQLSSGEHLLGPNRIMAYSRGQ
TDMCRCSKRSSHRRSQSSLTI
Enzyme 35 Number of Residues 1461
Enzyme 35 Molecular Weight 165392
Enzyme 35 Theoretical pI 6.87
Enzyme 35 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 35 General Function Inorganic ion transport and metabolism
Enzyme 35 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions
  • ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086] ALL_REAC R00086
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • 83-104 111-132 317-338 369-390 1112-1132 1145-1164 1195-1216 1224-1246 1253-1273 1292-1316
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 58257664 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID O94823 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name AT10B_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence Not Available
Enzyme 35 GenBank Gene ID AB018258 Link Image
Enzyme 35 GeneCard ID O94823 Link Image
Enzyme 35 GenAtlas ID ATP10B Link Image
Enzyme 35 HGNC ID HGNC:13543 Link Image
Enzyme 35 Chromosome Location Not Available
Enzyme 35 Locus Not Available
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Oct 30;5(5):277-86. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 12920
Enzyme 36 Name Probable phospholipid-transporting ATPase ID
Enzyme 36 Synonyms
  1. ATPase class I type 8B member 2
Enzyme 36 Gene Name ATP8B2
Enzyme 36 Protein Sequence >Probable phospholipid-transporting ATPase ID 
MTVPKEMPEKWARAQAPPSWSRKKPSWGTEEERRARANDREYNEKFQYASNCIKTSKYNI
LTFLPVNLFEQFQEVANTYFLFLLILQLIPQISSLSWFTTIVPLVLVLTITAVKDATDDY
FRHKSDNQVNNRQSQVLINGILQQEQWMNVCVGDIIKLENNQFVAADLLLLSSSEPHGLC
YIETAELDGETNMKVRQAIPVTSELGDISKLAKFDGEVICEPPNNKLDKFSGTLYWKENK
FPLSNQNMLLRGCVLRNTEWCFGLVIFAGPDTKLMQNSGRTKFKRTSIDRLMNTLVLWIF
GFLVCMGVILAIGNAIWEHEVGMRFQVYLPWDEAVDSAFFSGFLSFWSYIIILNTVVPIS
LYVSVEVIRLGHSYFINWDKKMFCMKKRTPAEARTTTLNEELGQVEYIFSDKTGTLTQNI
MVFNKCSINGHSYGDVFDVLGHKAELGERPEPVDFSFNPLADKKFLFWDPSLLEAVKIGD
PHTHEFFRLLSLCHTVMSEEKNEGELYYKAQSPDEGALVTAARNFGFVFRSRTPKTITVH
EMGTAITYQLLAILDFNNIRKRMSVIVRNPEGKIRLYCKGADTILLDRLHHSTQELLNTT
MDHLNEYAGEGLRTLVLAYKDLDEEYYEEWAERRLQASLAQDSREDRLASIYEEVENNMM
LLGATAIEDKLQQGVPETIALLTLANIKIWVLTGDKQETAVNIGYSCKMLTDDMTEVFIV
TGHTVLEVREELRKAREKMMDSSRSVGNGFTYQDKLSSSKLTSVLEAVAGEYALVINGHS
LAHALEADMELEFLETACACKAVICCRVTPLQKAQVVELVKKYKKAVTLAIGDGANDVSM
IKTAHIGVGISGQEGIQAVLASDYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFA
FTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGVFDQDVPEQRSMEYPKLYE
PGQLNLLFNKREFFICIAQGIYTSVLMFFIPYGVFADATRDDGTQLADYQSFAVTVATSL
VIVVSVQIGLDTGYWTAINHFFIWGSLAVYFAILFAMHSNGLFDMFPNQFRFVGNAQNTL
AQPTVWLTIVLTTVVCIMPVVAFRFLRLNLKPDLSDTVRYTQLVRKKQKAQHRCMRRVGR
TGSRRSGYAFSHQEGFGELIMSGKNMRLSSLALSSFTTRSSSSWIESLRRKKSDSASSPS
GGADKPLKG
Enzyme 36 Number of Residues 1209
Enzyme 36 Molecular Weight 137442
Enzyme 36 Theoretical pI 6.99
Enzyme 36 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 36 General Function Inorganic ion transport and metabolism
Enzyme 36 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions
  • ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086] ALL_REAC R00086
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • 65-86 93-112 296-317 347-368 890-910 923-942 973-994 1009-1031 1038-1058 1079-1103
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 16549511 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID P98198 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name AT8B2_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence Not Available
Enzyme 36 GenBank Gene ID AK054886 Link Image
Enzyme 36 GeneCard ID P98198 Link Image
Enzyme 36 GenAtlas ID ATP8B2 Link Image
Enzyme 36 HGNC ID HGNC:13534 Link Image
Enzyme 36 Chromosome Location Not Available
Enzyme 36 Locus Not Available
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Hirosawa M, Nagase T, Ishikawa K, Kikuno R, Nomura N, Ohara O: Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain. DNA Res. 1999 Oct 29;6(5):329-36. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 12925
Enzyme 37 Name N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
Enzyme 37 Synonyms
  1. N-acyl- phosphatidylethanolamine-hydrolyzing phospholipase D, isoform CRA_a
Enzyme 37 Gene Name NAPE-PLD
Enzyme 37 Protein Sequence >N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D 
MDENESNQSLMTSSQYPKEAVRKRQNSARNSGASDSSRFSRKSFKLDYRLEEDVTKSKKG
KDGRFVNPWPTWKNPSIPNVLRWLIMEKDHSSVPSSKEELDKELPVLKPYFITNPEEAGV
REAGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDA
VLISHNHYDHLDYNSVIALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPG
HDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGP
FDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHTDVQTKKSMAIHWGTFALANEHYLEPPVK
LNEALERYGLNAEDFFVLKHGESRYLNNNDENF
Enzyme 37 Number of Residues 393
Enzyme 37 Molecular Weight 45595
Enzyme 37 Theoretical pI 6.10
Enzyme 37 GO Classification Not Available
Enzyme 37 General Function Not Available
Enzyme 37 Specific Function Not Available
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions Not Available
Enzyme 37 Pfam Domain Function Not Available
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 47938140 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q6IQ20 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name Q6IQ20_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence Not Available
Enzyme 37 GenBank Gene ID BC071604 Link Image
Enzyme 37 GeneCard ID Q6IQ20 Link Image
Enzyme 37 GenAtlas ID NAPEPLD Link Image
Enzyme 37 HGNC ID HGNC:21683 Link Image
Enzyme 37 Chromosome Location Not Available
Enzyme 37 Locus Not Available
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 12931
Enzyme 38 Name Lysocardiolipin acyltransferase
Enzyme 38 Synonyms
  1. Acyl- CoA:lysocardiolipin acyltransferase 1
  2. 1-AGP acyltransferase 8
  3. 1- AGPAT 8
Enzyme 38 Gene Name LYCAT
Enzyme 38 Protein Sequence >Lysocardiolipin acyltransferase 
MHSRGREIVVLLNPWSINEAVSSYCTYFIKQDSKSFGIMVSWKGIYFILTLFWGSFFGSI
FMLSPFLPLMFVNPSWYRWINNRLVATWLTLPVALLETMFGVKVIITGDAFVPGERSVII
MNHRTRMDWMFLWNCLMRYSYLRLEKICLKASLKGVPGFGWAMQAAAYIFIHRKWKDDKS
HFEDMIDYFCDIHEPLQLLIFPEGTDLTENSKSRSNAFAEKNGLQKYEYVLHPRTTGFTF
VVDRLREGKNLDAVHDITVAYPHNIPQSEKHLLQGDFPREIHFHVHRYPIDTLPTSKEDL
QLWCHKRWEEKEERLRSFYQGEKNFYFTGQSVIPPCKSELRVLVVKLLSILYWTLFSPAM
CLLIYLYSLVKWYFIITIVIFVLQERIFGGLEIIELACYRLLHKQPHLNSKKNE
Enzyme 38 Number of Residues 414
Enzyme 38 Molecular Weight 48921
Enzyme 38 Theoretical pI 8.80
Enzyme 38 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 38 General Function Lipid transport and metabolism
Enzyme 38 Specific Function Acyl-CoA:lysocardiolipin acyltransferase. Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors. Acts as a remodeling enzyme for cardiolipin, a major membrane polyglycerophospholipid. Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) with a relatively low activity
Enzyme 38 Pathways
Enzyme 38 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241] ALL_REAC R02241 > R02760
  • (other) R04361
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • 47-67 86-106 340-360 362-382
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 37182526 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID Q6UWP7 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name LYCAT_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 AY358702 Link Image
Enzyme 38 GeneCard ID Q6UWP7 Link Image
Enzyme 38 GenAtlas ID LYCAT Link Image
Enzyme 38 HGNC ID HGNC:26756 Link Image
Enzyme 38 Chromosome Location Not Available
Enzyme 38 Locus Not Available
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 12939
Enzyme 39 Name Lipase member H precursor
Enzyme 39 Synonyms
  1. Membrane-associated phosphatidic acid-selective phospholipase A1-alpha
  2. mPA-PLA1 alpha
  3. LPD lipase-related protein
  4. Phospholipase A1 member B
Enzyme 39 Gene Name LIPH
Enzyme 39 Protein Sequence >Lipase member H precursor 
MLRFYLFISLLCLSRSDAEETCPSFTRLSFHSAVVGTGLNVRLMLYTRKNLTCAQTINSS
AFGNLNVTKKTTFIVHGFRPTGSPPVWMDDLVKGLLSVEDMNVVVVDWNRGATTLIYTHA
SSKTRKVAMVLKEFIDQMLAEGASLDDIYMIGVSLGAHISGFVGEMYDGWLGRITGLDPA
GPLFNGKPHQDRLDPSDAQFVDVIHSDTDALGYKEPLGNIDFYPNGGLDQPGCPKTILGG
FQYFKCDHQRSVYLYLSSLRESCTITAYPCDSYQDYRNGKCVSCGTSQKESCPLLGYYAD
NWKDHLRGKDPPMTKAFFDTAEESPFCMYHYFVDIITWNKNVRRGDITIKLRDKAGNTTE
SKINHEPTTFQKYHQVSLLARFNQDLDKVAAISLMFSTGSLIGPRYKLRILRMKLRSLAH
PERPQLCRYDLVLMENVETVFQPILCPELQL
Enzyme 39 Number of Residues 451
Enzyme 39 Molecular Weight 50860
Enzyme 39 Theoretical pI 7.46
Enzyme 39 GO Classification
Function
  • catalytic activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 39 General Function Not Available
Enzyme 39 Specific Function Hydrolyzes specifically phosphatidic acid (PA) to produce lysophosphatidic acid (LPA)
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions Not Available
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • 1-18
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 18031732 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q8WWY8 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name LIPH_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence Not Available
Enzyme 39 GenBank Gene ID AY036912 Link Image
Enzyme 39 GeneCard ID Q8WWY8 Link Image
Enzyme 39 GenAtlas ID LIPH Link Image
Enzyme 39 HGNC ID HGNC:18483 Link Image
Enzyme 39 Chromosome Location Not Available
Enzyme 39 Locus Not Available
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Jin W, Broedl UC, Monajemi H, Glick JM, Rader DJ: Lipase H, a new member of the triglyceride lipase family synthesized by the intestine. Genomics. 2002 Sep;80(3):268-73. [PubMed Link Image]
  2. Wen XY, Hegele RA, Wang J, Wang DY, Cheung J, Wilson M, Yahyapour M, Bai Y, Zhuang L, Skaug J, Young TK, Connelly PW, Koop BF, Tsui LC, Stewart AK: Identification of a novel lipase gene mutated in lpd mice with hypertriglyceridemia and associated with dyslipidemia in humans. Hum Mol Genet. 2003 May 15;12(10):1131-43. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 12940
Enzyme 40 Name Lipase member I precursor
Enzyme 40 Synonyms
  1. Membrane-associated phosphatidic acid-selective phospholipase A1-beta
  2. mPA-PLA1 beta
  3. LPD lipase
  4. Cancer/testis antigen 17
  5. CT17
Enzyme 40 Gene Name LIPI
Enzyme 40 Protein Sequence >Lipase member I precursor 
MRVYIFLCLMCWVRSDNKRPCLEFSQLSVKDSFRDLFIPRIETILMMYTRNNLNCAEPLF
EQNNSLNVNFNTQKKTVWLIHGYRPVGSIPLWLQNFVRILLNEEDMNVIVVDWSRGATTF
IYNRAVKNTRKVAVSLSVHIKNLLKHGASLDNFHFIGVSLGAHISGFVGKIFHGQLGRIT
GLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSNGLGIQEPLGHIDFYPNGGNKQPGCPK
SIFSGIQFIKCNHQRAVHLFMASLETNCNFISFPCRSYKDYKTSLCVDCDCFKEKSCPRL
GYQAKLFKGVLKERMEGRPLRTTVFLDTSGTYPFCTYYFVLSIIVPDKTMMDGSFSFKLL
NQLGMIEEPRLYEKNKPFYKLQEVKILAQFYNDFVNISSIGLTYFQSSNLQCSTCTYKIQ
RLMLKSLTYPERPPLCRYNIVLKDREEVFLNPNTCTPKNT
Enzyme 40 Number of Residues 460
Enzyme 40 Molecular Weight 52992
Enzyme 40 Theoretical pI 9.28
Enzyme 40 GO Classification
Function
  • catalytic activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 40 General Function Not Available
Enzyme 40 Specific Function Hydrolyzes specifically phosphatidic acid (PA) to produce lysophosphatidic acid (LPA)
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • 1-15
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 37781763 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID Q6XZB0 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name LIPI_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 AY197607 Link Image
Enzyme 40 GeneCard ID Q6XZB0 Link Image
Enzyme 40 GenAtlas ID LIPI Link Image
Enzyme 40 HGNC ID HGNC:18821 Link Image
Enzyme 40 Chromosome Location Not Available
Enzyme 40 Locus Not Available
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Wen XY, Hegele RA, Wang J, Wang DY, Cheung J, Wilson M, Yahyapour M, Bai Y, Zhuang L, Skaug J, Young TK, Connelly PW, Koop BF, Tsui LC, Stewart AK: Identification of a novel lipase gene mutated in lpd mice with hypertriglyceridemia and associated with dyslipidemia in humans. Hum Mol Genet. 2003 May 15;12(10):1131-43. [PubMed Link Image]
  2. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 12941
Enzyme 41 Name Plasticity related gene 1
Enzyme 41 Synonyms
  1. Plasticity related gene 1, isoform CRA_b
  2. PRG1
  3. Lipid phosphate phosphatase-related protein type 4
Enzyme 41 Gene Name LPPR4
Enzyme 41 Protein Sequence >Plasticity related gene 1 
MQRAGSSGGRGECDISGAGRLGLEEAARLSCAVHTSPGGGRRPGQAAGMSAKERPKGKVI
KDSVTLLPCFYFVELPILASSVVSLYFLELTDVFKPVHSGFSCYDRSLSMPYIEPTQEAI
PFLMLLSLAFAGPAITIMVGEGILYCCLSKRRNGVGLEPNINAGGCNFNSFLRRAVRFVG
VHVFGLCSTALITDIIQLSTGYQAPYFLTVCKPNYTSLNVSCKENSYIVEDICSGSDLTV
INSGRKSFPSQHATLAAFAAVYVSMYFNSTLTDSSKLLKPLLVFTFIICGIICGLTRITQ
YKNHPVDVYCGFLIGGGIALYLGLYAVGNFLPSDESMFQHRDALRSLTDLNQDPNRLLSA
KNGSSSDGIAHTEGILNRNHRDASSLTNLKRANADVEIITPRSPMGKENMVTFSNTLPRA
NTPSVEDPVRRNASIHASMDSARSKQLLTQWKNKNESRKLSLQVIEPEPGQSPPRSIEMR
SSSEPSRVGVNGDHHGPGNQYLKIQPGAVPGCNNSMPGGPRVSIQSRPGSSQLVHIPEET
QENISTSPKSSSARAKWLKAAEKTVACNRSNSQPRIMQVIAMSKQQGVLQSSPKNTEGST
VSCTGSIRYKTLTDHEPSGIVRVEAHPENNRPIIQIPSTEGEGSGSWKWKAPEKGSLRQT
YELNDLNRDSESCESLKDSFGSGDRKRSNIDSNEHHHHGITTIRVTPVEGSEIGSETLSI
SSSRDSTLRRKGNIILIPERSNSPENTRNIFYKGTSPTRAYKD
Enzyme 41 Number of Residues 763
Enzyme 41 Molecular Weight 82984
Enzyme 41 Theoretical pI 8.89
Enzyme 41 GO Classification Not Available
Enzyme 41 General Function Not Available
Enzyme 41 Specific Function Not Available
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions Not Available
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 31580551 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID Q7Z2D5 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name Q7Z2D5_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence Not Available
Enzyme 41 GenBank Gene ID AF541281 Link Image
Enzyme 41 GeneCard ID Q7Z2D5 Link Image
Enzyme 41 GenAtlas ID Not Available
Enzyme 41 HGNC ID Not Available
Enzyme 41 Chromosome Location Not Available
Enzyme 41 Locus Not Available
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Brauer AU, Savaskan NE, Kuhn H, Prehn S, Ninnemann O, Nitsch R: A new phospholipid phosphatase, PRG-1, is involved in axon growth and regenerative sprouting. Nat Neurosci. 2003 Jun;6(6):572-8. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 12942
Enzyme 42 Name PAP2 protein
Enzyme 42 Synonyms Not Available
Enzyme 42 Gene Name Not Available
Enzyme 42 Protein Sequence >PAP2 protein 
LEARTCLRLFLQRLHPASRASSSRRLRRRAPGGCLGGPGRGPTASTARSARLGPAREACM
PLLPAALTSSMLYFQMVIMAGTVMLAYYFEYTDTFTVNVQGFFCHDSAYRKPYPGPEDSS
AVPPVLLYSLAAGVPVLVIIVGETAVFCLQLATRDFENQEKTILTGDCCYINPLVRRTVR
FLGIYTFGLFATDIFVNAGQVVTGNLAPHFLALCKPNYTALGCQQYTQFISGEEACTGNP
DLIMRARKTFPSKEAALSVYAAMYLTMYITNTIKAKGTRLAKPVLCLGLMCLAFLTGLNR
VAEYRNHWSDVIAGFLVGISIAVFLVVCVVNNFKGRQAENEHIHMDNLAQMPMISIPRVE
SPLEKVTSVQNHITAFAEVT
Enzyme 42 Number of Residues 380
Enzyme 42 Molecular Weight 41694
Enzyme 42 Theoretical pI 8.79
Enzyme 42 GO Classification Not Available
Enzyme 42 General Function Lipid transport and metabolism
Enzyme 42 Specific Function Not Available
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions Not Available
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 45758731 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q32ZL2 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name Q32ZL2_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 AY574039 Link Image
Enzyme 42 GeneCard ID Q32ZL2 Link Image
Enzyme 42 GenAtlas ID Not Available
Enzyme 42 HGNC ID Not Available
Enzyme 42 Chromosome Location Not Available
Enzyme 42 Locus Not Available
Enzyme 42 SNPs Not Available
Enzyme 42 General References Not Available
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 12943
Enzyme 43 Name Presqualene diphosphate phosphatase
Enzyme 43 Synonyms
  1. Phosphatidic acid phosphatase type 2 domain-containing protein 2
Enzyme 43 Gene Name PPAPDC2
Enzyme 43 Protein Sequence >Presqualene diphosphate phosphatase 
MPSPRRSMEGRPLGVSASSSSSSPGSPAHGGGGGGSRFEFQSLLSSRATAVDPTCARLRA
SESPVHRRGSFPLAAAGPSQSPAPPLPEEDRMDLNPSFLGIALRSLLAIDLWLSKKLGVC
AGESSSWGSVRPLMKLLEISGHGIPWLLGTLYCLCRSDSWAGREVLMNLLFALLLDLLLV
ALIKGLVRRRRPAHNQMDMFVTLSVDKYSFPSGHATRAALMSRFILNHLVLAIPLRVLVV
LWAFVLGLSRVMLGRHNVTDVAFGFFLGYMQYSIVDYCWLSPHNAPVLFLLWSQR
Enzyme 43 Number of Residues 295
Enzyme 43 Molecular Weight 32194
Enzyme 43 Theoretical pI 10.42
Enzyme 43 GO Classification Not Available
Enzyme 43 General Function Lipid transport and metabolism
Enzyme 43 Specific Function Phosphatase that dephosphorylates presqualene diphosphate (PSDP) into presqualene monophosphate (PSMP), suggesting that it may be indirectly involved in innate immunity. PSDP is a bioactive lipid that rapidly remodels to presqualene monophosphate PSMP upon cell activation. Displays diphosphate phosphatase activity with a substrate preference for PSDP > FDP > phosphatidic acid
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • 133-153 165-185 229-249 261-281
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein Not Available
Enzyme 43 UniProtKB/Swiss-Prot ID Q8IY26 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name PPAC2_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 AK074672 Link Image
Enzyme 43 GeneCard ID Q8IY26 Link Image
Enzyme 43 GenAtlas ID PPAPDC2 Link Image
Enzyme 43 HGNC ID HGNC:23682 Link Image
Enzyme 43 Chromosome Location Not Available
Enzyme 43 Locus Not Available
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References Not Available
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 12944
Enzyme 44 Name Probable lipid phosphate phosphatase PPAPDC3
Enzyme 44 Synonyms
  1. Phosphatidic acid phosphatase type 2 domain-containing protein 3
Enzyme 44 Gene Name PPAPDC3
Enzyme 44 Protein Sequence >Probable lipid phosphate phosphatase PPAPDC3 
MPASQSRARARDRNNVLNRAEFLSLNQPPKGGPEPRSSGRKASGPSAQPPPAGDGARERR
QSQQLPEEDCMQLNPSFKGIAFNSLLAIDICMSKRLGVCAGRAASWASARSMVKLIGITG
HGIPWIGGTILCLVKSSTLAGQEVLMNLLLALLLDIMTVAGVQKLIKRRGPYETSPSLLD
YLTMDIYAFPAGHASRAAMVSKFFLSHLVLAVPLRVLLVLWALCVGLSRVMIGRHHVTDV
LSGFVIGYLQFRLVELVWMPSSTCQMLISAW
Enzyme 44 Number of Residues 271
Enzyme 44 Molecular Weight 29448
Enzyme 44 Theoretical pI 10.50
Enzyme 44 GO Classification Not Available
Enzyme 44 General Function Lipid transport and metabolism
Enzyme 44 Specific Function Probable lipid phosphate phosphatase
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions Not Available
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • 113-133 142-162 203-223 240-260
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 14042336 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID Q8NBV4 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name PPAC3_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 AK027568 Link Image
Enzyme 44 GeneCard ID Q8NBV4 Link Image
Enzyme 44 GenAtlas ID PPAPDC3 Link Image
Enzyme 44 HGNC ID HGNC:28174 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 12945
Enzyme 45 Name Phosphatidic acid phosphatase type 2 domain-containing protein 1A
Enzyme 45 Synonyms Not Available
Enzyme 45 Gene Name PPAPDC1A
Enzyme 45 Protein Sequence >Phosphatidic acid phosphatase type 2 domain-containing protein 1A 
MRELAIEIGVRALLFGVFVFTEFLDPFQRVIQPEEIWLYKNPLVQSDNIPTRLMFAISFL
TPLAVICVVKIIRRTDKTEIKEAFLAVSLALALNGVCTNTIKLIVGRPRPDFFYRCFPDG
VMNSEMHCTGDPDLVSEGRKSFPSIHSSFAFSGLGFTTFYLAGKLHCFTESGRGKSWRLC
AAILPLYCAMMIALSRMCDYKHHWQDSFVGGVIGLIFAYICYRQHYPPLANTACHKPYVS
LRVPASLKKEERPTADSAPSLPLEGITEGPV
Enzyme 45 Number of Residues 271
Enzyme 45 Molecular Weight 30395
Enzyme 45 Theoretical pI 8.26
Enzyme 45 GO Classification Not Available
Enzyme 45 General Function Lipid transport and metabolism
Enzyme 45 Specific Function Not Available
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions Not Available
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • 4-24 49-69 84-104 142-162 179-199 202-222
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein Not Available
Enzyme 45 UniProtKB/Swiss-Prot ID Q5VZY2 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name PPC1A_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 AL157782 Link Image
Enzyme 45 GeneCard ID Q5VZY2 Link Image
Enzyme 45 GenAtlas ID PPAPDC1A Link Image
Enzyme 45 HGNC ID HGNC:23531 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 12946
Enzyme 46 Name Phosphatidic acid phosphatase type 2 domain-containing protein 1B
Enzyme 46 Synonyms Not Available
Enzyme 46 Gene Name PPAPDC1B
Enzyme 46 Protein Sequence >Phosphatidic acid phosphatase type 2 domain-containing protein 1B 
MWLYRNPYVEAEYFPTKPMFVIAFLSPLSLIFLAKFLKKADTRDSRQACLAASLALALNG
VFTNTIKLIVGRPRPDFFYRCFPDGLAHSDLMCTGDKDVVNEGRKSFPSGHSSFAFAGLA
FASFYLAGKLHCFTPQGRGKSWRFCAFLSPLLFAAVIALSRTCDYKHHWQDVLVGSMIGM
TFAYVCYRQYYPPLTDAECHKPFQDKLVLSTAQKPGDSYCFDI
Enzyme 46 Number of Residues 223
Enzyme 46 Molecular Weight 25159
Enzyme 46 Theoretical pI 8.76
Enzyme 46 GO Classification Not Available
Enzyme 46 General Function Lipid transport and metabolism
Enzyme 46 Specific Function May be a metastatic suppressor for hepatocellular carcinoma
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • 14-34 50-70 114-134 139-159 168-187
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 13182757 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID Q8NEB5 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name PPC1B_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 AF212238 Link Image
Enzyme 46 GeneCard ID Q8NEB5 Link Image
Enzyme 46 GenAtlas ID PPAPDC1B Link Image
Enzyme 46 HGNC ID HGNC:25026 Link Image
Enzyme 46 Chromosome Location Not Available
Enzyme 46 Locus Not Available
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References Not Available
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 14039
Enzyme 47 Name Centaurin-beta-1
Enzyme 47 Synonyms
  1. Cnt-b1
  2. ARFGAP with coiled-coil, ANK repeat and PH domain-containing protein 1
  3. ACAP1
Enzyme 47 Gene Name CENTB1
Enzyme 47 Protein Sequence >Centaurin-beta-1 
MTVKLDFEECLKDSPRFRASIELVEAEVSELETRLEKLLKLGTGLLESGRHYLAASRAFV
VGICDLARLGPPEPMMAECLEKFTVSLNHKLDSHAELLDATQHTLQQQIQTLVKEGLRGF
REARRDFWRGAESLEAALTHNAEVPRRRAQEAEEAGAALRTARAGYRGRALDYALQINVI
EDKRKFDIMEFVLRLVEAQATHFQQGHEELSRLSQYRKELGAQLHQLVLNSAREKRDMEQ
RHVLLKQKELGGEEPEPSLREGPGGLVMEGHLFKRASNAFKTWSRRWFTIQSNQLVYQKK
YKDPVTVVVDDLRLCTVKLCPDSERRFCFEVVSTSKSCLLQADSERLLQLWVSAVQSSIA
SAFSQARLDDSPRGPGQGSGHLAIGSAATLGSGGMARGREPGGVGHVVAQVQSVDGNAQC
CDCREPAPEWASINLGVTLCIQCSGIHRSLGVHFSKVRSLTLDSWEPELVKLMCELGNVI
INQIYEARVEAMAVKKPGPSCSRQEKEAWIHAKYVEKKFLTKLPEIRGRRGGRGRPRGQP
PVPPKPSIRPRPGSLRSKPEPPSEDLGSLHPGALLFRASGHPPSLPTMADALAHGADVNW
VNGGQDNATPLIQATAANSLLACEFLLQNGANVNQADSAGRGPLHHATILGHTGLACLFL
KRGADLGARDSEGRDPLTIAMETANADIVTLLRLAKMREAEAAQGQAGDETYLDIFRDFS
LMASDDPEKLSRRSHDLHTL
Enzyme 47 Number of Residues 740
Enzyme 47 Molecular Weight 81537
Enzyme 47 Theoretical pI 7.70
Enzyme 47 GO Classification
Function
  • binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase C activity
  • phospholipase activity
  • protein binding
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • regulation of GTPase activity
  • regulation of biological process
  • regulation of enzyme activity
  • regulation of hydrolase activity
  • signal transduction
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 47 General Function Not Available
Enzyme 47 Specific Function GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions Not Available
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 40789069 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID Q15027 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name CENB1_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >2391 bp 
GACACCCCTTTCCCCTTGGGGAAAGAATTGTGCCCCCAGGCCCTTCCCCGCGGAGGTCCC
TCTCCTCCTTCCCCCTCATCTCCCCTTCCTGGGACAGAAAGTGCCTCCACCTGCATCCCC
AGGGGCCCGGCCTCCAGGGCCCGCTGGCCCCACAGCAGGCAAGCTGAGATGACGGTCAAG
CTGGATTTCGAGGAGTGTCTCAAGGACTCACCCCGTTTCCGAGCCTCTATTGAGCTGGTG
GAAGCCGAAGTGTCAGAATTGGAGACCCGTCTGGAAAAGCTCCTGAAACTGGGCACTGGT
CTCCTGGAAAGTGGGCGCCATTACCTTGCTGCCAGCCGCGCCTTCGTTGTCGGCATTTGT
GACCTGGCCCGCCTGGGTCCACCAGAGCCCATGATGGCGGAGTGTCTGGAAAAATTCACC
GTGAGCCTGAACCACAAGCTGGACAGCCATGCGGAGCTTCTAGATGCCACCCAACACACA
CTGCAGCAGCAGATCCAGACCCTGGTCAAGGAAGGTCTGCGGGGTTTCCGAGAGGCTCGC
CGGGATTTCTGGCGGGGGGCTGAGAGCCTGGAGGCTGCCCTGACCCACAACGCAGAGGTT
CCCAGGCGCCGGGCCCAGGAGGCAGAAGAGGCAGGAGCTGCTTTGAGGACGGCTCGAGCT
GGGTACCGGGGACGGGCACTGGATTATGCCCTGCAGATCAACGTGATTGAGGACAAGAGG
AAGTTTGACATCATGGAGTTTGTGCTGCGTTTGGTGGAGGCCCAGGCTACCCATTTCCAG
CAGGGCCATGAGGAGCTGAGCCGGCTGTCCCAGTATCGAAAGGAGCTGGGCGCCCAGTTG
CACCAGCTGGTCTTGAATTCAGCACGAGAGAAGAGGGACATGGAGCAGAGACACGTGCTG
CTGAAACAGAAGGAGCTGGGTGGGGAGGAGCCAGAACCAAGCTTAAGAGAGGGGCCTGGT
GGCCTGGTGATGGAAGGACATCTCTTCAAACGGGCCAGCAACGCATTTAAGACCTGGAGC
AGACGCTGGTTCACCATTCAGAGCAACCAACTGGTTTACCAGAAGAAGTACAAGGACCCT
GTGACTGTGGTGGTGGATGACCTTCGTCTCTGCACAGTGAAACTCTGCCCTGACTCAGAA
AGGCGGTTCTGCTTTGAGGTGGTGTCCACCAGCAAGTCCTGCCTCCTCCAGGCTGACTCA
GAGCGCCTCCTGCAGCTGTGGGTCAGTGCTGTGCAGAGCAGCATTGCTTCTGCCTTCAGT
CAGGCTCGCCTTGATGACAGCCCCCGGGGTCCAGGCCAGGGCTCAGGACACCTGGCCATA
GGCTCTGCTGCCACCCTGGGCTCTGGTGGAATGGCCAGGGGAAGGGAGCCTGGGGGAGTC
GGGCACGTGGTGGCCCAGGTCCAGAGTGTGGATGGCAATGCCCAGTGCTGCGACTGCCGG
GAGCCAGCCCCGGAGTGGGCCAGCATCAACCTTGGTGTCACCCTCTGCATTCAGTGTTCC
GGCATCCACAGGAGCCTTGGTGTTCACTTCTCCAAAGTCCGGTCTCTGACCCTTGACTCA
TGGGAGCCAGAACTAGTGAAGCTCATGTGTGAGCTGGGAAATGTCATCATCAACCAGATC
TATGAGGCCCGCGTGGAGGCCATGGCAGTGAAGAAACCAGGGCCCAGCTGCTCCCGGCAG
GAGAAGGAGGCCTGGATTCACGCTAAATACGTGGAGAAGAAGTTCCTGACCAAGCTGCCT
GAGATTCGAGGGCGAAGAGGTGGCCGGGGGCGCCCAAGGGGGCAGCCTCCTGTGCCCCCA
AAGCCTTCCATCAGGCCCCGGCCAGGGAGCTTGAGATCCAAGCCAGAGCCCCCCTCTGAG
GACCTGGGAAGCCTGCACCCTGGGGCCCTACTGTTTCGAGCGTCTGGGCATCCTCCATCT
CTTCCCACCATGGCTGATGCCCTTGCCCATGGAGCTGATGTCAACTGGGTCAATGGGGGC
CAAGATAATGCCACACCGCTGATCCAGGCCACAGCTGCTAATTCTCTTCTGGCCTGTGAG
TTTCTCCTCCAGAACGGGGCGAACGTGAACCAAGCGGACAGTGCGGGCCGGGGCCCGCTG
CACCACGCAACCATTCTTGGCCACACGGGGCTCGCCTGCCTGTTCCTGAAACGGGGAGCT
GATCTGGGGGCTCGAGACTCTGAAGGCAGGGACCCTCTGACCATCGCCATGGAAACAGCC
AACGCTGACATCGTCACCCTGCTACGACTGGCAAAGATGAGGGAGGCTGAAGCGGCCCAG
GGGCAGGCAGGAGATGAGACGTATCTTGACATCTTCCGCGACTTCTCCCTCATGGCGTCA
GACGACCCGGAGAAGCTGAGCCGTCGCAGTCATGACCTCCACACGCTGTGA
Enzyme 47 GenBank Gene ID D30758 Link Image
Enzyme 47 GeneCard ID Q15027 Link Image
Enzyme 47 GenAtlas ID CENTB1 Link Image
Enzyme 47 HGNC ID HGNC:16467 Link Image
Enzyme 47 Chromosome Location 17
Enzyme 47 Locus 17p13.1
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1994;1(5):223-9. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 14253
Enzyme 48 Name Rab11 family-interacting protein 2
Enzyme 48 Synonyms
  1. Rab11-FIP2
  2. NRip11
Enzyme 48 Gene Name RAB11FIP2
Enzyme 48 Protein Sequence >Rab11 family-interacting protein 2 
MMLSEQAQKWFPTHVQVTVLQAKDLKPKGKSGTNDTYTIIQLGKEKYSTSVAEKTLEPVW
KEEASFELPGLLIQGSPEKYILFLIVMHRSLVGLDKFLGQVAINLNDIFEDKQRRKTEWF
RLESKQGKRIKNRGEIKVNIQFMRNNMTASMFDLSMKDKTRSPFAKLKDKMKGRKNDGTF
SDTSSAIIPSTHMPDANSEFSSGEIQMKSKPKKPFLLGPQRLSSAHSMSDLSGSHMSSEK
LKAGTIGQTHLLGHQLDSFGTVPESGSLKSPHRRTLSFDTSKMNQPDSIVDEGELCFGRQ
NDPFTNVTASLPQKFATLPRKKNPFEESSETWDSSMNLFSKPIEIRKENKREKREKVSLF
ERVTGKKDSRRSDKLNNGGSDSPCDLKSPNAFSENRQDYFDYESTNPFTAKFRASNIMPS
SSFHMSPTSNEDLRKIPDSNPFDATAGYRSLTYEEVLQELVKHKELLRRKDTHIRELEDY
IDNLLVRVMEETPSILRVPYEPSRKAGKFSNS
Enzyme 48 Number of Residues 512
Enzyme 48 Molecular Weight 58280
Enzyme 48 Theoretical pI 9.95
Enzyme 48 GO Classification Not Available
Enzyme 48 General Function Not Available
Enzyme 48 Specific Function A Rab11 effector protein acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles. Binds preferentially to phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA)
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions Not Available
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 15822596 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID Q7L804 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name RFIP2_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >1539 bp 
ATGATGCTGTCCGAGCAAGCCCAAAAGTGGTTTCCAACCCACGTGCAGGTCACAGTGCTC
CAAGCCAAAGATCTGAAGCCAAAAGGCAAAAGTGGTACCAATGACACATACACTATAATT
CAGCTGGGCAAGGAAAAGTACTCCACCTCTGTAGCTGAGAAAACCCTTGAGCCAGTTTGG
AAGGAGGAGGCCTCTTTCGAGCTACCTGGATTGCTAATTCAGGGAAGTCCAGAGAAATAC
ATTCTTTTCCTTATAGTTATGCACAGGTCCCTGGTGGGTCTGGATAAATTTTTAGGGCAG
GTGGCAATCAATCTCAATGACATCTTTGAGGACAAACAAAGAAGGAAAACAGAGTGGTTT
AGATTAGAATCCAAACAAGGAAAACGAATCAAAAACAGGGGTGAGATAAAGGTCAATATT
CAGTTTATGAGGAACAATATGACCGCAAGTATGTTTGACTTATCAATGAAGGACAAAACC
AGATCTCCTTTTGCAAAGTTAAAAGATAAGATGAAGGGTAGAAAAAATGATGGAACATTT
TCTGATACGTCTTCTGCAATCATTCCAAGTACTCACATGCCCGATGCCAATAGTGAATTT
TCAAGTGGTGAAATACAGATGAAATCCAAACCAAAAAAGCCTTTTCTCTTGGGTCCTCAG
CGACTCTCGTCAGCGCATTCAATGTCTGATTTATCTGGGTCCCATATGTCTTCTGAGAAA
CTGAAGGCTGGCACCATAGGTCAAACACATCTTCTCGGACACCAGTTAGATTCCTTTGGA
ACAGTTCCAGAAAGTGGAAGTCTCAAATCTCCACACAGAAGAACATTAAGCTTTGATACT
TCTAAAATGAACCAACCTGACAGCATTGTGGATGAAGGTGAATTGTGTTTCGGAAGACAA
AATGACCCATTTACAAATGTGACTGCTTCATTACCCCAAAAATTTGCAACACTGCCAAGG
AAGAAAAATCCATTTGAAGAAAGCAGCGAAACATGGGACAGCAGCATGAATTTATTTTCA
AAACCAATTGAAATAAGAAAAGAAAATAAAAGAGAGAAAAGGGAGAAAGTTAGCCTGTTT
GAAAGAGTGACTGGAAAAAAAGATAGCAGAAGATCTGATAAACTTAACAATGGGGGATCT
GATAGCCCTTGTGACTTGAAATCACCTAATGCATTTAGTGAAAATCGCCAGGACTATTTT
GATTATGAGTCAACCAATCCATTTACAGCAAAATTCAGGGCTTCAAATATAATGCCATCT
TCAAGTTTTCATATGAGTCCAACAAGCAATGAAGACCTCAGGAAAATCCCGGACAGCAAC
CCCTTTGATGCCACTGCAGGGTATCGTAGTCTGACCTATGAAGAGGTTCTACAGGAGCTG
GTGAAACACAAAGAACTCCTTAGGAGGAAAGACACCCACATCCGGGAACTCGAGGACTAC
ATCGACAACCTCCTTGTAAGGGTAATGGAAGAAACGCCCAGTATTCTCAGAGTGCCATAT
GAACCATCCAGGAAAGCTGGCAAATTCTCTAACAGTTAA
Enzyme 48 GenBank Gene ID AY037299 Link Image
Enzyme 48 GeneCard ID Q7L804 Link Image
Enzyme 48 GenAtlas ID RAB11FIP2 Link Image
Enzyme 48 HGNC ID HGNC:29152 Link Image
Enzyme 48 Chromosome Location 10
Enzyme 48 Locus 10q26.11
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. 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]
  2. Hales CM, Griner R, Hobdy-Henderson KC, Dorn MC, Hardy D, Kumar R, Navarre J, Chan EK, Lapierre LA, Goldenring JR: Identification and characterization of a family of Rab11-interacting proteins. J Biol Chem. 2001 Oct 19;276(42):39067-75. Epub 2001 Aug 8. [PubMed Link Image]
  3. Wallace DM, Lindsay AJ, Hendrick AG, McCaffrey MW: Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells. Biochem Biophys Res Commun. 2002 Dec 20;299(5):770-9. [PubMed Link Image]
  4. Cullis DN, Philip B, Baleja JD, Feig LA: Rab11-FIP2, an adaptor protein connecting cellular components involved in internalization and recycling of epidermal growth factor receptors. J Biol Chem. 2002 Dec 20;277(51):49158-66. Epub 2002 Oct 2. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 14426
Enzyme 49 Name Acylglycerol kinase, mitochondrial precursor
Enzyme 49 Synonyms
  1. hAGK
  2. Multiple substrate lipid kinase
  3. Multi- substrate lipid kinase
  4. MuLK
  5. HsMuLK
Enzyme 49 Gene Name AGK
Enzyme 49 Protein Sequence >Acylglycerol kinase, mitochondrial precursor 
MTVFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQV
KKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTIVKTDYEGQAKKLLELMENTDVII
VAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATL
AIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFST
LKEWPQTHQASISYTGPTERPPNEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSP
EVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHV
EGTECLQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSP
TQ
Enzyme 49 Number of Residues 422
Enzyme 49 Molecular Weight 47138
Enzyme 49 Theoretical pI 8.21
Enzyme 49 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 49 General Function Lipid transport and metabolism
Enzyme 49 Specific Function Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively. Does not phosphorylate sphingosine. Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth
Enzyme 49 Pathways
Enzyme 49 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240] ALL_REAC R02240
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • 1-31
Enzyme 49 Transmembrane Regions
  • None
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 8250243 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q53H12 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name AGK_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >1269 bp 
ATGACGGTGTTCTTTAAAACGCTTCGAAATCACTGGAAGAAAACTACAGCTGGGCTCTGC
CTGCTGACCTGGGGAGGCCATTGGCTCTATGGAAAACACTGTGATAACCTCCTAAGGAGA
GCAGCCTGTCAAGAAGCTCAGGTGTTTGGCAATCAACTCATTCCTCCCAATGCACAAGTG
AAGAAGGCCACTGTTTTTCTCAATCCTGCAGCTTGCAAAGGAAAAGCCAGGACTCTATTT
GAAAAAAATGCTGCCCCGATTTTACATTTATCTGGCATGGATGTGACTATTGTTAAGACA
GATTATGAGGGACAAGCCAAGAAACTCCTGGAACTGATGGAAAACACGGATGTGATCATT
GTTGCAGGAGGAGATGGGACACTGCAGGAGGTTGTTACTGGTGTTCTTCGACGAACAGAT
GAGGCTACCTTCAGTAAGATTCCCATTGGATTTATCCCACTGGGAGAGACCAGTAGTTTG
AGTCATACCCTCTTTGCCGAAAGTGGAAACAAAGTCCAACATATTACTGATGCCACACTT
GCCATTGTGAAAGGAGAGACAGTTCCACTTGATGTCTTGCAGATCAAGGGTGAAAAGGAA
CAGCCTGTATTTGCAATGACCGGCCTTCGATGGGGATCTTTCAGAGATGCTGGCGTCAAA
GTTAGCAAGTACTGGTATCTTGGGCCTCTAAAAATCAAAGCAGCCCACTTTTTCAGCACT
CTTAAGGAGTGGCCTCAGACTCATCAAGCCTCTATCTCATACACGGGACCTACAGAGAGA
CCTCCCAATGAACCAGAGGAGACCCCTGTACAAAGGCCTTCTTTGTACAGGAGAATATTA
CGAAGGCTTGCGTCCTACTGGGCACAACCACAGGATGCCCTTTCCCAAGAGGTGAGCCCG
GAGGTCTGGAAAGATGTGCAGCTGTCCACCATTGAACTGTCCATCACAACACGGAATAAT
CAGCTTGACCCGACAAGCAAAGAAGATTTTCTGAATATCTGCATTGAACCTGACACCATC
AGCAAAGGAGACTTTATAACTATAGGAAGTCGAAAGGTGAGAAACCCCAAGCTGCACGTG
GAGGGCACGGAGTGTCTCCAAGCCAGCCAGTGCACTTTGCTTATCCCGGAGGGAGCAGGG
GGCTCTTTTAGCATTGACAGTGAGGAGTATGAAGCGATGCCTGTGGAGGTGAAACTGCTC
CCCAGGAAGCTGCAGTTCTTCTGTGATCCTAGGAAGAGAGAACAGATGCTCACAAGCCCC
ACCCAGTGA
Enzyme 49 GenBank Gene ID AJ278150 Link Image
Enzyme 49 GeneCard ID Q53H12 Link Image
Enzyme 49 GenAtlas ID AGK Link Image
Enzyme 49 HGNC ID HGNC:21869 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. 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 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 15207
Enzyme 50 Name Phospholipase D1 variant (Fragment)
Enzyme 50 Synonyms Not Available
Enzyme 50 Gene Name Not Available
Enzyme 50 Protein Sequence >Phospholipase D1 variant (Fragment) 
ANAQVLAAPSPCSPFAFTLSKVNMSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEG
EEVDYDVSPSDPKIQEVYIPFSAIYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRV
PSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEP
REMPSLPRSSENMIREEQFLGRRKQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDL
GPKGIEGMIMKRSGGHRIPGLNCCGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLL
VDKEFKIKVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKD
HRFGSYAAIQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGN
RWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSST
VYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAM
ESMESLRLKDKNEPVQNLPIQKSIDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSI
SSIDSTSNTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPR
MPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLLPKSQTTAHELRYQVP
GSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFN
KIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGEN
SILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANIN
DRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCFRVVLGYLDDPSEDIQ
DPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPVLAKEDPIRAEE
ELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
Enzyme 50 Number of Residues 1059
Enzyme 50 Molecular Weight 122010
Enzyme 50 Theoretical pI 9.03
Enzyme 50 GO Classification
Function
  • catalytic activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • metabolism
  • physiological process
  • signal transduction
Component
—
Enzyme 50 General Function Lipid transport and metabolism
Enzyme 50 Specific Function Not Available
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 62089400 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID Q59EA4 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name Q59EA4_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >3182 bp 
CCGCCAACGCGCAGGTGCTAGCGGCCCCTTCGCCCTGCAGCCCCTTTGCTTTTACTCTGT
CCAAAGTTAACATGTCACTGAAAAACGAGCCACGGGTAAATACCTCTGCACTGCAGAAAA
TTGCTGCTGACATGAGTAATATCATAGAAAATCTGGACACGCGGGAACTCCACTTTGAGG
GAGAGGAGGTAGACTACGACGTGTCTCCCAGCGATCCCAAGATACAAGAAGTGTATATCC
CTTTCTCTGCTATTTATAACACTCAAGGATTTAAGGAGCCTAATATACAGACGTATCTCT
CCGGCTGTCCAATAAAAGCACAAGTTCTGGAAGTGGAACGCTTCACATCTACAACAAGGG
TACCAAGTATTAATCTTTACACTATTGAATTAACACATGGGGAATTTAAATGGCAAGTTA
AGAGGAAATTCAAGCATTTTCAAGAATTTCACAGAGAGCTGCTCAAGTACAAAGCCTTTA
TCCGCATCCCCATTCCCACTAGAAGACACACGTTTAGGAGGCAAAACGTCAGAGAGGAGC
CTCGAGAGATGCCCAGTTTGCCCCGTTCATCTGAAAACATGATAAGAGAAGAACAATTCC
TTGGTAGAAGAAAACAACTGGAAGATTACTTGACAAAGATACTAAAAATGCCCATGTATA
GAAACTATCATGCCACAACAGAGTTTCTTGATATAAGCCAGCTGTCTTTCATCCATGATT
TGGGACCAAAGGGCATAGAAGGTATGATAATGAAAAGATCTGGAGGACACAGAATACCAG
GCTTGAATTGCTGTGGTCAGGGAAGAGCCTGCTACAGATGGTCAAAAAGATGGTTAATAG
TGAAAGATTCCTTTTTATTGTATATGAAACCAGACAGCGGTGCCATTGCCTTCGTCCTGC
TGGTAGACAAAGAATTCAAAATTAAGGTGGGGAAGAAGGAGACAGAAACGAAATATGGAA
TCCGAATTGATAATCTTTCAAGGACACTTATTTTAAAATGCAACAGCTATAGACATGCTC
GGTGGTGGGGAGGGGCTATAGAAGAATTCATCCAGAAACATGGCACCAACTTTCTCAAAG
ATCATCGATTTGGGTCATATGCTGCTATCCAAGAGAATGCTTTAGCTAAATGGTATGTTA
ATGCCAAAGGATATTTTGAAGATGTGGCAAATGCAATGGAAGAGGCAAATGAAGAGATTT
TTATCACAGACTGGTGGCTGAGTCCAGAAATCTTCCTGAAACGCCCAGTGGTTGAGGGAA
ATCGTTGGAGGTTGGACTGCATTCTTAAACGAAAAGCACAACAAGGAGTGAGGATCTTCA
TAATGCTCTACAAAGAGGTGGAACTCGCTCTTGGCATCAATAGTGAATACACCAAGAGGA
CTTTGATGCGTCTACATCCCAACATAAAGGTGATGAGACACCCGGATCATGTGTCATCCA
CCGTCTATTTGTGGGCTCACCATGAGAAGCTTGTCATCATTGACCAATCGGTGGCCTTTG
TGGGAGGGATTGACCTGGCCTATGGAAGGTGGGACGACAATGAGCACAGACTCACAGACG
TGGGCAGTGTGAAGCGGGTCACTTCAGGACCGTCTCTGGGTTCCCTCCCACCTGCCGCAA
TGGAGTCTATGGAATCCTTAAGACTCAAAGATAAAAATGAGCCTGTTCAAAACCTACCCA
TCCAGAAGAGTATTGATGATGTGGATTCAAAACTGAAAGGAATAGGAAAGCCAAGAAAGT
TCTCCAAATTTAGTCTCTACAAGCAGCTCCACAGGCACCACCTGCACGACGCAGATAGCA
TCAGCAGCATTGACAGCACCTCCAATACCGGGTCCATCCGTAGTTTACAGACAGGTGTGG
GAGAGCTGCATGGGGAAACCAGATTCTGGCATGGAAAGGACTACTGCAATTTCGTCTTCA
AAGACTGGGTTCAACTTGATAAACCTTTTGCTGATTTCATTGACAGGTACTCCACGCCCC
GGATGCCCTGGCATGACATTGCCTCTGCAGTCCACGGGAAGGCGGCTCGTGATGTGGCAC
GTCACTTCATCCAGCGCTGGAACTTCACAAAAATTATGAAATCAAAATATCGGTCCCTTT
CTTATCCTTTTCTGCTTCCAAAGTCTCAAACAACAGCCCATGAGTTGAGATATCAAGTGC
CTGGGTCTGTCCATGCTAACGTACAGTTGCTCCGCTCTGCTGCTGATTGGTCTGCTGGTA
TAAAGTACCATGAAGAGTCCATCCACGCCGCTTACGTCCATGTGATAGAGAACAGCAGGC
ACTATATCTATATCGAAAACCAGTTTTTCATAAGCTGTGCTGATGACAAAGTTGTGTTCA
ACAAGATAGGCGATGCCATTGCCCAGAGGATCCTGAAAGCTCACAGGGAAAACCAGAAAT
ACCGGGTATATGTCGTGATACCACTTCTGCCAGGGTTCGAAGGAGACATTTCAACCGGCG
GAGGAAATGCTCTACAGGCAATCATGCACTTCAACTACAGAACCATGTGCAGAGGAGAAA
ATTCCATCCTTGGACAGTTAAAAGCAGAGCTTGGTAATCAGTGGATAAATTACATATCAT
TCTGTGGTCTTAGAACACATGCAGAGCTCGAAGGAAACCTAGTAACTGAGCTTATCTATG
TCCACAGCAAGTTGTTAATTGCTGATGATAACACTGTTATTATTGGCTCTGCCAACATAA
ATGACCGCAGCATGCTGGGAAAGCGTGACAGTGAAATGGCTGTCATTGTGCAAGATACAG
AGACTGTTCCTTCAGTAATGGATGGAAAAGAGTACCAAGCTGGCCGGTTTGCCCGAGGAC
TTCGGCTACAGTGCTTTAGGGTTGTCCTTGGCTATCTTGATGACCCAAGTGAGGACATTC
AGGATCCAGTGAGTGACAAATTCTTCAAGGAGGTGTGGGTTTCAACAGCAGCTCGAAATG
CTACAATTTATGACAAGGTTTTCCGGTGCCTTCCCAATGATGAAGTACACAATTTAATTC
AGCTGAGAGACTTTATAAACAAGCCCGTATTAGCTAAGGAAGATCCCATTCGAGCTGAGG
AGGAACTGAAGAAGATCCGTGGATTTTTGGTGCAATTCCCCTTTTATTTCTTGTCTGAAG
AAAGCCTACTGCCTTCTGTTGGGACCAAAGAGGCCATAGTGCCCATGGAGGTTTGGACTT
AA
Enzyme 50 GenBank Gene ID AB209907 Link Image
Enzyme 50 GeneCard ID Q59EA4 Link Image
Enzyme 50 GenAtlas ID Not Available
Enzyme 50 HGNC ID HGNC:9067 Link Image
Enzyme 50 Chromosome Location Not Available
Enzyme 50 Locus Not Available
Enzyme 50 SNPs Not Available
Enzyme 50 General References Not Available
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 15287
Enzyme 51 Name 1-acylglycerol-3-phosphate O-acyltransferase 1 (Lysophosphatidic acid acyltransferase, alpha) (1-acylglycerol-3-phosphate O-acyltransferase 1 (Lysophosphatidic acid acyltransferase, alpha), isoform CRA_b)
Enzyme 51 Synonyms Not Available
Enzyme 51 Gene Name AGPAT1
Enzyme 51 Protein Sequence >1-acylglycerol-3-phosphate O-acyltransferase 1 (Lysophosphatidic acid acyltransferase, alpha) (1-acylglycerol-3-phosphate O-acyltransferase 1 (Lysophosphatidic acid acyltransferase, alpha), isoform CRA_b) 
MDLWPGAWMLLLLLFLLLLFLLPTLWFCSPSAKYFFKMAFYNGWILFLAVLAIPVCAVRG
RNVENMKILRLMLLHIKYLYGIRVEVRGAHHFPPSQPYVVVSNHQSSLDLLGMMEVLPGR
CVPIAKRELLWAGSAGLACWLAGVIFIDRKRTGDAISVMSEVAQTLLTQDVRVWVFPEGT
RNHNGSMLPFKRGAFHLAVQAQVPIVPIVMSSYQDFYCKKERRFTSGQCQVRVLPPVPTE
GLTPDDVPALADRVRHSMLTVFREISTDGRGGGDYLKKPGGGG
Enzyme 51 Number of Residues 283
Enzyme 51 Molecular Weight 31717
Enzyme 51 Theoretical pI 9.75
Enzyme 51 GO Classification
Function
  • 1-acylglycerol-3-phosphate O-acyltransferase activity
  • O-acyltransferase activity
  • acylglycerol O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid biosynthesis
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
  • cell
  • membrane
Enzyme 51 General Function Lipid transport and metabolism
Enzyme 51 Specific Function Not Available
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions Not Available
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • None
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 123209920 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID A2BFI5 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name A2BFI5_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >852 bp 
ATGGATTTGTGGCCAGGGGCATGGATGCTGCTGCTGCTGCTCTTCCTGCTGCTGCTCTTC
CTGCTGCCCACCCTGTGGTTCTGCAGCCCCAGTGCCAAGTACTTCTTCAAGATGGCCTTC
TACAATGGCTGGATCCTCTTCCTGGCTGTGCTCGCCATCCCTGTGTGTGCCGTGCGAGGA
CGCAACGTCGAGAACATGAAGATCTTGCGTCTAATGCTGCTCCACATCAAATACCTGTAC
GGGATCCGAGTGGAGGTGCGAGGGGCTCACCACTTCCCTCCCTCGCAGCCCTATGTTGTT
GTCTCCAACCACCAGAGCTCTCTCGATCTGCTTGGGATGATGGAGGTACTGCCAGGCCGC
TGTGTGCCCATTGCCAAGCGCGAGCTACTGTGGGCTGGCTCTGCCGGGCTGGCCTGCTGG
CTGGCAGGAGTCATCTTCATCGACCGGAAGCGCACGGGGGATGCCATCAGTGTCATGTCT
GAGGTCGCCCAGACCCTGCTCACCCAGGACGTGAGGGTCTGGGTGTTTCCTGAGGGAACG
AGAAACCACAATGGCTCCATGCTGCCCTTCAAACGTGGCGCCTTCCATCTTGCAGTGCAG
GCCCAGGTTCCCATTGTCCCCATAGTCATGTCCTCCTACCAAGACTTCTACTGCAAGAAG
GAGCGTCGCTTCACCTCGGGACAATGTCAGGTGCGGGTGCTGCCCCCAGTGCCCACGGAA
GGGCTGACACCAGATGACGTCCCAGCTCTGGCTGACAGAGTCCGGCACTCCATGCTCACT
GTTTTCCGGGAAATCTCCACTGATGGCCGGGGTGGTGGTGACTATCTGAAGAAGCCTGGG
GGCGGTGGGTGA
Enzyme 51 GenBank Gene ID BX284686 Link Image
Enzyme 51 GeneCard ID A2BFI5 Link Image
Enzyme 51 GenAtlas ID Not Available
Enzyme 51 HGNC ID Not Available
Enzyme 51 Chromosome Location Not Available
Enzyme 51 Locus Not Available
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 General References Not Available
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 15288
Enzyme 52 Name Testis spermatogenesis apoptosis-related protein 7 (1-acylglycerol-3- phosphate O-acyltransferase 6 (Lysophosphatidic acid acyltransferase, zeta), isoform CRA_b)
Enzyme 52 Synonyms Not Available
Enzyme 52 Gene Name AGPAT6
Enzyme 52 Protein Sequence >Testis spermatogenesis apoptosis-related protein 7 (1-acylglycerol-3- phosphate O-acyltransferase 6 (Lysophosphatidic acid acyltransferase, zeta), isoform CRA_b) 
MFLLLPFDSLIVNLLGISLTVLFTLLLVFIIVPAIFGVSFGIRKLYMKSLLKIFAWATLR
MERGAKEKNHQLYKPYTNGIIAKDPTSLEEEIKEIRRSGSSKALDNTPEFELSDIFYFCR
KGMETIMDDEVTKRFSAEELESWNLLSRTNYNFQYISLRLTVLWGLGVLIRYCFLLPLRI
ALAFTGISLLVVGTTVVGYLPNGRFKEFMSKHVHLMCYRICVRALTAIITYHDRENRPRN
GGICVANHTSPIDVIILASDGYYAMVGQVHGGLMGVIQRAMVKACPHVWFERSEVKDRHL
VAKRLTEHVQDKSKLPILIFPEGTCINNTSVMMFKKGSFEIGATVYPVAIKYDPQFGDAF
WNSSKYGMVTYLLRMMTSWAIVCSVWYLPPMTREADEDAVQFANRVKSAIARQGGLVDLL
WDGGLKREKVKDTFKEEQQKLYSKMIVGNHKDRSRS
Enzyme 52 Number of Residues 456
Enzyme 52 Molecular Weight 52072
Enzyme 52 Theoretical pI 9.56
Enzyme 52 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 52 General Function Not Available
Enzyme 52 Specific Function Not Available
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions Not Available
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 46241188 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID Q2TU73 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name Q2TU73_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >1371 bp 
ATGTTCCTGTTGCTGCCTTTTGATAGCCTGATTGTCAACCTTCTGGGCATCTCCCTGACT
GTCCTCTTCACCCTCCTTCTCGTTTTCATCATAGTGCCAGCCATTTTTGGAGTCTCCTTT
GGTATCCGCAAACTCTACATGAAAAGTCTGTTAAAAATCTTTGCGTGGGCTACCTTGAGA
ATGGAGCGAGGAGCCAAGGAGAAGAACCACCAGCTTTACAAGCCCTACACCAACGGAATC
ATTGCAAAGGATCCCACTTCACTAGAAGAAGAGATCAAAGAGATTCGTCGAAGTGGTAGT
AGTAAGGCTCTGGACAACACTCCAGAGTTCGAGCTCTCTGACATTTTCTACTTTTGCCGG
AAAGGAATGGAGACCATTATGGATGATGAGGTGACAAAGAGATTCTCAGCAGAAGAACTG
GAGTCCTGGAACCTGCTGAGCAGAACCAATTATAACTTCCAGTACATCAGCCTTCGGCTC
ACGGTCCTGTGGGGGTTAGGAGTGCTGATTCGGTACTGCTTTCTGCTGCCGCTCAGGATA
GCACTGGCTTTCACAGGGATTAGCCTTCTGGTGGTGGGCACAACTGTGGTGGGATACTTG
CCAAATGGGAGGTTTAAGGAGTTCATGAGTAAACATGTTCACTTAATGTGTTACCGGATC
TGCGTGCGAGCGCTGACAGCCATCATCACCTACCATGACAGGGAAAACAGACCAAGAAAT
GGTGGCATCTGTGTGGCCAATCATACCTCACCGATCGATGTGATCATCTTGGCCAGCGAT
GGCTATTATGCCATGGTGGGTCAAGTGCACGGGGGACTCATGGGTGTGATTCAGAGAGCC
ATGGTGAAGGCCTGCCCACACGTCTGGTTTGAGCGCTCGGAAGTGAAGGATCGCCACCTG
GTGGCTAAGAGACTGACTGAACATGTGCAAGATAAAAGCAAGCTGCCTATCCTCATCTTC
CCAGAAGGAACCTGCATCAATAATACATCGGTGATGATGTTCAAAAAGGGAAGTTTTGAA
ATTGGAGCCACAGTTTACCCTGTTGCTATCAAGTATGACCCTCAATTTGGCGATGCCTTC
TGGAACAGCAGCAAATACGGGATGGTGACGTACCTGCTGCGAATGATGACCAGCTGGGCC
ATTGTCTGCAGCGTGTGGTACCTGCCTCCCATGACTAGAGAGGCAGATGAAGATGCTGTC
CAGTTTGCGAATAGGGTGAAATCTGCCATTGCCAGGCAGGGAGGACTTGTGGACCTGCTG
TGGGATGGGGGCCTGAAGAGGGAGAAGGTGAAGGACACGTTCAAGGAGGAGCAGCAGAAG
CTGTACAGCAAGATGATCGTGGGGAACCACAAGGACAGGAGCCGCTCCTGA
Enzyme 52 GenBank Gene ID AY513610 Link Image
Enzyme 52 GeneCard ID Q2TU73 Link Image
Enzyme 52 GenAtlas ID AGPAT6 Link Image
Enzyme 52 HGNC ID HGNC:20880 Link Image
Enzyme 52 Chromosome Location Not Available
Enzyme 52 Locus Not Available
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References Not Available
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 15289
Enzyme 53 Name Lysocardiolipin acyltransferase (Uncharacterized protein LYCAT)
Enzyme 53 Synonyms Not Available
Enzyme 53 Gene Name LYCAT
Enzyme 53 Protein Sequence >Lysocardiolipin acyltransferase (Uncharacterized protein LYCAT) 
MVSWKGIYFILTLFWGSFFGSIFMLSPFLPLMFVNPSWYRWINNRLVATWLTLPVALLET
MFGVKVIITGDAFVPGERSVIIMNHRTRMDWMFLWNCLMRYSYLRLEKICLKASLKGVPG
FGWAMQAAAYIFIHRKWKDDKSHFEDMIDYFCDIHEPLQLLIFPEGTDLTENSKSRSNAF
AEKNGLQKYEYVLHPRTTGFTFVVDRLREGKNLDAVHDITVAYPHNIPQSEKHLLQGDFP
REIHFHVHRYPIDTLPTSKEDLQLWCHKRWEEKEERLRSFYQGEKNFYFTGQSVIPPCKS
ELRVLVVKLLSILYWTLFSPAMCLLIYLYSLVKWYFIITIVIFVLQERIFGGLEIIELAC
YRLLHKQPHLNSKKNE
Enzyme 53 Number of Residues 376
Enzyme 53 Molecular Weight 44562
Enzyme 53 Theoretical pI 8.76
Enzyme 53 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 53 General Function Lipid transport and metabolism
Enzyme 53 Specific Function Not Available
Enzyme 53 Pathways Not Available
Enzyme 53 Reactions Not Available
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein Not Available
Enzyme 53 UniProtKB/Swiss-Prot ID A6H8Z7 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name A6H8Z7_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence Not Available
Enzyme 53 GenBank Gene ID AC132154 Link Image
Enzyme 53 GeneCard ID A6H8Z7 Link Image
Enzyme 53 GenAtlas ID LYCAT Link Image
Enzyme 53 HGNC ID HGNC:26756 Link Image
Enzyme 53 Chromosome Location Not Available
Enzyme 53 Locus Not Available
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 15290
Enzyme 54 Name Diacylglycerol kinase, beta 90kDa (Diacylglycerol kinase, beta 90kDa, isoform CRA_b)
Enzyme 54 Synonyms Not Available
Enzyme 54 Gene Name DGKB
Enzyme 54 Protein Sequence >Diacylglycerol kinase, beta 90kDa (Diacylglycerol kinase, beta 90kDa, isoform CRA_b) 
MTNQEKWAHLSPSEFSQLQKYAEYSTKKLKDVLEEFHGNGVLAKYNPEGKQDILNQTIDF
EGFKLFMKTFLEAELPDDFTAHLFMSFSNKFPHSSPMVKSKPALLSGGLRMNKGAITPPR
TTSPANTCSPEVIHLKDIVCYLSLLERGRPEDKLEFMFRLYDTDGNGFLDSSELENIISQ
MMHVAEYLEWDVTELNPILHEMMEEIDYDHDGTVSLEEWIQGGMTTIPLLVLLGLENNVK
DDGQHVWRLKHFNKPAYCNLCLNMLIGVGKQGLCCSFCKYTVHERCVARAPPSCIKTYVK
SKRNTDVMHHYWVEGNCPTKCDKCHKTVKCYQGLTGLHCVWCQITLHNKCASHLKPECDC
GPLKDHILPPTTICPVVLQTLPTSGVSVPEERQSTVKKEKSGSQQPNKVIDKNKMQRANS
VTVDGQGLQVTPVPGTHPLLVFVNPKSGGKQGERIYRKFQYLLNPRQVYSLSGNGPMPGL
NFFRDVPDFRVLACGGDGTVGWVLDCIEKANVGKHPPVAILPLGTGNDLARCLRWGGGYE
GENLMKILKDIENSTEIMLDRWKFEVIPNDKDEKGDPVPYSIINNYFSIGVDASIAHRFH
IMREKHPEKFNSRMKNKFWYFEFGTSETFSATCKKLHESVEIECDGVQIDLINISLEGIA
ILNIPSMHGGSNLWGESKKRRSHRRIEKKGSDKRTTVTDAKELKFASQDLSDQLLEVVGL
EGAMEMGQIYTGLKSAGRRLAQCSCVVIRTSKSLPMQIDGEPWMQTPCTIKITHKNQAPM
LMGPPPKTGLFCSLVKRTRNRSKE
Enzyme 54 Number of Residues 804
Enzyme 54 Molecular Weight 90596
Enzyme 54 Theoretical pI 7.90
Enzyme 54 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • diacylglycerol kinase activity
  • ion binding
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 54 General Function Not Available
Enzyme 54 Specific Function Not Available
Enzyme 54 Pathways Not Available
Enzyme 54 Reactions Not Available
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • None
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein Not Available
Enzyme 54 UniProtKB/Swiss-Prot ID A4D116 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name A4D116_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence Not Available
Enzyme 54 GenBank Gene ID CH236948 Link Image
Enzyme 54 GeneCard ID A4D116 Link Image
Enzyme 54 GenAtlas ID Not Available
Enzyme 54 HGNC ID Not Available
Enzyme 54 Chromosome Location Not Available
Enzyme 54 Locus Not Available
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 15291
Enzyme 55 Name Diacylglycerol kinase, theta 110kDa
Enzyme 55 Synonyms Not Available
Enzyme 55 Gene Name DGKQ
Enzyme 55 Protein Sequence >Diacylglycerol kinase, theta 110kDa 
MAAAAEPGARAWLGGGSPRPGSPACSLVLGSGGRARPGPGPGPGPERAGVRAPGPAAAPG
HSFRKVTLTKPTFCHLCSDFIWGLAGFLCDVCNFMSHEKCLKHVRIPCTSVAPSLVRVPV
AHCFGPRGLHKRKFCAVCRKVLEAPALHCEVCELHLHPDCVPFACSDCRQCHQDGHQDHD
THHHHWREGNLPSGARCEVCRKTCGSSDVLAGVRCEWCGVQAHSLCSAALAPECGFGRLR
SLVLPPACVRLLPGGFSKTQSFRIVEAAEPGEGGDGADGSAAVGPGRETQATPESGKQTL
KIFDGDDAVRRSQFRLVTVSRLAGAEEVLEAALRAHHIPEDPGHLELCRLPPSSQACDAW
AGGKAGSAVISEEGRSPGSGEATPEAWVIRALPRAQEVLKIYPGWLKVGVAYVSVRVTPK
STARSVVLEVLPLLGRQAESPESFQLVEVAMGCRHVQRTMLMDEQPLLDRLQDIRQMSVR
QVSQTRFYVAESRDVAPHVSLFVGGLPPGLSPEEYSSLLHEAGATKATVVSVSHIYSSQG
AVVLDVACFAEAERLYMLLKDMAVRGRLLTALVLPDLLHAKLPPDSCPLLVFVNPKSGGL
KGRDLLCSFRKLLNPHQVFDLTNGGPLPGLHLFSQVPCFRVLVCGGDGTVGWVLGALEET
RYRLACPEPSVAILPLGTGNDLGRVLRWGAGYSGEDPFSVLLSVDEADAVLMDRWTILLD
AHEAGSAENDTADAEPPKIVQMSNYCGIGIDAELSLDFHQAREEEPGKFTSRLHNKGVYV
RVGLQKISHSRSLHKQIRLQVERQEVELPSIEGLIFINIPSWGSGADLWGSDSDTRFEKP
RMDDGLLEVVGVTGVVHMGQVQGGLRSGIRIAQGSYFRVTLLKATPVQVDGEPWVQAPGH
MIISAAGPKVHMLRKAKQKPRRAGTTRDARADAAPAPESDPR
Enzyme 55 Number of Residues 942
Enzyme 55 Molecular Weight 101172
Enzyme 55 Theoretical pI 7.50
Enzyme 55 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 55 General Function Not Available
Enzyme 55 Specific Function Not Available
Enzyme 55 Pathways Not Available
Enzyme 55 Reactions Not Available
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • None
Enzyme 55 Transmembrane Regions
  • None
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 39645110 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID Q6P3W4 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name Q6P3W4_HUMAN Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >2829 bp 
ATGGCGGCGGCGGCCGAGCCCGGGGCCCGCGCCTGGCTGGGCGGCGGCTCCCCGCGCCCC
GGCAGCCCGGCCTGCAGCCTCGTGCTGGGCTCAGGAGGCCGCGCGCGCCCGGGGCCGGGG
CCGGGGCCGGGACCCGAGCGGGCGGGCGTCAGAGCCCCGGGCCCCGCTGCCGCGCCGGGA
CACAGCTTCCGGAAGGTGACGCTCACCAAGCCCACCTTCTGCCACCTCTGCTCCGACTTC
ATCTGGGGGCTGGCCGGCTTCCTGTGCGACGTCTGCAATTTCATGTCTCATGAGAAGTGC
CTGAAGCACGTGAGGATCCCGTGCACGAGTGTGGCACCCAGCCTGGTCCGGGTTCCTGTA
GCCCACTGCTTCGGCCCCCGGGGGCTCCACAAGCGCAAGTTCTGTGCTGTCTGCCGCAAG
GTCCTGGAGGCACCGGCGCTCCACTGCGAAGTGTGTGAGCTGCACCTCCACCCAGACTGT
GTGCCCTTCGCCTGCAGTGACTGCCGCCAGTGCCACCAGGATGGGCACCAGGATCACGAC
ACCCATCACCACCACTGGCGGGAGGGGAACCTGCCCTCGGGAGCGCGCTGCGAGGTCTGC
AGGAAGACGTGCGGCTCCTCTGACGTGCTGGCCGGCGTGCGCTGCGAGTGGTGCGGGGTC
CAGGCGCACTCCCTCTGCTCCGCGGCACTGGCTCCCGAGTGTGGCTTCGGGCGTCTGCGC
TCCCTGGTCCTGCCTCCCGCGTGCGTGCGCCTTCTGCCCGGCGGCTTCAGCAAGACGCAG
AGCTTCCGCATCGTGGAGGCCGCGGAGCCGGGCGAGGGGGGCGACGGCGCCGACGGGAGC
GCTGCCGTGGGTCCAGGCAGAGAGACACAGGCAACTCCGGAGTCCGGGAAGCAAACGCTG
AAGATCTTTGATGGCGACGACGCGGTGAGAAGAAGCCAGTTCCGCCTCGTCACGGTGTCC
CGCCTGGCCGGTGCCGAGGAGGTGCTGGAGGCCGCACTGCGGGCCCACCACATCCCCGAG
GACCCTGGCCACCTGGAGCTGTGCCGGCTGCCCCCTTCCTCTCAGGCCTGTGACGCCTGG
GCTGGGGGCAAGGCTGGGAGTGCTGTGATCTCGGAGGAGGGCAGAAGCCCCGGGTCCGGC
GAGGCCACGCCAGAGGCCTGGGTCATCCGGGCTCTGCCGCGGGCCCAGGAGGTCCTGAAG
ATCTACCCTGGCTGGCTCAAGGTGGGCGTGGCCTACGTGTCCGTGCGAGTGACCCCGAAG
AGCACGGCCCGCTCTGTGGTGCTGGAGGTCCTGCCGCTGCTCGGCCGCCAGGCCGAGAGT
CCCGAGAGCTTCCAGCTGGTGGAGGTGGCGATGGGCTGCAGGCACGTCCAGCGGACGATG
CTGATGGACGAACAGCCCCTGCTGGACCGGCTACAGGACATCCGGCAGATGTCTGTGCGG
CAGGTGAGCCAGACGCGGTTCTACGTGGCAGAGAGCAGGGATGTAGCCCCGCACGTCTCC
CTGTTTGTTGGCGGCCTGCCTCCCGGCCTGTCTCCCGAGGAGTACAGCAGCCTGCTGCAT
GAGGCCGGGGCTACCAAAGCCACCGTGGTGTCCGTGAGTCACATCTACTCCTCCCAAGGC
GCGGTAGTGTTGGACGTTGCCTGCTTTGCGGAGGCCGAGCGGCTGTACATGCTGCTGAAG
GACATGGCTGTGCGGGGCCGGCTGCTCACTGCCCTGGTGCTCCCCGACCTGCTGCACGCG
AAGCTGCCCCCAGACAGCTGTCCCCTCCTTGTGTTCGTGAACCCCAAGAGTGGAGGCCTC
AAGGGCCGAGACCTGCTCTGCAGCTTCCGGAAGCTACTGAACCCTCATCAGGTCTTCGAC
CTGACCAACGGAGGTCCTCTTCCCGGGCTCCACCTGTTCTCCCAGGTGCCCTGCTTCCGG
GTGCTGGTGTGTGGTGGCGATGGCACTGTGGGCTGGGTGCTTGGCGCCCTGGAGGAGACA
CGGTACCGACTGGCCTGCCCGGAGCCTTCTGTGGCCATCCTGCCCCTGGGCACAGGGAAT
GACCTTGGTCGAGTCCTCCGCTGGGGGGCGGGCTACAGCGGCGAGGACCCGTTCTCCGTA
CTGCTGTCTGTGGACGAGGCCGACGCCGTGCTCATGGACCGCTGGACCATCCTGCTGGAT
GCCCACGAGGCTGGCAGTGCAGAGAACGACACGGCAGACGCAGAGCCCCCCAAGATCGTG
CAGATGAGTAACTACTGTGGCATTGGCATCGACGCGGAGCTGAGCCTGGACTTCCACCAG
GCACGGGAAGAGGAGCCTGGCAAGTTCACAAGCAGGCTGCACAACAAGGGTGTGTACGTG
CGGGTGGGGCTGCAGAAGATCAGTCACTCTCGGAGCCTGCACAAGCAGATCCGGCTGCAG
GTGGAGCGGCAGGAGGTGGAGCTGCCCAGTATTGAAGGCCTCATCTTCATCAACATCCCC
AGCTGGGGCTCGGGGGCCGACCTGTGGGGCTCCGACAGCGACACCAGGTTTGAGAAGCCA
CGCATGGACGACGGGCTGCTGGAGGTTGTGGGCGTGACGGGCGTCGTGCACATGGGCCAG
GTCCAGGGTGGGCTGCGCTCCGGAATCCGGATTGCCCAGGGTTCCTACTTCCGAGTCACG
CTCCTCAAGGCCACCCCGGTGCAGGTGGACGGGGAGCCCTGGGTCCAGGCCCCGGGGCAC
ATGATCATCTCAGCTGCTGGCCCTAAGGTGCACATGCTGAGGAAGGCCAAGCAGAAGCCG
AGGAGGGCCGGGACCACCAGGGATGCCCGGGCGGATGCTGCGCCTGCCCCTGAGAGCGAT
CCTAGGTAG
Enzyme 55 GenBank Gene ID BC063801 Link Image
Enzyme 55 GeneCard ID Q6P3W4 Link Image
Enzyme 55 GenAtlas ID DGKQ Link Image
Enzyme 55 HGNC ID HGNC:2856 Link Image
Enzyme 55 Chromosome Location Not Available
Enzyme 55 Locus Not Available
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 15292
Enzyme 56 Name Diacylglycerol kinase, epsilon 64kDa (cDNA FLJ75840, highly similar to Homo sapiens diacylglycerol kinase, epsilon 64kDa (DGKE), mRNA)
Enzyme 56 Synonyms Not Available
Enzyme 56 Gene Name DGKE
Enzyme 56 Protein Sequence >Diacylglycerol kinase, epsilon 64kDa (cDNA FLJ75840, highly similar to Homo sapiens diacylglycerol kinase, epsilon 64kDa (DGKE), mRNA) 
MEAERRPAPGSPSEGLFADGHLILWTLCSVLLPVFITFWCSLQRSRRQLHRRDIFRKSKH
GWRDTDLFSQPTYCCVCAQHILQGAFCDCCGLRVDEGCLRKADKRFQCKEIMLKNDTKVL
DAMPHHWIRGNVPLCSYCMVCKQQCGCQPKLCDYRCIWCQKTVHDECMKNSLKNEKCDFG
EFKNLIIPPSYLTSINQMRKDKKTDYEVLASKLGKQWTPLIILANSRSGTNMGEGLLGEF
RILLNPVQVFDVTKTPPIKALQLCTLLPYYSARVLVCGGDGTVGWVLDAVDDMKIKGQEK
YIPQVAVLPLGTGNDLSNTLGWGTGYAGEIPVAQVLRNVMEADGIKLDRWKVQVTNKGYY
NLRKPKEFTMNNYFSVGPDALMALNFHAHREKAPSLFSSRILNKAVYLFYGTKDCLVQEC
KDLNKKVELELDGERVALPSLEGIIVLNIGYWGGGCRLWEGMGDETYPLARHDDGLLEVV
GVYGSFHCAQIQVKLANPFRIGQAHTVRLILKCSMMPMQVDGEPWAQGPCTVTITHKTHA
MMLYFSGEQTDDDISSTSDQEDIKATE
Enzyme 56 Number of Residues 567
Enzyme 56 Molecular Weight 63928
Enzyme 56 Theoretical pI 7.78
Enzyme 56 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • diacylglycerol kinase activity
  • electron transporter activity
  • ion binding
  • iron ion binding
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • transporter activity
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular metabolism
  • cellular process
  • electron transport
  • generation of precursor metabolites and energy
  • intracellular signaling cascade
  • metabolism
  • physiological process
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 56 General Function Not Available
Enzyme 56 Specific Function Not Available
Enzyme 56 Pathways Not Available
Enzyme 56 Reactions Not Available
Enzyme 56 Pfam Domain Function
Enzyme 56 Signals
  • None
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein 120659970 Link Image
Enzyme 56 UniProtKB/Swiss-Prot ID A1L4Q0 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name A1L4Q0_HUMAN Link Image
Enzyme 56 PDB ID Not Available
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence >1704 bp 
ATGGAAGCGGAGAGGCGGCCGGCGCCGGGCTCGCCCTCCGAGGGCCTGTTTGCGGACGGG
CACCTGATCTTGTGGACGCTGTGCTCGGTCCTGCTGCCGGTGTTCATCACCTTCTGGTGT
AGCCTCCAGCGGTCGCGCCGGCAGCTGCACCGCAGGGACATCTTCCGCAAGAGCAAGCAC
GGGTGGCGCGACACGGACCTGTTCAGCCAGCCCACCTACTGCTGCGTGTGCGCGCAGCAC
ATTCTGCAGGGCGCCTTCTGCGACTGCTGCGGGCTCCGCGTGGACGAGGGCTGCCTCAGG
AAGGCCGACAAGCGCTTCCAGTGCAAGGAGATTATGCTCAAGAATGACACCAAGGTCCTG
GACGCCATGCCCCACCACTGGATCCGGGGCAACGTGCCCCTGTGCAGTTACTGTATGGTT
TGCAAGCAGCAGTGTGGCTGTCAACCCAAGCTTTGCGATTACAGGTGCATTTGGTGCCAG
AAAACAGTACATGATGAGTGCATGAAAAATAGTTTAAAGAATGAAAAATGTGATTTTGGA
GAATTCAAAAACCTAATCATTCCACCAAGTTATTTAACCTCCATTAATCAGATGCGTAAA
GACAAAAAAACAGATTATGAAGTGCTAGCCTCTAAGCTTGGAAAGCAGTGGACCCCATTA
ATAATCCTGGCCAACTCTCGTAGTGGAACTAATATGGGAGAAGGACTGTTGGGAGAATTT
AGGATCTTGTTGAATCCAGTCCAGGTTTTTGATGTAACTAAAACTCCTCCTATCAAAGCC
CTACAACTCTGTACTCTTCTCCCATATTATTCAGCTCGAGTACTTGTTTGTGGAGGGGAT
GGGACTGTAGGGTGGGTCCTGGATGCAGTTGATGACATGAAGATTAAGGGACAAGAAAAG
TACATTCCACAAGTTGCAGTTTTGCCTCTGGGAACAGGCAACGATCTATCCAATACATTG
GGTTGGGGTACAGGTTATGCTGGAGAAATTCCAGTTGCGCAGGTTTTGCGAAATGTAATG
GAAGCAGATGGAATTAAACTAGATCGATGGAAAGTTCAAGTAACAAATAAAGGATACTAC
AACTTAAGAAAACCCAAGGAATTCACAATGAACAACTATTTTTCTGTTGGACCTGATGCT
CTCATGGCTCTCAATTTTCATGCTCATCGTGAGAAGGCACCATCTCTGTTTTCTAGCAGA
ATTCTTAATAAGGCGGTTTACTTATTCTATGGAACCAAAGATTGTTTAGTGCAAGAATGT
AAAGATTTGAATAAAAAAGTTGAGCTAGAACTGGATGGTGAGCGAGTAGCACTGCCCAGC
TTGGAAGGTATTATAGTTCTGAACATCGGATACTGGGGCGGTGGCTGCAGACTATGGGAA
GGGATGGGGGACGAGACTTACCCTCTAGCCAGGCATGACGATGGTCTGCTGGAAGTCGTT
GGAGTATATGGGTCTTTCCACTGTGCTCAGATTCAAGTAAAACTGGCTAATCCTTTTCGA
ATAGGACAGGCACATACAGTGAGGCTGATTTTGAAGTGCTCCATGATGCCAATGCAGGTG
GATGGGGAGCCTTGGGCCCAAGGGCCCTGCACTGTCACCATAACTCACAAGACACATGCA
ATGATGTTATATTTCTCTGGAGAACAAACAGATGATGACATCTCTAGTACTTCGGATCAA
GAAGATATAAAGGCGACTGAATAG
Enzyme 56 GenBank Gene ID BC130629 Link Image
Enzyme 56 GeneCard ID A1L4Q0 Link Image
Enzyme 56 GenAtlas ID Not Available
Enzyme 56 HGNC ID Not Available
Enzyme 56 Chromosome Location 17
Enzyme 56 Locus 17q22
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 16477
Enzyme 57 Name cDNA, FLJ94990, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 1 (CDS1), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 1, isoform CRA_a)
Enzyme 57 Synonyms Not Available
Enzyme 57 Gene Name CDS1
Enzyme 57 Protein Sequence >cDNA, FLJ94990, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 1 (CDS1), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 1, isoform CRA_a) 
MLELRHRGSCPGPREAVSPPHREGEAAGGDHETESTSDKETDIDDRYGDLDSRTDSDIPE
IPPSSDRTPEILKKALSGLSSRWKNWWIRGILTLTMISLFFLIIYMGSFMLMLLVLGIQV
KCFHEIITIGYRVYHSYDLPWFRTLSWYFLLCVNYFFYGETVADYFATFVQREEQLQFLI
RYHRFISFALYLAGFCMFVLSLVKKHYRLQFYMFAWTHVTLLITVTQSHLVIQNLFEGMI
WFLVPISSVICNDITAYLFGFFFGRTPLIKLSPKKTWEGFIGGFFSTVVFGFIAAYVLSK
YQYFVCPVEYRSDVNSFVTECEPSELFQLQTYSLPPFLKAVLRQERVSLYPFQIHSIALS
TFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVHVYITSFIRG
PNPSKVLQQLLVLQPEQQLNIYKTLKTHLIEKGILQPTLKV
Enzyme 57 Number of Residues 461
Enzyme 57 Molecular Weight 53305
Enzyme 57 Theoretical pI 8.19
Enzyme 57 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • phosphatidate cytidylyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid biosynthesis
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
  • cell
  • membrane
Enzyme 57 General Function Lipid transport and metabolism
Enzyme 57 Specific Function Not Available
Enzyme 57 Pathways Not Available
Enzyme 57 Reactions Not Available