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Human Metabolome Database Version 2.5

 

Showing metabocard for PS(16:0/16:0) (HMDB00614)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-06-23 11:20:36
Accession Number HMDB00614
Secondary Accession Numbers Not Available
Common Name PS(16:0/16:0)
Description PS(16:0/16:0) is a phosphatidylserine (PS or GPSer). It is a glycerophospholipid in which a phosphorylserine moiety occupies a glycerol substitution site. As is the case with diacylglycerols, glycerophosphoserines 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. PS(16:0/16:0), in particular, consists of two chain of palmitic acid at the C-1 and C-2 positions. Phosphatidylserine or 1,2-diacyl-sn-glycero-3-phospho-L-serine is distributed widely among animals, plants and microorganisms. It is usually less than 10% of the total phospholipids, the greatest concentration being in myelin from brain tissue. However, it may comprise 10 to 20 mol% of the total phospholipid in the plasma membrane and endoplasmic reticulum of the cell. Phosphatidylserine is an acidic (anionic) phospholipid with three ionizable groups, i.e. the phosphate moiety, the amino group and the carboxyl function. As with other acidic lipids, it exists in nature in salt form, but it has a high propensity to chelate to calcium via the charged oxygen atoms of both the carboxyl and phosphate moieties, modifying the conformation of the polar head group. This interaction may be of considerable relevance to the biological function of phosphatidylserine, especially during bone formation for example. As phosphatidylserine is located entirely on the inner monolayer surface of the plasma membrane (and of other cellular membranes) and it is the most abundant anionic phospholipids. Therefore phosphatidylseriine may make the largest contribution to interfacial effects in membranes involving non-specific electrostatic interactions. This normal distribution is disturbed during platelet activation and cellular apoptosis. In human plasma, 1-stearoyl-2-oleoyl and 1-stearoyl-2-arachidonoyl species predominate, but in brain (especially grey matter), retina and many other tissues 1-stearoyl-2-docosahexaenoyl species are very abundant. Indeed, the ratio of n-3 to n-6 fatty acids in brain phosphatidylserine is very much higher than in most other lipids. While most phospholipids have a saturated fatty acid on C-1 and an unsaturated fatty acid on C-2 of the glycerol backbone, the fatty acid distribution at the C-1 and C-2 positions of glycerol within phospholipids is continually in flux, owing to phospholipid degradation and the continuous phospholipid remodeling that occurs while these molecules are in membranes. Phosphatidylserines typically carry a net charge of -1 at physiological pH. They mostly have palmitic or stearic acid on carbon 1 and a long chain unsaturated fatty acid (e.g. 18:2, 20:4 and 22:6) on carbon 2. PS biosynthesis involves an exchange reaction of serine for ethanolamine in PE.
Synonyms
  1. Phosphatidylserine (16:0/16:0)
  2. PSer(16:0/16:0)
  3. PS(32:0)
  4. Phosphatidylserine (32:0)
  5. PSer(32:0)
  6. 1,2-Dipalmitoylglycerophosphorylserine
  7. 1,2-Dipalmitoylphosphatidylserine
  8. DL-a-Dipalmitoyl phosphatidyl-L-serine
  9. DPPS
  10. Dipalmitoyl-DL-a-phosphatidyl-L-serine
  11. Dipalmitoylglycerophosphoserine
  12. Dipalmitoylphosphatidylserine
  13. DL-alpha-Dipalmitoyl phosphatidyl-L-serine
  14. Dipalmitoyl-DL-alpha-phosphatidyl-L-serine
Chemical IUPAC Name (2S)-2-amino-3-[2,3-di(hexadecanoyloxy)propoxy-hydroxyphosphoryl]oxypropanoic acid
Chemical Formula C38H74NO10P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Lipids
Class
  • Phospholipids
Sub Class
  • Phosphatidylserines
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • carboxylic acid ester
  • phosphoric acid ester
  • alpha-aminoacid
Biofunction
  • Membrane component
Application
—
Source
  • Endogenous
Average Molecular Weight 735.969
Monoisotopic Molecular Weight 735.505005
Isomeric SMILES CCCCCCCCCCCCCCCC(=O)OCC(COP(O)(=O)OC[C@H](N)C(O)=O)OC(=O)CCCCCCCCCCCCCCC
Canonical SMILES CCCCCCCCCCCCCCCC(=O)OCC(COP(O)(=O)OCC(N)C(O)=O)OC(=O)CCCCCCCCCCCCCCC
KEGG Compound ID C02737 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB00614 Link Image
Metagene Link HMDB00614 Link Image
METLIN ID 5587 Link Image
PubChem Compound 3081382 Link Image
PubChem Substance 14714345 Link Image
ChEBI ID Not Available
CAS Registry Number 3036-82-6
InChI Identifier InChI=1/C38H74NO10P/c1-3-5-7-9-11-13-15-17-19-21-23-25-27-29-36(40)46-31-34(32-47-50(44,45)48-33-35(39)38(42)43)49-37(41)30-28-26-24-22-20-18-16-14-12-10-8-6-4-2/h34-35H,3-33,39H2,1-2H3,(H,42,43)(H,44,45)/t34?,35-/m0/s1
Synthesis Reference Hermetter, A.; Paltauf, F.; Hauser, H. Synthesis of diacyl and alkylacyl glycerophosphoserines. Chemistry and Physics of Lipids (1982), 30(1), 35-45.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.05e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 4.32 [Predicted by ALOGPS]; 8 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
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
Phospholipid Biosynthesis SMP00025 Link Image map00564 Link Image
General References
  1. Chen S: Partial characterization of the molecular species of phosphatidylserine from human plasma by high-performance liquid chromatography and fast atom bombardment mass spectrometry. J Chromatogr B Biomed Appl. 1994 Nov 4;661(1):1-5. [PubMed Link Image]
  2. Thompson JA, Miles BS, Fennessey PV: Urinary organic acids quantitated by age groups in a healthy pediatric population. Clin Chem. 1977 Sep;23(9):1734-8. [PubMed Link Image]
  3. Gao F, Tian X, Wen D, Liao J, Wang T, Liu H: Analysis of phospholipid species in rat peritoneal surface layer by liquid chromatography/electrospray ionization ion-trap mass spectrometry. Biochim Biophys Acta. 2006 Jul;1761(7):667-76. Epub 2006 Apr 24. [PubMed Link Image]
Metabolic Enzymes
  1. Group 10 secretory phospholipase A2 precursor
  2. Diacylglycerol kinase gamma
  3. Diacylglycerol kinase alpha
  4. Diacylglycerol kinase delta
  5. Diacylglycerol kinase beta
  6. Protein kinase C alpha type
  7. Probable phospholipid-transporting ATPase IA
  8. Phospholipid scramblase 1
  9. Phosphatidylserine synthase 1
  10. Scavenger receptor class B member 1
  11. Small inducible cytokine B16 precursor
  12. Phosphatidylserine decarboxylase proenzyme
  13. JmjC domain-containing protein 6
  14. Phosphatidylserine synthase 2
  15. 2-acylglycerol O-acyltransferase 2
  16. Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing alpha polypeptide
  17. Inositol polyphosphate 5-phosphatase
  18. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
  19. Sphingomyelin phosphodiesterase 3
  20. Phospholipid scramblase 2
  21. Phospholipid scramblase 3
  22. Phospholipid scramblase 4
  23. Phospholipid scramblase family memmber 5
  24. Phospholipase A1 member A precursor
  25. Serum deprivation-response protein
  26. Transcriptional regulator ATRX
  27. Copine-1
  28. Cdc42-interacting protein 4
  29. Formin-binding protein 1-like
  30. Formin-binding protein 1
  31. Sphingomyelin phosphodiesterase 4
  32. Serine incorporator 1
  33. Protein kinase C delta-binding protein
  34. Annexin A9
  35. Phosphatidylserine receptor transcript variant 2
  36. cDNA FLJ38589 fis, clone HCHON2010074, highly similar to LACTADHERIN
  37. Putative uncharacterized protein DKFZp686M1886
  38. Serine incorporator 5
  39. Adseverin
  40. Serine incorporator 4
  41. Phosphatidylserine receptor transcript variant 1 (Phosphatidylserine receptor, isoform CRA_d)
  42. cDNA, FLJ94904, Homo sapiens copine VI (neuronal) (CPNE6), mRNA (Copine VI (Neuronal), isoform CRA_c)
  43. cDNA FLJ59612, highly similar to Lactadherin
  44. cDNA FLJ43205 fis, clone FEBRA2009185, highly similar to Copine-6
Enzyme 1 [top]
Enzyme 1 ID 5292
Enzyme 1 Name Group 10 secretory phospholipase A2 precursor
Enzyme 1 Synonyms
  1. Group X secretory phospholipase A2
  2. Phosphatidylcholine 2-acylhydrolase GX
  3. GX sPLA2
  4. sPLA2-X
Enzyme 1 Gene Name PLA2G10
Enzyme 1 Protein Sequence >Group 10 secretory phospholipase A2 precursor 
MLLLLLPSLLLLLLLPGPGSGEASRILRVHRRGILELAGTVGCVGPRTPIAYMKYGCFCG
LGGHGQPRDAIDWCCHGHDCCYTRAEEAGCSPKTERYSWQCVNQSVLCGPAENKCQELLC
KCDQEIANCLAQTEYNLKYLFYPQFLCEPDSPKCD
Enzyme 1 Number of Residues 155
Enzyme 1 Molecular Weight 17132
Enzyme 1 Theoretical pI 6.46
Enzyme 1 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. Prefers phosphatidylethanolamine and phosphatidylcholine liposomes to those of phosphatidylserine
Enzyme 1 Pathways
Enzyme 1 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-21
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 2289237 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O15496 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PA2GX_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >498 bp 
ATGGGGCCGCTACCTGTGTGCCTGCCAATCATGCTGCTCCTGCTACTGCCGTCGCTGCTG
CTGCTGCTGCTTCTACCTGGCCCCGGGTCCGGCGAGGCCTCCAGGATATTACGTGTGCAC
CGGCGTGGGATCCTGGAACTGGCAGGAACTGTGGGTTGTGTTGGTCCCCGAACCCCCATC
GCCTATATGAAATATGGTTGCTTTTGTGGCTTGGGAGGCCATGGCCAGCCCCGCGATGCC
ATTGACTGGTGCTGCCATGGCCACGACTGTTGTTACACTCGAGCTGAGGAGGCCGGCTGC
AGCCCCAAGACAGAGCGCTACTCCTGGCAGTGCGTCAATCAGAGCGTCCTGTGCGGACCG
GCAGAGAACAAATGCCAAGAACTGTTGTGCAAGTGTGACCAGGAGATTGCTAACTGCTTA
GCCCAAACTGAGTACAACTTAAAGTACCTCTTCTACCCCCAGTTCCTATGTGAGCCGGAC
TCGCCCAAGTGTGACTGA
Enzyme 1 GenBank Gene ID U95301 Link Image
Enzyme 1 GeneCard ID PLA2G10 Link Image
Enzyme 1 GenAtlas ID PLA2G10 Link Image
Enzyme 1 HGNC ID HGNC:9029 Link Image
Enzyme 1 Chromosome Location 16
Enzyme 1 Locus 16p13.1-p12
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Cupillard L, Koumanov K, Mattei MG, Lazdunski M, Lambeau G: Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2. J Biol Chem. 1997 Jun 20;272(25):15745-52. [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 5465
Enzyme 3 Name Diacylglycerol kinase alpha
Enzyme 3 Synonyms
  1. Diglyceride kinase alpha
  2. DGK-alpha
  3. DAG kinase alpha
  4. 80 kDa diacylglycerol kinase
Enzyme 3 Gene Name DGKA
Enzyme 3 Protein Sequence >Diacylglycerol kinase alpha 
MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIY
LEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFK
LYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEW
VRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKY
TVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHC
VWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNL
STSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRL
FKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQ
NLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIM
REKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVL
NIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLE
GAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDVEPWMQTPCTIKITHKNQMPML
MGPPPRSTNFFGFLS
Enzyme 3 Number of Residues 735
Enzyme 3 Molecular Weight 82673
Enzyme 3 Theoretical pI 6.71
Enzyme 3 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 3 General Function Not Available
Enzyme 3 Specific Function Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 30823 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P23743 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name DGKA_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 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 3 GenBank Gene ID X62535 Link Image
Enzyme 3 GeneCard ID DGKA Link Image
Enzyme 3 GenAtlas ID DGKA Link Image
Enzyme 3 HGNC ID HGNC:2849 Link Image
Enzyme 3 Chromosome Location 12
Enzyme 3 Locus 12q13.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5466
Enzyme 4 Name Diacylglycerol kinase delta
Enzyme 4 Synonyms
  1. Diglyceride kinase delta
  2. DGK-delta
  3. DAG kinase delta
  4. 130 kDa diacylglycerol kinase
Enzyme 4 Gene Name DGKD
Enzyme 4 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 4 Number of Residues 1214
Enzyme 4 Molecular Weight 134527
Enzyme 4 Theoretical pI 7.58
Enzyme 4 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 4 General Function Not Available
Enzyme 4 Specific Function May function as signaling molecule. Isoform 2 may be involved in cell growth and tumorigenesis
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 22773821 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q16760 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name DGKD_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 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 4 GenBank Gene ID AB078966 Link Image
Enzyme 4 GeneCard ID DGKD Link Image
Enzyme 4 GenAtlas ID DGKD Link Image
Enzyme 4 HGNC ID HGNC:2851 Link Image
Enzyme 4 Chromosome Location 2
Enzyme 4 Locus 2q37.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5470
Enzyme 5 Name Diacylglycerol kinase beta
Enzyme 5 Synonyms
  1. Diglyceride kinase beta
  2. DGK-beta
  3. DAG kinase beta
  4. 90 kDa diacylglycerol kinase
Enzyme 5 Gene Name DGKB
Enzyme 5 Protein Sequence >Diacylglycerol kinase beta 
MTNQEKWAHLSPSEFSQLQKYAEYSTKKLKDVLEEFHGNGVLAKYNPEGKQDILNQTIDF
EGFKLFMKTFLEAELPDDFTAHLFMSFSNKFPHSSPMVKSKPALLSGGLRMNKGAITPPR
TTSPANTCSPEVIHLKDIVCYLSLLERGRPEDKLEFMFRLYDTDGNGFLDSSELENIISQ
MMHVAEYLEWDVTELNPILHEMMEEIDYDHDGTVSLEEWIQGGMTTIPLLVLLGLENNVK
DDGQHVWRLKHFNKPAYCNLCLNMLIGVGKQGLCCSFCKYTVHERCVARAPPSCIKTYVK
SKRNTDVMHHYWVEGNCPTKCDKCHKTVKCYQGLTGLHCVWCQITLHNKCASHLKPECDC
GPLKDHILPPTTICPVVLQTLPTSGVSVPEERQSTVKKEKSGSQQPNKVIDKNKMQRANS
VTVDGQGLQVTPVPGTHPLLVFVNPKSGGKQGERIYRKFQYLLNPRQVYSLSGNGPMPGL
NFFRDVPDFRVLACGGDGTVGWVLDCIEKANVGKHPPVAILPLGTGNDLARCLRWGGGYE
GENLMKILKDIENSTEIMLDRWKFEVIPNDKDEKGDPVPYSIINNYFSIGVDASIAHRFH
IMREKHPEKFNSRMKNKFWYFEFGTSETFSATCKKLHESVEIECDGVQIDLINISLEGIA
ILNIPSMHGGSNLWGESKKRRSHRRIEKKGSDKRTTVTDAKELKFASQDLSDQLLEVVGL
EGAMEMGQIYTGLKSAGRRLAQCSCVVIRTSKSLPMQIDGEPWMQTPCTIKITHKNQAPM
LMGPPPKTGLFCSLVKRTRNRSKE
Enzyme 5 Number of Residues 804
Enzyme 5 Molecular Weight 90596
Enzyme 5 Theoretical pI 7.90
Enzyme 5 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 5 General Function Not Available
Enzyme 5 Specific Function Exhibits high phosphorylation activity for long-chain diacylglycerols
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 10279722 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9Y6T7 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name DGKB_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2415 bp 
ATGACAAACCAGGAAAAATGGGCCCACCTCAGCCCTTCGGAATTTTCCCAACTTCAGAAA
TATGCTGAGTATTCTACAAAGAAATTAAAGGATGTTCTTGAAGAATTCCATGGTAATGGT
GTGCTTGCAAAGTATAATCCTGAAGGGAAACAAGACATTCTTAACCAAACAATAGATTTT
GAAGGTTTCAAACTATTCATGAAGACATTCCTGGAAGCCGAGCTTCCTGATGATTTCACT
GCACACCTTTTCATGTCATTTAGCAACAAGTTTCCTCATTCTAGTCCAATGGTAAAAAGT
AAGCCTGCTCTCCTATCAGGCGGTCTGAGAATGAATAAAGGTGCCATCACCCCTCCCCGA
ACTACTTCTCCTGCAAATACGTGTTCCCCAGAAGTAATCCATCTGAAGGACATTGTCTGT
TACCTGTCTCTGCTTGAAAGAGGAAGACCTGAGGATAAGCTTGAGTTTATGTTTCGCCTT
TATGACACGGATGGGAATGGCTTCCTGGACAGCTCGGAGCTAGAAAATATCATCAGTCAG
ATGATGCATGTTGCAGAATACCTTGAGTGGGATGTCACTGAACTTAATCCAATCCTCCAT
GAAATGATGGAAGAAATTGACTATGATCATGATGGAACCGTGTCTCTGGAGGAATGGATT
CAAGGAGGAATGACAACGATTCCACTTCTTGTGCTCCTGGGCTTAGAAAATAACGTGAAG
GATGATGGACAGCACGTGTGGCGACTGAAGCACTTTAACAAACCTGCCTATTGCAACCTT
TGCCTGAACATGCTGATTGGCGTGGGGAAGCAGGGCCTCTGCTGTTCCTTCTGCAAGTAC
ACAGTCCATGAGCGCTGTGTGGCTCGAGCACCTCCCTCTTGCATCAAGACCTATGTGAAG
TCCAAAAGGAACACTGATGTCATGCACCATTACTGGGTTGAAGGTAACTGCCCAACCAAG
TGTGATAAGTGCCACAAAACTGTTAAATGTTACCAGGGCCTGACAGGACTGCATTGTGTT
TGGTGTCAGATCACACTGCATAATAAATGTGCTTCTCATCTAAAACCTGAATGTGACTGT
GGACCTTTGAAGGACCATATTTTACCACCCACAACAATCTGTCCAGTGGTACTGCAGACT
CTGCCCACTTCAGGAGTTTCAGTTCCTGAGGAAAGACAATCAACAGTGAAAAAGGAAAAG
AGTGGTTCCCAGCAGCCAAACAAAGTGATTGACAAGAATAAAATGCAAAGAGCCAACTCT
GTTACTGTAGATGGACAAGGCCTGCAGGTCACTCCTGTGCCTGGTACTCACCCACTTTTA
GTTTTTGTGAACCCCAAAAGTGGTGGAAAACAAGGAGAACGAATTTACAGAAAATTCCAG
TATCTATTAAATCCTCGTCAGGTTTACAGTCTTTCTGGAAATGGACCAATGCCAGGGTTA
AACTTTTTCCGTGATGTTCCTGACTTCAGAGTGTTAGCCTGTGGTGGAGATGGAACCGTG
GGCTGGGTTTTGGATTGCATAGAAAAGGCCAATGTAGGCAAGCATCCTCCAGTTGCGATT
CTGCCTCTTGGGACTGGCAATGATCTAGCAAGATGCCTGCGATGGGGAGGAGGTTACGAA
GGTGAGAATCTGATGAAAATTCTAAAAGACATTGAAAACAGCACAGAAATCATGTTGGAC
AGGTGGAAGTTTGAAGTCATACCTAATGACAAAGATGAGAAAGGAGACCCAGTGCCTTAC
AGTATCATCAATAATTACTTTTCCATTGGCGTGGATGCCTCCATTGCACACAGATTCCAC
ATCATGAGAGAAAAACACCCAGAGAAATTCAACAGTAGAATGAAGAACAAATTTTGGTAT
TTTGAGTTTGGCACATCTGAAACTTTCTCAGCCACCTGCAAGAAGCTACATGAATCTGTA
GAAATAGAATGTGATGGAGTACAGATAGATTTAATAAACATCTCTCTGGAAGGAATTGCT
ATTTTGAATATACCAAGCATGCATGGAGGATCCAATCTTTGGGGAGAGTCTAAGAAAAGA
CGAAGCCATCGACGAATAGAGAAAAAAGGGTCTGACAAAAGGACCACCGTCACAGATGCC
AAAGAGTTGAAGTTTGCAAGTCAAGATCTCAGTGACCAGCTGCTGGAGGTGGTCGGCTTG
GAAGGAGCCATGGAGATGGGGCAAATATACACAGGCCTGAAAAGTGCTGGCCGGCGGCTG
GCTCAGTGCTCCTGCGTGGTCATCAGGACGAGCAAGTCTCTGCCAATGCAAATTGATGGG
GAGCCATGGATGCAGACCCCATGCACAATAAAAATTACACACAAGAACCAAGCCCCAATG
CTGATGGGCCCGCCTCCAAAAACCGGTTTATTCTGCTCCCTCGTCAAAAGGACAAGAAAC
CGAAGCAAGGAATAA
Enzyme 5 GenBank Gene ID AX032742 Link Image
Enzyme 5 GeneCard ID DGKB Link Image
Enzyme 5 GenAtlas ID DGKB Link Image
Enzyme 5 HGNC ID HGNC:2850 Link Image
Enzyme 5 Chromosome Location 7
Enzyme 5 Locus 7p21.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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]
  2. 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6476
Enzyme 6 Name Protein kinase C alpha type
Enzyme 6 Synonyms
  1. PKC-alpha
  2. PKC-A
Enzyme 6 Gene Name PRKCA
Enzyme 6 Protein Sequence >Protein kinase C alpha type 
MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGF
GKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGS
LLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDA
KNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRL
SVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNME
LRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKG
TEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYV
NGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIA
DFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDG
EDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTKHPAKRLGCGPEGERDVREHAFFRRI
DWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVN
PQFVHPILQSAV
Enzyme 6 Number of Residues 672
Enzyme 6 Molecular Weight 76765
Enzyme 6 Theoretical pI 7.05
Enzyme 6 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid phosphorylation
  • protein modification
  • signal transduction
Component
—
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 35483 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P17252 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name KPCA_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >2019 bp 
ATGGCTGACGTTTTCCCGGGCAACGACTCCACGGCGTCTCAGGACGTGGCCAACCGCTTC
GCCCGCAAAGGGGCGCTGAGGCAGAAGAACGTGCACGAGGTGAAGGACCACAAATTCATC
GCGCGCTTCTTCAAGCAGCCCACCTTCTGCAGCCACTGCACCGACTTCATCTGGGGGTTT
GGGAAACAAGGCTTCCAGTGCCAAGTTTGCTGTTTTGTGGTCCACAAGAGGTGCCATGAA
TTTGTTACTTTTTCTTGTCCGGGTGCGGATAAGGGACCCGACACTGATGACCCCAGGAGC
AAGCACAAGTTCAAAATCCACACTTACGGAAGCCCCACCTTCTGCGATCACTGTGGGTCA
CTGCTCTATGGACTTATCCATCAAGGGATGAAATGTGACACCTGCGATATGAACGTTCAC
AAGCAATGCGTCATCAATGTCCCCAGCCTCTGCGGAATGGATCACACTGAGAAGAGGGGG
CGGATTTACCTAAAGGCTGAGGTTGCTGATGAAAAGCTCCATGTCACAGTACGAGATGCA
AAAAATCTAATCCCTATGGATCCAAACGGGCTTTCAGATCCTTATGTGAAGCTGAAACTT
ATTCCTGATCCCAAGAATGAAAGCAAGCAAAAAACCAAAACCATCCGCTCCACACTAAAT
CCGCAGTGGAATGAGTCCTTTACATTCAAATTGAAACCTTCAGACAAAGACCGACGACTG
TCTGTAGAAATCTGGGACTGGGATCGAACAACAAGGAATGACTTCATGGGATCCCTTTCC
TTTGGAGTTTCGGAGCTGATGAAGATGCCGGCCAGTGGATGGTACAAGTTGCTTAACCAA
GAAGAAGGTGAGTACTACAACGTACCCATTCCGGAAGGGGACGAGGAAGGAAACATGGAA
CTCAGGCAGAAATTCGAGAAAGCCAAACTTGGCCCTGCTGGCAACAAAGTCATCAGTCCC
TCTGAAGACAGGAAACAACCTTCCAACAACCTTGACCGAGTGAAACTCACGGACTTCAAT
TTCCTCATGGTGTTGGGAAAGGGGAGTTTTGGAAAGGTGATGCTTGCCGACAGGAAGGGC
ACAGAAGAACTGTATGCAATCAAAATCCTGAAGAAGGATGTGGTGATTCAGGATGATGAC
GTGGAGTGCACCATGGTAGAAAAGCGAGTCTTGGCCCTGCTTGACAAACCCCCGTTCTTG
ACGCAGCTGCACTCCTGCTTCCAGACAGTGGATCGGCTGTACTTCGTCATGGAATATGTC
AACGGTGGGGACCTCATGTACCACATTCAGCAAGTAGGAAAATTTAAGGAACCACAAGCA
GTATTCTATGCGGCAGAGATTTCCATCGGATTGTTCTTTCTTCATAAAAGAGGAATCATT
TATAGGGATCTGAAGTTAGATAACGTCATGTTGGATTCAGAAGGACATATCAAAATTGCT
GACTTTGGGATGTGCAAGGAACACATGATGGATGGAGTCACGACCAGGACCTTCTGTGGG
ACTCCAGATTATATCGCCCCAGAGATAATCGCTTATCAGCCGTATGGAAAATCTGTGGAC
TGGTGGGCCTATGGCGTCCTGTTGTATGAAATGCTTGCCGGGCAGCCTCCATTTGATGGT
GAAGATGAAGACGAGCTATTTCAGTCTATCATGGAGCACAACGTTTCCTATCCAAAATCC
TTGTCCAAGGAGGCTGTTTCTATCTGCAAAGGACTGATGACCAAACACCCAGCCAAGCGG
CTGGGCTGTGGGCCTGAGGGGGAGAGGGACGTGAGAGAGCATGCCTTCTTCCGGAGGATC
GACTGGGAAAAACTGGAGAACAGGGAGATCCAGCCACCATTCAAGCCCAAAGTGTGTGGC
AAAGGAGCAGAGAACTTTGACAAGTTCTTCACACGAGGACAGCCCGTCTTAACACCACCT
GATCAGCTGGTTATTGCTAACATAGACCAGTCTGATTTTGAAGGGTTCTCGTATGTCAAC
CCCCAGTTTGTGCACCCCATCTTACAGAGTGCAGTATGA
Enzyme 6 GenBank Gene ID X52479 Link Image
Enzyme 6 GeneCard ID PRKCA Link Image
Enzyme 6 GenAtlas ID PRKCA Link Image
Enzyme 6 HGNC ID HGNC:9393 Link Image
Enzyme 6 Chromosome Location 17
Enzyme 6 Locus 17q22-q23.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Finkenzeller G, Marme D, Hug H: Sequence of human protein kinase C alpha. Nucleic Acids Res. 1990 Apr 25;18(8):2183. [PubMed Link Image]
  2. McSwine-Kennick RL, McKeegan EM, Johnson MD, Morin MJ: Phorbol diester-induced alterations in the expression of protein kinase C isozymes and their mRNAs. Analysis in wild-type and phorbol diester-resistant HL-60 cell clones. J Biol Chem. 1991 Aug 15;266(23):15135-43. [PubMed Link Image]
  3. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  4. Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A: Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C. Biochem Biophys Res Commun. 2003 Aug 1;307(3):459-65. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6655
Enzyme 7 Name Probable phospholipid-transporting ATPase IA
Enzyme 7 Synonyms
  1. Chromaffin granule ATPase II
  2. ATPase class I type 8A member 1
Enzyme 7 Gene Name ATP8A1
Enzyme 7 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 7 Number of Residues 1164
Enzyme 7 Molecular Weight 131371
Enzyme 7 Theoretical pI 6.83
Enzyme 7 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 7 General Function Inorganic ion transport and metabolism
Enzyme 7 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 7 Pathways Not Available
Enzyme 7 Reactions
  • ATP + H2O = ADP + phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 66-86 93-115 298-319 345-366 858-878 891-910 941-962 977-999 1006-1026 1045-1070
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 4972583 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9Y2Q0 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name AT8A1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 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 7 GenBank Gene ID AF067820 Link Image
Enzyme 7 GeneCard ID ATP8A1 Link Image
Enzyme 7 GenAtlas ID ATP8A1 Link Image
Enzyme 7 HGNC ID HGNC:13531 Link Image
Enzyme 7 Chromosome Location 4
Enzyme 7 Locus 4p14-p12
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 7395
Enzyme 8 Name Phospholipid scramblase 1
Enzyme 8 Synonyms
  1. PL scramblase 1
  2. Ca(2+-dependent phospholipid scramblase 1
  3. Erythrocyte phospholipid scramblase
  4. MmTRA1b
Enzyme 8 Gene Name PLSCR1
Enzyme 8 Protein Sequence >Phospholipid scramblase 1 
MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAG
FPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVL
TGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLR
CSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCC
GDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLI
DFMFFESTGSQEQKSGVW
Enzyme 8 Number of Residues 318
Enzyme 8 Molecular Weight 35049
Enzyme 8 Theoretical pI 4.57
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes. May contribute to cytokine-regulated cell proliferation and differentiation
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 289-305
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 4092081 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O15162 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PLS1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >957 bp 
ATGGACAAACAAAACTCACAGATGAATGCTTCTCACCCGGAAACAAACTTGCCAGTTGGG
TATCCTCCTCAGTATCCACCGACAGCATTCCAAGGACCTCCAGGATATAGTGGCTACCCT
GGGCCCCAGGTCAGCTACCCACCCCCACCAGCCGGCCATTCAGGTCCTGGCCCAGCTGGC
TTTCCTGTCCCAAATCAGCCAGTGTATAATCAGCCAGTATATAATCAGCCAGTTGGAGCT
GCAGGGGTACCATGGATGCCAGCGCCACAGCCTCCATTAAACTGTCCACCTGGATTAGAA
TATTTAAGTCAGATAGATCAGATACTGATTCATCAGCAAATTGAACTTCTGGAAGTTTTA
ACAGGTTTTGAAACTAATAACAAATATGAAATTAAGAACAGCTTTGGACAGAGGGTTTAC
TTTGCAGCGGAAGATACTGATTGCTGTACCCGAAATTGCTGTGGGCCATCTAGACCTTTT
ACCTTGAGGATTATTGATAATATGGGTCAAGAAGTCATAACTCTGGAGAGACCACTAAGA
TGTAGCAGCTGTTGTTGTCCCTGCTGCCTTCAGGAGATAGAAATCCAAGCTCCTCCTGGT
GTACCAATAGGTTATGTTATTCAGACTTGGCACCCATGTCTACCAAAGTTTACAATTCAA
AATGAGAAAAGAGAGGATGTACTAAAAATAAGTGGTCCATGTGTTGTGTGCAGCTGTTGT
GGAGATGTTGATTTTGAGATTAAATCTCTTGATGAACAGTGTGTGGTTGGCAAAATTTCC
AAGCACTGGACTGGAATTTTGAGAGAGGCATTTACAGACGCTGATAACTTTGGAATCCAG
TTCCCTTTAGACCTTGATGTTAAAATGAAAGCTGTAATGATTGGTGCCTGTTTCCTCATT
GACTTCATGTTTTTTGAAAGCACTGGCAGCCAGGAACAAAAATCAGGAGTGTGGTAG
Enzyme 8 GenBank Gene ID AF098642 Link Image
Enzyme 8 GeneCard ID PLSCR1 Link Image
Enzyme 8 GenAtlas ID PLSCR1 Link Image
Enzyme 8 HGNC ID HGNC:9092 Link Image
Enzyme 8 Chromosome Location 3
Enzyme 8 Locus 3q23
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Zhou Q, Zhao J, Stout JG, Luhm RA, Wiedmer T, Sims PJ: Molecular cloning of human plasma membrane phospholipid scramblase. A protein mediating transbilayer movement of plasma membrane phospholipids. J Biol Chem. 1997 Jul 18;272(29):18240-4. [PubMed Link Image]
  2. Kasukabe T, Kobayashi H, Kaneko Y, Okabe-Kado J, Honma Y: Identity of human normal counterpart (MmTRA1b) of mouse leukemogenesis-associated gene (MmTRA1a) product as plasma membrane phospholipid scramblase and chromosome mapping of the human MmTRA1b/phospholipid scramblase gene. Biochem Biophys Res Commun. 1998 Aug 19;249(2):449-55. [PubMed Link Image]
  3. Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed Link Image]
  4. Basse F, Stout JG, Sims PJ, Wiedmer T: Isolation of an erythrocyte membrane protein that mediates Ca2+-dependent transbilayer movement of phospholipid. J Biol Chem. 1996 Jul 19;271(29):17205-10. [PubMed Link Image]
  5. Frasch SC, Henson PM, Kailey JM, Richter DA, Janes MS, Fadok VA, Bratton DL: Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cdelta. J Biol Chem. 2000 Jul 28;275(30):23065-73. [PubMed Link Image]
  6. Sun J, Zhao J, Schwartz MA, Wang JY, Wiedmer T, Sims PJ: c-Abl tyrosine kinase binds and phosphorylates phospholipid scramblase 1. J Biol Chem. 2001 Aug 3;276(31):28984-90. Epub 2001 Jun 4. [PubMed Link Image]
  7. Zhao J, Zhou Q, Wiedmer T, Sims PJ: Palmitoylation of phospholipid scramblase is required for normal function in promoting Ca2+-activated transbilayer movement of membrane phospholipids. Biochemistry. 1998 May 5;37(18):6361-6. [PubMed Link Image]
  8. Zhou Q, Sims PJ, Wiedmer T: Identity of a conserved motif in phospholipid scramblase that is required for Ca2+-accelerated transbilayer movement of membrane phospholipids. Biochemistry. 1998 Feb 24;37(8):2356-60. [PubMed Link Image]
Enzyme 8 Metabolite References
  1. Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed Link Image]
Enzyme 9 [top]
Enzyme 9 ID 7675
Enzyme 9 Name Phosphatidylserine synthase 1
Enzyme 9 Synonyms
  1. PtdSer synthase 1
  2. PSS-1
  3. Serine-exchange enzyme I
Enzyme 9 Gene Name PTDSS1
Enzyme 9 Protein Sequence >Phosphatidylserine synthase 1 
MASCVGSRTLSKDDVNYKMHFRMINEQQVEDITIDFFYRPHTITLLSFTIVSLMYFAFTR
DDSVPEDNIWRGILSVIFFFLIISVLAFPNGPFTRPHPALWRMVFGLSVLYFLFLVFLLF
LNFEQVKSLMYWLDPNLRYATREADVMEYAVNCHVITWERIISHFDIFAFGHFWGWAMKA
LLIRSYGLCWTISITWELTELFFMHLLPNFAECWWDQVILDILLCNGGGIWLGMVVCRFL
EMRTYHWASFKDIHTTTGKIKRAVLQFTPASWTYVRWFDPKSSFQRVAGVYLFMIIWQLT
ELNTFFLKHIFVFQASHPLSWGRILFIGGITAPTVRQYYAYLTDTQCKRVGTQCWVFGVI
GFLEAIVCIKFGQDLFSKTQILYVVLWLLCVAFTTFLCLYGMIWYAEHYGHREKTYSECE
DGTYSPEISWHHRKGTKGSEDSPPKHAGNNESHSSRRRNRHSKSKVTNGVGKK
Enzyme 9 Number of Residues 473
Enzyme 9 Molecular Weight 55528
Enzyme 9 Theoretical pI 8.52
Enzyme 9 GO Classification
Function
—
Process
  • cellular lipid metabolism
  • glycerophospholipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phosphatidylserine biosynthesis
  • phosphatidylserine metabolism
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Catalyzes a base-exchange reaction in which the polar head group of phosphatidylcholine is replaced by L-serine
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • 36-56 73-93 103-123 161-181 187-207 217-237 287-307 310-330 356-376 384-404
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 603802 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P48651 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PTSS1_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1422 bp 
ATGGCGTCCTGCGTGGGGAGCCGGACCCTAAGCAAGGATGATGTGAACTACAAAATGCAT
TTCCGGATGATCAACGAGCAGCAAGTGGAGGACATCACCATTGACTTCTTCTACCGGCCG
CATACCATCACCCTGCTCAGCTTCACCATCGTCAGCCTCATGTACTTCGCCTTTACCAGG
GATGACTCTGTTCCAGAAGACAACATCTGGAGAGGCATCCTCTCTGTTATTTTCTTCTTT
CTTATCATCAGTGTGTTAGCTTTCCCCAATGGTCCGTTCACTCGACCTCATCCAGCCTTA
TGGCGAATGGTTTTTGGACTCAGTGTGCTCTACTTCCTGTTCCTGGTATTCCTACTCTTC
CTGAATTTCGAGCAGGTTAAATCTCTAATGTATTGGCTAGATCCAAATCTTCGATACGCC
ACAAGGGAAGCAGATGTCATGGAGTATGCTGTGAACTGCCATGTGATCACCTGGGAGAGG
ATTATCAGCCACTTTGATATTTTTGCATTTGGACATTTCTGGGGCTGGGCCATGAAGGCC
TTGCTGATCCGTAGTTACGGTCTCTGCTGGACAATCAGTATTACCTGGGAGCTGACTGAG
CTCTTCTTCATGCATCTCCTCCCCAATTTTGCCGAGTGCTGGTGGGATCAAGTCATTCTG
GACATCCTGTTGTGCAATGGCGGTGGCATTTGGCTGGGCATGGTCGTTTGCCGGTTTTTA
GAGATGAGGACTTACCACTGGGCAAGCTTCAAGGACATTCATACCACCACCGGGAAGATC
AAGAGAGCTGTTCTGCAGTTCACTCCTGCTAGCTGGACCTATGTTCGATGGTTTGACCCC
AAATCTTCTTTTCAGAGAGTAGCTGGAGTGTACCTTTTCATGATCATCTGGCAGCTGACT
GAGTTGAATACCTTCTTCTTGAAGCATATCTTTGTGTTCCAAGCCAGTCATCCATTAAGT
TGGGGTAGAATTCTCTTTATTGGTGGCATCACAGCTCCCACAGTGAGACAGTACTACGCT
TACCTCACCGACACACAGTGCAAGCGCGTAGGAACACAATGCTGGGTGTTTGGGGTCATT
GGTTTCCTGGAGGCCATTGTTTGCATAAAATTTGGACAAGATCTCTTCTCTAAGACCCAA
ATACTCTATGTTGTGCTTTGGCTTCTTTGCGTGGCTTTCACCACTTTCCTCTGTCTGTAC
GGCATGATTTGGTATGCAGAACACTATGGTCACCGAGAAAAGACCTACTCGGAGTGTGAA
GATGGCACCTACAGTCCAGAGATCTCCTGGCATCACAGGAAAGGGACAAAAGGTTCTGAA
GACAGCCCACCCAAGCATGCAGGCAACAACGAAAGCCATTCTTCCAGGAGAAGGAATCGG
CATTCCAAGTCAAAAGTCACCAATGGCGTTGGAAAGAAATGA
Enzyme 9 GenBank Gene ID D14694 Link Image
Enzyme 9 GeneCard ID PTDSS1 Link Image
Enzyme 9 GenAtlas ID PTDSS1 Link Image
Enzyme 9 HGNC ID HGNC:9587 Link Image
Enzyme 9 Chromosome Location 8
Enzyme 9 Locus 8q22
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed Link Image]
Enzyme 9 Metabolite References
  1. Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed Link Image]
Enzyme 10 [top]
Enzyme 10 ID 7722
Enzyme 10 Name Scavenger receptor class B member 1
Enzyme 10 Synonyms
  1. SRB1
  2. SR-BI
  3. CD36 antigen-like 1
  4. CD36 and LIMPII analogous 1
  5. CLA-1
  6. Collagen type I receptor, thrombospondin receptor-like 1
Enzyme 10 Gene Name SCARB1
Enzyme 10 Protein Sequence >Scavenger receptor class B member 1 
MGCSAKARWAAGALGVAGLLCAVLGAVMIVMVPSLIKQQVLKNVRIDPSSLSFNMWKEIP
IPFYLSVYFFDVMNPSEILKGEKPQVRERGPYVYREFRHKSNITFNNNDTVSFLEYRTFQ
FQPSKSHGSESDYIVMPNILVLGAAVMMENKPMTLKLIMTLAFTTLGERAFMNRTVGEIM
WGYKDPLVNLINKYFPGMFPFKDKFGLFAELNNSDSGLFTVFTGVQNISRIHLVDKWNGL
SKVDFWHSDQCNMINGTSGQMWPPFMTPESSLEFYSPEACRSMKLMYKESGVFEGIPTYR
FVAPKTLFANGSIYPPNEGFCPCLESGIQNVSTCRFSAPLFLSHPHFLNADPVLAEAVTG
LHPNQEAHSLFLDIHPVTGIPMNCSVKLQLSLYMKSVAGIGQTGKIEPVVLPLLWFAESG
AMEGETLHTFYTQLVLMPKVMHYAQYVLLALGCVLLLVPVICQIRSQVGAGQRAARADSH
SLACWGKGASDRTLWPTAAWSPPPAAVLRLCRSGSGHCWGLRSTLASFACRVATTLPVLE
GLGPSLGGGTGS
Enzyme 10 Number of Residues 552
Enzyme 10 Molecular Weight 60879
Enzyme 10 Theoretical pI 8.31
Enzyme 10 GO Classification
Function
—
Process
  • cell adhesion
  • cellular process
Component
  • cell
  • membrane
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells. Probable receptor for HDL, located in particular region of the plasma membrane, called caveolae. Facilitates the flux of free and esterified cholesterol between the cell surface and extracellular donors and acceptors, such as HDL and to a lesser extent, apoB-containing lipoproteins and modified lipoproteins. Probably involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity. Receptor for hepatitis C virus glycoprotein E2. Binding between SCARB1 and E2 was found to be independent of the genotype of the viral isolate
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-25
Enzyme 10 Transmembrane Regions Not Available
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 397607 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q8WTV0 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name SCRB1_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1530 bp 
ATGGGCTGCTCCGCCAAAGCGCGCTGGGCTGCCGGGGCGCTGGGCGTCGCGGGGCTACTG
TGCGCTGTGCTGGGCGCTGTCATGATCGTGATGGTGCCGTCGCTCATCAAGCAGCAGGTC
CTTAAGAACGTGCGCATCGACCCCAGTAGCCTGTCCTTCAACATGTGGAAGGAGATCCCT
ATCCCCTTCTATCTCTCCGTCTACTTCTTTGACGTCATGAACCCCAGCGAGATCCTGAAG
GGCGAGAAGCCGCAGGTGCGGGAGCGCGGGCCCTACGTGTACAGGGAGTCCAGGCACAAA
AGCAACATCACCTTCAACAACAACGACACCGTGTCCTTCCTCGAGTACCGCACCTTCCAG
TTCCAGCCCTCCAAGTCCCACGGCTCGGAGAGCGACTACATCGTCATGCCCAACATCCTG
GTCTTGGGTGCGGCGGTGATGATGGAGAATAAGCCCATGACCCTGAAGCTCATCATGACC
TTGGCATTCACCACCCTCGGCGAACGTGCCTTCATGAACCGCACTGTGGGTGAGATCATG
TGGGGCTACAAGGACCCCCTTGTGAATCTCATCAACAAGTACTTTCCAGGCATGTTCCCC
TTCAAGGACAAGTTCGGATTATTTGCTGAGCTCAACAACTCCGACTCTGGGCTCTTCACG
GTGTTCACGGGGGTCCAGAACATCAGCAGGATCCACCTCGTGGACAAGTGGAACGGGCTG
AGCAAGGTTGACTTCTGGCATTCCGATCAGTGCAACATGATCAATGGAACTTCTGGGCAA
ATGTGGCCGCCCTTCATGACTCCTGAGTCCTCGCTGGAGTTCTACAGCCCGGAGGCCTGC
CGATCCATGAAGCTAATGTACAAGGAGTCAGGGGTGTTTGAAGGCATCCCCACCTATCGC
TTCGTGGCTCCCAAAACCCTGTTTGCCAACGGGTCCATCTACCCACCCAACGAAGGCTTC
TGCCCGTGCCTGGAGTCTGGAATTCAGAACGTCAGCACCTGCAGGTTCAGTGCCCCCTTG
TTTCTCTCCCATCCTCACTTCCTCAACGCCGACCCGGTTCTGGCAGAAGCGGTGACTGGC
CTGCACCCTAACCAGGAGGCACACTCCTTGTTCCTGGACATCCACCCGGTCACGGGAATC
CCCATGAACTGCTCTGTGAAACTGCAGCTGAGCCTCTACATGAAATCTGTCGCAGGCATT
GGACAAACTGGGAAGATTGAGCCTGTGGTCCTGCCGCTGCTCTGGTTTGCAGAGAGCGGG
GCCATGGAGGGGGAGACTCTTCACACATTCTACACTCAGCTGGTGTTGATGCCCAAGGTG
ATGCACTATGCCCAGTACGTCCTCCTGGCGCTGGGCTGCGTCCTGCTGCTGGTCCCTGTC
ATCTGCCAAATCCGGAGCCAAGAGAAATGCTATTTATTTTGGAGTAGTAGTAAAAAGGGC
TCAAAGGATAAGGAGGCCATTCAGGCCTATTCTGAATCCCTGATGACATCAGCTCCCAAG
GGCTCTGTGCTGCAGGAAGCAAAACTGTAG
Enzyme 10 GenBank Gene ID Z22555 Link Image
Enzyme 10 GeneCard ID SCARB1 Link Image
Enzyme 10 GenAtlas ID SCARB1 Link Image
Enzyme 10 HGNC ID HGNC:1664 Link Image
Enzyme 10 Chromosome Location 12
Enzyme 10 Locus 12q24.31
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Calvo D, Vega MA: Identification, primary structure, and distribution of CLA-1, a novel member of the CD36/LIMPII gene family. J Biol Chem. 1993 Sep 5;268(25):18929-35. [PubMed Link Image]
  2. Scarselli E, Ansuini H, Cerino R, Roccasecca RM, Acali S, Filocamo G, Traboni C, Nicosia A, Cortese R, Vitelli A: The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus. EMBO J. 2002 Oct 1;21(19):5017-25. [PubMed Link Image]
  3. Kawasaki Y, Nakagawa A, Nagaosa K, Shiratsuchi A, Nakanishi Y: Phosphatidylserine binding of class B scavenger receptor type I, a phagocytosis receptor of testicular sertoli cells. J Biol Chem. 2002 Jul 26;277(30):27559-66. Epub 2002 May 16. [PubMed Link Image]
  4. Bartosch B, Vitelli A, Granier C, Goujon C, Dubuisson J, Pascale S, Scarselli E, Cortese R, Nicosia A, Cosset FL: Cell entry of hepatitis C virus requires a set of co-receptors that include the CD81 tetraspanin and the SR-B1 scavenger receptor. J Biol Chem. 2003 Oct 24;278(43):41624-30. Epub 2003 Aug 11. [PubMed Link Image]
  5. Tai ES, Adiconis X, Ordovas JM, Carmena-Ramon R, Real J, Corella D, Ascaso J, Carmena R: Polymorphisms at the SRBI locus are associated with lipoprotein levels in subjects with heterozygous familial hypercholesterolemia. Clin Genet. 2003 Jan;63(1):53-8. [PubMed Link Image]
  6. 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 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 7731
Enzyme 11 Name Small inducible cytokine B16 precursor
Enzyme 11 Synonyms
  1. Transmembrane chemokine CXCL16
  2. SR-PSOX
  3. Scavenger receptor for phosphatidylserine and oxidized low density lipoprotein
Enzyme 11 Gene Name CXCL16
Enzyme 11 Protein Sequence >Small inducible cytokine B16 precursor 
MGRDLRPGSRVLLLLLLLLLVYLTQPGNGNEGSVTGSCYCGKRISSDSPPSVQFMNRLRK
HLRAYHRCLYYTRFQLLSWSVCGGNKDPWVQELMSCLDLKECGHAYSGIVAHQKHLLPTS
PPISQASEGASSDIHTPAQMLLSTLQSTQRPTLPVGSLSSDKELTRPNETTIHTAGHSLA
VGPEAGENQKQPEKNAGPTARTSATVPVLCLLAIIFILTAALSYVLCKRRRGQSPQSSPD
LPVHYIPVAPDSNT
Enzyme 11 Number of Residues 254
Enzyme 11 Molecular Weight 27607
Enzyme 11 Theoretical pI 8.91
Enzyme 11 GO Classification
Function
  • chemokine activity
  • cytokine activity
  • receptor binding
  • signal transducer activity
Process
  • defense response
  • immune response
  • response to biotic stimulus
  • response to stimulus
Component
  • extracellular region
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis. Induces a strong chemotactic response. Induces calcium mobilization. Binds to CXCR6/Bonzo
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function Not Available
Enzyme 11 Signals
  • 1-29
Enzyme 11 Transmembrane Regions
  • 206-226
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 11342658 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q9H2A7 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name SCYBG_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >822 bp 
ATGTCTGGGAGTCAGAGCGAGGTGGCTCCATCCCCGCAGAGTCCGCGGAGCCCCGAGATG
GGACGGGACTTGCGGCCCGGGTCCCGCGTGCTCCTGCTCCTGCTTCTGCTCCTGCTGGTG
TACCTGACTCAGCCAGGCAATGGCAACGAGGGCAGCGTCACTGGAAGTTGTTATTGTGGT
AAAAGAATTTCTTCCGACTCCCCGCCATCGGTTCAGTTCATGAATCGTCTCCGGAAACAC
CTGAGAGCTTACCATCGGTGTCTATACTACACGAGGTTCCAGCTCCTTTCCTGGAGCGTG
TGTGGAGGCAACAAGGACCCATGGGTTCAGGAATTGATGAGCTGTCTTGATCTCAAAGAA
TGTGGACATGCTTACTCGGGGATTGTGGCCCACCAGAAGCATTTACTTCCTACCAGCCCC
CCAACTTCTCAGGCCTCAGAGGGGGCATCTTCAGATATCCACACCCCTGCCCAGATGCTC
CTGTCCACCTTGCAGTCCACTCAGCGCCCCACCCTCCCAGTAGGATCACTGTCCTCGGAC
AAAGAGCTCACTCGTCCCAATGAAACCACCATTCACACTGCGGGCCACAGTCTGGCAGTT
GGGCCTGAGGCTGGGGAGAACCAGAAGCAGCCGGAAAAAAATGCTGGTCCCACAGCCAGG
ACATCAGCCACAGTGCCGGTCCTGTGCCTCCTGGCCATCATCTTCATCCTCACCGCAGCC
CTTTCCTATGTGCTGTGCAAGAGGAGGAGGGGGCAGTCACCGCAGTCCTCTCCAGATCTG
CCGGTTCATTATATACCTGTGGCACCTGACTCTAATACCTGA
Enzyme 11 GenBank Gene ID AF301016 Link Image
Enzyme 11 GeneCard ID CXCL16 Link Image
Enzyme 11 GenAtlas ID CXCL16 Link Image
Enzyme 11 HGNC ID HGNC:16642 Link Image
Enzyme 11 Chromosome Location 17
Enzyme 11 Locus 17p13
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Matloubian M, David A, Engel S, Ryan JE, Cyster JG: A transmembrane CXC chemokine is a ligand for HIV-coreceptor Bonzo. Nat Immunol. 2000 Oct;1(4):298-304. [PubMed Link Image]
  2. Wilbanks A, Zondlo SC, Murphy K, Mak S, Soler D, Langdon P, Andrew DP, Wu L, Briskin M: Expression cloning of the STRL33/BONZO/TYMSTRligand reveals elements of CC, CXC, and CX3C chemokines. J Immunol. 2001 Apr 15;166(8):5145-54. [PubMed Link Image]
  3. Shimaoka T, Kume N, Minami M, Hayashida K, Kataoka H, Kita T, Yonehara S: Molecular cloning of a novel scavenger receptor for oxidized low density lipoprotein, SR-PSOX, on macrophages. J Biol Chem. 2000 Dec 29;275(52):40663-6. [PubMed Link Image]
  4. 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 11 Metabolite References
  1. Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed Link Image]
Enzyme 12 [top]
Enzyme 12 ID 7740
Enzyme 12 Name Phosphatidylserine decarboxylase proenzyme
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name PISD
Enzyme 12 Protein Sequence >Phosphatidylserine decarboxylase proenzyme 
MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARKIHTAPART
MFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWEVALYKSVPTRLLS
RAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPV
CGLHSISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKN
QLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCH
NERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNRE
GVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL
Enzyme 12 Number of Residues 408
Enzyme 12 Molecular Weight 46573
Enzyme 12 Theoretical pI 9.80
Enzyme 12 GO Classification
Function
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
  • phosphatidylserine decarboxylase activity
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid biosynthesis
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 12 General Function Lipid transport and metabolism
Enzyme 12 Specific Function Phosphatidyl-L-serine = phosphatidylethanolamine + CO(2)
Enzyme 12 Pathways
Enzyme 12 Reactions
  • phosphatidyl-L-serine = phosphatidylethanolamine + CO2
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 57997016 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9UG56 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name PISD_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1227 bp 
ATGGCGACGTCCGTGGGGCACCGATGTCTGGGATTACTGCACGGGGTCGCGCCGTGGCGG
AGCAGCCTCCATCCCTGTGAGATCACTGCCCTGAGCCAATCCCTACAGCCCTTACGGAAG
CTGCCTTTTAGAGCCTTTCGCACAGATGCCAGAAAAATCCACACTGCCCCTGCCCGAACC
ATGTTCCTGCTGCGTCCCCTGCCCATTCTGTTGGTGACAGGCGGCGGGTATGCAGGGTAC
CGGCAGTATGAGAAGTACAGGGAGCGAGAGCTGGAGAAGCTGGGATTGGAGATTCCACCC
AAACTTGCTGGTCACTGGGAGGTGGCTTTGTACAAGTCAGTGCCAACGCGCTTGCTGTCA
CGGGCCTGGGGTCGCCTCAATCAGGTGGAGCTGCCACACTGGCTGCGCAGGCCCGTCTAC
AGCCTGTACATCTGGACGTTTGGGGTGAACATGAAAGAGGCCGCTGTGGAGGACCTGCAT
CACTACCGCAACCTCAGCGAGTTCTTCCGGCGCAAGCTGAAGCCGCAGGCCCGGCCTGTC
TGTGGCCTGCACAGCATTAGCCCATCGGATGGAAGGATCCTCAACTTTGGGCAGGTGAAG
AACTGTGAGGTGGAGCAGGTAAAGGGGGTCACCTACTCCCTGGAGTCGTTCCTGGGCCCG
CGTATGTGCACAGAGGACCTGCCCTTCCCACCAGCCGCGTCGTGTGACTCCTTCAAGAAC
CAGCTGGTCACCCGGGAAGGGAATGAGCTCTATCACTGTGTCATCTACCTGGCCCCTGGG
GACTACCACTGCTTCCACTCCCCCACCGACTGGACTGTGTCCCACCGGCGCCACTTCCCA
GGCTCCCTGATGTCAGTGAACCCTGGCATGGCTCGCTGGATCAAAGAGCTCTTCTGCCAT
AACGAGCGGGTGGTCCTGACGGGGGACTGGAAACATGGCTTCTTCTCACTGACAGCTGTG
GGGGCCACCAACGTGGGCTCCATTCGCATCTACTTTGACCGGGACCTGCACACAAACAGC
CCAAGGCACAGCAAGGGCTCCTACAATGACTTCAGCTTCGTGACGCACACCAATAGAGAG
GGCGTCCCCATGCGTAAGGGCGAGCACCTGGGCGAGTTCAACCTGGGCTCCACCATCGTG
CTCATCTTCGAGGCCCCCAAGGACTTCAATTTCCAGCTGAAAACAGGACAGAAAATCCGC
TTTGGGGAAGCCCTGGGCTCGCTCTAG
Enzyme 12 GenBank Gene ID AL050371 Link Image
Enzyme 12 GeneCard ID PISD Link Image
Enzyme 12 GenAtlas ID PISD Link Image
Enzyme 12 HGNC ID HGNC:8999 Link Image
Enzyme 12 Chromosome Location 22
Enzyme 12 Locus 22q12.2
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 12 Metabolite References
  1. Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed Link Image]
Enzyme 13 [top]
Enzyme 13 ID 8142
Enzyme 13 Name JmjC domain-containing protein 6
Enzyme 13 Synonyms
  1. Jumonji domain-containing protein 6
  2. Protein PTDSR
  3. Phosphatidylserine receptor
Enzyme 13 Gene Name JMJD6
Enzyme 13 Protein Sequence >JmjC domain-containing protein 6 
MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESFSLSPAAVADNVERADALQLSVEEFV
ERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEY
MESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPP
RSGTGIHIDPLGTSAWNALVQGHKRWCLFPTSTPRELIKVTRDEGGNQQDEAITWFNVIY
PRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHK
TVRGRPKLSRKWYRILKQEHPELAVLADSVDLQESTGIASDSSSDSSSSSSSSSSDSDSE
CESGSEGDGTVHRRKKRRTCSMVGNGDTTSQDDCVSKERSSSR
Enzyme 13 Number of Residues 403
Enzyme 13 Molecular Weight 46462
Enzyme 13 Theoretical pI 8.98
Enzyme 13 GO Classification Not Available
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Required during embryogenesis and differentiation of multiple organs during embryogenesis. Probably acts as a key regulator of hematopoietic differentiation. May not be required for apoptotic cell clearance by macrophages but seems to be necessary for the regulation of macrophage cytokine responses
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 23491564 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q6NYC1 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name JMJD6_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1119 bp 
ATGAACCACAAGAGCAAGAAGCGCATCCGCGAGGCCAAGCGGAGTGCGCGGCCGGAGCTC
AAGGACTCGCTGGATTGGACCCGGCACAACTACTACGAGAGCTTCTCGCTGAGCCCGGCG
GCCGTGGCGGATAACGTGGAAAGGGCAGATGCTTTACAGCTGTCTGTGGAAGAATTTGTG
GAGCGGTATGAAAGACCTTACAAGCCCGTGGTTTTGTTGAATGCGCAAGAGGGCTGGTCT
GCGCAGGAGAAATGGACTCTGGAGCGCCTAAAAAGGAAATATCGGAACCAGAAGTTCAAG
TGTGGTGAGGATAACGATGGCTACTCAGTGAAGATGAAGATGAAATACTACATCGAGTAC
ATGGAGAGCACTCGAGATGATAGTCCCCTTTACATCTTTGACAGCAGCTATGGTGAACAC
CCTAAAAGAAGGAAACTTTTGGAAGACTACAAGGTGCCAAAGTTTTTCACTGATGACCTT
TTCCAGTATGCTGGGGAGAAGCGCAGGCCCCCTTACAGGTGGTTTGTGATGGGGCCACCA
CGCTCCGGAACTGGGATTCACATCGACCCTCTGGGAACCAGTGCCTGGAATGCCTTAGTT
CAGGGCCACAAGCGCTGGTGCCTGTTTCCTACCAGCACTCCCAGGGAACTCATCAAAGTG
ACCCGAGACGAAGGAGGGAACCAGCAAGACGAAGCTATTACCTGGTTTAATGTTATTTAT
CCCCGGACACAGCTTCCAACCTGGCCACCTGAATTCAAACCCCTGGAAATCTTACAAAAA
CCAGGAGAGACTGTCTTTGTACCAGGAGGCTGGTGGCATGTTGTCCTCAATCTCGACACT
ACTATCGCCATCACCCAAAATTTTGCCAGCAGCACCAACTTCCCTGTGGTATGGCACAAG
ACGGTAAGAGGGAGACCAAAGTTATCAAGGAAATGGTATAGGATTTTGAAGCAAGAGCAC
CCCGAGTTGGCAGTCCTCGCAGACTCGGTTGACCTTCAGGAGTCCACAGGGATAGCTTCC
GACAGCTCCAGCGACTCTTCCAGCTCCTCCAGCTCCAGTTCGTCAGACTCCGACTCAGAG
AGGATTAGGGACACTTGTGGAGGCCGGGCTCACCCCTGA
Enzyme 13 GenBank Gene ID AB073711 Link Image
Enzyme 13 GeneCard ID JMJD6 Link Image
Enzyme 13 GenAtlas ID JMJD6 Link Image
Enzyme 13 HGNC ID HGNC:19355 Link Image
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. 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 13 Metabolite References
  1. Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed Link Image]
Enzyme 14 [top]
Enzyme 14 ID 8475
Enzyme 14 Name Phosphatidylserine synthase 2
Enzyme 14 Synonyms
  1. PtdSer synthase 2
  2. PSS-2
  3. Serine-exchange enzyme II
Enzyme 14 Gene Name PTDSS2
Enzyme 14 Protein Sequence >Phosphatidylserine synthase 2 
MRRGERRDAGGPRPESPVPAGRASLEEPPDGPSAGQATGPGEGRRSTESEVYDDGTNTFF
WRAHTLTVLFILTCTLGYVTLLEETPQDTAYNTKRGIVASILVFLCFGVTQAKDGPFSRP
HPAYWRFWLCVSVVYELFLIFILFQTVQDGRQFLKYVDPKLGVPLPERDYGGNCLIYDPD
NETDPFHNIWDKLDGFVPAHFLGWYLKTLMIRDWWMCMIISVMFEFLEYSLEHQLPNFSE
CWWDHWIMDVLVCNGLGIYCGMKTLEWLSLKTYKWQGLWNIPTYKGKMKRIAFQFTPYSW
VRFEWKPASSLRRWLAVCGIILVFLLAELNTFYLKFVLWMPPEHYLVLLRLVFFVNVGGV
AMREIYDFMDDPKPHKKLGPQAWLVAAITATELLIVVKYDPHTLTLSLPFYISQCWTLGS
VLALTWTVWRFFLRDITLRYKETRWQKWQNKDDQGSTVGNGDQHPLGLDEDLLGPGVAEG
EGAPTPN
Enzyme 14 Number of Residues 487
Enzyme 14 Molecular Weight 56253
Enzyme 14 Theoretical pI 6.19
Enzyme 14 GO Classification
Function
—
Process
  • cellular lipid metabolism
  • glycerophospholipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phosphatidylserine biosynthesis
  • phosphatidylserine metabolism
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine is replaced by L-serine
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals Not Available
Enzyme 14 Transmembrane Regions
  • 63-83 97-117 127-147 242-262 314-334 336-356 377-397 404-424
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 21740008 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q9BVG9 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name PTSS2_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1464 bp 
ATGCGGAGGGGCGAGCGCAGGGACGCCGGAGGTCCGCGGCCCGAGTCCCCGGTGCCCGCG
GGCAGGGCCTCGCTGGAGGAGCCGCCTGACGGGCCGTCTGCCGGCCAAGCCACCGGGCCG
GGCGAGGGCCGCCGCAGCACCGAGTCCGAGGTCTACGACGACGGCACCAACACCTTCTTC
TGGCGAGCCCACACCTTAACCGTGCTCTTCATCCTCACCTGTACGCTTGGCTATGTGACG
CTGCTGGAGGAAACACCTCAGGACACGGCCTACAACACCAAGAGAGGTATTGTGGCCAGT
ATTTTGGTTTTCTTATGTTTTGGAGTCACACAAGCTAAAGACGGGCCATTTTCCAGACCT
CATCCAGCTTACTGGAGGTTTTGGCTCTGCGTGAGTGTGGTCTACGAGCTGTTTCTCATC
TTTATACTCTTCCAGACTGTCCAGGACGGCCGGCAGTTTCTAAAGTATGTTGACCCCAAG
CTGGGAGTCCCACTGCCAGAGAGAGACTACGGGGGAAACTGCCTCATCTACGACCCAGAC
AATGAGACTGACCCCTTTCACAACATCTGGGACAAGTTGGATGGCTTTGTTCCCGCGCAC
TTTCTTGGCTGGTACCTGAAGACCCTGATGATCCGAGACTGGTGGATGTGCATGATCATC
AGCGTGATGTTCGAGTTCCTGGAGTACAGCCTGGAGCACCAGCTGCCCAACTTCAGCGAG
TGCTGGTGGGATCACTGGATCATGGACGTGCTCGTCTGCAACGGGCTGGGCATCTACTGC
GGCATGAAGACCCTTGAGTGGCTGTCCCTGAAGACGTACAAGTGGCAGGGCCTCTGGAAC
ATTCCGACCTACAAGGGCAAGATGAAGAGGATCGCCTTCCAGTTCACGCCGTACAGCTGG
GTTCGCTTCGAGTGGAAGCCGGCCTCCAGCCTGCGTCGCTGGCTGGCCGTGTGCGGCATC
ATCCTGGTGTTCCTGTTGGCAGAACTGAACACGTTCTACCTGAAGTTTGTGCTGTGGATG
CCCCCGGAGCACTACCTGGTCCTCCTGCGGCTCGTCTTCTTCGTGAACGTGGGTGGCGTG
GCCATGCGTGAGATCTACGACTTCATGGATGACCCGAAGCCCCACAAGAAGCTGGGCCCG
CAGGCCTGGCTGGTGGCGGCCATCACGGCCACGGAGCTGCTCATCGTGGTGAAGTACGAC
CCCCACACGCTCACCCTGTCCCTGCCCTTCTACATCTCCCAGTGCTGGACCCTCGGCTCC
GTCCTGGCGCTCACCTGGACCGTCTGGCGCTTCTTCCTGCGGGACATCACATTGAGGTAC
AAGGAGACCCGGTGGCAGAAGTGGCAGAACAAGGATGACCAGGGCAGCACCGTCGGCAAC
GGGGACCAGCACCCACTGGGGCTGGACGAAGACCTGCTGGGGCCTGGGGTGGCCGAGGGC
GAGGGAGCACCAACTCCAAACTGA
Enzyme 14 GenBank Gene ID AL834357 Link Image
Enzyme 14 GeneCard ID PTDSS2 Link Image
Enzyme 14 GenAtlas ID PTDSS2 Link Image
Enzyme 14 HGNC ID HGNC:15463 Link Image
Enzyme 14 Chromosome Location 11
Enzyme 14 Locus 11p15
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References Not Available
Enzyme 14 Metabolite References
  1. Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed Link Image]
Enzyme 15 [top]
Enzyme 15 ID 8626
Enzyme 15 Name 2-acylglycerol O-acyltransferase 2
Enzyme 15 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 15 Gene Name MOGAT2
Enzyme 15 Protein Sequence >2-acylglycerol O-acyltransferase 2 
MVEFAPLFMPWERRLQTLAVLQFVFSFLALAEICTVGFIALLFTRFWLLTVLYAAWWYLD
RDKPRQGGRHIQAIRCWTIWKYMKDYFPISLVKTAELDPSRNYIAGFHPHGVLAVGAFAN
LCTESTGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKESAAHILNRKGGGNL
LGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSG
SWLRYIQNRLQKIMGISLPLFHGRGVFQYSFGLIPYRRPITTVVGKPIEVQKTLHPSEEE
VNQLHQRYIKELCNLFEAHKLKFNIPADQHLEFC
Enzyme 15 Number of Residues 334
Enzyme 15 Molecular Weight 38196
Enzyme 15 Theoretical pI 9.77
Enzyme 15 GO Classification Not Available
Enzyme 15 General Function Lipid transport and metabolism
Enzyme 15 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 15 Pathways
Enzyme 15 Reactions
  • acyl-CoA + 2-acylglycerol = CoA + diacylglycerol
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-31
Enzyme 15 Transmembrane Regions
  • 23-37 38-59 103-123
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 28881910 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q3SYC2 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name MOGT2_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1005 bp 
ATGGTAGAGTTCGCGCCCTTGTTTATGCCGTGGGAGCGCAGGCTGCAGACACTTGCTGTC
CTACAGTTTGTCTTCTCCTTCTTGGCACTGGCCGAGATCTGCACTGTGGGCTTCATAGCC
CTCCTGTTTACAAGATTCTGGCTCCTCACTGTCCTGTATGCGGCCTGGTGGTATCTGGAC
CGAGACAAGCCACGGCAGGGGGGCCGGCACATCCAGGCCATCAGGTGCTGGACTATATGG
AAGTACATGAAGGACTATTTCCCCATCTCGCTGGTCAAGACTGCTGAGCTGGACCCCTCT
CGGAACTACATTGCGGGCTTCCACCCCCATGGAGTCCTGGCAGTCGGAGCCTTTGCCAAC
CTGTGCACTGAGAGCACAGGCTTCTCTTCGATCTTCCCCGGTATCCGCCCCCATCTGATG
ATGCTGACCTTGTGGTTCCGGGCCCCCTTCTTCAGAGATTACATCATGTCTGCAGGGTTG
GTCACATCAGAAAAGGAGAGTGCTGCTCACATTCTGAACAGGAAGGGTGGCGGAAACTTG
CTGGGCATCATTGTAGGGGGTGCCCAGGAGGCCCTGGATGCCAGGCCTGGATCCTTCACG
CTGTTACTGCGGAACCGAAAGGGCTTCGTCAGGCTCGCCCTGACACACGGGGCACCCCTG
GTGCCAATCTTCTCCTTCGGGGAGAATGACCTATTTGACCAGATTCCCAACTCTTCTGGC
TCCTGGTTACGCTATATCCAGAATCGGTTGCAGAAGATCATGGGCATCTCCCTCCCACTC
TTTCATGGCCGTGGTGTCTTCCAGTACAGCTTTGGTTTAATACCCTACCGCCGGCCCATC
ACCACTGTGGTGGGGAAGCCCATCGAGGTACAGAAGACGCTGCATCCCTCGGAGGAGGAG
GTGAACCAGCTGCACCAGCGTTATATCAAAGAGCTGTGCAACCTCTTCGAGGCCCACAAA
CTTAAGTTCAACATCCCTGCTGACCAGCACTTGGAGTTCTGCTGA
Enzyme 15 GenBank Gene ID AY157608 Link Image
Enzyme 15 GeneCard ID MOGAT2 Link Image
Enzyme 15 GenAtlas ID MOGAT2 Link Image
Enzyme 15 HGNC ID HGNC:23248 Link Image
Enzyme 15 Chromosome Location 11
Enzyme 15 Locus 11q13.5
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 8662
Enzyme 16 Name Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing alpha polypeptide
Enzyme 16 Synonyms
  1. Phosphoinositide 3-Kinase-C2-alpha
  2. PtdIns-3-kinase C2 alpha
  3. PI3K-C2alpha
Enzyme 16 Gene Name PIK3C2A
Enzyme 16 Protein Sequence >Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing alpha polypeptide 
MAQIFSNSGFKECPFSHPEPTRAKDVDKEEALQMEAEALAKLQKDRQVTDNQRGFELSSS
TRKKAQVYNKQDYDLMVFPESDSQKRALDIDVEKLTQAELEKLLLDDSFETKKTPVLPVT
PILSPSFSAQLYFRPTIQRGQWPPGLPGPSTYALPSIYPSTYSKQAAFQNGFNPRMPTFP
STEPIYLSLPGQSPYFSYPLTPATPFHPQGSLPIYRPVVSTDMAKLFDKIASTSEFLKNG
KARTDLEITDSKVSNLQVSPKSEDISKFDWLDLDPLSKPKVDNVEVLDHEEEKNVSSLLA
KDPWDAVLLEERSTANCHLERKVNGKSLSVATVTRSQSLNIRTTQLAKAQGHISQKDPNG
TSSLPTGSSLLQEVEVQNEEMAAFCRSITKLKTKFPYTNHRTNPGYLLSPVTAQRNICGE
NASVKVSIDIEGFQLPVTFTCDVSSTVEIIIMQALCWVHDDLNQVDVGSYVLKVCGQEEV
LQNNHCLGSHEHIQNCRKWDTEIRLQLLTFSAMCQNLARTAEDDETPVDLNKHLYQIEKP
CKEAMTRHPVEELLDSYHNQVELALQIENQHRAVDQVIKAVRKICSALDGVETLAITESV
KKLKRAVNLPRSKTADVTSLFGGEDTSRSSTRGSLNPENPVQVSINQLTAAIYDLLRLHA
NSGRSPTDCAQSSKSVKEAWTTTEQLQFTIFAAHGISSNWVSNYEKYYLICSLSHNGKDL
FKPIQSKKVGTYKNFFYLIKWDELIIFPIQISQLPLESVLHLTLFGILNQSSGSSPDSNK
QRKGPEALGKVSLPLCDFRRFLTCGTKLLYLWTSSHTNSVPGTVTKKGYVMERIVLQVDF
PSPAFDIIYTTPQVDRSIIQQHNLETLENDIKGKLLDILHKDSSLGLSKEDKAFLWEKRY
YCFKHPNCLPKILASAPNWKWGNLAKTYSLLHQWPALYPLIALELLDSKFADQEVRSLAV
TWIEAISDDELTDLLPQFVQALKYEIYLNSSLVQFLLSRALGNIQIAHNLYWLLKDALHD
VQFSTRYEHVLGALLSVGGKRLREELLKQTKLVQLLGGVAEKVRQASGSARQVVLQRSME
RVQSFFQKNKCRLPLKPSLVAKELNIKSCSFFSSNAVPLKVTMVNADPLGEEINVMFKVG
EDLRQDMLALQMIKIMDKIWLKEGLDLRMVIFKCLSTGRDRGMVELVPASDTLRKIQVEY
GVTGSFKDKPLAEWLRKYNPSEEEYEKASENFIYSCAGCCVATYVLGICDRHNDNIMLRS
TGHMFHIDFGKFLGHAQMFGSFKRDRAPFVLTSDMAYVINGGEKPTIRFQLFVDLCCQAY
NLIRKQTNLFLNLLSLMIPSGLPELTSIQDLKYVRDALQPQTTDAEATIFFTRLIESSLG
SIATKFNFFIHNLAQLRFSGLPSNDEPILSFSPKTYSFRQDGRIKEVSVFTYHKKYNPDK
HYIYVVRILWEGQIEPSFVFRTFVEFQELHNKLSIIFPLWKLPGFPNRMVLGRTHIKDVA
AKRKIELNSYLQSLMNASTDVAECDLVCTFFHPLLRDEKAEGIARSADAGSFSPTPGQIG
GAVKLSISYRNGTLFIMVMHIKDLVTEDGADPNPYVKTYLLPDNHKTSKRKTKISRKTRN
PTFNEMLVYSGYSKETLRQRELQLSVLSAESLRENFFLGGVTLPLKDFNLSKETVKWYQL
TAATYL
Enzyme 16 Number of Residues 1686
Enzyme 16 Molecular Weight 190740
Enzyme 16 Theoretical pI 8.08
Enzyme 16 GO Classification
Function
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • kinase activity
  • lipid kinase activity
  • phosphatidylinositol 3-kinase activity
  • phosphoinositide 3-kinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • signal transduction
Component
  • phosphoinositide 3-kinase complex
  • protein complex
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2. May play a role in clathrin-coated endocytic vesicle formation and EGF signaling cascade. May be involved in mitosis and UV-induced damage response. May be a downstream effector in insulin signaling cascade
Enzyme 16 Pathways
  • Phosphatidylinositol signaling system (map04070 Link Image)
Enzyme 16 Reactions
  • ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals Not Available
Enzyme 16 Transmembrane Regions Not Available
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 2143260 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID O00443 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name P3C2A_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >5061 bp 
ATGGCTCAGATATTTAGCAACAGCGGATTTAAAGAATGTCCATTTTCACATCCGGAACCA
ACAAGAGCAAAAGATGTGGACAAAGAAGAAGCATTACAGATGGAAGCAGAGGCTTTAGCA
AAACTGCAAAAGGATAGACAAGTGACTGACAATCAGAGAGGCTTTGAGTTGTCAAGCAGC
ACCAGAAAAAAAGCACAGGTTTATAACAAGCAGGATTATGATCTCATGGTGTTTCCTGAA
TCAGATTCCCAAAAAAGAGCATTAGATATTGATGTAGAAAAGCTCACCCAAGCTGAACTT
GAGAAACTATTGCTGGATGACAGTTTCGAGACTAAAAAAACACCTGTATTACCAGTTACT
CCTATTCTGAGCCCTTCCTTTTCAGCACAGCTCTATTTTAGACCTACTATTCAGAGAGGA
CAGTGGCCACCTGGATTACCTGGGCCTTCCACTTATGCTTTACCTTCTATTTATCCTTCT
ACTTACAGTAAACAGGCTGCATTCCAAAATGGCTTCAATCCAAGAATGCCCACTTTTCCA
TCTACAGAACCTATATATTTAAGTCTTCCGGGACAATCTCCATATTTCTCATATCCTTTG
ACACCTGCCACACCCTTTCATCCACAAGGAAGCTTACCTATCTATCGTCCAGTAGTCAGT
ACTGACATGGCAAAACTATTTGACAAAATAGCTAGTACATCAGAATTTTTAAAAAATGGG
AAAGCAAGGACTGATTTGGAGATAACAGATTCAAAAGTCAGCAATCTACAGGTATCTCCA
AAGTCTGAGGATATCAGTAAATTTGACTGGTTAGACTTGGATCCTCTAAGTAAGCCTAAG
GTGGATAATGTGGAGGTATTAGACCATGAGGAAGAGAAAAATGTTTCAAGTTTGCTAGCA
AAGGATCCTTGGGATGCTGTTCTTCTTGAAGAGAGATCGACAGCAAATTGTCATCTTGAA
AGAAAGGTGAATGGAAAATCCCTTTCTGTGGCAACTGTTACAAGAAGCCAGTCTTTAAAT
ATTCGAACAACTCAGCTTGCAAAAGCCCAGGGCCATATATCTCAGAAAGACCCAAATGGG
ACCAGTAGTTTGCCAACTGGAAGTTCTCTTCTTCAAGAAGTTGAAGTACAGAATGAGGAG
ATGGCAGCTTTTTGTCGATCCATTACAAAATTGAAGACCAAATTTCCATATACCAATCAC
CGCACAAACCCAGGCTATTTGTTAAGTCCAGTCACAGCGCAAAGAAACATATGCGGAGAA
AATGCTAGTGTGAAGGTCTCCATTGACATTGAAGGATTTCAGCTACCAGTTACTTTTACG
TGTGATGTGAGTTCTACTGTAGAAATCATTATAATGCAAGCCCTTTGCTGGGTACATGAT
GACTTGAATCAAGTAGATGTTGGCAGCTATGTTCTAAAAGTTTGTGGTCAAGAGGAAGTG
CTGCAGAATAATCATTGCCTTGGAAGTCATGAGCATATTCAAAACTGTCGAAAATGGGAC
ACAGAAATTAGACTACAACTCTTGACCTTCAGTGCAATGTGTCAAAATCTGGCCCGAACA
GCAGAAGATGATGAAACACCCGTGGATTTAAACAAACACCTGTATCAAATAGAAAAACCT
TGCAAAGAAGCCATGACGAGACACCCTGTTGAAGAACTCTTAGATTCTTATCACAACCAA
GTAGAACTGGCTCTTCAAATTGAAAACCAACACCGAGCAGTAGATCAAGTAATTAAAGCT
GTAAGAAAAATCTGTAGTGCTTTAGATGGTGTCGAGACTCTTGCCATTACAGAATCAGTA
AAGAAGCTAAAGAGAGCAGTTAATCTTCCAAGGAGTAAAACTGCTGATGTGACTTCTTTG
TTTGGAGGAGAAGACACTAGCAGGAGTTCAACTAGGGGCTCACTTAATCCTGAAAATCCT
GTTCAAGTAAGCATAAACCAATTAACTGCAGCAATTTATGATCTTCTCAGACTCCATGCA
AATTCTGGTAGGAGTCCTACAGACTGTGCCCAAAGTAGCAAGAGTGTCAAGGAAGCATGG
ACTACAACAGAGCAGCTCCAGTTTACTATTTTTGCTGCTCATGGAATTTCAAGTAATTGG
GTATCAAATTATGAAAAATACTACTTGATATGTTCACTGTCTCACAATGGAAAGGATCTT
TTTAAACCTATTCAATCAAAGAAGGTTGGCACTTACAAGAATTTCTTCTATCTTATTAAA
TGGGATGAACTAATCATTTTTCCTATCCAGATATCACAATTGCCATTAGAATCAGTTCTT
CACCTTACTCTTTTTGGAATTTTAAATCAGAGCAGTGGAAGTTCCCCTGATTCTAATAAG
CAGAGAAAGGGACCAGAAGCTTTGGGCAAAGTTTCTTTACCTCTTTGTGACTTTAGACGG
TTTTTAACATGTGGAACTAAACTTCTATATCTTTGGACTTCATCACATACAAATTCTGTT
CCTGGAACAGTTACCAAAAAAGGATATGTCATGGAAAGAATAGTGCTACAGGTTGATTTT
CCTTCTCCTGCATTTGATATTATTTATACAACTCCTCAAGTTGACAGAAGCATTATACAG
CAACATAACTTAGAAACACTAGAGAATGATATAAAAGGGAAACTTCTTGATATTCTTCAT
AAAGACTCATCACTTGGACTTTCTAAAGAAGATAAAGCTTTTTTATGGGAGAAACGTTAT
TATTGCTTCAAACACCCAAATTGTCTTCCTAAAATATTAGCAAGCGCCCCAAACTGGAAA
TGGGGTAATCTTGCCAAAACTTACTCATTGCTTCACCAGTGGCCTGCATTGTACCCACTA
ATTGCATTGGAACTTCTTGATTCAAAATTTGCTGATCAGGAAGTAAGATCCCTAGCTGTG
ACCTGGATTGAGGCCATTAGTGATGATGAGCTAACAGATCTTCTTCCACAGTTTGTACAA
GCTTTGAAATATGAAATTTACTTGAATAGTTCATTAGTGCAATTCCTTTTGTCCAGGGCA
TTGGGAAATATCCAGATAGCACACAATTTATATTGGCTTCTCAAAGATGCCCTGCATGAT
GTACAGTTTAGTACCCGATACGAACATGTTTTGGGTGCTCTCCTGTCAGTAGGAGGAAAA
CGACTTAGAGAAGAACTTCTAAAACAGACGAAACTTGTACAGCTTTTAGGAGGAGTAGCA
GAAAAAGTAAGGCAGGCTAGTGGATCAGCCAGACAGGTTGTTCTCCAAAGAAGTATGGAA
CGAGTACAGTCCTTTTTTCAGAAAAATAAATGCCGTCTCCCTCTCAAGCCAAGTCTAGTG
GCAAAAGAATTAAATATTAAGTCGTGTTCCTTCTTCAGTTCTAATGCTGTCCCCCTAAAA
GTCACAATGGTGAATGCTGACCCTCTGGGAGAAGAAATTAATGTCATGTTTAAGGTTGGT
GAAGATCTTCGGCAAGATATGTTAGCTTTACAGATGATAAAGATTATGGATAAGATCTGG
CTTAAAGAAGGACTAGATCTGAGGATGGTAATTTTCAAATGTCTCTCAACTGGCAGAGAT
CGAGGCATGGTGGAGCTGGTTCCTGCTTCCGATACCCTCAGGAAAATCCAAGTGGAATAT
GGTGTGACAGGATCCTTTAAAGATAAACCACTTGCAGAGTGGCTAAGGAAATACAATCCC
TCTGAAGAAGAATATGAAAAGGCTTCAGAGAACTTTATCTATTCCTGTGCTGGATGCTGT
GTAGCCACCTATGTTTTAGGCATCTGTGATCGACACAATGACAATATAATGCTTCGAAGC
ACGGGACACATGTTTCACATTGACTTTGGAAAGTTTTTGGGACATGCACAGATGTTTGGC
AGCTTCAAAAGGGATCGGGCTCCTTTTGTGCTGACCTCTGATATGGCATATGTCATTAAT
GGGGGTGAAAAGCCCACCATTCGTTTTCAGTTGTTTGTGGACCTCTGCTGTCAGGCCTAC
AACTTGATAAGAAAGCAGACAAACCTTTTTCTTAACCTCCTTTCACTGATGATTCCTTCA
GGGTTACCAGAACTTACAAGTATTCAAGATTTGAAATACGTTAGAGATGCACTTCAACCC
CAAACTACAGACGCAGAAGCTACAATTTTCTTTACTAGGCTTATTGAATCAAGTTTGGGA
AGCATTGCCACAAAGTTTAACTTCTTCATTCACAACCTTGCTCAGCTTCGTTTTTCTGGT
CTTCCTTCTAATGATGAGCCCATCCTTTCATTTTCACCTAAAACATACTCCTTTAGACAA
GATGGTCGAATCAAGGAAGTCTCTGTTTTTACATATCATAAGAAATACAACCCAGATAAA
CATTATATTTATGTAGTCCGAATTTTGTGGGAAGGACAGATTGAACCATCATTTGTCTTC
CGAACATTTGTCGAATTTCAGGAACTTCACAATAAGCTCAGTATTATTTTTCCACTTTGG
AAGTTACCAGGCTTTCCTAATAGGATGGTTCTAGGAAGAACACACATAAAAGATGTAGCA
GCCAAAAGGAAAATTGAGTTAAACAGTTACTTACAGAGTTTGATGAATGCTTCAACGGAT
GTAGCAGAGTGTGATCTTGTTTGTACTTTCTTCCACCCTTTACTTCGTGATGAGAAAGCT
GAAGGGATAGCTAGGTCTGCAGATGCAGGTTCCTTCAGTCCTACTCCAGGCCAAATAGGA
GGAGCTGTGAAATTATCCATCTCTTACCGAAATGGTACTCTTTTCATCATGGTGATGCAT
ATCAAAGATCTTGTTACTGAAGATGGAGCTGACCCAAATCCATATGTCAAAACATACCTA
CTTCCAGATAACCACAAAACATCCAAACGTAAAACCAAAATTTCACGAAAAACGAGGAAT
CCGACATTCAATGAAATGCTTGTATACAGTGGATATAGCAAAGAAACCCTAAGACAGCGA
GAACTTCAACTAAGTGTACTCAGTGCAGAATCTCTGCGGGAGAATTTTTTCTTGGGTGGA
GTAACCCTGCCTTTGAAAGATTTCAACTTGAGCAAAGAGACGGTTAAATGGTATCAGCTG
ACTGCGGCAACATACTTGTAA
Enzyme 16 GenBank Gene ID Y13367 Link Image
Enzyme 16 GeneCard ID PIK3C2A Link Image
Enzyme 16 GenAtlas ID PIK3C2A Link Image
Enzyme 16 HGNC ID HGNC:8971 Link Image
Enzyme 16 Chromosome Location 11
Enzyme 16 Locus 11p15.5-p14
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Domin J, Pages F, Volinia S, Rittenhouse SE, Zvelebil MJ, Stein RC, Waterfield MD: Cloning of a human phosphoinositide 3-kinase with a C2 domain that displays reduced sensitivity to the inhibitor wortmannin. Biochem J. 1997 Aug 15;326 ( Pt 1):139-47. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 8839
Enzyme 17 Name Inositol polyphosphate 5-phosphatase
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name INPPL1
Enzyme 17 Protein Sequence >Inositol polyphosphate 5-phosphatase 
MASACGAPGPGGALGSQAPSWYHRDLSRAAAEELLARAGRDGSFLVRDSESVAGAFALCV
LYQKHVHTYRILPDGEDFLAVQTSQGVPVRRFQTLGELIGLYAQPNQGLVCALLLPVEGE
REPDPPDDRDASDGEDEKPPLPPRSGSTSISAPTGPSSPLPAPETPTAPAAESAPNGLST
VSHDYLKGSYGLDLEAVRGGASHLPHLTRTLATSCRRLHSEVDKVLSGLEILSKVFDQQS
SPMVTRLLQQQNLPQTGEQELESLVLKLSVLKDFLSGIQKKALKALQDMSSTAPPAPQPS
TRKAKTIPVQAFEVKLDVTLGDLTKIGKSQKFTLSVDVEGGRLVLLRRQRDSQEDWTTFT
HDRIRQLIKSQRVQNKLGVVFEKEKDRTQRKDFIFVSARKREAFCQLLQLMKNKHSKQDE
PDMISVFIGTWNMGSVPPPKNVTSWFTSKGLGKTLDEVTVTIPHDIYVFGTQENSVGDRE
WLDLLRGGLKELTDLDYRPIAMQSLWNIKVAVLVKPEHENRISHVSTSSVKTGIANTLGN
KGAVGVSFMFNGTSFGFVNCHLTSGNEKTARRNQNYLDILRLLSLGDRQLNAFDISLRFT
HLFWFGDLNYRLDMDIQEILNYISRKEFEPLLRVDQLNLEREKHKVFLRFSEEEISFPPT
YRYERGSRDTYAWHKQKPTGVRTNVPSWCDRILWKSYPETHIICNSYGCTDDIVTSDHSP
VFGTFEVGVTSQFISKKGLSKTSDQAYIEFESIEAIVKTASRTKFFIEFYSTCLEEYKKS
FENDAQSSDNINFLKVQWSSRQLPTLKPILADIEYLQDQHLLLTVKSMDGYESYGECVVA
LKSMIGSTAQQFLTFLSHRGEETGNIRGSMKVRVPTERLGTRERLYEWISIDKDEAGAKS
KAPSVSRGSQEPRSGSRKPAFTEASCPLSRLFEEPEKPPPTGRPPAPPRAAPREEPLTPR
LKPEGAPEPEGVAAPPPKNSFNNPAYYVLEGVPHQLLPPEPPSPARAPVPSATKNKVAIT
VPAPQLGHHRHPRVGEGSSSDEESGGTLPPPDFPPPPLPDSAIFLPPSLDPLPGPVVRGR
GGAEARGPPPPKAHPRPPLPPGPSPASTFLGEVGSGDDRSCSVLQMAKTLSEVDYAPAGP
ARSALLPGPLELQPPRGLPSDYGRPLSFPPPRIRESIQEDLAEEAPCLQGGRASGLGEAG
MSAWLRAIGLERYEEGLVHNGWDDLEFLSDITEEDLEEAGVQDPAHKRLLLDTLQLSK
Enzyme 17 Number of Residues 1258
Enzyme 17 Molecular Weight 138586
Enzyme 17 Theoretical pI 6.49
Enzyme 17 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • signal transduction
Component
—
Enzyme 17 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 17 Specific Function Not Available
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals Not Available
Enzyme 17 Transmembrane Regions Not Available
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 2653424 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID O15357 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name O15357_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >3777 bp 
ATGGCCTCGGCCTGCGGGGCGCCGGGCCCGGGGGGCGCCCTGGGCAGCCAGGCCCCCTCC
TGGTACCACCGCGACCTGAGCCGGGCGGCCGCGGAGGAGCTGCTGGCCCGGGCGGGCCGC
GATGGCAGCTTCCTGGTCCGAGACAGCGAGAGCGTGGCGGGGGCCTTCGCGCTCTGCGTC
CTGTATCAGAAGCATGTGCACACGTATCGCATTCTGCCTGATGGAGAAGATTTCTTGGCT
GTGCAGACCTCGCAGGGTGTGCCTGTGCGCCGCTTCCAGACCCTGGGTGAGCTCATCGGC
CTGTACGCCCAGCCCAACCAGGGCCTTGTGTGCGCCCTGCTTCTTCCTGTAGAGGGTGAG
CGAGAGCCGGACCCACCGGATGACCGGGATGCCTCAGATGGGGAGGATGAGAAGCCCCCG
CTGCCCCCGCGCTCTGGCTCCACCAGCATTTCTGCCCCCACTGGGCCCAGCAGTCCCCTG
CCAGCTCCTGAGACTCCCACAGCTCCAGCTGCTGAGAGTGCTCCCAATGGGCTGAGCACC
GTCTCGCACGACTACCTGAAAGGCAGCTATGGGCTGGACCTGGAAGCTGTGAGGGGTGGA
GCCAGCCACCTGCCCCACCTCACCCGTACCCTCGCTACCTCATGCCGGAGGCTGCACAGT
GAGGTGGACAAGGTCCTGTCAGGCCTGGAGATCCTGTCCAAGGTGTTTGACCAGCAGAGC
TCGCCCATGGTGACCCGCCTTTTGCAGCAGCAGAACCTGCCACAGACAGGGGAGCAGGAA
CTAGAGAGCCTGGTGCTGAAGCTGTCAGTGCTAAAGGACTTCCTGTCAGGCATCCAGAAG
AAGGCCCTGAAGGCCCTACAGGACATGAGCTCCACAGCACCCCCAGCTCCGCAGCCATCC
ACACGTAAGGCCAAGACCATCCCCGTGCAGGCCTTTGAGGTGAAGCTAGATGTGACCCTG
GGTGACCTGACCAAGATTGGGAAGTCACAGAAGTTCACGCTGAGCGTGGATGTGGAGGGT
GGGCGGCTGGTGCTGCTGCGGAGACAGCGGGACTCCCAGGAGGACTGGACCACCTTCACG
CACGACCGCATCCGCCAGCTCATTAAGTCCCAGCGTGTCCAGAACAAGCTGGGTGTTGTG
TTTGAGAAGGAGAAGGACCGGACTCAGCGCAAGGACTTCATCTTTGTCAGTGCCCGGAAG
CGGGAGGCCTTCTGCCAGCTGTTGCAGCTCATGAAGAACAAGCACTCCAAGCAGGACGAG
CCCGACATGATCTCAGTCTTCATAGGCACCTGGAACATGGGAAGTGTACCACCTCCAAAA
AACGTGACATCCTGGTTCACATCGAAGGGTCTGGGGAAGACCCTGGACGAGGTCACAGTG
ACCATACCCCATGACATCTATGTCTTTGGGACCCAGGAGAACTCAGTGGGCGACCGCGAG
TGGCTGGACCTACTGCGCGGGGGCCTCAAGGAGCTTACGGATCTGGATTACCGCCCGATT
GCCATGCAATCACTGTGGAATATCAAGGTGGCAGTGCTGGTCAAGCCAGAGCACGAGAAC
CGTATCAGCCATGTCAGTACGTCCAGTGTGAAGACTGGCATCGCCAACACCCTGGGGAAC
AAGGGGGCTGTGGGCGTCTCCTTCATGTTTAATGGCACCTCATTTGGCTTTGTGAATTGT
CACCTCACCTCGGGAAATGAGAAGACGGCTCGGAGGAACCAAAACTACTTGGACATCCTG
CGGCTGCTCTCGCTGGGCGACCGGCAGCTCAATGCCTTTGACATCTCTCTGCGTTTCACA
CACCTCTTCTGGTTTGGGGACCTCAACTACCGCCTGGACATGGATATCCAGGAGATCCTG
AACTACATCAGCAGGAAAGAGTTTGAGCCCCTCCTCAGGGTGGACCAGCTCAACCTGGAG
CGGGAGAAGCACAAGGTCTTCCTTCGATTCAGTGAGGAGGAGATCTCCTTCCCACCCACC
TACCGCTATGAGCGGGGTTCCCGGGACACATATGCCTGGCACAAGCAGAAGCCAACTGGG
GTCCGGACCAATGTGCCCTCATGGTGTGACCGGATTCTGTGGAAATCCTACCCTGAAACT
CACATCATCTGCAATTCTTATGGTTGCACTGATGACATCGTCACCAGCGACCATTCCCCC
GTGTTTGGGACATTTGAGGTTGGAGTTACCTCCCAGTTCATCTCCAAGAAAGGGCTCTCA
AAGACTTCAGACCAGGCCTACATTGAGTTTGAGAGCATCGAGGCCATTGTGAAGACAGCC
AGCCGCACCAAGTTCTTCATCGAGTTCTACTCTACCTGCCTGGAGGAATACAAGAAGAGC
TTTGAGAATGATGCCCAGAGCAGTGACAACATCAACTTCCTCAAAGTGCAGTGGTCTTCA
CGCCAGCTGCCCACGCTCAAACCAATTCTGGCTGATATCGAGTACCTGCAGGACCAGCAC
CTCCTGCTCACAGTCAAGTCCATGGATGGCTATGAATCCTATGGGGAGTGTGTGGTTGCA
CTCAAATCCATGATCGGCAGCACGGCCCAACAGTTCCTGACCTTCCTATCCCACCGTGGC
GAGGAGACAGGCAATATCAGAGGCTCCATGAAGGTGCGGGTGCCCACGGAGCGCCTGGGC
ACCCGTGAGCGGCTCTACGAGTGGATCAGCATTGATAAGGATGAGGCAGGAGCAAAGAGC
AAAGCCCCCTCTGTGTCCCGAGGGAGCCAGGAGCCCAGGTCAGGGAGCCGCAAGCCAGCC
TTCACAGAGGCCTCCTGCCCGCTCTCCAGGTTATTTGAAGAACCAGAGAAACCGCCACCA
ACGGGGAGGCCCCCAGCCCCACCCCGAGCAGCTCCCCGGGAGGAGCCCTTGACCCCCAGG
TTGAAGCCAGAGGGAGCTCCTGAACCAGAAGGGGTGGCGGCCCCCCCACCCAAGAACAGC
TTCAATAACCCTGCCTACTACGTCCTTGAAGGGGTCCCGCACCAGCTGCTGCCCCCGGAG
CCACCCTCGCCTGCCAGGGCCCCTGTCCCATCTGCCACCAAGAACAAAGTGGCCATTACA
GTGCCTGCTCCACAGCTTGGGCACCACCGGCACCCTCGTGTGGGAGAGGGGAGTTCTTCA
GATGAGGAGTCTGGAGGCACACTGCCCCCTCCAGACTTTCCACCTCCACCACTGCCGGAC
TCAGCCATCTTCCTGCCCCCCAGCCTGGATCCTTTACCAGGGCCAGTGGTCCGGGGCCGT
GGTGGGGCTGAGGCCCGTGGCCCACCACCTCCCAAGGCCCATCCAAGGCCTCCACTGCCC
CCAGGCCCCTCACCAGCCAGCACTTTCCTGGGGGAAGTGGGCAGTGGGGATGACCGGTCC
TGCTCGGTGCTGCAGATGGCCAAGACGCTGAGCGAGGTGGACTATGCCCCTGCTGGGCCT
GCACGCTCAGCGCTCCTCCCAGGCCCCCTGGAGCTGCAGCCCCCCCGGGGACTGCCCTCG
GACTATGGCCGGCCCCTCAGCTTCCCTCCACCCCGCATCCGGGAGAGCATCCAGGAAGAC
CTGGCAGAGGAGGCTCCGTGCCTGCAGGGCGGGCGGGCCAGCGGGCTGGGCGAGGCAGGC
ATGAGTGCCTGGCTGCGGGCCATCGGCTTGGAGCGCTATGAGGAGGGCCTGGTGCATAAT
GGCTGGGACGACCTGGAGTTTCTCAGTGACATCACCGAGGAGGACTTGGAGGAGGCTGGG
GTGCAGGACCCGGCTCACAAGCGCCTCCTTCTGGACACCCTGCAGCTCAGCAAGTGA
Enzyme 17 GenBank Gene ID Y14385 Link Image
Enzyme 17 GeneCard ID INPPL1 Link Image
Enzyme 17 GenAtlas ID INPPL1 Link Image
Enzyme 17 HGNC ID HGNC:6080 Link Image
Enzyme 17 Chromosome Location 11
Enzyme 17 Locus 11q23
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Pesesse X, Deleu S, De Smedt F, Drayer L, Erneux C: Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP. Biochem Biophys Res Commun. 1997 Oct 29;239(3):697-700. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 10050
Enzyme 18 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
Enzyme 18 Synonyms
  1. Phosphoinositide phospholipase C delta-3
  2. PLC-delta-3
  3. Phospholipase C-delta-3
Enzyme 18 Gene Name PLCD3
Enzyme 18 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 18 Number of Residues 789
Enzyme 18 Molecular Weight 89259
Enzyme 18 Theoretical pI Not Available
Enzyme 18 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 18 General Function Not Available
Enzyme 18 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 18 Pathways
Enzyme 18 Reactions
  • H2O + 1-Phosphatidyl-1D-myo-inositol 4-phosphate (Homo sapiens) --> diacylglycerol (homo sapiens) + H+ + 1D-myo-Inositol 1,4-bisphosphate
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 18676791 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q8N3E9 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PLCD3_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence Not Available
Enzyme 18 GenBank Gene ID AK074240 Link Image
Enzyme 18 GeneCard ID Not Available
Enzyme 18 GenAtlas ID PLCD3 Link Image
Enzyme 18 HGNC ID HGNC:9061 Link Image
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 12250
Enzyme 19 Name Sphingomyelin phosphodiesterase 3
Enzyme 19 Synonyms
  1. Neutral sphingomyelinase 2
  2. Neutral sphingomyelinase II
  3. nSMase2
  4. nSMase- 2
Enzyme 19 Gene Name SMPD3
Enzyme 19 Protein Sequence >Sphingomyelin phosphodiesterase 3 
MVLYTTPFPNSCLSALHCVSWALIFPCYWLVDRLAASFIPTTYEKRQRADDPCCLQLLCT
ALFTPIYLALLVASLPFAFLGFLFWSPLQSARRPYIYSRLEDKGLAGGAALLSEWKGTGP
GKSFCFATANVCLLPDSLARVNNLFNTQARAKEIGQRIRNGAARPQIKIYIDSPTNTSIS
AASFSSLVSPQGGDGVARAVPGSIKRTASVEYKGDGGRHPGDEAANGPASGDPVDSSSPE
DACIVRIGGEEGGRPPEADDPVPGGQARNGAGGGPRGQTPNHNQQDGDSGSLGSPSASRE
SLVKGRAGPDTSASGEPGANSKLLYKASVVKKAAARRRRHPDEAFDHEVSAFFPANLDFL
CLQEVFDKRAATKLKEQLHGYFEYILYDVGVYGCQGCCSFKCLNSGLLFASRYPIMDVAY
HCYPNKCNDDALASKGALFLKVQVGSTPQDQRIVGYIACTHLHAPQEDSAIRCGQLDLLQ
DWLADFRKSTSSSSAANPEELVAFDVVCGDFNFDNCSSDDKLEQQHSLFTHYRDPCRLGP
GEEKPWAIGTLLDTNGLYDEDVCTPDNLQKVLESEEGRREYLAFPTSKSSGQKGRKELLK
GNGRRIDYMLHAEEGLCPDWKAEVEEFSFITQLSGLTDHLPVAMRLMVSSGEEEA
Enzyme 19 Number of Residues 655
Enzyme 19 Molecular Weight 71081
Enzyme 19 Theoretical pI Not Available
Enzyme 19 GO Classification Not Available
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization
Enzyme 19 Pathways
Enzyme 19 Reactions
  • H2O + sphingomyelin (homo sapiens) --> Choline phosphate + ceramide (homo sapiens) + H+
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • 11-31 65-85
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 8247250 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9NY59 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name NSMA2_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID AJ250460 Link Image
Enzyme 19 GeneCard ID Not Available
Enzyme 19 GenAtlas ID SMPD3 Link Image
Enzyme 19 HGNC ID HGNC:14240 Link Image
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Hofmann K, Tomiuk S, Wolff G, Stoffel W: Cloning and characterization of the mammalian brain-specific, Mg2+-dependent neutral sphingomyelinase. Proc Natl Acad Sci U S A. 2000 May 23;97(11):5895-900. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 12915
Enzyme 20 Name Phospholipid scramblase 2
Enzyme 20 Synonyms
  1. PL scramblase 2
  2. Ca(2+-dependent phospholipid scramblase 2
Enzyme 20 Gene Name PLSCR2
Enzyme 20 Protein Sequence >Phospholipid scramblase 2 
MPAPPPPLNCPPGLEYLSQIDMILIHQQIELLEVLFSFESSNMYEIKNSFGQRIYFAAED
TNFCIRNCCGRSRPFTLRITDNVGREVITLERPLRCNCCCCPCCLQEIEIQAPPGVPVGY
VTQTWHPCLTKFTIKNQKREDVLKISGPCIVCSCIAGVDFEITSLDEQIVVGRISKHWSG
FLREAFTDADNFGIQFPRDLDVKMKAVMIGACFLIDYMFFERTR
Enzyme 20 Number of Residues 224
Enzyme 20 Molecular Weight 25523
Enzyme 20 Theoretical pI 5.34
Enzyme 20 GO Classification Not Available
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 204-220
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 9651165 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q9NRY7 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name PLS2_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence Not Available
Enzyme 20 GenBank Gene ID AF159441 Link Image
Enzyme 20 GeneCard ID Q9NRY7 Link Image
Enzyme 20 GenAtlas ID PLSCR2 Link Image
Enzyme 20 HGNC ID HGNC:16494 Link Image
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus Not Available
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed Link Image]
Enzyme 20 Metabolite References
  1. Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed Link Image]
Enzyme 21 [top]
Enzyme 21 ID 12916
Enzyme 21 Name Phospholipid scramblase 3
Enzyme 21 Synonyms
  1. PL scramblase 3
  2. Ca(2+-dependent phospholipid scramblase 3
Enzyme 21 Gene Name PLSCR3
Enzyme 21 Protein Sequence >Phospholipid scramblase 3 
MAGYLPPKGYAPSPPPPYPVTPGYPEPALHPGPGQAPVPAQVPAPAPGFALFPSPGPVAL
GSAAPFLPLPGVPSGLEFLVQIDQILIHQKAERVETFLGWETCNRYELRSGAGQPLGQAA
EESNCCARLCCGARRPLRVRLADPGDREVLRLLRPLHCGCSCCPCGLQEMEVQAPPGTTI
GHVLQTWHPFLPKFSIQDADRQTVLRVVGPCWTCGCGTDTNFEVKTRDESRSVGRISKQW
GGLVREALTDADDFGLQFPLDLDVRVKAVLLGATFLIDYMFFEKRGGAGPSAITS
Enzyme 21 Number of Residues 295
Enzyme 21 Molecular Weight 31663
Enzyme 21 Theoretical pI 6.63
Enzyme 21 GO Classification Not Available
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 266-282
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 9651167 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q9NRY6 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name PLS3_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence Not Available
Enzyme 21 GenBank Gene ID AF159442 Link Image
Enzyme 21 GeneCard ID Q9NRY6 Link Image
Enzyme 21 GenAtlas ID PLSCR3 Link Image
Enzyme 21 HGNC ID HGNC:16495 Link Image
Enzyme 21 Chromosome Location Not Available
Enzyme 21 Locus Not Available
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed Link Image]
Enzyme 21 Metabolite References
  1. Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed Link Image]
Enzyme 22 [top]
Enzyme 22 ID 12917
Enzyme 22 Name Phospholipid scramblase 4
Enzyme 22 Synonyms
  1. PL scramblase 4
  2. Ca(2+-dependent phospholipid scramblase 4
  3. TRA1
  4. Cell growth-inhibiting gene 43 protein
Enzyme 22 Gene Name PLSCR4
Enzyme 22 Protein Sequence >Phospholipid scramblase 4 
MSGVVPTAPEQPAGEMENQTKPPDPRPDAPPEYSSHFLPGPPGTAVPPPTGYPGGLPMGY
YSPQQPSTFPLYQPVGGIHPVRYQPGKYPMPNQSVPITWMPGPTPMANCPPGLEYLVQLD
NIHVLQHFEPLEMMTCFETNNRYDIKNNSDQMVYVVTEDTDDFTRNAYRTLRPFVLRVTD
CMGREIMTMQRPFRCTCCCFCCPSARQELEVQCPPGVTIGFVAEHWNLCRAVYSIQNEKK
ENVMRVRGPCSTYGCGSDSVFEVKSLDGISNIGSIIRKWNGLLSAMADADHFDIHFPLDL
DVKMKAMIFGACFLIDFMYFERSPPQRSR
Enzyme 22 Number of Residues 329
Enzyme 22 Molecular Weight 36965
Enzyme 22 Theoretical pI 5.62
Enzyme 22 GO Classification Not Available
Enzyme 22 General Function Not Available
Enzyme 22 Specific Function May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 304-320
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 9622872 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q9NRQ2 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name PLS4_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 AF199023 Link Image
Enzyme 22 GeneCard ID Q9NRQ2 Link Image
Enzyme 22 GenAtlas ID PLSCR4 Link Image
Enzyme 22 HGNC ID HGNC:16497 Link Image
Enzyme 22 Chromosome Location Not Available
Enzyme 22 Locus Not Available
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed Link Image]
Enzyme 22 Metabolite References
  1. Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed Link Image]
Enzyme 23 [top]
Enzyme 23 ID 12918
Enzyme 23 Name Phospholipid scramblase family memmber 5
Enzyme 23 Synonyms Not Available
Enzyme 23 Gene Name PLSCR5
Enzyme 23 Protein Sequence >Phospholipid scramblase family memmber 5 
MASKDAQNQRRGLPGFLPGAPDPDQSLPASSNPGNQAWQLSLPLPSSFLPTVSLPPGLEY
LSQLDLIIIHQQVELLGMILGAETSNKYEIKNSLGQRIYFAVEESICFNRTFCSTLRSCT
LRITDNSGREVITVNRPLRCNSCWCPCYLQELEIQAPPGTIVGYVTQKWDPFLPKFTIQN
ANKEDILKIVGPCVTCGCFGDVDFEVKTINEKLTIGKISKYWSGFVNDVFTNADNFGIHV
PADLDVTVKAAMIGACFLFDFMFFEHSLAGL
Enzyme 23 Number of Residues 271
Enzyme 23 Molecular Weight 29997
Enzyme 23 Theoretical pI 4.90
Enzyme 23 GO Classification Not Available
Enzyme 23 General Function Not Available
Enzyme 23 Specific Function Not Available
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 41323046 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID A0PG75 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name PLS5_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence Not Available
Enzyme 23 GenBank Gene ID AY436642 Link Image
Enzyme 23 GeneCard ID A0PG75 Link Image
Enzyme 23 GenAtlas ID PLSCR5 Link Image
Enzyme 23 HGNC ID HGNC:19952 Link Image
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References Not Available
Enzyme 23 Metabolite References
  1. Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed Link Image]
Enzyme 24 [top]
Enzyme 24 ID 12929
Enzyme 24 Name Phospholipase A1 member A precursor
Enzyme 24 Synonyms
  1. Phosphatidylserine- specific phospholipase A1
  2. PS-PLA1
Enzyme 24 Gene Name PLA1A
Enzyme 24 Protein Sequence >Phospholipase A1 member A precursor 
MPPGPWESCFWVGGLILWLSVGSSGDAPPTPQPKCADFQSANLFEGTDLKVQFLLFVPSN
PSCGQLVEGSSDLQNSGFNATLGTKLIIHGFRVLGTKPSWIDTFIRTLLRATNANVIAVD
WIYGSTGVYFSAVKNVIKLSLEISLFLNKLLVLGVSESSIHIIGVSLGAHVGGMVGQLFG
GQLGQITGLDPAGPEYTRASVEERLDAGDALFVEAIHTDTDNLGIRIPVGHVDYFVNGGQ
DQPGCPTFFYAGYSYLICDHMRAVHLYISALENSCPLMAFPCASYKAFLAGRCLDCFNPF
LLSCPRIGLVEQGGVKIEPLPKEVKVYLLTTSSAPYCMHHSLVEFHLKELRNKDTNIEVT
FLSSNITSSSKITIPKQQRYGKGIIAHATPQCQINQVKFKFQSSNRVWKKDRTTIIGKFC
TALLPVNDREKMVCLPEPVNLQASVTVSCDLKIACV
Enzyme 24 Number of Residues 456
Enzyme 24 Molecular Weight 49716
Enzyme 24 Theoretical pI 7.40
Enzyme 24 GO Classification
Function
  • catalytic activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 24 General Function Not Available
Enzyme 24 Specific Function Hydrolyzes the ester bond at the sn-1 position of glycerophospholipids and produces 2-acyl lysophospholipids. Hydrolyzes phosphatidylserine (PS) in the form of liposomes and 1- acyl-2 lysophosphatidylserine (lyso-PS), but not triolein, phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidic acid (PA) or phosphatidylinositol (PI). Isoform 2 hydrolyzes lyso-PS but not PS. Hydrolysis of lyso-PS in peritoneal mast cells activated by receptors for IgE leads to stimulate histamine production
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • 1-25
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 4096697 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q53H76 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PLA1A_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence Not Available
Enzyme 24 GenBank Gene ID U37591 Link Image
Enzyme 24 GeneCard ID Q53H76 Link Image
Enzyme 24 GenAtlas ID PLA1A Link Image
Enzyme 24 HGNC ID HGNC:17661 Link Image
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Nagai Y, Aoki J, Sato T, Amano K, Matsuda Y, Arai H, Inoue K: An alternative splicing form of phosphatidylserine-specific phospholipase A1 that exhibits lysophosphatidylserine-specific lysophospholipase activity in humans. J Biol Chem. 1999 Apr 16;274(16):11053-9. [PubMed Link Image]
Enzyme 24 Metabolite References
  1. Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed Link Image]
Enzyme 25 [top]
Enzyme 25 ID 12930
Enzyme 25 Name Serum deprivation-response protein
Enzyme 25 Synonyms
  1. Phosphatidylserine-binding protein
  2. PS-p68
Enzyme 25 Gene Name SDPR
Enzyme 25 Protein Sequence >Serum deprivation-response protein 
MGEDAAQAEKFQHPGSDMRQEKPSSPSPMPSSTPSPSLNLGNTEEAIRDNSQVNAVTVLT
LLDKLVNMLDAVQENQHKMEQRQISLEGSVKGIQNDLTKLSKYQASTSNTVSKLLEKSRK
VSAHTRAVKERMDRQCAQVKRLENNHAQLLRRNHFKVLIFQEENEIPASVFVKQPVSGAV
EGKEELPDENKSLEETLHTVDLSSDDDLPHDEEALEDSAEEKVEESRAEKIKRSSLKKVD
SLKKAFSRQNIEKKMNKLGTKIVSVERREKIKKSLTSNHQKISSGKSSPFKVSPLTFGRK
KVREGESHAENETKSEDLPSSEQMPNDQEEESFAEGHSEASLASALVEGEIAEEAAEKAT
SRGSNSGMDSNIDLTIVEDEEEESVALEQAQKVRYEGSYALTSEEAERSDGDPVQPAVLQ
VHQTS
Enzyme 25 Number of Residues 425
Enzyme 25 Molecular Weight 47174
Enzyme 25 Theoretical pI 4.88
Enzyme 25 GO Classification Not Available
Enzyme 25 General Function Not Available
Enzyme 25 Specific Function May play a role in targeting PRKCA to caveolae
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function Not Available
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 4336416 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID O95810 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name SDPR_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence Not Available
Enzyme 25 GenBank Gene ID AF085481 Link Image
Enzyme 25 GeneCard ID O95810 Link Image
Enzyme 25 GenAtlas ID SDPR Link Image
Enzyme 25 HGNC ID HGNC:10690 Link Image
Enzyme 25 Chromosome Location Not Available
Enzyme 25 Locus Not Available
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Gustincich S, Vatta P, Goruppi S, Wolf M, Saccone S, Della Valle G, Baggiolini M, Schneider C: The human serum deprivation response gene (SDPR) maps to 2q32-q33 and codes for a phosphatidylserine-binding protein. Genomics. 1999 Apr 1;57(1):120-9. [PubMed Link Image]
  2. Burgener R, Wolf M, Ganz T, Baggiolini M: Purification and characterization of a major phosphatidylserine-binding phosphoprotein from human platelets. Biochem J. 1990 Aug 1;269(3):729-34. [PubMed Link Image]
Enzyme 25 Metabolite References
  1. Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed Link Image]
Enzyme 26 [top]
Enzyme 26 ID 13172
Enzyme 26 Name Transcriptional regulator ATRX
Enzyme 26 Synonyms
  1. ATP-dependent helicase ATRX
  2. X-linked helicase II
  3. X-linked nuclear protein
  4. XNP
  5. Znf- HX
Enzyme 26 Gene Name ATRX
Enzyme 26 Protein Sequence >Transcriptional regulator ATRX 
MTAEPMSESKLNTLVQKLHDFLAHSSEESEETSSPPRLAMNQNTDKISGSGSNSDMMENS
KEEGTSSSEKSKSSGSSRSKRKPSIVTKYVESDDEKPLDDETVNEDASNENSENDITMQS
LPKGTVIVQPEPVLNEDKDDFKGPEFRSRSKMKTENLKKRGEDGLHGIVSCTACGQQVNH
FQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFC
KKCILRNLGRKELSTIMDENNQWYCYICHPEPLLDLVTACNSVFENLEQLLQQNKKKIKV
DSEKSNKVYEHTSRFSPKKTSSNCNGEEKKLDDSCSGSVTYSYSALIVPKEMIKKAKKLI
ETTANMNSSYVKFLKQATDNSEISSATKLRQLKAFKSVLADIKKAHLALEEDLNSEFRAM
DAVNKEKNTKEHKVIDAKFETKARKGEKPCALEKKDISKSEAKLSRKQVDSEHMHQNVPT
EEQRTNKSTGGEHKKSDRKEEPQYEPANTSEDLDMDIVSVPSSVPEDIFENLETAMEVQS
SVDHQGDGSSGTEQEVESSSVKLNISSKDNRGGIKSKTTAKVTKELYVKLTPVSLPNSPI
KGADCQEVPQDKDGYKSCGLNPKLEKCGLGQENSDNEHLVENEVSLLLEESDLRRSPRVK
TTPLRRPTETNPVTSNSDEECNETVKEKQKLSVPVRKKDKRNSSDSAIDNPKPNKLPKSK
QSETVDQNSDSDEMLAILKGVSRMSHSSSSDTDINEIHTNHKTLYDLKTQAGKDDKGKRK
RKSSTSGSDFDTKKGKSAKSSIISKKKRQTQSESSNYDSELEKEIKSMSKIGAARTTKKR
IPNTKDFDSSEDEKHSKKGMDNQGHKNLKTSQEGSSDDAERKQERETFSSAEGTVDKDTT
IMELRDRLPKKQQASASTDGVDKLSGKEQSFTSLEVRKVAETKEKSKHLKTKTCKKVQDG
LSDIAEKFLKKDQSDETSEDDKKQSKKGTEEKKKPSDFKKKVIKMEQQYESSSDGTEKLP
EREEICHFPKGIKQIKNGTTDGEKKSKKIRDKTSKKKDELSDYAEKSTGKGDSCDSSEDK
KSKNGAYGREKKRCKLLGKSSRKRQDCSSSDTEKYSMKEDGCNSSDKRLKRIELRERRNL
SSKRNTKEIQSGSSSSDAEESSEDNKKKKQRTSSKKKAVIVKEKKRNSLRTSTKRKQADI
TSSSSSDIEDDDQNSIGEGSSDEQKIKPVTENLVLSSHTGFCQSSGDEALSKSVPVTVDD
DDDDNDPENRIAKKMLLEEIKANLSSDEDGSSDDEPEEGKKRTGKQNEENPGDEEAKNQV
NSESDSDSEESKKPRYRHRLLRHKLTVSDGESGEEKKTKPKEHKEVKGRNRRKVSSEDSE
DSDFQESGVSEEVSESEDEQRPRTRSAKKAELEENQRSYKQKKKRRRIKVQEDSSSENKS
NSEEEEEEKEEEEEEEEEEEEEEEDENDDSKSPGKGRKKIRKILKDDKLRTETQNALKEE
EERRKRIAEREREREKLREVIEIEDASPTKCPITTKLVLDEDEETKEPLVQVHRNMVIKL
KPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDFS
TALVVCPLNTALNWMNEFEKWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEDGGVMI
IGYEMYRNLAQGRNVKSRKLKEIFNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRS
RRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDVRVM
KKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTSIQCKLYQYYLDHLTGVGNN
SEGGRGKAGAKLFQDFQMLSRIWTHPWCLQLDYISKENKGYFDEDSMDEFIASDSDETSM
SLSSDDYTKKKKKGKKGKKDSSSSGSGSDNDVEVIKVWNSRSRGGGEGNVDETGNNPSVS
LKLEESKATSSSNPSSPAPDWYKDFVTDADAEVLEHSGKMVLLFEILRMAEEIGDKVLVF
SQSLISLDLIEDFLELASREKTEDKDKPLIYKGEGKWLRNIDYYRLDGSTTAQSRKKWAE
EFNDETNVRGRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPV
YVYRFLAQGTMEDKIYDRQVTKQSLSFRVVDQQQVERHFTMNELTELYTFEPDLLDDPNS
EKKKKRDTPMLPKDTILAELLQIHKEHIVGYHEHDSLLDHKEEEELTEEERKAAWAEYEA
EKKVLTMRFNIPTGTNLPPVSFNSQTPYIPFNLGALSAMSNQQLEDLINQGREKVVEATN
SVTAVRIQPLEDIISAVWKENMNLSEAQVQALALSRQASQELDVKRREAIYNDVLTKQQM
LISCVQRILMNRRLQQQYNQQQQQQMTYQQATLGHLMMPKPPNLIMNPSNYQQIDMRGMY
QPVAGGMQPPPLQRAPPPMRSKNPGPSQGKSM
Enzyme 26 Number of Residues 2492
Enzyme 26 Molecular Weight 282568
Enzyme 26 Theoretical pI 6.57
Enzyme 26 GO Classification
Function
  • ATP binding
  • DNA binding
  • acid-amino acid ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • helicase activity
  • ion binding
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleic acid binding
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
  • transition metal ion binding
  • ubiquitin-protein ligase activity
  • zinc ion binding
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein modification
  • protein ubiquitination
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • ubiquitin cycle
Component
  • protein complex
  • ubiquitin ligase complex
Enzyme 26 General Function Transcription
Enzyme 26 Specific Function Could be a global transcriptional regulator. Modifies gene expression by affecting chromatin. May be involved in brain development and facial morphogenesis
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 6960326 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P46100 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name ATRX_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >7479 bp 
ATGACCGCTGAGCCCATGAGTGAAAGCAAGTTGAATACATTGGTGCAGAAGCTTCATGAC
TTCCTTGCACACTCATCAGAAGAATCTGAAGAAACAAGTTCTCCTCCACGACTTGCAATG
AATCAAAACACAGATAAAATCAGTGGTTCTGGAAGTAACTCTGATATGATGGAAAACAGC
AAGGAAGAGGGAACTAGCTCTTCAGAAAAATCCAAGTCTTCAGGATCGTCACGATCAAAG
AGGAAACCTTCAATTGTAACAAAGTATGTAGAATCAGATGATGAAAAACCTTTGGATGAT
GAAACTGTAAATGAAGATGCGTCTAATGAAAATTCAGAAAATGATATTACTATGCAGAGC
TTGCCAAAAGGTACAGTGATTGTACAGCCAGAGCCAGTGCTGAATGAAGACAAAGATGAT
TTTAAAGGGCCTGAATTTAGAAGCAGAAGTAAAATGAAAACTGAAAATCTCAAAAAACGC
GGAGAAGATGGGCTTCATGGGATTGTGAGCTGCACTGCTTGTGGACAACAGGTCAATCAT
TTTCAAAAAGATTCCATTTATAGACACCCTTCATTGCAAGTTCTTATTTGTAAGAATTGC
TTTAAGTATTACATGAGTGATGATATTAGCCGTGACTCAGATGGAATGGATGAACAATGT
AGGTGGTGTGCGGAAGGTGGAAACTTGATTTGTTGTGACTTTTGCCATAATGCTTTCTGC
AAGAAATGCATTCTACGCAACCTTGGTCGAAAGGAGTTGTCCACAATAATGGATGAAAAC
AACCAATGGTATTGCTACATTTGTCACCCAGAGCCTTTGTTGGACTTGGTCACTGCATGT
AACAGCGTATTTGAGAATTTAGAACAGTTGTTGCAGCAAAATAAGAAGAAGATAAAAGTT
GACAGTGAAAAGAGTAATAAAGTATATGAACATACATCCAGATTTTCTCCAAAGAAGACT
AGTTCAAATTGTAATGGAGAAGAAAAGAAATTAGATGATTCCTGTTCTGGCTCTGTAACC
TACTCTTATTCCGCACTAATTGTGCCCAAAGAGATGATTAAGAAGGCAAAAAAACTGATT
GAGACCACAGCCAACATGAACTCCAGTTATGTTAAATTTTTAAAGCAGGCAACAGATAAT
TCAGAAATCAGTTCTGCTACAAAATTACGTCAGCTTAAGGCTTTTAAGTCTGTGTTGGCT
GATATTAAGAAGGCTCATCTTGCATTGGAAGAAGACTTAAATTCCGAGTTTCGAGCGATG
GATGCTGTAAACAAAGAGAAAAATACCAAAGAGCATAAAGTCATAGATGCTAAGTTTGAA
ACAAAAGCACGAAAAGGAGAAAAACCTTGTGCTTTGGAAAAGAAGGATATTTCAAAGTCA
GAAGCTAAACTTTCAAGAAAACAGGTAGATAGTGAGCACATGCATCAGAATGTTCCAACA
GAGGAACAAAGAACAAATAAAAGTACCGGTGGTGAACATAAGAAATCTGATAGAAAAGAA
GAACCTCAATATGAACCTGCCAACACTTCTGAAGATTTAGACATGGATATTGTGTCTGTT
CCTTCCTCAGTTCCAGAAGACATTTTTGAGAATCTTGAGACTGCTATGGAAGTTCAGAGT
TCAGTTGATCATCAAGGGGATGGCAGCAGTGGAACTGAACAAGAAGTGGAGAGTTCATCT
GTAAAATTAAATATTTCTTCAAAAGACAACAGAGGAGGTATTAAATCAAAAACTACAGCT
AAAGTAACAAAAGAATTATATGTTAAACTCACTCCTGTTTCCCTTTCTAATTCCCCAATT
AAAGGTGCTGATTGTCAGGAAGTTCCACAAGATAAAGATGGCTATAAAAGTTGTGGTCTG
AACCCCAAGTTAGAGAAATGTGGACTTGGACAGGAAAACAGTGATAATGAGCATTTGGTT
GAAAATGAAGTTTCATTACTTTTAGAGGAATCTGATCTTCGAAGATCCCCACGTGTAAAG
ACTACACCCTTGAGGCGACCGACAGAAACTAACCCTGTAACATCTAATTCAGATGAAGAA
TGTAATGAAACAGTTAAGGAGAAACAAAAACTATCAGTTCCAGTGAGAAAAAAGGATAAG
CGTAATTCTTCTGACAGTGCTATAGATAATCCTAAGCCTAATAAATTGCCAAAATCTAAG
CAATCAGAGACTGTGGATCAAAATTCAGATTCTGATGAAATGCTAGCAATCCTCAAAGAG
GTGAGCAGGATGAGTCACAGTTCTTCTTCAGATACTGATATTAATGAAATTCATACAAAC
CATAAGACTTTGTATGATTTAAAGACTCAGGCGGGGAAAGATGATAAAGGAAAAAGGAAA
CGAAAAAGTTCTACATCTGGCTCAGATTTTGATACTAAAAAGGGCAAATCAGCTAAGAGC
TCTATAATTTCTAAAAAGAAACGACAAACCCAGTCTGAGTCTTCTAATTATGACTCAGAA
TTAGAAAAAGAGATAAAGAGCATGAGTAAAATTGGTGCTGCCAGAACCACCAAAAAAAGA
ATTCCAAATACAAAAGATTTTGACTCTTCTGAAGATGAGAAACACAGCAAAAAAGGAATG
GATAATCAAGGGCACAAAAATTTGAAGACCTCACAAGAAGGATCATCTGATGATGCTGAA
AGAAAACAAGAGAGAGAGACTTTCTCTTCAGCAGAAGGCACAGTTGATAAAGACACGACC
ATCATGGAATTAAGAGATCGACTTCCTAAGAAGCAGCAAGCAAGTGCTTCCACTGATGGT
GTCGATAAGCTTTCTGGGAAAGAGCAGAGTTTTACTTCTTTGGAAGTTAGAAAAGTTGCT
GAAACTAAAGAAAAGAGCAAGCATCTCAAAACCAAAACATGTAAAAAAGTACAGGATGGC
TTATCTGATATTGCAGAGAAATTCCTAAAGAAAGACCAGAGCGATGAAACTTCTGAAGAT
GATAAAAAGCAGAGCAAAAAGGGAACTGAAGAAAAAAAGAAACCTTCAGACTTTAAGAAA
AAAGTAATTAAAATGGAACAACAGTATGAATCTTCATCTGATGGCACTGAAAAGTTACCT
GAGCGAGAAGAAATTTGTCATTTTCCTAAGGGCATAAAACAAATTAAGAATGGAACAACT
GATGGAGAAAAGAAAAGTAAAAAAATAAGAGATAAAACTTCTAAAAAGAAGGATGAATTA
TCTGATTATGCTGAGAAGTCAACAGGGAAAGGAGATAGTTGTGACTCTTCAGAGGATAAA
AAGAGTAAGAATGGAGCATATGGTAGAGAGAAGAAAAGGTGCAAGTTGCTTGGAAAGAGT
TCAAGGAAGAGACAAGATTGTTCATCATCTGATACTGAGAAATATTCCATGAAAGAAGAT
GGTTGTAACTCTTCTGATAAGAGACTGAAAAGAATAGAATTGAGGGAAAGAAGAAATTTA
AGTTCAAAGAGAAATACTAAGGAAATACAAAGTGGCTCATCATCATCTGATGCTGAGGAA
AGTTCTGAAGATAATAAAAAGAAGAAGCAAAGAACTTCATCTAAAAAGAAGGCAGTCATT
GTCAAGGAGAAAAAGAGAAACTCCCTAAGAACAAGCACTAAAAGGAAGCAAGCTGACATT
ACATCCTCATCTTCTTCTGATATAGAAGATGATGATCAGAATTCTATAGGTGAGGGAAGC
AGCGATGAACAGAAAATTAAGCCTGTGACTGAAAATTTAGTGCTGTCTTCACATACTGGA
TTTTGCCAATCTTCAGGAGATGAAGCCTTATCTAAATCAGTGCCTGTCACAGTGGATGAT
GATGATGACGACAATGATCCTGAGAATAGAATTGCCAAGAAGATGCTTTTAGAAGAAATT
AAAGCCAATCTTTCCTCTGATGAGGATGGATCTTCAGATGATGAGCCAGAAGAAGGGAAA
AAAAGAACTGGAAAACAAAATGAAGAAAACCCAGGAGATGAGGAAGCAAAAAATCAAGTC
AATTCTGAATCAGATTCAGATTCTGAAGAATCTAAGAAGCCAAGATACAGACATAGGCTT
TTGCGGCACAAATTGACTGTGAGTGACGGAGAATCTGGAGAAGAAAAAAAGACAAAGCCT
AAAGAGCATAAAGAAGTCAAAGGCAGAAACAGAAGAAAGGTGAGCAGTGAAGATTCAGAA
GATTCTGATTTTCAGGAATCAGGAGTTAGTGAAGAAGTTAGTGAATCCGAAGATGAACAG
CGGCCCAGAACAAGGTCTGCAAAGAAAGCAGAGTTGGAAGAAAATCAGCGGAGCTATAAA
CAGAAAAAGAAAAGGCGACGTATTAAGGTTCAAGAAGATTCATCCAGTGAAAACAAGAGT
AATTCTGAGGAAGAAGAGGAGGAAAAAGAAGAGGAGGAGGAAGAGGAGGAGGAGGAGGAA
GAGGAGGAGGAAGATGAAAATGATGATTCCAAGTCTCCTGGAAAAGGCAGAAAGAAAATT
CGGAAGATTCTTAAAGATGATAAACTGAGAACAGAAACACAAAATGCTCTTAAGGAAGAG
GAAGAGAGACGAAAACGTATTGCTGAGAGGGAGCGTGAGCGAGAAAAATTGAGAGAGGTG
ATAGAAATTGAAGATGCTTCACCCACCAAGTGTCCAATAACAACCAAGTTGGTTTTAGAT
GAAGATGAAGAAACCAAAGAACCTTTAGTGCAGGTTCATAGAAATATGGTTATCAAATTG
AAACCCCATCAAGTAGATGGTGTTCAGTTTATGTGGGATTGCTGCTGTGAGTCTGTGAAA
AAAACAAAGAAATCTCCAGGTTCAGGATGCATTCTTGCCCACTGTATGGGCCTTGGTAAG
ACTTTACAGGTGGTAAGTTTTCTTCATACAGTTCTTTTGTGTGACAAACTGGATTTCAGC
ACGGCGTTAGTGGTTTGTCCTCTTAATACTGCTTTGAATTGGATGAATGAATTTGAGAAG
TGGCAAGAGGGATTAAAAGATGATGAGAAGCTTGAGGTTTCTGAATTAGCAACTGTGAAA
CGTCCTCAGGAGAGAAGCTACATGCTGCAGAGGTGGCAAGAAGATGGTGGTGTTATGATC
ATAGGCTATGAGATGTATAGAAATCTTGCTCAAGGAAGGAATGTGAAGAGTCGGAAACTT
AAAGAAATATTTAACAAAGCTTTGGTTGATCCAGGCCCTGATTTTGTTGTTTGTGATGAA
GGCCATATTCTAAAAAATGAAGCATCTGCTGTTTCTAAAGCTATGAATTCTATACGATCA
AGGAGGAGGATTATTTTAACAGGAACACCACTTCAAAATAACCTAATTGAGTATCATTGT
ATGGTTAATTTTATCAAGGAAAATTTACTTGGATCCATTAAGGAGTTCAGGAATAGATTT
ATAAATCCAATTCAAAATGGTCAGTGTGCAGATTCTACCATGGTAGATGTCAGAGTGATG
AAAAAACGTGCTCACATTCTCTATGAGATGTTAGCTGGATGTGTTCAGAGGAAAGATTAT
ACAGCATTAACAAAATTCTTGCCTCCAAAACACGAATATGTGTTAGCTGTGAGAATGACT
TCTATTCAGTGCAAGCTCTATCAGTACTACTTAGATCACTTAACAGGTGTGGGCAATAAT
AGTGAAGGTGGAAGAGGAAAGGCAGGTGCAAAGCTTTTCCAAGATTTTCAGATGTTAAGT
AGAATATGGACTCATCCTTGGTGTTTGCAGCTAGACTACATTAGCAAAGAAAATAAGGGT
TATTTTGATGAAGACAGTATGGATGAATTTATAGCCTCAGATTCTGATGAAACCTCCATG
AGTTTAAGCTCCGATGATTATACAAAAAAGAAGAAAAAAGGGAAAAAGGGGAAAAAAGAT
AGTAGCTCAAGTGGAAGTGGCAGTGACAATGATGTTGAAGTGATTAAGGTCTGGAATTCA
AGATCTCGGGGAGGTGGTGAAGGAAATGTGGATGAAACAGGAAACAATCCTTCTGTTTCT
TTAAAACTGGAAGAAAGTAAAGCTACTTCTTCTTCTAATCCAAGCAGCCCAGCTCCAGAC
TGGTACAAAGATTTTGTTACAGATGCTGATGCTGAGGTTTTAGAGCATTCTGGGAAAATG
GTACTTCTCTTTGAAATTCTTCGAATGGCAGAGGAAATTGGGGATAAAGTCCTTGTTTTC
AGCCAGTCCCTCATATCTCTGGACTTGATTGAAGATTTTCTTGAATTAGCTAGTAGGGAG
AAGACAGAAGATAAAGATAAACCCCTTATTTATAAAGGTGAGGGGAAGTGGCTTCGAAAC
ATTGACTATTACCGTTTAGATGGTTCCACTACTGCACAGTCAAGGAAGAAGTGGGCTGAA
GAATTTAATGATGAAACTAATGTGAGAGGACGATTATTTATCATTTCTACTAAAGCAGGA
TCTCTAGGAATTAATCTGGTAGCTGCTAATCGAGTAATTATATTCGACGCTTCTTGGAAT
CCATCTTATGACATCCAGAGTATATTCAGAGTTTATCGCTTTGGACAAACTAAGCCTGTT
TATGTATATAGGTTCTTAGCTCAGGGAACCATGGAAGATAAGATTTATGATCGGCAAGTA
ACTAAGCAGTCACTGTCTTTTCGAGTTGTTGATCAGCAGCAGGTGGAGCGTCATTTTACT
ATGAATGAGCTTACTGAACTTTATACTTTTGAGCCAGACTTATTAGATGACCCTAATTCA
GAAAAGAAGAAGAAGAGGGATACTCCCATGCTGCCAAAGGATACCATACTTGCAGAGCTC
CTTCAGATACATAAAGAACACATTGTAGGATACCATGAACATGATTCTCTTTTGGACCAC
AAAGAAGAAGAAGAGTTGACTGAAGAAGAAAGAAAAGCAGCTTGGGCTGAGTATGAAGCA
GAGAAGAAGGGACTGACCATGCGTTTCAACATACCAACTGGGACCAATTTACCCCCTGTC
AGTTTCAACTCTCAAACTCCTTATATTCCTTTCAATTTGGGAGCCCTGTCAGCAATGAGT
AATCAACAGCTGGAGGACCTCATTAATCAAGGAAGAGAAAAAGTTGTAGAAGCAACAAAC
AGTGTGACAGCAGTGAGGATTCAACCTCTTGAGGATATAATTTCAGCTGTATGGAAGGAG
AACATGAATCTCTCAGAGGCCCAAGTACAGGCGTTAGCATTAAGTAGACAAGCCAGCCAG
GAGCTTGATGTTAAACGAAGAGAAGCAATCTACAATGATGTATTGACAAAACAACAGATG
TTAATCAGCTGTGTTCAGCGAATACTTATGAACAGAAGGCTCCAGCAGCAGTACAATCAG
CAGCAACAGCAACAAATGACTTATCAACAAGCAACACTGGGTCACCTCATGATGCCAAAG
CCCCCAAATTTGATCATGAATCCTTCTAACTACCAGCAGATTGATATGAGAGGAATGTAT
CAGCCAGTGGCTGGTGGTATGCAGCCACCACCATTACAGCGTGCACCACCCCCAATGAGA
AGCAAAAATCCAGGACCTTCCCAAGGGAAATCAATGTGA
Enzyme 26 GenBank Gene ID U72937 Link Image
Enzyme 26 GeneCard ID P46100 Link Image
Enzyme 26 GenAtlas ID ATRX Link Image
Enzyme 26 HGNC ID HGNC:886 Link Image
Enzyme 26 Chromosome Location Not Available
Enzyme 26 Locus Not Available
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Picketts DJ, Higgs DR, Bachoo S, Blake DJ, Quarrell OW, Gibbons RJ: ATRX encodes a novel member of the SNF2 family of proteins: mutations point to a common mechanism underlying the ATR-X syndrome. Hum Mol Genet. 1996 Dec;5(12):1899-907. [PubMed Link Image]
  2. Villard L, Lossi AM, Cardoso C, Proud V, Chiaroni P, Colleaux L, Schwartz C, Fontes M: Determination of the genomic structure of the XNP/ATRX gene encoding a potential zinc finger helicase. Genomics. 1997 Jul 15;43(2):149-55. [PubMed Link Image]
  3. Kitano T, Schwarz C, Nickel B, Paabo S: Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees. Mol Biol Evol. 2003 Aug;20(8):1281-9. Epub 2003 May 30. [PubMed Link Image]
  4. Stayton CL, Dabovic B, Gulisano M, Gecz J, Broccoli V, Giovanazzi S, Bossolasco M, Monaco L, Rastan S, Boncinelli E, et al.: Cloning and characterization of a new human Xq13 gene, encoding a putative helicase. Hum Mol Genet. 1994 Nov;3(11):1957-64. [PubMed Link Image]
  5. Gecz J, Pollard H, Consalez G, Villard L, Stayton C, Millasseau P, Khrestchatisky M, Fontes M: Cloning and expression of the murine homologue of a putative human X-linked nuclear protein gene closely linked to PGK1 in Xq13.3. Hum Mol Genet. 1994 Jan;3(1):39-44. [PubMed Link Image]
  6. Gibbons RJ, Picketts DJ, Villard L, Higgs DR: Mutations in a putative global transcriptional regulator cause X-linked mental retardation with alpha-thalassemia (ATR-X syndrome). Cell. 1995 Mar 24;80(6):837-45. [PubMed Link Image]
  7. Cardoso C, Timsit S, Villard L, Khrestchatisky M, Fontes M, Colleaux L: Specific interaction between the XNP/ATR-X gene product and the SET domain of the human EZH2 protein. Hum Mol Genet. 1998 Apr;7(4):679-84. [PubMed Link Image]
  8. McDowell TL, Gibbons RJ, Sutherland H, O'Rourke DM, Bickmore WA, Pombo A, Turley H, Gatter K, Picketts DJ, Buckle VJ, Chapman L, Rhodes D, Higgs DR: Localization of a putative transcriptional regulator (ATRX) at pericentromeric heterochromatin and the short arms of acrocentric chromosomes. Proc Natl Acad Sci U S A. 1999 Nov 23;96(24):13983-8. [PubMed Link Image]
  9. Villard L, Fontes M, Ades LC, Gecz J: Identification of a mutation in the XNP/ATR-X gene in a family reported as Smith-Fineman-Myers syndrome. Am J Med Genet. 2000 Mar 6;91(1):83-5. [PubMed Link Image]
  10. Gibbons RJ, Pellagatti A, Garrick D, Wood WG, Malik N, Ayyub H, Langford C, Boultwood J, Wainscoat JS, Higgs DR: Identification of acquired somatic mutations in the gene encoding chromatin-remodeling factor ATRX in the alpha-thalassemia myelodysplasia syndrome (ATMDS). Nat Genet. 2003 Aug;34(4):446-9. [PubMed Link Image]
  11. Villard L, Lacombe D, Fontes M: A point mutation in the XNP gene, associated with an ATR-X phenotype without alpha-thalassemia. Eur J Hum Genet. 1996;4(6):316-20. [PubMed Link Image]
  12. Villard L, Gecz J, Mattei JF, Fontes M, Saugier-Veber P, Munnich A, Lyonnet S: XNP mutation in a large family with Juberg-Marsidi syndrome. Nat Genet. 1996 Apr;12(4):359-60. [PubMed Link Image]
  13. Gibbons RJ, Bachoo S, Picketts DJ, Aftimos S, Asenbauer B, Bergoffen J, Berry SA, Dahl N, Fryer A, Keppler K, Kurosawa K, Levin ML, Masuno M, Neri G, Pierpont ME, Slaney SF, Higgs DR: Mutations in transcriptional regulator ATRX establish the functional significance of a PHD-like domain. Nat Genet. 1997 Oct;17(2):146-8. [PubMed Link Image]
  14. Fichera M, Romano C, Castiglia L, Failla P, Ruberto C, Amata S, Greco D, Cardoso C, Fontes M, Ragusa A: New mutations in XNP/ATR-X gene: a further contribution to genotype/phenotype relationship in ATR/X syndrome. Mutations in brief no. 176. Online. Hum Mutat. 1998;12(3):214. [PubMed Link Image]
  15. Lossi AM, Millan JM, Villard L, Orellana C, Cardoso C, Prieto F, Fontes M, Martinez F: Mutation of the XNP/ATR-X gene in a family with severe mental retardation, spastic paraplegia and skewed pattern of X inactivation: demonstration that the mutation is involved in the inactivation bias. Am J Hum Genet. 1999 Aug;65(2):558-62. [PubMed Link Image]
  16. Abidi F, Schwartz CE, Carpenter NJ, Villard L, Fontes M, Curtis M: Carpenter-Waziri syndrome results from a mutation in XNP. Am J Med Genet. 1999 Jul 30;85(3):249-51. [PubMed Link Image]
  17. Villard L, Bonino MC, Abidi F, Ragusa A, Belougne J, Lossi AM, Seaver L, Bonnefont JP, Romano C, Fichera M, Lacombe D, Hanauer A, Philip N, Schwartz C, Fontes M: Evaluation of a mutation screening strategy for sporadic cases of ATR-X syndrome. J Med Genet. 1999 Mar;36(3):183-6. [PubMed Link Image]
  18. Wada T, Kubota T, Fukushima Y, Saitoh S: Molecular genetic study of japanese patients with X-linked alpha-thalassemia/mental retardation syndrome (ATR-X). Am J Med Genet. 2000 Sep 18;94(3):242-8. [PubMed Link Image]
  19. Yntema HG, Poppelaars FA, Derksen E, Oudakker AR, van Roosmalen T, Jacobs A, Obbema H, Brunner HG, Hamel BC, van Bokhoven H: Expanding phenotype of XNP mutations: mild to moderate mental retardation. Am J Med Genet. 2002 Jul 1;110(3):243-7. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 13329
Enzyme 27 Name Copine-1
Enzyme 27 Synonyms
  1. Copine I
Enzyme 27 Gene Name CPNE1
Enzyme 27 Protein Sequence >Copine-1 
MAHCVTLVQLSISCDHLIDKDIGSKSDPLCVLLQDVGGGSWAELGRTERVRNCSSPEFSK
TLQLEYRFETVQKLRFGIYDIDNKTPELRDDDFLGGAECSLGQIVSSQVLTLPLMLKPGK
PAGRGTITVSAQELKDNRVVTMEVEARNLDKKDFLGKSDPFLEFFRQGDGKWHLVYRSEV
IKNNLNPTWKRFSVPVQHFCGGNPSTPIQVQCSDYDSDGSHDLIGTFHTSLAQLQAVPAE
FECIHPEKQQKKKSYKNSGTIRVKICRVETEYSFLDYVMGGCQINFTVGVDFTGSNGDPS
SPDSLHYLSPTGVNEYLMALWSVGSVVQDYDSDKLFPAFGFGAQVPPDWQVSHEFALNFN
PSNPYCAGIQGIVDAYRQALPQVRLYGPTNFAPIINHVARFAAQAAHQGTASQYFMLLLL
TDGAVTDVEATREAVVRASNLPMSVIIVGVGGADFEAMEQLDADGGPLHTRSGQAAARDI
VQFVPYRRFQNAPREALAQTVLAEVPTQLVSYFRAQGWAPLKPLPPSAKDPAQAPQA
Enzyme 27 Number of Residues 537
Enzyme 27 Molecular Weight 59059
Enzyme 27 Theoretical pI 5.62
Enzyme 27 GO Classification Not Available
Enzyme 27 General Function Not Available
Enzyme 27 Specific Function May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 1791257 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q99829 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name CPNE1_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1614 bp 
ATGGCCCACTGCGTGACCTTGGTTCAGCTGTCCATTTCCTGTGACCATCTCATTGACAAG
GACATCGGCTCCAAGTCTGACCCACTCTGCGTCCTTTTACAGGATGTGGGAGGGGGCAGC
TGGGCTGAGCTTGGCCGGACTGAACGGGTGCGGAACTGCTCAAGCCCTGAGTTCTCCAAG
ACTCTACAGCTTGAGTACCGCTTTGAGACAGTCCAGAAGCTACGCTTTGGAATCTATGAC
ATAGACAACAAGACGCCAGAGCTGAGGGATGATGACTTCCTAGGGGGTGCTGAGTGTTCC
CTAGGACAGATTGTGTCCAGCCAGGTACTGACTCTCCCCTTGATGCTGAAGCCTGGAAAA
CCTGCTGGGCGGGGGACCATCACGGTCTCAGCTCAGGAATTAAAGGACAATCGTGTAGTA
ACCATGGAGGTAGAGGCCAGAAACCTAGATAAGAAGGACTTCCTGGGAAAATCAGATCCA
TTTCTGGAGTTCTTCCGCCAGGGTGATGGGAAATGGCACCTGGTGTACAGATCTGAGGTC
ATCAAGAACAACCTGAACCCTACATGGAAGCGTTTCTCAGTCCCCGTTCAGCATTTCTGT
GGTGGGAACCCCAGCACACCCATCCAGGTGCAATGCTCCGATTATGACAGTGACGGGTCA
CATGATCTCATCGGTACCTTCCACACCAGCTTGGCCCAGCTGCAGGCAGTCCCGGCTGAG
TTTGAATGCATCCACCCTGAGAAGCAGCAGAAAAAGAAAAGCTACAAGAACTCTGGAACT
ATCCGTGTCAAGATTTGTCGGGTAGAAACAGAGTACTCCTTTCTGGACTATGTGATGGGA
GGCTGTCAGATCAACTTCACTGTGGGCGTGGACTTCACTGGCTCCAATGGAGACCCCTCC
TCACCTGACTCCCTACACTACCTGAGTCCAACAGGGGTCAATGAGTACCTGATGGCACTG
TGGAGTGTGGGCAGCGTGGTTCAGGACTATGACTCAGACAAGCTGTTCCCTGCATTTGGA
TTTGGGGCCCAGGTTCCCCCTGACTGGCAGGTCTCGCATGAATTTGCCTTGAATTTCAAC
CCCAGTAACCCCTACTGTGCAGGCATCCAGGGCATTGTGGATGCCTACCGCCAAGCCCTG
CCCCAAGTTCGCCTCTATGGCCCTACCAACTTTGCACCCATCATCAACCATGTGGCCAGG
TTTGCAGCCCAGGCTGCACATCAGGGGACTGCCTCGCAATACTTCATGCTGTTGCTGCTG
ACTGATGGTGCTGTGACGGATGTGGAAGCCACACGTGAGGCTGTGGTGCGTGCCTCGAAC
CTGCCCATGTCAGTGATCATTGTGGGTGTGGGTGGTGCTGACTTTGAGGCCATGGAGCAG
CTGGACGCTGATGGTGGACCCCTGCATACACGTTCTGGGCAGGCTGCTGCCCGCGACATT
GTGCAGTTTGTACCCTACCGCCGGTTCCAGAATGCCCCTCGGGAGGCATTGGCACAGACC
GTGCTCGCAGAAGTGCCCACACAACTGGTCTCATACTTCAGGGCCCAGGGTTGGGCCCCG
CTCAAGCCACTTCCACCCTCAGCCAAGGATCCTGCACAGGCCCCCCAGGCCTAG
Enzyme 27 GenBank Gene ID U83246 Link Image
Enzyme 27 GeneCard ID Q99829 Link Image
Enzyme 27 GenAtlas ID CPNE1 Link Image
Enzyme 27 HGNC ID HGNC:2314 Link Image
Enzyme 27 Chromosome Location 20
Enzyme 27 Locus 20q11.22
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Creutz CE, Tomsig JL, Snyder SL, Gautier MC, Skouri F, Beisson J, Cohen J: The copines, a novel class of C2 domain-containing, calcium-dependent, phospholipid-binding proteins conserved from Paramecium to humans. J Biol Chem. 1998 Jan 16;273(3):1393-402. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 14040
Enzyme 28 Name Cdc42-interacting protein 4
Enzyme 28 Synonyms
  1. Thyroid receptor-interacting protein 10
  2. TRIP-10
  3. Protein Felic
  4. Salt tolerant protein
  5. hSTP
Enzyme 28 Gene Name TRIP10
Enzyme 28 Protein Sequence >Cdc42-interacting protein 4 
MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAK
DDPESKFSQQQSFVQILQEVNDFAGQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEG
RRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAHLRS
HMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELE
VVPIIAKCLEGMKVAANAVDPKNDSHVLIELHKSGFARPGDVEFEDFSQPMNRAPSDSSL
GTPSDGRPELRGPGRSRTKRWPFGKKNKPRPPPLSPLGGPVPSALPNGPPSPRSGRDPLA
ILSEISKSVKPRLASFRSLRGSRGTVVTEDFSHLPPEQQRKRLQQQLEERSRELQKEVDQ
REALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESRVLSNRG
DSLSRHARPPDPPASAPPDSSSNSASQDTKESSEEPPSEESQDTPIYTEFDEDFEEEPTS
PIGHCVAIYHFEGSSEGTISMAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPTSYLRVTL
N
Enzyme 28 Number of Residues 601
Enzyme 28 Molecular Weight 68353
Enzyme 28 Theoretical pI 5.45
Enzyme 28 GO Classification Not Available
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling. Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N- WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 2274966 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID Q15642 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name CIP4_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1638 bp 
ATGGATTGGGGCACTGAGCTGTGGGATCAGTTCGAGGTGCTCGAGCGCCACACGCAGTGG
GGGCTGGACCTGTTGGACAGATATGTAAAGTTCGTGAAAGAACGCACCGAAGTGGAACAG
GCTTACGCCAAACAACTGCGGAGCCTGGTGAAAAAATATCTGCCCAAGAGACCTGCCAAG
GATGATCCTGAGTCCAAATTCAGCCAGCAACAGTCCTTCGTACAGATTCTCCAGGAGGTG
AATGACTTTGCAGGCCAGCGGGAGCTGGTGGCTGAGAACCTCAGTGTCCGTGTATGTCTT
GAGCTGACCAAGTACTCACAAGAGATGAAACAGGAGAGGAAGATGCACTTCCAAGAAGGG
CGGCGGGCCCAGCAGCAGCTGGAAAATGGCTTTAAACAGCTGGAGAATAGTAAGCGTAAA
TTTGAGCGGGACTGCCGGGAGGCAGAGAAGGCAGCCCAGACTGCTGAACGGCTAGACCAG
GATATCAACGCCACCAAGGCTGATGTGGAGAAGGCCAAGCAGCAAGCCCACCTTCGGAGT
CACATGGCCGAAGAAAGCAAAAACGAATATGCGGCTCAACTGCAGCGCTTCAACCGAGAC
CAAGCCCACTTCTATTTTTCACAGATGCCCCAGATATTCGATAAGCTCCAAGACATGGAT
GAACGCAGGGCCACCCGCCTGGGTGCCGGGTATGGGCTCCTGTCGGAGGCCGAGCTGGAG
GTGGTGCCCATAATAGCCAAGTGCTTGGAGGGCATGAAGGTGGCTGCAAATGCTGTGGAT
CCCAAGAACGACTCCCACGTCCTTATAGAGCTGCACAAGTCAGGTTTTGCCCGCCCGGGC
GACGTGGAATTCGAGGACTTCAGCCAGCCCATGAACCGTGCACCCTCCGACAGCAGTCTG
GGCACCCCCTCGGATGGACGGCCTGAACTCCGAGGCCCGGGTCGCAGCCGCACCAAGCGC
TGGCCTTTTGGCAAGAAGAACAAGACAGTGGTGACCGAGGATTTTAGCCACTTGCCCCCA
GAGCAGCAGCGAAAACGGCTTCAACAGCAGTTGGAAGAACGCAGTCGTGAACTTCAGAAG
GAGGTTGACCAGAGGGAAGCCCTAAAGAAAATGAAGGATGTCTATGAGAAGACACCTCAG
ATGGGGGACCCCGCCAGCTTGGAGCCCCAGATCGCTGAAACCCTGAGCAACATTGAACGG
CTGAAATTGGAAGTGCAGAAGTATGAGGCGTGGCTGGCAGAAGCTGAAAGTCGAGTCCTT
AGCAACCGGGGAGACAGCCTGAGCCGGCACGCCCGGCCTCCCGACCCCCCCGCTAGCGCC
CCGCCAGACAGCAGCAGCAACAGCGCATCACAGGACACCAAGGAGAGCTCTGAAGAGCCT
CCCTCAGAAGAGAGCCAGGACACCCCCATTTACACGGAGTTTGATGAGGATTTCGAGGAG
GAACCCACATCCCCCATAGGTCACTGTGTGGCCATCTACCACTTTGAAGGGTCCAGCGAG
GGCACTATCTCTATGGCCGAGGGTGAAGACCTCAGTCTTATGGAAGAAGACAAAGGGGAC
GGCTGGACCCGGGTCAGGCGGAAAGAGGGAGGCGAGGGCTACGTGCCCACCTCCTACCTC
CGAGTCACGCTCAATTGA
Enzyme 28 GenBank Gene ID AJ000414 Link Image
Enzyme 28 GeneCard ID Q15642 Link Image
Enzyme 28 GenAtlas ID TRIP10 Link Image
Enzyme 28 HGNC ID HGNC:12304 Link Image
Enzyme 28 Chromosome Location 19
Enzyme 28 Locus 19p13.3
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Aspenstrom P: A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton. Curr Biol. 1997 Jul 1;7(7):479-87. [PubMed Link Image]
  2. Wang L, Rudert WA, Grishin A, Dombrosky-Ferlan P, Sullivan K, Deng X, Whitcomb D, Corey S: Identification and genetic analysis of human and mouse activated Cdc42 interacting protein-4 isoforms. Biochem Biophys Res Commun. 2002 May 24;293(5):1426-30. [PubMed Link Image]
  3. Lee JW, Choi HS, Gyuris J, Brent R, Moore DD: Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. Mol Endocrinol. 1995 Feb;9(2):243-54. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 14100
Enzyme 29 Name Formin-binding protein 1-like
Enzyme 29 Synonyms
  1. Transducer of Cdc42-dependent actin assembly protein 1
  2. Toca-1
Enzyme 29 Gene Name FNBP1L
Enzyme 29 Protein Sequence >Formin-binding protein 1-like 
MSWGTELWDQFDSLDKHTQWGIDFLERYAKFVKERIEIEQNYAKQLRNLVKKYCPKRSSK
DEEPRFTSCVAFFNILNELNDYAGQREVVAEEMAHRVYGELMRYAHDLKTERKMHLQEGR
KAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNATKADVEKAKQQLNLRTH
MADENKNEYAAQLQNFNGEQHKHFYVVIPQIYKQLQEMDERRTIKLSECYRGFADSERKV
IPIISKCLEGMILAAKSVDERRDSQMVVDSFKSGFEPPGDFPFEDYSQHIYRTISDGTIS
ASKQESGKMDAKTTVGKAKGKLWLFGKKPKPQSPPLTPTSLFTSSTPNGSQFLTFSIEPV
HYCMNEIKTGKPRIPSFRSLKRGVSLIMGPALEDFSHLPPEQRRKKLQQRIDELNRELQK
ESDQKDALNKMKDVYEKNPQMGDPGSLQPKLAETMNNIDRLRMEIHKNEAWLSEVEGKTG
GRGDRRHSSDINHLVTQGRESPEGSYTDDANQEVRGPPQQHGHHNEFDDEFEDDDPLPAI
GHCKAIYPFDGHNEGTLAMKEGEVLYIIEEDKGDGWTRARRQNGEEGYVPTSYIDVTLEK
NSKGS
Enzyme 29 Number of Residues 605
Enzyme 29 Molecular Weight 69978
Enzyme 29 Theoretical pI 6.52
Enzyme 29 GO Classification Not Available
Enzyme 29 General Function Not Available
Enzyme 29 Specific Function Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by activating the WASL/N-WASP-WASPIP/WIP complex, the predominant form of WASL/N-WASP in cells. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 41057623 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q5T0N5 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name FBP1L_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >1644 bp 
ATGAGCTGGGGCACGGAGCTGTGGGATCAGTTCGACAGCTTAGACAAGCATACACAATGG
GGAATTGACTTCTTGGAAAGATATGCCAAATTTGTTAAAGAGAGGATAGAAATTGAACAG
AACTATGCGAAACAATTGAGAAATCTGGTTAAGAAGTACTGCCCCAAACGTTCATCCAAA
GATGAAGAGCCACGGTTTACCTCGTGTGTAGCCTTTTTTAATATCCTTAATGAGTTAAAT
GACTATGCAGGACAGCGAGAAGTTGTAGCAGAAGAAATGGCGCACAGAGTGTATGGTGAA
TTAATGAGATATGCTCATGATCTGAAAACTGAAAGAAAAATGCATCTGCAAGAAGGACGA
AAAGCTCAACAATATCTTGACATGTGCTGGAAACAGATGGATAATAGTAAAAAGAAGTTT
GAAAGAGAATGTAGAGAGGCAGAAAAGGCACAACAGAGTTATGAAAGATTGGATAATGAT
ACTAATGCAACCAAGGCAGATGTTGAAAAGGCCAAACAGCAGTTGAATCTGCGTACGCAT
ATGGCCGATGAAAATAAAAATGAATATGCTGCACAATTACAAAACTTTAATGGAGAACAA
CATAAACATTTTTATGTAGTGATTCCTCAGATTTACAAGCAACTACAAGAAATGGACGAA
CGAAGGACTATTAAACTCAGTGAGTGTTACAGAGGATTTGCTGACTCAGAACGCAAAGTT
ATTCCCATCATTTCAAAATGTTTGGAAGGAATGATTCTTGCAGCAAAATCAGTTGATGAA
AGAAGAGACTCTCAAATGGTGGTAGACTCCTTCAAATCTGGTTTTGAACCTCCAGGAGAC
TTTCCATTTGAAGATTACAGTCAACATATATATAGAACCATTTCTGATGGGACTATCAGT
GCATCCAAACAGGAGAGTGGGAAGATGGATGCCAAAACCACAGTAGGAAAGGCCAAGGGC
AAATTGTGGCTCTTTGGAAAGAAGCCAAAGGGCCCAGCACTAGAAGATTTCAGTCATCTG
CCACCAGAACAGAGACGTAAAAAACTACAGCAGCGCATTGATGAACTTAACAGAGAACTA
CAGAAAGAATCAGACCAAAAAGATGCACTCAACAAAATGAAAGATGTATATGAGAAGAAT
CCACAAATGGGGGATCCAGGGAGTTTGCAGCCTAAATTAGCAGAGACCATGAATAACATT
GACCGCCTACGAATGGAAATCCATAAGAATGAGGCTTGGCTCTCTGAAGTCGAAGGCAAA
ACAGGTGGGAGAGGAGACAGAAGACATAGCAGTGACATAAATCATCTTGTAACACAGGGA
CGAGAAAGTCCTGAGGGAAGTTACACTGATGATGCAAACCAGGAAGTCCGTGGGCCACCC
CAGCAGCATGGTCACCACAATGAGTTTGATGATGAATTTGAGGATGATGATCCCTTGCCT
GCTATTGGACACTGCAAAGCTATCTACCCTTTTGATGGACATAATGAAGGTACTCTAGCA
ATGAAAGAAGGTGAAGTTCTCTACATTATAGAGGAGGACAAAGGTGACGGATGGACAAGA
GCTCGGAGACAGAACGGTGAAGAAGGCTACGTTCCCACGTCATACATAGATGTAACTCTA
GAGAAAAACAGTAAAGGTTCCTGA
Enzyme 29 GenBank Gene ID AY514449 Link Image
Enzyme 29 GeneCard ID Q5T0N5 Link Image
Enzyme 29 GenAtlas ID FNBP1L Link Image
Enzyme 29 HGNC ID HGNC:20851 Link Image
Enzyme 29 Chromosome Location Not Available
Enzyme 29 Locus Not Available
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References Not Available
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 14108
Enzyme 30 Name Formin-binding protein 1
Enzyme 30 Synonyms
  1. Formin-binding protein 17
  2. hFBP17
Enzyme 30 Gene Name FNBP1
Enzyme 30 Protein Sequence >Formin-binding protein 1 
MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSK
EEEEYKYTSCKAFISNLNEMNDYAGQHEVISENMASQIIVDLARYVQELKQERKSNFHDG
RKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRH
QMAEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQEMEERRIVRMGESMKTYAEVDRQ
VIPIIGKCLDGIVKAAESIDQKNDSQLVIEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSL
SNSRGEGKPDLKFGGKSKGKLWPFIKKNKLMSLLTSPHQPPPPPPASASPSAVPNGPQSP
KQQKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGATPEDFSNLPPEQRRKKLQQKVDE
LNKEIQKEMDQRDAITKMKDVYLKNPQMGDPASLDHKLAEVSQNIEKLRVETQKFEAWLA
EVEGRLPARSEQARRQSGLYDSQNPPTVNNCAQDRESPDGSYTEEQSQESEMKVLATDFD
DEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLYVIEEDKGDGWTRIRRNEDEEGY
VPTSYVEVCLDKNAKDS
Enzyme 30 Number of Residues 617
Enzyme 30 Molecular Weight 71307
Enzyme 30 Theoretical pI 5.44
Enzyme 30 GO Classification Not Available
Enzyme 30 General Function Not Available
Enzyme 30 Specific Function May act as a link between RND2 signaling and regulation of the actin cytoskeleton. Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 13936547 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q96RU3 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name FNBP1_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >2042 bp 
GGCTGTGGAACGGCGGGGAGGAGGAGCCGCCGAGGAGACCCCGGGCGAGGAGCTGCGAGC
CGGAGGAGGCCGCGCGGACTCCGGGCTTTCCGCCGTCGCGGGGATCTCGGGGGGCAAAGG
GATCGCCGGGGAGGGGGACCAGAGAGCCGCGCCCGCCGCGCGGAGCGCCCCTTCGCGTCC
CCTGCACCATGAGCTGGGGCACCGAGCTCTGGGATCAGTTTGACAACTTAGAAAAACACA
CACAGTGGGGAATTGATATTCTTGAGAAATATATCAAGTTTGTGAAAGAAAGGACAGAGA
TTGAACTCAGCTATGCAAAGCAACTCAGGAATCTTTCAAAGAAGTACCAACCTAAAAAGA
ACTCGAAGGAGGAAGAAGAATACAAGTATACGTCATGTAAAGCTTTCATTTCCAACCTGA
ACGAAATGAATGATTACGCAGGGCAGCATGAAGTTATCTCCGAGAACATGGCATCACAGA
TCATTGTGGACTTGGCACGCTATGTTCAGGAACTGAAACAGGAGAGGAAATCAAACTTTC
ACGATGGCCGTAAAGCACAGCAGCACATCGAGACTTGCTGGAAGCAGCTTGAATCTAGTA
AAAGGCGATTTGAACGCGATTGCAAAGAGGCGGACAGGGCGCAGCAGTACTTTGAGAAAA
TGGACGCTGACATCAATGTCACAAAAGCGGATGTTGAAAAGGCCCGACAACAAGCTCAAA
TACGTCACCAAATGGCAGAGGACAGCAAAGCAGATTACTCATCCATTCTCCAGAAATTCA
ACCATGAGCAGCATGAATATTACCATACTCACATCCCCAACATCTTCCAGAAAATACAAG
AGATGGAGGAAAGGAGGATTGTGAGAATGGGAGAGTCCATGAAGACATATGCAGAGGTTG
ATCGGCAGGTGATCCCAATCATTGGGAAGTGCCTGGATGGAATAGTAAAAGCAGCCGAAT
CAATTGATCAGAAAAATGATTCACAGCTGGTAATAGAAGCTTATAAATCAGGGTTTGAGC
CTCCTGGAGACATTGAATTTGAGGATTACACTCAGCCAATGAAGCGCACTGTGTCAGATA
ACAGCCTTTCAAATTCCAGAGGAGAAGGCAAACCAGACCTCAAATTTGGTGGCAAATCCA
AAGGAAAGTTATGGCCGTTCATCAAAAAAAATAAGCTTATGTCCCTTTTAACATCCCCCC
ATCAGCCTCCCCCTCCCCCTCCTGCCTCTGCCTCACCCTCTGCTGTTCCCAACGGCCCCC
AGTCTCCCAAGCAGCAAAAGGAACCCCTCTCCCACCGCTTCAACGAGTTCATGACCTCCA
AACCCAAAATCCACTGCTTCAGGAGCCTAAAGCGTGGGCTTTCTCTCAAGCTGGGTGCAA
CACCGGAGGATTTCAGCAACCTCCCACCTGAACAAAGAAGGAAAAAGCTGCAGCAGAAAG
TCGATGAGTTAAATAAAGAAATTCAGAAGGAGATGGATCAAAGAGATGCCATAACAAAAA
TGAAAGATGTCTACCTAAAGAATCCTCAGATGGGAGACCCAGCCAGTTTGGATCACAAAT
TAGCAGAAGTCAGCCAAAATATAGAGAAACTGCGAGTAGAGACCCAGAAATTTGAGGCCT
GGCTGGCTGAGGTTGAAGGCCGGCTCCCAGCACGCAGCGAGCAGGCGCGCCGGCAGAGCG
GACTGTACGACAGCCAGAACCCACCCACAGTCAACAACTGCGCCCAGGACCGTGAGAGCC
CAGATGGCAGTTACACAGAGGAGCAGAGTCAGGAGAGTGAGATGAAGGTGCTGGCCACGG
ATTTTGACGACGAGTTTGATGATGAGGAGCCCCTCCCTGCCATAGGGACGTGCAAAGCTC
TCTACACATTTGAAGGTCAGAATGAAGGAACGATTTCCGTAGTTGAAGGAGAAACATTGT
ATGTCATAGAGGAAGACAAAGGCGATGGCTGGACCCGCATTCGGAGAAATGAAGATGAAG
AGGGTTATGTCCCCACTTCATATGTCGAAGTCTGTTTGGACAAAAATGCCAAAGATTCCT
AG
Enzyme 30 GenBank Gene ID AF265550 Link Image
Enzyme 30 GeneCard ID Q96RU3 Link Image
Enzyme 30 GenAtlas ID FNBP1 Link Image
Enzyme 30 HGNC ID HGNC:17069 Link Image
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Fuchs U, Rehkamp G, Haas OA, Slany R, Konig M, Bojesen S, Bohle RM, Damm-Welk C, Ludwig WD, Harbott J, Borkhardt A: The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia. Proc Natl Acad Sci U S A. 2001 Jul 17;98(15):8756-61. Epub 2001 Jul 3. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 14494
Enzyme 31 Name Sphingomyelin phosphodiesterase 4
Enzyme 31 Synonyms
  1. Neutral sphingomyelinase 3
  2. Neutral sphingomyelinase III
  3. nSMase3
  4. nSMase- 3
Enzyme 31 Gene Name SMPD4
Enzyme 31 Protein Sequence >Sphingomyelin phosphodiesterase 4 
MAFPHLQQPSFLLASLKADSINKPFAQQCQDLVKVIEDFPAKELHTIFPWLVESIFGSLD
GVLVGWNLRCLQGRVNPVEYSIVMEFLDPGGPMMKLVYKLQAEDYKFDFPVSYLPGPVKA
SIQECILPDSPLYHNKVQFTPTGGLGLNLALNPFEYYIFFFALSLITQKPLPVSLHVRTS
DCAYFILVDRYLSWFLPTEGSVPPPLSSSPGGTSPSPPPRTPAIPFASYGLHHTSLLKRH
ISHQTSVNADPASHEIWRSETLLQVFVEMWLHHYSLEMYQKMQSPHAKLEVLHYRLSVSS
ALYSPAQPSLQALHAYQESFTPTEEHVLVVRLLLKHLHAFANSLKPEQASPSAHSHATSP
LEEFKRAAVPRFVQQKLYLFLQHCFGHWPLDASFRAVLEMWLSYLQPWRYAPDKQAPGSD
SQPRCVSEKWAPFVQENLLMYTKLFVGFLNRALRTDLVSPKHALMVFRVAKVFAQPNLAE
MIQKGEQLFLEPELVIPHRQHRLFTAPTFTGSFLSPWPPAVTDASFKVKSHVYSLEGQDC
KYTPMFGPEARTLVLRLAQLITQAKHTAKSISDQCAESPAGHSFLSWLGFSSMDTNGSYT
ANDLDEMGQDSVRKTDEYLEKALEYLRQIFRLSEAQLRQFTLALGTTQDENGKKQLPDCI
VGEDGLILTPLGRYQIINGLRRFEIEYQGDPELQPIRSYEIASLVRTLFRLSSAINHRFA
GQMAALCSRDDFLGSFCRYHLTEPGLASRHLLSPVGRRQVAGHTRGPRLSLRFLGSYRTL
VSLLLAFFVASLFCVGPLPCTLLLTLGYVLYASAMTLLTERGKLHQP
Enzyme 31 Number of Residues 827
Enzyme 31 Molecular Weight 93353
Enzyme 31 Theoretical pI 8.04
Enzyme 31 GO Classification Not Available
Enzyme 31 General Function Not Available
Enzyme 31 Specific Function Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide
Enzyme 31 Pathways
Enzyme 31 Reactions
  • sphingomyelin + H2O = N-acylsphingosine + choline phosphate [RN:R02541] ALL_REAC R02541
Enzyme 31 Pfam Domain Function Not Available
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • 783-803
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 7243217 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q9NXE4 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name NSMA3_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >2670 bp 
GGTAACGGCCCAAAGAGGTGGAAGCGCTTTTCCCGCCCGGCCGCGGGGCGTGGCTCTGCG
CGCAGCTTGATGACGACTTTCGGCGCCGTGGCGGAATGGCGGCTTCCATCTCTGAGGCGA
GCGACGCTATGGATCCCACAGTGGTTTGCTAAGAAGGCCATTTTCAACTCTCCACTGGAG
GCTGCTATGGCGTTCCCTCACCTGCAGCAGCCCAGCTTTCTACTGGCTAGCCTGAAAGCT
GACTCTATAAATAAGCCCTTTGCACAGCAGTGCCAAGACTTGGTTAAAGTCATTGAGGAC
TTTCCAGCAAAGGAGCTGCACACCATCTTCCCATGGCTGGTAGAAAGCATTTTTGGCAGC
CTAGATGGTGTCCTCGTTGGCTGGAACCTCCGCTGCTTACAGGGGCGCGTGAATCCTGTG
GAGTACAGCATCGTGATGGAATTTCTCGACCCTGGTGGCCCAATGATGAAGTTGGTTTAT
AAGCTTCAAGCTGAAGACTATAAGTTCGACTTTCCTGTCTCCTACTTGCCTGGTCCTGTG
AAGGCGTCCATCCAGGAGTGCATCCTCCCTGACAGTCCTCTGTACCACAACAAGGTCCAG
TTCACCCCTACTGGGGGCCTTGGTCTGAACTTGGCCCTGAATCCGTTCGAGTATTACATA
TTCTTCTTTGCCTTGAGCCTCATCACTCAGAAGCCACTTCCTGTGTCCCTCCACGTCCGT
ACTTCAGACTGTGCCTATTTCATCCTGGTGGACAGGTACCTGTCATGGTTCCTGCCCACC
GAAGGCAGTGTGCCCCCACCACTCTCCTCCAGCCCAGGGGGGACCAGCCCCTCACCACCT
CCCAGGACACCAGCCATACCCTTTGCTTCCTATGGCCTCCACCACACTAGCCTCCTAAAG
CGACACATCTCTCATCAGACGTCTGTGAATGCAGACCCCGCCTCCCACGAGATCTGGAGG
TCAGAAACTCTGCTCCAGGTTTTTGTTGAAATGTGGCTTCATCACTATTCCTTGGAGATG
TATCAAAAAATGCAGTCCCCTCATGCCAAGCTGGAGGTTCTGCACTACCGACTCAGTGTC
TCCAGCGCCCTCTACAGCCCCGCCCAACCCAGCCTCCAGGCCCTCCACGCCTACCAAGAG
TCGTTCACGCCTACTGAGGAGCATGTGTTGGTGGTGCGCCTGCTGCTGAAGCACCTGCAC
GCCTTTGCCAACAGCCTGAAGCCAGAGCAGGCCTCACCCTCCGCCCACTCCCACGCCACC
AGCCCCCTGGAGGAGTTCAAACGGGCTGCTGTCCCGAGGTTCGTCCAGCAGAAACTCTAC
CTCTTCTTGCAGCATTGCTTTGGCCACTGGCCCCTGGACGCATCGTTCAGAGCTGTCCTG
GAGATGTGGCTGAGCTACCTGCAGCCGTGGCGGTACGCGCCTGACAAGCAGGCTCCGGGC
AGCGACTCCCAGCCCCGGTGTGTGTCGGAGAAATGGGCACCCTTTGTCCAGGAGAACCTG
CTGATGTACACCAAGTTGTTTGTGGGCTTTCTGAACCGCGCGCTCCGCACAGACCTGGTC
AGCCCCAAGCACGCGCTCATGGTGTTCCGAGTGGCCAAAGTCTTTGCCCAGCCCAACCTG
GCTGAGATGATTCAGAAAGGTGAGCAGCTATTCCTGGAGCCAGAGCTGGTCATCCCCCAC
CGCCAGCACCGACTCTTCACGGCCCCCACATTCACTGGGAGCTTCCTGTCACCCTGGCCA
CCAGCGGTCACTGATGCCTCCTTCAAGGTGAAGAGCCACGTCTACAGCCTGGAGGGCCAG
GACTGCAAGTACACCCCGATGTTTGGGCCCGAGGCCCGCACCCTGGTCCTGCGCCTCGCT
CAGCTCATCACACAGGCCAAACACACAGCCAAGTCCATCTCCGACCAGTGTGCGGAGAGC
CCGGCTGGCCACTCCTTCCTCTCATGGCTGGGCTTTAGCTCCATGGACACCAATGGCTCC
TACACAGCCAACGACCTGGACGAGATGGGGCAAGACAGTGTCCGGAAGACAGATGAATAC
CTGGAGAAGGCCCTGGAGTACCTGCGCCAGATATTCCGGCTCAGCGAAGCGCAGCTCAGG
CAGTTCACACTCGCCTTGGGCACCACCCAGGATGAGAATGGAAAAAAGCAACTCCCCGAC
TGCATCGTGGGTGAGGACGGACTCATCCTTACGCCCCTGGGGCGGTACCAGATCATCAAT
GGGCTGCGAAGGTTTGAAATTGAGTACCAGGGGGACCCGGAGCTGCAGCCCATCCGGAGC
TATGAGATCGCCAGCTTGGTCCGCACACTCTTTAGGCTGTCGTCTGCCATCAACCACAGA
TTTGCAGGACAGATGGCGGCTCTGTGTTCCCGGGATGACTTCCTCGGCAGCTTCTGTCGC
TACCACCTCACAGAACCTGGGCTGGCCAGCAGGCACCTGCTGAGCCCTGTGGGGCGGAGG
CAGGTGGCCGGCCACACCCGCGGCCCCAGGCTCAGCCTGCGCTTCCTGGGCAGTTACCGG
ACGCTGGTCTCGCTGCTGCTGGCCTTCTTCGTGGCCTCTCTGTTCTGCGTCGGGCCCCTC
CCATGCACGCTGCTGCTCACCCTGGGCTATGTCCTCTACGCCTCTGCCATGACACTGCTG
ACCGAGCGGGGGAAGCTGCACCAGCCCTGA
Enzyme 31 GenBank Gene ID AB037839 Link Image
Enzyme 31 GeneCard ID Q9NXE4 Link Image
Enzyme 31 GenAtlas ID SMPD4 Link Image
Enzyme 31 HGNC ID HGNC:32949 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. Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [PubMed Link Image]
  2. 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 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 17005
Enzyme 32 Name Serine incorporator 1
Enzyme 32 Synonyms
  1. Tumor differentially expressed protein 2
  2. Tumor differentially expressed 1 protein-like
Enzyme 32 Gene Name SERINC1
Enzyme 32 Protein Sequence >Serine incorporator 1 
MGSVLGLCSMASWIPCLCGSAPCLLCRCCPSGNNSTVTRLIYALFLLVGVCVACVMLIPG
MEEQLNKIPGFCENEKGVVPCNILVGYKAVYRLCFGLAMFYLLLSLLMIKVKSSSDPRAA
VHNGFWFFKFAAAIAIIIGAFFIPEGTFTTVWFYVGMAGAFCFILIQLVLLIDFAHSWNE
SWVEKMEEGNSRCWYAALLSATALNYLLSLVAIVLFFVYYTHPASCSENKAFISVNMLLC
VGASVMSILPKIQESQPRSGLLQSSVITVYTMYLTWSAMTNEPETNCNPSLLSIIGYNTT
STVPKEGQSVQWWHAQGIIGLILFLLCVFYSSIRTSNNSQVNKLTLTSDESTLIEDGGAR
SDGSLEDGDDVHRAVDNERDGVTYSYSFFHFMLFLASLYIMMTLTNWYRYEPSREMKSQW
TAVWVKISSSWIGIVLYVWTLVAPLVLTNRDFD
Enzyme 32 Number of Residues 453
Enzyme 32 Molecular Weight 50495
Enzyme 32 Theoretical pI 5.65
Enzyme 32 GO Classification
Function
—
Process
—
Component
  • cell
  • membrane
Enzyme 32 General Function Not Available
Enzyme 32 Specific Function Enhances the incorporation of serine into phosphatidylserine and sphingolipids
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • 89-109 124-144 152-172 198-218 232-252 260-280 310-330 388-408 427-447
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein Not Available
Enzyme 32 UniProtKB/Swiss-Prot ID Q9NRX5 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name SERC1_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 AF087902 Link Image
Enzyme 32 GeneCard ID Q9NRX5 Link Image
Enzyme 32 GenAtlas ID SERINC1 Link Image
Enzyme 32 HGNC ID HGNC:13464 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, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [PubMed Link Image]
  2. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed Link Image]
  3. 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]
  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 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 17258
Enzyme 33 Name Protein kinase C delta-binding protein
Enzyme 33 Synonyms
  1. Serum deprivation response factor-related gene product that binds to C-kinase
  2. hSRBC
Enzyme 33 Gene Name PRKCDBP
Enzyme 33 Protein Sequence >Protein kinase C delta-binding protein 
MRESALEPGPVPEAPAGGPVHAVTVVTLLEKLASMLETLRERQGGLARRQGGLAGSVRRI
QSGLGALSRSHDTTSNTLAQLLAKAERVSSHANAAQERAVRRAAQVQRLEANHGLLVARG
KLHVLLFKEEGEVPASAFQKAPEPLGPADQSELGPEQPEAEVGESSDEEPVESRAQRLRR
TGLQKVQSLRRALSGRKGPAAPPPTPVKPPRLGPGRSAEAQPEAQPALEPTLEPEPPQDT
EEDPGRPGAAEEALLQMESVA
Enzyme 33 Number of Residues 261
Enzyme 33 Molecular Weight 27626
Enzyme 33 Theoretical pI 6.07
Enzyme 33 GO Classification Not Available
Enzyme 33 General Function Not Available
Enzyme 33 Specific Function Seems to have an immune potentiation function
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions Not Available
Enzyme 33 Pfam Domain Function Not Available
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein Not Available
Enzyme 33 UniProtKB/Swiss-Prot ID Q969G5 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name PRDBP_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 AF339881 Link Image
Enzyme 33 GeneCard ID PRKCDBP Link Image
Enzyme 33 GenAtlas ID PRKCDBP Link Image
Enzyme 33 HGNC ID HGNC:9400 Link Image
Enzyme 33 Chromosome Location Not Available
Enzyme 33 Locus Not Available
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References Not Available
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 17306
Enzyme 34 Name Annexin A9
Enzyme 34 Synonyms
  1. Annexin-9
  2. Annexin-31
  3. Annexin XXXI
  4. Pemphaxin
Enzyme 34 Gene Name ANXA9
Enzyme 34 Protein Sequence >Annexin A9 
MSVTGGKMAPSLTQEILSHLGLASKTAAWGTLGTLRTFLNFSVDKDAQRLLRAITGQGVD
RSAIVDVLTNRSREQRQLISRNFQERTQQDLMKSLQAALSGNLERIVMALLQPTAQFDAQ
ELRTALKASDSAVDVAIEILATRTPPQLQECLAVYKHNFQVEAVDDITSETSGILQDLLL
ALAKGGRDSYSGIIDYNLAEQDVQALQRAEGPSREETWVPVFTQRNPEHLIRVFDQYQRS
TGQELEEAVQNRFHGDAQVALLGLASVIKNTPLYFADKLHQALQETEPNYQVLIRILISR
CETDLLSIRAEFRKKFGKSLYSSLQDAVKGDCQSALLALCRAEDM
Enzyme 34 Number of Residues 345
Enzyme 34 Molecular Weight 38364
Enzyme 34 Theoretical pI 5.48
Enzyme 34 GO Classification
Function
  • binding
  • calcium ion binding
  • calcium-dependent phospholipid binding
  • cation binding
  • ion binding
  • lipid binding
  • phospholipid binding
Process
—
Component
—
Enzyme 34 General Function Not Available
Enzyme 34 Specific Function May act as a low affinity receptor for acetylcholine
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions Not Available
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein Not Available
Enzyme 34 UniProtKB/Swiss-Prot ID O76027 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name ANXA9_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 AJ009985 Link Image
Enzyme 34 GeneCard ID ANXA9 Link Image
Enzyme 34 GenAtlas ID ANXA9 Link Image
Enzyme 34 HGNC ID HGNC:547 Link Image
Enzyme 34 Chromosome Location Not Available
Enzyme 34 Locus Not Available
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Morgan RO, Fernandez MP: Expression profile and structural divergence of novel human annexin 31. FEBS Lett. 1998 Sep 4;434(3):300-4. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 17307
Enzyme 35 Name Phosphatidylserine receptor transcript variant 2
Enzyme 35 Synonyms Not Available
Enzyme 35 Gene Name JMJD6
Enzyme 35 Protein Sequence >Phosphatidylserine receptor transcript variant 2 
MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESFSLSPAAVADNVERADALQLSVEEFV
ERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEY
MESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPP
RSGTGIHIDPLGTSAWNALVQGHKRWCLFPTSTPRELIKVTRDEGGNQQDEAITWFNVIY
PRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHK
TVRGRPKLSRKWYRTDTARAAAVQATHSHPVPLCPNPDLEGPALGDFEARAPRVGSPRRL
G
Enzyme 35 Number of Residues 361
Enzyme 35 Molecular Weight 42003
Enzyme 35 Theoretical pI 9.90
Enzyme 35 GO Classification Not Available
Enzyme 35 General Function Not Available
Enzyme 35 Specific Function Not Available
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein Not Available
Enzyme 35 UniProtKB/Swiss-Prot ID B2WTI4 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name B2WTI4_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 EF527407 Link Image
Enzyme 35 GeneCard ID JMJD6 Link Image
Enzyme 35 GenAtlas ID Not Available
Enzyme 35 HGNC ID Not Available
Enzyme 35 Chromosome Location Not Available
Enzyme 35 Locus Not Available
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References Not Available
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 17308
Enzyme 36 Name cDNA FLJ38589 fis, clone HCHON2010074, highly similar to LACTADHERIN
Enzyme 36 Synonyms Not Available
Enzyme 36 Gene Name Not Available
Enzyme 36 Protein Sequence >cDNA FLJ38589 fis, clone HCHON2010074, highly similar to LACTADHERIN 
MWPFPEGGNTIPILHTDICSKNPCHNGGLCEEISQEVRGDVFPSYTCTCLKGYAGNHCET
KCVEPLGMENGNIANSQIAASSVRVTFLGLQHWVPELARLNRAGMVNAWTSSSNDDNPWI
QVNLLRRMWVTGVVTQGASRLASHEYLKAFKVAYSLNGHEFDFIHDVNKKHKEFVGNWNK
NAVHVNLFETPVEAQYVRLYPTSCHTACTLRFELLGCELNGCANPLGLKNNSIPDKQITA
SSSYKTWGLHLFSWNPSYARLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGAR
NFGSVQFVASYKVAYSNDSANWTEYQDPRTGSSKIFPGNWDNHSHKKNLFETPILARYVR
ILPVAWHNRIALRLELLGC
Enzyme 36 Number of Residues 379
Enzyme 36 Molecular Weight 42460
Enzyme 36 Theoretical pI 7.88
Enzyme 36 GO Classification
Function
—
Process
  • cell adhesion
  • cellular process
Component
—
Enzyme 36 General Function Not Available
Enzyme 36 Specific Function Not Available
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein Not Available
Enzyme 36 UniProtKB/Swiss-Prot ID B3KTQ2 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name B3KTQ2_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 AK095908 Link Image
Enzyme 36 GeneCard ID Not Available
Enzyme 36 GenAtlas ID Not Available
Enzyme 36 HGNC ID HGNC:7036 Link Image
Enzyme 36 Chromosome Location Not Available
Enzyme 36 Locus Not Available
Enzyme 36 SNPs Not Available
Enzyme 36 General References Not Available
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 17309
Enzyme 37 Name Putative uncharacterized protein DKFZp686M1886
Enzyme 37 Synonyms Not Available
Enzyme 37 Gene Name DKFZp686M1886
Enzyme 37 Protein Sequence >Putative uncharacterized protein DKFZp686M1886 
MENGNIANSQIAASSVRVTFLGLQHWVPELARLNRAGMVNAWTPSSNDDNPWIQVNLLRR
MWVTGVVTQGASRLASHEYLKAFKVAYSLNGHEFDFIHDVNKKHKEFVGNWNKNAVHVNL
FETPVEAQYVRLYPTSCHTACTLRFELLGCELNGCANPLGLKNNSIPDKQITASSSYKTW
GLHLFSWNPSYAWLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGARNFGSVQF
VASYKVAYSNDSANWTEYQDPRTGSSKIFPGNWDNHTHKKNLFETPILARYVRILPVAWH
NRIALRLELLGC
Enzyme 37 Number of Residues 312
Enzyme 37 Molecular Weight 35233
Enzyme 37 Theoretical pI 8.89
Enzyme 37 GO Classification
Function
—
Process
  • cell adhesion
  • cellular process
Component
—
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
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein Not Available
Enzyme 37 UniProtKB/Swiss-Prot ID Q7Z3D2 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name Q7Z3D2_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 BX537974 Link Image
Enzyme 37 GeneCard ID DKFZp686M1886 Link Image
Enzyme 37 GenAtlas ID DKFZp686M1886 Link Image
Enzyme 37 HGNC ID HGNC:7036 Link Image
Enzyme 37 Chromosome Location Not Available
Enzyme 37 Locus Not Available
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References Not Available
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 17310
Enzyme 38 Name Serine incorporator 5
Enzyme 38 Synonyms Not Available
Enzyme 38 Gene Name SERINC5
Enzyme 38 Protein Sequence >Serine incorporator 5 
MSAQCCAGQLACCCGSAGCSLCCDCCPRIRQSLSTRFMYALYFILVVVLCCIMMSTTVAH
KMKEHIPFFEDMCKGIKAGDTCEKLVGYSAVYRVCFGMACFFFIFCLLTLKINNSKSCRA
HIHNGFWFFKLLLLGAMCSGAFFIPDQDTFLNAWRYVGAVGGFLFIGIQLLLLVEFAHKW
NKNWTAGTASNKLWYASLALVTLIMYSIATGGLVLMAVFYTQKDSCMENKILLGVNGGLC
LLISLVAISPWVQNRQPHSGLLQSGVISCYVTYLTFSALSSKPAEVVLDEHGKNVTICVP
DFGQDLYRDENLVTILGTSLLIGCILYSCLTSTTRSSSDALQGRYAAPELEIARCCFCFS
PGGEDTEEQQPGKEGPRVIYDEKKGTVYIYSYFHFVFFLASLYVMMTVTNWFNHVRSAFH
LLP
Enzyme 38 Number of Residues 423
Enzyme 38 Molecular Weight 47010
Enzyme 38 Theoretical pI 7.65
Enzyme 38 GO Classification
Function
  • electron transporter activity
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
  • cell
  • membrane
Enzyme 38 General Function Not Available
Enzyme 38 Specific Function Enhances the incorporation of serine into phosphatidylserine and sphingolipids. May play a role in providing serine molecules for the formation of myelin glycosphingolipids in oligodendrocytes
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions Not Available
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • 37-57 90-110 125-145 157-177 199-219 231-251 259-279 312-332 386-406
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein Not Available
Enzyme 38 UniProtKB/Swiss-Prot ID Q86VE9 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name SERC5_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 AF498273 Link Image
Enzyme 38 GeneCard ID SERINC5 Link Image
Enzyme 38 GenAtlas ID SERINC5 Link Image
Enzyme 38 HGNC ID HGNC:18825 Link Image
Enzyme 38 Chromosome Location Not Available
Enzyme 38 Locus Not Available
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References Not Available
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 17311
Enzyme 39 Name Adseverin
Enzyme 39 Synonyms
  1. Scinderin
Enzyme 39 Gene Name SCIN
Enzyme 39 Protein Sequence >Adseverin 
MARELYHEEFARAGKQAGLQVWRIEKLELVPVPQSAHGDFYVGDAYLVLHTAKTSRGFTY
HLHFWLGKECSQDESTAAAIFTVQMDDYLGGKPVQNRELQGYESNDFVSYFKGGLKYKAG
GVASGLNHVLTNDLTAKRLLHVKGRRVVRATEVPLSWDSFNKGDCFIIDLGTEIYQWCGS
SCNKYERLKANQVATGIRYNERKGRSELIVVEEGSEPSELIKVLGEKPELPDGGDDDDII
ADISNRKMAKLYMVSDASGSMRVTVVAEENPFSMAMLLSEECFILDHGAAKQIFVWKGKD
ANPQERKAAMKTAEEFLQQMNYSKNTQIQVLPEGGETPIFKQFFKDWRDKDQSDGFGKVY
VTEKVAQIKQIPFDASKLHSSPQMAAQHNMVDDGSGKVEIWRVENNGRIQVDQNSYGEFY
GGDCYIILYTYPRGQIIYTWQGANATRDELTTSAFLTVQLDRSLGGQAVQIRVSQGKEPV
HLLSLFKDKPLIIYKNGTSKKGGQAPAPPTRLFQVRRNLASITRIVEVDVDANSLNSNDV
FVLKLPQNSGYIWVGKGASQEEEKGAEYVASVLKCKTLRIQEGEEPEEFWNSLGGKKDYQ
TSPLLETQAEDHPPRLYGCSNKTGRFVIEEIPGEFTQDDLAEDDVMLLDAWEQIFIWIGK
DANEVEKKESLKSAKMYLETDPSGRDKRTPIVIIKQGHEPPTFTGWFLGWDSSKW
Enzyme 39 Number of Residues 715
Enzyme 39 Molecular Weight 80490
Enzyme 39 Theoretical pI 5.41
Enzyme 39 GO Classification
Function
  • actin binding
  • binding
  • cytoskeletal protein binding
  • protein binding
Process
—
Component
—
Enzyme 39 General Function Not Available
Enzyme 39 Specific Function Ca(2+)-dependent actin filament-severing protein that is presumed to have a regulatory function in exocytosis by affecting the organization of the microfilament network underneath the plasma membrane. In vitro, also has barbed end capping and nucleating activities in the presence of Ca(2+)
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions Not Available
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein Not Available
Enzyme 39 UniProtKB/Swiss-Prot ID Q9Y6U3 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name ADSV_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 AF276507 Link Image
Enzyme 39 GeneCard ID SCIN Link Image
Enzyme 39 GenAtlas ID SCIN Link Image
Enzyme 39 HGNC ID HGNC:21695 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. Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins. DNA Res. 2001 Aug 31;8(4):179-87. [PubMed Link Image]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 17312
Enzyme 40 Name Serine incorporator 4
Enzyme 40 Synonyms Not Available
Enzyme 40 Gene Name SERINC4
Enzyme 40 Protein Sequence >Serine incorporator 4 
MVGAKAGPSPGTSLGLAQQHSGGSSVLVKSPFCQVCCCGPAPCASCCHSRWPSLTASTCS
RLFYILLHVGASAICCLLLSRTVVERVWGKTHRIQMPSGLCAHLFGLSDCPVLSGSGAVY
RVCAGTATFHLLQAVLLVHLHSPTSPRAQLHNSFWLLKLLFLLGLCAIAFCIPDEHLFPA
WHYIGICGGFAFILLQLVLITAFAHSWNKNWQTGAAQDCSWFLAVLLATLGFYSMAGVGA
VLLFHYYTHPAGCLLNKMLLSLHLCFCGLISFLSIAPCIRLKQPRSGLLQASVISCYIMY
LTFSALSSRPPERVILQGQNHTLCLPGLSKMEPQTPDISLAMLSASIMYACVLFACNEAS
YLAEVFGPLWIVKVYSYEFQKPSLCFCCPETVEADKGQRGGAARPADQETPPAPPVQVQH
LSYNYSAFHFVFFLASLYVMVTLTNWFSYEGAELEKTFIKGSWATFWVKVASCWACVLLY
LGLLLAPLCWPPTQKPQPLILRRRRHRIISPDNKYPPV
Enzyme 40 Number of Residues 518
Enzyme 40 Molecular Weight 56871
Enzyme 40 Theoretical pI 8.39
Enzyme 40 GO Classification
Function
  • electron transporter activity
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
  • cell
  • membrane
Enzyme 40 General Function Not Available
Enzyme 40 Specific Function Incorporates a polar amino acid serine into membranes and facilitates the synthesis of two serine-derived lipids, phosphatidylserine and sphingolipids
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • 59-79 122-142 153-173 184-204 222-242 259-279 286-306 338-357 427-447 470-490
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein Not Available
Enzyme 40 UniProtKB/Swiss-Prot ID A6NH21 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name SERC4_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 DQ103711 Link Image
Enzyme 40 GeneCard ID SERINC4 Link Image
Enzyme 40 GenAtlas ID SERINC4 Link Image
Enzyme 40 HGNC ID HGNC:32237 Link Image
Enzyme 40 Chromosome Location Not Available
Enzyme 40 Locus Not Available
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References Not Available
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 17313
Enzyme 41 Name Phosphatidylserine receptor transcript variant 1 (Phosphatidylserine receptor, isoform CRA_d)
Enzyme 41 Synonyms Not Available
Enzyme 41 Gene Name JMJD6
Enzyme 41 Protein Sequence >Phosphatidylserine receptor transcript variant 1 (Phosphatidylserine receptor, isoform CRA_d) 
MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESFSLSPAAVADNVERADALQLSVEEFV
ERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEY
MESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPP
RSGTGIHIDPLGTSAWNALVQGHKRWCLFPTSTPRELIKVTRDEGGNQQDEAITWFNVIY
PRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHK
TVRGRPKLSRKWYRYSTGSGSASHPQPPRATVSQP
Enzyme 41 Number of Residues 335
Enzyme 41 Molecular Weight 39242
Enzyme 41 Theoretical pI 10.00
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 Not Available
Enzyme 41 UniProtKB/Swiss-Prot ID B2WTI3 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name B2WTI3_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 EF527406 Link Image
Enzyme 41 GeneCard ID JMJD6 Link Image
Enzyme 41 GenAtlas ID JMJD6 Link Image
Enzyme 41 HGNC ID HGNC:19355 Link Image
Enzyme 41 Chromosome Location Not Available
Enzyme 41 Locus Not Available
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References Not Available
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 17314
Enzyme 42 Name cDNA, FLJ94904, Homo sapiens copine VI (neuronal) (CPNE6), mRNA (Copine VI (Neuronal), isoform CRA_c)
Enzyme 42 Synonyms Not Available
Enzyme 42 Gene Name CPNE6
Enzyme 42 Protein Sequence >cDNA, FLJ94904, Homo sapiens copine VI (neuronal) (CPNE6), mRNA (Copine VI (Neuronal), isoform CRA_c) 
MSDPEMGWVPEPPTMTLGASRVELRVSCHGLLDRDTLTKPHPCVLLKLYSDEQWVEVERT
EVLRSCSSPVFSRVLALEYFFEEKQPLQFHVFDAEDGATSPRNDTFLGSTECTLGQIVSQ
TKVTKPLLLKNGKTAGKSTITIVAEEVSGTNDYVQLTFRAYKLDNKDLFSKSDPFMEIYK
TNEDQSDQLVWRTEVVKNNLNPSWEPFRLSLHSLCSCDVHRPLKFLVYDYDSSGKHDFIG
EFTSTFQEMQEGTANPGQEMQWDCINPKYRDKKKNYKSSGTVVLAQCTVEKVHTFLDYIM
GGCQISFTVAIDFTASNGDPRSSQSLHCLSPRQPNHYLQALRAVGGICQDYDSDKRFPAF
GFGARIPPNFEVSHDFAINFDPENPECEEISGVIASYRRCLPQIQLYGPTNVAPIINRVA
EPAQREQSTGQATKYSVLLVLTDGVVSDMAETRTAIVRASRLPMSIIIVGVGNADFSDMR
LLDGDDGPLRCPRGVPAARDIVQFVPFRDFKDAAPSALAKCVLAEVPRQVVEYYASQGIS
PGAPRPCTLATTPSPSP
Enzyme 42 Number of Residues 557
Enzyme 42 Molecular Weight 61992
Enzyme 42 Theoretical pI 5.17
Enzyme 42 GO Classification Not Available
Enzyme 42 General Function Not Available
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 Not Available
Enzyme 42 UniProtKB/Swiss-Prot ID B2RAG6 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name B2RAG6_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 AK314182 Link Image
Enzyme 42 GeneCard ID CPNE6 Link Image
Enzyme 42 GenAtlas ID CPNE6 Link Image
Enzyme 42 HGNC ID HGNC:2319 Link Image
Enzyme 42 Chromosome Location Not Available
Enzyme 42 Locus Not Available
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References Not Available
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 17315
Enzyme 43 Name cDNA FLJ59612, highly similar to Lactadherin
Enzyme 43 Synonyms Not Available
Enzyme 43 Gene Name Not Available
Enzyme 43 Protein Sequence >cDNA FLJ59612, highly similar to Lactadherin 
MPRPRLLAALCGALLRAPSLLVALECVESLGMENGNIANSQIAASSVRVTFLGLQHWVPE
LARLNRAGMVNAWTPSSNDDNPWIQVNLLRRMWVTGVVTQGASRLASHEYLKAFKVAYSL
NGHEFDFIHDVNKKHKEFVGNWNKNAVHVNLFETPVEAQYVRLYPTSCHTACTLRFELLG
CELNGCANPLGLKNNSIPDKQITASSSYKTWGLHLFSWNPSYARLDKQGNFNAWVAGSYG
NDQWLQVDLGSSKEVTGIITQGARNFGSVQFVASYKVAYSNDSANWTEYQDPRTGSSKIF
PGNWDNHSHKKNLFETPILARYVRILPVAWHNRIALRLELLGC
Enzyme 43 Number of Residues 343
Enzyme 43 Molecular Weight 38405
Enzyme 43 Theoretical pI 8.99
Enzyme 43 GO Classification
Function
—
Process
  • cell adhesion
  • cellular process
Component
—
Enzyme 43 General Function Not Available
Enzyme 43 Specific Function Not Available
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein Not Available
Enzyme 43 UniProtKB/Swiss-Prot ID B4E396 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name B4E396_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 AK304627 Link Image
Enzyme 43 GeneCard ID Not Available
Enzyme 43 GenAtlas ID Not Available
Enzyme 43 HGNC ID HGNC:7036 Link Image
Enzyme 43 Chromosome Location Not Available
Enzyme 43 Locus Not Available
Enzyme 43 SNPs Not Available
Enzyme 43 General References Not Available
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 17316
Enzyme 44 Name cDNA FLJ43205 fis, clone FEBRA2009185, highly similar to Copine-6
Enzyme 44 Synonyms
  1. SubName: Copine VI (Neuronal), isoform CRA_a
Enzyme 44 Gene Name CPNE6
Enzyme 44 Protein Sequence >cDNA FLJ43205 fis, clone FEBRA2009185, highly similar to Copine-6 
MEIYKTNEDQSDQLVWRTEVVKNNLNPSWEPFRLSLHSLCSCDVHRPLKFLVYDYDSSGK
HDFIGEFTSTFQEMQEGTANPGQEMQWDCINPKYRDKKKNYKSSGTVVLAQCTVEKVHTF
LDYIMGGCQISFTVAIDFTASNGDPRSSQSLHCLSPRQPNHYLQALRAVGGICQDYDSDK
RFPAFGFGARIPPNFEVSHDFAINFDPENPECEEISGVIASYRRCLPQIQLYGPTNVAPI
INRVAEPAQREQSTGQATKYSVLLVLTDGVVSDMAETRTAIVRASRLPMSIIIVGVGNAD
FSDMRLLDGDDGPLRCPRGVPAARDIVQFVPFRDFKDAAPSALAKCVLAEVPRQVVEYYA
SQGISPGAPRPCTLATTPSPSP
Enzyme 44 Number of Residues 382
Enzyme 44 Molecular Weight 42373
Enzyme 44 Theoretical pI 5.44
Enzyme 44 GO Classification Not Available
Enzyme 44 General Function Not Available
Enzyme 44 Specific Function Not Available
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions Not Available
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein Not Available
Enzyme 44 UniProtKB/Swiss-Prot ID B3KWK1 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name B3KWK1_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 AK125195 Link Image
Enzyme 44 GeneCard ID CPNE6 Link Image
Enzyme 44 GenAtlas ID CPNE6 Link Image
Enzyme 44 HGNC ID HGNC:2319 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