We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for LPA(16:0/0:0) (HMDB07853)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2008-09-12 02:27:12
Update Date 2009-05-05 21:02:41
Accession Number HMDB07853
Secondary Accession Numbers HMDB00327
Common Name LPA(16:0/0:0)
Description LPA(16:0/0:0) is a lysophosphatidic acid. It is a glycerophospholipid in which a phosphate moiety occupies a glycerol substitution site. Lysophosphatidic acids can have different combinations of fatty acids of varying lengths and saturation attached at the C-1 (sn-1) or C-2 (sn-2) position. Fatty acids containing 16 and 18 carbons are the most common. Lysophosphatidic acid is the simplest possible glycerophospholipid. It is the biosynthetic precursor of phosphatidic acid. Although it is present at very low levels only in animal tissues, it is extremely important biologically, influencing many biochemical processes. In particular, lysophosphatidic acid is an intercellular lipid mediator with growth factor-like activities, and is rapidly produced and released from activated platelets to influence target cells. 1-Palmitoyl lysophosphatidic acid is the major component of lysophosphatidic acid (LPA) in plasma, and is in a reduced ratio in individuals with gynecological cancers (PMID 11585410). LPA is a pluripotent lipid mediator controlling growth, motility, and differentiation, that has a strong influence on the chemotaxis and ultrastructure of human neutrophils (PMID 7416233). In serum and plasma, LPA is mainly converted from lysophospholipids, whereas in platelets and some cancer cells it is converted from phosphatidic acid. In each pathway, at least two phospholipase activities are required: phospholipase A1 (PLA1)/PLA2 plus lysophospholipase D (lysoPLD) activities are involved in the first pathway and phospholipase D (PLD) plus PLA1/PLA2 activities are involved in the second pathway. (PMID 15271293)
Synonyms
  1. Lysophosphatidic acid(16:0/0:0)
  2. Lysophosphatidic acid(16:0)
  3. 1-palmitoyl-glycero-3-phosphate
  4. 1-hexadecanoyl-phosphatidic acid
  5. LPA(16:0)
  6. LPA(16:0/0:0)
  7. 1-Palmitoyl lysophosphatidate
  8. 1-Palmitoyl lysophosphatidic acid
  9. 2-hydroxy-3-(phosphonooxy)propyl ester Hexadecanoic acid
  10. 1-Palmitoylglycerol 3-phosphate
  11. 1-Palmitoyllysophosphatidate
  12. 1-Palmitoyllysophosphatidic acid
  13. LysoPA(16:0/0:0)
  14. 2-hydroxy-3-(phosphonooxy)propyl ester Hexadecanoate
Chemical IUPAC Name 1-hexadecanoyl-glycero-3-phosphate
Chemical Formula C19H39O7P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Lipids
Class
  • Phospholipids
Sub Class
  • Lysophosphatidic acids
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • carboxylic acid ester
  • phosphoric acid ester
Biofunction
  • Membrane component
  • Energy source
  • Cell signaling
Application
—
Source
  • Endogenous
Average Molecular Weight 410.483
Monoisotopic Molecular Weight 410.243347
Isomeric SMILES CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)COP(O)(O)=O
Canonical SMILES CCCCCCCCCCCCCCCC(=O)OCC(O)COP(O)(O)=O
KEGG Compound ID C00416 Link Image
BioCyc ID L-PHOSPHATIDATE Link Image
BiGG ID Not Available
Wikipedia Link Lecithin Link Image
NuGOwiki Link HMDB07853 Link Image
Metagene Link HMDB07853 Link Image
METLIN ID Not Available
PubChem Compound Not Available
PubChem Substance Not Available
ChEBI ID Not Available
CAS Registry Number Not Available
InChI Identifier InChI=1/C19H39O7P/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-19(21)25-16-18(20)17-26-27(22,23)24/h18,20H,2-17H2,1H3,(H2,22,23,24)/t18-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.42e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 3.87 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Not Available
Not Available
Predicted 13C NMR Spectrum Not Available
Not Available
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane
Biofluid Location Not Available
Tissue Location
Tissue References
All Tissues —
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Glycerolipid Metabolism SMP00039 Link Image map00561 Link Image
Phospholipid Biosynthesis SMP00025 Link Image map00564 Link Image
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Phospholipase D2
  2. Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 precursor
  3. Lipid phosphate phosphohydrolase 2
  4. Diacylglycerol kinase alpha
  5. Diacylglycerol kinase delta
  6. Lipid phosphate phosphohydrolase 1
  7. Diacylglycerol kinase iota
  8. Lipid phosphate phosphohydrolase 3
  9. Diacylglycerol kinase zeta
  10. Acyl-CoA:lysophosphatidylglycerol acyltransferase 1
  11. Focal adhesion kinase 1
  12. Protein tyrosine kinase 2 beta
  13. 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
  14. 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
  15. 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
  16. Phosphatidylinositol-glycan-specific phospholipase D precursor
  17. Lysophosphatidic acid receptor Edg-4
  18. Lysophosphatidic acid receptor Edg-2
  19. 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
  20. 1-acyl-sn-glycerol-3-phosphate acyltransferase zeta precursor
  21. Diacylglycerol kinase eta
  22. 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
  23. 1-acylglycerophosphocholine O-acyltransferase 1
  24. Acyltransferase-like 1
  25. Lysocardiolipin acyltransferase
  26. Lysophosphatidic acid receptor Edg-7
  27. Lysophosphatidic acid receptor 4
  28. Probable G-protein coupled receptor 92
  29. 1-acyl-sn-glycerol-3-phosphate acyltransferase eta
  30. 1-acyl-sn-glycerol-3-phosphate acyltransferase theta
  31. Lysophosphatidic acid phosphatase type 6 precursor
  32. P2Y purinoceptor 5
  33. Lipase member H precursor
  34. Lipase member I precursor
  35. Plasticity related gene 1
  36. Acylglycerol kinase, mitochondrial precursor
  37. Phospholipase D1 variant (Fragment)
  38. 1-acylglycerol-3-phosphate O-acyltransferase 1 (Lysophosphatidic acid acyltransferase, alpha) (1-acylglycerol-3-phosphate O-acyltransferase 1 (Lysophosphatidic acid acyltransferase, alpha), isoform CRA_b)
  39. Testis spermatogenesis apoptosis-related protein 7 (1-acylglycerol-3- phosphate O-acyltransferase 6 (Lysophosphatidic acid acyltransferase, zeta), isoform CRA_b)
  40. Lysocardiolipin acyltransferase (Uncharacterized protein LYCAT)
  41. Diacylglycerol kinase, beta 90kDa (Diacylglycerol kinase, beta 90kDa, isoform CRA_b)
  42. Diacylglycerol kinase, theta 110kDa
  43. Diacylglycerol kinase, epsilon 64kDa (cDNA FLJ75840, highly similar to Homo sapiens diacylglycerol kinase, epsilon 64kDa (DGKE), mRNA)
  44. cDNA, FLJ94990, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 1 (CDS1), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 1, isoform CRA_a)
  45. cDNA, FLJ96552, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 2 (CDS2), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 2, isoform CRA_a)
  46. cDNA, FLJ92787, highly similar to Homo sapiens phosphatidic acid phosphatase type 2B (PPAP2B), mRNA (Phosphatidic acid phosphatase type 2B, isoform CRA_a)
  47. Lysophosphatidic acid receptor 1
  48. High-affinity lysophosphatidic acid receptor homolog
  49. LPAR1 protein
  50. cDNA FLJ61127, highly similar to Lysophosphatidic acid receptor Edg-2
  51. cDNA FLJ41048 fis, clone PROST2001213, highly similar to Lysophosphatidic acid receptor Edg-4
  52. cDNA FLJ12746 fis, clone NT2RP2000842, highly similar to Lysophosphatidic acid receptor Edg-2
  53. cDNA FLJ55767, highly similar to Lysophosphatidic acid receptor Edg-2
Enzyme 1 [top]
Enzyme 1 ID 5309
Enzyme 1 Name Phospholipase D2
Enzyme 1 Synonyms
  1. PLD 2
  2. Choline phosphatase 2
  3. Phosphatidylcholine-hydrolyzing phospholipase D2
  4. PLD1C
  5. hPLD2
Enzyme 1 Gene Name PLD2
Enzyme 1 Protein Sequence >Phospholipase D2 
MTATPESLFPTGDELDSSQLQMESDEVDTLKEGEDPADRMHPFLAIYELQSLKVHPLVFA
PGVPVTAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVL
MSLLPLARFAVAYSPARDAGNREMPSLPRAGPEGSTRHAASKQKYLENYLNRLLTMSFYR
NYHAMTEFLEVSQLSFIPDLGRKGLEGMIRKRSGGHRVPGLTCCGRDQVCYRWSKRWLVV
KDSFLLYMCLETGAISFVQLFDPGFEVQVGKRSTEARHGVRIDTSHRSLILKCSSYRQAR
WWAQEITELAQGPGRDFLQLHRHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIF
ITDWWLSPEVYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRAL
MLLHPNIKVMRHPDQVTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDLGDSSE
SAASQPPTPRPDSPATPDLSHNQFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPW
RDVGVVVHGLPARDLARHFIQRWNFTKTTKAKYKTPTYPYLLPKSTSTANQLPFTLPGGQ
CTTVQVLRSVDRWSAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDE
IVDRILKAHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHR
LKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSANINDRSLL
GKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILGANTRPDLDLRDPICD
DFFQLWQDMAESNANIYEQIFRCLPSNATRSLRTLREYVAVEPLATVSPPLARSELTQVQ
GHLVHFPLKFLEDESLLPPLGSKEGMIPLEVWT
Enzyme 1 Number of Residues 933
Enzyme 1 Molecular Weight 105988
Enzyme 1 Theoretical pI 7.68
Enzyme 1 GO Classification
Function
  • catalytic activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • metabolism
  • physiological process
  • signal transduction
Component
—
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 Specific Function May have a role in signal-induced cytoskeletal regulation and/or endocytosis
Enzyme 1 Pathways
Enzyme 1 Reactions
  • A phosphatidylcholine + H2O = choline + a phosphatidate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 2645858 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O14939 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PLD2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2802 bp 
ATGACGGCGACCCCTGAGAGCCTCTTCCCCACTGGGGACGAACTGGACTCCAGCCAGCTC
CAGATGGAGTCCGATGAGGTGGACACCCTGAAGGAGGGAGAGGACCCAGCCGACCGGATG
CACCCGTTTCTGGCCATCTATGAGCTTCAGTCTCTGAAAGTGCACCCCTTGGTGTTCGCA
CCTGGGGTCCCTGTCACAGCCCAGGTGGTGGGCACCGAAAGATATACCAGCGGATCCAAG
GTGGGAACCTGCACTCTGTATTCTGTCCGCTTGACTCACGGCGACTTTTCCTGGACAACC
AAGAAGAAATACCGTCATTTTCAGGAGCTGCATCGGGACCTCCTGAGACACAAAGTCTTG
ATGAGTCTGCTCCCTCTGGCTCGATTTGCCGTTGCCTATTCTCCAGCCCGAGATGCAGGC
AACAGAGAGATGCCCTCTCTACCCCGGGCAGGTCCTGAGGGCTCCACCAGACATGCAGCC
AGCAAACAGAAATACCTGGAGAATTACCTCAACTGTCTCTTGACCATGTCTTTCTATCGC
AACTACCATGCCATGACAGAGTTCCTGGAAGTCAGTCAGCTGTCCTTTATCCCGGACTTG
GGCCGCAAAGGACTGGAGGGGATGATCCGGAAGCGCTCAGGTGGCCACCGTGTTCCTGGC
CTCACCTGCTGTGGCCGAGACCAAGTTTGTTATCGCTGGTCCAAGAGGTGGCTGGTGGTG
AAGGACTCCTTCCTGCTGTACATGTGCCTCGAGACAGGTGCCATCTCATTTGTTCAGCTC
TTTGACCCTGGCTTTGAGGTGCAAGTGGGGAAAAGGAGCACGGAGGCACGGCACGGCGTG
CGGATCGATACCTCCCACAGGTCCTTGATTCTCAAGTGCAGCAGCTACCGGCAGGCACGG
TGGTGGGCCCAAGAGATCACTGAGCTGGCACAGGGCCCAGGCAGAGACTTCCTACAGCTG
CACCGGCATGACAGCTACGCCCCACCCCGGCCTGGGACCTTGGCCCGGTGGTTTGTGAAT
GGGGCAGGTTACTTTGCTGCTGTGGCAGATGCCATCCTTCGAGCTCAAGAGGAGATTTTC
ATCACAGACTGGTGGTTGAGTCCTGAGGTTTACCTGAAGCGTCCGGCCCATTCAGATGAC
TGGAGACTGGACATTATGCTCAAGAGGAAGGCGGAGGAAGGTGTCCGTGTGTCTATTCTG
CTGTTTAAAGAAGTGGAATTGGCCTTGGGCATCAACAGTGGCTATAGCAAGAGGGCGCTG
ATGCTGCTGCACCCCAACATAAAGGTGATGCGTCACCCAGACCAAGTGACGTTGTGGGCC
CATCATGAGAAGCTCCTGGTGGTGGACCAAGTGGTAGCATTCCTGGGGGGACTGGACCTT
GCCTATGGCCGCTGGGATGACCTGCACTACCGACTGACTGACCTTGGAGACTCCTCTGAA
TCAGCTGCCTCCCAGCCTCCCACCCCGCGCCCAGACTCACCAGCCACCCCAGACCTCTCT
CACAACCAATTCTTCTGGCTGGGCAAGGACTACAGCAATCTTATCACCAAGGACTGGGTG
CAGCTGGACCGGCCTTTCGAAGATTTCATTGACAGGGAGACGACCCCTCGGATGCCATGG
CGGGACGTTGGGGTGGTCGTCCATGGCCTACCGGCCCGGGACCTTGCCCGGCACTTCATC
CAGCGCTGGAACTTCACCAAGACCACCAAGGCCAAGTACAAGACTCCCACATACCCCTAC
CTGCTTCCCAAGTCTACCAGCACGGCCAATCAGCTCCCCTTCACACTTCCAGGAGGGCAG
TGCACCACCGTACAGGTCTTGCGATCAGTGGACCGCTGGTCAGCAGGGACTCTGGAGAAC
TCCATCCTCAATGCCTACCTGCACACCATCAGGGAGAGCCAGCACTTCCTCTACATTGAG
AATCAGTTCTTCATTAGCTGCTCAGATGGGCGGACGGTTCTGAACAAGGTGGGCGATGAG
ATTGTGGACAGAATCCTGAAGGCCCACAAACAGGGGTGGTGTTACCGAGTCTACGTGCTT
TTGCCCTTACTCCCTGGCTTCGAGGGTGACATCTCCACGGGCGGTGGCAACTCCATCCAG
GCCATTCTGCACTTTACTTACAGGACCCTGTGTCGTGGGGAGTATTCAATCCTGCATCGC
CTTAAAGCAGCCATGGGGACAGCATGGCGGGACTATATTTCCATCTGCGGGCTTCGTACA
CACGGAGAGCTGGGCGGGCACCCCGTCTCGGAGCTCATCTACATCCACAGCAAGGTGCTC
ATCGCAGATGACCGGACAGTCATCATTGGTTCTGCAAACATCAATGACCGGAGCTTGCTG
GGGAAGCGGGACAGTGAGCTGGCCGTGCTGATCGAGGACACAGAGACGGAACCATCCCTC
ATGAATGGGGCAGAGTATCAGGCGGGCAGGTTTGCCTTGAGTCTGCGGAAGCACTGCTTC
GGTGTGATTCTTGGAGCAAATACCCGGCCAGACTTGGATCTCCGAGACCCCATCTGTGAT
GACTTCTTCCAGTTGTGGCAAGACATGGCTGAGAGCAACGCCAATATCTATGAGCAGATC
TTCCGCTGCCTGCCATCCAATGCCACGCGTTCCCTGCGGACTCTCCGGGAGTACGTGGCC
GTGGAGCCCTTGGCCACGGTCAGTCCCCCCTTGGCTCGGTCTGAGCTCACCCAGGTCCAG
GGCCACCTGGTCCACTTCCCCCTCAAGTTCCTAGAGGATGAGTCTTTGCTGCCCCCGCTG
GGTAGCAAGGAGGGCATGATCCCCCTAGAAGTGTGGACATAG
Enzyme 1 GenBank Gene ID AF033850 Link Image
Enzyme 1 GeneCard ID PLD2 Link Image
Enzyme 1 GenAtlas ID PLD2 Link Image
Enzyme 1 HGNC ID HGNC:9068 Link Image
Enzyme 1 Chromosome Location 17
Enzyme 1 Locus 17p13.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Steed PM, Clark KL, Boyar WC, Lasala DJ: Characterization of human PLD2 and the analysis of PLD isoform splice variants. FASEB J. 1998 Oct;12(13):1309-17. [PubMed Link Image]
  2. Lopez I, Arnold RS, Lambeth JD: Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2. J Biol Chem. 1998 May 22;273(21):12846-52. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5399
Enzyme 2 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 precursor
Enzyme 2 Synonyms
  1. E-NPP 2
  2. Extracellular lysophospholipase D
  3. LysoPLD
  4. Autotaxin
Enzyme 2 Gene Name ENPP2
Enzyme 2 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 precursor 
MARRSSFQSCQIISLFTFAVGVNICLGFTAHRIKRAEGWEEGPPTVLSDSPWTNISGSCK
GRCFELQEAGPPDCRCDNLCKSYTSCCHDFDELCLKTARGWECTKDRCGEVRNEENACHC
SEDCLARGDCCTNYQVVCKGESHWVDDDCEEIKAAECPAGFVRPPLIIFSVDGFRASYMK
KGSKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDA
TFHLRGREKFNHRWWGGQPLWITATKQGVKAGTFFWSVVIPHERRILTILQWLTLPDHER
PSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDH
GMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRSKFSNNAKYDPKAIIANLTCKKPDQH
FKPYLKQHLPKRLHYANNRRIEDIHLLVERRWHVARKPLDVYKKPSGKCFFQGDHGFDNK
VNSMQTVFVGYGPTFKYKTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTF
RPTMPEEVTRPNYPGIMYLQSDFDLGCTCDDKVEPKNKLDELNKRLHTKGSTEERHLLYG
RPAVLYRTRYDILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVPDHLTSCVRPDVRVS
PSFSQNCLAYKNDKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWNYFQRVL
VKKYASERNGVNVISGPIFDYDYDGLHDTEDKIKQYVEGSSIPVPTHYYSIITSCLDFTQ
PADKCDGPLSVSSFILPHRPDNEESCNSSEDESKWVEELMKMHTARVRDIEHLTSLDFFR
KTSRSYPEILTLKTYLHTYESEI
Enzyme 2 Number of Residues 863
Enzyme 2 Molecular Weight 99004
Enzyme 2 Theoretical pI 7.39
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • endonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Hydrolyzes lysophospholipids to produce lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine. Also can act on sphingosylphosphphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP. Involved in several motility- related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. May have a role in induction of parturition. Possible involvement in cell proliferation and adipose tissue development Tumor cell motility-stimulating factor
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • 1-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-27
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 537906 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q13822 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ENPP2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2748 bp 
ATGGCAAGGAGGAGCTCGTTCCAGTCGTGTCAGATAATATCCCTGTTCACTTTTGCCGTT
GGAGTCAGTATCTGCTTAGGATTCACTGCACATCGAATTAAGAGAGCAGAAGGATGGGAG
GAAGGTCCTCCTACAGTGCTATCAGACTCCCCCTGGACCAACATCTCCGGATCTTGCAAG
GGCAGGTGCTTTGAACTTCAAGAGGCTGGACCTCCTGATTGTCGCTGTGACAACTTGTGT
AAGAGCTATACCAGTTGCTGCCATGACTTTGATGAGCTGTGTTTGAAGACAGCCCGTGGC
TGGGAGTGTACTAAGGACAGATGTGGAGAAGTCAGAAATGAAGAAAATGCCTGTCACTGC
TCAGAGGACTGCTTGGCCAGGGGAGACTGCTGTACCAATTACCAAGTGGTTTGCAAAGGA
GAGTCGCATTGGGTTGATGATGACTGTGAGGAAATAAAGGCCGCAGAATGCCCTGCAGGG
TTTGTTCGCCCTCCATTAATCATCTTCTCCGTGGATGGCTTCCGTGCATCATACATGAAG
AAAGGCAGCAAAGTCATGCCTAATATTGAAAAACTAAGGTCTTGTGGCACACACTCTCCC
TACATGAGGCCGGTGTACCCAACTAAAACCTTTCCTAACTTATACACTTTGGCCACTGGG
CTATATCCAGAATCACATGGAATTGTTGGCAATTCAATGTATGATCCTGTATTTGATGCC
ACTTTTCATCTGCGAGGGCGAGAGAAATTTAATCATAGATGGTGGGGAGGTCAACCGCTA
TGGATTACAGCCACCAAGCAAGGGGTGAAAGCTGGAACATTCTTTTGGTCTGTTGTCATC
CCTCACGAGCGGAGAATATTAACCATATTGCGGTGGCTCACCCTGCCAGATCATGAGAGG
CCTTCGGTCTATGCCTTCTATTCTGAGCAACCTGATTTCTCTGGACACAAATATGGCCCT
TTCGGCCCTGAGGAGAGTAGTTATGGCTCACCTTTTACTCCGGCTAAGAGACCTAAGAGG
AAAGTTGCCCCTAAGAGGAGACAGGAAAGACCAGTTGCTCCTCCAAAGAAAAGAAGAAGA
AAAATACATAGGATGGATCATTATGCTGCGGAAACTCGTCAGGACAAAATGACAAATCCT
CTGAGGGAAATCGACAAAATTGTGGGGCAATTAATGGATGGACTGAAACAACTAAAACTG
CGTCGGTGTGTCAACGTCATCTTTGTCGGAGACCATGGAATGGAAGATGTCACATGTGAT
AGAACTGAGTTCTTGAGTAATTACCTAACTAATGTGGATGATATTACTTTAGTGCCTGGA
ACTCTAGGAAGAATTCGATCCAAATTTAGCAACAATGCTAAATATGACCCCAAAGCCATT
ATTGCCAATCTCACGTGTAAAAAACCAGATCAGCACTTTAAGCCTTACTTGAAACAGCAC
CTTCCCAAACGTTTGCACTATGCCAACAACAGAAGAATTGAGGATATCCATTTATTGGTG
GAACGCAGATGGCATGTTGCAAGGAAACCTTTGGATGTTTATAAGAAACCATCAGGAAAA
TGCTTTTTCCAGGGAGACCACGGATTTGATAACAAGGTCAACAGCATGCAGACTGTTTTT
GTAGGTTATGGCCCAACATTTAAGTACAAGACTAAAGTGCCTCCATTTGAAAACATTGAA
CTTTACAATGTTATGTGTGATCTCCTGGGATTGAAGCCAGCTCCTAATAATGGGACCCAT
GGAAGTTTGAATCATCTCCTGCGCACTAATACCTTCAGGCCAACCATGCCAGAGGAAGTT
ACCAGACCCAATTATCCAGGGATTATGTACCTTCAGTCTGATTTTGACCTGGGCTGCACT
TGTGATGATAAGGTAGAGCCAAAGAACAAGTTGGATGAACTCAACAAACGGCTTCATACA
AAAGGGTCTACAGAAGAGAGACACCTCCTCTATGGGCGACCTGCAGTGCTTTATCGGACT
AGATATGATATCTTATATCACACTGACTTTGAAAGTGGTTATAGTGAAATATTCCTAATG
CTACTCTGGACATCATATACTGTTTCCAAACAGGCTGAGGTTTCCAGCGTTCCTGACCAT
CTGACCAGTTGCGTCCGGCCTGATGTCCGTGTTTCTCCGAGTTTCAGTCAGAACTGTTTG
GCCTACAAAAATGATAAGCAGATGTCCTACGGATTCCTCTTTCCTCCTTATCTGAGCTCT
TCACCAGAGGCTAAATATGATGCATTCCTTGTAACCAATATGGTTCCAATGTATCCTGCT
TTCAAACGGGTCTGGAATTATTTCCAAAGGGTATTGGTGAAGAAATATGCTTCGGAAAGA
AATGGAGTTAACGTGATAAGTGGACCAATCTTCGACTATGACTATGATGGCTTACATGAC
ACAGAAGACAAAATAAAACAGTACGTGGAAGGCAGTTCCATTCCTGTTCCAACTCACTAC
TACAGCATCATCACCAGCTGTCTGGATTTCACTCAGCCTGCCGACAAGTGTGACGGCCCT
CTCTCTGTGTCCTCCTTCATCCTGCCTCACCGGCCTGACAACGAGGAGAGCTGCAATAGC
TCAGAGGACGAATCAAAATGGGTAGAAGAACTCATGAAGATGCACACAGCTAGGGTGCGT
GACATTGAACATCTCACCAGCCTGGACTTCTTCCGAAAGACCAGCCGCAGCTACCCAGAA
ATCCTGACACTCAAGACATACCTGCATACATATGAGAGCGAGATTTAA
Enzyme 2 GenBank Gene ID L35594 Link Image
Enzyme 2 GeneCard ID ENPP2 Link Image
Enzyme 2 GenAtlas ID ENPP2 Link Image
Enzyme 2 HGNC ID HGNC:3357 Link Image
Enzyme 2 Chromosome Location 8
Enzyme 2 Locus 8q24.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Murata J, Lee HY, Clair T, Krutzsch HC, Arestad AA, Sobel ME, Liotta LA, Stracke ML: cDNA cloning of the human tumor motility-stimulating protein, autotaxin, reveals a homology with phosphodiesterases. J Biol Chem. 1994 Dec 2;269(48):30479-84. [PubMed Link Image]
  2. Lee HY, Murata J, Clair T, Polymeropoulos MH, Torres R, Manrow RE, Liotta LA, Stracke ML: Cloning, chromosomal localization, and tissue expression of autotaxin from human teratocarcinoma cells. Biochem Biophys Res Commun. 1996 Jan 26;218(3):714-9. [PubMed Link Image]
  3. Kawagoe H, Soma O, Goji J, Nishimura N, Narita M, Inazawa J, Nakamura H, Sano K: Molecular cloning and chromosomal assignment of the human brain-type phosphodiesterase I/nucleotide pyrophosphatase gene (PDNP2). Genomics. 1995 Nov 20;30(2):380-4. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5463
Enzyme 3 Name Lipid phosphate phosphohydrolase 2
Enzyme 3 Synonyms
  1. Phosphatidic acid phosphatase 2c
  2. Phosphatidate phosphohydrolase type 2c
  3. PAP2c
  4. PAP- 2c
  5. PAP2-gamma
  6. PAP2-G
Enzyme 3 Gene Name PPAP2C
Enzyme 3 Protein Sequence >Lipid phosphate phosphohydrolase 2 
MQRRWVFVLLDVLCLLVASLPFAILTLVNAPYKRGFYCGDDSIRYPYRPDTITHGLMAGV
TITATVILVSAGEAYLVYTDRLYSRSDFNNYVAAVYKVLGTFLFGAAVSQSLTDLAKYMI
GRLRPNFLAVCDPDWSRVNCSVYVQLEKVCRGNPADVTEARLSFYSGHSSFGMYCMVFLA
LYVQARLCWKWARLLRPTVQFFLVAFALYVGYTRVSDYKHHWSDVLVGLLQGALVAALTV
CYISDFFKARPPQHCLKEEELERKPSLSLTLTLGEADHNHYGYPHSSS
Enzyme 3 Number of Residues 288
Enzyme 3 Molecular Weight 32574
Enzyme 3 Theoretical pI 8.44
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1- phosphate (S-1-P). The relative catalytic efficiency is PA > C-1-P > LPA > S-1-P
Enzyme 3 Pathways
Enzyme 3 Reactions
  • A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-30
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 3123896 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O43688 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name LPP2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >867 bp 
ATGCAGCGGAGGTGGGTCTTCGTGCTGCTCGACGTGCTGTGCTTACTGGTCGCCTCCCTG
CCCTTCGCTATCCTGACGCTGGTGAACGCCCCGTACAAGCGAGGATTTTACTGCGGGGAT
GACTCCATCCGGTACCCCTACCGTCCAGATACCATCACCCACGGGCTCATGGCTGGGGTC
ACCATCACGGCCACCGTCATCCTTGTCTCGGCCGGGGAAGCCTACCTGGTGTACACAGAC
CGGCTCTATTCTCGCTCGGACTTCAACAACTACGTGGCTGCTGTATACAAGGTGCTGGGG
ACCTTCCTGTTTGGGGCTGCCGTGAGCCAGTCTCTGACAGACCTGGCCAAGTACATGATT
GGGCGTCTGAGGCCCAACTTCCTAGCCGTCTGCGACCCCGACTGGAGCCGGGTCAACTGC
TCGGTCTATGTGCAGCTGGAGAAGGTGTGCAGGGGAAACCCTGCTGATGTCACCGAGGCC
AGGTTGTCTTTCTACTCGGGACACTCTTCCTTTGGGATGTACTGCATGGTGTTCTTGGCG
CTGTATGTGCAGGCACGACTCTGTTGGAAGTGGGCACGGCTGCTGCGACCCACAGTCCAG
TTCTTCCTGGTGGCCTTTGCCCTCTACGTGGGCTACACCCGCGTGTCTGATTACAAACAC
CACTGGAGCGATGTCCTTGTTGGCCTCCTGCAGGGGGCACTGGTGGCTGCCCTCACTGTC
TGCTACATCTCAGACTTCTTCAAAGCCCGACCCCCACAGCACTGTCTGAAGGAGGAGGAG
CTGGAACGGAAGCCCAGCCTGTCACTGACGTTGACCCTGGGCGAGGCTGACCACAACCAC
TATGGATACCCGCACTCCTCCTCCTGA
Enzyme 3 GenBank Gene ID AF035959 Link Image
Enzyme 3 GeneCard ID PPAP2C Link Image
Enzyme 3 GenAtlas ID PPAP2C Link Image
Enzyme 3 HGNC ID HGNC:9230 Link Image
Enzyme 3 Chromosome Location 19
Enzyme 3 Locus 19p13
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Leung DW, Tompkins CK, White T: Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. DNA Cell Biol. 1998 Apr;17(4):377-85. [PubMed Link Image]
  2. Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5465
Enzyme 4 Name Diacylglycerol kinase alpha
Enzyme 4 Synonyms
  1. Diglyceride kinase alpha
  2. DGK-alpha
  3. DAG kinase alpha
  4. 80 kDa diacylglycerol kinase
Enzyme 4 Gene Name DGKA
Enzyme 4 Protein Sequence >Diacylglycerol kinase alpha 
MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIY
LEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFK
LYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEW
VRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKY
TVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHC
VWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNL
STSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRL
FKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQ
NLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIM
REKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVL
NIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLE
GAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDVEPWMQTPCTIKITHKNQMPML
MGPPPRSTNFFGFLS
Enzyme 4 Number of Residues 735
Enzyme 4 Molecular Weight 82673
Enzyme 4 Theoretical pI 6.71
Enzyme 4 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • diacylglycerol kinase activity
  • ion binding
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 30823 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P23743 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name DGKA_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2208 bp 
ATGGCCAAGGAGAGGGGCCTAATAAGCCCCAGTGATTTTGCCCAGCTGCAAAAATACATG
GAATACTCCACCAAAAAGGTCAGTGATGTCCTAAAGCTCTTCGAGGATGGCGAGATGGCT
AAATATGTCCAAGGAGATGCCATTGGGTACGAGGGATTCCAGCAATTCCTGAAAATCTAT
CTCGAAGTGGATAATGTTCCCAGACACCTAAGCCTGGCACTGTTTCAATCCTTTGAGACT
GGTCACTGCTTAAATGAGACAAATGTGACAAAAGATGTGGTGTGTCTCAATGATGTTTCC
TGCTACTTTTCCCTTCTGGAGGGTGGTCGGCCAGAAGACAAGTTAGAATTCACCTTCAAG
CTGTACGACACGGACAGAAATGGGATCCTGGACAGCTCAGAAGTGGACAAAATTATCCTA
CAGATGATGCGAGTGGCTGAATACCTGGATTGGGATGTGTCTGAGCTGAGGCCGATTCTT
CAGGAGATGATGAAAGAGATTGACTATGATGGCAGTGGCTCTGTCTCTCAAGCTGAGTGG
GTCCGGGCTGGGGCCACCACCGTGCCACTGCTAGTGCTGCTGGGTCTGGAGATGACTCTG
AAGGACGACGGACAGCACATGTGGAGGCCCAAGAGGTTCCCCAGACCAGTCTACTGCAAT
CTGTGCGAGTCAAGCATTGGTCTTGGCAAACAGGGACTGAGCTGTAACCTCTGTAAGTAC
ACTGTTCACGACCAGTGTGCCATGAAAGCCCTGCCTTGTGAAGTCAGCACCTATGCCAAG
TCTCGGAAGGACATTGGTGTCCAATCACATGTGTGGGTGCGAGGAGGCTGTGAGTCCGGG
CGCTGCGACCGCTGTCAGAAAAAGATCCGGATCTACCACAGTCTGACCGGGCTGCATTGT
GTATGGTGCCACCTAGAGATCCACGATGACTGCCTGCAAGCGGTGGGCCATGAGTGTGAC
TGTGGGCTGCTCCGGGATCACATCCTGCCTCCATCTTCCATCTATCCCAGTGTCCTGGCC
TCTGGACCGGATCGTAAAAATAGCAAAACAAGCCAGAAGACCATGGATGATTTAAATTTG
AGCACCTCTGAGGCTCTGCGGATTGACCCTGTTCCTAACACCCACCCACTTCTCGTCTTT
GTCAATCCTAAGAGTGGCGGGAAGCAGGGGCAGAGGGTGCTCTGGAAGTTCCAGTATATA
TTAAACCCTCGACAGGTGTTCAACCTCCTAAAGGATGGTCCTGAGATAGGGCTCCGATTA
TTCAAGGATGTTCCTGATAGCCGGATTTTGGTGTGTGGTGGAGACGGCACAGTAGGCTGG
ATTCTAGAGACCATTGACAAAGCTAACTTGCCAGTTTTGCCTCCTGTTGCTGTGTTGCCC
CTGGGTACTGGAAATGATCTGGCTCGATGCCTAAGATGGGGAGGAGGTTATGAAGGACAG
AATCTGGCAAAGATCCTCAAGGATTTAGAGATGAGTAAAGTGGTACATATGGATCGATGG
TCTGTGGAGGTGATACCTCAACAAACTGAAGAAAAAAGTGACCCAGTCCCCTTTCAAATC
ATCAATAACTACTTCTCTATTGGCGTGGATGCCTCTATTGCTCATCGATTCCACATCATG
CGAGAGAAATATCCGGAGAAGTTCAACAGCAGAATGAAGAACAAGCTATGGTACTTCGAA
TTTGCCACATCTGAATCCATCTTCTCAACATGCAAAAAGCTGGAGGAGTCTTTGACAGTT
GAGATCTGTGGGAAACCGCTGGATCTGAGCAACCTGTCCCTAGAAGGCATCGCAGTGCTA
AACATCCCTAGCATGCATGGTGGCTCCAACCTCTGGGGTGATACCAGGAGACCCCATGGG
GATATCTATGGGATCAACCAGGCCTTAGGTGCTACAGCTAAAGTCATCACCGACCCTGAT
ATCCTGAAAACCTGTGTACCAGACCTAAGTGACAAGAGACTGGAAGTGGTTGGGCTGGAG
GGTGCAATTGAGATGGGCCAAATCTATACCAAGCTCAAGAATGCTGGACGTCGGCTGGCC
AAGTGCTCTGAGATCACCTTCCACACCACAAAAACCCTTCCCATGCAAATTGACGTAGAA
CCCTGGATGCAGACGCCCTGTACAATCAAGATCACCCACAAGAACCAGATGCCCATGCTC
ATGGGCCCACCCCCCCGCTCCACCAATTTCTTTGGCTTCTTGAGCTAA
Enzyme 4 GenBank Gene ID X62535 Link Image
Enzyme 4 GeneCard ID DGKA Link Image
Enzyme 4 GenAtlas ID DGKA Link Image
Enzyme 4 HGNC ID HGNC:2849 Link Image
Enzyme 4 Chromosome Location 12
Enzyme 4 Locus 12q13.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Schaap D, de Widt J, van der Wal J, Vandekerckhove J, van Damme J, Gussow D, Ploegh HL, van Blitterswijk WJ, van der Bend RL: Purification, cDNA-cloning and expression of human diacylglycerol kinase. FEBS Lett. 1990 Nov 26;275(1-2):151-8. [PubMed Link Image]
  2. Hart TC, Champagne C, Zhou J, Van Dyke TE: Assignment of the gene for diacylglycerol kinase (DAGK) to human chromosome 12. Mamm Genome. 1994 Feb;5(2):123-4. [PubMed Link Image]
  3. Hart TC, Zhou J, Champagne C, Van Dyke TE, Rao PN, Pettenati MJ: Assignment of the human diacylglycerol kinase gene (DAGK) to 12q13.3 using fluorescence in situ hybridization analysis. Genomics. 1994 Jul 1;22(1):246-7. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5466
Enzyme 5 Name Diacylglycerol kinase delta
Enzyme 5 Synonyms
  1. Diglyceride kinase delta
  2. DGK-delta
  3. DAG kinase delta
  4. 130 kDa diacylglycerol kinase
Enzyme 5 Gene Name DGKD
Enzyme 5 Protein Sequence >Diacylglycerol kinase delta 
MAAAAGAPPPGPPQPPPPPPPEESSDSEPEAEPGSPQKLIRKVSTSGQIRQKTIIKEGML
TKQNNSFQRSKRRYFKLRGRTLYYAKTAKSIIFDEVDLTDASVAESSTKNVNNSFTVITP
CRKLILCADNRKEMEDWIAALKTVQNREHFEPTQYSMDHFSGMHNWYACSHARPTYCNVC
REALSGVTSHGLSCEVCKFKAHKRCAVRATNNCKWTTLASIGKDIIEDADGIAMPHQWLE
GNLPVSAKCTVCDKTCGSVLRLQDWRCLWCKAMVHTSCKESLLTKCPLGLCKVSVIPPTA
LNSIDSDGFWKASCPPSCTSPLLVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPH
LGLRLFQKFDTFRILVCGGDGSVGWVLSEIDSLNLHKQCQLGVLPLGTGNDLARVLGWGS
ACDDDTQLPQILEKLERASTKMLDRWSVMAYEAKLPRQASSSTVTEDFSEDSEVQQILFY
EDSVAAHLSKILTSDQHSVVISSAKVLCETVKDFVARVGKAYEKTTESSEESEVMAKKCS
VLKEKLDSLLKTLDDESQASSSLPNPPPTIAEEAEDGDGSGSICGSTGDRLVASACPARP
QIFRPREQLMLRANSLKKAIRQIIEHTEKAVDEQNAQTQEQEGFVLGLSESEEKMDHRVC
PPLSHSESFGVPKGRSQRKVSKSPCEKLISKGSLSLGSSASLPPQPGSRDGLPALNTKIL
YPNVRAGMSGSLPGGSVISRLLINADPFNSEPETLEYYTEKCVMNNYFGIGLDAKISLDF
NNKRDEHPEKCRSRTKNMMWYGVLGTKELLHRTYKNLEQKVLLECDGRPIPLPSLQGIAV
LNIPSYAGGTNFWGGTKEDDTFAAPSFDDKILEVVAVFGSMQMAVSRVIRLQHHRIAQCR
TVKISILGDEGVPVQVDGEAWVQPPGYIRIVHKNRAQTLTRDRAFESTLKSWEDKQKCEL
PRPPSCSLHPEMLSEEEATQMDQFGQAAGVLIHSIREIAQSHRDMEQELAHAVNASSKSM
DRVYGKPRTTEGLNCSFVLEMVNNFRALRSETELLLSGKMALQLDPPQKEQLGSALAEMD
RQLRRLADTPWLCQSAEPGDEESVMLDLAKRSRSGKFRLVTKFKKEKNNKNKEAHSSLGA
PVHLWGTEEVAAWLEHLSLCEYKDIFTRHDIRGSELLHLERRDLKDLGVTKVGHMKRILC
GIKELSRSAPAVEA
Enzyme 5 Number of Residues 1214
Enzyme 5 Molecular Weight 134527
Enzyme 5 Theoretical pI 7.58
Enzyme 5 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function May function as signaling molecule. Isoform 2 may be involved in cell growth and tumorigenesis
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 22773821 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q16760 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name DGKD_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >3645 bp 
ATGGCGGCGGCGGCGGGCGCCCCTCCGCCGGGTCCCCCGCAACCGCCTCCGCCGCCGCCG
CCCGAGGAGTCGTCCGACAGCGAGCCCGAGGCGGAGCCCGGCTCCCCACAGAAGCTCATC
CGCAAGGTGTCCACGTCGGGTCAGATCCGACAGAAGACCATCATCAAAGAGGGGATGCTG
ACCAAACAGAACAATTCATTCCAGCGATCAAAAAGGAGATACTTTAAGCTTCGAGGGCGA
ACGCTTTACTATGCCAAAACGGCAAAGTCAATCATATTTGATGAGGTGGATCTGACAGAT
GCCAGCGTAGCTGAATCCAGTACCAAAAACGTCAACAACAGTTTTACGGTCATAACTCCA
TGCAGGAAGCTCATCTTGTGTGCTGATAACAGAAAAGAAATGGAAGATTGGATTGCAGCA
TTAAAGACTGTGCAGAACAGGGAGCACTTTGAGCCCACCCAGTACAGCATGGACCACTTC
TCAGGGATGCACAATTGGTACGCCTGTTCCCACGCGAGGCCGACCTACTGCAATGTGTGC
CGTGAGGCTCTGTCTGGGGTCACGTCGCACGGGCTGTCCTGCGAGGTGTGCAAATTTAAG
GCCCACAAGCGCTGTGCTGTGCGTGCAACCAATAACTGCAAGTGGACCACACTGGCCTCG
ATCGGGAAGGACATCATTGAAGATGCAGATGGGATTGCAATGCCCCACCAGTGGTTGGAA
GGAAACCTACCTGTGAGCGCCAAGTGCACTGTGTGCGACAAGACCTGTGGCAGTGTGCTG
CGCCTGCAGGACTGGCGCTGCCTCTGGTGCAAGGCCATGGTTCACACATCGTGTAAAGAA
TCCTTGCTGACCAAGTGCCCACTTGGCCTGTGCAAAGTGTCAGTCATCCCACCCACGGCT
CTCAACAGCATCGACTCCGATGGGTTCTGGAAGGCCAGCTGTCCTCCTTCTTGCACAAGC
CCACTGTTGGTCTTCGTCAATTCAAAAAGTGGGGACAACCAGGGTGTGAAGTTCCTCAGA
AGATTCAAACAGCTACTAAACCCCGCCCAGGTCTTCGACCTCATGAACGGAGGCCCACAC
CTCGGCTTACGGTTATTCCAGAAGTTTGACACATTCCGGATTCTGGTTTGTGGCGGGGAT
GGAAGTGTTGGCTGGGTCCTCTCCGAAATCGACAGCCTCAACCTTCATAAACAGTGTCAG
CTGGGAGTGCTGCCGCTCGGCACAGGGAACGACTTGGCCCGAGTACTGGGCTGGGGCTCA
GCCTGCGATGACGACACCCAGCTCCCCCAGATCTTGGAGAAGTTGGAGAGAGCCAGCACC
AAGATGCTGGACAGGTGGAGCGTCATGGCATACGAGGCCAAGCTCCCCCGGCAGGCCTCC
TCCTCTACCGTCACCGAAGACTTCAGCGAGGATTCCGAGGTACAGCAGATTCTCTTCTAT
GAAGACTCGGTTGCAGCCCACCTTTCTAAAATCCTCACCTCGGACCAGCACTCGGTGGTC
ATCTCCTCGGCCAAAGTGCTCTGTGAGACGGTGAAGGACTTCGTGGCACGGGTGGGGAAG
GCCTATGAGAAGACGACCGAGAGCTCGGAGGAGTCAGAGGTCATGGCCAAGAAGTGCTCT
GTCCTGAAAGAGAAGCTGGATTCCCTTCTCAAGACCTTGGACGATGAGTCCCAGGCCTCG
TCCTCTCTGCCCAACCCGCCCCCCACCATTGCCGAGGAGGCTGAAGATGGAGATGGGTCG
GGCAGCATCTGCGGTTCCACCGGAGACCGCTTGGTGGCATCAGCTTGCCCGGCCCGGCCG
CAGATATTCCGGCCTCGAGAACAGCTCATGCTGAGAGCCAACAGCCTGAAGAAAGCAATT
CGTCAGATCATAGAACACACAGAAAAAGCTGTCGATGAGCAGAATGCCCAGACCCAGGAG
CAGGAGGGCTTCGTCCTGGGCCTCTCTGAGTCAGAGGAGAAGATGGACCACAGAGTGTGC
CCACCACTGTCCCACAGCGAGAGCTTCGGGGTCCCCAAGGGGAGGAGCCAGCGCAAAGTG
TCGAAATCTCCGTGTGAAAAGCTGATCAGCAAAGGGAGTCTGTCCCTAGGCAGTTCTGCT
TCCCTTCCGCCCCAGCCGGGAAGCCGGGACGGCCTGCCTGCGCTCAACACCAAGATCCTG
TACCCAAATGTCCGGGCTGGAATGTCTGGTTCCTTACCCGGTGGCTCAGTCATCAGTCGC
CTGTTAATTAATGCTGATCCCTTCAACTCTGAACCAGAAACCCTAGAGTATTACACGGAG
AAATGTGTCATGAACAACTATTTTGGCATTGGCCTGGATGCGAAGATATCCCTGGACTTT
AACAACAAGCGCGATGAGCACCCAGAGAAGTGCAGGAGCCGAACCAAGAACATGATGTGG
TATGGAGTTCTTGGAACCAAAGAGTTGCTGCACAGAACCTACAAGAACCTGGAGCAAAAG
GTCTTGCTGGAGTGTGACGGGCGACCCATCCCACTCCCCAGTCTTCAGGGAATTGCTGTC
CTTAACATTCCCAGCTATGCCGGAGGAACCAACTTCTGGGGGGGTACCAAGGAAGATGAT
ACTTTCGCAGCTCCATCATTCGATGACAAGATTCTGGAGGTGGTCGCCGTGTTCGGCAGC
ATGCAGATGGCCGTCTCTCGAGTCATCAGGCTACAGCATCATCGGATCGCCCAGTGTCGC
ACGGTGAAGATCTCCATCCTTGGGGATGAGGGCGTGCCTGTGCAGGTGGACGGAGAGGCC
TGGGTCCAGCCGCCAGGGTACATTCGGATTGTCCACAAGAACCGGGCACAGACACTGACC
AGAGACAGGGCATTTGAGAGCACCCTGAAGTCCTGGGAAGACAAGCAGAAGTGCGAGGTG
CCCCGCCCTCCATCCTGTTCCCTGCACCCGGAGATGCTGTCCGAGGAGGAGGCCACCCAG
ATGGACCAGTTTGGGCAGGCAGCAGGGGTCCTCATTCACAGTATCCGAGAAATAGCTCAG
TCTCACCGGGACATGGAGCAGGAACTGGCCCACGCCGTCAATGCCAGCTCCAAGTCCATG
GACCGTGTGTATGGCAAGCCCAGAACCACAGAGGGGCTCAACTGCAGCTTCGTCCTGGAA
ATGGTGAATAACTTCAGAGCTCTGCGCAGTGAGACGGAGCTGCTGCTGTCTGGGAAGATG
GCCCTGCAGCTGGATCCGCCTCAGAAGGAGCAGCTGGGGAGTGCTCTTGCCGAGATGGAC
CGACAGCTCAGGAGGCTGGCAGACACCCCGTGGCTCTGCCAGTCCGCAGAGCCCGGCGAC
GAAGAGAGTGTGATGCTGGATCTTGCCAAGCGCAGTCGCAGTGGTAAATTCCGCCTCGTG
ACCAAGTTTAAAAAGGAGAAAAACAACAAGAACAAAGAAGCTCACAGTAGCCTGGGAGCC
CCGGTTCACCTCTGGGGGACAGAGGAGGTTGCTGCCTGGCTGGAGCACCTCAGTCTCTGT
GAGTATAAGGACATCTTCACACGGCACGACATCCGGGGCTCTGAGCTCCTGCACCTGGAG
CGGAGGGACCTCAAGGACCTGGGCGTGACCAAGGTGGGCCACATGAAGAGGATCCTGTGT
GGCATCAAGGAGCTGAGCCGCAGCGCCCCCGCCGTCGAGGCCTAG
Enzyme 5 GenBank Gene ID AB078966 Link Image
Enzyme 5 GeneCard ID DGKD Link Image
Enzyme 5 GenAtlas ID DGKD Link Image
Enzyme 5 HGNC ID HGNC:2851 Link Image
Enzyme 5 Chromosome Location 2
Enzyme 5 Locus 2q37.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Sakane F, Imai S, Yamada K, Murakami T, Tsushima S, Kanoh H: Alternative splicing of the human diacylglycerol kinase delta gene generates two isoforms differing in their expression patterns and in regulatory functions. J Biol Chem. 2002 Nov 8;277(45):43519-26. Epub 2002 Aug 27. [PubMed Link Image]
  2. Nagase T, Seki N, Tanaka A, Ishikawa K, Nomura N: Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995 Aug 31;2(4):167-74, 199-210. [PubMed Link Image]
  3. Sakane F, Imai S, Kai M, Wada I, Kanoh H: Molecular cloning of a novel diacylglycerol kinase isozyme with a pleckstrin homology domain and a C-terminal tail similar to those of the EPH family of protein-tyrosine kinases. J Biol Chem. 1996 Apr 5;271(14):8394-401. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5469
Enzyme 6 Name Lipid phosphate phosphohydrolase 1
Enzyme 6 Synonyms
  1. Phosphatidic acid phosphatase 2a
  2. Phosphatidate phosphohydrolase type 2a
  3. PAP2a
  4. PAP- 2a
  5. PAP2-alpha
Enzyme 6 Gene Name PPAP2A
Enzyme 6 Protein Sequence >Lipid phosphate phosphohydrolase 1 
MFDKTRLPYVALDVLCVLLAGLPFAILTSRHTPFQRGVFCNDESIKYPYKEDTIPYALLG
GIIIPFSIIVIILGETLSVYCNLLHSNSFIRNNYIATIYKAIGTFLFGAAASQSLTDIAK
YSIGRLRPHFLDVCDPDWSKINCSDGYIEYYICRGNAERVKEGRLSFYSGHSSFSMYCML
FVALYLQARMKGDWARLLRPTLQFGLVAVSIYVGLSRVSDYKHHWSDVLTGLIQGALVAI
LVAVYVSDFFKERTSFKERKEEDSHTTLHETPTTGNHYPSNHQP
Enzyme 6 Number of Residues 284
Enzyme 6 Molecular Weight 32156
Enzyme 6 Theoretical pI 8.06
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Lipid transport and metabolism
Enzyme 6 Specific Function Broad-specificity phosphohydrolase that dephosphorylates exogenous bioactive glycerolipids and sphingolipids. Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). Pivotal regulator of lysophosphatidic acid (LPA) signaling in the cardiovascular system. Major enzyme responsible of dephosphorylating LPA in platelets, which terminates signaling actions of LPA. May control circulating, and possibly also regulate localized, LPA levels resulting from platelet activation. It has little activity towards ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA > PA > S-1-P > C-1-P. It's down-regulation may contribute to the development of colon adenocarcinoma
Enzyme 6 Pathways
Enzyme 6 Reactions
  • A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-27
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 2467298 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID O14494 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name LPP1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >855 bp 
ATGTTCGACAAGACGCGGCTGCCGTACGTGGCCCTCGATGTGCTCTGCGTGTTGCTGGCT
GGATTGCCTTTTGCAATTCTTACTTCAAGGCATACCCCCTTCCAACGAGGAGTATTCTGT
AATGATGAGTCCATCAAGTACCCTTACAAAGAAGACACCATACCTTATGCGTTATTAGGT
GGAATAATCATTCCATTCAGTATTATCGTTATTATTCTTGGAGAAACCCTGTCTGTTTAC
TGTAACCTTTTGCACTCAAATTCCTTTATCAGGAATAACTACATAGCCACTATTTACAAA
GCCATTGGAACCTTTTTATTTGGTGCAGCTGCTAGTCAGTCCCTGACTGACATTGCCAAG
TATTCAATAGGCAGACTGCGGCCTCACTTCTTGGATGTTTGTGATCCAGATTGGTCAAAA
ATCAACTGCAGCGATGGTTACATTGAATACTACATATGTCGAGGGAATGCAGAAAGAGTT
AAGGAAGGCAGGTTGTCCTTCTATTCAGGCCACTCTTCGTTTTCCATGTACTGCATGCTG
TTTGTGGCACTTTATCTTCAAGCCAGGATGAAGGGAGACTGGGCAAGACTCTTACGCCCC
ACACTGCAATTTGGTCTTGTTGCCGTATCCATTTATGTGGGCCTTTCTCGAGTTTCTGAT
TATAAACACCACTGGAGCGATGTGTTGACTGGACTCATTCAGGGAGCTCTGGTTGCAATA
TTAGTTGCTGTATATGTATCGGATTTCTTCAAAGAAAGAACTTCTTTTAAAGAAAGAAAA
GAGGAGGACTCTCATACAACTCTGCATGAAACACCAACAACTGGGAATCACTATCCGAGC
AATCACCAGCCTTGA
Enzyme 6 GenBank Gene ID AB000888 Link Image
Enzyme 6 GeneCard ID PPAP2A Link Image
Enzyme 6 GenAtlas ID PPAP2A Link Image
Enzyme 6 HGNC ID HGNC:9228 Link Image
Enzyme 6 Chromosome Location 5
Enzyme 6 Locus 5q11
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Kai M, Wada I, Imai S, Sakane F, Kanoh H: Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. J Biol Chem. 1997 Sep 26;272(39):24572-8. [PubMed Link Image]
  2. Leung DW, Tompkins CK, White T: Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. DNA Cell Biol. 1998 Apr;17(4):377-85. [PubMed Link Image]
  3. Ulrix W, Swinnen JV, Heyns W, Verhoeven G: Identification of the phosphatidic acid phosphatase type 2a isozyme as an androgen-regulated gene in the human prostatic adenocarcinoma cell line LNCaP. J Biol Chem. 1998 Feb 20;273(8):4660-5. [PubMed Link Image]
  4. Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5472
Enzyme 7 Name Diacylglycerol kinase iota
Enzyme 7 Synonyms
  1. Diglyceride kinase iota
  2. DGK-iota
  3. DAG kinase iota
Enzyme 7 Gene Name DGKI
Enzyme 7 Protein Sequence >Diacylglycerol kinase iota 
MDAAGRGCHLLPLPAARGPARAPAAAAAAAASPPGPCSGAACAPSAAAGAGAMNPSSSAG
EEKGATGGSSSSGSGAGSCCLGAEGGADPRGAGSAAAAGAAALDEPAAAGQKEKDEALEE
KLRNLTFRKQVSYRKAISRAGLQHLAPAHPLSLPVANGPAKEPRATLDWSENAVNGEHLW
LETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG
SRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCF
MLHHIEEPCSLGAHAAVIVPPTWIIKVKKPQNSLKASNRKKKRTSFKRKASKRGMEQENK
GRPFVIKPISSPLMKPLLVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEL
YRKVPNLRILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLARTLNWGGGYTDE
PVSKILCQVEDGTVVQLDRWNLHVERNPDLPPEELEDGVCKLPLNVFNNYFSLGFDAHVT
LEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIQEL
KFQCIVFLNIPRYCAGTMPWGNPGDHHDFEPQRHDDGYIEVIGFTMASLAALQVGGHGER
LHQCREVMLLTYKSIPMQVDGEPCRLAPAMIRISLRNQANMVQKSKRRTSMPLLNDPQSV
PDRLRIRVNKISLQDYEGFHYDKEKLREASISDWLRTIAGELVQSFGAIPLGILVVRGDC
DLETCRMYIDRLQEDLQSVSSGSQRVHYQDHETSFPRALSAQRLSPRWCFLDDRSQEHLH
FVMEISQDEIFILDPDMVVSQPAGTPPGMPDLVVEQASGISDWWNPALRKRMLSDSGLGM
IAPYYEDSDLKDLSHSRVLQSPVSSEDHAILQAVIAGDLMKLIESYKNGGSLLIQGPDHC
SLLHYAAKTGNGEIVKYILDHGPSELLDMADSETGETALHKAACQRNRAVCQLLVDAGAS
LRKTDSKGKTPQERAQQAGDPDLAAYLESRQNYKVIGHEDLETAV
Enzyme 7 Number of Residues 1065
Enzyme 7 Molecular Weight 116998
Enzyme 7 Theoretical pI 7.81
Enzyme 7 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl- sn-glycerol 3-phosphate
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 3676530 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID O75912 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name DGKI_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >3198 bp 
ATGGATGCTGCGGGAAGGGGCTGCCATTTGCTGCCCCTGCCAGCGGCGCGCGGACCTGCC
CGCGCTCCTGCAGCCGCCGCCGCCGCCGCCGCCAGCCCGCCCGGCCCCTGCAGCGGCGCC
GCCTGCGCTCCCTCCGCGGCCGCCGGAGCGGGCGCCATGAACCCCAGCTCCTCGGCGGGA
GAGGAGAAAGGGGCGACGGGCGGCAGCAGCAGCAGCGGAAGCGGCGCCGGGAGCTGCTGC
CTGGGCGCCGAGGGCGGCGCGGACCCGCGGGGCGCAGGGTCAGCCGCGGCGGCGGGGGCC
GCTGCCCTGGACGAGCCCGCGGCCGCCGGCCAGAAGGAGAAGGACGAAGCGCTGGAGGAG
AAGCTGAGGAACTTAACTTTCCGGAAGCAGGTCTCGTACAGGAAAGCAATCTCCCGGGCA
GGCCTCCAGCATCTGGCTCCTGCACATCCCCTCAGCCTTCCTGTGGCAAATGGTCCAGCC
AAGGAGCCCAGAGCGACTTTGGACTGGAGTGAGAATGCCGTGAATGGAGAACACCTGTGG
CTGGAGACCAACGTCTCGGGAGACCTCTGCTACCTTGGAGAGGAGAACTGCCAAGTCAGA
TTTGCAAAATCAGCTCTCAGGAGGAAGTGTGCAGTCTGTAAAATCGTCGTCCACACCGCC
TGCATTGAGCAGCTAGAAAAGATTAATTTCAGATGTAAACCAACATTTCGAGAAGGAGGC
TCAAGGTCACCAAGAGAAAATTTTGTACGTCATCACTGGGTGCACAGGCGTCGGCAGGAG
GGGAAATGTAAGCAGTGTGGTAAGGGCTTCCAGCAAAAGTTCTCCTTCCACAGTAAAGAG
ATTGTGGCTATCAGCTGTTCCTGGTGCAAGCAGGCGTTTCACAATAAGGTGACCTGCTTC
ATGCTGCATCACATTGAAGAACCCTGCTCCCTGGGGGCTCATGCTGCTGTTATTGTCCCG
CCCACTTGGATCATTAAGGTGAAGAAACCTCAGAACTCCCTGAAGGCTTCAAATCGGAAG
AAGAAGAGAACAAGCTTTAAAAGAAAAGCCAGTAAAAGAGGGATGGAACAGGAAAACAAA
GGTCGTCCTTTTGTGATAAAACCCATCTCTTCTCCTCTCATGAAACCCTTGCTTGTATTT
GTGAATCCCAAGAGTGGAGGCAACCAGGGAACCAAAGTCCTGCAGATGTTCATGTGGTAC
CTGAATCCACGGCAAGTCTTTGATCTTTCTCAGGAAGGGCCAAAAGATGCGCTTGAATTG
TATAGGAAAGTACCAAATCTGCGAATTCTGGCCTGTGGTGGGGATGGAACGGTGGGCTGG
ATCCTTTCCATCCTGGATGAACTGCAGCTGAGCCCTCAGCCTCCTGTGGGGGTCCTTCCT
CTGGGGACTGGGAATGACCTGGCTCGAACTCTCAACTGGGGAGGGGGCTACACTGATGAA
CCTGTTTCTAAGATCCTGTGTCAAGTGGAAGATGGGACAGTTGTACAGCTAGATCGCTGG
AACCTCCATGTGGAAAGAAACCCCGACTTGCCTCCAGAAGAACTTGAAGATGGCGTATGT
AAGCTCCCTCTGAATGTTTTCAATAACTACTTCAGCCTTGGATTTGATGCCCATGTCACA
CTGGAGTTCCATGAATCCAGAGAAGCAAATCCAGAGAAATTCAACAGTCGTTTTCGAAAT
AAAATGTTCTATGCAGGGGCAGCTTTTTCTGACTTCCTACAGAGAAGTTCTAGAGATCTA
TCCAAACATGTTAAAGTTGTTTGTGATGGAACAGATCTCACCCCAAAGATTCAGGAACTG
AAGTTCCAGTGTATAGTATTTTTAAATATACCCAGATATTGTGCTGGCACAATGCCCTGG
GGAAACCCAGGTGATCACCATGATTTCGAACCTCAGCGTCATGATGATGGTTATATTGAA
GTCATTGGATTTACCATGGCCTCTTTGGCAGCCCTGCAAGTTGGGGGCCATGGAGAGAGG
CTACACCAGTGTCGAGAAGTCATGCTTCTAACTTACAAATCCATCCCCATGCAAGTGGAT
GGGGAGCCCTGTAGGTTGGCCCCAGCTATGATTCGGATCTCCCTGAGGAATCAGGCCAAC
ATGGTACAGAAGAGCAAGAGGAGAACATCCATGCCTTTACTCAATGATCCCCAGTCTGTC
CCAGATCGTCTGAGGATCCGGGTGAACAAAATCAGTTTACAAGACTATGAAGGATTCCAC
TATGACAAGGAGAAACTCCGAGAAGCTTCTATTTCAGACTGGTTAAGAACCATTGCTGGG
GAACTAGTGCAGTCATTTGGAGCGATACCTCTGGGTATTCTAGTTGTGCGTGGAGACTGT
GATTTGGAGACTTGCCGTATGTACATAGACCGCCTACAGGAGGACCTACAGTCAGTTTCT
TCTGGCTCCCAGAGAGTTCATTACCAGGACCATGAAACCTCCTTCCCCAGGGCTCTCTCA
GCACAGAGGCTCTCTCCTCGGTGGTGCTTCCTAGATGACAGATCTCAGGAACATTTGCAC
TTTGTGATGGAGATTTCCCAAGATGAGATTTTTATTCTGGACCCAGATATGGTGGTGTCA
CAGCCGGCGGGGACACCTCCGGGCATGCCTGACCTGGTGGTGGAACAAGCCTCGGGGATC
TCAGACTGGTGGAATCCTGCCCTGCGGAAACGCATGCTGAGTGACAGTGGGCTGGGGATG
ATAGCTCCCTATTATGAGGACTCAGATCTGAAAGATCTCAGCCACTCCCGCGTGCTACAG
TCACCAGTCTCTTCAGAAGATCATGCAATTTTGCAGGCAGTAATAGCTGGTGATCTTATG
AAGCTAATAGAAAGCTATAAAAATGGAGGCAGTCTGCTAATTCAGGGACCAGACCACTGT
TCACTCCTTCACTACGCAGCTAAAACCGGCAACGGGGAGATTGTGAAATATATCCTTGAC
CACGGACCTTCCGAGTTATTGGATATGGCAGACAGTGAAACGGGTGAGACTGCACTGCAC
AAGGCTGCCTGCCAGCGGAACCGGGCTGTGTGCCAGCTTCTGGTGGATGCAGGAGCATCT
CTGAGAAAGACGGACTCCAAGGGTAAGACACCTCAAGAAAGAGCACAGCAGGCTGGGGAC
CCAGACTTGGCTGCTTACCTAGAAAGCCGTCAGAACTATAAGGTCATTGGCCATGAGGAC
CTGGAAACTGCTGTTTGA
Enzyme 7 GenBank Gene ID AF061936 Link Image
Enzyme 7 GeneCard ID DGKI Link Image
Enzyme 7 GenAtlas ID DGKI Link Image
Enzyme 7 HGNC ID HGNC:2855 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Ding L, Traer E, McIntyre TM, Zimmerman GA, Prescott SM: The cloning and characterization of a novel human diacylglycerol kinase, DGKiota. J Biol Chem. 1998 Dec 4;273(49):32746-52. [PubMed Link Image]
  2. Bowne SJ, Sullivan LS, Ding L, Traer E, Prescott SM, Birch DG, Kennan A, Humphries P, Daiger SP: Evaluation of human diacylglycerol kinase(iota), DGKI, a homolog of Drosophila rdgA, in inherited retinopathy mapping to 7q. Mol Vis. 2000 Feb 22;6:6-9. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5474
Enzyme 8 Name Lipid phosphate phosphohydrolase 3
Enzyme 8 Synonyms
  1. Phosphatidic acid phosphatase 2b
  2. Phosphatidate phosphohydrolase type 2b
  3. PAP2b
  4. PAP- 2b
  5. PAP2-beta
  6. Vascular endothelial growth factor and type I collagen-inducible protein
  7. VCIP
Enzyme 8 Gene Name PPAP2B
Enzyme 8 Protein Sequence >Lipid phosphate phosphohydrolase 3 
MQNYKYDKAIVPESKNGGSPALNNNPRRSGSKRVLLICLDLFCLFMAGLPFLIIETSTIK
PYHRGFYCNDESIKYPLKTGETINDAVLCAVGIVIAILAIITGEFYRIYYLKKSRSTIQN
PYVAALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLSVCNPDFSQINCSEGYIQNYR
CRGDDSKVQEARKSFFSGHASFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFY
TGLSRVSDHKHHPSDVLAGFAQGALVACCIVFFVSDLFKTKTTLSLPAPAIRKEILSPVD
IIDRNNHHNMM
Enzyme 8 Number of Residues 311
Enzyme 8 Molecular Weight 35116
Enzyme 8 Theoretical pI 9.40
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Lipid transport and metabolism
Enzyme 8 Specific Function Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1- phosphate (S-1-P). The relative catalytic efficiency is LPA = PA > C-1-P > S-1-P. May be involved in cell adhesion and in cell-cell interactions
Enzyme 8 Pathways
Enzyme 8 Reactions
  • A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 34-54 86-106 123-143 194-214 228-248 258-278
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 2467300 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O14495 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name LPP3_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >936 bp 
ATGCAAAACTACAAGTACGACAAAGCGATCGTCCCGGAGAGCAAGAACGGCGGCAGCCCG
GCGCTCAACAACAACCCGAGGAGGAGCGGCAGCAAGCGGGTGCTGCTCATCTGCCTCGAC
CTCTTCTGCCTCTTCATGGCGGGCCTCCCCTTCCTCATCATCGAGACAAGCACCATCAAG
CCTTACCACCGAGGGTTTTACTGCAATGATGAGAGCATCAAGTACCCACTGAAAACTGGT
GAGACAATAAATGACGCTGTGCTCTGTGCCGTGGGGATCGTCATTGCCATCCTCGCGATC
ATCACGGGGGAATTCTACCGGATCTATTACCTGAAGAAGTCGCGGTCGACGATTCAGAAC
CCCTACGTGGCAGCACTCTATAAGCAAGTGGGCTGCTTCCTCTTTGGCTGTGCCATCAGC
CAGTCTTTCACAGACATTGCCAAAGTGTCCATAGGGCGCCTGCGTCCTCACTTCTTGAGT
GTCTGCAACCCTGATTTCAGCCAGATCAACTGCTCTGAAGGCTACATTCAGAACTACAGA
TGCAGAGGTGATGACAGCAAAGTCCAGGAAGCCAGGAAGTCCTTCTTCTCTGGCCATGCC
TCCTTCTCCATGTACACTATGCTGTATTTGGTGCTATACCTGCAGGCCCGCTTCACTTGG
CGAGGAGCCCGCCTGCTCCGGCCCCTCCTGCAGTTCACCTTGATCATGATGGCCTTCTAC
ACGGGACTGTCTCGCGTATCAGACCACAAGCACCATCCCAGTGATGTTCTGGCAGGATTT
GCTCAAGGAGCCCTGGTGGCCTGCTGCATAGTTTTCTTCGTGTCTGACCTCTTCAAGACT
AAGACGACGCTCTCCCTGCCTGCCCCTGCTATCCGGAAGGAAATCCTTTCACCTGTGGAC
ATTATTGACAGGAACAATCACCACAACATGATGTAG
Enzyme 8 GenBank Gene ID AB000889 Link Image
Enzyme 8 GeneCard ID PPAP2B Link Image
Enzyme 8 GenAtlas ID PPAP2B Link Image
Enzyme 8 HGNC ID HGNC:9229 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1pter-p22.1
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Kai M, Wada I, Imai S, Sakane F, Kanoh H: Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. J Biol Chem. 1997 Sep 26;272(39):24572-8. [PubMed Link Image]
  2. Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed Link Image]
  3. Humtsoe JO, Feng S, Thakker GD, Yang J, Hong J, Wary KK: Regulation of cell-cell interactions by phosphatidic acid phosphatase 2b/VCIP. EMBO J. 2003 Apr 1;22(7):1539-54. [PubMed Link Image]
  4. Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5478
Enzyme 9 Name Diacylglycerol kinase zeta
Enzyme 9 Synonyms
  1. Diglyceride kinase zeta
  2. DGK-zeta
  3. DAG kinase zeta
Enzyme 9 Gene Name DGKZ
Enzyme 9 Protein Sequence >Diacylglycerol kinase zeta 
METFFRRHFRGKVPGPGEGQRRPSSVGLPTGKARRRSPAGQASSSLAQRRRSSAQLQGCL
LSCGVRAQGSSRRRSSTVPPSCNPRFIVDKVLTPQPTTVGAQLLGAPLLLTGLVGMNEEE
GVQEDVVAEASSAIQPGTKTPGPPPPRGAQPLLPLPRYVRRASSHCCPADAVYDHALWGL
HGYYRRLSQRRPSGQHPGPGGRRASGTTAGTMLPTRVRPLSRRRQVALRRKAAGPQAWSA
LLAKAITKSGLQHLAPPPPTPGAPCSESERQIRSTVDWSESATYGEHIWFETNVSGDFCY
VGEQYCVARMLKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESGSRNVREPTFVR
HHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCS
LGVHAAVVIPPTWILRARRPQNTLKASKKKKRASFKRKSSKKGPEEGRWRPFIIRPTPSP
LMKPLLVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHNLRILAC
GGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEG
NVVQLDRWDLHAEPNPEAGPEDRDEGATDRLPLDVFNNYFSLGFDAHVTLEFHESREANP
EKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIQDLKPQCVVFLNIP
RYCAGTMPWGHPGEHHDFEPQRHDDGYLEVIGFTMTSLAALQVGGHGERLTQCREVVLTT
SKAIPVQVDGEPCKLAASRIRIALRNQATMVQKAKRRSAAPLHSDQQPVPEQLRIQVSRV
SMHDYEALHYDKEQLKEASVPLGTVVVPGDSDLELCRAHIERLQQEPDGAGAKSPTCQKL
SPKWCFLDATTASRFYRIDRAQEHLNYVTEIAQDEIYILDPELLGASARPDLPTPTSPLP
TSPCSPTPRSLQGDAAPPQGEELIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAV
STGSKDVVRYLLDHAPPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQG
DTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETAV
Enzyme 9 Number of Residues 1117
Enzyme 9 Molecular Weight 124124
Enzyme 9 Theoretical pI 9.27
Enzyme 9 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols
Enzyme 9 Pathways
Enzyme 9 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 1293079 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q13574 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name DGKZ_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >2787 bp 
ATGGAGCCGCGGGACGGTAGCCCCGAGGCCCGGAGCAGCGACTCCGAGTCGGCTTCCGCC
TCGTCCAGCGGCTCCGAGCGCGACGCCGGTCCCGAGCCGGACAAGGCGCCGCGGCGACTC
AACAAGCGGCGCTTCCCGGGGCTGCGGCTCTTCGGGCACAGGAAAGCCATCACCAAGTCG
GGCCTCCAGCACCTGGCCCCCCCTCCGCCCACCCCTGGGGCCCCGTGCAGCGAGTCAGAG
CGGCAGATCCGGAGTACAGTGGACTGGAGCGAGTCAGCGACATATGGGGAGCACATCTGG
TTCGAGACCAACGTGTCCGGGGACTTCTGCTACGTTGGGGAGCAGTACTGTGTAGCCAGG
ATGCTGAAGTCAGTGTCTCGAAGAAAGTGCGCAGCCTGCAAGATTGTGGTGCACACGCCC
TGCATCGAGCAGCTGGAGAAGATAAATTTCCGCTGTAAGCCGTCCTTCCGTGAATCAGGC
TCCAGGAATGTCCGCGAGCCAACCTTTGTACGGCACCACTGGGTACACAGACGACGCCAG
GACGGCAAGTGTCGGCACTGTGGGAAGGGATTCCAGCAGAAGTTCACCTTCCACAGCAAG
GAGATTGTGGCCATCAGCTGCTCGTGGTGCAAGCAGGCATACCACAGCAAGGTGTCCTGC
TTCATGCTGCAGCAGATCGAGGAGCCGTGCTCGCTGGGGGTCCACGCAGCCGTGGTCATC
CCGCCCACCTGGATCCTCCGCGCCCGGAGGCCCCAGAATACTCTGAAAGCAAGCAAGAAG
AAGAAGAGGGCATCCTTCAAGAGGAAGTCCAGCAAGAAAGGGCCTGAGGAGGGCCGCTGG
AGACCCTTCATCATCAGGCCCACCCCCTCCCCGCTCATGAAGCCCCTGCTGGTGTTTGTG
AACCCCAAGAGTGGGGGCAACCAGGGTGCAAAGATCATCCAGTCTTTCCTCTGGTATCTC
AATCCCCGACAAGTCTTCGACCTGAGCCAGGGAGGGCCCAAGGAGGCGCTGGAGATGTAC
CGCAAAGTGCACAACCTGCGGATCCTGGCGTGCGGGGGCGACGGCACGGTGGGCTGGATC
CTCTCCACCCTGGACCAGCTACGCCTGAAGCCGCCACCCCCTGTTGCCATCCTGCCCCTG
GGTACTGGCAACGACTTGGCCCGAACCCTCAACTGGGGTGGGGGCTACACAGATGAGCCT
GTGTCCAAGATCCTCTCCCACGTGGAGGAGGGGAACGTGGTACAGCTGGACCGCTGGGAC
CTCCACGCTGAGCCCAACCCCGAGGCAGGGCCTGAGGACCGAGATGAAGGCGCCACCGAC
CGGTTGCCCCTGGATGTCTTCAACAACTACTTCAGCCTGGGCTTTGACGCCCACGTCACC
CTGGAGTTCCACGAGTCTCGAGAGGCCAACCCAGAGAAATTCAACAGCCGCTTTCGGAAT
AAGATGTTCTACGCCGGGACAGCTTTCTCTGACTTCCTGATGGGCAGCTCCAAGGACCTG
GCCAAGCACATCCGAGTGGTGTGTGATGGAATGGACTTGACTCCCAAGATCCAGGACCTG
AAACCCCAGTGTGTTGTTTTCCTGAACATCCCCAGGTACTGTGCGGGCACCATGCCCTGG
GGCCACCCTGGGGAGCACCACGACTTTGAGCCCCAGCGGCATGACGACGGCTACCTCGAG
GTCATTGGCTTCACCATGACGTCGTTGGCCGCGCTGCAGGTGGGCGGACACGGCGAGCGG
CTGACGCAGTGTCGCGAGGTGGTGCTCACCACATCCAAGGCCATCCCGGTGCAGGTGGAT
GGCGAGCCCTGCAAGCTTGCAGCCTCACGCATCCGCATCGCCCTGCGCAACCAGGCCACC
ATGGTGCAGAAGGCCAAGCGGCGGAGCGCCGCCCCCCTGCACAGCGACCAGCAGCCGGTG
CCAGAGCAGTTGCGCATCCAGGTGAGTCGCGTCAGCATGCACGACTATGAGGCCCTGCAC
TACGACAAGGAGCAGCTCAAGGAGGCCTCTGTGCCGCTGGGCACTGTGGTGGTCCCAGGA
GACAGTGACCTAGAGCTCTGCCGTGCCCACATTGAGAGACTCCAGCAGGAGCCCGATGGT
GCTGGAGCCAAGTCCCCGACATGCCAGAAACTGTCCCCCAAGTGGTGCTTCCTGGACGCC
ACCACTGCCAGCCGCTTCTACAGGATCGACCGAGCCCAGGAGCACCTCAACTATGTGACT
GAGATCGCACAGGATGAGATTTATATCCTGGACCCTGAGCTGCTGGGGGCATCGGCCCGG
CCTGACCTCCCAACCCCCACTTCCCCTCTCCCCACCTCACCCTGCTCACCCACGCCCCGG
TCACTGCAAGGGGATGCTGCACCCCCTCAAGGTGAAGAGCTGATTGAGGCTGCCAAGAGG
AACGACTTCTGTAAGCTCCAGGAGCTGCACCGAGCTGGGGGCGACCTCATGCACCGAGAC
GAGCAGAGTCGCACGCTCCTGCACCACGCAGTCAGCACTGGCAGCAAGGATGTGGTCCGC
TACCTGCTGGACCACGCCCCCCCAGAGATCCTTGATGCGGTGGAGGAAAACGGGGAGACC
TGTTTGCACCAAGCAGCGGCCCTGGGCCAGCGCACCATCTGCCACTACATCGTGGAGGCC
GGGGCCTCGCTCATGAAGACAGACCAGCAGGGCGACACTCCCCGGCAGCGGGCTGAGAAG
GCTCAGGACACCGAGCTGGCCGCCTACCTGGAGAACCGGCAGCACTACCAGATGATCCAG
CGGGAGGACCAGGAGACGGCTGTGTAG
Enzyme 9 GenBank Gene ID U51477 Link Image
Enzyme 9 GeneCard ID DGKZ Link Image
Enzyme 9 GenAtlas ID DGKZ Link Image
Enzyme 9 HGNC ID HGNC:2857 Link Image
Enzyme 9 Chromosome Location 11
Enzyme 9 Locus 11p11.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Bunting M, Tang W, Zimmerman GA, McIntyre TM, Prescott SM: Molecular cloning and characterization of a novel human diacylglycerol kinase zeta. J Biol Chem. 1996 Apr 26;271(17):10230-6. [PubMed Link Image]
  2. Ding L, Bunting M, Topham MK, McIntyre TM, Zimmerman GA, Prescott SM: Alternative splicing of the human diacylglycerol kinase zeta gene in muscle. Proc Natl Acad Sci U S A. 1997 May 27;94(11):5519-24. [PubMed Link Image]
  3. Topham MK, Bunting M, Zimmerman GA, McIntyre TM, Blackshear PJ, Prescott SM: Protein kinase C regulates the nuclear localization of diacylglycerol kinase-zeta. Nature. 1998 Aug 13;394(6694):697-700. [PubMed Link Image]
  4. Hogan A, Shepherd L, Chabot J, Quenneville S, Prescott SM, Topham MK, Gee SH: Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta. Regulation of nuclear localization by PDZ interactions. J Biol Chem. 2001 Jul 13;276(28):26526-33. Epub 2001 May 14. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6421
Enzyme 10 Name Acyl-CoA:lysophosphatidylglycerol acyltransferase 1
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name LPGAT1
Enzyme 10 Protein Sequence >Acyl-CoA:lysophosphatidylglycerol acyltransferase 1 
MAITLEEAPWLGWLLVKALMRFAFMVVNNLVAIPSYICYVIILQPLRVLDSKRFWYIEGI
MYKWLLGMVASWGWYAGYTVMEWGEDIKAVSKDEAVMLVNHQATGDVCTLMMCLQDKGLV
VAQMMWLMDHIFKYTNFGIVSLVHGDFFIRQGRSYRDQQLLLLKKHLENNYRSRDRKWIV
LFPEGGFLRKRRETSQAFAKKNNLPFLTNVTLPRSGATKIILNALVAQQKNGSPAGGDAK
ELDSKSKGLQWIIDTTIAYPKAEPIDIQTWILGYRKPTVTHVHYRIFPIKDVPLETDDLT
TWLYQRFVEKEDLLSHFYETGAFPPSKGHKEAVSREMTLSNLWIFLIQSFAFLSGYMWYN
IIQYFYHCLF
Enzyme 10 Number of Residues 370
Enzyme 10 Molecular Weight 43090
Enzyme 10 Theoretical pI 9.24
Enzyme 10 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 10 General Function Lipid transport and metabolism
Enzyme 10 Specific Function Lysophoshatidylglycerol (LPG) specific acyltransferase that recognizes various acyl-CoAs and LPGs as substrates but demonstrates a clear preference for long chain saturated fatty acyl-CoAs and oleoyl-CoA as acyl donors. Prefers oleoyl-LPG over palmitoyl-LPG as an acyl receptor and oleoyl-CoA over lauroyl-CoA as an acyl donor
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function Not Available
Enzyme 10 Signals
  • 1-32
Enzyme 10 Transmembrane Regions Not Available
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 40788908 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q92604 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name LGAT1_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1176 bp 
CTCCCAAAGCCCCGGCTGGGGCCCGGCCAGCCCGAGAAAGACAGGACGGAGTCCAGTGTG
AGAATGGCTATAACTTTGGAAGAAGCTCCGTGGCTGGGCTGGCTCTTGGTGAAAGCACTG
ATGAGGTTTGCCTTCATGGTCGTCAACAACCTGGTTGCTATTCCATCCTACATCTGCTAT
GTAATTATACTTCAGCCCCTTCGAGTGCTGGACAGTAAGCGGTTCTGGTATATCGAAGGA
ATCATGTATAAATGGCTTTTAGGAATGGTAGCTTCCTGGGGATGGTATGCTGGATATACA
GTGATGGAATGGGGAGAAGATATTAAAGCAGTTTCAAAAGATGAAGCAGTGATGTTGGTG
AATCATCAGGCAACAGGAGATGTGTGCACACTGATGATGTGCCTCCAGGACAAAGGACTG
GTTGTTGCTCAGATGATGTGGTTGATGGATCATATTTTTAAGTACACAAACTTTGGAATT
GTTTCTCTAGTTCATGGAGACTTCTTTATAAGACAGGGAAGATCTTATCGTGACCAACAG
CTGCTGCTTCTCAAGAAGCACTTAGAAAATAATTACAGGAGCAGAGATCGAAAATGGATT
GTTTTGTTTCCAGAAGGGGGCTTCCTCAGGAAGAGGCGAGAAACAAGTCAGGCATTTGCC
AAGAAAAATAACTTGCCATTTCTTACAAATGTTACTCTGCCAAGGTCTGGGGCAACAAAA
ATTATTTTGAATGCACTTGTAGCACAACAGAAAAATGGAAGTCCAGCAGGAGGAGATGCT
AAAGAATTAGACAGCAAATCAAAAGGCCTCCAGTGGATAATAGATACAACGATAGCTTAT
CCCAAAGCTGAACCTATAGATATTCAAACCTGGATCCTTGGATACAGGAAACCAACAGTC
ACACATGTACATTACAGGATCTTTCCAATTAAAGATGTACCCCTGGAGACTGATGACCTT
ACCACTTGGCTCTATCAGCGGTTTGTTGAAAAAGAAGACCTCTTATCACATTTTTATGAA
ACAGGAGCTTTTCCACCTTCCAAGGGCCATAAGGAAGCTGTTTCCAGGGAGATGACCCTC
AGCAACTTGTGGATATTTCTCATACAGTCTTTTGCATTTTTGTCAGGCTATATGTGGTAC
AACATCATTCAGTATTTTTACCATTGCCTGTTTTAG
Enzyme 10 GenBank Gene ID D86960 Link Image
Enzyme 10 GeneCard ID LPGAT1 Link Image
Enzyme 10 GenAtlas ID LPGAT1 Link Image
Enzyme 10 HGNC ID HGNC:28985 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 1p36.13-q42.3
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Nagase T, Seki N, Ishikawa K, Ohira M, Kawarabayasi Y, Ohara O, Tanaka A, Kotani H, Miyajima N, Nomura N: Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. DNA Res. 1996 Oct 31;3(5):321-9, 341-54. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6577
Enzyme 11 Name Focal adhesion kinase 1
Enzyme 11 Synonyms
  1. FADK 1
  2. pp125FAK
  3. Protein- tyrosine kinase 2
Enzyme 11 Gene Name PTK2
Enzyme 11 Protein Sequence >Focal adhesion kinase 1 
MAAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGD
ATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEW
KYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSY
WEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESI
LKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQ
TIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFII
RPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRE
RIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDH
PHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESK
RFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFT
SASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWA
YDPSRRPRFTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGY
PSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGITAMAGSIYPGQASLLDQTDSWNHRPQE
IAMWQPNVEDSTVLDLRGIGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLS
RGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNE
GVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLA
LRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQM
LTAAHALAVDAKNLLDVIDQARLKMLGQTRPH
Enzyme 11 Number of Residues 1052
Enzyme 11 Molecular Weight 119234
Enzyme 11 Theoretical pI 6.61
Enzyme 11 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • protein kinase activity
  • protein-tyrosine kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid phosphorylation
  • protein modification
Component
  • cytoskeleton
  • intracellular non-membrane-bound organelle
  • non-membrane-bound organelle
  • organelle
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Plays a potential role in oncogenic transformations resulting in increased kinase activity
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 439875 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q05397 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name FAK1_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >3159 bp 
ATGGCAGCTGCTTACCTTGACCCCAACTTGAATCACACACCAAATTCGAGTACTAAGACT
CACCTGGGTACTGGTATGGAACGTTCTCCTGGTGCAATGGAGCGAGTATTAAAGGTCTTT
CATTATTTTGAAAGCAATAGTGAGCCAACCACCTGGGCCAGTATTATCAGGCATGGAGAT
GCTACTGATGTCAGGGGCATCATTCAGAAGATAGTGGACAGTCACAAAGTAAAGCATGTG
GCCTGCTATGGATTCCGCCTCAGTCACCTGCGGTCAGAGGAGGTTCACTGGCTTCACGTG
GATATGGGCGTCTCCAGTGTGAGGGAGAAGTATGAGCTTGCTCACCCACCAGAGGAGTGG
AAATATGAATTGAGAATTCGTTATTTGCCAAAAGGATTTCTAAACCAGTTTACTGAAGAT
AAGCCAACTTTGAATTTCTTCTATCAACAGGTGAAGAGCGATTATATGTTAGAGATAGCT
GATCAAGTGGACCAGGAAATTGCTTTGAAGTTGGGTTGTCTAGAAATACGGCGATCATAC
TGGGAGATGCGGGGCAATGCACTAGAAAAGAAGTCTAACTATGAAGTATTAGAAAAAGAT
GTTGGTTTAAAGCGATTTTTTCCTAAGAGTTTACTGGATTCTGTCAAGGCCAAAACACTA
AGAAAACTGATCCAACAAACATTTAGACAATTTGCCAACCTTAATAGAGAAGAAAGTATT
CTGAAATTCTTTGAGATCCTGTCTCCAGTCTACAGATTTGATAAGGAATGCTTCAAGTGT
GCTCTTGGTTCAAGCTGGATTATTTCAGTGGAACTGGCAATCGGCCCAGAAGAAGGAATC
AGTTACCTAACGGACAAGGGCTGCAATCCCACACATCTTGCTGACTTCACTCAAGTGCAA
ACCATTCAGTATTCAAACAGTGAAGACAAGGACAGAAAAGGAATGCTACAACTAAAAATA
GCAGGTGCACCCGAGCCTCTGACAGTGACGGCACCATCCCTAACCATTGCGGAGAATATG
GCTGACCTAATAGATGGGTACTGCCGGCTGGTGAATGGAACCTCGCAGTCATTTATCATC
AGACCTCAGAAAGAAGGTGAACGGGCTTTGCCATCAATACCAAAGTTGGCCAACAGCGAA
AAGCAAGGCATGCGGACACACGCCGTCTCTGTGTCAGAAACAGATGATTATGCTGAGATT
ATAGATGAAGAAGATACTTACACCATGCCCTCAACCAGGGATTATGAGATTCAAAGAGAA
AGAATAGAACTTGGACGATGTATTGGAGAAGGCCAATTTGGAGATGTACATCAAGGCATT
TATATGAGTCCAGAGAATCCAGCTTTGGCGGTTGCAATTAAAACATGTAAAAACTGTACT
TCGGACAGCGTGAGAGAGAAATTTCTTCAAGAAGCCTTAACAATGCGTCAGTTTGACCAT
CCTCATATTGTGAAGCTGATTGGAGTCATCACAGAGAATCCTGTCTGGATAATCATGGAG
CTGTGCACACTTGGAGAGCTGAGGTCATTTTTGCAAGTAAGGAAATACAGTTTGGATCTA
GCATCTTTGATCCTGTATGCCTATCAGCTTAGTACAGCTCTTGCATATCTAGAGAGCAAA
AGATTTGTACACAGGGACATTGCTGCTCGGAATGTTCTGGTGTCCTCAAATGATTGTGTA
AAATTAGGAGACTTTGGATTATCCCGATATATGGAAGATAGTACTTACTACAAAGCTTCC
AAAGGAAAATTGCCTATTAAATGGATGGCTCCAGAGTCAATCAATTTTCGACGTTTTACC
TCAGCTAGTGACGTATGGATGTTTGGTGTGTGTATGTGGGAGATACTGATGCATGGTGTG
AAGCCTTTTCAAGGAGTGAAGAACAATGATGTAATCGGTCGAATTGAAAATGGGGAAAGA
TTACCAATGCCTCCAAATTGTCCTCCTACCCTCTACAGCCTTATGACGAAATGCTGGGCC
TATGACCCCAGCAGGCGGCCCAGGTTTACTGAACTTAAAGCTCAGCTCAGCACAATCCTG
GAGGAAGAGAAGGCTCAGCAAGAAGAGCGCATGAGGATGGAGTCCAGAAGACAGGCCACA
GTGTCCTGGGACTCCGGAGGGTCTGATGAAGCACCGCCCAAGCCCAGCAGACCGGGTTAT
CCCAGTCCGAGGTCCAGCGAAGGATTTTATCCCAGCCCACAGCACATGGTACAAACCAAT
CATTACCAGGTTTCTGGCTACCCTGGTTCACATGGAATCACAGCCATGGCTGGCAGCATC
TATCCAGGTCAGGCATCTCTTTTGGACCAAACAGATTCATGGAATCATAGACCTCAGGAG
ATAGCAATGTGGCAGCCCAATGTGGAGGACTCTACAGTATTGGACCTGCGAGGGATTGGG
CAAGTGTTGCCAACCCATCTGATGGAAGAGCGTCTAATCCGACAGCAACAGGAAATGGAA
GAAGATCAGCGCTGGCTGGAAAAAGAGGAAAGATTTCTGAAACCTGATGTGAGACTCTCT
CGAGGCAGTATTGACAGGGAGGATGGAAGTCTTCAGGGTCCGATTGGAAACCAACATATA
TATCAGCCTGTGGGTAAACCAGATCCTGCAGCTCCACCAAAGAAACCGCCTCGCCCTGGA
GCTCCCGGTCATCTGGGAAGCCTTGCCAGCCTCAGCAGCCCTGCTGACAGCTACAACGAG
GGTGTCAAGCTTCAGCCCCAGGAAATCAGCCCCCCTCCTACTGCCAACCTGGACCGGTCG
AATGATAAGGTGTACGAGAATGTGACGGGCCTGGTGAAAGCTGTCATCGAGATGTCCAGT
AAAATCCAGCCAGCCCCACCAGAGGAGTATGTCCCTATGGTGAAGGAAGTCGGCTTGGCC
CTGAGGACATTATTGGCCACTGTGGATGAGACCATTCCCCTCCTACCAGCCAGCACCCAC
CGAGAGATTGAGATGGCACAGAAGCTATTGAACTCTGACCTGGGTGAGCTCATCAACAAG
ATGAAACTGGCCCAGCAGTATGTCATGACCAGCCTCCAGCAAGAGTACAAAAAGCAAATG
CTGACTGCTGCTCACGCCCTGGCTGTGGATGCCAAAAACTTACTCGATGTCATTGACCAA
GCAAGACTGAAAATGCTTGGGCAGACGAGACCACACTGA
Enzyme 11 GenBank Gene ID L13616 Link Image
Enzyme 11 GeneCard ID PTK2 Link Image
Enzyme 11 GenAtlas ID PTK2 Link Image
Enzyme 11 HGNC ID HGNC:9611 Link Image
Enzyme 11 Chromosome Location 8
Enzyme 11 Locus 8q24-qter
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Whitney GS, Chan PY, Blake J, Cosand WL, Neubauer MG, Aruffo A, Kanner SB: Human T and B lymphocytes express a structurally conserved focal adhesion kinase, pp125FAK. DNA Cell Biol. 1993 Nov;12(9):823-30. [PubMed Link Image]
  2. Andre E, Becker-Andre M: Expression of an N-terminally truncated form of human focal adhesion kinase in brain. Biochem Biophys Res Commun. 1993 Jan 15;190(1):140-7. [PubMed Link Image]
  3. Lee ST, Strunk KM, Spritz RA: A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes. Oncogene. 1993 Dec;8(12):3403-10. [PubMed Link Image]
  4. Relou IA, Bax LA, van Rijn HJ, Akkerman JW: Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein. Biochem J. 2003 Jan 15;369(Pt 2):407-16. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6721
Enzyme 12 Name Protein tyrosine kinase 2 beta
Enzyme 12 Synonyms
  1. Focal adhesion kinase 2
  2. FADK 2
  3. Proline-rich tyrosine kinase 2
  4. Cell adhesion kinase beta
  5. CAK beta
  6. Calcium-dependent tyrosine kinase
  7. CADTK
  8. Related adhesion focal tyrosine kinase
  9. RAFTK
Enzyme 12 Gene Name PTK2B
Enzyme 12 Protein Sequence >Protein tyrosine kinase 2 beta 
MSGVSEPLSRVKLGTLRRPEGPAEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVK
CTVQTEIREIITSILLSGRIGPNIRLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYEC
LHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRNDYMQRYASKVSEGMALQLGC
LELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYAS
LREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDAKPTCLA
EFKQIRSIRCLPLEEGQAVLQLGIEGAPQALSIKTSSLAEAENMADLIDGYCRLQGEHQG
SLIIHPRKDGEKRNSLPQIPMLNLEARRSHLSESCSIESDIYAEIPDETLRRPGGPQYGI
AREDVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTLDNKEKFMSEAVIMKN
LDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVLTLVLYSLQICKAMAYL
ESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFR
RFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPDLCPPVLYTLMTR
CWDYDPSDRPRFTELVCSLSDVYQMEKDIAMEQERNARYRTPKILEPTAFQEPPPKPSRP
KYRPPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMR
EEDFIQPSSREEAQQLWEAEKVKMRQILDKQQKQMVEDYQWLRQEEKSLDPMVYMNDKSP
LTPEKEVGYLEFTGPPQKPPRLGAQSIQPTANLDRTDDLVYLNVMELVRAVLELKNELCQ
LPPEGYVVVVKNVGLTLRKLIGSVDDLLPSLPSSSRTEIEGTQKLLNKDLAELINKMRLA
QQNAVTSLSEECKRQMLTASHTLAVDAKNLLDAVDQAKVLANLAHPPAE
Enzyme 12 Number of Residues 1009
Enzyme 12 Molecular Weight 115876
Enzyme 12 Theoretical pI 6.16
Enzyme 12 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • protein kinase activity
  • protein-tyrosine kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid phosphorylation
  • protein modification
Component
  • cytoskeleton
  • intracellular non-membrane-bound organelle
  • non-membrane-bound organelle
  • organelle
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Involved in calcium induced regulation of ion channel and activation of the map kinase signaling pathway. May represent an important signaling intermediate between neuropeptide activated receptors or neurotransmitters that increase calcium flux and the downstream signals that regulate neuronal activity. Interacts with the SH2 domain of Grb2. May phosphorylate the voltage-gated potassium channel protein Kv1.2. Its activation is highly correlated with the stimulation of c-Jun N-terminal kinase activity. Involved in osmotic stress-dependent SNCA 'Tyr-125' phosphorylation
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 988305 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q14289 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name FAK2_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >3030 bp 
ATGTCTGGGGTGTCCGAGCCCCTGAGCCGAGTAAAGTTGGGCACATTACGCCGGCCTGAA
GGCCCTGCAGAGCCCATGGTGGTGGTACCAGTAGATGTGGAAAAGGAGGACGTGCGTATC
CTCAAGGTCTGCTTCTATAGCAACAGCTTCAATCCTGGGAAGAACTTCAAACTGGTCAAA
TGCACTGTCCAGACGGAGATCCGGGAGATCATCACCTCCATCCTGCTGAGCGGGCGGATC
GGGCCCAACATCCGGTTGGCTGAGTGCTATGGGCTGAGGCTGAAGCACATGAAGTCCGAT
GAGATCCACTGGCTGCACCCACAGATGACGGTGGGTGAGGTGCAGGACAAGTATGAGTGT
CTGCACGTGGAAGCCGAGTGGAGGTATGACCTTCAAATCCGCTACTTGCCAGAAGACTTC
ATGGAGAGCCTGAAGGAGGACAGGACCACGCTGCTCTATTTTTACCAACAGCTCCGGAAC
GACTACATGCAGCGCTACGCCAGCAAGGTCAGCGAGGGCATGGCCCTGCAGCTGGGCTGC
CTGGAGCTCAGGCGGTTCTTCAAGGATATGCCCCACAATGCACTTGACAAGAAGTCCAAC
TTCGAGCTCCTAGAAAAGGAAGTGGGGCTGGACTTGTTTTTCCCAAAGCAGATGCAGGAG
AACTTAAAGCCCAAACAGTTCCGGAAGATGATCCAGCAGACCTTCCAGCAGTACGCCTCG
CTCAGGGAGGAGGAGTGCGTCATGAAGTTCTTCAACACTCTCGCCGGCTTCGCCAACATC
GACCAGGAGACCTACCGCTGTGAACTCATTCAAGGATGGAACATTACTGTGGACCTGGTC
ATTGGCCCTAAAGGGATCCGCCAGCTGACTAGTCAGGACGCAAAGCCCACCTGCCTGGCC
GAGTTCAAGCAGATCAGGTCCATCAGGTGCCTCCCGCTGGAGGAGGGCCAGGCAGTACTT
CAGCTGGGCATTGAAGGTGCCCCCCAGGCCTTGTCCATCAAAACCTCATCCCTAGCAGAG
GCTGAGAACATGGCTGACCTCATAGACGGCTACTGCCGGCTGCAGGGTGAGCACCAAGGC
TCTCTCATCATCCATCCTAGGAAAGATGGTGAGAAGCGGAACAGCCTGCCCCAGATCCCC
ATGCTAAACCTGGAGGCCCGGCGGTCCCACCTCTCAGAGAGCTGCAGCATAGAGTCAGAC
ATCTACGCAGAGATTCCCGACGAAACCCTGCGAAGGCCCGGAGGTCCACAGTATGGCATT
GCCCGTGAAGATGTGGTCCTGAATCGTATTCTTGGGGAAGGCTTTTTTGGGGAGGTCTAT
GAAGGTGTCTACACAAATCACAAAGGGGAGAAAATCAATGTAGCTGTCAAGACCTGCAAG
AAAGACTGCACTCTGGACAACAAGGAGAAGTTCATGAGCGAGGCAGTGATCATGAAGAAC
CTCGACCACCCGCACATCGTGAAGCTGATCGGCATCATTGAAGAGGAGCCCACCTGGATC
ATCATGGAATTGTATCCCTATGGGGAGCTGGGCCACTACCTGGAGCGGAACAAGAACTCC
CTGAAGGTGCTCACCCTCGTGCTGTACTCACTGCAGATATGCAAAGCCATGGCCTACCTG
GAGAGCATCAACTGCGTGCACAGGGACATTGCTGTCCGGAACATCCTGGTGGCCTCCCCT
GAGTGTGTGAAGCTGGGGGACTTTGGTCTTTCCCGGTACATTGAGGACGAGGACTATTAC
AAAGCCTCTGTGACTCGTCTCCCCATCAAATGGATGTCCCCAGAGTCCATTAACTTCCGA
CGCTTCACGACAGCCAGTGACGTCTGGATGTTCGCCGTGTGCATGTGGGAGATCCTGAGC
TTTGGGAAGCAGCCCTTCTTCTGGCTGGAGAACAAGGATGTCATCGGGGTGCTGGAGAAA
GGAGACCGGCTGCCCAAGCCTGATCTCTGTCCACCGGTCCTTTATACCCTCATGACCCGC
TGCTGGGACTACGACCCCAGTGACCGGCCCCGCTTCACCGAGCTGGTGTGCAGCCTCAGT
GACGTTTATCAGATGGAGAAGGACATTGCCATGGAGCAAGAGAGGAATGCTCGCTACCGA
ACCCCCAAAATCTTGGAGCCCACAGCCTTCCAGGAACCCCCACCCAAGCCCAGCCGACCT
AAGTACAGACCCCCTCCGCAAACCAACCTCCTGGCTCCAAAGCTGCAGTTCCAGGTTCCT
GAGGGTCTGTGTGCCAGCTCTCCTACGCTCACCAGCCCTATGGAGTATCCATCTCCCGTT
AACTCACTGCACACCCCACCTCTCCACCGGCACAATGTCTTCAAACGCCACAGCATGCGG
GAGGAGGACTTCATCCAACCCAGCAGCCGAGAAGAGGCCCAGCAGCTGTGGGAGGCTGAA
AAGGTCAAAATGCGGCAAATCCTGGACAAACAGCAGAAGCAGATGGTGGAGGACTACCAG
TGGCTCAGGCAGGAGGAGAAGTCCCTGGACCCCATGGTTTATATGAATGATAAGTCCCCA
TTGACGCCAGAGAAGGAGGTCGGCTACCTGGAGTTCACAGGGCCCCCACAGAAGCCCCCG
AGGCTGGGCGCACAGTCCATCCAGCCCACAGCTAACCTGGACCGGACCGATGACCTGGTG
TACCTCAATGTCATGGAGCTGGTGCGGGCCGTGCTGGAGCTCAAGAATGAGCTCTGTCAG
CTGCCCCCCGAGGGCTACGTGGTGGTGGTGAAGAATGTGGGGCTGACCCTGCGGAAGCTC
ATCGGGAGCGTGGATGATCTCCTGCCTTCCTTGCCGTCATCTTCACGGACAGAGATCGAG
GGCACCCAGAAACTGCTCAACAAAGACCTGGCAGAGCTCATCAACAAGATGCGGCTGGCG
CAGCAGAACGCCGTGACCTCCCTGAGTGAGGAGTGCAAGAGGCAGATGCTGACGGCTTCA
CACACCCTGGCTGTGGACGCCAAGAACCTGCTCGACGCTGTGGACCAGGCCAAGGTTCTG
GCCAATCTGGCCCACCCACCTGCAGAGTGA
Enzyme 12 GenBank Gene ID U33284 Link Image
Enzyme 12 GeneCard ID PTK2B Link Image
Enzyme 12 GenAtlas ID PTK2B Link Image
Enzyme 12 HGNC ID HGNC:9612 Link Image
Enzyme 12 Chromosome Location 8
Enzyme 12 Locus 8p21.1
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Lev S, Moreno H, Martinez R, Canoll P, Peles E, Musacchio JM, Plowman GD, Rudy B, Schlessinger J: Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions. Nature. 1995 Aug 31;376(6543):737-45. [PubMed Link Image]
  2. Herzog H, Nicholl J, Hort YJ, Sutherland GR, Shine J: Molecular cloning and assignment of FAK2, a novel human focal adhesion kinase, to 8p11.2-p22 by nonisotopic in situ hybridization. Genomics. 1996 Mar 15;32(3):484-6. [PubMed Link Image]
  3. Sasaki H, Nagura K, Ishino M, Tobioka H, Kotani K, Sasaki T: Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily. J Biol Chem. 1995 Sep 8;270(36):21206-19. [PubMed Link Image]
  4. Avraham S, London R, Fu Y, Ota S, Hiregowdara D, Li J, Jiang S, Pasztor LM, White RA, Groopman JE, et al.: Identification and characterization of a novel related adhesion focal tyrosine kinase (RAFTK) from megakaryocytes and brain. J Biol Chem. 1995 Nov 17;270(46):27742-51. [PubMed Link Image]
  5. Li X, Hunter D, Morris J, Haskill JS, Earp HS: A calcium-dependent tyrosine kinase splice variant in human monocytes. Activation by a two-stage process involving adherence and a subsequent intracellular signal. J Biol Chem. 1998 Apr 17;273(16):9361-4. [PubMed Link Image]
  6. Andreev J, Simon JP, Sabatini DD, Kam J, Plowman G, Randazzo PA, Schlessinger J: Identification of a new Pyk2 target protein with Arf-GAP activity. Mol Cell Biol. 1999 Mar;19(3):2338-50. [PubMed Link Image]
  7. Benzing T, Gerke P, Hopker K, Hildebrandt F, Kim E, Walz G: Nephrocystin interacts with Pyk2, p130(Cas), and tensin and triggers phosphorylation of Pyk2. Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9784-9. Epub 2001 Aug 7. [PubMed Link Image]
  8. Salomon AR, Ficarro SB, Brill LM, Brinker A, Phung QT, Ericson C, Sauer K, Brock A, Horn DM, Schultz PG, Peters EC: Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry. Proc Natl Acad Sci U S A. 2003 Jan 21;100(2):443-8. Epub 2003 Jan 9. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6873
Enzyme 13 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
Enzyme 13 Synonyms
  1. 1- AGP acyltransferase 3
  2. 1-AGPAT 3
  3. Lysophosphatidic acid acyltransferase gamma
  4. LPAAT-gamma
  5. 1-acylglycerol-3-phosphate O- acyltransferase 3
Enzyme 13 Gene Name AGPAT3
Enzyme 13 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase gamma 
MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQ
LVMLLEWWSCTECTLFTDQATVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKV
LAKKELLYVPLIGWTWYFLEIVFCKRKWEEDRDTVVEGLRRLSDYPEYMWFLLYCEGTRF
TETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSL
LGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFK
PARRPWTLLNFLSWATILLSPLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTE
IEKGSSYGNQEFKKKE
Enzyme 13 Number of Residues 376
Enzyme 13 Molecular Weight 43381
Enzyme 13 Theoretical pI 8.91
Enzyme 13 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 13 General Function Lipid transport and metabolism
Enzyme 13 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 13 Pathways
Enzyme 13 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-25
Enzyme 13 Transmembrane Regions Not Available
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 8886001 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q9NRZ7 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name PLCC_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1131 bp 
ATGGGCCTGCTGGCCTTCCTGAAGACCCAGTTCGTGCTGCACCTGCTGGTCGGCTTTGTC
TTCGTGGTGAGTGGTCTGGTCATCAACTTCGTCCAGCTGTGCACGCTGGCGCTCTGGCCG
GTCAGCAAGCAGCTCTACCGCCGCCTCAACTGCCGCCTCGCATACTCACTCTGGAGCCAA
CTGGTCATGCTGCTGGAGTGGTGGTCCTGCACGGAGTGTACACTGTTCACGGACCAGGCC
ACGGTAGAGCGCTTTGGGAAGGAGCACGCAGTCATCATCCTCAACCACAACTTCGAGATC
GACTTCCTCTGTGGGTGGACCATGTGTGAGCGCTTCGGAGTGCTGGGGAGCTCCAAGGTC
CTCGCTAAGAAGGAGCTGCTCTACGTGCCCCTCATCGGCTGGACGTGGTACTTTCTGGAG
ATTGTGTTCTGCAAGCGGAAGTGGGAGGAGGACCGGGACACCGTGGTCGAAGGGCTGAGG
CGCCTGTCGGACTACCCCGAGTACATGTGGTTTCTCCTGTACTGCGAGGGGACGCGCTTC
ACGGAGACCAAGCACCGCGTTAGCATGGAGGTGGCGGCTGCTAAGGGGCTTCCTGTCCTC
AAGTACCACCTGCTGCCGCGGACCAAGGGCTTCACCACCGCAGTCAAGTGCCTCCGGGGG
ACAGTCGCAGCTGTCTATGATGTAACCCTGAACTTCAGAGGAAACAAGAACCCGTCCCTG
CTGGGGATCCTCTACGGGAAGAAGTACGAGGCGGACATGTGCGTGAGGAGATTTCCTCTG
GAAGACATCCCGCTGGATGAAAAGGAAGCAGCTCAGTGGCTTCATAAACTGTACCAGGAG
AAGGACGCGCTCCAGGAGATATATAATCAGAAGGGCATGTTTCCAGGGGAGCAGTTTAAG
CCTGCCCGGAGGCCGTGGACCCTCCTGAACTTCCTGTCCTGGGCCACCATTCTCCTGTCT
CCCCTCTTCAGTTTTGTCTTGGGCGTCTTTGCCAGCGGATCACCTCTCCTGATCCTGACT
TTCTTGGGGTTTGTGGGAGCAGCTTCCTTTGGAGTTCGCAGACTGATAGGAGTAACTGAG
ATAGAAAAAGGCTCCAGCTACGGAAACCAAGAGTTTAAGAAAAAGGAATAA
Enzyme 13 GenBank Gene ID AF156774 Link Image
Enzyme 13 GeneCard ID AGPAT3 Link Image
Enzyme 13 GenAtlas ID AGPAT3 Link Image
Enzyme 13 HGNC ID HGNC:326 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. 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 6875
Enzyme 14 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
Enzyme 14 Synonyms
  1. 1- AGP acyltransferase 2
  2. 1-AGPAT 2
  3. Lysophosphatidic acid acyltransferase beta
  4. LPAAT-beta
  5. 1-acylglycerol-3-phosphate O- acyltransferase 2
Enzyme 14 Gene Name AGPAT2
Enzyme 14 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase beta 
MELWPCLAAALLLLLLLVQLSRAAEFYAKVALYCALCFTVSAVASLVCLLRHGGRTVENM
SIIGWFVRSFKYFYGLRFEVRDPRRLQEARPCVIVSNHQSILDMMGLMEVLPERCVQIAK
RELLFLGPVGLIMYLGGVFFINRQRSSTAMTVMADLGERMVRENLKVWIYPEGTRNDNGD
LLPFKKGAFYLAVQAQVPIVPVVYSSFSSFYNTKKKFFTSGTVTVQVLEAIPTSGLTAAD
VPALVDTCHRAMRTTFLHISKTPQENGATAGSGVQPAQ
Enzyme 14 Number of Residues 278
Enzyme 14 Molecular Weight 30915
Enzyme 14 Theoretical pI 9.22
Enzyme 14 GO Classification
Function
  • 1-acylglycerol-3-phosphate O-acyltransferase activity
  • O-acyltransferase activity
  • acylglycerol O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid biosynthesis
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
  • cell
  • membrane
Enzyme 14 General Function Lipid transport and metabolism
Enzyme 14 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 14 Pathways
Enzyme 14 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-23
Enzyme 14 Transmembrane Regions Not Available
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 2282590 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID O15120 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name PLCB_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >837 bp 
ATGGAGCTGTGGCCGTGTCTGGCCGCGGCGCTGCTGTTGCTGCTGCTGCTGGTGCAGCTG
AGCCGCGCGGCCGAGTTCTACGCCAAGGTCGCCCTGTACTGCGCGCTGTGCTTCACGGTG
TCCGCCGTGGCCTCGCTCGTCTGCCTGCTGCGCCACGGCGGCCGGACGGTGGAGAACATG
AGCATCATCGGCTGGTTCGTGCGAAGCTTCAAGTACTTTTACGGGCTCCGCTTCGAGGTG
CGGGACCCGCGCAGGCTGCAGGAGGCCCGTCCCTGTGTCATCGTCTCCAACCACCAGAGC
ATCCTGGACATGATGGGCCTCATGGAGGTCCTTCCGGAGCGCTGCGTGCAGATCGCCAAG
CGGGAGCTGCTCTTCCTGGGGCCCGTGGGCCTCATCATGTACCTCGGGGGCGTCTTCTTC
ATCAACCGGCAGCGCTCTAGCACTGCCATGACAGTGATGGCCGACCTGGGCGAGCGCATG
GTCAGGGAGAACCTCAAAGTGTGGATCTATCCCGAGGGTACTCGCAACGACAATGGGGAC
CTGCTGCCTTTTAAGAAGGGCGCCTTCTACCTGGCAGTCCAGGCACAGGTGCCCATCGTC
CCCGTGGTGTACTCTTCCTTCTCCTCCTTCTACAACACCAAGAAGAAGTTCTTCACTTCA
GGAACAGTCACAGTGCAGGTGCTGGAAGCCATCCCCACCAGCGGCCTCACTGCGGCGGAC
GTCCCTGCGCTCGTGGACACCTGCCACCGGGCCATGAGGACCACCTTCCTCCACATCTCC
AAGACCCCCCAGGAGAACGGGGCCACTGCGGGGTCTGGCGTGCAGCCGGCCCAGTAG
Enzyme 14 GenBank Gene ID AF000237 Link Image
Enzyme 14 GeneCard ID AGPAT2 Link Image
Enzyme 14 GenAtlas ID AGPAT2 Link Image
Enzyme 14 HGNC ID HGNC:325 Link Image
Enzyme 14 Chromosome Location 9
Enzyme 14 Locus 9q34.3
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Eberhardt C, Gray PW, Tjoelker LW: Human lysophosphatidic acid acyltransferase. cDNA cloning, expression, and localization to chromosome 9q34.3. J Biol Chem. 1997 Aug 8;272(32):20299-305. [PubMed Link Image]
  2. Stamps AC, Elmore MA, Hill ME, Kelly K, Makda AA, Finnen MJ: A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases. Biochem J. 1997 Sep 1;326 ( Pt 2):455-61. [PubMed Link Image]
  3. West J, Tompkins CK, Balantac N, Nudelman E, Meengs B, White T, Bursten S, Coleman J, Kumar A, Singer JW, Leung DW: Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells. DNA Cell Biol. 1997 Jun;16(6):691-701. [PubMed Link Image]
  4. Agarwal AK, Arioglu E, De Almeida S, Akkoc N, Taylor SI, Bowcock AM, Barnes RI, Garg A: AGPAT2 is mutated in congenital generalized lipodystrophy linked to chromosome 9q34. Nat Genet. 2002 May;31(1):21-3. Epub 2002 Apr 22. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 6877
Enzyme 15 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
Enzyme 15 Synonyms
  1. 1- AGP acyltransferase 1
  2. 1-AGPAT 1
  3. Lysophosphatidic acid acyltransferase alpha
  4. LPAAT-alpha
  5. 1-acylglycerol-3-phosphate O- acyltransferase 1
  6. Protein G15
Enzyme 15 Gene Name AGPAT1
Enzyme 15 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase alpha 
MDLWPGAWMLLLLLFLLLLFLLPTLWFCSPSAKYFFKMAFYNGWILFLAVLAIPVCAVRG
RNVENMKILRLMLLHIKYLYGIRVEVRGAHHFPPSQPYVVVSNHQSSLDLLGMMEVLPGR
CVPIAKRELLWAGSAGLACWLAGVIFIDRKRTGDAISVMSEVAQTLLTQDVRVWVFPEGT
RNHNGSMLPFKRGAFHLAVQAQVPIVPIVMSSYQDFYCKKERRFTSGQCQVRVLPPVPTE
GLTPDDVPALADRVRHSMLTVFREISTDGRGGGDYLKKPGGGG
Enzyme 15 Number of Residues 283
Enzyme 15 Molecular Weight 31717
Enzyme 15 Theoretical pI 9.75
Enzyme 15 GO Classification
Function
  • 1-acylglycerol-3-phosphate O-acyltransferase activity
  • O-acyltransferase activity
  • acylglycerol O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid biosynthesis
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
  • cell
  • membrane
Enzyme 15 General Function Lipid transport and metabolism
Enzyme 15 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 15 Pathways
Enzyme 15 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-26
Enzyme 15 Transmembrane Regions Not Available
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 2155238 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q99943 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name PLCA_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >852 bp 
ATGGATTTGTGGCCAGGGGCATGGATGCTGCTGCTGCTGCTCTTCCTGCTGCTGCTCTTC
CTGCTGCCCACCCTGTGGTTCTGCAGCCCCAGTGCCAAGTACTTCTTCAAGATGGCCTTC
TACAATGGCTGGATCCTCTTCCTGGCTGTGCTCGCCATCCCTGTGTGTGCCGTGCGAGGA
CGCAACGTCGAGAACATGAAGATCTTGCGTCTAATGCTGCTCCACATCAAATACCTGTAC
GGGATCCGAGTGGAGGTGCGAGGGGCTCACCACTTCCCTCCCTCGCAGCCCTATGTTGTT
GTCTCCAACCACCAGAGCTCTCTCGATCTGCTTGGGATGATGGAGGTACTGCCAGGCCGC
TGTGTGCCCATTGCCAAGCGCGAGCTACTGTGGGCTGGCTCTGCCGGGCTGGCCTGCTGG
CTGGCAGGAGTCATCTTCATCGACCGGAAGCGCACGGGGGATGCCATCAGTGTCATGTCT
GAGGTCGCCCAGACCCTGCTCACCCAGGACGTGAGGGTCTGGGTGTTTCCTGAGGGAACG
AGAAACCACAATGGCTCCATGCTGCCCTTCAAACGTGGCGCCTTCCATCTTGCAGTGCAG
GCCCAGGTTCCCATTGTCCCCATAGTCATGTCCTCCTACCAAGACTTCTACTGCAAGAAG
GAGCGTCGCTTCACCTCGGGACAATGTCAGGTGCGGGTGCTGCCCCCAGTGCCCACGGAA
GGGCTGACACCAGATGACGTCCCAGCTCTGGCTGACAGAGTCCGGCACTCCATGCTCACT
GTTTTCCGGGAAATCTCCACTGATGGCCGGGGTGGTGGTGACTATCTGAAGAAGCCTGGG
GGCGGTGGGTGA
Enzyme 15 GenBank Gene ID U56417 Link Image
Enzyme 15 GeneCard ID AGPAT1 Link Image
Enzyme 15 GenAtlas ID AGPAT1 Link Image
Enzyme 15 HGNC ID HGNC:324 Link Image
Enzyme 15 Chromosome Location 6
Enzyme 15 Locus 6p21.3
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. West J, Tompkins CK, Balantac N, Nudelman E, Meengs B, White T, Bursten S, Coleman J, Kumar A, Singer JW, Leung DW: Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells. DNA Cell Biol. 1997 Jun;16(6):691-701. [PubMed Link Image]
  2. Stamps AC, Elmore MA, Hill ME, Kelly K, Makda AA, Finnen MJ: A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases. Biochem J. 1997 Sep 1;326 ( Pt 2):455-61. [PubMed Link Image]
  3. Aguado B, Campbell RD: Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene located in the class III region of the human major histocompatibility complex. J Biol Chem. 1998 Feb 13;273(7):4096-105. [PubMed Link Image]
  4. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 6881
Enzyme 16 Name Phosphatidylinositol-glycan-specific phospholipase D precursor
Enzyme 16 Synonyms
  1. PI-G PLD
  2. Glycoprotein phospholipase D
  3. Glycosyl- phosphatidylinositol-specific phospholipase D
Enzyme 16 Gene Name GPLD1
Enzyme 16 Protein Sequence >Phosphatidylinositol-glycan-specific phospholipase D precursor 
MSAFRLWPGLLIMLGSLCHRGSPCGLSTHVEIGHRALEFLQLHNGRVNYRELLLEHQDAY
QAGIVFPDCFYPSICKGGKFHDVSESTHWTPFLNASVHYIRENYPLPWEKDTEKLVAFLF
GITSHMAADVSWHSLGLEQGFLRTMGAIDFHGSYSEAHSAGDFGGDVLSQFEFNFNYLAR
RWYVPVKDLLGIYEKLYGRKVITENVIVDCSHIQFLEMYGEMLAVSKLYPTYSTKSPFLV
EQFQEYFLGGLDDMAFWSTNIYHLTSFMLENGTSDCNLPENPLFIACGGQQNHTQGSKMQ
KNDFHRNLTTSLTESVDRNINYTERGVFFSVNSWTPDSMSFIYKALERNIRTMFIGGSQL
SQKHVSSPLASYFLSFPYARLGWAMTSADLNQDGHGDLVVGAPGYSRPGHIHIGRVYLIY
GNDLGLPPVDLDLDKEAHRILEGFQPSGRFGSALAVLDFNVDGVPDLAVGAPSVGSEQLT
YKGAVYVYFGSKQGGMSSSPNITISCQDIYCNLGWTLLAADVNGDSEPDLVIGSPFAPGG
GKQKGIVAAFYSGPSLSDKEKLNVEAANWTVRGEEDFSWFGYSLHGVTVDNRTLLLVGSP
TWKNASRLGHLLHIRDEKKSLGRVYGYFPPNGQSWFTISGDKAMGKLGTSLSSGHVLMNG
TLKQVLLVGAPTYDDVSKVAFLTVTLHQGGATRMYALTSDAQPLLLSTFSGDRRFSRFGG
VLHLSDLDDDGLDEIIMAAPLRIADVTSGLIGGEDGRVYVYNGKETTLGDMTGKCKSWIT
PCPEEKAQYVLISPEASSRFGSSLITVRSKAKNQVVIAAGRSSLGARLSGALHVYSLGSD
Enzyme 16 Number of Residues 840
Enzyme 16 Molecular Weight 92337
Enzyme 16 Theoretical pI 6.33
Enzyme 16 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • glycosylphosphatidylinositol phospholipase D activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase D activity
  • phospholipase activity
Process
—
Component
  • extracellular region
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions
  • 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + phosphatidate
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-23
Enzyme 16 Transmembrane Regions Not Available
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 388763 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P80108 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name PHLD_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >2526 bp 
ATGTCTGCTTTCAGGTTGTGGCCCGGCCTGCTGATGATCGTGATGGCTTCTCTCTGCCAT
AGAGGTTCATCGTGTGGCCTTTCAACGCACATAGAAATCGGACACAGAGCTCTGGAGTTT
CTTCATCTTCACAATGGGCATGTTAACTACAAAGAGCTGTTACTAGAACACCAGGATGCA
TATCAGGCTGGAACCGTGTTTCCTGATTGTTTTTACCCTAGCCTCTGCAAAGGAGGAAAA
TTCCATGATGTGTCTGAGAGCACTCACTGGACTCCGTTTCTTAACGCAAGCGTTCATTAT
ATCCGAGAGAACTATCCCCTTCCCTGGGAGAAGGACACAGAGAAACTGGTAGCTTTCTTG
TTTGGAATTACTTCTCATATGGTAGCAGATGTCAGCTGGCATAGTCTGGGCATTGAACAA
GGATTCCTTAGGACCATGGGAGCTATTGATTTTCACGGCTCCTATTCTGAGGCTCATTCA
GCTGGTGATTTTGGAGGAGATGTGTTGAGCCAGTTTGAATTTAATTTTAATTACCTTGCA
CGACGCTGGTATGTGCCAGTCAAAGATCTGCTGGGAATTTATGAGAAACTCTATGGTCGA
GAAGTCATCACTGAAAATGTAATTGTTGATTGTTCACATATCCAGTTCTTAGAAATGTAT
GGTGAGATGCTAGCTGTTTCCAAGTTATATCCCTCTTACTCTACAAAGTCCCCGTTTTTG
GTGGAACAATTCCAAGAGTATTTTCTTGGAGGACTGGATGATATGGCGTTTTGGTCCACT
AATATTTACCATCTAACGAGCTTCATGTTGGAGAATGGGACCAGTGACTGCAGCCTACCT
GAGAACCCTCTGTTCATTGCATGTGGTGGCCAGCAAAACCACACCCAGGGCTCGAAAATG
CAGAAAAATGATTTTCACAGAAATTTGACTTCATCCCTAACTGAAAACATTGACAGGAAT
ATAAACTATACCGAAAGAGGAGTGTTCTTCAGTGTAAATTCCTGGACCCCGGATTCCATG
TCCTTTATCTACAAGGCTTTGGAAAGGAACGTAAGGACAATGTTCATAGGTGGCTCTCAG
TTGTCACAGAAGCACATCTCTAGCCCCTTAGCATCTTACTTCTTGTCATTTCCTTATGCA
AGGCTTGGCTGGGCAATGACCTCAGCTGACCTCAACCAGGATGGGTACGGCGACCTCGTG
GTGGGCGCACCAGGCTACAGCCGCCCTGGCCGCATCCACATCGGGCGCGTGTACCTCATC
TACGGCAATGAACTGGGTCTGCCGCCCGTTGACCTGGACCTGGACAAGGAGGCCCACGGG
ATCCTTGAAGGTTTCCAGCCCTCAGGTCGGTTTGGCTCGGCCTTGGCTATGTTGGACTTT
AACATGGATGGCGTGCCTGACCTGGCCGTGGGAGCTCCCTCGGTGGGCTCTGAGCAGCTC
ACCTACAAAGGTGCTGTGTATGTCTACTTTGGTTCCAAACAAGGAAGAATGTCTTCTTCC
CCTAACATCACCATCTCTTGCCAGGACATCTACTGTAACTTGGGCTGGACTCTCTTGGCT
GCAGATGTGAATGGAGACAGTGAGCCCGATCTGGTCATTGGCTCCCCTTTTGCACCAGGT
GGAGGGAAGCAGAAGGGAATTGTGGCTGCGTTTTATTCTGGCCCCAGCCTGAGCAACAAA
GAGAAACTGAACGTGGAGGCGGCCAACTGGACGGTGAGAGGCGAGGAAGACTTTGCCTGG
TTTGGATACTCCCTTCACGGTGTCACTGTGGACAACAGAACCTTGCTGCTGGTTGGGAGC
CCGACCTGGAAGAATGCCAGCAGGCTGGGCCGTTTGTTACACATCCGAGATGAGAAAAAG
AGCCTTGGGAGGGTGTATGGCTACTTCCCACCAAACAGCCAAAGCTGGTTTACCATTGTT
GGAGACAAGGCAATGGGGAAACTGGGTACTTCCCTGTCCAGTGGCCACGTGCTGATGAAT
GGAACTCTGACCCAGGTGCTGCTGGTGGGAGCCCCGACACGTGATGATGTGTCTAAGATG
GCATTCCTGACCATGACCCTGCACCAAGGCGGAGCCACTCGGATGTACGCGCTCACATCC
GACCTGCAGCCACCGCTGCTCAGCACCTTCAGCGGAGACCGCCGCTTCTCTCGATTTGGT
GGCGTTCTGCACTTGAGTGACCTGGATGATGATGGCGTAGATGAAATCATCGTGGCAGCC
CCCCTGAGGATAGCAGATGTAACCTCTGGGCTGATTGGGGGAGAAGATGGCCGAGTTTAT
GTATATAATGGCAAAGAGACCACCCTTGGTGACATGACTGGCAAATGCAAATCGTGGATG
ACTCCATGTCCAGAAGAAAAGGCCCAATATGTATTGATTTCTCCTGAAGCCAGCTCAAGG
TTTGGGAGCTCCCTGATCACCGTGAGGTCCAAGGCAAAGAATCAAGTCGTCATTGCCGCT
GGAAGGAGCTCTTTGGGAGCCCGACTCTCCGGGGCACTTCACGTCTATAGCTTTGGCTCA
GATTGA
Enzyme 16 GenBank Gene ID L11701 Link Image
Enzyme 16 GeneCard ID GPLD1 Link Image
Enzyme 16 GenAtlas ID GPLD1 Link Image
Enzyme 16 HGNC ID HGNC:4459 Link Image
Enzyme 16 Chromosome Location 6
Enzyme 16 Locus 6p22.3-p22.2
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Schofield JN, Rademacher TW: Structure and expression of the human glycosylphosphatidylinositol phospholipase D1 (GPLD1) gene. Biochim Biophys Acta. 2000 Nov 15;1494(1-2):189-94. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  3. Hoener MC, Brodbeck U: Phosphatidylinositol-glycan-specific phospholipase D is an amphiphilic glycoprotein that in serum is associated with high-density lipoproteins. Eur J Biochem. 1992 Jun 15;206(3):747-57. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 8354
Enzyme 17 Name Lysophosphatidic acid receptor Edg-4
Enzyme 17 Synonyms
  1. LPA receptor 2
  2. LPA-2
Enzyme 17 Gene Name EDG4
Enzyme 17 Protein Sequence >Lysophosphatidic acid receptor Edg-4 
MVIMGQCYYNETIGFFYNNSGKELSSHWRPKDVVVVALGLTVSVLVLLTNLLVIAAIASN
RRFHQPIYYLLGNLAAADLFAGVAYLFLMFHTGPRTARLSLEGWFLRQGLLDTSLTASVA
TLLAIAVERHRSVMAVQLHSRLPRGRVVMLIVGVWVAALGLGLLPAHSWHCLCALDRCSR
MAPLLSRSYLAVWALSSLLVFLLMVAVYTRIFFYVRRRVQRMAEHVSCHPRYRETTLSLV
KTVVIILGAFVVCWTPGQVVLLLDGLGCESCNVLAVEKYFLLLAEANSLVNAAVYSCRDA
EMRRTFRRLLCCACLRQSTRESVHYTSSAQGGASTRIMLPENGHPLMDSTL
Enzyme 17 Number of Residues 351
Enzyme 17 Molecular Weight 39085
Enzyme 17 Theoretical pI 9.42
Enzyme 17 GO Classification
Function
  • G-protein coupled receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Seems to be coupled to the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins. Plays a key role in phospholipase C-beta (PLC-beta) signaling pathway
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • 34-54 70-90 104-126 147-167 189-209 243-263 280-297
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 2735849 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q9HBW0 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name EDG4_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1149 bp 
ATGGTCATCATGGGCCAGTGCTACTACAACGAGACCATCGGCTTCTTCTATAACAACAGT
GGCAAAGAGCTCAGCTCCCACTGGCGGCCCAAGGATGTGGTCGTGGTGGCACTGGGGCTG
ACCGTCAGCGTGCTGGTGCTGCTGACCAATCTGCTGGTCATAGCAGCCATCGCCTCCAAC
CGCCGCTTCCACCAGCCCATCTACTACCTGCTCGGCAATCTGGCCGCGGCTGACCTCTTC
GCGGGCGTGGCCTACCTCTTCCTCATGTTCCACACTGGTCCCCGCACAGCCCGACTTTCA
CTTGAGGGCTGGTTCCTGCGGCAGGGCTTGCTGGACACAAGCCTCACTGCGTCGGTGGCC
ACACTGCTGGCCATCGCCGTGGAGCGGCACCGCAGTGTGATGGCCGTGCAGCTGCACAGC
CGCCTGCCCCGTGGCCGCGTGGTCATGCTCATTGTGGGCGTGTGGGTGGCTGCCCTGGGC
CTGGGGCTGCTGCCTGCCCACTCCTGGCACTGCCTCTGTGCCCTGGACCGCTGCTCACGC
ATGGCACCCCTGCTCAGCCGCTCCTATTTGGCCGTCTGGGCTCTGTCGAGCCTGCTTGTC
TTCCTGCTCATGGTGGCTGTGTACACCCGCATTTTCTTCTACGTGCGGCGGCGAGTGCAG
CGCATGGCAGAGCATGTCAGCTGCCACCCCCGCTACCGAGAGACCACGCTCAGCCTGGTC
AAGACTGTTGTCATCATCCTGGGGGCGTTCGTGGTCTGCTGGACACCAGGCCAGGTGGTA
CTGCTCCTGGATGGTTTAGGCTGTGAGTCCTGCAATGTCCTGGCTGTAGAAAAGTACTTC
CTACTGTTGGCCGAGGCCAACTCACTGGTCAATGCTGCTGTGTACTCTTGCCGAGATGCT
GAGATGCGCCGCACCTTCCGCCGCCTTCTCTGCTGCGCGTGCCTCCGCCAGTCCACCCGC
GAGTCTGTCCACTATACATCCTCTGCCCAGGGAGGTGCCAGCACTCGCATCATGCTTCCC
GAGAACGGCCACCCACTGATGACTCCACCCTTTAGCTACCTTGAACTTCAGCGGTACGCG
GCAAGCAACAAATCCACAGCCCCTGATGACTTGTGGGTGCTCCTGGCTCAACCCAACCAA
CAGGACTGA
Enzyme 17 GenBank Gene ID AF011466 Link Image
Enzyme 17 GeneCard ID EDG4 Link Image
Enzyme 17 GenAtlas ID EDG4 Link Image
Enzyme 17 HGNC ID HGNC:3168 Link Image
Enzyme 17 Chromosome Location 19
Enzyme 17 Locus 19p12
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. An S, Bleu T, Hallmark OG, Goetzl EJ: Characterization of a novel subtype of human G protein-coupled receptor for lysophosphatidic acid. J Biol Chem. 1998 Apr 3;273(14):7906-10. [PubMed Link Image]
  2. Bandoh K, Aoki J, Taira A, Tsujimoto M, Arai H, Inoue K: Lysophosphatidic acid (LPA) receptors of the EDG family are differentially activated by LPA species. Structure-activity relationship of cloned LPA receptors. FEBS Lett. 2000 Jul 28;478(1-2):159-65. [PubMed Link Image]
  3. Contos JJ, Ishii I, Chun J: Lysophosphatidic acid receptors. Mol Pharmacol. 2000 Dec;58(6):1188-96. [PubMed Link Image]
  4. Contos JJ, Chun J: Genomic characterization of the lysophosphatidic acid receptor gene, lp(A2)/Edg4, and identification of a frameshift mutation in a previously characterized cDNA. Genomics. 2000 Mar 1;64(2):155-69. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 8359
Enzyme 18 Name Lysophosphatidic acid receptor Edg-2
Enzyme 18 Synonyms
  1. LPA receptor 1
  2. LPA-1
Enzyme 18 Gene Name EDG2
Enzyme 18 Protein Sequence >Lysophosphatidic acid receptor Edg-2 
MAAISTSIPVISQPQFTAMNEPQCFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITVC
IFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVST
WLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMGA
IPSVGWNCICDIENCSNMAPLYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRMS
RHSSGPRRNRDTMMSLLKTVVIVLGAFIICWTPGLVLLLLDVCCPQCDVLAYEKFFLLLA
EFNSAMNPIIYSYRDKEMSATFRQILCCQRSENPTGPTEGSDRSASSLNHTILAGVHSND
HSVV
Enzyme 18 Number of Residues 364
Enzyme 18 Molecular Weight 41110
Enzyme 18 Theoretical pI 8.60
Enzyme 18 GO Classification
Function
  • G-protein coupled receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Seems to be coupled to the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • 51-75 83-111 126-144 164-189 206-226 259-280 295-315
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 1857425 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q92633 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name EDG2_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1095 bp 
ATGGCTGCCATCTCTACTTCCATCCCTGTAATTTCACAGCCCCAGTTCACAGCCATGAAT
GAACCACAGTGCTTCTACAACGAGTCCATTGCCTTCTTTTATAACCGAAGTGGAAAGCAT
CTTGCCACAGAATGGAACACAGTCAGCAAGCTGGTGATGGGACTTGGAATCACTGTTTGT
ATCTTCATCATGTTGGCCAACCTATTGGTCATGGTGGCAATCTATGTCAACCGCCGCTTC
CATTTTCCTATTTATTACCTAATGGCTAATCTGGCTGCTGCAGACTTCTTTGCTGGGTTG
GCCTACTTCTATCTCATGTTCAACACAGGACCCAATACTCGGAGACTGACTGTTAGCACA
TGGCTCCTGCGTCAGGGCCTCATTGACACCAGCCTGACGGCATCTGTGGCCAACTTACTG
GCTATTGCAATCGAGAGGCACATTACGGTTTTCCGCATGCAGCTCCACACACGGATGAGC
AACCGGCGGGTAGTGGTGGTCATTGTGGTCATCTGGACTATGGCCATCGTTATGGGTGCT
ATACCCAGTGTGGGCTGGAACTGTATCTGTGATATTGAAAATTGTTCCAACATGGCACCC
CTCTACAGTGACTCTTACTTAGTCTTCTGGGCCATTTTCAACTTGGTGACCTTTGTGGTA
ATGGTGGTTCTCTATGCTCACATCTTTGGCTATGTTCGCCAGAGGACTATGAGAATGTCT
CGGCATAGTTCTGGACCCCGGCGGAATCGGGATACCATGATGAGTCTTCTGAAGACTGTG
GTCATTGTGCTTGGGGCCTTTATCATCTGCTGGACTCCTGGATTGGTTTTGTTACTTCTA
GACGTGTGCTGTCCACAGTGCGACGTGCTGGCCTATGAGAAATTCTTCCTTCTCCTTGCT
GAATTCAACTCTGCCATGAACCCCATCATTTACTCCTACCGCGACAAAGAAATGAGCGCC
ACCTTTAGGCAGATCCTCTGCTGCCAGCGCAGTGAGAACCCCACCGGCCCCACAGAAAGC
TCAGACCGCTCGGCTTCCTCCCTCAACCACACCATCTTGGCTGGAGTTCACAGCAATGAC
CACTCTGTGGTTTAG
Enzyme 18 GenBank Gene ID U80811 Link Image
Enzyme 18 GeneCard ID EDG2 Link Image
Enzyme 18 GenAtlas ID EDG2 Link Image
Enzyme 18 HGNC ID HGNC:3166 Link Image
Enzyme 18 Chromosome Location 9
Enzyme 18 Locus 9q31.3
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. An S, Dickens MA, Bleu T, Hallmark OG, Goetzl EJ: Molecular cloning of the human Edg2 protein and its identification as a functional cellular receptor for lysophosphatidic acid. Biochem Biophys Res Commun. 1997 Feb 24;231(3):619-22. [PubMed Link Image]
  2. Moolenaar WH, Kranenburg O, Postma FR, Zondag GC: Lysophosphatidic acid: G-protein signalling and cellular responses. Curr Opin Cell Biol. 1997 Apr;9(2):168-73. [PubMed Link Image]
  3. Contos JJ, Ishii I, Chun J: Lysophosphatidic acid receptors. Mol Pharmacol. 2000 Dec;58(6):1188-96. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 8524
Enzyme 19 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
Enzyme 19 Synonyms
  1. 1-AGP acyltransferase 5
  2. 1-AGPAT 5
  3. Lysophosphatidic acid acyltransferase epsilon
  4. LPAAT-epsilon
  5. 1-acylglycerol-3-phosphate O-acyltransferase 5
Enzyme 19 Gene Name AGPAT5
Enzyme 19 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon 
MLLSLVLHTYSMRYLLPSVVLLGTAPTYVLAWGVWRLLSAFLPARFYQALDDRLYCVYQS
MVLFFFENYTGVQILLYGDLPKNKENIIYLANHQSTVDWIVADILAIRQNALGHVRYVLK
EGLKWLPLYGCYFAQHGGIYVKRSAKFNEKEMRNKLQSYVDAGTPMYLVIFPEGTRYNPE
QTKVLSASQAFAAQRGLAVLKHVLTPRIKATHVAFDCMKNYLDAIYDVTVVYEGKDDGGQ
RRESPTMTEFLCKECPKIHIHIDRIDKKDVPEEQEHMRRWLHERFEIKDKMLIEFYESPD
PERRKRFPGKSVNSKLSIKKTLPSMLILSGLTAGMLMTDAGRKLYVNTWIYGTLLGCLWV
TIKA
Enzyme 19 Number of Residues 364
Enzyme 19 Molecular Weight 42073
Enzyme 19 Theoretical pI 9.41
Enzyme 19 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 19 General Function Lipid transport and metabolism
Enzyme 19 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 19 Pathways
Enzyme 19 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-31
Enzyme 19 Transmembrane Regions
  • 15-35 61-81 344-364
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 14161585 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9NUQ2 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name PLCE_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1095 bp 
ATGCTGCTGTCCCTGGTGCTCCACACGTACTCCATGCGCTACCTGCTGCCCAGCGTCGTG
CTCCTGGGCACGGCGCCCACCTACGTGTTGGCCTGGGGGGTCTGGCGGCTGCTCTCCGCC
TTCCTGCCCGCCCGCTTCTACCAAGCGCTGGACGACCGGCTCTACTGCGTCTACCAGAGC
ATGGTGCTCTTCTTCTTCGAGAATTACACCGGGGTCCAGATATTGCTATATGGAGATTTG
CCAAAAAATAAAGAAAATATAATATATTTAGCAAATCATCAAAGCACAGTTGACTGGATT
GTTGCTGACATCTTGGCCATCAGGCAGAATGCGCTAGGACATGTGCGCTACGTGCTGAAA
GAAGGGTTAAAATGGCTGCCATTGTATGGGTGTTACTTTGCTCAGCATGGAGGAATCTAT
GTAAAGCGCAGTGCCAAATTTAACGAGAAAGAGATGCGAAACAAGTTGCAGAGCTACGTG
GACGCAGGAACTCCAATGTATCTTGTGATTTTTCCAGAAGGTACAAGGTATAATCCAGAG
CAAACAAAAGTCCTTTCAGCTAGTCAGGCATTTGCTGCCCAACGTGGCCTTGCAGTATTA
AAACATGTGCTAACACCACGAATAAAGGCAACTCACGTTGCTTTTGATTGCATGAAGAAT
TATTTAGATGCAATTTATGATGTTACGGTGGTTTATGAAGGGAAAGACGATGGAGGGCAG
CGAAGAGAGTCACCGACCATGACGGAATTTCTCTGCAAAGAATGTCCAAAAATTCATATT
CACATTGATCGTATCGACAAAAAAGATGTCCCAGAAGAACAAGAACATATGAGAAGATGG
CTGCATGAACGTTTCGAAATCAAAGATAAGATGCTTATAGAATTTTATGAGTCACCAGAT
CCAGAAAGAAGAAAAAGATTTCCTGGGAAAAGTGTTAATTCCAAATTAAGTATCAAGAAG
ACTTTACCATCAATGTTGATCTTAAGTGGTTTGACTGCAGGCATGCTTATGACCGATGCT
GGAAGGAAGCTGTATGTGAACACCTGGATATATGGAACCCTACTTGGCTGCCTGTGGGTT
ACTATTAAAGCATAG
Enzyme 19 GenBank Gene ID AF375789 Link Image
Enzyme 19 GeneCard ID AGPAT5 Link Image
Enzyme 19 GenAtlas ID AGPAT5 Link Image
Enzyme 19 HGNC ID HGNC:20886 Link Image
Enzyme 19 Chromosome Location 8
Enzyme 19 Locus 8p23.1
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 8871
Enzyme 20 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase zeta precursor
Enzyme 20 Synonyms
  1. 1-AGP acyltransferase 6
  2. 1-AGPAT 6
  3. Lysophosphatidic acid acyltransferase zeta
  4. LPAAT-zeta
Enzyme 20 Gene Name AGPAT6
Enzyme 20 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase zeta precursor 
MFLLLPFDSLIVNLLGISLTVLFTLLLVFIIVPAIFGVSFGIRKLYMKSLLKIFAWATLR
MERGAKEKNHQLYKPYTNGIIAKDPTSLEEEIKEIRRSGSSKALDNTPEFELSDIFYFCR
KGMETIMDDEVTKRFSAEELESWNLLSRTNYNFQYISLRLTVLWGLGVLIRYCFLLPLRI
ALAFTGISLLVVGTTVVGYLPNGRFKEFMSKHVHLMCYRICVRALTAIITYHDRENRPRN
GGICVANHTSPIDVIILASDGYYAMVGQVHGGLMGVIQRAMVKACPHVWFERSEVKDRHL
VAKRLTEHVQDKSKLPILIFPEGTCINNTSVMMFKKGSFEIGATVYPVAIKYDPQFGDAF
WNSSKYGMVTYLLRMMTSWAIVCSVWYLPPMTREADEDAVQFANRVKSAIARQGGLVDLL
WDGGLKREKVKDTFKEEQQKLYSKMIVGNHKDRSRS
Enzyme 20 Number of Residues 456
Enzyme 20 Molecular Weight 52072
Enzyme 20 Theoretical pI 9.56
Enzyme 20 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 20 Pathways
Enzyme 20 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • 1-37
Enzyme 20 Transmembrane Regions
  • 156-176 180-200
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein Not Available
Enzyme 20 UniProtKB/Swiss-Prot ID Q86UL3 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name PLCF_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 AF406612 Link Image
Enzyme 20 GeneCard ID AGPAT6 Link Image
Enzyme 20 GenAtlas ID AGPAT6 Link Image
Enzyme 20 HGNC ID HGNC:20880 Link Image
Enzyme 20 Chromosome Location 8
Enzyme 20 Locus 8p11.21
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Li D, Yu L, Wu H, Shan Y, Guo J, Dang Y, Wei Y, Zhao S: Cloning and identification of the human LPAAT-zeta gene, a novel member of the lysophosphatidic acid acyltransferase family. J Hum Genet. 2003;48(8):438-42. Epub 2003 Aug 19. [PubMed Link Image]
  2. 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 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 9821
Enzyme 21 Name Diacylglycerol kinase eta
Enzyme 21 Synonyms
  1. Diglyceride kinase eta
  2. DGK-eta
  3. DAG kinase eta
Enzyme 21 Gene Name DGKH
Enzyme 21 Protein Sequence >Diacylglycerol kinase eta 
MAGAGGQHHPPGAAGGAAAGAGAAVTSAAASAGPGEDSSDSEAEQEGPQKLIRKVSTSGQ
IRTKTSIKEGQLLKQTSSFQRWKKRYFKLRGRTLYYAKDSKSLIFDEVDLSDASVAEAST
KNANNSFTIITPFRRLMLCAENRKEMEDWISSLKSVQTREPYEVAQFNVEHFSGMHNWYA
CSHARPTFCNVCRESLSGVTSHGLSCEVCKFKAHKRCAVRATNNCKWTTLASIGKDIIED
EDGVAMPHQWLEGNLPVSAKCAVCDKTCGSVLRLQDWKCLWCKTMVHTACKDLYHPICPL
GQCKVSIIPPIALNSTDSDGFCRATFSFCVSPLLVFVNSKSGDNQGVKFLRRFKQLLNPA
QVFDLMNGGPHLGLRLFQKFDNFRILVCGGDGSVGWVLSEIDKLNLNKQCQLGVLPLGTG
NDLARVLGWGGSYDDDTQLPQILEKLERASTKMLDRWSIMTYELKLPPKASLLPGPPEAS
EEFYMTIYEDSVATHLTKILNSDEHAVVISSAKTLCETVKDFVAKVEKTYDKTLENAVVA
DAVASKCSVLNEKLEQLLQALHTDSQAAPVLPGLSPLIVEEDAVESSSEESLGESKEQLG
DDVTKPSSQKAVKPREIMLRANSLKKAVRQVIEEAGKVMDDPTVHPCEPANQSSDYDSTE
TDESKEEAKDDGAKESITVKTAPRSPDARASYGHSQTDSVPGPAVAASKENLPVLNTRII
CPGLRAGLAASIAGSSIINKMLLANIDPFGATPFIDPDLDSVDGYSEKCVMNNYFGIGLD
AKISLEFNNKREEHPEKCRSRTKNLMWYGVLGTRELLQRSYKNLEQRVQLECDGQYIPLP
SLQGIAVLNIPSYAGGTNFWGGTKEDDIFAAPSFDDKILEVVAIFDSMQMAVSRVIKLQH
HRIAQCRTVKITIFGDEGVPVQVDGEAWVQPPGIIKIVHKNRAQMLTRDRAFESTLKSWE
DKQKCDSGKPVLRTHLYIHHAIDLATEEVSQMQLCSQAAEELITRICDAATIHCLLEQEL
AHAVNACSHALNKANPRCPESLTRDTATEIAINVKALYNETESLLVGRVPLQLESPHEER
VSNALHSVEVELQKLTEIPWLYYILHPNEDEEPPMDCTKRNNRSTVFRIVPKFKKEKVQK
QKTSSQPVQKWGTEEVAAWLDLLNLGEYKDIFIRHDIRGAELLHLERRDLKDLGIPKVGH
VKRILQGIKELGRSTPQSEV
Enzyme 21 Number of Residues 1220
Enzyme 21 Molecular Weight 134867
Enzyme 21 Theoretical pI Not Available
Enzyme 21 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 21 General Function Not Available
Enzyme 21 Specific Function Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA)
Enzyme 21 Pathways
Enzyme 21 Reactions
  • ATP + diacylglycerol (homo sapiens) <==> ADP + H+ + phosphatidic acid (homo sapiens)
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 29467042 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q86XP1 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name DGKH_HUMAN Link Image
Enzyme 21 PDB ID 1R79 Link Image
Enzyme 21 PDB File Show
Enzyme 21 3D Structure
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence Not Available
Enzyme 21 GenBank Gene ID AB078967 Link Image
Enzyme 21 GeneCard ID Not Available
Enzyme 21 GenAtlas ID DGKH Link Image
Enzyme 21 HGNC ID HGNC:2854 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. Murakami T, Sakane F, Imai S, Houkin K, Kanoh H: Identification and characterization of two splice variants of human diacylglycerol kinase eta. J Biol Chem. 2003 Sep 5;278(36):34364-72. Epub 2003 Jun 16. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 10119
Enzyme 22 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
Enzyme 22 Synonyms
  1. 1- AGP acyltransferase 4
  2. 1-AGPAT 4
  3. Lysophosphatidic acid acyltransferase delta
  4. LPAAT-delta
  5. 1-acylglycerol-3-phosphate O- acyltransferase 4
Enzyme 22 Gene Name AGPAT4
Enzyme 22 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase delta 
MDLAGLLKSQFLCHLVFCYVFIASGLIINTIQLFTLLLWPINKQLFRKINCRLSYCISSQ
LVMLLEWWSGTECTIFTDPRAYLKYGKENAIVVLNHKFEIDFLCGWSLSERFGLLGGSKV
LAKKELAYVPIIGWMWYFTEMVFCSRKWEQDRKTVATSLQHLRDYPEKYFFLIHCEGTRF
TEKKHEISMQVARAKGLPRLKHHLLPRTKGFAITVRSLRNVVSAVYDCTLNFRNNENPTL
LGVLNGKKYHADLYVRRIPLEDIPEDDDECSAWLHKLYQEKDAFQEEYYRTGTFPETPMV
PPRRPWTLVNWLFWASLVLYPFFQFLVSMIRSGSSLTLASFILVFFVASVGVRWMIGVTE
IDKGSAYGNSDSKQKLND
Enzyme 22 Number of Residues 378
Enzyme 22 Molecular Weight 44022
Enzyme 22 Theoretical pI Not Available
Enzyme 22 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 22 General Function Lipid transport and metabolism
Enzyme 22 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 22 Pathways
Enzyme 22 Reactions
  • R total 2 coenzyme A + lysophosphatidic acid (homo sapiens) --> Coenzyme A + phosphatidic acid (homo sapiens)
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 11-31 125-145 307-327 338-358
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 8886005 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q9NRZ5 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name PLCD_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 AF156776 Link Image
Enzyme 22 GeneCard ID Not Available
Enzyme 22 GenAtlas ID AGPAT4 Link Image
Enzyme 22 HGNC ID HGNC:20885 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. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 12909
Enzyme 23 Name 1-acylglycerophosphocholine O-acyltransferase 1
Enzyme 23 Synonyms
  1. Lung- type acyl-CoA:lysophosphatidylcholine acyltransferase 1
  2. Acyltransferase-like 2
  3. Phosphonoformate immuno-associated protein 3
Enzyme 23 Gene Name AYTL2
Enzyme 23 Protein Sequence >1-acylglycerophosphocholine O-acyltransferase 1 
MRLRGCGPRAAPASSAGASDARLLAPPGRNPFVHELRLSALQKAQVALMTLTLFPVRLLV
AAAMMLLAWPLALVASLGSAEKEPEQPPALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGR
QALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQ
DSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPN
KLDTITWTWQGPGALEILWLTLCQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAE
ALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPEKLEKDLDRYSERAR
MKGGEKIGIAEFAASLEVPVSDLLEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDT
IQLAFKMYGAQEDGSVGEGDLSCILKTALGVAELTVTDLFRAIDQEEKGKITFADFHRFA
EMYPAFAEEYLYPDQTHFESCAETSPAPIPNGFCADFSPENSDAGRKPVRKKLD
Enzyme 23 Number of Residues 534
Enzyme 23 Molecular Weight 59152
Enzyme 23 Theoretical pI 5.82
Enzyme 23 GO Classification
Function
  • acyltransferase activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • ion binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 23 General Function Not Available
Enzyme 23 Specific Function Acetyltransferase which mediates the convertion of 1- acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). Has a calcium-independent activity. Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1- palmitoyl LPC as acyl donors and acceptors, respectively. May synthesize phosphatidylcholine in pulmonary surfactant thereby playing a pivotal role in respiratory physiology
Enzyme 23 Pathways
Enzyme 23 Reactions
  • acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine [RN:R01318] ALL_REAC R01318
  • (other) R04480
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 58-78
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 100811832 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q8NF37 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name PCAT1_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 AB244719 Link Image
Enzyme 23 GeneCard ID Q8NF37 Link Image
Enzyme 23 GenAtlas ID LPCAT1 Link Image
Enzyme 23 HGNC ID HGNC:25718 Link Image
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones. DNA Res. 2003 Feb 28;10(1):49-57. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 12910
Enzyme 24 Name Acyltransferase-like 1
Enzyme 24 Synonyms Not Available
Enzyme 24 Gene Name AYTL1
Enzyme 24 Protein Sequence >Acyltransferase-like 1 
MSRCAQAAEVAATVPGAGVGNVGLRPPMVPRQASFFPPPVPNPFVQQTQIGSARRVQIVL
LGIILLPIRVLLVALILLLAWPFAAISTVCCPEKLTHPITGWRRKITQTALKFLGRAMFF
SMGFIVAVKGKIASPLEAPVFVAAPHSTFFDGIACVVAGLPSMVSRNENAQVPLIGRLLR
AVQPVLVSRVDPDSRKNTINEIIKRTTSGGEWPQILVFPEGTCTNRSCLITFKPGAFIPG
VPVQPVLLRYPNKLDTVTWTWQGYTFIQLCMLTFCQLFTKVEVEFMPVQVPNDEEKNDPV
LFANKVRNLMAEALGIPVTDHTYEDCRLMISAGQLTLPMEAGLVEFTKISRKLKLDWDGV
RKHLDEYASIASSSKGGRIGIEEFAKYLKLPVSDVLRQLFALFDRNHDGSIDFREYVIGL
AVLCNPSNTEEIIQVAFKLFDVDEDGYITEEEFSTILQASLGVPDLDVSGLFKEIAQGDS
ISYEEFKSFALKHPEYAKIFTTYLDLQTCHVFSLPKEVQTTPSTASNKVSPEKHEESTSD
KKDD
Enzyme 24 Number of Residues 544
Enzyme 24 Molecular Weight 60208
Enzyme 24 Theoretical pI 6.51
Enzyme 24 GO Classification
Function
  • acyltransferase activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • ion binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 24 General Function Not Available
Enzyme 24 Specific Function Probable acetyltransferase
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • 58-78
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 34364994 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q7L5N7 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name AYTL1_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 BX641069 Link Image
Enzyme 24 GeneCard ID Q7L5N7 Link Image
Enzyme 24 GenAtlas ID LPCAT2 Link Image
Enzyme 24 HGNC ID HGNC:26032 Link Image
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References Not Available
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 12931
Enzyme 25 Name Lysocardiolipin acyltransferase
Enzyme 25 Synonyms
  1. Acyl- CoA:lysocardiolipin acyltransferase 1
  2. 1-AGP acyltransferase 8
  3. 1- AGPAT 8
Enzyme 25 Gene Name LYCAT
Enzyme 25 Protein Sequence >Lysocardiolipin acyltransferase 
MHSRGREIVVLLNPWSINEAVSSYCTYFIKQDSKSFGIMVSWKGIYFILTLFWGSFFGSI
FMLSPFLPLMFVNPSWYRWINNRLVATWLTLPVALLETMFGVKVIITGDAFVPGERSVII
MNHRTRMDWMFLWNCLMRYSYLRLEKICLKASLKGVPGFGWAMQAAAYIFIHRKWKDDKS
HFEDMIDYFCDIHEPLQLLIFPEGTDLTENSKSRSNAFAEKNGLQKYEYVLHPRTTGFTF
VVDRLREGKNLDAVHDITVAYPHNIPQSEKHLLQGDFPREIHFHVHRYPIDTLPTSKEDL
QLWCHKRWEEKEERLRSFYQGEKNFYFTGQSVIPPCKSELRVLVVKLLSILYWTLFSPAM
CLLIYLYSLVKWYFIITIVIFVLQERIFGGLEIIELACYRLLHKQPHLNSKKNE
Enzyme 25 Number of Residues 414
Enzyme 25 Molecular Weight 48921
Enzyme 25 Theoretical pI 8.80
Enzyme 25 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 25 General Function Lipid transport and metabolism
Enzyme 25 Specific Function Acyl-CoA:lysocardiolipin acyltransferase. Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors. Acts as a remodeling enzyme for cardiolipin, a major membrane polyglycerophospholipid. Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) with a relatively low activity
Enzyme 25 Pathways
Enzyme 25 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241] ALL_REAC R02241 > R02760
  • (other) R04361
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • 47-67 86-106 340-360 362-382
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 37182526 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q6UWP7 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name LYCAT_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 AY358702 Link Image
Enzyme 25 GeneCard ID Q6UWP7 Link Image
Enzyme 25 GenAtlas ID LYCAT Link Image
Enzyme 25 HGNC ID HGNC:26756 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. 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 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 12932
Enzyme 26 Name Lysophosphatidic acid receptor Edg-7
Enzyme 26 Synonyms
  1. LPA receptor 3
  2. LPA-3
Enzyme 26 Gene Name EDG7
Enzyme 26 Protein Sequence >Lysophosphatidic acid receptor Edg-7 
MNECHYDKHMDFFYNRSNTDTVDDWTGTKLVIVLCVGTFFCLFIFFSNSLVIAAVIKNRK
FHFPFYYLLANLAAADFFAGIAYVFLMFNTGPVSKTLTVNRWFLRQGLLDSSLTASLTNL
LVIAVERHMSIMRMRVHSNLTKKRVTLLILLVWAIAIFMGAVPTLGWNCLCNISACSSLA
PIYSRSYLVFWTVSNLMAFLIMVVVYLRIYVYVKRKTNVLSPHTSGSISRRRTPMKLMKT
VMTVLGAFVVCWTPGLVVLLLDGLNCRQCGVQHVKRWFLLLALLNSVVNPIIYSYKDEDM
YGTMKKMICCFSQENPERRPSRIPSTVLSRSDTGSQYIEDSISQGAVCNKSTS
Enzyme 26 Number of Residues 353
Enzyme 26 Molecular Weight 40129
Enzyme 26 Theoretical pI 9.75
Enzyme 26 GO Classification
Function
  • G-protein coupled receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 26 General Function Not Available
Enzyme 26 Specific Function Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. May play a role in the development of ovarian cancer. Seems to be coupled to the G(i)/G(o) and G(q) families of heteromeric G proteins
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • 32-52 68-88 102-124 147-167 187-207 241-261 277-297
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 5922725 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q9UBY5 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name EDG7_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence Not Available
Enzyme 26 GenBank Gene ID AF127138 Link Image
Enzyme 26 GeneCard ID Q9UBY5 Link Image
Enzyme 26 GenAtlas ID LPAR3 Link Image
Enzyme 26 HGNC ID HGNC:14298 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. Bandoh K, Aoki J, Hosono H, Kobayashi S, Kobayashi T, Murakami-Murofushi K, Tsujimoto M, Arai H, Inoue K: Molecular cloning and characterization of a novel human G-protein-coupled receptor, EDG7, for lysophosphatidic acid. J Biol Chem. 1999 Sep 24;274(39):27776-85. [PubMed Link Image]
  2. Im DS, Heise CE, Harding MA, George SR, O'Dowd BF, Theodorescu D, Lynch KR: Molecular cloning and characterization of a lysophosphatidic acid receptor, Edg-7, expressed in prostate. Mol Pharmacol. 2000 Apr;57(4):753-9. [PubMed Link Image]
  3. Contos JJ, Ishii I, Chun J: Lysophosphatidic acid receptors. Mol Pharmacol. 2000 Dec;58(6):1188-96. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 12933
Enzyme 27 Name Lysophosphatidic acid receptor 4
Enzyme 27 Synonyms
  1. LPA receptor 4
  2. LPA-4
  3. P2Y purinoceptor 9
  4. P2Y9
  5. Purinergic receptor 9
  6. G-protein coupled receptor 23
  7. P2Y5-like receptor
Enzyme 27 Gene Name GPR23
Enzyme 27 Protein Sequence >Lysophosphatidic acid receptor 4 
MGDRRFIDFQFQDSNSSLRPRLGNATANNTCIVDDSFKYNLNGAVYSVVFILGLITNSVS
LFVFCFRMKMRSETAIFITNLAVSDLLFVCTLPFKIFYNFNRHWPFGDTLCKISGTAFLT
NIYGSMLFLTCISVDRFLAIVYPFRSRTIRTRRNSAIVCAGVWILVLSGGISASLFSTTN
VNNATTTCFEGFSKRVWKTYLSKITIFIEVVGFIIPLILNVSCSSVVLRTLRKPATLSQI
GTNKKKVLKMITVHMAVFVVCFVPYNSVLFLYALVRSQAITNCFLERFAKIMYPITLCLA
TLNCCFDPFIYYFTLESFQKSFYINAHIRMESLFKTETPLTTKPSLPAIQEEVSDQTTNN
GGELMLESTF
Enzyme 27 Number of Residues 370
Enzyme 27 Molecular Weight 41896
Enzyme 27 Theoretical pI 9.28
Enzyme 27 GO Classification
Function
  • G-protein coupled receptor activity
  • nucleotide receptor activity, G-protein coupled
  • purinergic nucleotide receptor activity, G-protein coupled
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 27 General Function Not Available
Enzyme 27 Specific Function Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Transduces a signal by increasing the intracellular calcium ions and by stimulating adenylyl cyclase activity. The rank order of potency for agonists of this receptor is 1-oleoyl- > 1-stearoyl- > 1-palmitoyl- > 1-myristoyl- > 1- alkyl- > 1-alkenyl-LPA
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • 44-64 74-94 113-133 156-176 204-224 255-275 295-315
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 1753101 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q99677 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name P2RY9_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence Not Available
Enzyme 27 GenBank Gene ID U66578 Link Image
Enzyme 27 GeneCard ID Q99677 Link Image
Enzyme 27 GenAtlas ID LPAR4 Link Image
Enzyme 27 HGNC ID HGNC:4478 Link Image
Enzyme 27 Chromosome Location Not Available
Enzyme 27 Locus Not Available
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. O'Dowd BF, Nguyen T, Jung BP, Marchese A, Cheng R, Heng HH, Kolakowski LF Jr, Lynch KR, George SR: Cloning and chromosomal mapping of four putative novel human G-protein-coupled receptor genes. Gene. 1997 Mar 10;187(1):75-81. [PubMed Link Image]
  2. Janssens R, Boeynaems JM, Godart M, Communi D: Cloning of a human heptahelical receptor closely related to the P2Y5 receptor. Biochem Biophys Res Commun. 1997 Jul 9;236(1):106-12. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 12934
Enzyme 28 Name Probable G-protein coupled receptor 92
Enzyme 28 Synonyms Not Available
Enzyme 28 Gene Name GPR92
Enzyme 28 Protein Sequence >Probable G-protein coupled receptor 92 
MLANSSSTNSSVLPCPDYRPTHRLHLVVYSLVLAAGLPLNALALWVFLRALRVHSVVSVY
MCNLAASDLLFTLSLPVRLSYYALHHWPFPDLLCQTTGAIFQMNMYGSCIFLMLINVDRY
AAIVHPLRLRHLRRPRVARLLCLGVWALILVFAVPAARVHRPSRCRYRDLEVRLCFESFS
DELWKGRLLPLVLLAEALGFLLPLAAVVYSSGRVFWTLARPDATQSQRRRKTVRLLLANL
VIFLLCFVPYNSTLAVYGLLRSKLVAASVPARDRVRGVLMVMVLLAGANCVLDPLVYYFS
AEGFRNTLRGLGTPHRARTSATNGTRAALAQSERSAVTTDATRPDAASQGLLRPSDSHSL
SSFTQCPQDSAL
Enzyme 28 Number of Residues 372
Enzyme 28 Molecular Weight 41347
Enzyme 28 Theoretical pI 10.44
Enzyme 28 GO Classification
Function
  • G-protein coupled receptor activity
  • nucleotide receptor activity, G-protein coupled
  • purinergic nucleotide receptor activity, G-protein coupled
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function Orphan receptor
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • 27-47 56-76 97-117 137-157 188-208 240-260 277-297
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 9843746 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID Q9H1C0 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name GPR92_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence Not Available
Enzyme 28 GenBank Gene ID AJ272207 Link Image
Enzyme 28 GeneCard ID Q9H1C0 Link Image
Enzyme 28 GenAtlas ID LPAR5 Link Image
Enzyme 28 HGNC ID HGNC:13307 Link Image
Enzyme 28 Chromosome Location Not Available
Enzyme 28 Locus Not Available
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Autosomal dominant hypophosphataemic rickets is associated with mutations in FGF23. Nat Genet. 2000 Nov;26(3):345-8. [PubMed Link Image]
  2. Lee DK, Nguyen T, Lynch KR, Cheng R, Vanti WB, Arkhitko O, Lewis T, Evans JF, George SR, O'Dowd BF: Discovery and mapping of ten novel G protein-coupled receptor genes. Gene. 2001 Sep 5;275(1):83-91. [PubMed Link Image]
  3. Takeda S, Kadowaki S, Haga T, Takaesu H, Mitaku S: Identification of G protein-coupled receptor genes from the human genome sequence. FEBS Lett. 2002 Jun 5;520(1-3):97-101. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 12935
Enzyme 29 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase eta
Enzyme 29 Synonyms
  1. 1- AGP acyltransferase 7
  2. 1-AGPAT 7
  3. Lysophosphatidic acid acyltransferase eta
  4. LPAAT-eta
  5. Acyltransferase-like 3
Enzyme 29 Gene Name AGPAT7
Enzyme 29 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase eta 
MSQGSPGDWAPLDPTPGPPASPNPFVHELHLSRLQRVKFCLLGALLAPIRVLLAFIVLFL
LWPFAWLQVAGLSEEQLQEPITGWRKTVCHNGVLGLSRLLFFLLGFLRIRVRGQRASRLQ
APVLVAAPHSTFFDPIVLLPCDLPKVVSRAENLSVPVIGALLRFNQAILVSRHDPASRRR
VVEEVRRRATSGGKWPQVLFFPEGTCSNKKALLKFKPGAFIAGVPVQPVLIRYPNSLDTT
SWAWRGPGVLKVLWLTASQPCSIVDVEFLPVYHPSPEESRDPTLYANNVQRVMAQALGIP
ATECEFVGSLPVIVVGRLKVALEPQLWELGKVLRKAGLSAGYVDAGAEPGRSRMISQEEF
ARQLQLSDPQTVAGAFGYFQQDTKGLVDFRDVALALAALDGGRSLEELTRLAFELFAEEQ
AEGPNRLLYKDGFSTILHLLLGSPHPAATALHAELCQAGSSQGLSLCQFQNFSLHDPLYG
KLFSTYLRPPHTSRGTSQTPNASSPGNPTALANGTVQAPKQKGD
Enzyme 29 Number of Residues 524
Enzyme 29 Molecular Weight 57220
Enzyme 29 Theoretical pI 9.24
Enzyme 29 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 29 General Function Lipid transport and metabolism
Enzyme 29 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 29 Pathways
Enzyme 29 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241] ALL_REAC R02241 > R02760
  • (other) R04361
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • 40-62 87-107
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 52222822 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q643R3 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name PLCG_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence Not Available
Enzyme 29 GenBank Gene ID AY734233 Link Image
Enzyme 29 GeneCard ID Q643R3 Link Image
Enzyme 29 GenAtlas ID AGPAT7 Link Image
Enzyme 29 HGNC ID HGNC:30059 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 12936
Enzyme 30 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase theta
Enzyme 30 Synonyms
  1. Lysophosphatidic acid acyltransferase theta
  2. LPAAT-theta
  3. Acyl- CoA:glycerol-3-phosphate acyltransferase 3
  4. hGPAT3
  5. Lung cancer metastasis-associated protein 1
  6. MAG-1
Enzyme 30 Gene Name GPAT3
Enzyme 30 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase theta 
MEGAELAGKILSTWLTLVLGFILLPSVFGVSLGISEIYMKILVKTLEWATIRIEKGTPKE
SILKNSASVGIIQRDESPMEKGLSGLRGRDFELSDVFYFSKKGLEAIVEDEVTQRFSSEE
LVSWNLLTRTNVNFQYISLRLTMVWVLGVIVRYCVLLPLRVTLAFIGISLLVIGTTLVGQ
LPDSSLKNWLSELVHLTCCRICVRALSGTIHYHNKQYRPQKGGICVANHTSPIDVLILTT
DGCYAMVGQVHGGLMGIIQRAMVKACPHVWFERSEMKDRHLVTKRLKEHIADKKKLPILI
FPEGTCINNTSVMMFKKGSFEIGGTIHPVAIKYNPQFGDAFWNSSKYNMVSYLLRMMTSW
AIVCDVWYMPPMTREEGEDAVQFANRVKSAIAIQGGLTELPWDGGLKRAKVKDIFKEEQQ
KNYSKMIVGNGSLS
Enzyme 30 Number of Residues 434
Enzyme 30 Molecular Weight 48706
Enzyme 30 Theoretical pI 9.15
Enzyme 30 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 30 General Function Not Available
Enzyme 30 Specific Function Endoplasmic reticulum acyl-CoA:glycerol-3-phosphate acyltransferase, which catalyzes the first step during de novo synthesis of triacylglycerol. Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Overexpression activates the mTOR pathway
Enzyme 30 Pathways
Enzyme 30 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241] ALL_REAC R02241 > R02760
  • (other) R04361
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • 14-34 137-157 161-181
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 84314125 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q53EU6 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name PLCH_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence Not Available
Enzyme 30 GenBank Gene ID DQ324782 Link Image
Enzyme 30 GeneCard ID Q53EU6 Link Image
Enzyme 30 GenAtlas ID AGPAT9 Link Image
Enzyme 30 HGNC ID HGNC:28157 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. 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 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 12937
Enzyme 31 Name Lysophosphatidic acid phosphatase type 6 precursor
Enzyme 31 Synonyms
  1. Acid phosphatase 6, lysophosphatidic
  2. Acid phosphatase-like protein 1
  3. PACPL1
Enzyme 31 Gene Name ACP6
Enzyme 31 Protein Sequence >Lysophosphatidic acid phosphatase type 6 precursor 
MITGVFSMRLWTPVGVLTSLAYCLHQRRVALAELQEADGQCPVDRSLLKLKMVQVVFRHG
ARSPLKPLPLEEQVEWNPQLLEVPPQTQFDYTVTNLAGGPKPYSPYDSQYHETTLKGGMF
AGQLTKVGMQQMFALGERLRKNYVEDIPFLSPTFNPQEVFIRSTNIFRNLESTRCLLAGL
FQCQKEGPIIIHTDEADSEVLYPNYQSCWSLRQRTRGRRQTASLQPGISEDLKKVKDRMG
IDSSDKVDFFILLDNVAAEQAHNLPSCPMLKRFARMIEQRAVDTSLYILPKEDRESLQMA
VGPFLHILESNLLKAMDSATAPDKIRKLYLYAAHDVTFIPLLMTLGIFDHKWPPFAVDLT
MELYQHLESKEWFVQLYYHGKEQVPRGCPDGLCPLDMFLNAMSVYTLSPEKYHALCSQTQ
VMEVGNEE
Enzyme 31 Number of Residues 428
Enzyme 31 Molecular Weight 48887
Enzyme 31 Theoretical pI 6.44
Enzyme 31 GO Classification
Function
  • acid phosphatase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
—
Component
—
Enzyme 31 General Function Not Available
Enzyme 31 Specific Function Hydrolyzes lysophosphatidic acid to monoacylglycerol
Enzyme 31 Pathways
Enzyme 31 Reactions
  • a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626] ALL_REAC R00626 > R00548 R03024
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • 1-32
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 6691475 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q9NPH0 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name PPA6_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence Not Available
Enzyme 31 GenBank Gene ID AB031478 Link Image
Enzyme 31 GeneCard ID Q9NPH0 Link Image
Enzyme 31 GenAtlas ID ACP6 Link Image
Enzyme 31 HGNC ID HGNC:29609 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. Hiroyama M, Takenawa T: Isolation of a cDNA encoding human lysophosphatidic acid phosphatase that is involved in the regulation of mitochondrial lipid biosynthesis. J Biol Chem. 1999 Oct 8;274(41):29172-80. [PubMed Link Image]
  2. Takayama I, Daigo Y, Ward SM, Sanders KM, Walker RL, Horowitz B, Yamanaka T, Fujino MA: Novel human and mouse genes encoding an acid phosphatase family member and its downregulation in W/W(V) mouse jejunum. Gut. 2002 Jun;50(6):790-6. [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]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 12938
Enzyme 32 Name P2Y purinoceptor 5
Enzyme 32 Synonyms
  1. P2Y5
  2. Purinergic receptor 5
  3. RB intron encoded G-protein coupled receptor
Enzyme 32 Gene Name P2RY5
Enzyme 32 Protein Sequence >P2Y purinoceptor 5 
MVSVNSSHCFYNDSFKYTLYGCMFSMVFVLGLISNCVAIYIFICVLKVRNETTTYMINLA
MSDLLFVFTLPFRIFYFTTRNWPFGDLLCKISVMLFYTNMYGSILFLTCISVDRFLAIVY
PFKSKTLRTKRNAKIVCTGVWLTVIGGSAPAVFVQSTHSQGNNASEACFENFPEATWKTY
LSRIVIFIEIVGFFIPLILNVTCSSMVLKTLTKPVTLSRSKINKTKVLKMIFVHLIIFCF
CFVPYNINLILYSLVRTQTFVNCSVVAAVRTMYPITLCIAVSNCCFDPIVYYFTSDTIQN
SIKMKNWSVRRSDFRFSEVHGAENFIQHNLQTLKSKIFDNESAA
Enzyme 32 Number of Residues 344
Enzyme 32 Molecular Weight 39392
Enzyme 32 Theoretical pI 9.16
Enzyme 32 GO Classification
Function
  • G-protein coupled receptor activity
  • nucleotide receptor activity, G-protein coupled
  • purinergic nucleotide receptor activity, G-protein coupled
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 32 General Function Not Available
Enzyme 32 Specific Function Not Available
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • 20-46 56-79 93-112 134-154 182-209 228-253 273-292
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 17466994 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID P43657 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name P2RY5_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 L78805 Link Image
Enzyme 32 GeneCard ID P43657 Link Image
Enzyme 32 GenAtlas ID P2RY5 Link Image
Enzyme 32 HGNC ID HGNC:15520 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. Herzog H, Darby K, Hort YJ, Shine J: Intron 17 of the human retinoblastoma susceptibility gene encodes an actively transcribed G protein-coupled receptor gene. Genome Res. 1996 Sep;6(9):858-61. [PubMed Link Image]
  2. Toguchida J, McGee TL, Paterson JC, Eagle JR, Tucker S, Yandell DW, Dryja TP: Complete genomic sequence of the human retinoblastoma susceptibility gene. Genomics. 1993 Sep;17(3):535-43. [PubMed Link Image]
  3. Adrian K, Bernhard MK, Breitinger HG, Ogilvie A: Expression of purinergic receptors (ionotropic P2X1-7 and metabotropic P2Y1-11) during myeloid differentiation of HL60 cells. Biochim Biophys Acta. 2000 Jun 21;1492(1):127-38. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 12939
Enzyme 33 Name Lipase member H precursor
Enzyme 33 Synonyms
  1. Membrane-associated phosphatidic acid-selective phospholipase A1-alpha
  2. mPA-PLA1 alpha
  3. LPD lipase-related protein
  4. Phospholipase A1 member B
Enzyme 33 Gene Name LIPH
Enzyme 33 Protein Sequence >Lipase member H precursor 
MLRFYLFISLLCLSRSDAEETCPSFTRLSFHSAVVGTGLNVRLMLYTRKNLTCAQTINSS
AFGNLNVTKKTTFIVHGFRPTGSPPVWMDDLVKGLLSVEDMNVVVVDWNRGATTLIYTHA
SSKTRKVAMVLKEFIDQMLAEGASLDDIYMIGVSLGAHISGFVGEMYDGWLGRITGLDPA
GPLFNGKPHQDRLDPSDAQFVDVIHSDTDALGYKEPLGNIDFYPNGGLDQPGCPKTILGG
FQYFKCDHQRSVYLYLSSLRESCTITAYPCDSYQDYRNGKCVSCGTSQKESCPLLGYYAD
NWKDHLRGKDPPMTKAFFDTAEESPFCMYHYFVDIITWNKNVRRGDITIKLRDKAGNTTE
SKINHEPTTFQKYHQVSLLARFNQDLDKVAAISLMFSTGSLIGPRYKLRILRMKLRSLAH
PERPQLCRYDLVLMENVETVFQPILCPELQL
Enzyme 33 Number of Residues 451
Enzyme 33 Molecular Weight 50860
Enzyme 33 Theoretical pI 7.46
Enzyme 33 GO Classification
Function
  • catalytic activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 33 General Function Not Available
Enzyme 33 Specific Function Hydrolyzes specifically phosphatidic acid (PA) to produce lysophosphatidic acid (LPA)
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions Not Available
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • 1-18
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 18031732 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q8WWY8 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name LIPH_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 AY036912 Link Image
Enzyme 33 GeneCard ID Q8WWY8 Link Image
Enzyme 33 GenAtlas ID LIPH Link Image
Enzyme 33 HGNC ID HGNC:18483 Link Image
Enzyme 33 Chromosome Location Not Available
Enzyme 33 Locus Not Available
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Jin W, Broedl UC, Monajemi H, Glick JM, Rader DJ: Lipase H, a new member of the triglyceride lipase family synthesized by the intestine. Genomics. 2002 Sep;80(3):268-73. [PubMed Link Image]
  2. Wen XY, Hegele RA, Wang J, Wang DY, Cheung J, Wilson M, Yahyapour M, Bai Y, Zhuang L, Skaug J, Young TK, Connelly PW, Koop BF, Tsui LC, Stewart AK: Identification of a novel lipase gene mutated in lpd mice with hypertriglyceridemia and associated with dyslipidemia in humans. Hum Mol Genet. 2003 May 15;12(10):1131-43. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 12940
Enzyme 34 Name Lipase member I precursor
Enzyme 34 Synonyms
  1. Membrane-associated phosphatidic acid-selective phospholipase A1-beta
  2. mPA-PLA1 beta
  3. LPD lipase
  4. Cancer/testis antigen 17
  5. CT17
Enzyme 34 Gene Name LIPI
Enzyme 34 Protein Sequence >Lipase member I precursor 
MRVYIFLCLMCWVRSDNKRPCLEFSQLSVKDSFRDLFIPRIETILMMYTRNNLNCAEPLF
EQNNSLNVNFNTQKKTVWLIHGYRPVGSIPLWLQNFVRILLNEEDMNVIVVDWSRGATTF
IYNRAVKNTRKVAVSLSVHIKNLLKHGASLDNFHFIGVSLGAHISGFVGKIFHGQLGRIT
GLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSNGLGIQEPLGHIDFYPNGGNKQPGCPK
SIFSGIQFIKCNHQRAVHLFMASLETNCNFISFPCRSYKDYKTSLCVDCDCFKEKSCPRL
GYQAKLFKGVLKERMEGRPLRTTVFLDTSGTYPFCTYYFVLSIIVPDKTMMDGSFSFKLL
NQLGMIEEPRLYEKNKPFYKLQEVKILAQFYNDFVNISSIGLTYFQSSNLQCSTCTYKIQ
RLMLKSLTYPERPPLCRYNIVLKDREEVFLNPNTCTPKNT
Enzyme 34 Number of Residues 460
Enzyme 34 Molecular Weight 52992
Enzyme 34 Theoretical pI 9.28
Enzyme 34 GO Classification
Function
  • catalytic activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 34 General Function Not Available
Enzyme 34 Specific Function Hydrolyzes specifically phosphatidic acid (PA) to produce lysophosphatidic acid (LPA)
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions Not Available
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • 1-15
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 37781763 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q6XZB0 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name LIPI_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 AY197607 Link Image
Enzyme 34 GeneCard ID Q6XZB0 Link Image
Enzyme 34 GenAtlas ID LIPI Link Image
Enzyme 34 HGNC ID HGNC:18821 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. Wen XY, Hegele RA, Wang J, Wang DY, Cheung J, Wilson M, Yahyapour M, Bai Y, Zhuang L, Skaug J, Young TK, Connelly PW, Koop BF, Tsui LC, Stewart AK: Identification of a novel lipase gene mutated in lpd mice with hypertriglyceridemia and associated with dyslipidemia in humans. Hum Mol Genet. 2003 May 15;12(10):1131-43. [PubMed Link Image]
  2. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 12941
Enzyme 35 Name Plasticity related gene 1
Enzyme 35 Synonyms
  1. Plasticity related gene 1, isoform CRA_b
  2. PRG1
  3. Lipid phosphate phosphatase-related protein type 4
Enzyme 35 Gene Name LPPR4
Enzyme 35 Protein Sequence >Plasticity related gene 1 
MQRAGSSGGRGECDISGAGRLGLEEAARLSCAVHTSPGGGRRPGQAAGMSAKERPKGKVI
KDSVTLLPCFYFVELPILASSVVSLYFLELTDVFKPVHSGFSCYDRSLSMPYIEPTQEAI
PFLMLLSLAFAGPAITIMVGEGILYCCLSKRRNGVGLEPNINAGGCNFNSFLRRAVRFVG
VHVFGLCSTALITDIIQLSTGYQAPYFLTVCKPNYTSLNVSCKENSYIVEDICSGSDLTV
INSGRKSFPSQHATLAAFAAVYVSMYFNSTLTDSSKLLKPLLVFTFIICGIICGLTRITQ
YKNHPVDVYCGFLIGGGIALYLGLYAVGNFLPSDESMFQHRDALRSLTDLNQDPNRLLSA
KNGSSSDGIAHTEGILNRNHRDASSLTNLKRANADVEIITPRSPMGKENMVTFSNTLPRA
NTPSVEDPVRRNASIHASMDSARSKQLLTQWKNKNESRKLSLQVIEPEPGQSPPRSIEMR
SSSEPSRVGVNGDHHGPGNQYLKIQPGAVPGCNNSMPGGPRVSIQSRPGSSQLVHIPEET
QENISTSPKSSSARAKWLKAAEKTVACNRSNSQPRIMQVIAMSKQQGVLQSSPKNTEGST
VSCTGSIRYKTLTDHEPSGIVRVEAHPENNRPIIQIPSTEGEGSGSWKWKAPEKGSLRQT
YELNDLNRDSESCESLKDSFGSGDRKRSNIDSNEHHHHGITTIRVTPVEGSEIGSETLSI
SSSRDSTLRRKGNIILIPERSNSPENTRNIFYKGTSPTRAYKD
Enzyme 35 Number of Residues 763
Enzyme 35 Molecular Weight 82984
Enzyme 35 Theoretical pI 8.89
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 31580551 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q7Z2D5 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name Q7Z2D5_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 AF541281 Link Image
Enzyme 35 GeneCard ID Q7Z2D5 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
  1. Brauer AU, Savaskan NE, Kuhn H, Prehn S, Ninnemann O, Nitsch R: A new phospholipid phosphatase, PRG-1, is involved in axon growth and regenerative sprouting. Nat Neurosci. 2003 Jun;6(6):572-8. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 14426
Enzyme 36 Name Acylglycerol kinase, mitochondrial precursor
Enzyme 36 Synonyms
  1. hAGK
  2. Multiple substrate lipid kinase
  3. Multi- substrate lipid kinase
  4. MuLK
  5. HsMuLK
Enzyme 36 Gene Name AGK
Enzyme 36 Protein Sequence >Acylglycerol kinase, mitochondrial precursor 
MTVFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQV
KKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTIVKTDYEGQAKKLLELMENTDVII
VAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATL
AIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFST
LKEWPQTHQASISYTGPTERPPNEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSP
EVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHV
EGTECLQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSP
TQ
Enzyme 36 Number of Residues 422
Enzyme 36 Molecular Weight 47138
Enzyme 36 Theoretical pI 8.21
Enzyme 36 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 36 General Function Lipid transport and metabolism
Enzyme 36 Specific Function Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively. Does not phosphorylate sphingosine. Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth
Enzyme 36 Pathways
Enzyme 36 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240] ALL_REAC R02240
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • 1-31
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 8250243 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q53H12 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name AGK_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >1269 bp 
ATGACGGTGTTCTTTAAAACGCTTCGAAATCACTGGAAGAAAACTACAGCTGGGCTCTGC
CTGCTGACCTGGGGAGGCCATTGGCTCTATGGAAAACACTGTGATAACCTCCTAAGGAGA
GCAGCCTGTCAAGAAGCTCAGGTGTTTGGCAATCAACTCATTCCTCCCAATGCACAAGTG
AAGAAGGCCACTGTTTTTCTCAATCCTGCAGCTTGCAAAGGAAAAGCCAGGACTCTATTT
GAAAAAAATGCTGCCCCGATTTTACATTTATCTGGCATGGATGTGACTATTGTTAAGACA
GATTATGAGGGACAAGCCAAGAAACTCCTGGAACTGATGGAAAACACGGATGTGATCATT
GTTGCAGGAGGAGATGGGACACTGCAGGAGGTTGTTACTGGTGTTCTTCGACGAACAGAT
GAGGCTACCTTCAGTAAGATTCCCATTGGATTTATCCCACTGGGAGAGACCAGTAGTTTG
AGTCATACCCTCTTTGCCGAAAGTGGAAACAAAGTCCAACATATTACTGATGCCACACTT
GCCATTGTGAAAGGAGAGACAGTTCCACTTGATGTCTTGCAGATCAAGGGTGAAAAGGAA
CAGCCTGTATTTGCAATGACCGGCCTTCGATGGGGATCTTTCAGAGATGCTGGCGTCAAA
GTTAGCAAGTACTGGTATCTTGGGCCTCTAAAAATCAAAGCAGCCCACTTTTTCAGCACT
CTTAAGGAGTGGCCTCAGACTCATCAAGCCTCTATCTCATACACGGGACCTACAGAGAGA
CCTCCCAATGAACCAGAGGAGACCCCTGTACAAAGGCCTTCTTTGTACAGGAGAATATTA
CGAAGGCTTGCGTCCTACTGGGCACAACCACAGGATGCCCTTTCCCAAGAGGTGAGCCCG
GAGGTCTGGAAAGATGTGCAGCTGTCCACCATTGAACTGTCCATCACAACACGGAATAAT
CAGCTTGACCCGACAAGCAAAGAAGATTTTCTGAATATCTGCATTGAACCTGACACCATC
AGCAAAGGAGACTTTATAACTATAGGAAGTCGAAAGGTGAGAAACCCCAAGCTGCACGTG
GAGGGCACGGAGTGTCTCCAAGCCAGCCAGTGCACTTTGCTTATCCCGGAGGGAGCAGGG
GGCTCTTTTAGCATTGACAGTGAGGAGTATGAAGCGATGCCTGTGGAGGTGAAACTGCTC
CCCAGGAAGCTGCAGTTCTTCTGTGATCCTAGGAAGAGAGAACAGATGCTCACAAGCCCC
ACCCAGTGA
Enzyme 36 GenBank Gene ID AJ278150 Link Image
Enzyme 36 GeneCard ID Q53H12 Link Image
Enzyme 36 GenAtlas ID AGK Link Image
Enzyme 36 HGNC ID HGNC:21869 Link Image
Enzyme 36 Chromosome Location Not Available
Enzyme 36 Locus Not Available
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. 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 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 15207
Enzyme 37 Name Phospholipase D1 variant (Fragment)
Enzyme 37 Synonyms Not Available
Enzyme 37 Gene Name Not Available
Enzyme 37 Protein Sequence >Phospholipase D1 variant (Fragment) 
ANAQVLAAPSPCSPFAFTLSKVNMSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEG
EEVDYDVSPSDPKIQEVYIPFSAIYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRV
PSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEP
REMPSLPRSSENMIREEQFLGRRKQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDL
GPKGIEGMIMKRSGGHRIPGLNCCGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLL
VDKEFKIKVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKD
HRFGSYAAIQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGN
RWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSST
VYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAM
ESMESLRLKDKNEPVQNLPIQKSIDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSI
SSIDSTSNTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPR
MPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLLPKSQTTAHELRYQVP
GSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFN
KIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGEN
SILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANIN
DRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCFRVVLGYLDDPSEDIQ
DPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPVLAKEDPIRAEE
ELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
Enzyme 37 Number of Residues 1059
Enzyme 37 Molecular Weight 122010
Enzyme 37 Theoretical pI 9.03
Enzyme 37 GO Classification
Function
  • catalytic activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • metabolism
  • physiological process
  • signal transduction
Component
—
Enzyme 37 General Function Lipid transport and metabolism
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 62089400 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q59EA4 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name Q59EA4_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >3182 bp 
CCGCCAACGCGCAGGTGCTAGCGGCCCCTTCGCCCTGCAGCCCCTTTGCTTTTACTCTGT
CCAAAGTTAACATGTCACTGAAAAACGAGCCACGGGTAAATACCTCTGCACTGCAGAAAA
TTGCTGCTGACATGAGTAATATCATAGAAAATCTGGACACGCGGGAACTCCACTTTGAGG
GAGAGGAGGTAGACTACGACGTGTCTCCCAGCGATCCCAAGATACAAGAAGTGTATATCC
CTTTCTCTGCTATTTATAACACTCAAGGATTTAAGGAGCCTAATATACAGACGTATCTCT
CCGGCTGTCCAATAAAAGCACAAGTTCTGGAAGTGGAACGCTTCACATCTACAACAAGGG
TACCAAGTATTAATCTTTACACTATTGAATTAACACATGGGGAATTTAAATGGCAAGTTA
AGAGGAAATTCAAGCATTTTCAAGAATTTCACAGAGAGCTGCTCAAGTACAAAGCCTTTA
TCCGCATCCCCATTCCCACTAGAAGACACACGTTTAGGAGGCAAAACGTCAGAGAGGAGC
CTCGAGAGATGCCCAGTTTGCCCCGTTCATCTGAAAACATGATAAGAGAAGAACAATTCC
TTGGTAGAAGAAAACAACTGGAAGATTACTTGACAAAGATACTAAAAATGCCCATGTATA
GAAACTATCATGCCACAACAGAGTTTCTTGATATAAGCCAGCTGTCTTTCATCCATGATT
TGGGACCAAAGGGCATAGAAGGTATGATAATGAAAAGATCTGGAGGACACAGAATACCAG
GCTTGAATTGCTGTGGTCAGGGAAGAGCCTGCTACAGATGGTCAAAAAGATGGTTAATAG
TGAAAGATTCCTTTTTATTGTATATGAAACCAGACAGCGGTGCCATTGCCTTCGTCCTGC
TGGTAGACAAAGAATTCAAAATTAAGGTGGGGAAGAAGGAGACAGAAACGAAATATGGAA
TCCGAATTGATAATCTTTCAAGGACACTTATTTTAAAATGCAACAGCTATAGACATGCTC
GGTGGTGGGGAGGGGCTATAGAAGAATTCATCCAGAAACATGGCACCAACTTTCTCAAAG
ATCATCGATTTGGGTCATATGCTGCTATCCAAGAGAATGCTTTAGCTAAATGGTATGTTA
ATGCCAAAGGATATTTTGAAGATGTGGCAAATGCAATGGAAGAGGCAAATGAAGAGATTT
TTATCACAGACTGGTGGCTGAGTCCAGAAATCTTCCTGAAACGCCCAGTGGTTGAGGGAA
ATCGTTGGAGGTTGGACTGCATTCTTAAACGAAAAGCACAACAAGGAGTGAGGATCTTCA
TAATGCTCTACAAAGAGGTGGAACTCGCTCTTGGCATCAATAGTGAATACACCAAGAGGA
CTTTGATGCGTCTACATCCCAACATAAAGGTGATGAGACACCCGGATCATGTGTCATCCA
CCGTCTATTTGTGGGCTCACCATGAGAAGCTTGTCATCATTGACCAATCGGTGGCCTTTG
TGGGAGGGATTGACCTGGCCTATGGAAGGTGGGACGACAATGAGCACAGACTCACAGACG
TGGGCAGTGTGAAGCGGGTCACTTCAGGACCGTCTCTGGGTTCCCTCCCACCTGCCGCAA
TGGAGTCTATGGAATCCTTAAGACTCAAAGATAAAAATGAGCCTGTTCAAAACCTACCCA
TCCAGAAGAGTATTGATGATGTGGATTCAAAACTGAAAGGAATAGGAAAGCCAAGAAAGT
TCTCCAAATTTAGTCTCTACAAGCAGCTCCACAGGCACCACCTGCACGACGCAGATAGCA
TCAGCAGCATTGACAGCACCTCCAATACCGGGTCCATCCGTAGTTTACAGACAGGTGTGG
GAGAGCTGCATGGGGAAACCAGATTCTGGCATGGAAAGGACTACTGCAATTTCGTCTTCA
AAGACTGGGTTCAACTTGATAAACCTTTTGCTGATTTCATTGACAGGTACTCCACGCCCC
GGATGCCCTGGCATGACATTGCCTCTGCAGTCCACGGGAAGGCGGCTCGTGATGTGGCAC
GTCACTTCATCCAGCGCTGGAACTTCACAAAAATTATGAAATCAAAATATCGGTCCCTTT
CTTATCCTTTTCTGCTTCCAAAGTCTCAAACAACAGCCCATGAGTTGAGATATCAAGTGC
CTGGGTCTGTCCATGCTAACGTACAGTTGCTCCGCTCTGCTGCTGATTGGTCTGCTGGTA
TAAAGTACCATGAAGAGTCCATCCACGCCGCTTACGTCCATGTGATAGAGAACAGCAGGC
ACTATATCTATATCGAAAACCAGTTTTTCATAAGCTGTGCTGATGACAAAGTTGTGTTCA
ACAAGATAGGCGATGCCATTGCCCAGAGGATCCTGAAAGCTCACAGGGAAAACCAGAAAT
ACCGGGTATATGTCGTGATACCACTTCTGCCAGGGTTCGAAGGAGACATTTCAACCGGCG
GAGGAAATGCTCTACAGGCAATCATGCACTTCAACTACAGAACCATGTGCAGAGGAGAAA
ATTCCATCCTTGGACAGTTAAAAGCAGAGCTTGGTAATCAGTGGATAAATTACATATCAT
TCTGTGGTCTTAGAACACATGCAGAGCTCGAAGGAAACCTAGTAACTGAGCTTATCTATG
TCCACAGCAAGTTGTTAATTGCTGATGATAACACTGTTATTATTGGCTCTGCCAACATAA
ATGACCGCAGCATGCTGGGAAAGCGTGACAGTGAAATGGCTGTCATTGTGCAAGATACAG
AGACTGTTCCTTCAGTAATGGATGGAAAAGAGTACCAAGCTGGCCGGTTTGCCCGAGGAC
TTCGGCTACAGTGCTTTAGGGTTGTCCTTGGCTATCTTGATGACCCAAGTGAGGACATTC
AGGATCCAGTGAGTGACAAATTCTTCAAGGAGGTGTGGGTTTCAACAGCAGCTCGAAATG
CTACAATTTATGACAAGGTTTTCCGGTGCCTTCCCAATGATGAAGTACACAATTTAATTC
AGCTGAGAGACTTTATAAACAAGCCCGTATTAGCTAAGGAAGATCCCATTCGAGCTGAGG
AGGAACTGAAGAAGATCCGTGGATTTTTGGTGCAATTCCCCTTTTATTTCTTGTCTGAAG
AAAGCCTACTGCCTTCTGTTGGGACCAAAGAGGCCATAGTGCCCATGGAGGTTTGGACTT
AA
Enzyme 37 GenBank Gene ID AB209907 Link Image
Enzyme 37 GeneCard ID Q59EA4 Link Image
Enzyme 37 GenAtlas ID Not Available
Enzyme 37 HGNC ID HGNC:9067 Link Image
Enzyme 37 Chromosome Location Not Available
Enzyme 37 Locus Not Available
Enzyme 37 SNPs Not Available
Enzyme 37 General References Not Available
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 15287
Enzyme 38 Name 1-acylglycerol-3-phosphate O-acyltransferase 1 (Lysophosphatidic acid acyltransferase, alpha) (1-acylglycerol-3-phosphate O-acyltransferase 1 (Lysophosphatidic acid acyltransferase, alpha), isoform CRA_b)
Enzyme 38 Synonyms Not Available
Enzyme 38 Gene Name AGPAT1
Enzyme 38 Protein Sequence >1-acylglycerol-3-phosphate O-acyltransferase 1 (Lysophosphatidic acid acyltransferase, alpha) (1-acylglycerol-3-phosphate O-acyltransferase 1 (Lysophosphatidic acid acyltransferase, alpha), isoform CRA_b) 
MDLWPGAWMLLLLLFLLLLFLLPTLWFCSPSAKYFFKMAFYNGWILFLAVLAIPVCAVRG
RNVENMKILRLMLLHIKYLYGIRVEVRGAHHFPPSQPYVVVSNHQSSLDLLGMMEVLPGR
CVPIAKRELLWAGSAGLACWLAGVIFIDRKRTGDAISVMSEVAQTLLTQDVRVWVFPEGT
RNHNGSMLPFKRGAFHLAVQAQVPIVPIVMSSYQDFYCKKERRFTSGQCQVRVLPPVPTE
GLTPDDVPALADRVRHSMLTVFREISTDGRGGGDYLKKPGGGG
Enzyme 38 Number of Residues 283
Enzyme 38 Molecular Weight 31717
Enzyme 38 Theoretical pI 9.75
Enzyme 38 GO Classification
Function
  • 1-acylglycerol-3-phosphate O-acyltransferase activity
  • O-acyltransferase activity
  • acylglycerol O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid biosynthesis
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
  • cell
  • membrane
Enzyme 38 General Function Lipid transport and metabolism
Enzyme 38 Specific Function Not Available
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions Not Available
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 123209920 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID A2BFI5 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name A2BFI5_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >852 bp 
ATGGATTTGTGGCCAGGGGCATGGATGCTGCTGCTGCTGCTCTTCCTGCTGCTGCTCTTC
CTGCTGCCCACCCTGTGGTTCTGCAGCCCCAGTGCCAAGTACTTCTTCAAGATGGCCTTC
TACAATGGCTGGATCCTCTTCCTGGCTGTGCTCGCCATCCCTGTGTGTGCCGTGCGAGGA
CGCAACGTCGAGAACATGAAGATCTTGCGTCTAATGCTGCTCCACATCAAATACCTGTAC
GGGATCCGAGTGGAGGTGCGAGGGGCTCACCACTTCCCTCCCTCGCAGCCCTATGTTGTT
GTCTCCAACCACCAGAGCTCTCTCGATCTGCTTGGGATGATGGAGGTACTGCCAGGCCGC
TGTGTGCCCATTGCCAAGCGCGAGCTACTGTGGGCTGGCTCTGCCGGGCTGGCCTGCTGG
CTGGCAGGAGTCATCTTCATCGACCGGAAGCGCACGGGGGATGCCATCAGTGTCATGTCT
GAGGTCGCCCAGACCCTGCTCACCCAGGACGTGAGGGTCTGGGTGTTTCCTGAGGGAACG
AGAAACCACAATGGCTCCATGCTGCCCTTCAAACGTGGCGCCTTCCATCTTGCAGTGCAG
GCCCAGGTTCCCATTGTCCCCATAGTCATGTCCTCCTACCAAGACTTCTACTGCAAGAAG
GAGCGTCGCTTCACCTCGGGACAATGTCAGGTGCGGGTGCTGCCCCCAGTGCCCACGGAA
GGGCTGACACCAGATGACGTCCCAGCTCTGGCTGACAGAGTCCGGCACTCCATGCTCACT
GTTTTCCGGGAAATCTCCACTGATGGCCGGGGTGGTGGTGACTATCTGAAGAAGCCTGGG
GGCGGTGGGTGA
Enzyme 38 GenBank Gene ID BX284686 Link Image
Enzyme 38 GeneCard ID A2BFI5 Link Image
Enzyme 38 GenAtlas ID Not Available
Enzyme 38 HGNC ID Not Available
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 15288
Enzyme 39 Name Testis spermatogenesis apoptosis-related protein 7 (1-acylglycerol-3- phosphate O-acyltransferase 6 (Lysophosphatidic acid acyltransferase, zeta), isoform CRA_b)
Enzyme 39 Synonyms Not Available
Enzyme 39 Gene Name AGPAT6
Enzyme 39 Protein Sequence >Testis spermatogenesis apoptosis-related protein 7 (1-acylglycerol-3- phosphate O-acyltransferase 6 (Lysophosphatidic acid acyltransferase, zeta), isoform CRA_b) 
MFLLLPFDSLIVNLLGISLTVLFTLLLVFIIVPAIFGVSFGIRKLYMKSLLKIFAWATLR
MERGAKEKNHQLYKPYTNGIIAKDPTSLEEEIKEIRRSGSSKALDNTPEFELSDIFYFCR
KGMETIMDDEVTKRFSAEELESWNLLSRTNYNFQYISLRLTVLWGLGVLIRYCFLLPLRI
ALAFTGISLLVVGTTVVGYLPNGRFKEFMSKHVHLMCYRICVRALTAIITYHDRENRPRN
GGICVANHTSPIDVIILASDGYYAMVGQVHGGLMGVIQRAMVKACPHVWFERSEVKDRHL
VAKRLTEHVQDKSKLPILIFPEGTCINNTSVMMFKKGSFEIGATVYPVAIKYDPQFGDAF
WNSSKYGMVTYLLRMMTSWAIVCSVWYLPPMTREADEDAVQFANRVKSAIARQGGLVDLL
WDGGLKREKVKDTFKEEQQKLYSKMIVGNHKDRSRS
Enzyme 39 Number of Residues 456
Enzyme 39 Molecular Weight 52072
Enzyme 39 Theoretical pI 9.56
Enzyme 39 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 39 General Function Not Available
Enzyme 39 Specific Function Not Available
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 46241188 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q2TU73 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name Q2TU73_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >1371 bp 
ATGTTCCTGTTGCTGCCTTTTGATAGCCTGATTGTCAACCTTCTGGGCATCTCCCTGACT
GTCCTCTTCACCCTCCTTCTCGTTTTCATCATAGTGCCAGCCATTTTTGGAGTCTCCTTT
GGTATCCGCAAACTCTACATGAAAAGTCTGTTAAAAATCTTTGCGTGGGCTACCTTGAGA
ATGGAGCGAGGAGCCAAGGAGAAGAACCACCAGCTTTACAAGCCCTACACCAACGGAATC
ATTGCAAAGGATCCCACTTCACTAGAAGAAGAGATCAAAGAGATTCGTCGAAGTGGTAGT
AGTAAGGCTCTGGACAACACTCCAGAGTTCGAGCTCTCTGACATTTTCTACTTTTGCCGG
AAAGGAATGGAGACCATTATGGATGATGAGGTGACAAAGAGATTCTCAGCAGAAGAACTG
GAGTCCTGGAACCTGCTGAGCAGAACCAATTATAACTTCCAGTACATCAGCCTTCGGCTC
ACGGTCCTGTGGGGGTTAGGAGTGCTGATTCGGTACTGCTTTCTGCTGCCGCTCAGGATA
GCACTGGCTTTCACAGGGATTAGCCTTCTGGTGGTGGGCACAACTGTGGTGGGATACTTG
CCAAATGGGAGGTTTAAGGAGTTCATGAGTAAACATGTTCACTTAATGTGTTACCGGATC
TGCGTGCGAGCGCTGACAGCCATCATCACCTACCATGACAGGGAAAACAGACCAAGAAAT
GGTGGCATCTGTGTGGCCAATCATACCTCACCGATCGATGTGATCATCTTGGCCAGCGAT
GGCTATTATGCCATGGTGGGTCAAGTGCACGGGGGACTCATGGGTGTGATTCAGAGAGCC
ATGGTGAAGGCCTGCCCACACGTCTGGTTTGAGCGCTCGGAAGTGAAGGATCGCCACCTG
GTGGCTAAGAGACTGACTGAACATGTGCAAGATAAAAGCAAGCTGCCTATCCTCATCTTC
CCAGAAGGAACCTGCATCAATAATACATCGGTGATGATGTTCAAAAAGGGAAGTTTTGAA
ATTGGAGCCACAGTTTACCCTGTTGCTATCAAGTATGACCCTCAATTTGGCGATGCCTTC
TGGAACAGCAGCAAATACGGGATGGTGACGTACCTGCTGCGAATGATGACCAGCTGGGCC
ATTGTCTGCAGCGTGTGGTACCTGCCTCCCATGACTAGAGAGGCAGATGAAGATGCTGTC
CAGTTTGCGAATAGGGTGAAATCTGCCATTGCCAGGCAGGGAGGACTTGTGGACCTGCTG
TGGGATGGGGGCCTGAAGAGGGAGAAGGTGAAGGACACGTTCAAGGAGGAGCAGCAGAAG
CTGTACAGCAAGATGATCGTGGGGAACCACAAGGACAGGAGCCGCTCCTGA
Enzyme 39 GenBank Gene ID AY513610 Link Image
Enzyme 39 GeneCard ID Q2TU73 Link Image
Enzyme 39 GenAtlas ID AGPAT6 Link Image
Enzyme 39 HGNC ID HGNC:20880 Link Image
Enzyme 39 Chromosome Location Not Available
Enzyme 39 Locus Not Available
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References Not Available
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 15289
Enzyme 40 Name Lysocardiolipin acyltransferase (Uncharacterized protein LYCAT)
Enzyme 40 Synonyms Not Available
Enzyme 40 Gene Name LYCAT
Enzyme 40 Protein Sequence >Lysocardiolipin acyltransferase (Uncharacterized protein LYCAT) 
MVSWKGIYFILTLFWGSFFGSIFMLSPFLPLMFVNPSWYRWINNRLVATWLTLPVALLET
MFGVKVIITGDAFVPGERSVIIMNHRTRMDWMFLWNCLMRYSYLRLEKICLKASLKGVPG
FGWAMQAAAYIFIHRKWKDDKSHFEDMIDYFCDIHEPLQLLIFPEGTDLTENSKSRSNAF
AEKNGLQKYEYVLHPRTTGFTFVVDRLREGKNLDAVHDITVAYPHNIPQSEKHLLQGDFP
REIHFHVHRYPIDTLPTSKEDLQLWCHKRWEEKEERLRSFYQGEKNFYFTGQSVIPPCKS
ELRVLVVKLLSILYWTLFSPAMCLLIYLYSLVKWYFIITIVIFVLQERIFGGLEIIELAC
YRLLHKQPHLNSKKNE
Enzyme 40 Number of Residues 376
Enzyme 40 Molecular Weight 44562
Enzyme 40 Theoretical pI 8.76
Enzyme 40 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 40 General Function Lipid transport and metabolism
Enzyme 40 Specific Function Not Available
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein Not Available
Enzyme 40 UniProtKB/Swiss-Prot ID A6H8Z7 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name A6H8Z7_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 AC132154 Link Image
Enzyme 40 GeneCard ID A6H8Z7 Link Image
Enzyme 40 GenAtlas ID LYCAT Link Image
Enzyme 40 HGNC ID HGNC:26756 Link Image
Enzyme 40 Chromosome Location Not Available
Enzyme 40 Locus Not Available
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 15290
Enzyme 41 Name Diacylglycerol kinase, beta 90kDa (Diacylglycerol kinase, beta 90kDa, isoform CRA_b)
Enzyme 41 Synonyms Not Available
Enzyme 41 Gene Name DGKB
Enzyme 41 Protein Sequence >Diacylglycerol kinase, beta 90kDa (Diacylglycerol kinase, beta 90kDa, isoform CRA_b) 
MTNQEKWAHLSPSEFSQLQKYAEYSTKKLKDVLEEFHGNGVLAKYNPEGKQDILNQTIDF
EGFKLFMKTFLEAELPDDFTAHLFMSFSNKFPHSSPMVKSKPALLSGGLRMNKGAITPPR
TTSPANTCSPEVIHLKDIVCYLSLLERGRPEDKLEFMFRLYDTDGNGFLDSSELENIISQ
MMHVAEYLEWDVTELNPILHEMMEEIDYDHDGTVSLEEWIQGGMTTIPLLVLLGLENNVK
DDGQHVWRLKHFNKPAYCNLCLNMLIGVGKQGLCCSFCKYTVHERCVARAPPSCIKTYVK
SKRNTDVMHHYWVEGNCPTKCDKCHKTVKCYQGLTGLHCVWCQITLHNKCASHLKPECDC
GPLKDHILPPTTICPVVLQTLPTSGVSVPEERQSTVKKEKSGSQQPNKVIDKNKMQRANS
VTVDGQGLQVTPVPGTHPLLVFVNPKSGGKQGERIYRKFQYLLNPRQVYSLSGNGPMPGL
NFFRDVPDFRVLACGGDGTVGWVLDCIEKANVGKHPPVAILPLGTGNDLARCLRWGGGYE
GENLMKILKDIENSTEIMLDRWKFEVIPNDKDEKGDPVPYSIINNYFSIGVDASIAHRFH
IMREKHPEKFNSRMKNKFWYFEFGTSETFSATCKKLHESVEIECDGVQIDLINISLEGIA
ILNIPSMHGGSNLWGESKKRRSHRRIEKKGSDKRTTVTDAKELKFASQDLSDQLLEVVGL
EGAMEMGQIYTGLKSAGRRLAQCSCVVIRTSKSLPMQIDGEPWMQTPCTIKITHKNQAPM
LMGPPPKTGLFCSLVKRTRNRSKE
Enzyme 41 Number of Residues 804
Enzyme 41 Molecular Weight 90596
Enzyme 41 Theoretical pI 7.90
Enzyme 41 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 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 A4D116 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name A4D116_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 CH236948 Link Image
Enzyme 41 GeneCard ID A4D116 Link Image
Enzyme 41 GenAtlas ID Not Available
Enzyme 41 HGNC ID Not Available
Enzyme 41 Chromosome Location Not Available
Enzyme 41 Locus Not Available
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 15291
Enzyme 42 Name Diacylglycerol kinase, theta 110kDa
Enzyme 42 Synonyms Not Available
Enzyme 42 Gene Name DGKQ
Enzyme 42 Protein Sequence >Diacylglycerol kinase, theta 110kDa 
MAAAAEPGARAWLGGGSPRPGSPACSLVLGSGGRARPGPGPGPGPERAGVRAPGPAAAPG
HSFRKVTLTKPTFCHLCSDFIWGLAGFLCDVCNFMSHEKCLKHVRIPCTSVAPSLVRVPV
AHCFGPRGLHKRKFCAVCRKVLEAPALHCEVCELHLHPDCVPFACSDCRQCHQDGHQDHD
THHHHWREGNLPSGARCEVCRKTCGSSDVLAGVRCEWCGVQAHSLCSAALAPECGFGRLR
SLVLPPACVRLLPGGFSKTQSFRIVEAAEPGEGGDGADGSAAVGPGRETQATPESGKQTL
KIFDGDDAVRRSQFRLVTVSRLAGAEEVLEAALRAHHIPEDPGHLELCRLPPSSQACDAW
AGGKAGSAVISEEGRSPGSGEATPEAWVIRALPRAQEVLKIYPGWLKVGVAYVSVRVTPK
STARSVVLEVLPLLGRQAESPESFQLVEVAMGCRHVQRTMLMDEQPLLDRLQDIRQMSVR
QVSQTRFYVAESRDVAPHVSLFVGGLPPGLSPEEYSSLLHEAGATKATVVSVSHIYSSQG
AVVLDVACFAEAERLYMLLKDMAVRGRLLTALVLPDLLHAKLPPDSCPLLVFVNPKSGGL
KGRDLLCSFRKLLNPHQVFDLTNGGPLPGLHLFSQVPCFRVLVCGGDGTVGWVLGALEET
RYRLACPEPSVAILPLGTGNDLGRVLRWGAGYSGEDPFSVLLSVDEADAVLMDRWTILLD
AHEAGSAENDTADAEPPKIVQMSNYCGIGIDAELSLDFHQAREEEPGKFTSRLHNKGVYV
RVGLQKISHSRSLHKQIRLQVERQEVELPSIEGLIFINIPSWGSGADLWGSDSDTRFEKP
RMDDGLLEVVGVTGVVHMGQVQGGLRSGIRIAQGSYFRVTLLKATPVQVDGEPWVQAPGH
MIISAAGPKVHMLRKAKQKPRRAGTTRDARADAAPAPESDPR
Enzyme 42 Number of Residues 942
Enzyme 42 Molecular Weight 101172
Enzyme 42 Theoretical pI 7.50
Enzyme 42 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 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 39645110 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q6P3W4 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name Q6P3W4_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >2829 bp 
ATGGCGGCGGCGGCCGAGCCCGGGGCCCGCGCCTGGCTGGGCGGCGGCTCCCCGCGCCCC
GGCAGCCCGGCCTGCAGCCTCGTGCTGGGCTCAGGAGGCCGCGCGCGCCCGGGGCCGGGG
CCGGGGCCGGGACCCGAGCGGGCGGGCGTCAGAGCCCCGGGCCCCGCTGCCGCGCCGGGA
CACAGCTTCCGGAAGGTGACGCTCACCAAGCCCACCTTCTGCCACCTCTGCTCCGACTTC
ATCTGGGGGCTGGCCGGCTTCCTGTGCGACGTCTGCAATTTCATGTCTCATGAGAAGTGC
CTGAAGCACGTGAGGATCCCGTGCACGAGTGTGGCACCCAGCCTGGTCCGGGTTCCTGTA
GCCCACTGCTTCGGCCCCCGGGGGCTCCACAAGCGCAAGTTCTGTGCTGTCTGCCGCAAG
GTCCTGGAGGCACCGGCGCTCCACTGCGAAGTGTGTGAGCTGCACCTCCACCCAGACTGT
GTGCCCTTCGCCTGCAGTGACTGCCGCCAGTGCCACCAGGATGGGCACCAGGATCACGAC
ACCCATCACCACCACTGGCGGGAGGGGAACCTGCCCTCGGGAGCGCGCTGCGAGGTCTGC
AGGAAGACGTGCGGCTCCTCTGACGTGCTGGCCGGCGTGCGCTGCGAGTGGTGCGGGGTC
CAGGCGCACTCCCTCTGCTCCGCGGCACTGGCTCCCGAGTGTGGCTTCGGGCGTCTGCGC
TCCCTGGTCCTGCCTCCCGCGTGCGTGCGCCTTCTGCCCGGCGGCTTCAGCAAGACGCAG
AGCTTCCGCATCGTGGAGGCCGCGGAGCCGGGCGAGGGGGGCGACGGCGCCGACGGGAGC
GCTGCCGTGGGTCCAGGCAGAGAGACACAGGCAACTCCGGAGTCCGGGAAGCAAACGCTG
AAGATCTTTGATGGCGACGACGCGGTGAGAAGAAGCCAGTTCCGCCTCGTCACGGTGTCC
CGCCTGGCCGGTGCCGAGGAGGTGCTGGAGGCCGCACTGCGGGCCCACCACATCCCCGAG
GACCCTGGCCACCTGGAGCTGTGCCGGCTGCCCCCTTCCTCTCAGGCCTGTGACGCCTGG
GCTGGGGGCAAGGCTGGGAGTGCTGTGATCTCGGAGGAGGGCAGAAGCCCCGGGTCCGGC
GAGGCCACGCCAGAGGCCTGGGTCATCCGGGCTCTGCCGCGGGCCCAGGAGGTCCTGAAG
ATCTACCCTGGCTGGCTCAAGGTGGGCGTGGCCTACGTGTCCGTGCGAGTGACCCCGAAG
AGCACGGCCCGCTCTGTGGTGCTGGAGGTCCTGCCGCTGCTCGGCCGCCAGGCCGAGAGT
CCCGAGAGCTTCCAGCTGGTGGAGGTGGCGATGGGCTGCAGGCACGTCCAGCGGACGATG
CTGATGGACGAACAGCCCCTGCTGGACCGGCTACAGGACATCCGGCAGATGTCTGTGCGG
CAGGTGAGCCAGACGCGGTTCTACGTGGCAGAGAGCAGGGATGTAGCCCCGCACGTCTCC
CTGTTTGTTGGCGGCCTGCCTCCCGGCCTGTCTCCCGAGGAGTACAGCAGCCTGCTGCAT
GAGGCCGGGGCTACCAAAGCCACCGTGGTGTCCGTGAGTCACATCTACTCCTCCCAAGGC
GCGGTAGTGTTGGACGTTGCCTGCTTTGCGGAGGCCGAGCGGCTGTACATGCTGCTGAAG
GACATGGCTGTGCGGGGCCGGCTGCTCACTGCCCTGGTGCTCCCCGACCTGCTGCACGCG
AAGCTGCCCCCAGACAGCTGTCCCCTCCTTGTGTTCGTGAACCCCAAGAGTGGAGGCCTC
AAGGGCCGAGACCTGCTCTGCAGCTTCCGGAAGCTACTGAACCCTCATCAGGTCTTCGAC
CTGACCAACGGAGGTCCTCTTCCCGGGCTCCACCTGTTCTCCCAGGTGCCCTGCTTCCGG
GTGCTGGTGTGTGGTGGCGATGGCACTGTGGGCTGGGTGCTTGGCGCCCTGGAGGAGACA
CGGTACCGACTGGCCTGCCCGGAGCCTTCTGTGGCCATCCTGCCCCTGGGCACAGGGAAT
GACCTTGGTCGAGTCCTCCGCTGGGGGGCGGGCTACAGCGGCGAGGACCCGTTCTCCGTA
CTGCTGTCTGTGGACGAGGCCGACGCCGTGCTCATGGACCGCTGGACCATCCTGCTGGAT
GCCCACGAGGCTGGCAGTGCAGAGAACGACACGGCAGACGCAGAGCCCCCCAAGATCGTG
CAGATGAGTAACTACTGTGGCATTGGCATCGACGCGGAGCTGAGCCTGGACTTCCACCAG
GCACGGGAAGAGGAGCCTGGCAAGTTCACAAGCAGGCTGCACAACAAGGGTGTGTACGTG
CGGGTGGGGCTGCAGAAGATCAGTCACTCTCGGAGCCTGCACAAGCAGATCCGGCTGCAG
GTGGAGCGGCAGGAGGTGGAGCTGCCCAGTATTGAAGGCCTCATCTTCATCAACATCCCC
AGCTGGGGCTCGGGGGCCGACCTGTGGGGCTCCGACAGCGACACCAGGTTTGAGAAGCCA
CGCATGGACGACGGGCTGCTGGAGGTTGTGGGCGTGACGGGCGTCGTGCACATGGGCCAG
GTCCAGGGTGGGCTGCGCTCCGGAATCCGGATTGCCCAGGGTTCCTACTTCCGAGTCACG
CTCCTCAAGGCCACCCCGGTGCAGGTGGACGGGGAGCCCTGGGTCCAGGCCCCGGGGCAC
ATGATCATCTCAGCTGCTGGCCCTAAGGTGCACATGCTGAGGAAGGCCAAGCAGAAGCCG
AGGAGGGCCGGGACCACCAGGGATGCCCGGGCGGATGCTGCGCCTGCCCCTGAGAGCGAT
CCTAGGTAG
Enzyme 42 GenBank Gene ID BC063801 Link Image
Enzyme 42 GeneCard ID Q6P3W4 Link Image
Enzyme 42 GenAtlas ID DGKQ Link Image
Enzyme 42 HGNC ID HGNC:2856 Link Image
Enzyme 42 Chromosome Location Not Available
Enzyme 42 Locus Not Available
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 15292
Enzyme 43 Name Diacylglycerol kinase, epsilon 64kDa (cDNA FLJ75840, highly similar to Homo sapiens diacylglycerol kinase, epsilon 64kDa (DGKE), mRNA)
Enzyme 43 Synonyms Not Available
Enzyme 43 Gene Name DGKE
Enzyme 43 Protein Sequence >Diacylglycerol kinase, epsilon 64kDa (cDNA FLJ75840, highly similar to Homo sapiens diacylglycerol kinase, epsilon 64kDa (DGKE), mRNA) 
MEAERRPAPGSPSEGLFADGHLILWTLCSVLLPVFITFWCSLQRSRRQLHRRDIFRKSKH
GWRDTDLFSQPTYCCVCAQHILQGAFCDCCGLRVDEGCLRKADKRFQCKEIMLKNDTKVL
DAMPHHWIRGNVPLCSYCMVCKQQCGCQPKLCDYRCIWCQKTVHDECMKNSLKNEKCDFG
EFKNLIIPPSYLTSINQMRKDKKTDYEVLASKLGKQWTPLIILANSRSGTNMGEGLLGEF
RILLNPVQVFDVTKTPPIKALQLCTLLPYYSARVLVCGGDGTVGWVLDAVDDMKIKGQEK
YIPQVAVLPLGTGNDLSNTLGWGTGYAGEIPVAQVLRNVMEADGIKLDRWKVQVTNKGYY
NLRKPKEFTMNNYFSVGPDALMALNFHAHREKAPSLFSSRILNKAVYLFYGTKDCLVQEC
KDLNKKVELELDGERVALPSLEGIIVLNIGYWGGGCRLWEGMGDETYPLARHDDGLLEVV
GVYGSFHCAQIQVKLANPFRIGQAHTVRLILKCSMMPMQVDGEPWAQGPCTVTITHKTHA
MMLYFSGEQTDDDISSTSDQEDIKATE
Enzyme 43 Number of Residues 567
Enzyme 43 Molecular Weight 63928
Enzyme 43 Theoretical pI 7.78
Enzyme 43 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • diacylglycerol kinase activity
  • electron transporter activity
  • ion binding
  • iron ion binding
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • transporter activity
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular metabolism
  • cellular process
  • electron transport
  • generation of precursor metabolites and energy
  • intracellular signaling cascade
  • metabolism
  • physiological process
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 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 120659970 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID A1L4Q0 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name A1L4Q0_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >1704 bp 
ATGGAAGCGGAGAGGCGGCCGGCGCCGGGCTCGCCCTCCGAGGGCCTGTTTGCGGACGGG
CACCTGATCTTGTGGACGCTGTGCTCGGTCCTGCTGCCGGTGTTCATCACCTTCTGGTGT
AGCCTCCAGCGGTCGCGCCGGCAGCTGCACCGCAGGGACATCTTCCGCAAGAGCAAGCAC
GGGTGGCGCGACACGGACCTGTTCAGCCAGCCCACCTACTGCTGCGTGTGCGCGCAGCAC
ATTCTGCAGGGCGCCTTCTGCGACTGCTGCGGGCTCCGCGTGGACGAGGGCTGCCTCAGG
AAGGCCGACAAGCGCTTCCAGTGCAAGGAGATTATGCTCAAGAATGACACCAAGGTCCTG
GACGCCATGCCCCACCACTGGATCCGGGGCAACGTGCCCCTGTGCAGTTACTGTATGGTT
TGCAAGCAGCAGTGTGGCTGTCAACCCAAGCTTTGCGATTACAGGTGCATTTGGTGCCAG
AAAACAGTACATGATGAGTGCATGAAAAATAGTTTAAAGAATGAAAAATGTGATTTTGGA
GAATTCAAAAACCTAATCATTCCACCAAGTTATTTAACCTCCATTAATCAGATGCGTAAA
GACAAAAAAACAGATTATGAAGTGCTAGCCTCTAAGCTTGGAAAGCAGTGGACCCCATTA
ATAATCCTGGCCAACTCTCGTAGTGGAACTAATATGGGAGAAGGACTGTTGGGAGAATTT
AGGATCTTGTTGAATCCAGTCCAGGTTTTTGATGTAACTAAAACTCCTCCTATCAAAGCC
CTACAACTCTGTACTCTTCTCCCATATTATTCAGCTCGAGTACTTGTTTGTGGAGGGGAT
GGGACTGTAGGGTGGGTCCTGGATGCAGTTGATGACATGAAGATTAAGGGACAAGAAAAG
TACATTCCACAAGTTGCAGTTTTGCCTCTGGGAACAGGCAACGATCTATCCAATACATTG
GGTTGGGGTACAGGTTATGCTGGAGAAATTCCAGTTGCGCAGGTTTTGCGAAATGTAATG
GAAGCAGATGGAATTAAACTAGATCGATGGAAAGTTCAAGTAACAAATAAAGGATACTAC
AACTTAAGAAAACCCAAGGAATTCACAATGAACAACTATTTTTCTGTTGGACCTGATGCT
CTCATGGCTCTCAATTTTCATGCTCATCGTGAGAAGGCACCATCTCTGTTTTCTAGCAGA
ATTCTTAATAAGGCGGTTTACTTATTCTATGGAACCAAAGATTGTTTAGTGCAAGAATGT
AAAGATTTGAATAAAAAAGTTGAGCTAGAACTGGATGGTGAGCGAGTAGCACTGCCCAGC
TTGGAAGGTATTATAGTTCTGAACATCGGATACTGGGGCGGTGGCTGCAGACTATGGGAA
GGGATGGGGGACGAGACTTACCCTCTAGCCAGGCATGACGATGGTCTGCTGGAAGTCGTT
GGAGTATATGGGTCTTTCCACTGTGCTCAGATTCAAGTAAAACTGGCTAATCCTTTTCGA
ATAGGACAGGCACATACAGTGAGGCTGATTTTGAAGTGCTCCATGATGCCAATGCAGGTG
GATGGGGAGCCTTGGGCCCAAGGGCCCTGCACTGTCACCATAACTCACAAGACACATGCA
ATGATGTTATATTTCTCTGGAGAACAAACAGATGATGACATCTCTAGTACTTCGGATCAA
GAAGATATAAAGGCGACTGAATAG
Enzyme 43 GenBank Gene ID BC130629 Link Image
Enzyme 43 GeneCard ID A1L4Q0 Link Image
Enzyme 43 GenAtlas ID Not Available
Enzyme 43 HGNC ID Not Available
Enzyme 43 Chromosome Location 17
Enzyme 43 Locus 17q22
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 16477
Enzyme 44 Name cDNA, FLJ94990, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 1 (CDS1), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 1, isoform CRA_a)
Enzyme 44 Synonyms Not Available
Enzyme 44 Gene Name CDS1
Enzyme 44 Protein Sequence >cDNA, FLJ94990, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 1 (CDS1), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 1, isoform CRA_a) 
MLELRHRGSCPGPREAVSPPHREGEAAGGDHETESTSDKETDIDDRYGDLDSRTDSDIPE
IPPSSDRTPEILKKALSGLSSRWKNWWIRGILTLTMISLFFLIIYMGSFMLMLLVLGIQV
KCFHEIITIGYRVYHSYDLPWFRTLSWYFLLCVNYFFYGETVADYFATFVQREEQLQFLI
RYHRFISFALYLAGFCMFVLSLVKKHYRLQFYMFAWTHVTLLITVTQSHLVIQNLFEGMI
WFLVPISSVICNDITAYLFGFFFGRTPLIKLSPKKTWEGFIGGFFSTVVFGFIAAYVLSK
YQYFVCPVEYRSDVNSFVTECEPSELFQLQTYSLPPFLKAVLRQERVSLYPFQIHSIALS
TFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVHVYITSFIRG
PNPSKVLQQLLVLQPEQQLNIYKTLKTHLIEKGILQPTLKV
Enzyme 44 Number of Residues 461
Enzyme 44 Molecular Weight 53305
Enzyme 44 Theoretical pI 8.19
Enzyme 44 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • phosphatidate cytidylyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid biosynthesis
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
  • cell
  • membrane
Enzyme 44 General Function Lipid transport and metabolism
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 B2RAL5 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name B2RAL5_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 AK314245 Link Image
Enzyme 44 GeneCard ID B2RAL5 Link Image
Enzyme 44 GenAtlas ID Not Available
Enzyme 44 HGNC ID Not Available
Enzyme 44 Chromosome Location Not Available
Enzyme 44 Locus Not Available
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References Not Available
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 16478
Enzyme 45 Name cDNA, FLJ96552, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 2 (CDS2), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 2, isoform CRA_a)
Enzyme 45 Synonyms Not Available
Enzyme 45 Gene Name CDS2
Enzyme 45 Protein Sequence >cDNA, FLJ96552, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 2 (CDS2), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 2, isoform CRA_a) 
MTELRQRVAHEPVAPPEDKESESEAKVDGETASDSESRAESAPLPVSADDTPEVLNRALS
NLSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMIIVMCVQIKCFHEIITIGYNVYHSY
DLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFTLYLIGFCM
FVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAY
MFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSF
TVDCEPSDLFRLQEYNIPGVIQSVIGWKTVRMYPFQIHSIALSTFASLIGPFGGFFASGF
KRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLIQQFLTLRPDQ
QLHIFNTLRSHLIDKGMLTSTTEDE
Enzyme 45 Number of Residues 445
Enzyme 45 Molecular Weight 51419
Enzyme 45 Theoretical pI 7.10
Enzyme 45 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • phosphatidate cytidylyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid biosynthesis
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
  • cell
  • membrane
Enzyme 45 General Function Lipid transport and metabolism
Enzyme 45 Specific Function Not Available
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions Not Available
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein Not Available
Enzyme 45 UniProtKB/Swiss-Prot ID B2RDC6 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name B2RDC6_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence Not Available
Enzyme 45 GenBank Gene ID AK315489 Link Image
Enzyme 45 GeneCard ID B2RDC6 Link Image
Enzyme 45 GenAtlas ID Not Available
Enzyme 45 HGNC ID Not Available
Enzyme 45 Chromosome Location 20
Enzyme 45 Locus 20p13
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References Not Available
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 16543
Enzyme 46 Name cDNA, FLJ92787, highly similar to Homo sapiens phosphatidic acid phosphatase type 2B (PPAP2B), mRNA (Phosphatidic acid phosphatase type 2B, isoform CRA_a)
Enzyme 46 Synonyms Not Available
Enzyme 46 Gene Name PPAP2B
Enzyme 46 Protein Sequence >cDNA, FLJ92787, highly similar to Homo sapiens phosphatidic acid phosphatase type 2B (PPAP2B), mRNA (Phosphatidic acid phosphatase type 2B, isoform CRA_a) 
MQNYKYDKAIVPESKNGGSPALNNNPRRSGSKRVLLICLDLFCLFMAGLPFLIIETSTIK
PYHRGFYCNDESIKYPLKTGETINDAVLCAVGIVIAILAIITGEFYRIYYLKKSRSTIQN
PYVAALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLSVCNPDFSQINCSEGYIQNYR
CRGDDSKVQEARKSFFSGHASFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFY
TGLSRVSDHKHHPSDVLAGFAQGALVACCIVFFVSDLFKTKTTLSLPAPAIRKEILSPVD
IIDRNNHHNMM
Enzyme 46 Number of Residues 311
Enzyme 46 Molecular Weight 35116
Enzyme 46 Theoretical pI 9.40
Enzyme 46 GO Classification Not Available
Enzyme 46 General Function Lipid transport and metabolism
Enzyme 46 Specific Function Not Available
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein Not Available
Enzyme 46 UniProtKB/Swiss-Prot ID B2R651 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name B2R651_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence Not Available
Enzyme 46 GenBank Gene ID AK312439 Link Image
Enzyme 46 GeneCard ID B2R651 Link Image
Enzyme 46 GenAtlas ID Not Available
Enzyme 46 HGNC ID Not Available
Enzyme 46 Chromosome Location Not Available
Enzyme 46 Locus Not Available
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References Not Available
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 17294
Enzyme 47 Name Lysophosphatidic acid receptor 1
Enzyme 47 Synonyms Not Available
Enzyme 47 Gene Name LPAR1
Enzyme 47 Protein Sequence >Lysophosphatidic acid receptor 1 
MAAISTSIPVISQPQFTAMNEPQCFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITVC
IFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVST
WLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMGA
IP
Enzyme 47 Number of Residues 182
Enzyme 47 Molecular Weight 20565
Enzyme 47 Theoretical pI 10.14
Enzyme 47 GO Classification
Function
  • G-protein coupled receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 47 General Function Not Available
Enzyme 47 Specific Function Not Available
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions Not Available
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein Not Available
Enzyme 47 UniProtKB/Swiss-Prot ID B1AP63 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name B1AP63_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence Not Available
Enzyme 47 GenBank Gene ID AL442064 Link Image
Enzyme 47 GeneCard ID LPAR1 Link Image
Enzyme 47 GenAtlas ID Not Available
Enzyme 47 HGNC ID Not Available
Enzyme 47 Chromosome Location Not Available
Enzyme 47 Locus Not Available
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References Not Available
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 17295
Enzyme 48 Name High-affinity lysophosphatidic acid receptor homolog
Enzyme 48 Synonyms Not Available
Enzyme 48 Gene Name Not Available
Enzyme 48 Protein Sequence >High-affinity lysophosphatidic acid receptor homolog 
MACNSTSLEAYTYLLLNTSNASDSGSTQLPAPLRISLAIVMLLMTVVGFLGNTVVCIIVY
QRPAMRSAINLLLATLAFSDIMLSLCCMPFTAVTLITVRWHFGDHFCRLSATLYWFFVLE
GVAILLIISVDRFLIIVQRQDKLNPRRAKVIIAVSWVLSWVLSFCIAGPSLTGWTLVEVP
ARAPQCVLGYTELPADRAYVVTLVVAVFFAPFGVMLCAYMCILNTVRKNAVRVHNQSDSL
DLRQLTRAGLRRLQRQQQVSVDLSFKTKAFTTILILFVGFSLCWLPHSVYSLLSVFSQRF
YCGSSFYATSTCVLWLSYLKSVFNPIVYCWRIKKFREACIELLPQTFQILPKVPERIRRR
IQPSTVYCCNENQSAV
Enzyme 48 Number of Residues 376
Enzyme 48 Molecular Weight 42457
Enzyme 48 Theoretical pI 9.33
Enzyme 48 GO Classification
Function
  • G-protein coupled receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 48 General Function Not Available
Enzyme 48 Specific Function Not Available
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions Not Available
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein Not Available
Enzyme 48 UniProtKB/Swiss-Prot ID O43898 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name O43898_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence Not Available
Enzyme 48 GenBank Gene ID U92642 Link Image
Enzyme 48 GeneCard ID Not Available
Enzyme 48 GenAtlas ID Not Available
Enzyme 48 HGNC ID HGNC:4503 Link Image
Enzyme 48 Chromosome Location Not Available
Enzyme 48 Locus Not Available
Enzyme 48 SNPs Not Available
Enzyme 48 General References Not Available
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 17296
Enzyme 49 Name LPAR1 protein
Enzyme 49 Synonyms
  1. SubName: cDNA FLJ51746, highly similar to Lysophosphatidic acid receptor Edg-2
Enzyme 49 Gene Name LPAR1
Enzyme 49 Protein Sequence >LPAR1 protein 
MNEPQCFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITVCIFIMLANLLVMVAIYVNR
RFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVSTWLLRQGLIDTSLTASVAN
LLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMGAIPSVGWNCICDIENCSNM
APLYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRMSRHSSGPRRNRDTMMSLLK
TVVIVLGAFIICWTPGLVLLLLDVCCPQCDVLAYEKFFLLLAEFNSAMNPIIYSYRDKEM
SATFRQILCCQRSENPTGPTEGSDRSASSLNHTILAGVHSNDHSVV
Enzyme 49 Number of Residues 346
Enzyme 49 Molecular Weight 39266
Enzyme 49 Theoretical pI 8.60
Enzyme 49 GO Classification
Function
  • G-protein coupled receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 49 General Function Not Available
Enzyme 49 Specific Function Not Available
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions Not Available
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • None
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein Not Available
Enzyme 49 UniProtKB/Swiss-Prot ID Q6GPG7 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name Q6GPG7_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence Not Available
Enzyme 49 GenBank Gene ID BC073167 Link Image
Enzyme 49 GeneCard ID LPAR1 Link Image
Enzyme 49 GenAtlas ID LPAR1 Link Image
Enzyme 49 HGNC ID HGNC:3166 Link Image
Enzyme 49 Chromosome Location Not Available
Enzyme 49 Locus Not Available
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References Not Available
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 17297
Enzyme 50 Name cDNA FLJ61127, highly similar to Lysophosphatidic acid receptor Edg-2
Enzyme 50 Synonyms Not Available
Enzyme 50 Gene Name Not Available
Enzyme 50 Protein Sequence >cDNA FLJ61127, highly similar to Lysophosphatidic acid receptor Edg-2 
MLLLLIPAHSSVLENEFTAMNEPQCFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITV
CIFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVS
TWLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMG
AIPSVGWNCICDIENCSNMAPLYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRM
SRHSSGPRRNRDTMMSLLKTVVIVLGAFIICWTPGLVLLLLDVCCPQCDVLAYEKFFLLL
AEFNSAMNPIIYSYRDKEMSATFRQILCCQRSENPTGPTEGSDRSASSLNHTILAGVHSN
DHSVV
Enzyme 50 Number of Residues 365
Enzyme 50 Molecular Weight 41346
Enzyme 50 Theoretical pI 8.34
Enzyme 50 GO Classification
Function
  • G-protein coupled receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 50 General Function Not Available
Enzyme 50 Specific Function Not Available
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein Not Available
Enzyme 50 UniProtKB/Swiss-Prot ID B4DK36 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name B4DK36_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence Not Available
Enzyme 50 GenBank Gene ID AK296374 Link Image
Enzyme 50 GeneCard ID Not Available
Enzyme 50 GenAtlas ID Not Available
Enzyme 50 HGNC ID Not Available
Enzyme 50 Chromosome Location Not Available
Enzyme 50 Locus Not Available
Enzyme 50 SNPs Not Available
Enzyme 50 General References Not Available
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 17298
Enzyme 51 Name cDNA FLJ41048 fis, clone PROST2001213, highly similar to Lysophosphatidic acid receptor Edg-4
Enzyme 51 Synonyms Not Available
Enzyme 51 Gene Name Not Available
Enzyme 51 Protein Sequence >cDNA FLJ41048 fis, clone PROST2001213, highly similar to Lysophosphatidic acid receptor Edg-4 
MVIMGQCYYNETIGFFYNNSGKELSSHWRPKDVVVVALGLTVSVLVLLTNLLVIAAIASN
RRFHQPIYYLLGNLAAADLFAGVAYLFLMFHTGPRTARLSLEGWFLRQGLLDTSLTASVA
TLLAIAVERHRSVMAVQLHSRLPRGRVVMLIVGVWVAALGLGLLPAHSWHCLCALDRCSR
MAPLLSRSYLAVWALSGLLVFLLMVAVYTRIFFYVRRRVQRMAEHVSCHPRYRETTLSLV
KTVVIILGAFVVCWTPGQVVLLLDGLGCESCNVLAVEKYFLLLAEANSLVNAAVYSCRDA
EMRRTFHRLLCCACLRQSTRESVHYTSSAQGGASTRIMLPENGHPLMDSTL
Enzyme 51 Number of Residues 351
Enzyme 51 Molecular Weight 39036
Enzyme 51 Theoretical pI 9.29
Enzyme 51 GO Classification
Function
  • G-protein coupled receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 51 General Function Not Available
Enzyme 51 Specific Function Not Available
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions Not Available
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • None
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein Not Available
Enzyme 51 UniProtKB/Swiss-Prot ID B3KVP9 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name B3KVP9_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence Not Available
Enzyme 51 GenBank Gene ID AK123043 Link Image
Enzyme 51 GeneCard ID Not Available
Enzyme 51 GenAtlas ID Not Available
Enzyme 51 HGNC ID Not Available
Enzyme 51 Chromosome Location Not Available
Enzyme 51 Locus Not Available
Enzyme 51 SNPs Not Available
Enzyme 51 General References Not Available
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 17299
Enzyme 52 Name cDNA FLJ12746 fis, clone NT2RP2000842, highly similar to Lysophosphatidic acid receptor Edg-2
Enzyme 52 Synonyms
  1. SubName: cDNA FLJ78319, highly similar to Homo sapiens endothelial differentiation, lysophosphatidic acid G-protein-coupled receptor, 2 (EDG2), transcript variant 2, mRNA
  2. SubName: Endothelial differentiation, lysophosphatidic acid G-protein-coupled receptor, 2, isoform CRA_a
  3. SubName: Lysophosphatidic acid receptor 1
Enzyme 52 Gene Name LPAR1
Enzyme 52 Protein Sequence >cDNA FLJ12746 fis, clone NT2RP2000842, highly similar to Lysophosphatidic acid receptor Edg-2 
MAAISTSIPVISQPQFTAMNEPQCFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITVC
IFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVST
WLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMGA
IPSVGWNCICDIENCSNMAPLYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRMS
RHSSGPRRNRDTMMSLLKTVVIVLGAFIICWTPGLVLLLLDVCCPQCDVLAYEKFFLLLA
EFNSAMNPIIYSYRDKEMSATFRQILCCQRSENPTGPTEGSDRSASSLNHTILAGVHSND
HSVV
Enzyme 52 Number of Residues 364
Enzyme 52 Molecular Weight 41110
Enzyme 52 Theoretical pI 8.60
Enzyme 52 GO Classification
Function
  • G-protein coupled receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 52 General Function Not Available
Enzyme 52 Specific Function Not Available
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions Not Available
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein Not Available
Enzyme 52 UniProtKB/Swiss-Prot ID Q5VZX0 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name Q5VZX0_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence Not Available
Enzyme 52 GenBank Gene ID AK290287 Link Image
Enzyme 52 GeneCard ID LPAR1 Link Image
Enzyme 52 GenAtlas ID LPAR1 Link Image
Enzyme 52 HGNC ID HGNC:3166 Link Image
Enzyme 52 Chromosome Location Not Available
Enzyme 52 Locus Not Available
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References Not Available
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 17300
Enzyme 53 Name cDNA FLJ55767, highly similar to Lysophosphatidic acid receptor Edg-2
Enzyme 53 Synonyms Not Available
Enzyme 53 Gene Name Not Available
Enzyme 53 Protein Sequence >cDNA FLJ55767, highly similar to Lysophosphatidic acid receptor Edg-2 
MEEGAQRSGALGAPHQFTAMNEPQCFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITV
CIFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVS
TWLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMG
AIPSVGWNCICDIENCSNMAPLYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRM
SRHSSGPRRNRDTMMSLLKTVVIVLGAFIICWTPGLVLLLLDVCCPQCDVLAYEKFFLLL
AEFNSAMNPIIYSYRDKEMSATFRQILCCQRSENPTGPTEGSDRSASSLNHTILAGVHSN
DHSVV
Enzyme 53 Number of Residues 365
Enzyme 53 Molecular Weight 41206
Enzyme 53 Theoretical pI 8.47
Enzyme 53 GO Classification
Function
  • G-protein coupled receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 53 General Function Not Available
Enzyme 53 Specific Function Not Available
Enzyme 53 Pathways Not Available
Enzyme 53 Reactions Not Available
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein Not Available
Enzyme 53 UniProtKB/Swiss-Prot ID B4DQ18 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name B4DQ18_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence Not Available
Enzyme 53 GenBank Gene ID AK298590 Link Image
Enzyme 53 GeneCard ID Not Available
Enzyme 53 GenAtlas ID Not Available
Enzyme 53 HGNC ID Not Available
Enzyme 53 Chromosome Location Not Available
Enzyme 53 Locus Not Available
Enzyme 53 SNPs Not Available
Enzyme 53 General References Not Available
Enzyme 53 Metabolite References Not Available