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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 Link Image
SDF File Show Link Image
PDB File Show Link Image
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
  3. Lipid phosphate phosphohydrolase 2
  4. Diacylglycerol kinase alpha
  5. Diacylglycerol kinase delta
  6. Lipid phosphate phosphohydrolase 1
  7. Diacylglycerol kinase beta
  8. Diacylglycerol kinase iota
  9. Lipid phosphate phosphohydrolase 3
  10. Diacylglycerol kinase zeta
  11. Phosphatidate cytidylyltransferase 2
  12. Phosphatidate cytidylyltransferase 1
  13. Acyl-CoA:lysophosphatidylglycerol acyltransferase 1
  14. Focal adhesion kinase 1
  15. Protein-tyrosine kinase 2-beta
  16. 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
  17. 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
  18. 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
  19. Phosphatidylinositol-glycan-specific phospholipase D
  20. Lysophosphatidic acid receptor 2
  21. Lysophosphatidic acid receptor 1
  22. 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
  23. Glycerol-3-phosphate acyltransferase 4
  24. Diacylglycerol kinase eta
  25. 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
  26. Lysophosphatidylcholine acyltransferase 1
  27. Lysophosphatidylcholine acyltransferase 2
  28. Lysocardiolipin acyltransferase 1
  29. Lysophosphatidic acid receptor 3
  30. Lysophosphatidic acid receptor 4
  31. Lysophosphatidic acid receptor 5
  32. Lysophospholipid acyltransferase LPCAT4
  33. Glycerol-3-phosphate acyltransferase 3
  34. Lysophosphatidic acid phosphatase type 6
  35. Lysophosphatidic acid receptor 6
  36. Lipase member H
  37. Lipase member I
  38. Lipid phosphate phosphatase-related protein type 4
  39. Acylglycerol kinase, mitochondrial
  40. Phospholipase D1 variant
  41. 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)
  42. 1-acylglycerol-3-phosphate O-acyltransferase 6 (Lysophosphatidic acid acyltransferase, zeta), isoform CRA_b
  43. Lysocardiolipin acyltransferase 1
  44. Diacylglycerol kinase, beta 90kDa (Diacylglycerol kinase, beta 90kDa, isoform CRA_b)
  45. Diacylglycerol kinase, theta 110kDa
  46. Diacylglycerol kinase, epsilon 64kDa
  47. cDNA, FLJ94990, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 1 (CDS1), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 1, isoform CRA_a)
  48. cDNA, FLJ96552, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 2 (CDS2), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 2, isoform CRA_a)
  49. cDNA, FLJ92787, highly similar to Homo sapiens phosphatidic acid phosphatase type 2B (PPAP2B), mRNA (Phosphatidic acid phosphatase type 2B, isoform CRA_a)
  50. Lysophosphatidic acid receptor 1
  51. High-affinity lysophosphatidic acid receptor homolog
  52. LPAR1 protein
  53. cDNA FLJ61127, highly similar to Lysophosphatidic acid receptor Edg-2
  54. cDNA FLJ41048 fis, clone PROST2001213, highly similar to Lysophosphatidic acid receptor Edg-4
  55. Endothelial differentiation, lysophosphatidic acid G-protein-coupled receptor, 2, isoform CRA_a
  56. 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. hPLD2
  3. Choline phosphatase 2
  4. PLD1C
  5. Phosphatidylcholine-hydrolyzing phospholipase D2
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 105986.1
Enzyme 1 Theoretical pI 7.68
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • lipid binding
  • phosphoinositide binding
  • phospholipid binding
  • protein binding
Process
  • cell communication
  • cellular process
  • metabolic process
Component
Enzyme 1 General Function Involved in protein binding
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 [RN:R01310]
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 1
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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Divecha N, Roefs M, Halstead JR, D'Andrea S, Fernandez-Borga M, Oomen L, Saqib KM, Wakelam MJ, D'Santos C: Interaction of the type Ialpha PIPkinase with phospholipase D: a role for the local generation of phosphatidylinositol 4, 5-bisphosphate in the regulation of PLD2 activity. EMBO J. 2000 Oct 16;19(20):5440-9. [PubMed Link Image]
  5. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [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
Enzyme 2 Synonyms
  1. E-NPP 2
  2. Autotaxin
  3. Extracellular lysophospholipase D
  4. LysoPLD
Enzyme 2 Gene Name ENPP2
Enzyme 2 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 2
MARRSSFQSCQIISLFTFAVGVNICLGFTAHRIKRAEGWEEGPPTVLSDSPWTNISGSCK
GRCFELQEAGPPDCRCDNLCKSYTSCCHDFDELCLKTARGWECTKDRCGEVRNEENACHC
SEDCLARGDCCTNYQVVCKGESHWVDDDCEEIKAAECPAGFVRPPLIIFSVDGFRASYMK
KGSKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDA
TFHLRGREKFNHRWWGGQPLWITATKQGVKAGTFFWSVVIPHERRILTILQWLTLPDHER
PSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDH
GMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRSKFSNNAKYDPKAIIANLTCKKPDQH
FKPYLKQHLPKRLHYANNRRIEDIHLLVERRWHVARKPLDVYKKPSGKCFFQGDHGFDNK
VNSMQTVFVGYGSTFKYKTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTF
RPTMPEEVTRPNYPGIMYLQSDFDLGCTCDDKVEPKNKLDELNKRLHTKGSTEERHLLYG
RPAVLYRTRYDILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVPDHLTSCVRPDVRVS
PSFSQNCLAYKNDKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWNYFQRVL
VKKYASERNGVNVISGPIFDYDYDGLHDTEDKIKQYVEGSSIPVPTHYYSIITSCLDFTQ
PADKCDGPLSVSSFILPHRPDNEESCNSSEDESKWVEELMKMHTARVRDIEHLTSLDFFR
KTSRSYPEILTLKTYLHTYESEI
Enzyme 2 Number of Residues 863
Enzyme 2 Molecular Weight 98992.8
Enzyme 2 Theoretical pI 7.39
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • ion binding
  • metal ion binding
  • molecular transducer activity
  • nucleic acid binding
  • pattern binding
  • polysaccharide binding
  • receptor activity
  • scavenger receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • immune response
  • immune system process
  • metabolic process
Component
Enzyme 2 General Function Involved in catalytic activity
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. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. 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 [RN:R04362]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-27
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 91823602 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 >2592 bp
ATGGCAAGGAGGAGCTCGTTCCAGTCGTGTCAGATAATATCCCTGTTCACTTTTGCCGTT
GGAGTCAATATCTGCTTAGGATTCACTGCACATCGAATTAAGAGAGCAGAAGGATGGGAG
GAAGGTCCTCCTACAGTGCTATCAGACTCCCCCTGGACCAACATCTCCGGATCTTGCAAG
GGCAGGTGCTTTGAACTTCAAGAGGCTGGACCTCCTGATTGTCGCTGTGACAACTTGTGT
AAGAGCTATACCAGTTGCTGCCATGACTTTGATGAGCTGTGTTTGAAGACAGCCCGTGGC
TGGGAGTGTACTAAGGACAGATGTGGAGAAGTCAGAAATGAAGAAAATGCCTGTCACTGC
TCAGAGGACTGCTTGGCCAGGGGAGACTGCTGTACCAATTACCAAGTGGTTTGCAAAGGA
GAGTCGCATTGGGTTGATGATGACTGTGAGGAAATAAAGGCCGCAGAATGCCCTGCAGGG
TTTGTTCGCCCTCCATTAATCATCTTCTCCGTGGATGGCTTCCGTGCATCATACATGAAG
AAAGGCAGCAAAGTCATGCCTAATATTGAAAAACTAAGGTCTTGTGGCACACACTCTCCC
TACATGAGGCCGGTGTACCCAACTAAAACCTTTCCTAACTTATACACTTTGGCCACTGGG
CTATATCCAGAATCACATGGAATTGTTGGCAATTCAATGTATGATCCTGTATTTGATGCC
ACTTTTCATCTGCGAGGGCGAGAGAAATTTAATCATAGATGGTGGGGAGGTCAACCGCTA
TGGATTACAGCCACCAAGCAAGGGGTGAAAGCTGGAACATTCTTTTGGTCTGTTGTCATC
CCTCACGAGCGGAGAATATTAACCATATTGCAGTGGCTCACCCTGCCAGATCATGAGAGG
CCTTCGGTCTATGCCTTCTATTCTGAGCAACCTGATTTCTCTGGACACAAATATGGCCCT
TTCGGCCCTGAGATGACAAATCCTCTGAGGGAAATCGACAAAATTGTGGGGCAATTAATG
GATGGACTGAAACAACTAAAACTGCATCGGTGTGTCAACGTCATCTTTGTCGGAGACCAT
GGAATGGAAGATGTCACATGTGATAGAACTGAGTTCTTGAGTAATTACCTAACTAATGTG
GATGATATTACTTTAGTGCCTGGAACTCTAGGAAGAATTCGATCCAAATTTAGCAACAAT
GCTAAATATGACCCCAAAGCCATTATTGCCAATCTCACGTGTAAAAAACCAGATCAGCAC
TTTAAGCCTTACTTGAAACAGCACCTTCCCAAACGTTTGCACTATGCCAACAACAGAAGA
ATTGAGGATATCCATTTATTGGTGGAACGCAGATGGCATGTTGCAAGGAAACCTTTGGAT
GTTTATAAGAAACCATCAGGAAAATGCTTTTTCCAGGGAGACCACGGATTTGATAACAAG
GTCAACAGCATGCAGACTGTTTTTGTAGGTTATGGCTCAACATTTAAGTACAAGACTAAA
GTGCCTCCATTTGAAAACATTGAACTTTACAATGTTATGTGTGATCTCCTGGGATTGAAG
CCAGCTCCTAATAATGGGACCCATGGAAGTTTGAATCATCTCCTGCGCACTAATACCTTC
AGGCCAACCATGCCAGAGGAAGTTACCAGACCCAATTATCCAGGGATTATGTACCTTCAG
TCTGATTTTGACCTGGGCTGCACTTGTGATGATAAGGTAGAGCCAAAGAACAAGTTGGAT
GAACTCAACAAACGGCTTCATACAAAAGGGTCTACAGAAGAGAGACACCTCCTCTATGGG
CGACCTGCAGTGCTTTATCGGACTAGATATGATATCTTATATCACACTGACTTTGAAAGT
GGTTATAGTGAAATATTCCTAATGCCACTCTGGACATCATATACTGTTTCCAAACAGGCT
GAGGTTTCCAGCGTTCCTGACCATCTGACCAGTTGCGTCCGGCCTGATGTCCGTGTTTCT
CCGAGTTTCAGTCAGAACTGTTTGGCCTACAAAAATGATAAGCAGATGTCCTACGGATTC
CTCTTTCCTCCTTATCTGAGCTCTTCACCAGAGGCTAAATATGATGCATTCCTTGTAACC
AATATGGTTCCAATGTATCCTGCTTTCAAACGGGTCTGGAATTATTTCCAAAGGGTATTG
GTGAAGAAATATGCTTCGGAAAGAAATGGAGTTAACGTGATAAGTGGACCAATCTTCGAC
TATGACTATGATGGCTTACATGACACAGAAGACAAAATAAAACAGTACGTGGAAGGCAGT
TCCATTCCTGTTCCAACTCACTACTACAGCATCATCACCAGCTGTCTGGATTTCACTCAG
CCTGCCGACAAGTGTGACGGCCCTCTCTCTGTGTCCTCCTTCATCCTGCCTCACCGGCCT
GACAACGAGGAGAGCTGCAATAGCTCAGAGGACGAATCAAAATGGGTAGAAGAACTCATG
AAGATGCACACAGCTAGGGTGCGTGACATTGAACATCTCACCAGCCTGGACTTCTTCCGA
AAGACCAGCCGCAGCTACCCAGAAATCCTGACACTCAAGACATACCTGCATACATATGAG
AGCGAGATTTAA
Enzyme 2 GenBank Gene ID NM_001040092.1 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. 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]
  3. 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]
  4. van Meeteren LA, Ruurs P, Christodoulou E, Goding JW, Takakusa H, Kikuchi K, Perrakis A, Nagano T, Moolenaar WH: Inhibition of autotaxin by lysophosphatidic acid and sphingosine 1-phosphate. J Biol Chem. 2005 Jun 3;280(22):21155-61. Epub 2005 Mar 15. [PubMed Link Image]
  5. Giganti A, Rodriguez M, Fould B, Moulharat N, Coge F, Chomarat P, Galizzi JP, Valet P, Saulnier-Blache JS, Boutin JA, Ferry G: Murine and human autotaxin alpha, beta, and gamma isoforms: gene organization, tissue distribution, and biochemical characterization. J Biol Chem. 2008 Mar 21;283(12):7776-89. Epub 2008 Jan 6. [PubMed Link Image]
  6. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Tokumura A, Majima E, Kariya Y, Tominaga K, Kogure K, Yasuda K, Fukuzawa K: Identification of human plasma lysophospholipase D, a lysophosphatidic acid-producing enzyme, as autotaxin, a multifunctional phosphodiesterase. J Biol Chem. 2002 Oct 18;277(42):39436-42. Epub 2002 Aug 9. [PubMed Link Image]
  9. Stracke ML, Krutzsch HC, Unsworth EJ, Arestad A, Cioce V, Schiffmann E, Liotta LA: Identification, purification, and partial sequence analysis of autotaxin, a novel motility-stimulating protein. J Biol Chem. 1992 Feb 5;267(4):2524-9. [PubMed Link Image]
  10. Nam SW, Clair T, Kim YS, McMarlin A, Schiffmann E, Liotta LA, Stracke ML: Autotaxin (NPP-2), a metastasis-enhancing motogen, is an angiogenic factor. Cancer Res. 2001 Sep 15;61(18):6938-44. [PubMed Link Image]
  11. Boucher J, Quilliot D, Praderes JP, Simon MF, Gres S, Guigne C, Prevot D, Ferry G, Boutin JA, Carpene C, Valet P, Saulnier-Blache JS: Potential involvement of adipocyte insulin resistance in obesity-associated up-regulation of adipocyte lysophospholipase D/autotaxin expression. Diabetologia. 2005 Mar;48(3):569-77. Epub 2005 Feb 8. [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. PAP2-gamma
  2. PAP2-G
  3. Phosphatidate phosphohydrolase type 2c
  4. Phosphatidic acid phosphatase 2c
  5. PAP-2c
  6. PAP2c
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 32573.4
Enzyme 3 Theoretical pI 8.44
Enzyme 3 GO Classification
Function
  • catalytic activity
Process
Component
  • cell part
  • membrane
Enzyme 3 General Function Involved in catalytic activity
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 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate [RN:R02239]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 5-25 52-72 88-108 163-183 197-217 227-247
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 4505977 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 NM_003712.2 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 1
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]
  3. Hooks SB, Ragan SP, Lynch KR: Identification of a novel human phosphatidic acid phosphatase type 2 isoform. FEBS Lett. 1998 May 8;427(2):188-92. [PubMed Link Image]
  4. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [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. DAG kinase alpha
  2. 80 kDa diacylglycerol kinase
  3. Diglyceride kinase alpha
  4. DGK-alpha
Enzyme 4 Gene Name DGKA
Enzyme 4 Protein Sequence >Diacylglycerol kinase alpha
MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIY
LEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFK
LYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEW
VRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKY
TVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHC
VWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNL
STSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRL
FKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQ
NLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIM
REKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVL
NIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLE
GAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDGEPWMQTPCTIKITHKNQMPML
MGPPPRSTNFFGFLS
Enzyme 4 Number of Residues 735
Enzyme 4 Molecular Weight 82629.5
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
  • metal ion binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 4 General Function Involved in diacylglycerol kinase activity
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-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
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 1TUZ Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
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 1
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. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. 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]
  6. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  7. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [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. DAG kinase delta
  2. 130 kDa diacylglycerol kinase
  3. Diglyceride kinase delta
  4. DGK-delta
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 134524.2
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
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 5 General Function Involved in diacylglycerol kinase activity
Enzyme 5 Specific Function Isoform 2 may be involved in cell growth and tumorigenesis. Involved in clathrin-dependent endocytosis
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
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 1R79 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Imai S, Sakane F, Kanoh H: Phorbol ester-regulated oligomerization of diacylglycerol kinase delta linked to its phosphorylation and translocation. J Biol Chem. 2002 Sep 20;277(38):35323-32. Epub 2002 Jun 25. [PubMed Link Image]
  6. Kawasaki T, Kobayashi T, Ueyama T, Shirai Y, Saito N: Regulation of clathrin-dependent endocytosis by diacylglycerol kinase delta: importance of kinase activity and binding to AP2alpha. Biochem J. 2008 Jan 15;409(2):471-9. [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. PAP2-alpha
  2. Phosphatidate phosphohydrolase type 2a
  3. Phosphatidic acid phosphatase 2a
  4. PAP-2a
  5. PAP2a
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 32155.7
Enzyme 6 Theoretical pI 8.06
Enzyme 6 GO Classification
Function
  • catalytic activity
Process
Component
  • cell part
  • membrane
Enzyme 6 General Function Involved in catalytic activity
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 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate [RN:R02239]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 7-27 54-74 95-115 165-185 200-220 230-250
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]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Smyth SS, Sciorra VA, Sigal YJ, Pamuklar Z, Wang Z, Xu Y, Prestwich GD, Morris AJ: Lipid phosphate phosphatases regulate lysophosphatidic acid production and signaling in platelets: studies using chemical inhibitors of lipid phosphate phosphatase activity. J Biol Chem. 2003 Oct 31;278(44):43214-23. Epub 2003 Aug 8. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5470
Enzyme 7 Name Diacylglycerol kinase beta
Enzyme 7 Synonyms
  1. DAG kinase beta
  2. 90 kDa diacylglycerol kinase
  3. Diglyceride kinase beta
  4. DGK-beta
Enzyme 7 Gene Name DGKB
Enzyme 7 Protein Sequence >Diacylglycerol kinase beta
MTNQEKWAHLSPSEFSQLQKYAEYSTKKLKDVLEEFHGNGVLAKYNPEGKQDILNQTIDF
EGFKLFMKTFLEAELPDDFTAHLFMSFSNKFPHSSPMVKSKPALLSGGLRMNKGAITPPR
TTSPANTCSPEVIHLKDIVCYLSLLERGRPEDKLEFMFRLYDTDGNGFLDSSELENIISQ
MMHVAEYLEWDVTELNPILHEMMEEIDYDHDGTVSLEEWIQGGMTTIPLLVLLGLENNVK
DDGQHVWRLKHFNKPAYCNLCLNMLIGVGKQGLCCSFCKYTVHERCVARAPPSCIKTYVK
SKRNTDVMHHYWVEGNCPTKCDKCHKTVKCYQGLTGLHCVWCQITLHNKCASHLKPECDC
GPLKDHILPPTTICPVVLQTLPTSGVSVPEERQSTVKKEKSGSQQPNKVIDKNKMQRANS
VTVDGQGLQVTPVPGTHPLLVFVNPKSGGKQGERIYRKFQYLLNPRQVYSLSGNGPMPGL
NFFRDVPDFRVLACGGDGTVGWVLDCIEKANVGKHPPVAILPLGTGNDLARCLRWGGGYE
GENLMKILKDIENSTEIMLDRWKFEVIPNDKDEKGDPVPYSIINNYFSIGVDASIAHRFH
IMREKHPEKFNSRMKNKFWYFEFGTSETFSATCKKLHESVEIECDGVQIDLINISLEGIA
ILNIPSMHGGSNLWGESKKRRSHRRIEKKGSDKRTTVTDAKELKFASQDLSDQLLEVVGL
EGAMEMGQIYTGLKSAGRRLAQCSCVVIRTSKSLPMQIDGEPWMQTPCTIKITHKNQAPM
LMGPPPKTGLFCSLVKRTRNRSKE
Enzyme 7 Number of Residues 804
Enzyme 7 Molecular Weight 90594.7
Enzyme 7 Theoretical pI 7.90
Enzyme 7 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • diacylglycerol kinase activity
  • ion binding
  • kinase activity
  • metal ion binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 7 General Function Involved in diacylglycerol kinase activity
Enzyme 7 Specific Function Exhibits high phosphorylation activity for long-chain diacylglycerols
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 22027632 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9Y6T7 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name DGKB_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2415 bp
ATGACAAACCAGGAAAAATGGGCCCACCTCAGCCCTTCGGAATTTTCCCAACTTCAGAAA
TATGCTGAGTATTCTACAAAGAAATTAAAGGATGTTCTTGAAGAATTCCATGGTAATGGT
GTGCTTGCAAAGTATAATCCTGAAGGGAAACAAGACATTCTTAACCAAACAATAGATTTT
GAAGGTTTCAAACTATTCATGAAGACATTCCTGGAAGCCGAGCTTCCTGATGATTTCACT
GCACACCTTTTCATGTCATTTAGCAACAAGTTTCCTCATTCTAGTCCAATGGTAAAAAGT
AAGCCTGCTCTCCTATCAGGCGGTCTGAGAATGAATAAAGGTGCCATCACCCCTCCCCGG
ACTACTTCTCCTGCAAATACGTGTTCCCCAGAAGTAATCCATCTGAAGGACATTGTCTGT
TACCTGTCTCTGCTTGAAAGAGGAAGACCTGAGGATAAGCTTGAGTTTATGTTTCGCCTT
TATGACACGGATGGGAATGGCTTCCTGGACAGCTCGGAGCTAGAAAATATCATCAGTCAG
ATGATGCATGTTGCAGAATACCTTGAGTGGGATGTCACTGAACTTAATCCAATCCTCCAT
GAAATGATGGAAGAAATTGACTATGATCATGATGGAACCGTGTCTCTGGAGGAATGGATT
CAAGGAGGAATGACAACGATTCCACTTCTTGTGCTCCTGGGCTTAGAAAATAACGTGAAG
GATGATGGACAGCACGTGTGGCGACTGAAGCACTTTAACAAACCTGCCTATTGCAACCTT
TGCCTGAACATGCTGATTGGCGTGGGGAAGCAGGGCCTCTGCTGTTCCTTCTGCAAGTAC
ACAGTCCATGAGCGCTGTGTGGCTCGAGCACCTCCCTCTTGCATCAAGACCTATGTGAAG
TCCAAAAGGAACACTGATGTCATGCACCATTACTGGGTTGAAGGTAACTGCCCAACCAAG
TGTGATAAGTGCCACAAAACTGTTAAATGTTACCAGGGCCTGACAGGACTGCATTGTGTT
TGGTGTCAGATCACACTGCATAATAAATGTGCTTCTCATCTAAAACCTGAATGTGACTGT
GGACCTTTGAAGGACCATATTTTACCACCCACAACAATCTGTCCAGTGGTACTGCAGACT
CTGCCCACTTCAGGAGTTTCAGTTCCTGAGGAAAGACAATCAACAGTGAAAAAGGAAAAG
AGTGGTTCCCAGCAGCCAAACAAAGTGATTGACAAGAATAAAATGCAAAGAGCCAACTCT
GTTACTGTAGATGGACAAGGCCTGCAGGTCACTCCTGTGCCTGGTACTCACCCACTTTTA
GTTTTTGTGAACCCCAAAAGTGGTGGAAAACAAGGAGAACGAATTTACAGAAAATTCCAG
TATCTATTAAATCCTCGTCAGGTTTACAGTCTTTCTGGAAATGGACCAATGCCAGGGTTA
AACTTTTTCCGTGATGTTCCTGACTTCAGAGTGTTAGCCTGTGGTGGAGATGGAACCGTG
GGCTGGGTTTTGGATTGCATAGAAAAGGCCAATGTAGGCAAGCATCCTCCAGTTGCGATT
CTGCCTCTTGGGACTGGCAATGATCTAGCAAGATGCCTGCGATGGGGAGGAGGTTACGAA
GGTGAGAATCTGATGAAAATTCTAAAAGACATTGAAAACAGCACAGAAATCATGTTGGAC
AGGTGGAAGTTTGAAGTCATACCTAATGACAAAGATGAGAAAGGAGACCCAGTGCCTTAC
AGTATCATCAATAATTACTTTTCCATTGGCGTGGATGCCTCCATTGCACACAGATTCCAC
ATCATGAGAGAAAAACACCCAGAGAAATTCAACAGTAGAATGAAGAACAAATTTTGGTAT
TTTGAGTTTGGCACATCTGAAACTTTCTCAGCCACCTGCAAGAAGCTACATGAATCTGTA
GAAATAGAATGTGATGGAGTACAGATAGATTTAATAAACATCTCTCTGGAAGGAATTGCT
ATTTTGAATATACCAAGCATGCATGGAGGATCCAATCTTTGGGGAGAGTCTAAGAAAAGA
CGAAGCCATCGACGAATAGAGAAAAAAGGGTCTGACAAAAGGACCACCGTCACAGATGCC
AAAGAGTTGAAGTTTGCAAGTCAAGATCTCAGTGACCAGCTGCTGGAGGTGGTCGGCTTG
GAAGGAGCCATGGAGATGGGGCAAATATACACAGGCCTGAAAAGTGCTGGCCGGCGGCTG
GCTCAGTGCTCCTGCGTGGTCATCAGGACGAGCAAGTCTCTGCCAATGCAAATTGATGGG
GAGCCATGGATGCAGACCCCATGCACAATAAAAATTACACACAAGAACCAAGCCCCAATG
CTGATGGGCCCGCCTCCAAAAACCGGTTTATTCTGCTCCCTCGTCAAAAGGACAAGAAAC
CGAAGCAAGGAATAA
Enzyme 7 GenBank Gene ID NM_004080.2 Link Image
Enzyme 7 GeneCard ID DGKB Link Image
Enzyme 7 GenAtlas ID DGKB Link Image
Enzyme 7 HGNC ID HGNC:2850 Link Image
Enzyme 7 Chromosome Location 7
Enzyme 7 Locus 7p21.2
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  2. 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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Oct 30;5(5):277-86. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5472
Enzyme 8 Name Diacylglycerol kinase iota
Enzyme 8 Synonyms
  1. DAG kinase iota
  2. Diglyceride kinase iota
  3. DGK-iota
Enzyme 8 Gene Name DGKI
Enzyme 8 Protein Sequence >Diacylglycerol kinase iota
MDAAGRGCHLLPLPAARGPARAPAAAAAAAASPPGPCSGAACAPSAAAGAGAMNPSSSAG
EEKGATGGSSSSGSGAGSCCLGAEGGADPRGAGSAAAAGAAALDEPAAAGQKEKDEALEE
KLRNLTFRKQVSYRKAISRAGLQHLAPAHPLSLPVANGPAKEPRATLDWSENAVNGEHLW
LETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG
SRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCF
MLHHIEEPCSLGAHAAVIVPPTWIIKVKKPQNSLKASNRKKKRTSFKRKASKRGMEQENK
GRPFVIKPISSPLMKPLLVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEL
YRKVPNLRILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLARTLNWGGGYTDE
PVSKILCQVEDGTVVQLDRWNLHVERNPDLPPEELEDGVCKLPLNVFNNYFSLGFDAHVT
LEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIQEL
KFQCIVFLNIPRYCAGTMPWGNPGDHHDFEPQRHDDGYIEVIGFTMASLAALQVGGHGER
LHQCREVMLLTYKSIPMQVDGEPCRLAPAMIRISLRNQANMVQKSKRRTSMPLLNDPQSV
PDRLRIRVNKISLQDYEGFHYDKEKLREASISDWLRTIAGELVQSFGAIPLGILVVRGDC
DLETCRMYIDRLQEDLQSVSSGSQRVHYQDHETSFPRALSAQRLSPRWCFLDDRSQEHLH
FVMEISQDEIFILDPDMVVSQPAGTPPGMPDLVVEQASGISDWWNPALRKRMLSDSGLGM
IAPYYEDSDLKDLSHSRVLQSPVSSEDHAILQAVIAGDLMKLIESYKNGGSLLIQGPDHC
SLLHYAAKTGNGEIVKYILDHGPSELLDMADSETGETALHKAACQRNRAVCQLLVDAGAS
LRKTDSKGKTPQERAQQAGDPDLAAYLESRQNYKVIGHEDLETAV
Enzyme 8 Number of Residues 1065
Enzyme 8 Molecular Weight 116996.2
Enzyme 8 Theoretical pI 7.81
Enzyme 8 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
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 8 General Function Involved in diacylglycerol kinase activity
Enzyme 8 Specific Function ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl- sn-glycerol 3-phosphate
Enzyme 8 Pathways
Enzyme 8 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 3676530 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O75912 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name DGKI_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 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 8 GenBank Gene ID AF061936 Link Image
Enzyme 8 GeneCard ID DGKI Link Image
Enzyme 8 GenAtlas ID DGKI Link Image
Enzyme 8 HGNC ID HGNC:2855 Link Image
Enzyme 8 Chromosome Location 7
Enzyme 8 Locus 7q32.3-q33
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 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. 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]
  3. 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]
  4. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5474
Enzyme 9 Name Lipid phosphate phosphohydrolase 3
Enzyme 9 Synonyms
  1. PAP2-beta
  2. Phosphatidate phosphohydrolase type 2b
  3. Phosphatidic acid phosphatase 2b
  4. PAP-2b
  5. PAP2b
  6. Vascular endothelial growth factor and type I collagen-inducible protein
  7. VCIP
Enzyme 9 Gene Name PPAP2B
Enzyme 9 Protein Sequence >Lipid phosphate phosphohydrolase 3
MQNYKYDKAIVPESKNGGSPALNNNPRRSGSKRVLLICLDLFCLFMAGLPFLIIETSTIK
PYHRGFYCNDESIKYPLKTGETINDAVLCAVGIVIAILAIITGEFYRIYYLKKSRSTIQN
PYVAALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLSVCNPDFSQINCSEGYIQNYR
CRGDDSKVQEARKSFFSGHASFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFY
TGLSRVSDHKHHPSDVLAGFAQGALVACCIVFFVSDLFKTKTTLSLPAPAIRKEILSPVD
IIDRNNHHNMM
Enzyme 9 Number of Residues 311
Enzyme 9 Molecular Weight 35115.6
Enzyme 9 Theoretical pI 9.40
Enzyme 9 GO Classification
Function
  • catalytic activity
Process
Component
  • cell part
  • membrane
Enzyme 9 General Function Involved in catalytic activity
Enzyme 9 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 9 Pathways
Enzyme 9 Reactions
  • a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate [RN:R02239]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • 34-54 86-106 123-143 194-214 228-248 258-278
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID O14495 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name LPP3_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >936 bp
ATGCAAAACTACAAGTACGACAAAGCGATCGTCCCGGAGAGCAAGAACGGCGGCAGCCCG
GCGCTCAACAACAACCCGAGGAGGAGCGGCAGCAAGCGGGTGCTGCTCATCTGCCTCGAC
CTCTTCTGCCTCTTCATGGCGGGCCTCCCCTTCCTCATCATCGAGACAAGCACCATCAAG
CCTTACCACCGAGGGTTTTACTGCAATGATGAGAGCATCAAGTACCCACTGAAAACTGGT
GAGACAATAAATGACGCTGTGCTCTGTGCCGTGGGGATCGTCATTGCCATCCTCGCGATC
ATCACGGGGGAATTCTACCGGATCTATTACCTGAAGAAGTCGCGGTCGACGATTCAGAAC
CCCTACGTGGCAGCACTCTATAAGCAAGTGGGCTGCTTCCTCTTTGGCTGTGCCATCAGC
CAGTCTTTCACAGACATTGCCAAAGTGTCCATAGGGCGCCTGCGTCCTCACTTCTTGAGT
GTCTGCAACCCTGATTTCAGCCAGATCAACTGCTCTGAAGGCTACATTCAGAACTACAGA
TGCAGAGGTGATGACAGCAAAGTCCAGGAAGCCAGGAAGTCCTTCTTCTCTGGCCATGCC
TCCTTCTCCATGTACACTATGCTGTATTTGGTGCTATACCTGCAGGCCCGCTTCACTTGG
CGAGGAGCCCGCCTGCTCCGGCCCCTCCTGCAGTTCACCTTGATCATGATGGCCTTCTAC
ACGGGACTGTCTCGCGTATCAGACCACAAGCACCATCCCAGTGATGTTCTGGCAGGATTT
GCTCAAGGAGCCCTGGTGGCCTGCTGCATAGTTTTCTTCGTGTCTGACCTCTTCAAGACT
AAGACGACGCTCTCCCTGCCTGCCCCTGCTATCCGGAAGGAAATCCTTTCACCTGTGGAC
ATTATTGACAGGAACAATCACCACAACATGATGTAG
Enzyme 9 GenBank Gene ID AB000889 Link Image
Enzyme 9 GeneCard ID PPAP2B Link Image
Enzyme 9 GenAtlas ID PPAP2B Link Image
Enzyme 9 HGNC ID HGNC:9229 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 1pter-p22.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Burnett C, Makridou P, Hewlett L, Howard K: Lipid phosphate phosphatases dimerise, but this interaction is not required for in vivo activity. BMC Biochem. 2004 Jan 16;5:2. [PubMed Link Image]
  8. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  9. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5478
Enzyme 10 Name Diacylglycerol kinase zeta
Enzyme 10 Synonyms
  1. DAG kinase zeta
  2. Diglyceride kinase zeta
  3. DGK-zeta
Enzyme 10 Gene Name DGKZ
Enzyme 10 Protein Sequence >Diacylglycerol kinase zeta
METFFRRHFRGKVPGPGEGQQRPSSVGLPTGKARRRSPAGQASSSLAQRRRSSAQLQGCL
LSCGVRAQGSSRRRSSTVPPSCNPRFIVDKVLTPQPTTVGAQLLGAPLLLTGLVGMNEEE
GVQEDVVAEASSAIQPGTKTPGPPPPRGAQPLLPLPRYLRRASSHLLPADAVYDHALWGL
HGYYRRLSQRRPSGQHPGPGGRRASGTTAGTMLPTRVRPLSRRRQVALRRKAAGPQAWSA
LLAKAITKSGLQHLAPPPPTPGAPCSESERQIRSTVDWSESATYGEHIWFETNVSGDFCY
VGEQYCVARMLKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESGSRNVREPTFVR
HHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCS
LGVHAAVVIPPTWILRARRPQNTLKASKKKKRASFKRKSSKKGPEEGRWRPFIIRPTPSP
LMKPLLVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHNLRILAC
GGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEG
NVVQLDRWDLHAEPNPEAGPEDRDEGATDRLPLDVFNNYFSLGFDAHVTLEFHESREANP
EKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIQDLKPQCVVFLNIP
RYCAGTMPWGHPGEHHDFEPQRHDDGYLEVIGFTMTSLAALQVGGHGERLTQCREVVLTT
SKAIPVQVDGEPCKLAASRIRIALRNQATMVQKAKRRSAAPLHSDQQPVPEQLRIQVSRV
SMHDYEALHYDKEQLKEASVPLGTVVVPGDSDLELCRAHIERLQQEPDGAGAKSPTCQKL
SPKWCFLDATTASRFYRIDRAQEHLNYVTEIAQDEIYILDPELLGASARPDLPTPTSPLP
TSPCSPTPRSLQGDAAPPQGEELIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAV
STGSKDVVRYLLDHAPPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQG
DTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETAV
Enzyme 10 Number of Residues 1117
Enzyme 10 Molecular Weight 124127.3
Enzyme 10 Theoretical pI 9.31
Enzyme 10 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
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 10 General Function Involved in diacylglycerol kinase activity
Enzyme 10 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. Isoform 2 but not isoform 1 regulates RASGRP1 activity
Enzyme 10 Pathways
Enzyme 10 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 157688564 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q13574 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name DGKZ_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >3354 bp
ATGGAGACTTTCTTTAGGAGACATTTCCGGGGGAAGGTGCCAGGCCCTGGAGAGGGGCAG
CAGCGGCCCAGCAGCGTGGGGCTGCCCACAGGCAAGGCCCGGCGTCGCTCCCCCGCTGGG
CAGGCCTCCTCCTCACTGGCACAGCGGCGCCGCTCCAGCGCCCAGCTCCAGGGCTGCCTC
CTGAGTTGCGGGGTGAGGGCCCAGGGTTCCAGCCGCCGGCGCTCCAGCACTGTGCCCCCT
TCCTGCAACCCCCGCTTCATCGTGGATAAGGTGCTCACTCCACAGCCTACCACCGTGGGG
GCCCAGCTTCTGGGTGCACCCCTGCTGTTGACCGGGCTTGTGGGCATGAATGAGGAGGAG
GGTGTCCAGGAGGATGTGGTAGCCGAGGCATCGAGCGCCATCCAGCCAGGCACCAAGACA
CCAGGGCCACCCCCACCTCGGGGCGCCCAGCCGCTGTTGCCCCTACCCCGCTACCTGCGC
CGAGCCTCCTCCCACCTGCTCCCCGCGGATGCCGTATATGACCACGCTCTCTGGGGCCTG
CACGGCTACTATCGGCGCCTCAGCCAGCGGCGGCCCTCAGGCCAGCACCCTGGCCCTGGG
GGCCGAAGAGCCTCAGGCACCACCGCCGGCACCATGCTGCCCACCCGTGTGCGCCCACTG
TCCCGCAGGCGCCAGGTAGCCCTACGGCGCAAGGCGGCCGGACCCCAGGCCTGGAGCGCC
CTGCTCGCGAAAGCCATCACCAAGTCGGGCCTCCAGCACCTGGCCCCCCCTCCGCCCACC
CCTGGGGCCCCGTGCAGCGAGTCAGAGCGGCAGATCCGGAGTACAGTGGACTGGAGCGAG
TCAGCGACATATGGGGAGCACATCTGGTTCGAGACCAACGTGTCCGGGGACTTCTGCTAC
GTTGGGGAGCAGTACTGTGTAGCCAGGATGCTGAAGTCAGTGTCTCGAAGAAAGTGCGCA
GCCTGCAAGATTGTGGTGCACACGCCCTGCATCGAGCAGCTGGAGAAGATAAATTTCCGC
TGTAAGCCGTCCTTCCGTGAATCAGGCTCCAGGAATGTCCGCGAGCCAACCTTTGTACGG
CACCACTGGGTACACAGACGACGCCAGGACGGCAAGTGTCGGCACTGTGGGAAGGGATTC
CAGCAGAAGTTCACCTTCCACAGCAAGGAGATTGTGGCCATCAGCTGCTCGTGGTGCAAG
CAGGCATACCACAGCAAGGTGTCCTGCTTCATGCTGCAGCAGATCGAGGAGCCGTGCTCG
CTGGGGGTCCACGCAGCCGTGGTCATCCCGCCCACCTGGATCCTCCGCGCCCGGAGGCCC
CAGAATACTCTGAAAGCAAGCAAGAAGAAGAAGAGGGCATCCTTCAAGAGGAAGTCCAGC
AAGAAAGGGCCTGAGGAGGGCCGCTGGAGACCCTTCATCATCAGGCCCACCCCCTCCCCG
CTCATGAAGCCCCTGCTGGTGTTTGTGAACCCCAAGAGTGGGGGCAACCAGGGTGCAAAG
ATCATCCAGTCTTTCCTCTGGTATCTCAATCCCCGACAAGTCTTCGACCTGAGCCAGGGA
GGGCCCAAGGAGGCGCTGGAGATGTACCGCAAAGTGCACAACCTGCGGATCCTGGCGTGC
GGGGGCGACGGCACGGTGGGCTGGATCCTCTCCACCCTGGACCAGCTACGCCTGAAGCCG
CCACCCCCTGTTGCCATCCTGCCCCTGGGTACTGGCAACGACTTGGCCCGAACCCTCAAC
TGGGGTGGGGGCTACACAGATGAGCCTGTGTCCAAGATCCTCTCCCACGTGGAGGAGGGG
AACGTGGTACAGCTGGACCGCTGGGACCTCCACGCTGAGCCCAACCCCGAGGCAGGGCCT
GAGGACCGAGATGAAGGCGCCACCGACCGGTTGCCCCTGGATGTCTTCAACAACTACTTC
AGCCTGGGCTTTGACGCCCACGTCACCCTGGAGTTCCACGAGTCTCGAGAGGCCAACCCA
GAGAAATTCAACAGCCGCTTTCGGAATAAGATGTTCTACGCCGGGACAGCTTTCTCTGAC
TTCCTGATGGGCAGCTCCAAGGACCTGGCCAAGCACATCCGAGTGGTGTGTGATGGAATG
GACTTGACTCCCAAGATCCAGGACCTGAAACCCCAGTGTGTTGTTTTCCTGAACATCCCC
AGGTACTGTGCGGGCACCATGCCCTGGGGCCACCCTGGGGAGCACCACGACTTTGAGCCC
CAGCGGCATGACGACGGCTACCTCGAGGTCATTGGCTTCACCATGACGTCGTTGGCCGCG
CTGCAGGTGGGCGGACACGGCGAGCGGCTGACGCAGTGTCGCGAGGTGGTGCTCACCACA
TCCAAGGCCATCCCGGTGCAGGTGGATGGCGAGCCCTGCAAGCTTGCAGCCTCACGCATC
CGCATCGCCCTGCGCAACCAGGCCACCATGGTGCAGAAGGCCAAGCGGCGGAGCGCCGCC
CCCCTGCACAGCGACCAGCAGCCGGTGCCAGAGCAGTTGCGCATCCAGGTGAGTCGCGTC
AGCATGCACGACTATGAGGCCCTGCACTACGACAAGGAGCAGCTCAAGGAGGCCTCTGTG
CCGCTGGGCACTGTGGTGGTCCCAGGAGACAGTGACCTAGAGCTCTGCCGTGCCCACATT
GAGAGACTCCAGCAGGAGCCCGATGGTGCTGGAGCCAAGTCCCCGACATGCCAGAAACTG
TCCCCCAAGTGGTGCTTCCTGGACGCCACCACTGCCAGCCGCTTCTACAGGATCGACCGA
GCCCAGGAGCACCTCAACTATGTGACTGAGATCGCACAGGATGAGATTTATATCCTGGAC
CCTGAGCTGCTGGGGGCATCGGCCCGGCCTGACCTCCCAACCCCCACTTCCCCTCTCCCC
ACCTCACCCTGCTCACCCACGCCCCGGTCACTGCAAGGGGATGCTGCACCCCCTCAAGGT
GAAGAGCTGATTGAGGCTGCCAAGAGGAACGACTTCTGTAAGCTCCAGGAGCTGCACCGA
GCTGGGGGCGACCTCATGCACCGAGACGAGCAGAGTCGCACGCTCCTGCACCACGCAGTC
AGCACTGGCAGCAAGGATGTGGTCCGCTACCTGCTGGACCACGCCCCCCCAGAGATCCTT
GATGCGGTGGAGGAAAACGGGGAGACCTGTTTGCACCAAGCAGCGGCCCTGGGCCAGCGC
ACCATCTGCCACTACATCGTGGAGGCCGGGGCCTCGCTCATGAAGACAGACCAGCAGGGC
GACACTCCCCGGCAGCGGGCTGAGAAGGCTCAGGACACCGAGCTGGCCGCCTACCTGGAG
AACCGGCAGCACTACCAGATGATCCAGCGGGAGGACCAGGAGACGGCTGTGTAG
Enzyme 10 GenBank Gene ID NM_001105540.1 Link Image
Enzyme 10 GeneCard ID DGKZ Link Image
Enzyme 10 GenAtlas ID DGKZ Link Image
Enzyme 10 HGNC ID HGNC:2857 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 11p11.2
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed Link Image]
  4. 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]
  5. 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]
  6. Topham MK, Prescott SM: Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism. J Cell Biol. 2001 Mar 19;152(6):1135-43. [PubMed Link Image]
  7. Rincon E, Santos T, Avila-Flores A, Albar JP, Lalioti V, Lei C, Hong W, Merida I: Proteomics identification of sorting nexin 27 as a diacylglycerol kinase zeta-associated protein: new diacylglycerol kinase roles in endocytic recycling. Mol Cell Proteomics. 2007 Jun;6(6):1073-87. Epub 2007 Mar 9. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6021
Enzyme 11 Name Phosphatidate cytidylyltransferase 2
Enzyme 11 Synonyms
  1. CDP-DAG synthase 2
  2. CDP-DG synthase 2
  3. CDP-diacylglycerol synthase 2
  4. CDS 2
  5. CDP-diglyceride pyrophosphorylase 2
  6. CDP-diglyceride synthase 2
  7. CTP:phosphatidate cytidylyltransferase 2
Enzyme 11 Gene Name CDS2
Enzyme 11 Protein Sequence >Phosphatidate cytidylyltransferase 2
MTELRQRVAHEPVAPPEDKESESEAKVDGETASDSESRAESAPLPVSADDTPEVLNRALS
NLSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMIIVMCVQIKCFHEIITIGYNVYHSY
DLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFTLYLIGFCM
FVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAY
MFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSF
TVDCEPSDLFRLQEYNIPGVIQSVIGWKTVRMYPFQIHSIALSTFASLIGPFGGFFASGF
KRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLIQQFLTLRPDQ
QLHIFNTLRSHLIDKGMLTSTTEDE
Enzyme 11 Number of Residues 445
Enzyme 11 Molecular Weight 51417.5
Enzyme 11 Theoretical pI 7.10
Enzyme 11 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
Component
  • cell part
  • membrane
Enzyme 11 General Function Involved in transferase activity, transferring phosphorus-containing groups
Enzyme 11 Specific Function Provides CDP-diacylglycerol an important precursor for the synthesis of phosphatidylinositol, phosphatidylglycerol, and cardiolipin
Enzyme 11 Pathways
Enzyme 11 Reactions
  • CTP + phosphatidate = diphosphate + CDP-diacylglycerol [RN:R01799]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • 79-99 132-152 166-186 213-233 262-282 340-360
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 4186023 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID O95674 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name CDS2_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1338 bp
ATGACAGAGCTGAGGCAGAGGGTGGCCCATGAGCCGGTTGCGCCACCCGAGGACAAGGAG
TCAGAGTCAGAAGCAAAGGTAGATGGAGAGACTGCATCGGACAGTGAGAGCCGGGCAGAA
TCCGCACCCCTGCCAGTCTCTGCAGATGATACCCCGGAGGTCCTCAATAGGGCCCTTTCC
AACTTGTCTTCAAGATGGAAGAACTGGTGGGTGAGAGGCATCCTGACTTTGGCCATGATT
GCATTTTTCTTCATCATCATTTACCTGGGACCAATGGTTTTGATGATAATCGTGATGTGC
GTTCAGATTAAGTGTTTCCATGAGATAATCACTATTGGCTACAACGTCTACCACTCATAT
GATCTGCCCTGGTTCAGGACGCTCAGCTGGTACTTTCTCCTGTGTGTAAACTATTTCTTC
TATGGTGAGACAGTGACGGATTACTTCTTCACCCTGGTCCAGAGAGAAGAGCCTTTGCGG
ATTCTCAGTAAATACCACCGGTTCATTTCCTTTACTCTCTATCTAATAGGATTCTGCATG
TTTGTACTGAGTCTGGTCAAGAAGCATTATCGACTGCAGTTCTACATGTTTGGCTGGACC
CATGTGACATTGCTGATTGTTGTAACACAGTCACATCTTGTTATCCACAACCTATTTGAA
GGAATGATCTGGTTCATTGTCCCCATATCTTGTGTGATCTGTAATGACATCATGGCCTAT
ATGTTTGGCTTTTTCTTTGGTCGGACCCCACTCATCAAGCTGTCCCCGAAGAAGACCTGG
GAAGGCTTCATTGGGGGCTTCTTTGCTACTGTGGTGTTTGGCCTTCTGCTGTCCTATGTG
ATGTCCGGGTACAGATGCTTTGTCTGCCCTGTGGAGTACAACAATGACACCAACAGCTTC
ACTGTGGACTGTGAGCCCTCGGACCTGTTTCGCCTGCAGGAGTACAACATTCCTGGGGTG
ATCCAGTCAGTCATTGGCTGGAAAACGGTCCGGATGTACCCCTTCCAGATTCACAGCATC
GCTCTCTCCACCTTTGCCTCGCTCATTGGCCCCTTTGGAGGATTCTTCGCAAGTGGATTC
AAACGAGCCTTTAAAATCAAAGACTTTGCCAATACCATTCCTGGCCATGGAGGCATCATG
GATCGCTTTGACTGCCAGTATCTGATGGCCACCTTTGTCAATGTATACATCGCCAGTTTT
ATCAGAGGCCCTAACCCAAGCAAACTGATTCAGCAGTTCCTGACTTTACGGCCAGATCAG
CAGCTCCACATCTTCAACACGCTGCGGTCTCATCTGATCGACAAAGGGATGCTGACATCC
ACCACAGAGGACGAGTAG
Enzyme 11 GenBank Gene ID Y16521 Link Image
Enzyme 11 GeneCard ID CDS2 Link Image
Enzyme 11 GenAtlas ID CDS2 Link Image
Enzyme 11 HGNC ID HGNC:1801 Link Image
Enzyme 11 Chromosome Location 2
Enzyme 11 Locus 20p13
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Volta M, Bulfone A, Gattuso C, Rossi E, Mariani M, Consalez GG, Zuffardi O, Ballabio A, Banfi S, Franco B: Identification and characterization of CDS2, a mammalian homolog of the Drosophila CDP-diacylglycerol synthase gene. Genomics. 1999 Jan 1;55(1):68-77. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Halford S, Dulai KS, Daw SC, Fitzgibbon J, Hunt DM: Isolation and chromosomal localization of two human CDP-diacylglycerol synthase (CDS) genes. Genomics. 1998 Nov 15;54(1):140-4. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed Link Image]
  10. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6040
Enzyme 12 Name Phosphatidate cytidylyltransferase 1
Enzyme 12 Synonyms
  1. CDP-DAG synthase 1
  2. CDP-DG synthase 1
  3. CDP-diacylglycerol synthase 1
  4. CDS 1
  5. CDP-diglyceride pyrophosphorylase 1
  6. CDP-diglyceride synthase 1
  7. CTP:phosphatidate cytidylyltransferase 1
Enzyme 12 Gene Name CDS1
Enzyme 12 Protein Sequence >Phosphatidate cytidylyltransferase 1
MLELRHRGSCPGPREAVSPPHREGEAAGGDHETESTSDKETDIDDRYGDLDSRTDSDIPE
IPPSSDRTPEILKKALSGLSSRWKNWWIRGILTLTMISLFFLIIYMGSFMLMLLVLGIQV
KCFHEIITIGYRVYHSYDLPWFRTLSWYFLLCVNYFFYGETVADYFATFVQREEQLQFLI
RYHRFISFALYLAGFCMFVLSLVKKHYRLQFYMFAWTHVTLLITVTQSHLVIQNLFEGMI
WFLVPISSVICNDITAYLFGFFFGRTPLIKLSPKKTWEGFIGGFFSTVVFGFIAAYVLSK
YQYFVCPVEYRSDVNSFVTECEPSELFQLQTYSLPPFLKAVLRQERVSLYPFQIHSIALS
TFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVHVYITSFIRG
PNPSKVLQQLLVLQPEQQLNIYKTLKTHLIEKGILQPTLKV
Enzyme 12 Number of Residues 461
Enzyme 12 Molecular Weight 53303.6
Enzyme 12 Theoretical pI 8.19
Enzyme 12 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
Component
  • cell part
  • membrane
Enzyme 12 General Function Involved in transferase activity, transferring phosphorus-containing groups
Enzyme 12 Specific Function Provides CDP-diacylglycerol an important precursor for the synthesis of phosphatidylinositol (PtdIns), phosphatidylglycerol, and cardiolipin. Overexpression may amplify cellular signaling responses from cytokines. May also play an important role in the signal transduction mechanism of retina and neural cells
Enzyme 12 Pathways
Enzyme 12 Reactions
  • CTP + phosphatidate = diphosphate + CDP-diacylglycerol [RN:R01799]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 96-116 149-169 183-203 230-250 279-299 357-377
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 189054385 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q92903 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name CDS1_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1386 bp
ATGTTGGAGCTGAGGCACCGGGGAAGCTGCCCCGGCCCCAGGGAAGCGGTGTCGCCGCCA
CACCGCGAGGGAGAGGCGGCCGGCGGCGACCACGAAACCGAGAGCACCAGCGACAAAGAA
ACAGATATTGATGACAGATATGGAGATTTGGATTCCAGAACAGATTCTGATATTCCGGAA
ATTCCACCATCCTCAGATAGAACCCCTGAGATTCTCAAAAAAGCTCTATCTGGTTTATCT
TCAAGGTGGAAAAACTGGTGGATACGTGGAATTCTCACTCTAACTATGATCTCGTTGTTT
TTCCTGATCATCTATATGGGATCCTTCATGCTGATGCTTCTTGTTCTGGGCATCCAAGTG
AAATGCTTCCATGAAATTATCACTATAGGTTATAGAGTCTATCATTCTTATGATCTACCA
TGGTTTAGAACACTAAGTTGGTACTTTCTATTGTGTGTAAACTACTTTTTCTATGGAGAG
ACTGTAGCTGATTATTTTGCTACATTTGTTCAAAGAGAAGAACAACTTCAGTTCCTCATT
CGCTACCATAGATTTATATCATTTGCCCTCTATCTGGCAGGTTTCTGCATGTTTGTACTG
AGTTTGGTGAAGAAACATTATCGTCTGCAGTTTTATATGTTCGCATGGACTCATGTCACT
TTACTGATAACTGTCACTCAGTCACACCTTGTCATCCAAAATCTGTTTGAAGGCATGATA
TGGTTCCTTGTTCCAATATCAAGTGTTATCTGCAATGACATAACTGCTTACCTTTTTGGA
TTTTTTTTTGGGAGAACTCCATTAATTAAGTTGTCTCCTAAAAAGACTTGGGAAGGATTC
ATTGGTGGTTTCTTTTCCACAGTTGTGTTTGGATTCATTGCTGCCTATGTGTTATCCAAA
TACCAGTACTTTGTCTGCCCAGTGGAATACCGAAGTGATGTAAACTCCTTCGTGACAGAA
TGTGAGCCCTCAGAACTTTTCCAGCTTCAGACTTACTCACTTCCACCCTTTCTAAAGGCA
GTCTTGAGACAGGAAAGAGTGAGCTTGTACCCTTTCCAGATCCACAGCATTGCACTGTCA
ACCTTTGCATCTTTAATTGGCCCATTTGGAGGCTTCTTTGCTAGTGGATTCAAAAGAGCC
TTCAAAATCAAGGATTTTGCAAATACCATTCCTGGACATGGTGGGATAATGGACAGATTT
GATTGTCAGTATTTGATGGCAACTTTTGTACATGTGTACATCACAAGTTTTATAAGGGGC
CCAAATCCCAGCAAAGTGCTACAGCAGTTGTTGGTGCTTCAACCTGAACAGCAGTTAAAT
ATATATAAAACCCTGAAGACTCATCTCATTGAGAAAGGAATCCTACAACCCACCTTGAAG
GTATAA
Enzyme 12 GenBank Gene ID AK314245 Link Image
Enzyme 12 GeneCard ID CDS1 Link Image
Enzyme 12 GenAtlas ID CDS1 Link Image
Enzyme 12 HGNC ID HGNC:1800 Link Image
Enzyme 12 Chromosome Location 4
Enzyme 12 Locus 4q21.23
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Heacock AM, Uhler MD, Agranoff BW: Cloning of CDP-diacylglycerol synthase from a human neuronal cell line. J Neurochem. 1996 Nov;67(5):2200-3. [PubMed Link Image]
  2. Weeks R, Dowhan W, Shen H, Balantac N, Meengs B, Nudelman E, Leung DW: Isolation and expression of an isoform of human CDP-diacylglycerol synthase cDNA. DNA Cell Biol. 1997 Mar;16(3):281-9. [PubMed Link Image]
  3. Lykidis A, Jackson PD, Rock CO, Jackowski S: The role of CDP-diacylglycerol synthetase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content. J Biol Chem. 1997 Dec 26;272(52):33402-9. [PubMed Link Image]
  4. Halford S, Dulai KS, Daw SC, Fitzgibbon J, Hunt DM: Isolation and chromosomal localization of two human CDP-diacylglycerol synthase (CDS) genes. Genomics. 1998 Nov 15;54(1):140-4. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6421
Enzyme 13 Name Acyl-CoA:lysophosphatidylglycerol acyltransferase 1
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name LPGAT1
Enzyme 13 Protein Sequence >Acyl-CoA:lysophosphatidylglycerol acyltransferase 1
MAITLEEAPWLGWLLVKALMRFAFMVVNNLVAIPSYICYVIILQPLRVLDSKRFWYIEGI
MYKWLLGMVASWGWYAGYTVMEWGEDIKAVSKDEAVMLVNHQATGDVCTLMMCLQDKGLV
VAQMMWLMDHIFKYTNFGIVSLVHGDFFIRQGRSYRDQQLLLLKKHLENNYRSRDRKWIV
LFPEGGFLRKRRETSQAFAKKNNLPFLTNVTLPRSGATKIILNALVAQQKNGSPAGGDAK
ELDSKSKGLQWIIDTTIAYPKAEPIDIQTWILGYRKPTVTHVHYRIFPIKDVPLETDDLT
TWLYQRFVEKEDLLSHFYETGAFPPSKGHKEAVSREMTLSNLWIFLIQSFAFLSGYMWYN
IIQYFYHCLF
Enzyme 13 Number of Residues 370
Enzyme 13 Molecular Weight 43089.1
Enzyme 13 Theoretical pI 9.24
Enzyme 13 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 13 General Function Involved in acyltransferase activity
Enzyme 13 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 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • 22-42 342-362
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 22902215 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q92604 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name LGAT1_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1113 bp
ATGGCTATAACTTTGGAAGAAGCTCCGTGGCTGGGCTGGCTCTTGGTGAAAGCACTGATG
AGGTTTGCCTTCATGGTCGTCAACAACCTGGTTGCTATTCCATCCTACATCTGCTATGTA
ATTATACTTCAGCCCCTTCGAGTGCTGGACAGTAAGCGGTTCTGGTATATCGAAGGAATC
ATGTATAAATGGCTTTTAGGAATGGTAGCTTCCTGGGGATGGTATGCTGGATATACAGTG
ATGGAATGGGGAGAAGATATTAAAGCAGTTTCAAAAGATGAAGCAGTGATGTTGGTGAAT
CATCAGGCAACAGGAGATGTGTGCACACTGATGATGTGCCTCCAGGACAAAGGACTGGTT
GTTGCTCAGATGATGTGGTTGATGGATCATATTTTTAAGTACACAAACTTTGGAATTGTT
TCTCTAGTTCATGGAGACTTCTTTATAAGACAGGGAAGATCTTATCGTGACCAACAGCTG
CTGCTTCTCAAGAAGCACTTAGAAAATAATTACAGGAGCAGAGATCGAAAATGGATTGTT
TTGTTTCCAGAAGGGGGCTTCCTCAGGAAGAGGCGAGAAACAAGTCAGGCATTTGCCAAG
AAAAATAACTTGCCATTTCTTACAAATGTTACTCTGCCAAGGTCTGGGGCAACAAAAATT
ATTTTGAATGCACTTGTAGCACAACAGAAAAATGGAAGTCCAGCAGGAGGAGATGCTAAA
GAATTAGACAGCAAATCAAAAGGCCTCCAGTGGATAATAGATACAACGATAGCTTATCCC
AAAGCTGAACCTATAGATATTCAAACCTGGATCCTTGGATACAGGAAACCAACAGTCACA
CATGTACATTACAGGATCTTTCCAATTAAAGATGTACCCCTGGAGACTGATGACCTTACC
ACTTGGCTCTATCAGCGGTTTGTTGAAAAAGAAGACCTCTTATCACATTTTTATGAAACA
GGAGCTTTTCCACCTTCCAAGGGCCATAAGGAAGCTGTTTCCAGGGAGATGACCCTCAGC
AACTTGTGGATATTTCTCATACAGTCTTTTGCATTTTTGTCAGGCTATATGTGGTACAAC
ATCATTCAGTATTTTTACCATTGCCTGTTTTAG
Enzyme 13 GenBank Gene ID BC034621 Link Image
Enzyme 13 GeneCard ID LPGAT1 Link Image
Enzyme 13 GenAtlas ID LPGAT1 Link Image
Enzyme 13 HGNC ID HGNC:28985 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 1q32
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Yang Y, Cao J, Shi Y: Identification and characterization of a gene encoding human LPGAT1, an endoplasmic reticulum-associated lysophosphatidylglycerol acyltransferase. J Biol Chem. 2004 Dec 31;279(53):55866-74. Epub 2004 Oct 12. [PubMed Link Image]
  2. 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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 6577
Enzyme 14 Name Focal adhesion kinase 1
Enzyme 14 Synonyms
  1. FADK 1
  2. Protein-tyrosine kinase 2
  3. pp125FAK
Enzyme 14 Gene Name PTK2
Enzyme 14 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 14 Number of Residues 1052
Enzyme 14 Molecular Weight 119232.0
Enzyme 14 Theoretical pI 6.61
Enzyme 14 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • molecular transducer activity
  • nucleoside binding
  • protein binding
  • protein kinase activity
  • protein tyrosine kinase activity
  • purine nucleoside binding
  • signal transducer activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular component assembly
  • cellular component organization
  • cellular component organization or biogenesis
  • cellular metabolic process
  • cellular protein complex assembly
  • macromolecular complex assembly
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • protein complex assembly
  • signal complex assembly
Component
  • adherens junction
  • anchoring junction
  • cell junction
  • cell part
  • cell-substrate adherens junction
  • cytoskeleton
  • focal adhesion
  • intracellular non-membrane-bounded organelle
  • membrane part
  • non-membrane-bounded organelle
  • organelle
  • plasma membrane part
Enzyme 14 General Function Involved in binding
Enzyme 14 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 14 Pathways Not Available
Enzyme 14 Reactions
  • ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate [RN:R02584]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein Not Available
Enzyme 14 UniProtKB/Swiss-Prot ID Q05397 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name FAK1_HUMAN Link Image
Enzyme 14 PDB ID 1MP8 Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 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 14 GenBank Gene ID L13616 Link Image
Enzyme 14 GeneCard ID PTK2 Link Image
Enzyme 14 GenAtlas ID PTK2 Link Image
Enzyme 14 HGNC ID HGNC:9611 Link Image
Enzyme 14 Chromosome Location 8
Enzyme 14 Locus 8q24.3
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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. Matsuya M, Sasaki H, Aoto H, Mitaka T, Nagura K, Ohba T, Ishino M, Takahashi S, Suzuki R, Sasaki T: Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions. J Biol Chem. 1998 Jan 9;273(2):1003-14. [PubMed Link Image]
  5. Fujita H, Kamiguchi K, Cho D, Shibanuma M, Morimoto C, Tachibana K: Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase. J Biol Chem. 1998 Oct 9;273(41):26516-21. [PubMed Link Image]
  6. 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]
  7. Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  10. Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed Link Image]
  11. Wolf-Yadlin A, Hautaniemi S, Lauffenburger DA, White FM: Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5860-5. Epub 2007 Mar 26. [PubMed Link Image]
  12. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  13. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  14. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  15. Tamura T, Chiba J: STEAP4 regulates focal adhesion kinase activation and CpG motifs within STEAP4 promoter region are frequently methylated in DU145, human androgen-independent prostate cancer cells. Int J Mol Med. 2009 Nov;24(5):599-604. [PubMed Link Image]
  16. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  17. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  18. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 6721
Enzyme 15 Name Protein-tyrosine kinase 2-beta
Enzyme 15 Synonyms
  1. Calcium-dependent tyrosine kinase
  2. CADTK
  3. Cell adhesion kinase beta
  4. CAK-beta
  5. Focal adhesion kinase 2
  6. FADK 2
  7. Proline-rich tyrosine kinase 2
  8. Related adhesion focal tyrosine kinase
  9. RAFTK
Enzyme 15 Gene Name PTK2B
Enzyme 15 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 15 Number of Residues 1009
Enzyme 15 Molecular Weight 115873.6
Enzyme 15 Theoretical pI 6.16
Enzyme 15 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • molecular transducer activity
  • nucleoside binding
  • protein binding
  • protein kinase activity
  • protein tyrosine kinase activity
  • purine nucleoside binding
  • signal transducer activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular component assembly
  • cellular component organization
  • cellular component organization or biogenesis
  • cellular metabolic process
  • cellular protein complex assembly
  • macromolecular complex assembly
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • protein complex assembly
  • signal complex assembly
Component
  • adherens junction
  • anchoring junction
  • cell junction
  • cell part
  • cell-substrate adherens junction
  • cytoskeleton
  • focal adhesion
  • intracellular non-membrane-bounded organelle
  • membrane part
  • non-membrane-bounded organelle
  • organelle
  • plasma membrane part
Enzyme 15 General Function Involved in binding
Enzyme 15 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 15 Pathways Not Available
Enzyme 15 Reactions
  • ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate [RN:R02584]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID Q14289 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name FAK2_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 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 15 GenBank Gene ID U33284 Link Image
Enzyme 15 GeneCard ID PTK2B Link Image
Enzyme 15 GenAtlas ID PTK2B Link Image
Enzyme 15 HGNC ID HGNC:9612 Link Image
Enzyme 15 Chromosome Location 8
Enzyme 15 Locus 8p21.1
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Matsuya M, Sasaki H, Aoto H, Mitaka T, Nagura K, Ohba T, Ishino M, Takahashi S, Suzuki R, Sasaki T: Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions. J Biol Chem. 1998 Jan 9;273(2):1003-14. [PubMed Link Image]
  9. 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]
  10. 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]
  11. Takahashi T, Yamashita H, Nagano Y, Nakamura T, Ohmori H, Avraham H, Avraham S, Yasuda M, Matsumoto M: Identification and characterization of a novel Pyk2/related adhesion focal tyrosine kinase-associated protein that inhibits alpha-synuclein phosphorylation. J Biol Chem. 2003 Oct 24;278(43):42225-33. Epub 2003 Jul 31. [PubMed Link Image]
  12. 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]
  13. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  14. Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed Link Image]
  15. Wolf-Yadlin A, Hautaniemi S, Lauffenburger DA, White FM: Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5860-5. Epub 2007 Mar 26. [PubMed Link Image]
  16. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  17. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  18. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  19. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  20. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 6873
Enzyme 16 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
Enzyme 16 Synonyms
  1. 1-acylglycerol-3-phosphate O-acyltransferase 3
  2. 1-AGP acyltransferase 3
  3. 1-AGPAT 3
  4. Lysophosphatidic acid acyltransferase gamma
  5. LPAAT-gamma
Enzyme 16 Gene Name AGPAT3
Enzyme 16 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQ
LVMLLEWWSCTECTLFTDQATVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKV
LAKKELLYVPLIGWTWYFLEIVFCKRKWEEDRDTVVEGLRRLSDYPEYMWFLLYCEGTRF
TETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSL
LGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFK
PARRPWTLLNFLSWATILLSPLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTE
IEKGSSYGNQEFKKKE
Enzyme 16 Number of Residues 376
Enzyme 16 Molecular Weight 43380.6
Enzyme 16 Theoretical pI 8.91
Enzyme 16 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 16 General Function Involved in acyltransferase activity
Enzyme 16 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 16 Pathways
Enzyme 16 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • 11-31 124-144 308-330 335-357
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 11611541 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q9NRZ7 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name PLCC_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1131 bp
ATGGGCCTGCTGGCCTTCCTGAAGACCCAGTTCGTGCTGCACCTGCTGGTCGGCTTTGTC
TTCGTGGTGAGTGGTCTGGTCATCAACTTCGTCCAGCTGTGCACGCTGGCGCTCTGGCCG
GTCAGCAAGCAGCTCTACCGCCGCCTCAACTGCCGCCTCGCCTACTCACTCTGGAGCCAA
CTGGTCATGCTGCTGGAGTGGTGGTCCTGCACGGAGTGTACACTGTTCACGGACCAGGCC
ACGGTAGAGCGCTTTGGGAAGGAGCACGCAGTCATCATCCTCAACCACAACTTCGAGATC
GACTTCCTCTGTGGGTGGACCATGTGTGAGCGCTTCGGAGTGCTGGGGAGCTCCAAGGTC
CTCGCTAAGAAGGAGCTGCTCTACGTGCCCCTCATCGGCTGGACGTGGTACTTTCTGGAG
ATTGTGTTCTGCAAGCGGAAGTGGGAGGAGGACCGGGACACCGTGGTCGAAGGGCTGAGG
CGCCTGTCGGACTACCCCGAGTACATGTGGTTTCTCCTGTACTGCGAGGGGACGCGCTTC
ACGGAGACCAAGCACCGCGTTAGCATGGAGGTGGCGGCTGCTAAGGGGCTTCCTGTCCTC
AAGTACCACCTGCTGCCGCGGACCAAGGGCTTCACCACCGCAGTCAAGTGCCTCCGGGGG
ACAGTCGCAGCTGTCTATGATGTAACCCTGAACTTCAGAGGAAACAAGAACCCGTCCCTG
CTGGGGATCCTCTACGGGAAGAAGTACGAGGCGGACATGTGCGTGAGGAGATTTCCTCTG
GAAGACATCCCGCTGGATGAAAAGGAAGCAGCTCAGTGGCTTCATAAACTGTACCAGGAG
AAGGACGCGCTCCAGGAGATATATAATCAGAAGGGCATGTTTCCAGGGGAGCAGTTTAAG
CCTGCCCGGAGGCCGTGGACCCTCCTGAACTTCCTGTCCTGGGCCACCATTCTCCTGTCT
CCCCTCTTCAGTTTTGTCTTGGGCGTCTTTGCCAGCGGATCACCTCTCCTGATCCTGACT
TTCTTGGGGTTTGTGGGAGCAGCTTCCTTTGGAGTTCGCAGACTGATAGGAGTAACTGAG
ATAGAAAAAGGCTCCAGCTACGGAAACCAAGAGTTTAAGAAAAAGGAATAA
Enzyme 16 GenBank Gene ID AB040138 Link Image
Enzyme 16 GeneCard ID AGPAT3 Link Image
Enzyme 16 GenAtlas ID AGPAT3 Link Image
Enzyme 16 HGNC ID HGNC:326 Link Image
Enzyme 16 Chromosome Location 2
Enzyme 16 Locus 21q22.3
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Leung DW: The structure and functions of human lysophosphatidic acid acyltransferases. Front Biosci. 2001 Aug 1;6:D944-53. [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]
  3. 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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 6875
Enzyme 17 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
Enzyme 17 Synonyms
  1. 1-acylglycerol-3-phosphate O-acyltransferase 2
  2. 1-AGP acyltransferase 2
  3. 1-AGPAT 2
  4. Lysophosphatidic acid acyltransferase beta
  5. LPAAT-beta
Enzyme 17 Gene Name AGPAT2
Enzyme 17 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase beta
MELWPCLAAALLLLLLLVQLSRAAEFYAKVALYCALCFTVSAVASLVCLLRHGGRTVENM
SIIGWFVRSFKYFYGLRFEVRDPRRLQEARPCVIVSNHQSILDMMGLMEVLPERCVQIAK
RELLFLGPVGLIMYLGGVFFINRQRSSTAMTVMADLGERMVRENLKVWIYPEGTRNDNGD
LLPFKKGAFYLAVQAQVPIVPVVYSSFSSFYNTKKKFFTSGTVTVQVLEAIPTSGLTAAD
VPALVDTCHRAMRTTFLHISKTPQENGATAGSGVQPAQ
Enzyme 17 Number of Residues 278
Enzyme 17 Molecular Weight 30914.1
Enzyme 17 Theoretical pI 9.22
Enzyme 17 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 acyl groups other than amino-acyl groups
Process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid biosynthetic process
  • phospholipid metabolic process
Component
  • cell part
  • membrane
Enzyme 17 General Function Lipid transport and metabolism
Enzyme 17 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 17 Pathways
Enzyme 17 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • 1-21 30-50 122-142
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 2282590 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID O15120 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name PLCB_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >837 bp
ATGGAGCTGTGGCCGTGTCTGGCCGCGGCGCTGCTGTTGCTGCTGCTGCTGGTGCAGCTG
AGCCGCGCGGCCGAGTTCTACGCCAAGGTCGCCCTGTACTGCGCGCTGTGCTTCACGGTG
TCCGCCGTGGCCTCGCTCGTCTGCCTGCTGCGCCACGGCGGCCGGACGGTGGAGAACATG
AGCATCATCGGCTGGTTCGTGCGAAGCTTCAAGTACTTTTACGGGCTCCGCTTCGAGGTG
CGGGACCCGCGCAGGCTGCAGGAGGCCCGTCCCTGTGTCATCGTCTCCAACCACCAGAGC
ATCCTGGACATGATGGGCCTCATGGAGGTCCTTCCGGAGCGCTGCGTGCAGATCGCCAAG
CGGGAGCTGCTCTTCCTGGGGCCCGTGGGCCTCATCATGTACCTCGGGGGCGTCTTCTTC
ATCAACCGGCAGCGCTCTAGCACTGCCATGACAGTGATGGCCGACCTGGGCGAGCGCATG
GTCAGGGAGAACCTCAAAGTGTGGATCTATCCCGAGGGTACTCGCAACGACAATGGGGAC
CTGCTGCCTTTTAAGAAGGGCGCCTTCTACCTGGCAGTCCAGGCACAGGTGCCCATCGTC
CCCGTGGTGTACTCTTCCTTCTCCTCCTTCTACAACACCAAGAAGAAGTTCTTCACTTCA
GGAACAGTCACAGTGCAGGTGCTGGAAGCCATCCCCACCAGCGGCCTCACTGCGGCGGAC
GTCCCTGCGCTCGTGGACACCTGCCACCGGGCCATGAGGACCACCTTCCTCCACATCTCC
AAGACCCCCCAGGAGAACGGGGCCACTGCGGGGTCTGGCGTGCAGCCGGCCCAGTAG
Enzyme 17 GenBank Gene ID AF000237 Link Image
Enzyme 17 GeneCard ID AGPAT2 Link Image
Enzyme 17 GenAtlas ID Not Available
Enzyme 17 HGNC ID Not Available
Enzyme 17 Chromosome Location 9
Enzyme 17 Locus 9q34.3
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 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. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Garg A: Acquired and inherited lipodystrophies. N Engl J Med. 2004 Mar 18;350(12):1220-34. [PubMed Link Image]
  7. 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 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6877
Enzyme 18 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
Enzyme 18 Synonyms
  1. 1-acylglycerol-3-phosphate O-acyltransferase 1
  2. 1-AGP acyltransferase 1
  3. 1-AGPAT 1
  4. Lysophosphatidic acid acyltransferase alpha
  5. LPAAT-alpha
  6. Protein G15
Enzyme 18 Gene Name AGPAT1
Enzyme 18 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
MDLWPGAWMLLLLLFLLLLFLLPTLWFCSPSAKYFFKMAFYNGWILFLAVLAIPVCAVRG
RNVENMKILRLMLLHIKYLYGIRVEVRGAHHFPPSQPYVVVSNHQSSLDLLGMMEVLPGR
CVPIAKRELLWAGSAGLACWLAGVIFIDRKRTGDAISVMSEVAQTLLTQDVRVWVFPEGT
RNHNGSMLPFKRGAFHLAVQAQVPIVPIVMSSYQDFYCKKERRFTSGQCQVRVLPPVPTE
GLTPDDVPALADRVRHSMLTVFREISTDGRGGGDYLKKPGGGG
Enzyme 18 Number of Residues 283
Enzyme 18 Molecular Weight 31716.3
Enzyme 18 Theoretical pI 9.75
Enzyme 18 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 acyl groups other than amino-acyl groups
Process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid biosynthetic process
  • phospholipid metabolic process
Component
  • cell part
  • membrane
Enzyme 18 General Function Involved in acyltransferase activity
Enzyme 18 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 18 Pathways
Enzyme 18 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • 7-27 38-58 128-148
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 55961399 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q99943 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PLCA_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >852 bp
ATGGATTTGTGGCCAGGGGCATGGATGCTGCTGCTGCTGCTCTTCCTGCTGCTGCTCTTC
CTGCTGCCCACCCTGTGGTTCTGCAGCCCCAGTGCCAAGTACTTCTTCAAGATGGCCTTC
TACAATGGCTGGATCCTCTTCCTGGCTGTGCTCGCCATCCCTGTGTGTGCCGTGCGAGGA
CGCAACGTCGAGAACATGAAGATCTTGCGTCTAATGCTGCTCCACATCAAATACCTGTAC
GGGATCCGAGTGGAGGTGCGAGGGGCTCACCACTTCCCTCCCTCGCAGCCCTATGTTGTT
GTCTCCAACCACCAGAGCTCTCTCGATCTGCTTGGGATGATGGAGGTACTGCCAGGCCGC
TGTGTGCCCATTGCCAAGCGCGAGCTACTGTGGGCTGGCTCTGCCGGGCTGGCCTGCTGG
CTGGCAGGAGTCATCTTCATCGACCGGAAGCGCACGGGGGATGCCATCAGTGTCATGTCT
GAGGTCGCCCAGACCCTGCTCACCCAGGACGTGAGGGTCTGGGTGTTTCCTGAGGGAACG
AGAAACCACAATGGCTCCATGCTGCCCTTCAAACGTGGCGCCTTCCATCTTGCAGTGCAG
GCCCAGGTTCCCATTGTCCCCATAGTCATGTCCTCCTACCAAGACTTCTACTGCAAGAAG
GAGCGTCGCTTCACCTCGGGACAATGTCAGGTGCGGGTGCTGCCCCCAGTGCCCACGGAA
GGGCTGACACCAGATGACGTCCCAGCTCTGGCTGACAGAGTCCGGCACTCCATGCTCACT
GTTTTCCGGGAAATCTCCACTGATGGCCGGGGTGGTGGTGACTATCTGAAGAAGCCTGGG
GGCGGTGGGTGA
Enzyme 18 GenBank Gene ID AL662828 Link Image
Enzyme 18 GeneCard ID AGPAT1 Link Image
Enzyme 18 GenAtlas ID AGPAT1 Link Image
Enzyme 18 HGNC ID HGNC:324 Link Image
Enzyme 18 Chromosome Location 6
Enzyme 18 Locus 6p21.3
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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. Xie T, Rowen L, Aguado B, Ahearn ME, Madan A, Qin S, Campbell RD, Hood L: Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse. Genome Res. 2003 Dec;13(12):2621-36. [PubMed Link Image]
  5. 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]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 6881
Enzyme 19 Name Phosphatidylinositol-glycan-specific phospholipase D
Enzyme 19 Synonyms
  1. PI-G PLD
  2. Glycoprotein phospholipase D
  3. Glycosyl-phosphatidylinositol-specific phospholipase D
  4. GPI-PLD
  5. GPI-specific phospholipase D
Enzyme 19 Gene Name GPLD1
Enzyme 19 Protein Sequence >Phosphatidylinositol-glycan-specific phospholipase D
MSAFRLWPGLLIMLGSLCHRGSPCGLSTHVEIGHRALEFLQLHNGRVNYRELLLEHQDAY
QAGIVFPDCFYPSICKGGKFHDVSESTHWTPFLNASVHYIRENYPLPWEKDTEKLVAFLF
GITSHMAADVSWHSLGLEQGFLRTMGAIDFHGSYSEAHSAGDFGGDVLSQFEFNFNYLAR
RWYVPVKDLLGIYEKLYGRKVITENVIVDCSHIQFLEMYGEMLAVSKLYPTYSTKSPFLV
EQFQEYFLGGLDDMAFWSTNIYHLTSFMLENGTSDCNLPENPLFIACGGQQNHTQGSKMQ
KNDFHRNLTTSLTESVDRNINYTERGVFFSVNSWTPDSMSFIYKALERNIRTMFIGGSQL
SQKHVSSPLASYFLSFPYARLGWAMTSADLNQDGHGDLVVGAPGYSRPGHIHIGRVYLIY
GNDLGLPPVDLDLDKEAHRILEGFQPSGRFGSALAVLDFNVDGVPDLAVGAPSVGSEQLT
YKGAVYVYFGSKQGGMSSSPNITISCQDIYCNLGWTLLAADVNGDSEPDLVIGSPFAPGG
GKQKGIVAAFYSGPSLSDKEKLNVEAANWTVRGEEDFSWFGYSLHGVTVDNRTLLLVGSP
TWKNASRLGHLLHIRDEKKSLGRVYGYFPPNGQSWFTISGDKAMGKLGTSLSSGHVLMNG
TLKQVLLVGAPTYDDVSKVAFLTVTLHQGGATRMYALTSDAQPLLLSTFSGDRRFSRFGG
VLHLSDLDDDGLDEIIMAAPLRIADVTSGLIGGEDGRVYVYNGKETTLGDMTGKCKSWIT
PCPEEKAQYVLISPEASSRFGSSLITVRSKAKNQVVIAAGRSSLGARLSGALHVYSLGSD
Enzyme 19 Number of Residues 840
Enzyme 19 Molecular Weight 92335.7
Enzyme 19 Theoretical pI 6.33
Enzyme 19 GO Classification
Function
  • 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 19 General Function Involved in glycosylphosphatidylinositol phospholipase D activity
Enzyme 19 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 19 Pathways Not Available
Enzyme 19 Reactions
  • 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + 3-sn-phosphatidate [RN:R06623]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-23
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 20269065 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID P80108 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name PHLD_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >2523 bp
ATGTCTGCTTTCAGGTTGTGGCCTGGCCTGCTGATCATGTTGGGTTCTCTCTGCCATAGA
GGTTCACCGTGTGGCCTTTCAACACACATAGAAATAGGACACAGAGCTCTGGAGTTTCTT
CAGCTTCACAATGGGCGTGTTAACTACAGAGAGCTGTTACTAGAACACCAGGATGCGTAT
CAGGCTGGAATCGTGTTTCCTGATTGTTTTTACCCTAGCATCTGCAAAGGAGGAAAATTC
CATGATGTGTCTGAGAGCACTCACTGGACTCCGTTTCTTAATGCAAGCGTTCATTATATC
CGAGAGAACTATCCCCTTCCCTGGGAGAAGGACACAGAGAAACTGGTAGCTTTCTTGTTT
GGAATTACTTCTCACATGGCGGCAGATGTCAGCTGGCATAGTCTGGGCCTTGAACAAGGA
TTCCTTAGGACCATGGGAGCTATTGATTTTCACGGCTCCTATTCAGAGGCTCATTCGGCT
GGTGATTTTGGAGGAGATGTGTTGAGCCAGTTTGAATTTAATTTTAATTACCTTGCACGA
CGCTGGTATGTGCCAGTCAAAGATCTACTGGGAATTTATGAGAAACTGTATGGTCGAAAA
GTCATCACCGAAAATGTAATCGTTGATTGTTCACATATCCAGTTCTTAGAAATGTATGGT
GAGATGCTAGCTGTTTCCAAGTTATATCCCACTTACTCTACAAAGTCCCCGTTTTTGGTG
GAACAATTCCAAGAGTATTTTCTTGGAGGACTGGATGATATGGCATTTTGGTCCACTAAT
ATTTACCATCTAACAAGCTTCATGTTGGAGAATGGGACCAGTGACTGCAACCTGCCTGAG
AACCCTCTGTTCATTGCATGTGGCGGCCAGCAAAACCACACCCAGGGCTCAAAAATGCAG
AAAAATGATTTTCACAGAAATTTGACTACATCCCTAACTGAAAGTGTTGACAGGAATATA
AACTATACTGAAAGAGGAGTGTTCTTTAGTGTAAATTCCTGGACCCCGGATTCCATGTCC
TTTATCTACAAGGCTTTGGAAAGGAACATAAGGACAATGTTCATAGGTGGCTCTCAGTTG
TCACAAAAGCACGTCTCCAGCCCCTTAGCATCTTACTTCTTGTCATTTCCTTATGCGAGG
CTTGGCTGGGCAATGACCTCAGCTGACCTCAACCAGGATGGGCACGGTGACCTCGTGGTG
GGCGCACCAGGCTACAGCCGCCCCGGCCACATCCACATCGGGCGCGTGTACCTCATCTAC
GGCAATGACCTGGGCCTGCCACCTGTTGACCTGGACCTGGACAAGGAGGCCCACAGGATC
CTTGAAGGCTTCCAGCCCTCAGGTCGGTTTGGCTCGGCCTTGGCTGTGTTGGACTTTAAC
GTGGACGGCGTGCCTGACCTGGCCGTGGGAGCTCCCTCGGTGGGCTCCGAGCAGCTCACC
TACAAAGGTGCCGTGTATGTCTACTTTGGTTCCAAACAAGGAGGAATGTCTTCTTCCCCT
AACATCACCATTTCTTGCCAGGACATCTACTGTAACTTGGGCTGGACTCTCTTGGCTGCA
GATGTGAATGGAGACAGTGAACCCGATCTGGTCATCGGCTCCCCTTTTGCACCAGGTGGA
GGGAAGCAGAAGGGAATTGTGGCTGCGTTTTATTCTGGCCCCAGCCTGAGCGACAAAGAA
AAACTGAACGTGGAGGCAGCCAACTGGACGGTGAGAGGCGAGGAAGACTTCTCCTGGTTT
GGATATTCCCTTCACGGTGTCACTGTGGACAACAGAACCTTGCTGTTGGTTGGGAGCCCG
ACCTGGAAGAATGCCAGCAGGCTGGGCCATTTGTTACACATCCGAGATGAGAAAAAGAGC
CTTGGGAGGGTGTATGGCTACTTCCCACCAAACGGCCAAAGCTGGTTTACCATTTCTGGA
GACAAGGCAATGGGGAAACTGGGTACTTCCCTTTCCAGTGGCCACGTACTGATGAATGGG
ACTCTGAAACAAGTGCTGCTGGTTGGAGCCCCTACGTACGATGACGTGTCTAAGGTGGCA
TTCCTGACCGTGACCCTACACCAAGGCGGAGCCACTCGCATGTACGCACTCATATCTGAC
GCGCAGCCTCTGCTGCTCAGCACCTTCAGCGGAGACCGCCGCTTCTCCCGATTTGGTGGC
GTTCTGCACTTGAGTGACCTGGATGATGATGGCTTAGATGAAATCATCATGGCAGCCCCC
CTGAGGATAGCAGATGTAACCTCTGGACTGATTGGGGGAGAAGACGGCCGAGTATATGTA
TATAATGGCAAAGAGACCACCCTTGGTGACATGACTGGCAAATGCAAATCATGGATAACT
CCATGTCCAGAAGAAAAGGCCCAATATGTATTGATTTCTCCTGAAGCCAGCTCAAGGTTT
GGGAGCTCCCTCATCACCGTGAGGTCCAAGGCAAAGAACCAAGTCGTCATTGCTGCTGGA
AGGAGTTCTTTGGGAGCCCGACTCTCCGGGGCACTTCACGTCTATAGCCTTGGCTCAGAT
TGA
Enzyme 19 GenBank Gene ID AJ308108 Link Image
Enzyme 19 GeneCard ID GPLD1 Link Image
Enzyme 19 GenAtlas ID GPLD1 Link Image
Enzyme 19 HGNC ID HGNC:4459 Link Image
Enzyme 19 Chromosome Location 6
Enzyme 19 Locus 6p22.1
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  6. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 8354
Enzyme 20 Name Lysophosphatidic acid receptor 2
Enzyme 20 Synonyms
  1. LPA receptor 2
  2. LPA-2
  3. Lysophosphatidic acid receptor Edg-4
Enzyme 20 Gene Name LPAR2
Enzyme 20 Protein Sequence >Lysophosphatidic acid receptor 2
MVIMGQCYYNETIGFFYNNSGKELSSHWRPKDVVVVALGLTVSVLVLLTNLLVIAAIASN
RRFHQPIYYLLGNLAAADLFAGVAYLFLMFHTGPRTARLSLEGWFLRQGLLDTSLTASVA
TLLAIAVERHRSVMAVQLHSRLPRGRVVMLIVGVWVAALGLGLLPAHSWHCLCALDRCSR
MAPLLSRSYLAVWALSSLLVFLLMVAVYTRIFFYVRRRVQRMAEHVSCHPRYRETTLSLV
KTVVIILGAFVVCWTPGQVVLLLDGLGCESCNVLAVEKYFLLLAEANSLVNAAVYSCRDA
EMRRTFRRLLCCACLRQSTRESVHYTSSAQGGASTRIMLPENGHPLMDSTL
Enzyme 20 Number of Residues 351
Enzyme 20 Molecular Weight 39083.8
Enzyme 20 Theoretical pI 9.42
Enzyme 20 GO Classification
Function
  • G-protein coupled receptor activity
  • bioactive lipid receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 20 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 20 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. Stimulates phospholipase C (PLC) activity in a manner that is independent of RALA activation
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 34-54 70-90 104-126 147-167 189-209 243-263 280-297
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 2213635 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q9HBW0 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name LPAR2_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1056 bp
ATGGTCATCATGGGCCAGTGCTACTACAACGAGACCATCGGCTTCTTCTATAACAACAGT
GGCAAAGAGCTCAGCTCCCACTGGCGGCCCAAGGATGTGGTCGTGGTGGCACTGGGGCTG
ACCGTCAGCGTGCTGGTGCTGCTGACCAATCTGCTGGTCATAGCAGCCATCGCCTCCAAC
CGCCGCTTCCACCAGCCCATCTACTACCTGCTCGGCAATCTGGCCGCGGCTGACCTCTTC
GCGGGCGTGGCCTACCTCTTCCTCATGTTCCACACTGGTCCCCGCACAGCCCGACTTTCA
CTTGAGGGCTGGTTCCTGCGGCAGGGCTTGCTGGACACAAGCCTCACTGCGTCGGTGGCC
ACACTGCTGGCCATCGCCGTGGAGCGGCACCGCAGTGTGATGGCCGTGCAGCTGCACAGC
CGCCTGCCCCGTGGCCGCGTGGTCATGCTCATTGTGGGCGTGTGGGTGGCTGCCCTGGGC
CTGGGGCTGCTGCCTGCCCACTCCTGGCACTGCCTCTGTGCCCTGGACCGCTGCTCACGC
ATGGCACCCCTGCTCAGCCGCTCCTATTTGGCCGTCTGGGCTCTGTCGAGCCTGCTTGTC
TTCCTGCTCATGGTGGCTGTGTACACCCGCATTTTCTTCTACGTGCGGCGGCGAGTGCAG
CGCATGGCAGAGCATGTCAGCTGCCACCCCCGCTACCGAGAGACCACGCTCAGCCTGGTC
AAGACTGTTGTCATCATCCTGGGGGCGTTCGTGGTCTGCTGGACACCAGGCCAGGTGGTA
CTGCTCCTGGATGGTTTAGGCTGTGAGTCCTGCAATGTCCTGGCTGTAGAAAAGTACTTC
CTACTGTTGGCCGAGGCCAACTCACTGGTCAATGCTGCTGTGTACTCTTGCCGAGATGCT
GAGATGCGCCGCACCTTCCGCCGCCTTCTCTGCTGCGCGTGCCTCCGCCAGTCCACCCGC
GAGTCTGTCCACTATACATCCTCTGCCCAGGGAGGTGCCAGCACTCGCATCATGCTTCCC
GAGAACGGCCACCCACTGATGGACTCCACCCTTTAG
Enzyme 20 GenBank Gene ID AC002306 Link Image
Enzyme 20 GeneCard ID LPAR2 Link Image
Enzyme 20 GenAtlas ID LPAR2 Link Image
Enzyme 20 HGNC ID HGNC:3168 Link Image
Enzyme 20 Chromosome Location 1
Enzyme 20 Locus 19p12
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 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. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Contos JJ, Ishii I, Chun J: Lysophosphatidic acid receptors. Mol Pharmacol. 2000 Dec;58(6):1188-96. [PubMed Link Image]
  6. 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]
  7. Oh YS, Jo NW, Choi JW, Kim HS, Seo SW, Kang KO, Hwang JI, Heo K, Kim SH, Kim YH, Kim IH, Kim JH, Banno Y, Ryu SH, Suh PG: NHERF2 specifically interacts with LPA2 receptor and defines the specificity and efficiency of receptor-mediated phospholipase C-beta3 activation. Mol Cell Biol. 2004 Jun;24(11):5069-79. [PubMed Link Image]
  8. Zhang H, Wang D, Sun H, Hall RA, Yun CC: MAGI-3 regulates LPA-induced activation of Erk and RhoA. Cell Signal. 2007 Feb;19(2):261-8. Epub 2006 Aug 9. [PubMed Link Image]
  9. Aziziyeh AI, Li TT, Pape C, Pampillo M, Chidiac P, Possmayer F, Babwah AV, Bhattacharya M: Dual regulation of lysophosphatidic acid (LPA1) receptor signalling by Ral and GRK. Cell Signal. 2009 Jul;21(7):1207-17. Epub 2009 Mar 21. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 8359
Enzyme 21 Name Lysophosphatidic acid receptor 1
Enzyme 21 Synonyms
  1. LPA receptor 1
  2. LPA-1
  3. Lysophosphatidic acid receptor Edg-2
Enzyme 21 Gene Name LPAR1
Enzyme 21 Protein Sequence >Lysophosphatidic acid receptor 1
MAAISTSIPVISQPQFTAMNEPQCFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITVC
IFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVST
WLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMGA
IPSVGWNCICDIENCSNMAPLYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRMS
RHSSGPRRNRDTMMSLLKTVVIVLGAFIICWTPGLVLLLLDVCCPQCDVLAYEKFFLLLA
EFNSAMNPIIYSYRDKEMSATFRQILCCQRSENPTGPTEGSDRSASSLNHTILAGVHSND
HSVV
Enzyme 21 Number of Residues 364
Enzyme 21 Molecular Weight 41109.0
Enzyme 21 Theoretical pI 8.60
Enzyme 21 GO Classification
Function
  • G-protein coupled receptor activity
  • bioactive lipid receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 21 General Function Involved in lysosphingolipid and lysophosphatidic acid
Enzyme 21 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. Stimulates phospholipase C (PLC) activity in a manner that is dependent on RALA activation
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 51-75 83-111 126-144 164-189 206-226 259-280 295-315
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 32482013 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q92633 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name LPAR1_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1095 bp
ATGGCTGCCATCTCTACTTCCATCCCTGTAATTTCACAGCCCCAGTTCACAGCCATGAAT
GAACCACAGTGCTTCTACAACGAGTCCATTGCCTTCTTTTATAACCGAAGTGGAAAGCAT
CTTGCCACAGAATGGAACACAGTCAGCAAGCTGGTGATGGGACTTGGAATCACTGTTTGT
ATCTTCATCATGTTGGCCAACCTATTGGTCATGGTGGCAATCTATGTCAACCGCCGCTTC
CATTTTCCTATTTATTACCTAATGGCTAATCTGGCTGCTGCAGACTTCTTTGCTGGGTTG
GCCTACTTCTATCTCATGTTCAACACAGGACCCAATACTCGGAGACTGACTGTTAGCACA
TGGCTCCTTCGTCAGGGCCTCATTGACACCAGCCTGACGGCATCTGTGGCCAACTTACTG
GCTATTGCAATCGAGAGGCACATTACGGTTTTCCGCATGCAGCTCCACACACGGATGAGC
AACCGGCGGGTAGTGGTGGTCATTGTGGTCATCTGGACTATGGCCATCGTTATGGGTGCT
ATACCCAGTGTGGGCTGGAACTGTATCTGTGATATTGAAAATTGTTCCAACATGGCACCC
CTCTACAGTGACTCTTACTTAGTCTTCTGGGCCATTTTCAACTTGGTGACCTTTGTGGTA
ATGGTGGTTCTCTATGCTCACATCTTTGGCTATGTTCGCCAGAGGACTATGAGAATGTCT
CGGCATAGTTCTGGACCCCGGCGGAATCGGGATACCATGATGAGTCTTCTGAAGACTGTG
GTCATTGTGCTTGGGGCCTTTATCATCTGCTGGACTCCTGGATTGGTTTTGTTACTTCTA
GACGTGTGCTGTCCACAGTGCGACGTGCTGGCCTATGAGAAATTCTTCCTTCTCCTTGCT
GAATTCAACTCTGCCATGAACCCCATCATTTACTCCTACCGCGACAAAGAAATGAGCGCC
ACCTTTAGGCAGATCCTCTGCTGCCAGCGCAGTGAGAACCCCACCGGCCCCACAGAAGGC
TCAGACCGCTCGGCTTCCTCCCTCAACCACACCATCTTGGCTGGAGTTCACAGCAATGAC
CACTCTGTGGTTTAG
Enzyme 21 GenBank Gene ID AY322546 Link Image
Enzyme 21 GeneCard ID LPAR1 Link Image
Enzyme 21 GenAtlas ID Not Available
Enzyme 21 HGNC ID Not Available
Enzyme 21 Chromosome Location 9
Enzyme 21 Locus 9q31.3
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Contos JJ, Ishii I, Chun J: Lysophosphatidic acid receptors. Mol Pharmacol. 2000 Dec;58(6):1188-96. [PubMed Link Image]
  5. Aziziyeh AI, Li TT, Pape C, Pampillo M, Chidiac P, Possmayer F, Babwah AV, Bhattacharya M: Dual regulation of lysophosphatidic acid (LPA1) receptor signalling by Ral and GRK. Cell Signal. 2009 Jul;21(7):1207-17. Epub 2009 Mar 21. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 8524
Enzyme 22 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
Enzyme 22 Synonyms
  1. 1-acylglycerol-3-phosphate O-acyltransferase 5
  2. 1-AGP acyltransferase 5
  3. 1-AGPAT 5
  4. Lysophosphatidic acid acyltransferase epsilon
  5. LPAAT-epsilon
Enzyme 22 Gene Name AGPAT5
Enzyme 22 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
MLLSLVLHTYSMRYLLPSVVLLGTAPTYVLAWGVWRLLSAFLPARFYQALDDRLYCVYQS
MVLFFFENYTGVQILLYGDLPKNKENIIYLANHQSTVDWIVADILAIRQNALGHVRYVLK
EGLKWLPLYGCYFAQHGGIYVKRSAKFNEKEMRNKLQSYVDAGTPMYLVIFPEGTRYNPE
QTKVLSASQAFAAQRGLAVLKHVLTPRIKATHVAFDCMKNYLDAIYDVTVVYEGKDDGGQ
RRESPTMTEFLCKECPKIHIHIDRIDKKDVPEEQEHMRRWLHERFEIKDKMLIEFYESPD
PERRKRFPGKSVNSKLSIKKTLPSMLILSGLTAGMLMTDAGRKLYVNTWIYGTLLGCLWV
TIKA
Enzyme 22 Number of Residues 364
Enzyme 22 Molecular Weight 42071.8
Enzyme 22 Theoretical pI 9.41
Enzyme 22 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 22 General Function Involved in acyltransferase activity
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
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 15-35 61-81 344-364
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 14161585 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q9NUQ2 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name PLCE_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1095 bp
ATGCTGCTGTCCCTGGTGCTCCACACGTACTCCATGCGCTACCTGCTGCCCAGCGTCGTG
CTCCTGGGCACGGCGCCCACCTACGTGTTGGCCTGGGGGGTCTGGCGGCTGCTCTCCGCC
TTCCTGCCCGCCCGCTTCTACCAAGCGCTGGACGACCGGCTCTACTGCGTCTACCAGAGC
ATGGTGCTCTTCTTCTTCGAGAATTACACCGGGGTCCAGATATTGCTATATGGAGATTTG
CCAAAAAATAAAGAAAATATAATATATTTAGCAAATCATCAAAGCACAGTTGACTGGATT
GTTGCTGACATCTTGGCCATCAGGCAGAATGCGCTAGGACATGTGCGCTACGTGCTGAAA
GAAGGGTTAAAATGGCTGCCATTGTATGGGTGTTACTTTGCTCAGCATGGAGGAATCTAT
GTAAAGCGCAGTGCCAAATTTAACGAGAAAGAGATGCGAAACAAGTTGCAGAGCTACGTG
GACGCAGGAACTCCAATGTATCTTGTGATTTTTCCAGAAGGTACAAGGTATAATCCAGAG
CAAACAAAAGTCCTTTCAGCTAGTCAGGCATTTGCTGCCCAACGTGGCCTTGCAGTATTA
AAACATGTGCTAACACCACGAATAAAGGCAACTCACGTTGCTTTTGATTGCATGAAGAAT
TATTTAGATGCAATTTATGATGTTACGGTGGTTTATGAAGGGAAAGACGATGGAGGGCAG
CGAAGAGAGTCACCGACCATGACGGAATTTCTCTGCAAAGAATGTCCAAAAATTCATATT
CACATTGATCGTATCGACAAAAAAGATGTCCCAGAAGAACAAGAACATATGAGAAGATGG
CTGCATGAACGTTTCGAAATCAAAGATAAGATGCTTATAGAATTTTATGAGTCACCAGAT
CCAGAAAGAAGAAAAAGATTTCCTGGGAAAAGTGTTAATTCCAAATTAAGTATCAAGAAG
ACTTTACCATCAATGTTGATCTTAAGTGGTTTGACTGCAGGCATGCTTATGACCGATGCT
GGAAGGAAGCTGTATGTGAACACCTGGATATATGGAACCCTACTTGGCTGCCTGTGGGTT
ACTATTAAAGCATAG
Enzyme 22 GenBank Gene ID AF375789 Link Image
Enzyme 22 GeneCard ID AGPAT5 Link Image
Enzyme 22 GenAtlas ID AGPAT5 Link Image
Enzyme 22 HGNC ID HGNC:20886 Link Image
Enzyme 22 Chromosome Location 8
Enzyme 22 Locus 8p23.1
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 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]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 8871
Enzyme 23 Name Glycerol-3-phosphate acyltransferase 4
Enzyme 23 Synonyms
  1. GPAT4
  2. 1-acylglycerol-3-phosphate O-acyltransferase 6
  3. 1-AGP acyltransferase 6
  4. 1-AGPAT 6
  5. Acyl-CoA:glycerol-3-phosphate acyltransferase 4
  6. Lysophosphatidic acid acyltransferase zeta
  7. LPAAT-zeta
Enzyme 23 Gene Name AGPAT6
Enzyme 23 Protein Sequence >Glycerol-3-phosphate acyltransferase 4
MFLLLPFDSLIVNLLGISLTVLFTLLLVFIIVPAIFGVSFGIRKLYMKSLLKIFAWATLR
MERGAKEKNHQLYKPYTNGIIAKDPTSLEEEIKEIRRSGSSKALDNTPEFELSDIFYFCR
KGMETIMDDEVTKRFSAEELESWNLLSRTNYNFQYISLRLTVLWGLGVLIRYCFLLPLRI
ALAFTGISLLVVGTTVVGYLPNGRFKEFMSKHVHLMCYRICVRALTAIITYHDRENRPRN
GGICVANHTSPIDVIILASDGYYAMVGQVHGGLMGVIQRAMVKACPHVWFERSEVKDRHL
VAKRLTEHVQDKSKLPILIFPEGTCINNTSVMMFKKGSFEIGATVYPVAIKYDPQFGDAF
WNSSKYGMVTYLLRMMTSWAIVCSVWYLPPMTREADEDAVQFANRVKSAIARQGGLVDLL
WDGGLKREKVKDTFKEEQQKLYSKMIVGNHKDRSRS
Enzyme 23 Number of Residues 456
Enzyme 23 Molecular Weight 52070.6
Enzyme 23 Theoretical pI 9.56
Enzyme 23 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 23 General Function Involved in acyltransferase activity
Enzyme 23 Specific Function Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Active against both saturated and unsaturated long- chain fatty acyl-CoAs
Enzyme 23 Pathways
Enzyme 23 Reactions
  • acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate [RN:R00851]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-37
Enzyme 23 Transmembrane Regions
  • 156-176 180-200
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 30142570 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q86UL3 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name GPAT4_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 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 23 GenBank Gene ID AF406612 Link Image
Enzyme 23 GeneCard ID AGPAT6 Link Image
Enzyme 23 GenAtlas ID AGPAT6 Link Image
Enzyme 23 HGNC ID HGNC:20880 Link Image
Enzyme 23 Chromosome Location 8
Enzyme 23 Locus 8p11.21
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 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. Chen YQ, Kuo MS, Li S, Bui HH, Peake DA, Sanders PE, Thibodeaux SJ, Chu S, Qian YW, Zhao Y, Bredt DS, Moller DE, Konrad RJ, Beigneux AP, Young SG, Cao G: AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase. J Biol Chem. 2008 Apr 11;283(15):10048-57. Epub 2008 Jan 31. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 9821
Enzyme 24 Name Diacylglycerol kinase eta
Enzyme 24 Synonyms
  1. DAG kinase eta
  2. Diglyceride kinase eta
  3. DGK-eta
Enzyme 24 Gene Name DGKH
Enzyme 24 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 24 Number of Residues 1220
Enzyme 24 Molecular Weight 134864.3
Enzyme 24 Theoretical pI 6.51
Enzyme 24 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
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 24 General Function Involved in diacylglycerol kinase activity
Enzyme 24 Specific Function Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA)
Enzyme 24 Pathways
Enzyme 24 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 29788751 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q86XP1 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name DGKH_HUMAN Link Image
Enzyme 24 PDB ID 1R79 Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >3663 bp
ATGGCAGGGGCCGGAGGCCAGCACCACCCTCCGGGCGCCGCTGGAGGAGCGGCCGCCGGA
GCCGGCGCCGCGGTCACCTCCGCCGCTGCCTCGGCGGGGCCGGGAGAGGATTCGTCTGAC
AGCGAAGCGGAGCAAGAGGGACCCCAGAAACTGATCCGCAAAGTGTCTACCTCGGGGCAG
ATCCGGACCAAGACCAGTATTAAAGAGGGACAGCTATTGAAGCAAACCAGTTCTTTCCAA
AGGTGGAAAAAGCGATACTTCAAACTTCGAGGCCGCACCCTTTACTATGCAAAGGACTCA
AAGTCTCTGATATTTGATGAAGTTGACCTCTCAGATGCTAGTGTAGCTGAAGCAAGCACG
AAAAATGCTAACAACAGCTTCACGATCATCACTCCATTCAGAAGGCTAATGCTGTGTGCT
GAGAACAGAAAGGAGATGGAGGATTGGATCAGCTCACTGAAGTCTGTACAGACCAGAGAA
CCCTACGAGGTGGCCCAGTTTAATGTGGAACATTTCTCAGGGATGCACAACTGGTACGCC
TGCTCCCACGCCCGACCCACCTTCTGTAACGTGTGCAGAGAGAGTCTTTCTGGAGTCACC
TCCCATGGCCTGTCCTGCGAAGTGTGTAAATTCAAGGCTCACAAAAGATGTGCAGTGAGA
GCAACAAATAACTGTAAATGGACTACCCTGGCCTCCATCGGGAAGGACATTATAGAAGAT
GAAGATGGCGTCGCGATGCCTCACCAGTGGCTTGAGGGCAACCTGCCTGTAAGTGCCAAG
TGTGCTGTCTGCGACAAAACATGTGGCAGTGTTCTCCGTCTACAGGATTGGAAATGCCTT
TGGTGTAAGACAATGGTACACACTGCCTGCAAAGATTTATACCATCCAATATGTCCACTT
GGTCAATGTAAAGTATCTATCATACCTCCAATTGCACTAAACAGCACCGATTCCGATGGT
TTCTGTAGAGCAACATTTTCGTTCTGTGTTAGTCCTCTATTGGTTTTTGTCAATTCTAAG
AGTGGAGATAATCAGGGAGTAAAGTTCCTCCGTCGCTTTAAACAGTTGCTAAATCCGGCT
CAGGTGTTTGATTTAATGAATGGAGGTCCTCATTTAGGTTTAAGATTATTTCAGAAGTTT
GACAATTTCCGGATTCTTGTTTGTGGAGGCGATGGAAGTGTAGGTTGGGTTTTGTCAGAA
ATCGATAAGCTCAACTTGAATAAACAGTGTCAGCTGGGAGTGTTGCCTTTGGGTACAGGA
AATGACCTTGCCCGAGTTCTTGGCTGGGGAGGTTCATATGACGATGACACCCAACTTCCT
CAGATCCTAGAGAAACTGGAACGAGCCAGTACCAAAATGTTGGACAGGTGGAGTATAATG
ACATATGAACTCAAATTGCCACCAAAAGCTTCCCTACTTCCAGGACCTCCAGAAGCATCT
GAAGAATTTTATATGACGATTTATGAAGACTCAGTTGCAACGCATCTTACAAAAATCCTC
AATTCTGATGAACATGCAGTGGTCATATCTTCTGCCAAGACGCTATGTGAAACTGTAAAG
GACTTCGTTGCCAAAGTAGAAAAGACGTATGACAAAACCTTGGAAAATGCCGTTGTAGCT
GATGCCGTGGCCAGTAAATGTTCAGTCCTAAACGAGAAGCTCGAACAACTGCTGCAGGCT
TTGCACACAGATTCCCAGGCTGCGCCTGTTCTCCCTGGCCTCAGCCCTCTCATTGTGGAA
GAAGATGCTGTGGAATCGTCCAGTGAAGAGTCCCTGGGTGAAAGCAAAGAGCAGCTTGGG
GATGACGTTACAAAACCTTCCTCCCAGAAAGCCGTCAAACCAAGGGAAATCATGTTGCGG
GCAAATAGTTTAAAGAAAGCAGTGAGGCAAGTCATTGAGGAAGCCGGAAAAGTTATGGAT
GACCCGACAGTTCACCCCTGTGAACCAGCTAATCAGTCCTCTGATTATGACAGCACAGAA
ACAGATGAATCTAAGGAGGAAGCTAAAGATGATGGTGCCAAAGAATCAATAACTGTTAAA
ACTGCACCTCGGTCTCCAGATGCCCGGGCAAGTTATGGCCATTCCCAAACTGATTCTGTC
CCTGGTCCAGCTGTGGCAGCCAGCAAAGAAAACCTCCCTGTGCTCAATACCAGAATAATC
TGCCCAGGTTTAAGAGCAGGACTGGCTGCCTCAATTGCTGGGAGTTCGATTATCAACAAA
ATGTTACTGGCAAACATTGATCCTTTTGGTGCCACGCCGTTTATTGACCCGGATCTAGAT
TCCGTAGATGGATATTCAGAAAAATGTGTCATGAACAATTACTTTGGGATTGGATTAGAT
GCAAAAATTTCATTAGAATTTAATAATAAAAGAGAGGAGCACCCTGAAAAATGCAGGAGC
CGAACTAAAAACTTGATGTGGTATGGAGTCCTTGGAACCCGGGAGTTATTACAGAGATCG
TACAAGAATTTAGAACAAAGGGTTCAACTTGAGTGTGATGGGCAGTATATTCCTCTTCCC
AGCTTGCAAGGCATAGCCGTGTTGAACATTCCCAGCTATGCTGGAGGCACTAACTTTTGG
GGTGGAACTAAAGAGGATGATATATTTGCTGCACCATCCTTTGATGACAAGATCCTGGAA
GTTGTAGCAATATTTGATAGCATGCAAATGGCAGTTTCAAGGGTCATTAAACTGCAGCAT
CATCGAATAGCCCAGTGCCGTACAGTGAAAATCACTATATTTGGTGACGAAGGAGTCCCA
GTGCAAGTGGATGGTGAAGCGTGGGTTCAGCCTCCAGGGATTATCAAAATTGTGCACAAA
AACAGAGCACAAATGCTAACAAGGGACAGAGCCTTTGAGAGCACTCTGAAATCTTGGGAA
GATAAGCAGAAGTGTGATTCTGGTAAACCAGTTCTCCGAACCCATTTGTACATCCATCAC
GCCATTGACTTGGCAACAGAAGAGGTGTCGCAGATGCAGCTATGCTCCCAGGCTGCAGAG
GAGCTCATTACTAGGATATGTGACGCAGCCACAATTCACTGTCTTTTGGAGCAAGAACTG
GCCCATGCTGTGAATGCCTGCTCCCATGCCCTGAATAAAGCCAACCCAAGGTGCCCGGAG
AGTCTTACAAGAGACACTGCCACTGAAATAGCCATCAATGTGAAGGCGCTGTATAATGAA
ACAGAATCTTTGCTAGTTGGCAGGGTTCCTTTGCAGCTGGAATCGCCACATGAAGAGCGA
GTATCCAATGCCTTACACTCTGTGGAGGTGGAATTACAGAAACTGACAGAGATTCCTTGG
CTTTATTATATCTTACACCCAAATGAGGATGAGGAACCTCCTATGGATTGCACCAAAAGG
AACAACAGAAGCACCGTATTTCGAATAGTGCCAAAGTTTAAAAAGGAAAAGGTTCAGAAG
CAGAAGACAAGTTCACAGCCTGTTCAGAAATGGGGCACAGAGGAAGTTGCTGCTTGGCTG
GATCTGCTCAATTTGGGAGAGTACAAAGATATCTTCATCCGTCATGACATCAGAGGGGCT
GAACTTTTGCATCTGGAAAGGCGAGATCTTAAGGATCTGGGGATACCGAAAGTGGGTCAT
GTGAAGCGAATTCTCCAGGGAATTAAAGAGCTTGGAAGGAGCACTCCACAGTCGGAGGTG
TAA
Enzyme 24 GenBank Gene ID NM_178009.2 Link Image
Enzyme 24 GeneCard ID DGKH Link Image
Enzyme 24 GenAtlas ID DGKH Link Image
Enzyme 24 HGNC ID HGNC:2854 Link Image
Enzyme 24 Chromosome Location 1
Enzyme 24 Locus 13q14.11
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 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]
  2. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 10119
Enzyme 25 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
Enzyme 25 Synonyms
  1. 1-acylglycerol-3-phosphate O-acyltransferase 4
  2. 1-AGP acyltransferase 4
  3. 1-AGPAT 4
  4. Lysophosphatidic acid acyltransferase delta
  5. LPAAT-delta
Enzyme 25 Gene Name AGPAT4
Enzyme 25 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase delta
MDLAGLLKSQFLCHLVFCYVFIASGLIINTIQLFTLLLWPINKQLFRKINCRLSYCISSQ
LVMLLEWWSGTECTIFTDPRAYLKYGKENAIVVLNHKFEIDFLCGWSLSERFGLLGGSKV
LAKKELAYVPIIGWMWYFTEMVFCSRKWEQDRKTVATSLQHLRDYPEKYFFLIHCEGTRF
TEKKHEISMQVARAKGLPRLKHHLLPRTKGFAITVRSLRNVVSAVYDCTLNFRNNENPTL
LGVLNGKKYHADLYVRRIPLEDIPEDDDECSAWLHKLYQEKDAFQEEYYRTGTFPETPMV
PPRRPWTLVNWLFWASLVLYPFFQFLVSMIRSGSSLTLASFILVFFVASVGVRWMIGVTE
IDKGSAYGNSDSKQKLND
Enzyme 25 Number of Residues 378
Enzyme 25 Molecular Weight 44020.9
Enzyme 25 Theoretical pI 8.90
Enzyme 25 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 25 General Function Involved in acyltransferase activity
Enzyme 25 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 25 Pathways
Enzyme 25 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • 11-31 125-145 307-327 338-358
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 8886005 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q9NRZ5 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name PLCD_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >1137 bp
ATGGACCTCGCGGGACTGCTGAAGTCTCAGTTCCTGTGCCACCTGGTCTTCTGCTACGTC
TTTATTGCCTCAGGGCTAATCATCAACACCATTCAGCTCTTCACTCTCCTCCTCTGGCCC
ATTAACAAGCAGCTCTTCCGGAAGATCAACTGCAGACTGTCCTATTGCATCTCAAGCCAG
CTGGTGATGCTGCTGGAGTGGTGGTCGGGCACGGAATGCACCATCTTCACGGACCCGCGC
GCCTACCTCAAGTATGGGAAGGAAAATGCCATCGTGGTTCTCAACCACAAGTTTGAAATT
GACTTTCTGTGTGGCTGGAGCCTGTCCGAACGCTTTGGGCTGTTAGGGGGCTCCAAGGTC
CTGGCCAAGAAAGAGCTGGCCTATGTCCCAATTATCGGCTGGATGTGGTACTTCACCGAG
ATGGTCTTCTGTTCGCGCAAGTGGGAGCAGGATCGCAAGACGGTTGCCACCAGTTTGCAG
CACCTCCGGGACTACCCCGAGAAGTATTTTTTCCTGATTCACTGTGAGGGCACACGGTTC
ACGGAGAAGAAGCATGAGATCAGCATGCAGGTGGCCCGGGCCAAGGGGCTGCCTCGCCTC
AAGCATCACCTGTTGCCACGAACCAAGGGCTTCGCCATCACCGTGAGGAGCTTGAGAAAT
GTAGTTTCAGCTGTATATGACTGTACACTCAATTTCAGAAATAATGAAAATCCAACACTG
CTGGGAGTCCTAAACGGAAAGAAATACCATGCAGATTTGTATGTTAGGAGGATCCCACTG
GAAGACATCCCTGAAGACGATGACGAGTGCTCGGCCTGGCTGCACAAGCTCTACCAGGAG
AAGGATGCCTTTCAGGAGGAGTACTACAGGACGGGCACCTTCCCAGAGACGCCCATGGTG
CCCCCCCGGCGGCCCTGGACCCTCGTGAACTGGCTGTTTTGGGCCTCGCTGGTGCTCTAC
CCTTTCTTCCAGTTCCTGGTCAGCATGATCAGGAGCGGGTCTTCCCTGACGCTGGCCAGC
TTCATCCTCGTCTTCTTTGTGGCCTCCGTGGGAGTTCGATGGATGATTGGTGTGACGGAA
ATTGACAAGGGCTCTGCCTACGGCAACTCTGACAGCAAGCAGAAACTGAATGACTGA
Enzyme 25 GenBank Gene ID AF156776 Link Image
Enzyme 25 GeneCard ID AGPAT4 Link Image
Enzyme 25 GenAtlas ID AGPAT4 Link Image
Enzyme 25 HGNC ID HGNC:20885 Link Image
Enzyme 25 Chromosome Location 6
Enzyme 25 Locus 6q26
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Leung DW: The structure and functions of human lysophosphatidic acid acyltransferases. Front Biosci. 2001 Aug 1;6:D944-53. [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]
  3. 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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 12909
Enzyme 26 Name Lysophosphatidylcholine acyltransferase 1
Enzyme 26 Synonyms
  1. LPC acyltransferase 1
  2. LPCAT-1
  3. LysoPC acyltransferase 1
  4. 1-acylglycerophosphocholine O-acyltransferase
  5. 1-alkylglycerophosphocholine O-acetyltransferase
  6. Acetyl-CoA:lyso-platelet-activating factor acetyltransferase
  7. Acetyl-CoA:lyso-PAF acetyltransferase
  8. Lyso-PAF acetyltransferase
  9. LysoPAFAT
  10. Acyltransferase-like 2
  11. Phosphonoformate immuno-associated protein 3
Enzyme 26 Gene Name LPCAT1
Enzyme 26 Protein Sequence >Lysophosphatidylcholine acyltransferase 1
MRLRGCGPRAAPASSAGASDARLLAPPGRNPFVHELRLSALQKAQVALMTLTLFPVRLLV
AAAMMLLAWPLALVASLGSAEKEPEQPPALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGR
QALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQ
DSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPN
KLDTITWTWQGPGALEILWLTLCQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAE
ALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPEKLEKDLDRYSERAR
MKGGEKIGIAEFAASLEVPVSDLLEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDT
IQLAFKMYGAQEDGSVGEGDLSCILKTALGVAELTVTDLFRAIDQEEKGKITFADFHRFA
EMYPAFAEEYLYPDQTHFESCAETSPAPIPNGFCADFSPENSDAGRKPVRKKLD
Enzyme 26 Number of Residues 534
Enzyme 26 Molecular Weight 59150.7
Enzyme 26 Theoretical pI 5.82
Enzyme 26 GO Classification
Function
  • acyltransferase activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 26 General Function Involved in acyltransferase activity
Enzyme 26 Specific Function Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-independent. Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). 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 26 Pathways
Enzyme 26 Reactions
  • acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine [RN:R03437]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • 58-78
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 100811832 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q8NF37 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name PCAT1_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1605 bp
ATGAGGCTGCGGGGATGCGGACCCCGGGCCGCCCCTGCCTCCAGCGCAGGGGCCAGCGAC
GCTCGGCTGCTGGCGCCCCCGGGGCGGAACCCCTTCGTGCACGAGCTGCGCCTCAGCGCC
CTGCAGAAGGCCCAGGTGGCCCTCATGACACTGACGCTCTTCCCGGTCCGGCTCCTGGTT
GCCGCTGCCATGATGCTGCTGGCCTGGCCCCTCGCACTTGTCGCATCCCTGGGCTCTGCG
GAGAAGGAACCCGAGCAGCCCCCGGCCCTGTGGAGGAAGGTTGTGGACTTCCTGCTGAAG
GCCATCATGCGCACCATGTGGTTCGCCGGCGGCTTCCACCGGGTGGCCGTGAAGGGGCGG
CAGGCGCTGCCCACCGAGGCGGCCATCCTCACGCTCGCGCCTCACTCGTCCTACTTCGAC
GCCATCCCTGTGACCATGACGATGTCCTCCATCGTGATGAAGGCAGAGAGCAGAGACATC
CCGATCTGGGGAACTCTGATCCAGTATATACGGCCTGTGTTCGTGTCCCGGTCAGACCAG
GATTCTCGCAGGAAAACAGTAGAAGAAATCAAGAGACGGGCGCAGTCCAACGGAAAGTGG
CCACAGATAATGATTTTTCCAGAAGGAACTTGTACAAACAGGACCTGCCTAATTACCTTC
AAACCTGGTGCATTCATCCCTGGAGCGCCCGTCCAGCCTGTGGTTTTACGATATCCAAAT
AAACTGGACACCATCACATGGACGTGGCAAGGACCTGGAGCGCTGGAAATCCTGTGGCTC
ACGCTGTGTCAGTTTCACAACCAAGTGGAAATCGAGTTCCTTCCTGTGTACAGCCCTTCT
GAGGAGGAGAAGAGGAACCCCGCGCTGTATGCCAGCAACGTGCGGCGAGTCATGGCCGAG
GCCTTGGGTGTCTCCGTGACTGACTACACGTTCGAGGACTGCCAGCTGGCCCTGGCGGAA
GGACAGCTCCGTCTCCCCGCTGACACTTGCCTTTTAGAATTTGCCAGGCTCGTGCGGGGC
CTCGGGCTAAAACCAGAAAAGCTTGAAAAAGATCTGGACAGATACTCAGAAAGAGCCAGG
ATGAAGGGAGGAGAGAAGATAGGTATTGCGGAGTTTGCCGCCTCCCTGGAAGTCCCCGTT
TCTGACTTGCTGGAAGACATGTTTTCACTGTTCGACGAGAGCGGCAGCGGCGAGGTGGAC
CTGCGAGAGTGTGTGGTTGCCCTGTCTGTCGTCTGCCGGCCGGCCCGGACCCTGGACACC
ATCCAGCTGGCTTTCAAGATGTACGGAGCGCAAGAGGACGGCAGCGTCGGCGAAGGTGAC
CTGTCCTGCATCCTCAAGACGGCCCTGGGGGTGGCAGAGCTCACCGTGACCGACCTATTC
CGAGCCATTGACCAAGAGGAGAAGGGGAAGATCACATTCGCTGACTTCCACAGGTTTGCA
GAAATGTACCCTGCCTTCGCAGAGGAATACCTGTACCCGGATCAGACACATTTCGAAAGC
TGTGCAGAGACCTCACCTGCGCCAATCCCAAACGGCTTCTGTGCCGATTTCAGCCCGGAA
AACTCAGACGCTGGGCGGAAGCCTGTTCGCAAGAAGCTGGATTAG
Enzyme 26 GenBank Gene ID AB244719 Link Image
Enzyme 26 GeneCard ID LPCAT1 Link Image
Enzyme 26 GenAtlas ID LPCAT1 Link Image
Enzyme 26 HGNC ID HGNC:25718 Link Image
Enzyme 26 Chromosome Location 5
Enzyme 26 Locus 5p15.33
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Nakanishi H, Shindou H, Hishikawa D, Harayama T, Ogasawara R, Suwabe A, Taguchi R, Shimizu T: Cloning and characterization of mouse lung-type acyl-CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1). Expression in alveolar type II cells and possible involvement in surfactant production. J Biol Chem. 2006 Jul 21;281(29):20140-7. Epub 2006 May 16. [PubMed Link Image]
  2. 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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. Chen X, Hyatt BA, Mucenski ML, Mason RJ, Shannon JM: Identification and characterization of a lysophosphatidylcholine acyltransferase in alveolar type II cells. Proc Natl Acad Sci U S A. 2006 Aug 1;103(31):11724-9. Epub 2006 Jul 24. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 12910
Enzyme 27 Name Lysophosphatidylcholine acyltransferase 2
Enzyme 27 Synonyms
  1. LPC acyltransferase 2
  2. LPCAT-2
  3. LysoPC acyltransferase 2
  4. 1-acylglycerophosphocholine O-acyltransferase
  5. 1-alkylglycerophosphocholine O-acetyltransferase
  6. Acetyl-CoA:lyso-platelet-activating factor acetyltransferase
  7. Acetyl-CoA:lyso-PAF acetyltransferase
  8. Lyso-PAF acetyltransferase
  9. LysoPAFAT
  10. Acyltransferase-like 1
Enzyme 27 Gene Name LPCAT2
Enzyme 27 Protein Sequence >Lysophosphatidylcholine acyltransferase 2
MSRCAQAAEVAATVPGAGVGNVGLRPPMVPRQASFFPPPVPNPFVQQTQIGSARRVQIVL
LGIILLPIRVLLVALILLLAWPFAAISTVCCPEKLTHPITGWRRKITQTALKFLGRAMFF
SMGFIVAVKGKIASPLEAPVFVAAPHSTFFDGIACVVAGLPSMVSRNENAQVPLIGRLLR
AVQPVLVSRVDPDSRKNTINEIIKRTTSGGEWPQILVFPEGTCTNRSCLITFKPGAFIPG
VPVQPVLLRYPNKLDTVTWTWQGYTFIQLCMLTFCQLFTKVEVEFMPVQVPNDEEKNDPV
LFANKVRNLMAEALGIPVTDHTYEDCRLMISAGQLTLPMEAGLVEFTKISRKLKLDWDGV
RKHLDEYASIASSSKGGRIGIEEFAKYLKLPVSDVLRQLFALFDRNHDGSIDFREYVIGL
AVLCNPSNTEEIIQVAFKLFDVDEDGYITEEEFSTILQASLGVPDLDVSGLFKEIAQGDS
ISYEEFKSFALKHPEYAKIFTTYLDLQTCHVFSLPKEVQTTPSTASNKVSPEKHEESTSD
KKDD
Enzyme 27 Number of Residues 544
Enzyme 27 Molecular Weight 60207.3
Enzyme 27 Theoretical pI 6.51
Enzyme 27 GO Classification
Function
  • acyltransferase activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 27 General Function Involved in acyltransferase activity
Enzyme 27 Specific Function Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-dependent. Involved in platelet- activating factor (PAF) biosynthesis by catalyzing the conversion of the PAF precursor, 1-O-alkyl-sn-glycero-3-phosphocholine (lyso- PAF) into 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (PAF). Also converts lyso-PAF to 1-alkyl-phosphatidylcholine (PC), a major component of cell membranes and a PAF precursor. Under resting conditions, acyltransferase activity is preferred. Upon acute inflammatory stimulus, acetyltransferase activity is enhanced and PAF synthesis increases
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions
  • acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine [RN:R03437]
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • 58-78
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 126364244 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q7L5N7 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name PCAT2_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1635 bp
ATGAGCCGGTGCGCCCAGGCGGCGGAAGTGGCGGCCACAGTGCCAGGTGCCGGCGTCGGG
AACGTGGGGCTGCGGCCGCCCATGGTGCCCCGTCAGGCGTCCTTCTTCCCGCCGCCGGTG
CCGAACCCCTTCGTGCAGCAGACGCAGATCGGCTCCGCGAGGCGGGTCCAGATTGTCCTT
CTTGGGATTATCTTGCTTCCAATTCGTGTCTTATTGGTTGCGTTAATTTTATTACTTGCA
TGGCCATTTGCTGCAATTTCAACAGTATGCTGTCCTGAAAAGCTGACCCACCCAATAACT
GGTTGGAGGAGGAAAATTACTCAAACAGCTTTGAAATTTCTGGGTCGTGCTATGTTCTTT
TCAATGGGATTTATAGTTGCTGTAAAAGGAAAGATTGCAAGTCCTTTGGAAGCACCAGTT
TTTGTTGCTGCCCCTCATTCAACATTCTTTGATGGAATTGCCTGTGTTGTAGCTGGGTTA
CCTTCTATGGTATCTCGAAATGAGAATGCACAAGTCCCTCTGATTGGCAGACTGTTACGG
GCTGTGCAACCAGTTTTGGTGTCCCGTGTAGATCCGGATTCCCGAAAAAACACAATAAAT
GAAATAATAAAGCGAACAACATCAGGAGGAGAATGGCCCCAGATACTAGTTTTCCCAGAA
GGTACTTGTACTAATCGTTCCTGTTTGATTACTTTTAAACCAGGAGCCTTCATTCCAGGA
GTTCCAGTGCAGCCAGTCCTCCTCAGATACCCAAACAAGCTGGATACTGTGACCTGGACA
TGGCAAGGATATACATTCATTCAGCTTTGTATGCTTACTTTCTGCCAGCTCTTCACAAAG
GTAGAAGTTGAGTTTATGCCAGTTCAAGTACCAAATGATGAAGAAAAAAATGATCCTGTC
CTTTTTGCCAATAAAGTCCGGAATTTAATGGCAGAAGCTCTGGGAATACCAGTAACAGAT
CATACCTATGAAGACTGCAGATTGATGATTTCAGCAGGACAGCTAACATTGCCTATGGAA
GCTGGGCTGGTGGAATTTACTAAAATTAGCCGAAAATTGAAATTAGATTGGGATGGTGTT
CGTAAGCATTTGGATGAATATGCATCTATTGCGAGTTCCTCAAAAGGAGGAAGAATTGGA
ATTGAAGAATTCGCCAAGTATTTAAAGTTGCCTGTTTCAGATGTCTTGAGACAACTTTTT
GCACTCTTTGACAGGAACCATGATGGCAGCATTGACTTCCGAGAGTATGTGATTGGCCTG
GCTGTCTTGTGCAACCCTTCCAACACAGAGGAGATCATCCAGGTGGCATTTAAGCTGTTT
GACGTTGATGAGGATGGCTACATAACGGAGGAAGAGTTCTCCACCATTCTACAGGCTTCC
CTTGGAGTGCCTGACCTTGATGTTTCTGGTCTCTTCAAGGAAATAGCCCAAGGGGACTCA
ATTTCCTATGAGGAATTTAAAAGTTTTGCCTTAAAGCATCCAGAATATGCTAAGATATTT
ACAACATACCTAGACCTCCAGACGTGCCATGTGTTTTCATTACCAAAAGAAGTCCAGACA
ACCCCCTCCACCGCCAGTAATAAAGTCAGCCCTGAAAAGCATGAAGAGAGTACCTCAGAC
AAAAAAGATGACTGA
Enzyme 27 GenBank Gene ID AB244718 Link Image
Enzyme 27 GeneCard ID LPCAT2 Link Image
Enzyme 27 GenAtlas ID LPCAT2 Link Image
Enzyme 27 HGNC ID HGNC:26032 Link Image
Enzyme 27 Chromosome Location 1
Enzyme 27 Locus 16q12.2
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Shindou H, Hishikawa D, Nakanishi H, Harayama T, Ishii S, Taguchi R, Shimizu T: A single enzyme catalyzes both platelet-activating factor production and membrane biogenesis of inflammatory cells. Cloning and characterization of acetyl-CoA:LYSO-PAF acetyltransferase. J Biol Chem. 2007 Mar 2;282(9):6532-9. Epub 2006 Dec 20. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 12931
Enzyme 28 Name Lysocardiolipin acyltransferase 1
Enzyme 28 Synonyms
  1. 1-acylglycerol-3-phosphate O-acyltransferase 8
  2. 1-AGP acyltransferase 8
  3. 1-AGPAT 8
  4. Acyl-CoA:lysocardiolipin acyltransferase 1
Enzyme 28 Gene Name LCLAT1
Enzyme 28 Protein Sequence >Lysocardiolipin acyltransferase 1
MHSRGREIVVLLNPWSINEAVSSYCTYFIKQDSKSFGIMVSWKGIYFILTLFWGSFFGSI
FMLSPFLPLMFVNPSWYRWINNRLVATWLTLPVALLETMFGVKVIITGDAFVPGERSVII
MNHRTRMDWMFLWNCLMRYSYLRLEKICLKASLKGVPGFGWAMQAAAYIFIHRKWKDDKS
HFEDMIDYFCDIHEPLQLLIFPEGTDLTENSKSRSNAFAEKNGLQKYEYVLHPRTTGFTF
VVDRLREGKNLDAVHDITVAYPHNIPQSEKHLLQGDFPREIHFHVHRYPIDTLPTSKEDL
QLWCHKRWEEKEERLRSFYQGEKNFYFTGQSVIPPCKSELRVLVVKLLSILYWTLFSPAM
CLLIYLYSLVKWYFIITIVIFVLQERIFGGLEIIELACYRLLHKQPHLNSKKNE
Enzyme 28 Number of Residues 414
Enzyme 28 Molecular Weight 48919.8
Enzyme 28 Theoretical pI 8.80
Enzyme 28 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 28 General Function Involved in acyltransferase activity
Enzyme 28 Specific Function Acyl-CoA:lysocardiolipin acyltransferase. Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities. 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. Required for establishment of the hematopoietic and endothelial lineages
Enzyme 28 Pathways
Enzyme 28 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • 47-67 86-106 340-360 362-382
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 42558246 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID Q6UWP7 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name LCLT1_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1245 bp
ATGCATTCCAGGGGAAGGGAAATTGTGGTGCTTCTGAACCCATGGTCAATTAACGAGGCA
GTTTCTAGCTACTGCACGTACTTCATAAAGCAGGACTCTAAAAGCTTTGGAATCATGGTG
TCATGGAAAGGGATTTACTTTATACTGACTCTGTTTTGGGGAAGCTTTTTTGGAAGCATT
TTCATGCTGAGTCCCTTTTTACCTTTGATGTTTGTAAACCCATCTTGGTATCGCTGGATC
AACAACCGCCTTGTGGCAACATGGCTCACCCTACCTGTGGCATTATTGGAGACCATGTTT
GGTGTAAAAGTGATTATAACTGGGGATGCATTTGTTCCTGGAGAAAGAAGTGTCATTATC
ATGAACCATCGGACAAGAATGGACTGGATGTTCCTGTGGAATTGCCTGATGCGATATAGC
TACCTCAGATTGGAGAAAATTTGCCTCAAAGCGAGTCTCAAAGGTGTTCCTGGATTTGGT
TGGGCCATGCAGGCTGCTGCCTATATCTTCATTCATAGGAAATGGAAGGATGACAAGAGC
CATTTCGAAGACATGATTGATTACTTTTGTGATATTCACGAACCACTTCAACTCCTCATA
TTCCCAGAAGGGACTGATCTCACAGAAAACAGCAAGTCTCGAAGTAATGCATTTGCTGAA
AAAAATGGACTTCAGAAATATGAATATGTTTTACATCCAAGAACTACAGGCTTTACTTTT
GTGGTAGACCGTCTAAGAGAAGGTAAGAACCTTGATGCTGTCCATGATATCACTGTGGCG
TATCCTCACAACATTCCTCAATCAGAGAAGCACCTCCTCCAAGGAGACTTTCCCAGGGAA
ATCCACTTTCACGTCCACCGGTATCCAATAGACACCCTCCCCACATCCAAGGAGGACCTT
CAACTCTGGTGCCACAAACGGTGGGAAGAGAAAGAAGAGAGGCTGCGTTCCTTCTATCAA
GGGGAGAAGAATTTTTATTTTACCGGACAGAGTGTCATTCCACCTTGCAAGTCTGAACTC
AGGGTCCTTGTGGTCAAATTGCTCTCTATACTGTATTGGACCCTGTTCAGCCCTGCAATG
TGCCTACTCATATATTTGTACAGTCTTGTTAAGTGGTATTTTATAATCACCATTGTAATC
TTTGTGCTGCAAGAGAGAATATTTGGTGGACTGGAGATCATAGAACTTGCATGTTACCGA
CTTTTACACAAACAGCCACATTTAAATTCAAAGAAAAATGAGTAA
Enzyme 28 GenBank Gene ID NM_182551.3 Link Image
Enzyme 28 GeneCard ID LCLAT1 Link Image
Enzyme 28 GenAtlas ID LCLAT1 Link Image
Enzyme 28 HGNC ID HGNC:26756 Link Image
Enzyme 28 Chromosome Location 2
Enzyme 28 Locus 2p23.1
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Agarwal AK, Barnes RI, Garg A: Functional characterization of human 1-acylglycerol-3-phosphate acyltransferase isoform 8: cloning, tissue distribution, gene structure, and enzymatic activity. Arch Biochem Biophys. 2006 May 15;449(1-2):64-76. Epub 2006 Mar 29. [PubMed Link Image]
  4. Zhao Y, Chen YQ, Li S, Konrad RJ, Cao G: The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin acyltransferase is an acyltransferase of multiple anionic lysophospholipids. J Lipid Res. 2009 May;50(5):945-56. Epub 2008 Dec 15. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 12932
Enzyme 29 Name Lysophosphatidic acid receptor 3
Enzyme 29 Synonyms
  1. LPA receptor 3
  2. LPA-3
  3. Lysophosphatidic acid receptor Edg-7
Enzyme 29 Gene Name LPAR3
Enzyme 29 Protein Sequence >Lysophosphatidic acid receptor 3
MNECHYDKHMDFFYNRSNTDTVDDWTGTKLVIVLCVGTFFCLFIFFSNSLVIAAVIKNRK
FHFPFYYLLANLAAADFFAGIAYVFLMFNTGPVSKTLTVNRWFLRQGLLDSSLTASLTNL
LVIAVERHMSIMRMRVHSNLTKKRVTLLILLVWAIAIFMGAVPTLGWNCLCNISACSSLA
PIYSRSYLVFWTVSNLMAFLIMVVVYLRIYVYVKRKTNVLSPHTSGSISRRRTPMKLMKT
VMTVLGAFVVCWTPGLVVLLLDGLNCRQCGVQHVKRWFLLLALLNSVVNPIIYSYKDEDM
YGTMKKMICCFSQENPERRPSRIPSTVLSRSDTGSQYIEDSISQGAVCNKSTS
Enzyme 29 Number of Residues 353
Enzyme 29 Molecular Weight 40128.1
Enzyme 29 Theoretical pI 9.75
Enzyme 29 GO Classification
Function
  • G-protein coupled receptor activity
  • bioactive lipid receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 29 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 29 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 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • 32-52 68-88 102-124 147-167 187-207 241-261 277-297
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 5922725 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q9UBY5 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name LPAR3_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >1062 bp
ATGAATGAGTGTCACTATGACAAGCACATGGACTTTTTTTATAATAGGAGCAACACTGAT
ACTGTCGATGACTGGACAGGAACAAAGCTTGTGATTGTTTTGTGTGTTGGGACGTTTTTC
TGCCTGTTTATTTTTTTTTCTAATTCTCTGGTCATCGCGGCAGTGATCAAAAACAGAAAA
TTTCATTTCCCCTTCTACTACCTGTTGGCTAATTTAGCTGCTGCCGATTTCTTCGCTGGA
ATTGCCTATGTATTCCTGATGTTTAACACAGGCCCAGTTTCAAAAACTTTGACTGTCAAC
CGCTGGTTTCTCCGTCAGGGGCTTCTGGACAGTAGCTTGACTGCTTCCCTCACCAACTTG
CTGGTTATCGCCGTGGAGAGGCACATGTCAATCATGAGGATGCGGGTCCATAGCAACCTG
ACCAAAAAGAGGGTGACACTGCTCATTTTGCTTGTCTGGGCCATCGCCATTTTTATGGGG
GCGGTCCCCACACTGGGCTGGAATTGCCTCTGCAACATCTCTGCCTGCTCTTCCCTGGCC
CCCATTTACAGCAGGAGTTACCTTGTTTTCTGGACAGTGTCCAACCTCATGGCCTTCCTC
ATCATGGTTGTGGTGTACCTGCGGATCTACGTGTACGTCAAGAGGAAAACCAACGTCTTG
TCTCCGCATACAAGTGGGTCCATCAGCCGCCGGAGGACACCCATGAAGCTAATGAAGACG
GTGATGACTGTCTTAGGGGCGTTTGTGGTATGCTGGACCCCGGGCCTGGTGGTTCTGCTC
CTCGACGGCCTGAACTGCAGGCAGTGTGGCGTGCAGCATGTGAAAAGGTGGTTCCTGCTG
CTGGCGCTGCTCAACTCCGTCGTGAACCCCATCATCTACTCCTACAAGGACGAGGACATG
TATGGCACCATGAAGAAGATGATCTGCTGCTTCTCTCAGGAGAACCCAGAGAGGCGTCCC
TCTCGCATCCCCTCCACAGTCCTCAGCAGGAGTGACACAGGCAGCCAGTACATAGAGGAT
AGTATTAGCCAAGGTGCAGTCTGCAATAAAAGCACTTCCTAA
Enzyme 29 GenBank Gene ID AF127138 Link Image
Enzyme 29 GeneCard ID LPAR3 Link Image
Enzyme 29 GenAtlas ID LPAR3 Link Image
Enzyme 29 HGNC ID HGNC:14298 Link Image
Enzyme 29 Chromosome Location 1
Enzyme 29 Locus 1p22.3
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Contos JJ, Ishii I, Chun J: Lysophosphatidic acid receptors. Mol Pharmacol. 2000 Dec;58(6):1188-96. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 12933
Enzyme 30 Name Lysophosphatidic acid receptor 4
Enzyme 30 Synonyms
  1. LPA receptor 4
  2. LPA-4
  3. G-protein coupled receptor 23
  4. P2Y purinoceptor 9
  5. P2Y9
  6. P2Y5-like receptor
  7. Purinergic receptor 9
Enzyme 30 Gene Name LPAR4
Enzyme 30 Protein Sequence >Lysophosphatidic acid receptor 4
MGDRRFIDFQFQDSNSSLRPRLGNATANNTCIVDDSFKYNLNGAVYSVVFILGLITNSVS
LFVFCFRMKMRSETAIFITNLAVSDLLFVCTLPFKIFYNFNRHWPFGDTLCKISGTAFLT
NIYGSMLFLTCISVDRFLAIVYPFRSRTIRTRRNSAIVCAGVWILVLSGGISASLFSTTN
VNNATTTCFEGFSKRVWKTYLSKITIFIEVVGFIIPLILNVSCSSVVLRTLRKPATLSQI
GTNKKKVLKMITVHMAVFVVCFVPYNSVLFLYALVRSQAITNCFLERFAKIMYPITLCLA
TLNCCFDPFIYYFTLESFQKSFYINAHIRMESLFKTETPLTTKPSLPAIQEEVSDQTTNN
GGELMLESTF
Enzyme 30 Number of Residues 370
Enzyme 30 Molecular Weight 41894.7
Enzyme 30 Theoretical pI 9.28
Enzyme 30 GO Classification
Function
  • G-protein coupled receptor activity
  • molecular transducer activity
  • nucleotide receptor activity, G-protein coupled
  • purinergic nucleotide receptor activity, G-protein coupled
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 30 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 30 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 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • 44-64 74-94 113-133 156-176 204-224 255-275 295-315
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 2240035 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q99677 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name LPAR4_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >1113 bp
ATGGGTGACAGAAGATTCATTGACTTCCAATTCCAAGATTCAAATTCAAGCCTCAGACCC
AGGTTGGGCAATGCTACTGCCAATAATACTTGCATTGTTGATGATTCCTTCAAGTATAAT
CTCAATGGTGCTGTCTACAGTGTTGTATTCATCTTGGGTCTGATAACCAACAGTGTCTCT
CTGTTTGTCTTCTGTTTCCGCATGAAAATGAGAAGTGAGACTGCTATTTTTATCACCAAT
CTAGCTGTCTCTGATTTGCTTTTTGTCTGTACACTACCTTTTAAAATATTTTACAACTTC
AACCGCCACTGGCCTTTTGGTGACACCCTCTGCAAGATCTCTGGAACTGCATTCCTTACC
AACATCTATGGGAGCATGCTCTTTCTCACCTGTATTAGTGTGGATCGTTTCCTGGCCATT
GTCTATCCTTTTCGATCTCGTACTATTAGGACTAGGAGGAATTCTGCCATTGTGTGTGCT
GGTGTCTGGATCCTAGTCCTCAGTGGCGGTATTTCAGCCTCTTTGTTTTCCACCACTAAT
GTCAACAATGCAACCACCACCTGCTTTGAAGGCCTCTCCAAACGTGTCTGGAAGACTTAT
TTATCCAAGATCACAATATTTATTGAAGTTGTTGGGTTTATCATTCCTCTAATATTGAAT
GTCTCTTGCTCTTCTGTGGTGCTGAGAACTCTTCGCAAGCCTGCTACTCTGTCTCAAATT
GGGACCAATAAGAAAAAAGTACTGAAAATGATCACAGTACATATGGCAGTCTTTGTGGTA
TGCTTTGTACCCTACAACTCTGTCCTCTTCTTGTATGCCCTGGTGCGCTCCCAAGCTATT
ACTAATTGCTTTTTGGAAAGATTTGCAAAGATCATGTACCCAATCACCTTGTGCCTTGCA
ACTCTGAACTGTTGTTTTGACCCTTTCATCTATTACTTCACCCTTGAATCCTTTCAGAAG
TCCTTCTACATCAATGCCCACATCAGAATGGAGTCCCTGTTTAAGACTGAAACACCTTTG
ACCACAAAGCCTTCCCTTCCAGCTATTCAAGAGGAAGTGAGTGATCAAACAACAAATAAT
GGTGGTGAATTAATGCTAGAATCCACCTTTTAG
Enzyme 30 GenBank Gene ID AF005419 Link Image
Enzyme 30 GeneCard ID LPAR4 Link Image
Enzyme 30 GenAtlas ID LPAR4 Link Image
Enzyme 30 HGNC ID HGNC:4478 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. 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]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Noguchi K, Ishii S, Shimizu T: Identification of p2y9/GPR23 as a novel G protein-coupled receptor for lysophosphatidic acid, structurally distant from the Edg family. J Biol Chem. 2003 Jul 11;278(28):25600-6. Epub 2003 Apr 30. [PubMed Link Image]
  7. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 12934
Enzyme 31 Name Lysophosphatidic acid receptor 5
Enzyme 31 Synonyms
  1. LPA receptor 5
  2. LPA-5
  3. G-protein coupled receptor 92
  4. G-protein coupled receptor 93
Enzyme 31 Gene Name LPAR5
Enzyme 31 Protein Sequence >Lysophosphatidic acid receptor 5
MLANSSSTNSSVLPCPDYRPTHRLHLVVYSLVLAAGLPLNALALWVFLRALRVHSVVSVY
MCNLAASDLLFTLSLPVRLSYYALHHWPFPDLLCQTTGAIFQMNMYGSCIFLMLINVDRY
AAIVHPLRLRHLRRPRVARLLCLGVWALILVFAVPAARVHRPSRCRYRDLEVRLCFESFS
DELWKGRLLPLVLLAEALGFLLPLAAVVYSSGRVFWTLARPDATQSQRRRKTVRLLLANL
VIFLLCFVPYNSTLAVYGLLRSKLVAASVPARDRVRGVLMVMVLLAGANCVLDPLVYYFS
AEGFRNTLRGLGTPHRARTSATNGTRAALAQSERSAVTTDATRPDAASQGLLRPSDSHSL
SSFTQCPQDSAL
Enzyme 31 Number of Residues 372
Enzyme 31 Molecular Weight 41346.0
Enzyme 31 Theoretical pI 10.44
Enzyme 31 GO Classification
Function
  • G-protein coupled receptor activity
  • molecular transducer activity
  • nucleotide receptor activity, G-protein coupled
  • purinergic nucleotide receptor activity, G-protein coupled
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 31 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 31 Specific Function Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • 27-47 56-76 97-117 137-157 188-208 240-260 277-297
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 20152264 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q9H1C0 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name LPAR5_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1119 bp
ATGTTAGCCAACAGCTCCTCAACCAACAGTTCTGTTCTCCCGTGTCCTGACTACCGACCT
ACCCACCGCCTGCACTTGGTGGTCTACAGCTTGGTGCTGGCTGCCGGGCTCCCCCTCAAC
GCGCTAGCCCTCTGGGTCTTCCTGCGCGCGCTGCGCGTGCACTCGGTGGTGAGCGTGTAC
ATGTGTAACCTGGCGGCCAGCGACCTGCTCTTCACCCTCTCGCTGCCCGTTCGTCTCTCC
TACTACGCACTGCACCACTGGCCCTTCCCCGACCTCCTGTGCCAGACGACGGGCGCCATC
TTCCAGATGAACATGTACGGCAGCTGCATCTTCCTGATGCTCATCAACGTGGACCGCTAC
GCCGCCATCGTGCACCCGCTGCGACTGCGCCACCTGCGGCGGCCCCGCGTGGCGCGGCTG
CTCTGCCTGGGCGTGTGGGCGCTCATCCTGGTGTTTGCCGTGCCCGCCGCCCGCGTGCAC
AGGCCCTCGCGTTGCCGCTACCGGGACCTCGAGGTGCGCCTATGCTTCGAGAGCTTCAGC
GACGAGCTGTGGAAAGGCAGGCTGCTGCCCCTCGTGCTGCTGGCCGAGGCGCTGGGCTTC
CTGCTGCCCCTGGCGGCGGTGGTCTACTCGTCGGGCCGAGTCTTCTGGACGCTGGCGCGC
CCCGACGCCACGCAGAGCCAGCGGCGGCGGAAGACCGTGCGCCTCCTGCTGGCTAACCTC
GTCATCTTCCTGCTGTGCTTCGTGCCCTACAACAGCACGCTGGCGGTCTACGGGCTGCTG
CGGAGCAAGCTGGTGGCGGCCAGCGTGCCTGCCCGCGATCGCGTGCGCGGGGTGCTGATG
GTGATGGTGCTGCTGGCCGGCGCCAACTGCGTGCTGGACCCGCTGGTGTACTACTTTAGC
GCCGAGGGCTTCCGCAACACCCTGCGCGGCCTGGGCACTCCGCACCGGGCCAGGACCTCG
GCCACCAACGGGACGCGGGCGGCGCTCGCGCAATCCGAAAGGTCCGCCGTCACCACCGAC
GCCACCAGGCCGGATGCCGCCAGTCAGGGGCTGCTCCGACCCTCCGACTCCCACTCTCTG
TCTTCCTTCACACAGTGTCCCCAGGATTCCGCCCTCTGA
Enzyme 31 GenBank Gene ID AB083600 Link Image
Enzyme 31 GeneCard ID LPAR5 Link Image
Enzyme 31 GenAtlas ID LPAR5 Link Image
Enzyme 31 HGNC ID HGNC:13307 Link Image
Enzyme 31 Chromosome Location 1
Enzyme 31 Locus 12p13.31
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 12935
Enzyme 32 Name Lysophospholipid acyltransferase LPCAT4
Enzyme 32 Synonyms
  1. 1-acylglycerol-3-phosphate O-acyltransferase 7
  2. 1-AGP acyltransferase 7
  3. 1-AGPAT 7
  4. Acyltransferase-like 3
  5. Lysophosphatidylcholine acyltransferase 4
  6. Lysophosphatidylethanolamine acyltransferase 2
Enzyme 32 Gene Name LPCAT4
Enzyme 32 Protein Sequence >Lysophospholipid acyltransferase LPCAT4
MSQGSPGDWAPLDPTPGPPASPNPFVHELHLSRLQRVKFCLLGALLAPIRVLLAFIVLFL
LWPFAWLQVAGLSEEQLQEPITGWRKTVCHNGVLGLSRLLFFLLGFLRIRVRGQRASRLQ
APVLVAAPHSTFFDPIVLLPCDLPKVVSRAENLSVPVIGALLRFNQAILVSRHDPASRRR
VVEEVRRRATSGGKWPQVLFFPEGTCSNKKALLKFKPGAFIAGVPVQPVLIRYPNSLDTT
SWAWRGPGVLKVLWLTASQPCSIVDVEFLPVYHPSPEESRDPTLYANNVQRVMAQALGIP
ATECEFVGSLPVIVVGRLKVALEPQLWELGKVLRKAGLSAGYVDAGAEPGRSRMISQEEF
ARQLQLSDPQTVAGAFGYFQQDTKGLVDFRDVALALAALDGGRSLEELTRLAFELFAEEQ
AEGPNRLLYKDGFSTILHLLLGSPHPAATALHAELCQAGSSQGLSLCQFQNFSLHDPLYG
KLFSTYLRPPHTSRGTSQTPNASSPGNPTALANGTVQAPKQKGD
Enzyme 32 Number of Residues 524
Enzyme 32 Molecular Weight 57218.6
Enzyme 32 Theoretical pI 9.24
Enzyme 32 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 32 General Function Involved in acyltransferase activity
Enzyme 32 Specific Function Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates; converts lysophosphatidylethanolamine to phosphatidylethanolamine, lysophosphatidylcholine to phosphatidycholine, 1-alkenyl-lysophatidylethanolamine to 1- alkenyl-phosphatidylethanolamine, lysophosphatidylglycerol and alkyl-lysophosphatidylcholine to phosphatidylglycerol and alkyl- phosphatidylcholine, respectively. In contrast, has no lysophosphatidylinositol, glycerol-3-phosphate, diacylglycerol or lysophosphatidic acid acyltransferase activity. Prefers long chain acyl-CoAs (C16, C18) as acyl donors
Enzyme 32 Pathways
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • 40-62 87-107
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 87116681 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q643R3 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name LPCT4_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >1575 bp
ATGAGCCAGGGAAGTCCGGGGGACTGGGCCCCCCTAGATCCCACCCCCGGACCCCCAGCA
TCCCCCAACCCCTTCGTGCATGAGTTACATCTCTCTCGCCTCCAGAGGGTTAAGTTCTGC
CTCCTGGGGGCATTGCTGGCCCCCATCCGAGTGCTTCTGGCCTTTATCGTCCTCTTTCTC
CTCTGGCCCTTTGCCTGGCTTCAAGTGGCCGGTCTTAGTGAGGAGCAGCTTCAGGAGCCA
ATTACAGGATGGAGGAAGACTGTGTGCCACAACGGGGTGCTAGGCCTGAGCCGCCTGCTG
TTTTTCCTGCTGGGCTTCCTCCGGATTCGCGTTCGTGGCCAGCGAGCCTCTCGCCTTCAA
GCCCCTGTCCTTGTTGCTGCCCCACACTCCACTTTCTTTGACCCCATTGTTCTGCTGCCC
TGTGACCTGCCCAAAGTTGTGTCCCGAGCTGAGAACCTTTCCGTTCCTGTCATTGGAGCC
CTTCTTCGATTCAACCAAGCCATCCTGGTATCCCGGCATGACCCGGCTTCTCGACGCAGA
GTGGTGGAGGAGGTCCGAAGGCGGGCCACCTCAGGAGGCAAGTGGCCGCAGGTGCTATTC
TTTCCTGAGGGCACCTGTTCCAACAAGAAGGCTTTGCTTAAGTTCAAACCAGGAGCCTTC
ATCGCAGGGGTGCCTGTGCAGCCTGTCCTCATCCGCTACCCCAACAGTCTGGACACCACC
AGCTGGGCATGGAGGGGTCCTGGAGTACTCAAAGTCCTCTGGCTCACAGCCTCTCAGCCC
TGCAGCATTGTGGATGTGGAGTTCCTTCCTGTGTATCACCCCAGCCCTGAGGAGAGCAGG
GACCCCACCCTCTATGCCAACAATGTTCAGAGGGTCATGGCACAGGCTCTGGGCATTCCA
GCCACCGAATGTGAGTTTGTAGGGAGCTTACCTGTGATTGTGGTGGGCCGGCTGAAGGTG
GCGTTGGAACCACAGCTCTGGGAACTGGGAAAAGTGCTTCGGAAGGCTGGGCTGTCCGCT
GGCTATGTGGACGCTGGGGCAGAGCCAGGCCGGAGTCGAATGATCAGCCAGGAAGAGTTT
GCCAGGCAGCTACAGCTCTCTGATCCTCAGACGGTGGCTGGTGCCTTTGGCTACTTCCAG
CAGGATACCAAGGGTTTGGTGGACTTCCGAGATGTGGCCCTTGCACTAGCAGCTCTGGAT
GGGGGCAGGAGCCTGGAAGAGCTAACTCGTCTGGCCTTTGAGCTCTTTGCTGAAGAGCAA
GCAGAGGGTCCCAACCGCCTGCTGTACAAAGACGGCTTCAGCACCATCCTGCACCTGCTG
CTGGGTTCACCCCACCCTGCTGCCACAGCTTTGCATGCTGAGCTGTGCCAGGCAGGATCC
AGCCAAGGCCTCTCCCTCTGTCAGTTCCAGAACTTCTCCCTCCATGACCCACTCTATGGG
AAACTCTTCAGCACCTACCTGCGCCCCCCACACACCTCTCGAGGCACCTCCCAGACACCA
AATGCCTCATCCCCAGGCAACCCCACTGCTCTGGCCAATGGGACTGTGCAAGCACCCAAG
CAGAAGGGAGACTGA
Enzyme 32 GenBank Gene ID NM_153613.2 Link Image
Enzyme 32 GeneCard ID LPCAT4 Link Image
Enzyme 32 GenAtlas ID LPCAT4 Link Image
Enzyme 32 HGNC ID HGNC:30059 Link Image
Enzyme 32 Chromosome Location 1
Enzyme 32 Locus 15q14
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Ye GM, Chen C, Huang S, Han DD, Guo JH, Wan B, Yu L: Cloning and characterization a novel human 1-acyl-sn-glycerol-3-phosphate acyltransferase gene AGPAT7. DNA Seq. 2005 Oct;16(5):386-90. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Cao J, Shan D, Revett T, Li D, Wu L, Liu W, Tobin JF, Gimeno RE: Molecular identification of a novel mammalian brain isoform of acyl-CoA:lysophospholipid acyltransferase with prominent ethanolamine lysophospholipid acylating activity, LPEAT2. J Biol Chem. 2008 Jul 4;283(27):19049-57. Epub 2008 May 5. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 12936
Enzyme 33 Name Glycerol-3-phosphate acyltransferase 3
Enzyme 33 Synonyms
  1. GPAT-3
  2. 1-acylglycerol-3-phosphate O-acyltransferase 9
  3. 1-AGP acyltransferase 9
  4. 1-AGPAT 9
  5. Acyl-CoA:glycerol-3-phosphate acyltransferase 3
  6. hGPAT3
  7. Lung cancer metastasis-associated protein 1
  8. Lysophosphatidic acid acyltransferase theta
  9. LPAAT-theta
  10. MAG-1
Enzyme 33 Gene Name AGPAT9
Enzyme 33 Protein Sequence >Glycerol-3-phosphate acyltransferase 3
MEGAELAGKILSTWLTLVLGFILLPSVFGVSLGISEIYMKILVKTLEWATIRIEKGTPKE
SILKNSASVGIIQRDESPMEKGLSGLRGRDFELSDVFYFSKKGLEAIVEDEVTQRFSSEE
LVSWNLLTRTNVNFQYISLRLTMVWVLGVIVRYCVLLPLRVTLAFIGISLLVIGTTLVGQ
LPDSSLKNWLSELVHLTCCRICVRALSGTIHYHNKQYRPQKGGICVANHTSPIDVLILTT
DGCYAMVGQVHGGLMGIIQRAMVKACPHVWFERSEMKDRHLVTKRLKEHIADKKKLPILI
FPEGTCINNTSVMMFKKGSFEIGGTIHPVAIKYNPQFGDAFWNSSKYNMVSYLLRMMTSW
AIVCDVWYMPPMTREEGEDAVQFANRVKSAIAIQGGLTELPWDGGLKRAKVKDIFKEEQQ
KNYSKMIVGNGSLS
Enzyme 33 Number of Residues 434
Enzyme 33 Molecular Weight 48704.8
Enzyme 33 Theoretical pI 9.15
Enzyme 33 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 33 General Function Involved in acyltransferase activity
Enzyme 33 Specific Function Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Overexpression activates the mTOR pathway
Enzyme 33 Pathways
Enzyme 33 Reactions
  • acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate [RN:R00851]
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • 14-34 137-157 161-181
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 21362092 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q53EU6 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name GPAT3_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >1305 bp
ATGGAGGGCGCAGAGCTGGCCGGGAAGATCCTTTCCACCTGGCTGACGCTGGTTCTCGGC
TTCATCCTTTTACCTTCGGTCTTCGGAGTGTCTCTGGGCATCTCCGAGATCTACATGAAG
ATCCTAGTGAAAACTTTAGAGTGGGCCACAATACGAATTGAAAAAGGAACCCCAAAGGAG
TCGATTCTTAAAAACTCTGCTTCTGTTGGTATTATCCAAAGAGATGAGTCACCCATGGAA
AAAGGGCTCTCTGGTCTACGAGGAAGGGACTTTGAGCTGTCTGACGTGTTTTATTTCTCC
AAGAAGGGATTGGAAGCCATTGTAGAAGATGAAGTGACCCAGAGGTTTTCCTCAGAGGAG
CTAGTGTCATGGAATCTCCTCACAAGAACCAATGTAAATTTCCAGTACATCAGTCTGCGG
CTCACTATGGTGTGGGTGCTGGGCGTCATAGTGCGCTATTGTGTCCTACTGCCTCTGAGG
GTTACCTTGGCTTTCATTGGGATCAGTTTGCTGGTTATAGGAACTACACTGGTTGGGCAG
CTGCCAGACAGCAGCCTCAAAAACTGGCTGAGTGAACTGGTCCATCTGACTTGCTGCCGG
ATCTGTGTGCGAGCCCTCTCTGGTACCATTCATTATCATAACAAGCAGTACAGACCCCAG
AAGGGAGGCATTTGTGTTGCCAACCATACTTCCCCCATTGATGTTTTAATCTTGACAACG
GATGGATGTTATGCTATGGTTGGCCAGGTTCATGGCGGCTTGATGGGAATTATTCAGAGA
GCTATGGTCAAGGCTTGTCCTCATGTCTGGTTTGAACGCTCAGAAATGAAGGATCGACAC
CTGGTTACTAAGAGACTAAAAGAACATATTGCTGATAAGAAGAAACTACCCATACTAATT
TTTCCTGAAGGAACTTGCATCAACAATACTTCAGTCATGATGTTTAAAAAGGGGAGCTTT
GAAATTGGAGGAACCATACATCCAGTTGCAATTAAGTATAACCCTCAGTTCGGTGATGCA
TTTTGGAACAGTAGTAAATACAACATGGTGAGCTACCTGCTTCGAATGATGACCAGCTGG
GCCATCGTCTGTGACGTGTGGTACATGCCCCCCATGACCAGAGAGGAAGGAGAAGATGCA
GTCCAGTTTGCTAACAGGGTTAAGTCTGCTATTGCTATACAAGGAGGCCTGACTGAACTT
CCCTGGGATGGAGGACTAAAGAGAGCAAAGGTGAAGGACATCTTTAAGGAAGAGCAGCAG
AAAAATTACAGCAAGATGATTGTGGGCAATGGATCTCTCAGCTAA
Enzyme 33 GenBank Gene ID NM_032717.3 Link Image
Enzyme 33 GeneCard ID AGPAT9 Link Image
Enzyme 33 GenAtlas ID AGPAT9 Link Image
Enzyme 33 HGNC ID HGNC:28157 Link Image
Enzyme 33 Chromosome Location 4
Enzyme 33 Locus 4q21.23
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Tang W, Yuan J, Chen X, Gu X, Luo K, Li J, Wan B, Wang Y, Yu L: Identification of a novel human lysophosphatidic acid acyltransferase, LPAAT-theta, which activates mTOR pathway. J Biochem Mol Biol. 2006 Sep 30;39(5):626-35. [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]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A: Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene. 2004 Aug 5;23(35):5901-11. [PubMed Link Image]
  6. Cao J, Li JL, Li D, Tobin JF, Gimeno RE: Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de novo triacylglycerol synthesis. Proc Natl Acad Sci U S A. 2006 Dec 26;103(52):19695-700. Epub 2006 Dec 14. [PubMed Link Image]
  7. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 12937
Enzyme 34 Name Lysophosphatidic acid phosphatase type 6
Enzyme 34 Synonyms
  1. Acid phosphatase 6, lysophosphatidic
  2. Acid phosphatase-like protein 1
  3. PACPL1
Enzyme 34 Gene Name ACP6
Enzyme 34 Protein Sequence >Lysophosphatidic acid phosphatase type 6
MITGVFSMRLWTPVGVLTSLAYCLHQRRVALAELQEADGQCPVDRSLLKLKMVQVVFRHG
ARSPLKPLPLEEQVEWNPQLLEVPPQTQFDYTVTNLAGGPKPYSPYDSQYHETTLKGGMF
AGQLTKVGMQQMFALGERLRKNYVEDIPFLSPTFNPQEVFIRSTNIFRNLESTRCLLAGL
FQCQKEGPIIIHTDEADSEVLYPNYQSCWSLRQRTRGRRQTASLQPGISEDLKKVKDRMG
IDSSDKVDFFILLDNVAAEQAHNLPSCPMLKRFARMIEQRAVDTSLYILPKEDRESLQMA
VGPFLHILESNLLKAMDSATAPDKIRKLYLYAAHDVTFIPLLMTLGIFDHKWPPFAVDLT
MELYQHLESKEWFVQLYYHGKEQVPRGCPDGLCPLDMFLNAMSVYTLSPEKYHALCSQTQ
VMEVGNEE
Enzyme 34 Number of Residues 428
Enzyme 34 Molecular Weight 48886.0
Enzyme 34 Theoretical pI 6.44
Enzyme 34 GO Classification
Function
  • acid phosphatase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphatase activity
  • phosphoric ester hydrolase activity
Process
Component
Enzyme 34 General Function Involved in acid phosphatase activity
Enzyme 34 Specific Function Hydrolyzes lysophosphatidic acid to monoacylglycerol
Enzyme 34 Pathways
Enzyme 34 Reactions
  • a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626]
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • 1-32
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 7594827 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q9NPH0 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name PPA6_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1287 bp
ATGATCACTGGTGTGTTCAGCATGCGCTTGTGGACCCCAGTGGGCGTCCTGACCTCGCTG
GCGTACTGCCTGCACCAGCGGCGGGTGGCCCTGGCCGAGCTGCAGGAGGCCGATGGCCAG
TGTCCGGTCGACCGCAGCCTGCTGAAGTTGAAAATGGTGCAGGTCGTGTTTCGACACGGG
GCTCGGAGTCCTCTCAAGCCGCTCCCGCTGGAGGAGCAGGTAGAGTGGAACCCCCAGCTA
TTAGAGGTCCCACCCCAAACTCAGTTTGATTACACAGTCACCAATCTAGCTGGTGGTCCG
AAACCATATTCTCCTTACGACTCTCAATACCATGAGACCACCCTGAAGGGGGGCATGTTT
GCTGGGCAGCTGACCAAGGTGGGCATGCAGCAAATGTTTGCCTTGGGAGAGAGACTGAGG
AAGAACTATGTGGAAGACATTCCCTTTCTTTCACCAACCTTCAACCCACAGGAGGTCTTT
ATTCGTTCCACTAACATTTTTCGGAATCTGGAGTCCACCCGTTGTTTGCTGGCTGGGCTT
TTCCAGTGTCAGAAAGAAGGACCCATCATCATCCACACTGATGAAGCAGATTCAGAAGTC
TTGTATCCCAACTACCAAAGCTGCTGGAGCCTGAGGCAGAGAACCAGAGGCCGGAGGCAG
ACTGCCTCTTTACAGCCAGGAATCTCAGAGGATTTGAAAAAGGTGAAGGACAGGATGGGC
ATTGACAGTAGTGATAAAGTGGACTTCTTCATCCTCCTGGACAACGTGGCTGCCGAGCAG
GCACACAACCTCCCAAGCTGCCCCATGCTGAAGAGATTTGCACGGATGATCGAACAGAGA
GCTGTGGACACATCCTTGTACATACTGCCCAAGGAAGACAGGGAAAGTCTTCAGATGGCA
GTAGGCCCATTCCTCCACATCCTAGAGAGCAACCTGCTGAAAGCCATGGACTCTGCCACT
GCCCCCGACAAGATCAGAAAGCTGTATCTCTATGCGGCTCATGATGTGACCTTCATACCG
CTCTTAATGACCCTGGGGATTTTTGACCACAAATGGCCACCGTTTGCTGTTGACCTGACC
ATGGAACTTTACCAGCACCTGGAATCTAAGGAGTGGTTTGTGCAGCTCTATTACCACGGG
AAGGAGCAGGTGCCGAGAGGTTGCCCTGATGGGCTCTGCCCGCTGGACATGTTCTTGAAT
GCCATGTCAGTTTATACCTTAAGCCCAGAAAAATACCATGCACTCTGCTCTCAAACTCAG
GTGATGGAAGTTGGAAATGAAGAGTAA
Enzyme 34 GenBank Gene ID AB030039 Link Image
Enzyme 34 GeneCard ID ACP6 Link Image
Enzyme 34 GenAtlas ID ACP6 Link Image
Enzyme 34 HGNC ID HGNC:29609 Link Image
Enzyme 34 Chromosome Location 1
Enzyme 34 Locus 1q21
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 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]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Zhang Z, Henzel WJ: Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 2004 Oct;13(10):2819-24. Epub 2004 Aug 31. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 12938
Enzyme 35 Name Lysophosphatidic acid receptor 6
Enzyme 35 Synonyms
  1. LPA receptor 6
  2. LPA-6
  3. Oleoyl-L-alpha-lysophosphatidic acid receptor
  4. P2Y purinoceptor 5
  5. P2Y5
  6. Purinergic receptor 5
  7. RB intron encoded G-protein coupled receptor
Enzyme 35 Gene Name LPAR6
Enzyme 35 Protein Sequence >Lysophosphatidic acid receptor 6
MVSVNSSHCFYNDSFKYTLYGCMFSMVFVLGLISNCVAIYIFICVLKVRNETTTYMINLA
MSDLLFVFTLPFRIFYFTTRNWPFGDLLCKISVMLFYTNMYGSILFLTCISVDRFLAIVY
PFKSKTLRTKRNAKIVCTGVWLTVIGGSAPAVFVQSTHSQGNNASEACFENFPEATWKTY
LSRIVIFIEIVGFFIPLILNVTCSSMVLKTLTKPVTLSRSKINKTKVLKMIFVHLIIFCF
CFVPYNINLILYSLVRTQTFVNCSVVAAVRTMYPITLCIAVSNCCFDPIVYYFTSDTIQN
SIKMKNWSVRRSDFRFSEVHGAENFIQHNLQTLKSKIFDNESAA
Enzyme 35 Number of Residues 344
Enzyme 35 Molecular Weight 39391.2
Enzyme 35 Theoretical pI 9.16
Enzyme 35 GO Classification
Function
  • G-protein coupled receptor activity
  • molecular transducer activity
  • nucleotide receptor activity, G-protein coupled
  • purinergic nucleotide receptor activity, G-protein coupled
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 35 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 35 Specific Function Binds to oleoyl-L-alpha-lysophosphatidic acid (LPA). Intracellular cAMP is involved in the receptor activation. Important for the maintenance of hair growth and texture
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • 20-46 56-79 93-112 134-154 182-209 228-253 273-292
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 2232069 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID P43657 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name LPAR6_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >1035 bp
ATGGTAAGCGTTAACAGCTCCCACTGCTTCTATAATGACTCCTTTAAGTACACTTTGTAT
GGGTGCATGTTCAGCATGGTGTTTGTGCTTGGGTTAGTATCCAATTGTGTTGCCATATAC
ATTTTCATCTGCGTCCTCAAAGTCCGAAATGAAACTACAACTTACATGATTAACTTGGCA
ATGTCAGACTTGCTTTTTGTTTTTACTTTACCCTTCAGGATTTTTTACTTCACAACACGG
AATTGGCCATTTGGAGATTTACTTTGTAAGATTTCTGTGATGCTGTTTTATACCAACATG
TACGGAAGCATTCTGTTCTTAACCTGTATTAGTGTAGATCGATTTCTGGCAATTGTCTAC
CCATTTAAGTCAAAGACTCTAAGAACCAAAAGAAATGCAAAGATTGTTTGCACTGGCGTG
TGGTTAACTGTGATCGGAGGAAGTGCACCCGCCGTTTTTGTTCAGTCTACCCACTCTCAG
GGTAACAATGCCTCAGAAGCCTGCTTTGAAAATTTTCCAGAAGCCACATGGAAAACATAT
CTCTCAAGGATTGTAATTTTCATCGAAATAGTGGGATTTTTTATTCCTCTAATTTTAAAT
GTAACTTGTTCTAGTATGGTGCTAAAAACTTTAACCAAACCAGTTACATTAAGTAGAAGC
AAAATAAACAAAACTAAGGTTTTAAAAATGATTTTTGTACATTTGATCATATTCTGTTTC
TGTTTTGTTCCTTACAATATCAATCTTATTTTATATTCTCTTGTGAGAACACAAACATTT
GTTAATTGCTCAGTAGTGGCAGCAGTAAGGACAATGTACCCAATCACTCTCTGTATTGCT
GTTTCCAACTGTTGTTTTGACCCTATAGTTTACTACTTTACATCGGACACAATTCAGAAT
TCAATAAAAATGAAAAACTGGTCTGTCAGGAGAAGTGACTTCAGATTCTCTGAAGTTCAT
GGTGCAGAGAATTTTATTCAGCATAACCTACAGACCTTAAAAAGTAAGATATTTGACAAT
GAATCTGCTGCCTGA
Enzyme 35 GenBank Gene ID AF000546 Link Image
Enzyme 35 GeneCard ID LPAR6 Link Image
Enzyme 35 GenAtlas ID LPAR6 Link Image
Enzyme 35 HGNC ID HGNC:15520 Link Image
Enzyme 35 Chromosome Location 1
Enzyme 35 Locus 13q14
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. 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]
  2. 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]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. 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]
  8. Pasternack SM, von Kugelgen I, Aboud KA, Lee YA, Ruschendorf F, Voss K, Hillmer AM, Molderings GJ, Franz T, Ramirez A, Nurnberg P, Nothen MM, Betz RC: G protein-coupled receptor P2Y5 and its ligand LPA are involved in maintenance of human hair growth. Nat Genet. 2008 Mar;40(3):329-34. Epub 2008 Feb 24. [PubMed Link Image]
  9. Shimomura Y, Wajid M, Ishii Y, Shapiro L, Petukhova L, Gordon D, Christiano AM: Disruption of P2RY5, an orphan G protein-coupled receptor, underlies autosomal recessive woolly hair. Nat Genet. 2008 Mar;40(3):335-9. Epub 2008 Feb 24. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 12939
Enzyme 36 Name Lipase member H
Enzyme 36 Synonyms
  1. LPD lipase-related protein
  2. Membrane-associated phosphatidic acid-selective phospholipase A1-alpha
  3. mPA-PLA1 alpha
  4. Phospholipase A1 member B
Enzyme 36 Gene Name LIPH
Enzyme 36 Protein Sequence >Lipase member H
MLRFYLFISLLCLSRSDAEETCPSFTRLSFHSAVVGTGLNVRLMLYTRKNLTCAQTINSS
AFGNLNVTKKTTFIVHGFRPTGSPPVWMDDLVKGLLSVEDMNVVVVDWNRGATTLIYTHA
SSKTRKVAMVLKEFIDQMLAEGASLDDIYMIGVSLGAHISGFVGEMYDGWLGRITGLDPA
GPLFNGKPHQDRLDPSDAQFVDVIHSDTDALGYKEPLGNIDFYPNGGLDQPGCPKTILGG
FQYFKCDHQRSVYLYLSSLRESCTITAYPCDSYQDYRNGKCVSCGTSQKESCPLLGYYAD
NWKDHLRGKDPPMTKAFFDTAEESPFCMYHYFVDIITWNKNVRRGDITIKLRDKAGNTTE
SKINHEPTTFQKYHQVSLLARFNQDLDKVAAISLMFSTGSLIGPRYKLRILRMKLRSLAH
PERPQLCRYDLVLMENVETVFQPILCPELQL
Enzyme 36 Number of Residues 451
Enzyme 36 Molecular Weight 50858.9
Enzyme 36 Theoretical pI 7.46
Enzyme 36 GO Classification
Function
  • catalytic activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 36 General Function Involved in catalytic activity
Enzyme 36 Specific Function Hydrolyzes specifically phosphatidic acid (PA) to produce lysophosphatidic acid (LPA)
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • 1-18
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 21245106 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q8WWY8 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name LIPH_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >1356 bp
ATGTTGAGATTCTACTTATTCATCAGTTTGTTGTGCTTGTCAAGATCAGACGCAGAAGAA
ACATGTCCTTCATTCACCAGGCTGAGCTTTCACAGTGCAGTGGTTGGTACGGGACTAAAT
GTGAGGCTGATGCTCTACACAAGGAAAAACCTGACCTGCGCACAAACCATCAACTCCTCA
GCTTTTGGGAACTTGAATGTGACCAAGAAAACCACCTTCATTGTCCATGGATTCAGGCCA
ACAGGCTCCCCTCCTGTTTGGATGGATGACTTAGTAAAGGGTTTGCTCTCTGTTGAAGAC
ATGAACGTAGTTGTTGTTGATTGGAATCGAGGAGCTACAACTTTAATATATACCCATGCC
TCTAGTAAGACCAGAAAAGTAGCCATGGTCTTGAAGGAATTTATTGACCAGATGTTGGCA
GAAGGAGCTTCTCTTGATGACATTTACATGATCGGAGTAAGTCTAGGAGCCCACATATCT
GGGTTTGTTGGAGAGATGTACGATGGATGGCTGGGGAGAATTACAGGCCTCGACCCTGCA
GGCCCTTTATTCAACGGGAAACCTCACCAAGACAGATTAGATCCCAGTGATGCGCAGTTT
GTTGATGTCATCCATTCCGACACTGATGCACTGGGCTACAAGGAGCCATTAGGAAACATA
GACTTCTACCCAAATGGAGGATTGGATCAACCTGGCTGCCCCAAAACAATATTGGGAGGA
TTTCAGTATTTTAAATGTGACCACCAGAGGTCTGTATACCTGTACCTGTCTTCCCTGAGA
GAGAGCTGCACCATCACTGCGTATCCCTGTGACTCCTACCAGGATTATAGGAATGGCAAG
TGTGTCAGCTGCGGCACGTCACAAAAAGAGTCCTGTCCCCTTCTGGGCTATTATGCTGAT
AATTGGAAAGACCATCTAAGGGGGAAAGATCCTCCAATGACGAAGGCATTCTTTGACACA
GCTGAGGAGAGCCCATTCTGCATGTATCATTACTTTGTGGATATTATAACATGGAACAAG
AATGTAAGAAGAGGGGACATTACCATCAAATTGAGAGACAAAGCTGGAAACACCACAGAA
TCCAAAATCAATCATGAACCCACCACATTTCAGAAATATCACCAAGTGAGTCTACTTGCA
AGATTTAATCAAGATCTGGATAAAGTGGCTGCAATTTCCTTGATGTTCTCTACAGGATCT
CTAATAGGCCCAAGGTACAAGCTCAGGATTCTCCGAATGAAGTTAAGGTCCCTTGCCCAT
CCGGAGAGGCCTCAGCTGTGTCGGTATGATCTTGTCCTGATGGAAAACGTTGAAACAGTC
TTCCAACCTATTCTTTGCCCAGAGTTGCAGTTGTAA
Enzyme 36 GenBank Gene ID NM_139248.2 Link Image
Enzyme 36 GeneCard ID LIPH Link Image
Enzyme 36 GenAtlas ID LIPH Link Image
Enzyme 36 HGNC ID HGNC:18483 Link Image
Enzyme 36 Chromosome Location 3
Enzyme 36 Locus 3q27
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H: A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid. J Biol Chem. 2002 Sep 13;277(37):34254-63. Epub 2002 Jun 12. [PubMed Link Image]
  2. 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]
  3. Kazantseva A, Goltsov A, Zinchenko R, Grigorenko AP, Abrukova AV, Moliaka YK, Kirillov AG, Guo Z, Lyle S, Ginter EK, Rogaev EI: Human hair growth deficiency is linked to a genetic defect in the phospholipase gene LIPH. Science. 2006 Nov 10;314(5801):982-5. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. 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]
  7. Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H: Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta. J Biol Chem. 2003 Dec 5;278(49):49438-47. Epub 2003 Sep 8. [PubMed Link Image]
  8. Naz G, Khan B, Ali G, Azeem Z, Wali A, Ansar M, Ahmad W: Novel missense mutations in lipase H (LIPH) gene causing autosomal recessive hypotrichosis (LAH2). J Dermatol Sci. 2009 Apr;54(1):12-6. Epub 2009 Jan 23. [PubMed Link Image]
  9. Shimomura Y, Wajid M, Petukhova L, Shapiro L, Christiano AM: Mutations in the lipase H gene underlie autosomal recessive woolly hair/hypotrichosis. J Invest Dermatol. 2009 Mar;129(3):622-8. Epub 2008 Oct 2. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 12940
Enzyme 37 Name Lipase member I
Enzyme 37 Synonyms
  1. Cancer/testis antigen 17
  2. CT17
  3. LPD lipase
  4. Membrane-associated phosphatidic acid-selective phospholipase A1-beta
  5. mPA-PLA1 beta
Enzyme 37 Gene Name LIPI
Enzyme 37 Protein Sequence >Lipase member I
MRVYIFLCLMCWVRSDNKRPCLEFSQLSVKDSFRDLFIPRIETILMMYTRNNLNCAEPLF
EQNNSLNVNFNTQKKTVWLIHGYRPVGSIPLWLQNFVRILLNEEDMNVIVVDWSRGATTF
IYNRAVKNTRKVAVSLSVHIKNLLKHGASLDNFHFIGVSLGAHISGFVGKIFHGQLGRIT
GLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSNGLGIQEPLGHIDFYPNGGNKQPGCPK
SIFSGIQFIKCNHQRAVHLFMASLETNCNFISFPCRSYKDYKTSLCVDCDCFKEKSCPRL
GYQAKLFKGVLKERMEGRPLRTTVFLDTSGTYPFCTYYFVLSIIVPDKTMMDGSFSFKLL
NQLGMIEEPRLYEKNKPFYKLQEVKILAQFYNDFVNISSIGLTYFQSSNLQCSTCTYKIQ
RLMLKSLTYPERPPLCRYNIVLKDREEVFLNPNTCTPKNT
Enzyme 37 Number of Residues 460
Enzyme 37 Molecular Weight 52991.0
Enzyme 37 Theoretical pI 9.28
Enzyme 37 GO Classification
Function
  • catalytic activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 37 General Function Involved in catalytic activity
Enzyme 37 Specific Function Hydrolyzes specifically phosphatidic acid (PA) to produce lysophosphatidic acid (LPA)
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions Not Available
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • 1-15
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 39752679 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q6XZB0 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name LIPI_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >1446 bp
ATGTTGCTCAAATGTTTACATAATAACTTGTGCCAAAAATATAGTGCTCATGCTTTTCAG
TTCTCACCCAGAAATGTCCTGTGGCTTCTAGTTGTGTGCCTGAGATCAGATAATAAAAGA
CCATGCCTTGAATTCTCTCAGCTAAGTGTAAAGGATTCCTTCAGAGATTTATTTATTCCG
AGAATAGAGACCATTCTGATGATGTATACAAGGAACAACCTAAACTGTGCTGAGCCACTG
TTTGAACAAAATAACTCACTTAATGTTAATTTCAACACACAAAAGAAAACAGTCTGGCTT
ATTCACGGATACAGACCAGTAGGCTCCATCCCATTATGGCTTCAGAACTTCGTAAGGATT
TTGCTGAATGAAGAAGATATGAATGTAATTGTAGTAGACTGGAGCCGGGGTGCTACAACT
TTTATTTATAATAGAGCAGTTAAAAACACCAGAAAAGTTGCTGTGAGTTTGAGTGTGCAC
ATTAAAAATCTTTTGAAGCATGGTGCATCTCTTGACAATTTTCATTTCATAGGTGTGAGC
TTAGGGGCTCATATCAGTGGATTTGTTGGAAAGATATTTCATGGTCAACTTGGAAGAATA
ACAGGTCTTGACCCTGCTGGGCCAAGGTTCTCCAGAAAACCACCATATAGCAGATTAGAT
TACACGGATGCAAAGTTTGTGGATGTCATCCATTCTGACTCCAATGGTTTAGGCATTCAA
GAGCCCTTGGGACATATAGATTTTTATCCAAATGGAGGAAATAAACAACCTGGCTGTCCT
AAATCAATTTTCTCAGGAATTCAATTCATTAAATGCAACCACCAGAGAGCAGTTCACTTG
TTCATGGCATCTTTAGAAACAAACTGCAATTTTATTTCATTTCCTTGTCGTTCATACAAA
GATTACAAGACTAGCTTATGTGTGGACTGTGACTGTTTTAAGGAAAAATCATGTCCTCGG
CTGGGTTATCAAGCCAAGCTATTTAAAGGTGTTTTAAAAGAAAGGATGGAAGGAAGACCT
CTTAGGACCACTGTGTTTTTGGATACAAGTGGTACATATCCATTCTGTACCTATTATTTT
GTTCTCAGTATAATTGTTCCAGATAAAACTATGATGGATGGCTCGTTTTCATTTAAATTA
TTAAATCAGCTTGGAATGATTGAAGAGCCAAGGCTTTATGAAAAGAACAAACCATTTTAT
AAACTTCAAGAAGTCAAGATTCTTGCTCAATTTTATAATGACTTTGTAAATATTTCAAGC
ATTGGTTTGACATATTTCCAGAGCTCAAATCTGCAGTGTTCCACATGCACATACAAGATC
CAGAGACTCATGTTAAAATCACTTACATACCCAGAAAGACCACCACTTTGCAGGTATAAT
ATTGTACTTAAAGACAGAGAGGAAGTGTTTCTTAATCCAAACACATGTACACCAAAGAAC
ACATAA
Enzyme 37 GenBank Gene ID Not Available
Enzyme 37 GeneCard ID LIPI Link Image
Enzyme 37 GenAtlas ID LIPI Link Image
Enzyme 37 HGNC ID HGNC:18821 Link Image
Enzyme 37 Chromosome Location 2
Enzyme 37 Locus 21q11.2
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H: Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta. J Biol Chem. 2003 Dec 5;278(49):49438-47. Epub 2003 Sep 8. [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]
  3. 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]
  4. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 12941
Enzyme 38 Name Lipid phosphate phosphatase-related protein type 4
Enzyme 38 Synonyms
  1. Brain-specific phosphatidic acid phosphatase-like protein 1
  2. Plasticity-related gene 1 protein
  3. PRG-1
Enzyme 38 Gene Name LPPR4
Enzyme 38 Protein Sequence >Lipid phosphate phosphatase-related protein type 4
MQRAGSSGGRGECDISGAGRLGLEEAARLSCAVHTSPGGGRRPGQAAGMSAKERPKGKVI
KDSVTLLPCFYFVELPILASSVVSLYFLELTDVFKPVHSGFSCYDRSLSMPYIEPTQEAI
PFLMLLSLAFAGPAITIMVGEGILYCCLSKRRNGVGLEPNINAGGCNFNSFLRRAVRFVG
VHVFGLCSTALITDIIQLSTGYQAPYFLTVCKPNYTSLNVSCKENSYIVEDICSGSDLTV
INSGRKSFPSQHATLAAFAAVYVSMYFNSTLTDSSKLLKPLLVFTFIICGIICGLTRITQ
YKNHPVDVYCGFLIGGGIALYLGLYAVGNFLPSDESMFQHRDALRSLTDLNQDPNRLLSA
KNGSSSDGIAHTEGILNRNHRDASSLTNLKRANADVEIITPRSPMGKENMVTFSNTLPRA
NTPSVEDPVRRNASIHASMDSARSKQLLTQWKNKNESRKLSLQVIEPEPGQSPPRSIEMR
SSSEPSRVGVNGDHHGPGNQYLKIQPGAVPGCNNSMPGGPRVSIQSRPGSSQLVHIPEET
QENISTSPKSSSARAKWLKAAEKTVACNRSNSQPRIMQVIAMSKQQGVLQSSPKNTEGST
VSCTGSIRYKTLTDHEPSGIVRVEAHPENNRPIIQIPSTEGEGSGSWKWKAPEKGSLRQT
YELNDLNRDSESCESLKDSFGSGDRKRSNIDSNEHHHHGITTIRVTPVEGSEIGSETLSI
SSSRDSTLRRKGNIILIPERSNSPENTRNIFYKGTSPTRAYKD
Enzyme 38 Number of Residues 763
Enzyme 38 Molecular Weight 82982.1
Enzyme 38 Theoretical pI 8.89
Enzyme 38 GO Classification
Function
  • catalytic activity
Process
Component
  • cell part
  • membrane
Enzyme 38 General Function Involved in catalytic activity
Enzyme 38 Specific Function Hydrolyzes lysophosphatidic acid (LPA). Facilitates axonal outgrowth during development and regenerative sprouting. In the outgrowing axons acts as an ecto-enzyme and attenuates phospholipid-induced axon collapse in neurons and facilitates outgrowth in the hippocampus
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions
  • a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate [RN:R02239]
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • 67-87 119-139 178-198 247-267 276-296 308-328
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 33636722 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID Q7Z2D5 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name LPPR4_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >2292 bp
ATGCAGCGCGCTGGCTCCAGCGGTGGCCGCGGGGAATGTGACATCAGCGGCGCCGGGCGC
TTGGGGCTGGAGGAGGCAGCTCGCCTCAGCTGCGCTGTGCACACCTCGCCCGGGGGAGGA
CGCAGACCCGGGCAGGCGGCAGGGATGTCGGCGAAGGAGAGGCCAAAGGGCAAAGTGATC
AAGGACAGCGTCACCCTCCTGCCCTGCTTTTATTTCGTCGAGTTGCCTATATTGGCATCA
TCGGTGGTTAGCCTCTATTTCCTCGAACTCACAGATGTCTTCAAACCTGTGCACTCTGGA
TTTAGCTGCTATGACCGGAGTCTTAGCATGCCGTACATTGAACCAACCCAGGAGGCAATT
CCATTCCTCATGTTGCTTAGCTTGGCTTTTGCTGGACCTGCAATTACGATTATGGTAGGA
GAAGGAATTCTCTACTGTTGCCTCTCCAAAAGAAGAAATGGGGTCGGACTAGAGCCCAAC
ATTAATGCTGGAGGCTGCAACTTCAATTCCTTCCTCAGACGAGCTGTCAGATTCGTTGGT
GTTCATGTATTTGGATTATGCTCTACAGCTCTCATTACAGATATCATACAGCTGTCCACA
GGATATCAAGCACCTTACTTTCTGACTGTGTGCAAACCAAACTATACCTCTCTGAATGTA
TCTTGCAAAGAAAATTCCTACATTGTGGAAGATATTTGCTCAGGATCTGACCTCACAGTT
ATCAACAGTGGCAGAAAGTCCTTCCCTTCTCAACATGCAACCCTTGCTGCCTTTGCAGCT
GTGTATGTTTCGATGTACTTCAATTCCACATTAACGGATTCCTCTAAGCTTCTGAAACCT
CTCTTGGTCTTCACATTTATCATCTGTGGAATAATCTGCGGGCTAACACGGATAACTCAG
TATAAGAACCACCCAGTTGATGTCTATTGTGGCTTTTTAATAGGAGGAGGAATTGCACTG
TACTTGGGCTTGTATGCTGTGGGGAATTTCCTGCCCAGTGATGAGAGTATGTTTCAGCAC
AGAGACGCCCTCAGGTCTCTGACAGACCTCAATCAAGATCCCAACCGACTTTTATCTGCT
AAAAATGGTAGCAGCAGTGATGGAATTGCTCATACAGAAGGCATCCTCAACCGAAACCAC
AGAGATGCTAGCTCTCTGACAAATCTCAAAAGAGCAAATGCTGATGTGGAAATCATTACT
CCACGGAGCCCCATGGGGAAGGAGAACATGGTTACCTTCAGCAATACCTTGCCGCGAGCC
AATACCCCATCTGTAGAAGACCCTGTCAGAAGAAATGCGAGCATTCATGCCTCTATGGAT
TCCGCTCGATCAAAGCAGCTCCTCACCCAGTGGAAGAATAAGAATGAAAGTCGAAAGTTG
TCCTTGCAAGTTATAGAGCCTGAGCCTGGGCAGTCACCACCCAGATCCATAGAAATGAGG
TCAAGCTCAGAGCCATCGAGGGTAGGGGTGAATGGAGACCACCATGGTCCTGGCAATCAG
TACCTCAAAATCCAGCCTGGCGCTGTCCCCGGATGTAACAACAGCATGCCTGGAGGGCCA
AGAGTGTCCATTCAGTCCCGTCCTGGGTCCTCACAGTTGGTGCACATCCCTGAGGAGACT
CAGGAAAACATAAGCACCTCCCCCAAAAGCAGCTCTGCTCGGGCCAAGTGGTTAAAAGCT
GCTGAAAAGACTGTGGCCTGTAACAGAAGCAACAGCCAGCCCCGAATCATGCAAGTCATA
GCCATGTCCAAGCAGCAGGGTGTCCTCCAAAGCAGCCCCAAGAACACTGAAGGCAGCACG
GTCTCCTGCACTGGCTCCATCCGCTATAAAACCTTGACAGACCATGAGCCCAGTGGGATA
GTGAGGGTTGAGGCTCACCCAGAGAACAACAGGCCCATCATACAGATCCCGTCCACTGAA
GGTGAAGGCAGTGGCTCCTGGAAGTGGAAAGCCCCTGAAAAGGGCAGCCTTCGCCAAACT
TACGAGCTCAACGATCTCAACAGGGACTCAGAAAGCTGTGAGTCTCTGAAAGACAGCTTT
GGTTCTGGAGATCGCAAGAGAAGCAACATTGATAGCAATGAGCATCACCACCACGGAATT
ACCACCATCCGCGTCACCCCAGTAGAGGGCAGCGAAATTGGCTCAGAGACGCTGTCCATT
TCTTCTTCCCGCGACTCCACCCTGCGGAGAAAGGGCAATATCATTCTAATCCCTGAAAGA
AGCAACAGCCCCGAAAACACTAGAAATATCTTCTACAAAGGAACCTCCCCCACACGGGCT
TATAAGGATTGA
Enzyme 38 GenBank Gene ID NM_014839.4 Link Image
Enzyme 38 GeneCard ID LPPR4 Link Image
Enzyme 38 GenAtlas ID Not Available
Enzyme 38 HGNC ID Not Available
Enzyme 38 Chromosome Location 1
Enzyme 38 Locus 1p21.2
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 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]
  2. Seki N, Ohira M, Nagase T, Ishikawa K, Miyajima N, Nakajima D, Nomura N, Ohara O: Characterization of cDNA clones in size-fractionated cDNA libraries from human brain. DNA Res. 1997 Oct 31;4(5):345-9. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 14426
Enzyme 39 Name Acylglycerol kinase, mitochondrial
Enzyme 39 Synonyms
  1. hAGK
  2. Multiple substrate lipid kinase
  3. HsMuLK
  4. MuLK
  5. Multi-substrate lipid kinase
Enzyme 39 Gene Name AGK
Enzyme 39 Protein Sequence >Acylglycerol kinase, mitochondrial
MTVFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQV
KKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTIVKTDYEGQAKKLLELMENTDVII
VAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATL
AIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFST
LKEWPQTHQASISYTGPTERPPNEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSP
EVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHV
EGTECLQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSP
TQ
Enzyme 39 Number of Residues 422
Enzyme 39 Molecular Weight 47136.8
Enzyme 39 Theoretical pI 8.21
Enzyme 39 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
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 39 General Function Involved in NAD+ kinase activity
Enzyme 39 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 39 Pathways
Enzyme 39 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 8922701 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q53H12 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name AGK_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 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 39 GenBank Gene ID NM_018238.3 Link Image
Enzyme 39 GeneCard ID AGK Link Image
Enzyme 39 GenAtlas ID AGK Link Image
Enzyme 39 HGNC ID HGNC:21869 Link Image
Enzyme 39 Chromosome Location 7
Enzyme 39 Locus 7q34
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Van Overloop H, Gijsbers S, Van Veldhoven PP: Further characterization of mammalian ceramide kinase: substrate delivery and (stereo)specificity, tissue distribution, and subcellular localization studies. J Lipid Res. 2006 Feb;47(2):268-83. Epub 2005 Nov 3. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. 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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Bektas M, Payne SG, Liu H, Goparaju S, Milstien S, Spiegel S: A novel acylglycerol kinase that produces lysophosphatidic acid modulates cross talk with EGFR in prostate cancer cells. J Cell Biol. 2005 Jun 6;169(5):801-11. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 15207
Enzyme 40 Name Phospholipase D1 variant
Enzyme 40 Synonyms Not Available
Enzyme 40 Gene Name Not Available
Enzyme 40 Protein Sequence >Phospholipase D1 variant
ANAQVLAAPSPCSPFAFTLSKVNMSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEG
EEVDYDVSPSDPKIQEVYIPFSAIYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRV
PSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEP
REMPSLPRSSENMIREEQFLGRRKQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDL
GPKGIEGMIMKRSGGHRIPGLNCCGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLL
VDKEFKIKVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKD
HRFGSYAAIQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGN
RWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSST
VYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAM
ESMESLRLKDKNEPVQNLPIQKSIDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSI
SSIDSTSNTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPR
MPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLLPKSQTTAHELRYQVP
GSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFN
KIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGEN
SILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANIN
DRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCFRVVLGYLDDPSEDIQ
DPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPVLAKEDPIRAEE
ELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
Enzyme 40 Number of Residues 1059
Enzyme 40 Molecular Weight 122007.8
Enzyme 40 Theoretical pI 9.03
Enzyme 40 GO Classification
Function
  • binding
  • catalytic activity
  • lipid binding
  • phosphoinositide binding
  • phospholipid binding
  • protein binding
Process
  • cell communication
  • cellular process
  • metabolic process
Component
Enzyme 40 General Function Involved in protein binding
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 62089400 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID Q59EA4 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name Q59EA4_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 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 40 GenBank Gene ID AB209907 Link Image
Enzyme 40 GeneCard ID Not Available
Enzyme 40 GenAtlas ID Not Available
Enzyme 40 HGNC ID HGNC:9067 Link Image
Enzyme 40 Chromosome Location Not Available
Enzyme 40 Locus Not Available
Enzyme 40 SNPs Not Available
Enzyme 40 General References Not Available
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 15287
Enzyme 41 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 41 Synonyms Not Available
Enzyme 41 Gene Name AGPAT1
Enzyme 41 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 41 Number of Residues 283
Enzyme 41 Molecular Weight 31717
Enzyme 41 Theoretical pI 9.75
Enzyme 41 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 41 General Function Lipid transport and metabolism
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 123209920 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID A2BFI5 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name A2BFI5_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >852 bp
ATGGATTTGTGGCCAGGGGCATGGATGCTGCTGCTGCTGCTCTTCCTGCTGCTGCTCTTC
CTGCTGCCCACCCTGTGGTTCTGCAGCCCCAGTGCCAAGTACTTCTTCAAGATGGCCTTC
TACAATGGCTGGATCCTCTTCCTGGCTGTGCTCGCCATCCCTGTGTGTGCCGTGCGAGGA
CGCAACGTCGAGAACATGAAGATCTTGCGTCTAATGCTGCTCCACATCAAATACCTGTAC
GGGATCCGAGTGGAGGTGCGAGGGGCTCACCACTTCCCTCCCTCGCAGCCCTATGTTGTT
GTCTCCAACCACCAGAGCTCTCTCGATCTGCTTGGGATGATGGAGGTACTGCCAGGCCGC
TGTGTGCCCATTGCCAAGCGCGAGCTACTGTGGGCTGGCTCTGCCGGGCTGGCCTGCTGG
CTGGCAGGAGTCATCTTCATCGACCGGAAGCGCACGGGGGATGCCATCAGTGTCATGTCT
GAGGTCGCCCAGACCCTGCTCACCCAGGACGTGAGGGTCTGGGTGTTTCCTGAGGGAACG
AGAAACCACAATGGCTCCATGCTGCCCTTCAAACGTGGCGCCTTCCATCTTGCAGTGCAG
GCCCAGGTTCCCATTGTCCCCATAGTCATGTCCTCCTACCAAGACTTCTACTGCAAGAAG
GAGCGTCGCTTCACCTCGGGACAATGTCAGGTGCGGGTGCTGCCCCCAGTGCCCACGGAA
GGGCTGACACCAGATGACGTCCCAGCTCTGGCTGACAGAGTCCGGCACTCCATGCTCACT
GTTTTCCGGGAAATCTCCACTGATGGCCGGGGTGGTGGTGACTATCTGAAGAAGCCTGGG
GGCGGTGGGTGA
Enzyme 41 GenBank Gene ID BX284686 Link Image
Enzyme 41 GeneCard ID A2BFI5 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 Not Available
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 15288
Enzyme 42 Name 1-acylglycerol-3-phosphate O-acyltransferase 6 (Lysophosphatidic acid acyltransferase, zeta), isoform CRA_b
Enzyme 42 Synonyms
  1. SubName: Testis spermatogenesis apoptosis-related protein 7
Enzyme 42 Gene Name AGPAT6
Enzyme 42 Protein Sequence >1-acylglycerol-3-phosphate O-acyltransferase 6 (Lysophosphatidic acid acyltransferase, zeta), isoform CRA_b
MFLLLPFDSLIVNLLGISLTVLFTLLLVFIIVPAIFGVSFGIRKLYMKSLLKIFAWATLR
MERGAKEKNHQLYKPYTNGIIAKDPTSLEEEIKEIRRSGSSKALDNTPEFELSDIFYFCR
KGMETIMDDEVTKRFSAEELESWNLLSRTNYNFQYISLRLTVLWGLGVLIRYCFLLPLRI
ALAFTGISLLVVGTTVVGYLPNGRFKEFMSKHVHLMCYRICVRALTAIITYHDRENRPRN
GGICVANHTSPIDVIILASDGYYAMVGQVHGGLMGVIQRAMVKACPHVWFERSEVKDRHL
VAKRLTEHVQDKSKLPILIFPEGTCINNTSVMMFKKGSFEIGATVYPVAIKYDPQFGDAF
WNSSKYGMVTYLLRMMTSWAIVCSVWYLPPMTREADEDAVQFANRVKSAIARQGGLVDLL
WDGGLKREKVKDTFKEEQQKLYSKMIVGNHKDRSRS
Enzyme 42 Number of Residues 456
Enzyme 42 Molecular Weight 52070.6
Enzyme 42 Theoretical pI 9.56
Enzyme 42 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 42 General Function Involved in acyltransferase activity
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 46241188 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q2TU73 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name Q2TU73_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 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 42 GenBank Gene ID AY513610 Link Image
Enzyme 42 GeneCard ID AGPAT6 Link Image
Enzyme 42 GenAtlas ID AGPAT6 Link Image
Enzyme 42 HGNC ID HGNC:20880 Link Image
Enzyme 42 Chromosome Location 8
Enzyme 42 Locus 8p11.21
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Tan XJ, Huang ZP, Li LY, Nie DS, Zhong CG, Fu JJ, Lu GX: Molecular cloning and preliminary function study of a novel human gene, TSARG7, related to spermatogenesis. Yi Chuan Xue Bao. 2006 Apr;33(4):294-303. [PubMed Link Image]
  2. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 15289
Enzyme 43 Name Lysocardiolipin acyltransferase 1
Enzyme 43 Synonyms
  1. SubName: Putative uncharacterized protein LCLAT1
Enzyme 43 Gene Name LCLAT1
Enzyme 43 Protein Sequence >Lysocardiolipin acyltransferase 1
MVSWKGIYFILTLFWGSFFGSIFMLSPFLPLMFVNPSWYRWINNRLVATWLTLPVALLET
MFGVKVIITGDAFVPGERSVIIMNHRTRMDWMFLWNCLMRYSYLRLEKICLKASLKGVPG
FGWAMQAAAYIFIHRKWKDDKSHFEDMIDYFCDIHEPLQLLIFPEGTDLTENSKSRSNAF
AEKNGLQKYEYVLHPRTTGFTFVVDRLREGKNLDAVHDITVAYPHNIPQSEKHLLQGDFP
REIHFHVHRYPIDTLPTSKEDLQLWCHKRWEEKEERLRSFYQGEKNFYFTGQSVIPPCKS
ELRVLVVKLLSILYWTLFSPAMCLLIYLYSLVKWYFIITIVIFVLQERIFGGLEIIELAC
YRLLHKQPHLNSKKNE
Enzyme 43 Number of Residues 376
Enzyme 43 Molecular Weight 44560.8
Enzyme 43 Theoretical pI 8.76
Enzyme 43 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 43 General Function Involved in acyltransferase activity
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 50659059 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID A6H8Z7 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name A6H8Z7_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >1131 bp
ATGGTGTCATGGAAAGGGATTTACTTTATACTGACTCTGTTTTGGGGAAGCTTTTTTGGA
AGCATTTTCATGCTGAGTCCCTTTTTACCTTTGATGTTTGTAAACCCATCTTGGTATCGC
TGGATCAACAACCGCCTTGTGGCAACATGGCTCACCCTACCTGTGGCATTATTGGAGACC
ATGTTTGGTGTAAAAGTGATTATAACTGGGGATGCATTTGTTCCTGGAGAAAGAAGTGTC
ATTATCATGAACCATCGGACAAGAATGGACTGGATGTTCCTGTGGAATTGCCTGATGCGA
TATAGCTACCTCAGATTGGAGAAAATTTGCCTCAAAGCGAGTCTCAAAGGTGTTCCTGGA
TTTGGTTGGGCCATGCAGGCTGCTGCCTATATCTTCATTCATAGGAAATGGAAGGATGAC
AAGAGCCATTTCGAAGACATGATTGATTACTTTTGTGATATTCACGAACCACTTCAACTC
CTCATATTCCCAGAAGGGACTGATCTCACAGAAAACAGCAAGTCTCGAAGTAATGCATTT
GCTGAAAAAAATGGACTTCAGAAATATGAATATGTTTTACATCCAAGAACTACAGGCTTT
ACTTTTGTGGTAGACCGTCTAAGAGAAGGTAAGAACCTTGATGCTGTCCATGATATCACT
GTGGCGTATCCTCACAACATTCCTCAATCAGAGAAGCACCTCCTCCAAGGAGACTTTCCC
AGGGAAATCCACTTTCACGTCCACCGGTATCCAATAGACACCCTCCCCACATCCAAGGAG
GACCTTCAACTCTGGTGCCACAAACGGTGGGAAGAGAAAGAAGAGAGGCTGCGTTCCTTC
TATCAAGGGGAGAAGAATTTTTATTTTACCGGACAGAGTGTCATTCCACCTTGCAAGTCT
GAACTCAGGGTCCTTGTGGTCAAATTGCTCTCTATACTGTATTGGACCCTGTTCAGCCCT
GCAATGTGCCTACTCATATATTTGTACAGTCTTGTTAAGTGGTATTTTATAATCACCATT
GTAATCTTTGTGCTGCAAGAGAGAATATTTGGTGGACTGGAGATCATAGAACTTGCATGT
TACCGACTTTTACACAAACAGCCACATTTAAATTCAAAGAAAAATGAGTAA
Enzyme 43 GenBank Gene ID NM_001002257.1 Link Image
Enzyme 43 GeneCard ID LCLAT1 Link Image
Enzyme 43 GenAtlas ID LCLAT1 Link Image
Enzyme 43 HGNC ID HGNC:26756 Link Image
Enzyme 43 Chromosome Location 2
Enzyme 43 Locus 2p23.1
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 15290
Enzyme 44 Name Diacylglycerol kinase, beta 90kDa (Diacylglycerol kinase, beta 90kDa, isoform CRA_b)
Enzyme 44 Synonyms Not Available
Enzyme 44 Gene Name DGKB
Enzyme 44 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 44 Number of Residues 804
Enzyme 44 Molecular Weight 90596
Enzyme 44 Theoretical pI 7.90
Enzyme 44 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 44 General Function Not Available
Enzyme 44 Specific Function Not Available
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions Not Available
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein Not Available
Enzyme 44 UniProtKB/Swiss-Prot ID A4D116 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name A4D116_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 CH236948 Link Image
Enzyme 44 GeneCard ID A4D116 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
  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 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 15291
Enzyme 45 Name Diacylglycerol kinase, theta 110kDa
Enzyme 45 Synonyms Not Available
Enzyme 45 Gene Name DGKQ
Enzyme 45 Protein Sequence >Diacylglycerol kinase, theta 110kDa
MAAAAEPGARAWLGGGSPRPGSPACSLVLGSGGRARPGPGPGPGPERAGVRAPGPAAAPG
HSFRKVTLTKPTFCHLCSDFIWGLAGFLCDVCNFMSHEKCLKHVRIPCTSVAPSLVRVPV
AHCFGPRGLHKRKFCAVCRKVLEAPALHCEVCELHLHPDCVPFACSDCRQCHQDGHQDHD
THHHHWREGNLPSGARCEVCRKTCGSSDVLAGVRCEWCGVQAHSLCSAALAPECGFGRLR
SLVLPPACVRLLPGGFSKTQSFRIVEAAEPGEGGDGADGSAAVGPGRETQATPESGKQTL
KIFDGDDAVRRSQFRLVTVSRLAGAEEVLEAALRAHHIPEDPGHLELCRLPPSSQACDAW
AGGKAGSAVISEEGRSPGSGEATPEAWVIRALPRAQEVLKIYPGWLKVGVAYVSVRVTPK
STARSVVLEVLPLLGRQAESPESFQLVEVAMGCRHVQRTMLMDEQPLLDRLQDIRQMSVR
QVSQTRFYVAESRDVAPHVSLFVGGLPPGLSPEEYSSLLHEAGATKATVVSVSHIYSSQG
AVVLDVACFAEAERLYMLLKDMAVRGRLLTALVLPDLLHAKLPPDSCPLLVFVNPKSGGL
KGRDLLCSFRKLLNPHQVFDLTNGGPLPGLHLFSQVPCFRVLVCGGDGTVGWVLGALEET
RYRLACPEPSVAILPLGTGNDLGRVLRWGAGYSGEDPFSVLLSVDEADAVLMDRWTILLD
AHEAGSAENDTADAEPPKIVQMSNYCGIGIDAELSLDFHQAREEEPGKFTSRLHNKGVYV
RVGLQKISHSRSLHKQIRLQVERQEVELPSIEGLIFINIPSWGSGADLWGSDSDTRFEKP
RMDDGLLEVVGVTGVVHMGQVQGGLRSGIRIAQGSYFRVTLLKATPVQVDGEPWVQAPGH
MIISAAGPKVHMLRKAKQKPRRAGTTRDARADAAPAPESDPR
Enzyme 45 Number of Residues 942
Enzyme 45 Molecular Weight 101172
Enzyme 45 Theoretical pI 7.50
Enzyme 45 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 45 General Function Not Available
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 39645110 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID Q6P3W4 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name Q6P3W4_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 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 45 GenBank Gene ID BC063801 Link Image
Enzyme 45 GeneCard ID Q6P3W4 Link Image
Enzyme 45 GenAtlas ID DGKQ Link Image
Enzyme 45 HGNC ID HGNC:2856 Link Image
Enzyme 45 Chromosome Location Not Available
Enzyme 45 Locus Not Available
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 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 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 15292
Enzyme 46 Name Diacylglycerol kinase, epsilon 64kDa
Enzyme 46 Synonyms
  1. SubName: cDNA FLJ75840, highly similar to Homo sapiens diacylglycerol kinase, epsilon 64kDa (DGKE), mRNA
Enzyme 46 Gene Name DGKE
Enzyme 46 Protein Sequence >Diacylglycerol kinase, epsilon 64kDa
MEAERRPAPGSPSEGLFADGHLILWTLCSVLLPVFITFWCSLQRSRRQLHRRDIFRKSKH
GWRDTDLFSQPTYCCVCAQHILQGAFCDCCGLRVDEGCLRKADKRFQCKEIMLKNDTKVL
DAMPHHWIRGNVPLCSYCMVCKQQCGCQPKLCDYRCIWCQKTVHDECMKNSLKNEKCDFG
EFKNLIIPPSYLTSINQMRKDKKTDYEVLASKLGKQWTPLIILANSRSGTNMGEGLLGEF
RILLNPVQVFDVTKTPPIKALQLCTLLPYYSARVLVCGGDGTVGWVLDAVDDMKIKGQEK
YIPQVAVLPLGTGNDLSNTLGWGTGYAGEIPVAQVLRNVMEADGIKLDRWKVQVTNKGYY
NLRKPKEFTMNNYFSVGPDALMALNFHAHREKAPSLFSSRILNKAVYLFYGTKDCLVQEC
KDLNKKVELELDGERVALPSLEGIIVLNIGYWGGGCRLWEGMGDETYPLARHDDGLLEVV
GVYGSFHCAQIQVKLANPFRIGQAHTVRLILKCSMMPMQVDGEPWAQGPCTVTITHKTHA
MMLYFSGEQTDDDISSTSDQEDIKATE
Enzyme 46 Number of Residues 567
Enzyme 46 Molecular Weight 63926.6
Enzyme 46 Theoretical pI 7.78
Enzyme 46 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
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 46 General Function Involved in diacylglycerol kinase activity
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 158259539 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID A1L4Q0 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name A1L4Q0_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 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 46 GenBank Gene ID AK293039 Link Image
Enzyme 46 GeneCard ID DGKE Link Image
Enzyme 46 GenAtlas ID DGKE Link Image
Enzyme 46 HGNC ID HGNC:2852 Link Image
Enzyme 46 Chromosome Location 1
Enzyme 46 Locus 17q22
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 16477
Enzyme 47 Name cDNA, FLJ94990, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 1 (CDS1), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 1, isoform CRA_a)
Enzyme 47 Synonyms Not Available
Enzyme 47 Gene Name CDS1
Enzyme 47 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 47 Number of Residues 461
Enzyme 47 Molecular Weight 53305
Enzyme 47 Theoretical pI 8.19
Enzyme 47 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 47 General Function Lipid transport and metabolism
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 B2RAL5 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name B2RAL5_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 AK314245 Link Image
Enzyme 47 GeneCard ID B2RAL5 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 16478
Enzyme 48 Name cDNA, FLJ96552, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 2 (CDS2), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 2, isoform CRA_a)
Enzyme 48 Synonyms Not Available
Enzyme 48 Gene Name CDS2
Enzyme 48 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 48 Number of Residues 445
Enzyme 48 Molecular Weight 51419
Enzyme 48 Theoretical pI 7.10
Enzyme 48 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 48 General Function Lipid transport and metabolism
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 B2RDC6 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name B2RDC6_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 AK315489 Link Image
Enzyme 48 GeneCard ID B2RDC6 Link Image
Enzyme 48 GenAtlas ID Not Available
Enzyme 48 HGNC ID Not Available
Enzyme 48 Chromosome Location 20
Enzyme 48 Locus 20p13
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References Not Available
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 16543
Enzyme 49 Name cDNA, FLJ92787, highly similar to Homo sapiens phosphatidic acid phosphatase type 2B (PPAP2B), mRNA (Phosphatidic acid phosphatase type 2B, isoform CRA_a)
Enzyme 49 Synonyms Not Available
Enzyme 49 Gene Name PPAP2B
Enzyme 49 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 49 Number of Residues 311
Enzyme 49 Molecular Weight 35116
Enzyme 49 Theoretical pI 9.40
Enzyme 49 GO Classification Not Available
Enzyme 49 General Function Lipid transport and metabolism
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 B2R651 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name B2R651_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 AK312439 Link Image
Enzyme 49 GeneCard ID B2R651 Link Image
Enzyme 49 GenAtlas ID Not Available
Enzyme 49 HGNC ID Not Available
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 17294
Enzyme 50 Name Lysophosphatidic acid receptor 1
Enzyme 50 Synonyms Not Available
Enzyme 50 Gene Name LPAR1
Enzyme 50 Protein Sequence >Lysophosphatidic acid receptor 1
MAAISTSIPVISQPQFTAMNEPQCFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITVC
IFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVST
WLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMGA
IP
Enzyme 50 Number of Residues 182
Enzyme 50 Molecular Weight 20564.3
Enzyme 50 Theoretical pI 10.14
Enzyme 50 GO Classification
Function
  • G-protein coupled receptor activity
  • bioactive lipid receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 50 General Function Involved in G-protein coupled receptor protein signaling pathway
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 55959842 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID B1AP63 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name B1AP63_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >546 bp
ATGGCTGCCATCTCTACTTCCATCCCTGTAATTTCACAGCCCCAGTTCACAGCCATGAAT
GAACCACAGTGCTTCTACAACGAGTCCATTGCCTTCTTTTATAACCGAAGTGGAAAGCAT
CTTGCCACAGAATGGAACACAGTCAGCAAGCTGGTGATGGGACTTGGAATCACTGTTTGT
ATCTTCATCATGTTGGCCAACCTATTGGTCATGGTGGCAATCTATGTCAACCGCCGCTTC
CATTTTCCTATTTATTACCTAATGGCTAATCTGGCTGCTGCAGACTTCTTTGCTGGGTTG
GCCTACTTCTATCTCATGTTCAACACAGGACCCAATACTCGGAGACTGACTGTTAGCACA
TGGCTCCTTCGTCAGGGCCTCATTGACACCAGCCTGACGGCATCTGTGGCCAACTTACTG
GCTATTGCAATCGAGAGGCACATTACGGTTTTCCGCATGCAGCTCCACACACGGATGAGC
AACCGGCGGGTAGTGGTGGTCATTGTGGTCATCTGGACTATGGCCATCGTTATGGGTGCT
ATACCC
Enzyme 50 GenBank Gene ID AL442064 Link Image
Enzyme 50 GeneCard ID LPAR1 Link Image
Enzyme 50 GenAtlas ID LPAR1 Link Image
Enzyme 50 HGNC ID HGNC:3166 Link Image
Enzyme 50 Chromosome Location 9
Enzyme 50 Locus 9q31.3
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References Not Available
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 17295
Enzyme 51 Name High-affinity lysophosphatidic acid receptor homolog
Enzyme 51 Synonyms Not Available
Enzyme 51 Gene Name Not Available
Enzyme 51 Protein Sequence >High-affinity lysophosphatidic acid receptor homolog
MACNSTSLEAYTYLLLNTSNASDSGSTQLPAPLRISLAIVMLLMTVVGFLGNTVVCIIVY
QRPAMRSAINLLLATLAFSDIMLSLCCMPFTAVTLITVRWHFGDHFCRLSATLYWFFVLE
GVAILLIISVDRFLIIVQRQDKLNPRRAKVIIAVSWVLSWVLSFCIAGPSLTGWTLVEVP
ARAPQCVLGYTELPADRAYVVTLVVAVFFAPFGVMLCAYMCILNTVRKNAVRVHNQSDSL
DLRQLTRAGLRRLQRQQQVSVDLSFKTKAFTTILILFVGFSLCWLPHSVYSLLSVFSQRF
YCGSSFYATSTCVLWLSYLKSVFNPIVYCWRIKKFREACIELLPQTFQILPKVPERIRRR
IQPSTVYCCNENQSAV
Enzyme 51 Number of Residues 376
Enzyme 51 Molecular Weight 42455.9
Enzyme 51 Theoretical pI 9.33
Enzyme 51 GO Classification
Function
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 51 General Function Involved in G-protein coupled receptor protein signaling pathway
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 2735351 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID O43898 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name O43898_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >1131 bp
ATGGCCTGCAACAGCACGTCCCTTGAGGCTTACACATACCTGCTGCTGAACACCAGCAAC
GCCTCAGACTCGGGGTCCACCCAGTTGCCCGCACCCCTCAGGATCTCCTTGGCCATAGTG
ATGCTGCTGATGACCGTGGTGGGGTTCCTGGGCAACACTGTGGTCTGCATCATCGTGTAC
CAGAGGCCGGCTATGCGCTCGGCCATCAACCTGCTGCTGGCCACCCTGGCCTTCTCCGAC
ATCATGCTGTCCCTCTGCTGCATGCCCTTCACCGCCGTCACCCTCATCACCGTGCGCTGG
CACTTTGGGGACCACTTCTGCCGCCTCTCAGCCACGCTCTACTGGTTTTTTGTCCTGGAG
GGCGTGGCCATCCTGCTCATCATCAGCGTGGACCGCTTCCTCATCATCGTCCAGCGCCAG
GACAAGCTGAACCCGCGCAGGGCCAAGGTGATCATCGCGGTCTCCTGGGTGCTGTCCTGG
GTGCTGTCCTTCTGCATCGCGGGGCCCTCGCTCACGGGCTGGACGCTGGTGGAGGTGCCG
GCGCGGGCCCCACAGTGCGTGCTGGGCTACACGGAGCTCCCCGCTGACCGCGCCTACGTG
GTCACCTTGGTGGTGGCCGTGTTCTTCGCGCCCTTTGGCGTCATGCTGTGCGCCTACATG
TGCATCCTCAACACGGTCCGCAAGAACGCCGTGCGCGTGCACAACCAGTCGGACAGCCTG
GACCTGCGGCAGCTCACCAGGGCGGGCCTGCGGCGCCTGCAGCGGCAGCAACAGGTCAGC
GTGGACTTGAGCTTCAAGACCAAGGCCTTCACCACCATCCTGATCCTCTTCGTGGGCTTC
TCCCTCTGCTGGCTGCCCCACTCCGTCTACAGCCTCCTGTCTGTGTTTAGCCAGCGCTTT
TACTGCGGTTCCTCCTTCTACGCCACCAGCACCTGCGTCCTGTGGCTCAGTTACCTCAAG
TCCGTCTTCAACCCCATCGTCTACTGCTGGAGAATCAAAAAATTCCGCGAGGCCTGCATA
GAGTTGCTGCCCCAGACCTTCCAAATCCTCCCCAAAGTGCCTGAGCGGATCCGAAGGAGA
ATCCAGCCAAGCACAGTCTACTGTTGCAATGAAAACCAGTCTGCGGTTTAG
Enzyme 51 GenBank Gene ID U92642 Link Image
Enzyme 51 GeneCard ID Not Available
Enzyme 51 GenAtlas ID Not Available
Enzyme 51 HGNC ID HGNC:4503 Link Image
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 17296
Enzyme 52 Name LPAR1 protein
Enzyme 52 Synonyms
  1. SubName: cDNA FLJ51746, highly similar to Lysophosphatidic acid receptor Edg-2
Enzyme 52 Gene Name LPAR1
Enzyme 52 Protein Sequence >LPAR1 protein
MNEPQCFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITVCIFIMLANLLVMVAIYVNR
RFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVSTWLLRQGLIDTSLTASVAN
LLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMGAIPSVGWNCICDIENCSNM
APLYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRMSRHSSGPRRNRDTMMSLLK
TVVIVLGAFIICWTPGLVLLLLDVCCPQCDVLAYEKFFLLLAEFNSAMNPIIYSYRDKEM
SATFRQILCCQRSENPTGPTEGSDRSASSLNHTILAGVHSNDHSVV
Enzyme 52 Number of Residues 346
Enzyme 52 Molecular Weight 39264.8
Enzyme 52 Theoretical pI 8.60
Enzyme 52 GO Classification
Function
  • G-protein coupled receptor activity
  • bioactive lipid receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 52 General Function Involved in G-protein coupled receptor protein signaling pathway
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 194387766 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID Q6GPG7 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name Q6GPG7_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >1041 bp
ATGAATGAACCACAGTGCTTCTACAACGAGTCCATTGCCTTCTTTTATAACCGAAGTGGA
AAGCATCTTGCCACAGAATGGAACACAGTCAGCAAGCTGGTGATGGGACTTGGAATCACT
GTTTGTATCTTCATCATGTTGGCCAACCTATTGGTCATGGTGGCAATCTATGTCAACCGC
CGCTTCCATTTTCCTATTTATTACCTAATGGCTAATCTGGCTGCTGCAGACTTCTTTGCT
GGGTTGGCCTACTTCTATCTCATGTTCAACACAGGACCCAATACTCGGAGACTGACTGTT
AGCACATGGCTCCTTCGTCAGGGCCTCATTGACACCAGCCTGACGGCATCTGTGGCCAAC
TTACTGGCTATTGCAATCGAGAGGCACATTACGGTTTTCCGCATGCAGCTCCACACACGG
ATGAGCAACCGGCGGGTAGTGGTGGTCATTGTGGTCATCTGGACTATGGCCATCGTTATG
GGTGCTATACCCAGTGTGGGCTGGAACTGTATCTGTGATATTGAAAATTGTTCCAACATG
GCACCCCTCTACAGTGACTCTTACTTAGTCTTCTGGGCCATTTTCAACTTGGTGACCTTT
GTGGTAATGGTGGTTCTCTATGCTCACATCTTTGGCTATGTTCGCCAGAGGACTATGAGA
ATGTCTCGGCATAGTTCTGGACCCCGGCGGAATCGGGATACCATGATGAGTCTTCTGAAG
ACTGTGGTCATTGTGCTTGGGGCCTTTATCATCTGCTGGACTCCTGGATTGGTTTTGTTA
CTTCTAGACGTGTGCTGTCCACAGTGCGACGTGCTGGCCTATGAGAAATTCTTCCTTCTC
CTTGCTGAATTCAACTCTGCCATGAACCCCATCATTTACTCCTACCGCGACAAAGAAATG
AGCGCCACCTTTAGGCAGATCCTCTGCTGCCAGCGCAGTGAGAACCCCACCGGCCCCACA
GAAGGCTCAGACCGCTCGGCTTCCTCCCTCAACCACACCATCTTGGCTGGAGTTCACAGC
AATGACCACTCTGTGGTTTAG
Enzyme 52 GenBank Gene ID AK299279 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 9
Enzyme 52 Locus 9q31.3
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 17297
Enzyme 53 Name cDNA FLJ61127, highly similar to Lysophosphatidic acid receptor Edg-2
Enzyme 53 Synonyms Not Available
Enzyme 53 Gene Name Not Available
Enzyme 53 Protein Sequence >cDNA FLJ61127, highly similar to Lysophosphatidic acid receptor Edg-2
MLLLLIPAHSSVLENEFTAMNEPQCFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITV
CIFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVS
TWLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMG
AIPSVGWNCICDIENCSNMAPLYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRM
SRHSSGPRRNRDTMMSLLKTVVIVLGAFIICWTPGLVLLLLDVCCPQCDVLAYEKFFLLL
AEFNSAMNPIIYSYRDKEMSATFRQILCCQRSENPTGPTEGSDRSASSLNHTILAGVHSN
DHSVV
Enzyme 53 Number of Residues 365
Enzyme 53 Molecular Weight 41345.3
Enzyme 53 Theoretical pI 8.34
Enzyme 53 GO Classification
Function
  • G-protein coupled receptor activity
  • bioactive lipid receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 53 General Function Involved in G-protein coupled receptor protein signaling pathway
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 194382984 Link Image
Enzyme 53 UniProtKB/Swiss-Prot ID B4DK36 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name B4DK36_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence >1098 bp
ATGCTGCTGCTACTCATTCCTGCTCATTCCAGTGTTCTGGAAAATGAGTTCACAGCCATG
AATGAACCACAGTGCTTCTACAACGAGTCCATTGCCTTCTTTTATAACCGAAGTGGAAAG
CATCTTGCCACAGAATGGAACACAGTCAGCAAGCTGGTGATGGGACTTGGAATCACTGTT
TGTATCTTCATCATGTTGGCCAACCTATTGGTCATGGTGGCAATCTATGTCAACCGCCGC
TTCCATTTTCCTATTTATTACCTAATGGCTAATCTGGCTGCTGCAGACTTCTTTGCTGGG
TTGGCCTACTTCTATCTCATGTTCAACACAGGACCCAATACTCGGAGACTGACTGTTAGC
ACATGGCTCCTTCGTCAGGGCCTCATTGACACCAGCCTGACGGCATCTGTGGCCAACTTA
CTGGCTATTGCAATCGAGAGGCACATTACGGTTTTCCGCATGCAGCTCCACACACGGATG
AGCAACCGGCGGGTAGTGGTGGTCATTGTGGTCATCTGGACTATGGCCATCGTTATGGGT
GCTATACCCAGTGTGGGCTGGAACTGTATCTGTGATATTGAAAATTGTTCCAACATGGCA
CCCCTCTACAGTGACTCTTACTTAGTCTTCTGGGCCATTTTCAACTTGGTGACCTTTGTG
GTAATGGTGGTTCTCTATGCTCACATCTTTGGCTATGTTCGCCAGAGGACTATGAGAATG
TCTCGGCATAGTTCTGGACCCCGGCGGAATCGGGATACCATGATGAGTCTTCTGAAGACT
GTGGTCATTGTGCTTGGGGCCTTTATCATCTGCTGGACTCCTGGATTGGTTTTGTTACTT
CTAGACGTGTGCTGTCCACAGTGCGACGTGCTGGCCTATGAGAAATTCTTCCTTCTCCTT
GCTGAATTCAACTCTGCCATGAACCCCATCATTTACTCCTACCGCGACAAAGAAATGAGC
GCCACCTTTAGGCAGATCCTCTGCTGCCAGCGCAGTGAGAACCCCACCGGCCCCACAGAA
GGCTCAGACCGCTCGGCTTCCTCCCTCAACCACACCATCTTGGCTGGAGTTCACAGCAAT
GACCACTCTGTGGTTTAG
Enzyme 53 GenBank Gene ID AK296374 Link Image
Enzyme 53 GeneCard ID Not Available
Enzyme 53 GenAtlas ID Not Available
Enzyme 53 HGNC ID HGNC:3166 Link Image
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
Enzyme 54 [top]
Enzyme 54 ID 17298
Enzyme 54 Name cDNA FLJ41048 fis, clone PROST2001213, highly similar to Lysophosphatidic acid receptor Edg-4
Enzyme 54 Synonyms Not Available
Enzyme 54 Gene Name Not Available
Enzyme 54 Protein Sequence >cDNA FLJ41048 fis, clone PROST2001213, highly similar to Lysophosphatidic acid receptor Edg-4
MVIMGQCYYNETIGFFYNNSGKELSSHWRPKDVVVVALGLTVSVLVLLTNLLVIAAIASN
RRFHQPIYYLLGNLAAADLFAGVAYLFLMFHTGPRTARLSLEGWFLRQGLLDTSLTASVA
TLLAIAVERHRSVMAVQLHSRLPRGRVVMLIVGVWVAALGLGLLPAHSWHCLCALDRCSR
MAPLLSRSYLAVWALSGLLVFLLMVAVYTRIFFYVRRRVQRMAEHVSCHPRYRETTLSLV
KTVVIILGAFVVCWTPGQVVLLLDGLGCESCNVLAVEKYFLLLAEANSLVNAAVYSCRDA
EMRRTFHRLLCCACLRQSTRESVHYTSSAQGGASTRIMLPENGHPLMDSTL
Enzyme 54 Number of Residues 351
Enzyme 54 Molecular Weight 39034.7
Enzyme 54 Theoretical pI 9.29
Enzyme 54 GO Classification
Function
  • G-protein coupled receptor activity
  • bioactive lipid receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 54 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 54 Specific Function Not Available
Enzyme 54 Pathways Not Available
Enzyme 54 Reactions Not Available
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • None
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein 193784708 Link Image
Enzyme 54 UniProtKB/Swiss-Prot ID B3KVP9 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name B3KVP9_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence >1056 bp
ATGGTCATCATGGGCCAGTGCTACTACAACGAGACCATCGGCTTCTTCTATAACAACAGT
GGCAAAGAGCTCAGCTCCCACTGGCGGCCCAAGGATGTGGTCGTGGTGGCGCTGGGGCTG
ACCGTCAGCGTGCTGGTGCTGCTGACCAATCTGCTGGTCATAGCAGCCATCGCCTCCAAC
CGCCGCTTCCACCAGCCCATCTACTACCTGCTCGGCAATCTGGCCGCGGCTGACCTCTTC
GCGGGCGTGGCCTACCTCTTCCTCATGTTCCACACTGGTCCCCGCACAGCCCGACTTTCA
CTTGAGGGCTGGTTCCTGCGGCAGGGCTTGCTGGACACAAGCCTCACTGCGTCGGTGGCC
ACACTGCTGGCCATCGCCGTGGAGCGGCACCGCAGTGTGATGGCCGTGCAGCTGCACAGC
CGCCTGCCCCGTGGCCGCGTGGTCATGCTCATTGTGGGCGTGTGGGTGGCTGCCCTGGGC
CTGGGGCTGCTGCCTGCCCACTCCTGGCACTGCCTCTGTGCCCTGGACCGCTGCTCACGC
ATGGCACCCCTGCTCAGCCGCTCCTATTTGGCCGTCTGGGCTCTGTCGGGCCTGCTTGTC
TTCCTGCTCATGGTGGCTGTGTACACCCGCATTTTCTTCTACGTGCGGCGGCGAGTGCAG
CGCATGGCAGAGCATGTCAGCTGCCACCCCCGCTACCGAGAGACCACGCTCAGCCTGGTC
AAGACTGTTGTCATCATCCTGGGGGCGTTCGTGGTCTGCTGGACACCAGGCCAGGTGGTA
CTGCTCCTGGATGGTTTAGGCTGTGAGTCCTGCAATGTCCTGGCTGTAGAAAAGTACTTC
CTACTGTTGGCCGAGGCCAACTCACTGGTCAATGCTGCTGTGTACTCTTGCCGAGATGCT
GAGATGCGCCGCACCTTCCACCGCCTTCTCTGCTGCGCGTGCCTCCGCCAGTCCACCCGC
GAGTCTGTCCACTATACATCCTCTGCCCAGGGAGGTGCCAGCACTCGCATCATGCTTCCC
GAGAACGGCCACCCACTGATGGACTCCACCCTTTAG
Enzyme 54 GenBank Gene ID AK123043 Link Image
Enzyme 54 GeneCard ID Not Available
Enzyme 54 GenAtlas ID Not Available
Enzyme 54 HGNC ID HGNC:3168 Link Image
Enzyme 54 Chromosome Location Not Available
Enzyme 54 Locus Not Available
Enzyme 54 SNPs Not Available
Enzyme 54 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 17299
Enzyme 55 Name Endothelial differentiation, lysophosphatidic acid G-protein-coupled receptor, 2, isoform CRA_a
Enzyme 55 Synonyms
  1. SubName: Lysophosphatidic acid receptor 1
  2. SubName: cDNA FLJ12746 fis, clone NT2RP2000842, highly similar to Lysophosphatidic acid receptor Edg-2
  3. SubName: cDNA FLJ78319, highly similar to Homo sapiens endothelial differentiation, lysophosphatidic acid G-protein-coupled receptor, 2 (EDG2), transcript variant 2, mRNA
Enzyme 55 Gene Name LPAR1
Enzyme 55 Protein Sequence >Endothelial differentiation, lysophosphatidic acid G-protein-coupled receptor, 2, isoform CRA_a
MAAISTSIPVISQPQFTAMNEPQCFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITVC
IFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVST
WLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMGA
IPSVGWNCICDIENCSNMAPLYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRMS
RHSSGPRRNRDTMMSLLKTVVIVLGAFIICWTPGLVLLLLDVCCPQCDVLAYEKFFLLLA
EFNSAMNPIIYSYRDKEMSATFRQILCCQRSENPTGPTEGSDRSASSLNHTILAGVHSND
HSVV
Enzyme 55 Number of Residues 364
Enzyme 55 Molecular Weight 41109.0
Enzyme 55 Theoretical pI 8.60
Enzyme 55 GO Classification
Function
  • G-protein coupled receptor activity
  • bioactive lipid receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 55 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 55 Specific Function Not Available
Enzyme 55 Pathways Not Available
Enzyme 55 Reactions Not Available
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • None
Enzyme 55 Transmembrane Regions
  • None
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 193785683 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID Q5VZX0 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name Q5VZX0_HUMAN Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >1095 bp
ATGGCTGCCATCTCTACTTCCATCCCTGTAATTTCACAGCCCCAGTTCACAGCCATGAAT
GAACCACAGTGCTTCTACAACGAGTCCATTGCCTTCTTTTATAACCGAAGTGGAAAGCAT
CTTGCCACAGAATGGAACACAGTCAGCAAGCTGGTGATGGGACTTGGAATCACTGTTTGT
ATCTTCATCATGTTGGCCAACCTATTGGTCATGGTGGCAATCTATGTCAACCGCCGCTTC
CATTTTCCTATTTATTACCTAATGGCTAATCTGGCTGCTGCAGACTTCTTTGCTGGGTTG
GCCTACTTCTATCTCATGTTCAACACAGGACCCAATACTCGGAGACTGACTGTTAGCACA
TGGCTCCTTCGTCAGGGCCTCATTGACACCAGCCTGACGGCATCTGTGGCCAACTTACTG
GCTATTGCAATCGAGAGGCACATTACGGTTTTCCGCATGCAGCTCCACACACGGATGAGC
AACCGGCGGGTAGTGGTGGTCATTGTGGTCATCTGGACTATGGCCATCGTTATGGGTGCT
ATACCCAGTGTGGGCTGGAACTGTATCTGTGATATTGAAAATTGTTCCAACATGGCACCC
CTCTACAGTGACTCTTACTTAGTCTTCTGGGCCATTTTCAACTTGGTGACCTTTGTGGTA
ATGGTGGTTCTCTATGCTCACATCTTTGGCTATGTTCGCCAGAGGACTATGAGAATGTCT
CGGCATAGTTCTGGACCCCGGCGGAATCGGGATACCATGATGAGTCTTCTGAAGACTGTG
GTCATTGTGCTTGGGGCCTTTATCATCTGCTGGACTCCTGGATTGGTTTTGTTACTTCTA
GACGTGTGCTGTCCACAGTGCGACGTGCTGGCCTATGAGAAATTCTTCCTTCTCCTTGCT
GAATTCAACTCTGCCATGAACCCCATCATTTACTCCTACCGCGACAAAGAAATGAGCGCC
ACCTTTAGGCAGATCCTCTGCTGCCAGCGCAGTGAGAACCCCACCGGCCCCACAGAAGGC
TCAGACCGCTCGGCTTCCTCCCTCAACCACACCATCTTGGCTGGAGTTCACAGCAATGAC
CACTCTGTGGTTTAG
Enzyme 55 GenBank Gene ID AK022808 Link Image
Enzyme 55 GeneCard ID LPAR1 Link Image
Enzyme 55 GenAtlas ID LPAR1 Link Image
Enzyme 55 HGNC ID HGNC:3166 Link Image
Enzyme 55 Chromosome Location 9
Enzyme 55 Locus 9q31.3
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 17300
Enzyme 56 Name cDNA FLJ55767, highly similar to Lysophosphatidic acid receptor Edg-2
Enzyme 56 Synonyms Not Available
Enzyme 56 Gene Name Not Available
Enzyme 56 Protein Sequence >cDNA FLJ55767, highly similar to Lysophosphatidic acid receptor Edg-2
MEEGAQRSGALGAPHQFTAMNEPQCFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITV
CIFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVS
TWLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMG
AIPSVGWNCICDIENCSNMAPLYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRM
SRHSSGPRRNRDTMMSLLKTVVIVLGAFIICWTPGLVLLLLDVCCPQCDVLAYEKFFLLL
AEFNSAMNPIIYSYRDKEMSATFRQILCCQRSENPTGPTEGSDRSASSLNHTILAGVHSN
DHSVV
Enzyme 56 Number of Residues 365
Enzyme 56 Molecular Weight 41204.9
Enzyme 56 Theoretical pI 8.47
Enzyme 56 GO Classification
Function
  • G-protein coupled receptor activity
  • bioactive lipid receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 56 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 56 Specific Function Not Available
Enzyme 56 Pathways Not Available
Enzyme 56 Reactions Not Available
Enzyme 56 Pfam Domain Function
Enzyme 56 Signals
  • None
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein 194391324 Link Image
Enzyme 56 UniProtKB/Swiss-Prot ID B4DQ18 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name B4DQ18_HUMAN Link Image
Enzyme 56 PDB ID Not Available
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence >1098 bp
ATGGAGGAGGGGGCGCAGAGGTCAGGGGCGCTGGGGGCGCCACACCAGTTCACAGCCATG
AATGAACCACAGTGCTTCTACAACGAGTCCATTGCCTTCTTTTATAACCGAAGTGGAAAG
CATCTTGCCACAGAATGGAACACAGTCAGCAAGCTGGTGATGGGACTTGGAATCACTGTT
TGTATCTTCATCATGTTGGCCAACCTATTGGTCATGGTGGCAATCTATGTCAACCGCCGC
TTCCATTTTCCTATTTATTACCTAATGGCTAATCTGGCTGCTGCAGACTTCTTTGCTGGG
TTGGCCTACTTCTATCTCATGTTCAACACAGGACCCAATACTCGGAGACTGACTGTTAGC
ACATGGCTCCTTCGTCAGGGCCTCATTGACACCAGCCTGACGGCATCTGTGGCCAACTTA
CTGGCTATTGCAATCGAGAGGCACATTACGGTTTTCCGCATGCAGCTCCACACACGGATG
AGCAACCGGCGGGTAGTGGTGGTCATTGTGGTCATCTGGACTATGGCCATCGTTATGGGT
GCTATACCCAGTGTGGGCTGGAACTGTATCTGTGATATTGAAAATTGTTCCAACATGGCA
CCCCTCTACAGTGACTCTTACTTAGTCTTCTGGGCCATTTTCAACTTGGTGACCTTTGTG
GTAATGGTGGTTCTCTATGCTCACATCTTTGGCTATGTTCGCCAGAGGACTATGAGAATG
TCTCGGCATAGTTCTGGACCCCGGCGGAATCGGGATACCATGATGAGTCTTCTGAAGACT
GTGGTCATTGTGCTTGGGGCCTTTATCATCTGCTGGACTCCTGGATTGGTTTTGTTACTT
CTAGACGTGTGCTGTCCACAGTGCGACGTGCTGGCCTATGAGAAATTCTTCCTTCTCCTT
GCTGAATTCAACTCTGCCATGAACCCCATCATTTACTCCTACCGCGACAAAGAAATGAGC
GCCACCTTTAGGCAGATCCTCTGCTGCCAGCGCAGTGAGAACCCCACCGGCCCCACAGAA
GGCTCAGACCGCTCGGCTTCCTCCCTCAACCACACCATCTTGGCTGGAGTTCACAGCAAT
GACCACTCTGTGGTTTAG
Enzyme 56 GenBank Gene ID AK298590 Link Image
Enzyme 56 GeneCard ID Not Available
Enzyme 56 GenAtlas ID Not Available
Enzyme 56 HGNC ID HGNC:3166 Link Image
Enzyme 56 Chromosome Location Not Available
Enzyme 56 Locus Not Available
Enzyme 56 SNPs Not Available
Enzyme 56 General References Not Available
Enzyme 56 Metabolite References Not Available