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

Human Metabolome Database Version 2.5

 

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

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2008-09-12 02:59:36
Update Date 2009-05-05 21:05:43
Accession Number HMDB09778
Secondary Accession Numbers Not Available
Common Name PI(16:0/16:0)
Description PI(16:0/16:0) is a phosphatidylinositol. Phosphatidylinositols are important lipids, both as a key membrane constituent and as a participant in essential metabolic processes, both directly and via a number of metabolites. Phosphatidylinositols are acidic (anionic) phospholipids that consist of a phosphatidic acid backbone, linked via the phosphate group to inositol (hexahydroxycyclohexane). Phosphatidylinositols can have many different combinations of fatty acids of varying lengths and saturation attached at the C-1 and C-2 positions. Fatty acids containing 18 and 20 carbons are the most common. PI(16:0/16:0), in particular, consists of one chain of palmitic acid at the C-1 position and one chain of palmitic acid at the C-2 position. The palmitic acid moiety is derived from fish oils, milk fats, vegetable oils and animal fats, while the palmitic acid moiety is derived from fish oils, milk fats, vegetable oils and animal fats. In most organisms, the stereochemical form of the last is myo-D-inositol (with one axial hydroxyl in position 2 with the remainder equatorial. Phosphatidylinositol is especially abundant in brain tissue, where it can amount to 10% of the phospholipids, but it is present in all tissues and cell types. There is usually less of it than of phosphatidylcholine, phosphatidylethanolamine and phosphatidylserine. In animal tissues, phosphatidylinositol is the primary source of the arachidonic acid required for biosynthesis of eicosanoids, including prostaglandins, via the action of the enzyme phospholipase A2. Phosphatidylinositol can be phosphorylated by a number of different kinases that place the phosphate moiety on positions 4 and 5 of the inositol ring, although position 3 can also be phosphorylated by a specific kinase. Seven different isomers are known, but the most important in both quantitative and biological terms are phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate. Phosphatidylinositol and the phosphatidylinositol phosphates are the main source of diacylglycerols that serve as signaling molecules, via the action of phospholipase C enzymes. While most phospholipids have a saturated fatty acid on C-1 and an unsaturated fatty acid on C-2 of the glycerol backbone, the fatty acid distribution at the C-1 and C-2 positions of glycerol within phospholipids is continually in flux, owing to phospholipid degradation and the continuous phospholipid remodeling that occurs while these molecules are in membranes. PIs contain almost exclusively stearic acid at carbon 1 and arachidonic acid at carbon 2. PIs composed exclusively of non-phosphorylated inositol exhibit a net charge of -1 at physiological pH. Molecules with phosphorylated inositol (such as PIP, PIP2, PIP3, etc.) are termed polyphosphoinositides. The polyphosphoinositides are important intracellular transducers of signals emanating from the plasma membrane. The synthesis of PI involves CDP-activated 1,2-diacylglycerol condensation with myo-inositol.
Synonyms
  1. Phosphatidylinositol(32:0)
  2. PIno(16:0/16:0)
  3. PIno(32:0)
  4. 1,2-dipalmitoyl-rac-glycero-3-phosphoinositol
  5. Phosphatidylinositol(16:0/16:0)
  6. PI(32:0)
  7. 1,2-dihexadecanoyl-rac-glycero-3-phospho-(1'-myo-inositol)
  8. PI(16:0/16:0)
Chemical IUPAC Name 1,2-dihexadecanoyl-rac-glycero-3-phosphoinositol
Chemical Formula C41H79O13P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Lipids
Class
  • Phospholipids
Sub Class
  • Phosphatidylinositols
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • carboxylic acid ester
  • phosphoric acid ester
Biofunction
  • Membrane component
  • Energy source
  • Cell signaling
Application
Source
  • Endogenous
Average Molecular Weight 811.032
Monoisotopic Molecular Weight 810.525818
Isomeric SMILES CCCCCCCCCCCCCCCC(=O)OC[C@H](COP(O)(=O)O[C@H]1C(O)C(O)C(O)[C@@H](O)C1O)OC(=O)CCCCCCCCCCCCCCC
Canonical SMILES CCCCCCCCCCCCCCCC(=O)OCC(COP(O)(=O)OC1C(O)C(O)C(O)C(O)C1O)OC(=O)CCCCCCCCCCCCCCC
KEGG Compound ID C00626 Link Image
BioCyc ID Phosphatidylinositols Link Image
BiGG ID Not Available
Wikipedia Link Lecithin Link Image
NuGOwiki Link HMDB09778 Link Image
Metagene Link HMDB09778 Link Image
METLIN ID Not Available
PubChem Compound Not Available
PubChem Substance Not Available
ChEBI ID Not Available
CAS Registry Number Not Available
InChI Identifier InChI=1/C41H79O13P/c1-3-5-7-9-11-13-15-17-19-21-23-25-27-29-34(42)51-31-33(32-52-55(49,50)54-41-39(47)37(45)36(44)38(46)40(41)48)53-35(43)30-28-26-24-22-20-18-16-14-12-10-8-6-4-2/h33,36-41,44-48H,3-32H2,1-2H3,(H,49,50)/t33-,36?,37-,38?,39-,40?,41-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.40e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 6.79 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show 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
Brain
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Phospholipid Biosynthesis SMP00025 Link Image map00564 Link Image
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1
  2. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4
  3. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2
  4. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3
  5. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2
  6. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1
  7. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1
  8. N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
  9. Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
  10. Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
  11. Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
  12. Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
  13. Probable phospholipid-transporting ATPase IG
  14. Probable phospholipid-transporting ATPase IH
  15. Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta isoform
  16. Probable phospholipid-transporting ATPase VA
  17. Probable phospholipid-transporting ATPase IC
  18. Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform
  19. Probable phospholipid-transporting ATPase IIA
  20. Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
  21. Probable phospholipid-transporting ATPase VD
  22. Probable phospholipid-transporting ATPase IB
  23. Probable phospholipid-transporting ATPase IA
  24. Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
  25. Probable phospholipid-transporting ATPase IM
  26. Probable phospholipid-transporting ATPase IF
  27. Probable phospholipid-transporting ATPase IK
  28. Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
  29. Phosphatidylinositol transfer protein beta isoform
  30. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-2
  31. Phospholipid scramblase 1
  32. Phosphatidylserine synthase 1
  33. Phosphatidylserine decarboxylase proenzyme
  34. Phosphatidylinositol transfer protein alpha isoform
  35. Phospholipid transfer protein
  36. GPI mannosyltransferase 1
  37. Phosphatidylserine synthase 2
  38. Phosphatidylinositol-glycan biosynthesis class W protein
  39. Phosphatidylinositol-glycan biosynthesis class X protein
  40. GPI mannosyltransferase 4
  41. Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2
  42. Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1
  43. Phosphatidylinositol 3-kinase catalytic subunit type 3
  44. PI-PLC X domain-containing protein 2
  45. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
  46. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-1
  47. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1
  48. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
  49. Phospholipid scramblase 2
  50. Phospholipid scramblase 3
  51. Phospholipid scramblase 4
  52. Phospholipid scramblase family member 5
  53. Probable phospholipid-transporting ATPase VB
  54. Probable phospholipid-transporting ATPase ID
  55. Phospholipase A1 member A
  56. Serum deprivation-response protein
  57. GPI mannosyltransferase 3
  58. Phosphatidylinositol-glycan biosynthesis class F protein
  59. GPI ethanolamine phosphate transferase 2
  60. GPI ethanolamine phosphate transferase 1
  61. GPI ethanolamine phosphate transferase 3
  62. GPI transamidase component PIG-S
  63. GPI transamidase component PIG-T
  64. Phosphatidylinositol glycan anchor biosynthesis class U protein
  65. GPI mannosyltransferase 2
  66. Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
  67. Cytoplasmic phosphatidylinositol transfer protein 1
  68. Membrane-associated phosphatidylinositol transfer protein 1
  69. Membrane-associated phosphatidylinositol transfer protein 2
  70. Membrane-associated phosphatidylinositol transfer protein 3
  71. Pleckstrin homology domain-containing family A member 8
  72. PI-PLC X domain-containing protein 1
  73. PI-PLC X domain-containing protein 3
  74. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase zeta-1
  75. Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
  76. Transmembrane protein 55A
  77. Transmembrane protein 55B
  78. Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase TPTE2
  79. Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1
  80. Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1
Enzyme 1 [top]
Enzyme 1 ID 5454
Enzyme 1 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1
Enzyme 1 Synonyms
  1. PLC-154
  2. Phosphoinositide phospholipase C-beta-1
  3. Phospholipase C-I
  4. PLC-I
  5. Phospholipase C-beta-1
  6. PLC-beta-1
Enzyme 1 Gene Name PLCB1
Enzyme 1 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1
MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKE
TELLDLSLVKDARCGRHAKAPKDPKLRELLDVGNIGRLEQRMITVVYGPDLVNISHLNLV
AFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSA
DRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYL
TVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLARKGQISVDGFMRYLS
GEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCV
ELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQ
QAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKK
KLSEQASNTYSDSSSMFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEM
SNLVNYIQPVKFESFEISKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPK
GTRVDSSNYMPQLFWNAGCQMVALNFQTMDLAMQINMGMYEYNGKSGYRLKPEFMRRPDK
HFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQG
NAVNPVWEEEPIVFKKVVLPTLACLRIAVYEEGGKFIGHRILPVQAIRPGYHYICLRNER
NQPLTLPAVFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKK
EADPGETPSEAPSEARTTPAENGVNHTTTLTPKPPSQALHSQPAPGSVKAPAKTEDLIQS
VLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTTKYNEIQNDYL
RRRAALEKSAKKDSKKKSEPSSPDHGSSTIEQDLAALDAEMTQKLIDLKDKQQQQLLNLR
QEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKI
TEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHKEIRQQILDEKP
KLQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPLSLSSDPGKVNHKTPSS
EELGGDIPGKEFDTPL
Enzyme 1 Number of Residues 1216
Enzyme 1 Molecular Weight 138565.8
Enzyme 1 Theoretical pI 6.12
Enzyme 1 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 1 General Function Involved in calcium ion binding
Enzyme 1 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 12083581 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9NQ66 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PLCB1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >3651 bp
ATGGCCGGGGCTCAACCCGGAGTGCACGCCTTGCAACTCAAGCCCGTGTGCGTGTCCGAC
AGCCTCAAGAAGGGCACCAAATTCGTCAAGTGGGATGATGACTCAACTATTGTTACTCCA
ATTATTTTGAGGACTGACCCTCAGGGATTTTTCTTTTACTGGACAGATCAAAACAAGGAG
ACAGAGCTACTGGATCTCAGCCTTGTCAAAGATGCCAGATGTGGGAGACACGCCAAAGCT
CCCAAGGACCCCAAATTACGTGAACTTTTGGATGTGGGGAACATCGGGCGCCTGGAGCAG
CGCATGATCACAGTGGTGTATGGGCCTGACCTCGTGAACATCTCCCATTTGAATCTCGTG
GCTTTCCAAGAAGAAGTGGCCAAGGAATGGACAAATGAGGTTTTCAGTTTGGCAACAAAC
CTGCTGGCCCAAAACATGTCCAGGGATGCATTTCTGGAAAAAGCCTATACTAAACTTAAG
CTGCAAGTCACTCCAGAAGGGCGTATTCCTCTCAAAAACATATATCGCTTGTTTTCAGCA
GATCGGAAGCGAGTTGAAACTGCTTTAGAGGCTTGTAGTCTTCCATCTTCAAGGAATGAT
TCAATACCTCAAGAAGATTTCACTCCAGAAGTGTACAGAGTTTTCCTCAACAACCTTTGC
CCTCGACCTGAAATTGATAACATCTTTTCAGAATTTGGTGCAAAAAGCAAACCATATCTT
ACCGTTGATCAGATGATGGATTTTATCAACCTTAAGCAGCGAGATCCTCGGCTTAATGAA
ATACTTTATCCACCTCTAAAACAAGAGCAAGTCCAAGTATTGATTGAGAAGTATGAACCC
AACAACAGCCTCGCCAGAAAAGGACAAATATCAGTGGATGGGTTCATGCGCTATCTGAGT
GGAGAAGAAAACGGAGTCGTTTCACCTGAGAAACTGGATTTGAATGAAGACATGTCTCAG
CCCCTTTCTCACTATTTCATTAATTCCTCGCACAACACCTACCTCACAGCTGGCCAACTG
GCTGGAAACTCCTCTGTTGAGATGTATCGCCAAGTGCTCCTGTCTGGTTGTCGCTGTGTG
GAGCTGGACTGCTGGAAGGGACGGACTGCAGAAGAGGAACCTGTCATCACCCATGGCTTC
ACCATGACAACTGAAATATCTTTCAAGGAAGTGATAGAAGCAATTGCGGAGTGTGCATTT
AAGACTTCACCTTTTCCAATTCTCCTTTCGTTTGAGAACCATGTGGATTCCCCAAAGCAG
CAAGCCAAGATGGCGGAGTACTGCCGACTGATCTTTGGGGATGCCCTTCTCATGGAGCCC
CTGGAAAAATATCCACTGGAATCTGGAGTTCCTCTTCCAAGCCCTATGGATTTAATGTAT
AAAATTTTGGTGAAAAATAAGAAGAAATCACACAAGTCATCAGAAGGAAGCGGCAAAAAG
AAGCTCTCAGAACAAGCCTCCAACACCTACAGTGACTCCTCCAGCATGTTCGAGCCCTCA
TCCCCAGGAGCCGGAGAAGCTGATACGGAAAGTGACGACGACGATGATGATGATGACTGT
AAAAAATCTTCAATGGATGAGGGGACTGCTGGAAGTGAGGCTATGGCCACAGAAGAAATG
TCTAATCTGGTGAACTATATTCAGCCAGTCAAGTTTGAGTCATTTGAAATTTCAAAAAAA
AGAAATAAAAGTTTTGAAATGTCTTCCTTCGTGGAAACCAAAGGACTTGAACAACTCACC
AAGTCTCCAGTGGAATTTGTAGAATATAACAAAATGCAGCTTAGCAGGATATATCCAAAA
GGAACACGTGTGGATTCATCCAACTATATGCCTCAGCTCTTCTGGAATGCAGGTTGTCAG
ATGGTGGCACTTAATTTCCAGACAATGGACCTGGCTATGCAAATAAATATGGGGATGTAT
GAATACAACGGGAAGAGTGGCTACAGATTGAAGCCAGAGTTCATGAGGAGGCCTGACAAG
CATTTTGATCCATTTACTGAAGGCATCGTAGATGGGATAGTGGCAAACACTTTGTCTGTT
AAGATTATTTCAGGTCAGTTTCTTTCTGATAAGAAAGTTGGGACTTACGTGGAAGTAGAT
ATGTTTGGTTTGCCTGTGGATACAAGGAGGAAGGCATTTAAGACCAAAACATCCCAAGGA
AATGCTGTGAATCCTGTCTGGGAAGAAGAACCTATTGTGTTCAAAAAGGTGGTTCTTCCT
ACTCTGGCCTGTTTGAGAATAGCAGTTTATGAAGAAGGAGGTAAATTCATTGGCCACCGT
ATCTTGCCAGTGCAAGCCATTCGGCCAGGCTATCACTATATCTGTCTAAGGAATGAAAGG
AACCAGCCTCTGACGCTGCCTGCTGTCTTTGTCTACATAGAAGTGAAAGACTATGTGCCA
GACACATATGCAGATGTCATCGAAGCTTTATCAAACCCAATCCGATATGTGAACCTGATG
GAACAGAGAGCTAAGCAATTGGCTGCTTTGACACTGGAAGATGAAGAAGAAGTAAAGAAA
GAGGCTGATCCTGGAGAAACACCATCAGAGGCTCCAAGTGAAGCGAGAACGACTCCAGCA
GAAAATGGGGTGAATCACACTACAACCCTGACACCCAAGCCACCCTCCCAGGCTCTCCAC
AGCCAGCCAGCTCCAGGTTCTGTAAAGGCACCTGCCAAAACAGAAGATCTTATTCAGAGT
GTCTTAACAGAAGTGGAAGCACAGACCATCGAAGAACTAAAGCAACAGAAATCGTTTGTG
AAACTTCAAAAGAAACACTACAAAGAAATGAAAGACCTGGTTAAGAGACACCACAAGAAA
ACCACTGACCTTATCAAAGAACACACTACCAAGTATAATGAAATTCAGAATGACTACTTG
AGAAGGAGAGCCGCTTTGGAAAAGTCCGCCAAAAAGGACAGTAAGAAAAAATCGGAACCC
AGCAGCCCTGATCATGGTTCATCAACGATTGAGCAAGACCTCGCTGCTCTGGATGCTGAA
ATGACCCAAAAGTTAATAGACTTGAAGGACAAACAACAGCAGCAGCTGCTTAATCTTCGG
CAAGAACAGTATTATAGTGAAAAATACCAGAAGCGAGAACATATTAAACTGCTTATTCAA
AAGTTGACGGATGTCGCAGAAGAGTGTCAGAACAATCAGTTAAAGAAGCTCAAAGAAATC
TGTGAGAAAGAAAAGAAAGAATTAAAGAAGAAAATGGATAAAAAGAGGCAGGAGAAGATA
ACAGAAGCTAAATCCAAAGACAAAAGTCAGATGGAAGAGGAGAAGACAGAGATGATCCGG
TCATATATCCAGGAAGTGGTGCAGTATATCAAGAGGCTAGAAGAAGCGCAAAGTAAACGG
CAAGAAAAACTCGTAGAGAAACACAAGGAAATACGTCAGCAGATCCTGGATGAAAAGCCC
AAGCTGCAGGTGGAGCTGGAGCAAGAATACCAAGACAAATTCAAAAGACTGCCCCTCGAG
ATTTTGGAATTCGTGCAGGAAGCCATGAAAGGAAAGATCAGTGAAGACAGCAATCACGGT
TCTGCCCCTCTCTCCCTGTCCTCAGACCCTGGAAAAGTGAACCACAAGACTCCCTCCAGT
GAGGAGCTGGGAGGAGACATCCCAGGAAAAGAATTTGATACTCCTCTGTGA
Enzyme 1 GenBank Gene ID NM_015192.2 Link Image
Enzyme 1 GeneCard ID PLCB1 Link Image
Enzyme 1 GenAtlas ID PLCB1 Link Image
Enzyme 1 HGNC ID HGNC:15917 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 20p12
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Caricasole A, Sala C, Roncarati R, Formenti E, Terstappen GC: Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1). Biochim Biophys Acta. 2000 Dec 15;1517(1):63-72. [PubMed Link Image]
  2. Peruzzi D, Calabrese G, Faenza I, Manzoli L, Matteucci A, Gianfrancesco F, Billi AM, Stuppia L, Palka G, Cocco L: Identification and chromosomal localisation by fluorescence in situ hybridisation of human gene of phosphoinositide-specific phospholipase C beta(1). Biochim Biophys Acta. 2000 Apr 12;1484(2-3):175-82. [PubMed Link Image]
  3. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  4. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  5. 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]
  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. 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]
  8. 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]
  9. Tabellini G, Bortul R, Santi S, Riccio M, Baldini G, Cappellini A, Billi AM, Berezney R, Ruggeri A, Cocco L, Martelli AM: Diacylglycerol kinase-theta is localized in the speckle domains of the nucleus. Exp Cell Res. 2003 Jul 1;287(1):143-54. [PubMed Link Image]
  10. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed Link Image]
  11. 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]
  12. 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 5455
Enzyme 2 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4
Enzyme 2 Synonyms
  1. Phosphoinositide phospholipase C-beta-4
  2. Phospholipase C-beta-4
  3. PLC-beta-4
Enzyme 2 Gene Name PLCB4
Enzyme 2 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4
MAKPYEFNWQKEVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWRSEGKEGQVL
ECSLINSIRSGAIPKDPKILAALEAVGKSENDLEGRIVCVCSGTDLVNISFTYMVAENPE
VTKQWVEGLRSIIHNFRANNVSPMTCLKKHWMKLAFMTNTNGKIPVRSITRTFASGKTEK
VIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVD
QLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE
NAPVFLDRLELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELD
CWDGKGEDQEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKM
SKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRLKPEVEKKQLEALRSM
MEAGESASPANILEDDNEEEIESADQEEEAHPEFKFGNELSADDLGHKEAVANSVKKGLV
TVEDEQAWMASYKYVGATTNIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVG
LGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQL
NQGKFEYNGSCGYLLKPDFMRRPDRTFDPFSETPVDGVIAATCSVQVISGQFLSDKKIGT
YVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNK
LIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNIVLKTYVPDGFGDIVDALSDPKK
FLSITEKRADQMRAMGIETSDIADVPSDTSKNDKKGKANTAKANVTPQSSSELRPTTTAA
LASGVEAKKGIELIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHCTQ
VDKIVAQYDKEKSTHEKILEKAMKKKGGSNCLEMKKETEIKIQTLTSDHKSKVKEIVAQH
TKEWSEMINTHSAEEQEIRDLHLSQQCELLKKLLINAHEQQTQQLKLSHDRESKEMRAHQ
AKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQ
LEHLEFLEKQNEQAKEMQQMVKLEAEMDRRPATVV
Enzyme 2 Number of Residues 1175
Enzyme 2 Molecular Weight 134462.6
Enzyme 2 Theoretical pI 6.90
Enzyme 2 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 2 General Function Involved in calcium ion binding
Enzyme 2 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This form has a role in retina signal transduction
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 57284038 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q15147 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PLCB4_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >3528 bp
ATGGCCAAACCTTATGAATTTAACTGGCAGAAGGAAGTTCCCTCCTTTTTGCAAGAAGGA
GCAGTTTTTGACAGATACGAGGAGGAATCCTTTGTGTTTGAACCCAACTGCCTCTTCAAA
GTGGATGAGTTTGGCTTCTTTCTGACATGGAGAAGTGAAGGCAAGGAAGGACAGGTGCTA
GAATGCTCCCTCATCAACAGTATTCGGTCGGGAGCCATACCAAAGGATCCCAAAATCTTG
GCTGCTCTTGAAGCTGTTGGAAAATCAGAAAATGATCTGGAAGGGCGGATAGTTTGTGTC
TGCAGTGGCACAGATCTAGTGAACATTAGTTTTACCTACATGGTGGCTGAAAATCCAGAA
GTAACTAAGCAATGGGTAGAAGGCCTGAGATCAATCATACACAACTTCAGGGCCAACAAC
GTCAGTCCAATGACATGCCTCAAGAAACACTGGATGAAATTGGCATTTATGACCAACACA
AATGGTAAAATTCCAGTTAGGAGTATTACTAGAACATTTGCATCGGGAAAAACAGAAAAG
GTGATCTTTCAAGCACTCAAGGAGTTAGGTCTTCCCAGTGGAAAGAATGATGAAATTGAG
CCCACAGCATTTTCTTATGAAAAGTTCTATGAACTGACACAAAAGATTTGTCCTCGGACA
GATATAGAAGATCTTTTCAAAAAAATCAATGGAGACAAAACTGATTATTTAACGGTAGAC
CAATTAGTGAGCTTTCTAAATGAACATCAACGAGATCCTCGATTGAATGAAATTTTATTT
CCATTTTATGATGCCAAAAGGGCAATGCAGATCATTGAGATGTATGAACCTGATGAAGAT
TTGAAGAAAAAAGGCCTTATATCAAGTGATGGGTTTTGCAGATATCTGATGTCAGATGAA
AACGCCCCAGTCTTCCTAGATCGTTTAGAACTTTACCAAGAAATGGACCATCCTCTGGCT
CACTACTTCATCAGTTCTTCCCATAACACTTATCTCACTGGCAGACAGTTCGGCGGGAAG
TCTTCGGTAGAAATGTACAGACAGGTTCTCCTGGCTGGTTGCAGATGTGTTGAACTTGAC
TGCTGGGATGGAAAAGGTGAAGACCAAGAACCAATAATAACTCATGGAAAAGCAATGTGT
ACAGATATCCTTTTTAAGGATGTAATTCAAGCCATCAAGGAAACTGCATTTGTCACATCA
GAATATCCTGTAATTCTCTCCTTTGAAAATCACTGCAGCAAATATCAACAGTACAAGATG
TCCAAATATTGCGAAGATCTATTTGGGGATCTCCTGTTGAAACAAGCACTTGAATCACAT
CCACTTGAACCAGGCAGGGCTTTGCCATCCCCCAATGACCTCAAAAGAAAAATACTCATA
AAAAACAAGCGGCTGAAACCTGAAGTTGAAAAAAAACAGCTGGAAGCTTTGAGAAGCATG
ATGGAAGCTGGAGAATCTGCCTCCCCAGCAAACATCTTAGAGGACGATAATGAAGAGGAG
ATCGAAAGTGCTGACCAAGAGGAGGAAGCTCACCCCGAATTCAAATTTGGAAATGAACTT
TCTGCTGATGACTTGGGTCACAAGGAAGCTGTTGCAAATAGCGTCAAGAAGGGCCTGGTC
ACTGTAGAAGATGAGCAGGCGTGGATGGCATCTTATAAATATGTAGGTGCTACCACTAAT
ATCCATCCATATTTGTCCACAATGATCAACTACGCCCAGCCTGTAAAGTTTCAAGGTTTC
CATGTGGCAGAAGAACGCAATATTCATTATAACATGTCTTCTTTTAATGAATCAGTCGGT
CTTGGCTACTTGAAGACACATGCAATTGAATTTGTCAATTATAACAAACGGCAAATGAGT
CGCATTTACCCCAAGGGAGGCCGAGTCGATTCCAGTAATTACATGCCTCAGATTTTCTGG
AACGCTGGCTGCCAGATGGTTTCACTGAACTATCAAACCCCAGATTTAGCGATGCAATTG
AATCAGGGAAAATTTGAGTATAATGGATCGTGCGGGTACCTTCTCAAACCAGATTTCATG
AGGCGGCCTGATCGAACATTTGACCCCTTCTCTGAAACTCCTGTTGATGGTGTTATTGCA
GCCACTTGCTCAGTGCAGGTTATATCAGGTCAATTCTTATCAGATAAGAAAATTGGCACC
TACGTAGAGGTGGATATGTATGGGTTGCCCACTGACACCATACGTAAGGAATTCCGAACT
CGCATGGTTATGAATAATGGACTCAATCCAGTTTACAATGAAGAGTCATTTGTATTTCGG
AAGGTGATCCTGCCGGACCTGGCTGTCTTGAGAATAGCTGTGTATGATGATAACAACAAG
CTGATTGGCCAGAGGATCCTCCCGCTTGATGGCCTCCAAGCCGGATATCGACACATTTCC
CTTCGAAATGAGGGAAATAAACCATTATCACTACCAACAATTTTCTGCAATATTGTTCTT
AAAACATATGTGCCTGATGGATTTGGAGATATCGTGGATGCTTTATCAGATCCAAAGAAA
TTTCTCTCAATTACAGAAAAGAGAGCAGACCAAATGAGAGCTATGGGCATTGAAACTAGT
GACATAGCCGACGTGCCCAGTGACACTTCCAAAAATGACAAGAAAGGAAAGGCCAACACC
GCCAAAGCAAATGTGACCCCTCAGAGTAGCTCTGAGCTCAGACCAACCACCACGGCTGCC
CTGGCCTCTGGTGTGGAAGCCAAGAAAGGTATTGAACTTATCCCTCAAGTAAGGATAGAA
GACTTAAAGCAGATGAAGGCTTACTTGAAGCATTTAAAGAAACAGCAGAAGGAGCTAAAT
TCTTTAAAGAAGAAACATGCAAAGGAACACAGTACCATGCAGAAGTTACACTGCACGCAA
GTTGACAAAATTGTGGCACAGTATGACAAAGAGAAGTCGACTCATGAGAAAATCCTAGAG
AAGGCAATGAAGAAGAAGGGGGGAAGTAATTGTCTCGAAATGAAAAAAGAAACAGAAATC
AAAATTCAGACGCTGACATCAGATCACAAATCTAAGGTCAAAGAGATTGTAGCACAGCAC
ACAAAGGAATGGTCAGAAATGATCAATACCCACAGTGCTGAGGAGCAAGAAATCCGAGAC
CTGCACCTCAGCCAGCAGTGTGAGCTGCTGAAAAAGCTACTCATCAATGCCCACGAGCAG
CAAACCCAGCAGCTGAAACTGTCCCATGACAGGGAAAGCAAGGAAATGCGAGCACACCAG
GCTAAGATTTCTATGGAAAATAGCAAAGCCATCAGCCAAGATAAATCTATCAAGAATAAA
GCAGAACGGGAAAGGCGAGTCAGGGAGTTAAACAGCAGCAACACTAAAAAGTTTCTGGAA
GAAAGAAAGAGACTTGCCATGAAGCAGTCCAAAGAAATGGATCAGTTGAAAAAAGTCCAG
CTTGAACATCTAGAATTCCTAGAGAAACAGAATGAGCAGGCGAAGGAGATGCAGCAGATG
GTGAAATTGGAAGCCGAGATGGACCGCAGACCAGCAACAGTAGTATGA
Enzyme 2 GenBank Gene ID AL023805 Link Image
Enzyme 2 GeneCard ID PLCB4 Link Image
Enzyme 2 GenAtlas ID PLCB4 Link Image
Enzyme 2 HGNC ID HGNC:9059 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 20p12
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Alvarez RA, Ghalayini AJ, Xu P, Hardcastle A, Bhattacharya S, Rao PN, Pettenati MJ, Anderson RE, Baehr W: cDNA sequence and gene locus of the human retinal phosphoinositide-specific phospholipase-C beta 4 (PLCB4). Genomics. 1995 Sep 1;29(1):53-61. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  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. 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]
  5. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5456
Enzyme 3 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2
Enzyme 3 Synonyms
  1. Phosphoinositide phospholipase C-beta-2
  2. Phospholipase C-beta-2
  3. PLC-beta-2
Enzyme 3 Gene Name PLCB2
Enzyme 3 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2
MSLLNPVLLPPKVKAYLSQGERFIKWDDETTVASPVILRVDPKGYYLYWTYQSKEMEFLD
ITSIRDTRFGKFAKMPKSQKLRDVFNMDFPDNSFLLKTLTVVSGPDMVDLTFHNFVSYKE
NVGKAWAEDVLALVKHPLTANASRSTFLDKILVKLKMQLNSEGKIPVKNFFQMFPADRKR
VEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSYHAKAKPYMTKEH
LTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPEN
SVLAQDKLLLHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDC
WKGKPPDEEPIITHGFTMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVDSPRQQAKM
AEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKNQFSGPTSSSKDTGGE
AEGSSPPSAPAGEGTVWAGEEGTELEEEEVEEEEEEESGNLDEEEIKKMQSDEGTAGLEV
TAYEEMSSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQM
SRIYPKGTRMDSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEF
MRRPDKQFNPFSVDRIDVVVATTLSITVISGQFLSERSVRTYVEVELFGLPGDPKRRYRT
KLSPSTNSINPVWKEEPFVFEKILMPELASLRVAVMEEGNKFLGHRIIPINALNSGYHHL
CLHSESNMPLTMPALFIFLEMKDYIPGAWADLTVALANPIKFFSAHDTKSVKLKEAMGGL
PEKPFPLASPVASQVNGALAPTSNGSPAARAGAREEAMKEAAEPRTASLEELRELKGVVK
LQRRHEKELRELERRGARRWEELLQRGAAQLAELGPPGVGGVGACKLGPGKGSRKKRSLP
REESAGAAPGEGPEGVDGRVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMEL
AREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNSHI
QEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAEVKE
SVRACLRTCFPSEAKDKPERACECPPELCEQDPLIAKADAQESRL
Enzyme 3 Number of Residues 1185
Enzyme 3 Molecular Weight 134023.2
Enzyme 3 Theoretical pI 6.21
Enzyme 3 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 3 General Function Involved in calcium ion binding
Enzyme 3 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes
Enzyme 3 Pathways
Enzyme 3 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 95147333 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q00722 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PLCB2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >3558 bp
ATGTCTCTGCTCAACCCTGTCCTGCTGCCCCCCAAGGTGAAGGCCTATCTGAGCCAAGGG
GAGCGCTTCATCAAATGGGATGATGAAACTACAGTTGCCTCTCCAGTTATCCTCCGTGTG
GATCCTAAGGGCTACTACTTATACTGGACGTATCAAAGTAAGGAGATGGAGTTTCTGGAT
ATCACCAGCATCCGGGATACTCGCTTTGGGAAGTTTGCCAAGATGCCCAAGAGCCAGAAG
CTCCGGGACGTCTTCAACATGGACTTTCCTGATAACAGTTTCCTGCTGAAGACACTCACG
GTGGTGTCCGGCCCGGACATGGTGGACCTCACCTTCCACAACTTCGTCTCCTACAAGGAG
AACGTGGGCAAGGCCTGGGCTGAGGACGTACTGGCCCTAGTCAAACATCCGCTGACGGCC
AACGCCTCCCGCAGCACCTTCCTGGACAAGATCCTTGTGAAGCTCAAGATGCAGCTCAAC
TCTGAAGGGAAGATTCCGGTGAAGAACTTTTTCCAGATGTTTCCTGCTGACCGCAAGCGG
GTGGAAGCTGCTCTCAGTGCCTGCCACCTCCCCAAAGGCAAAAATGACGCCATCAATCCT
GAGGACTTCCCAGAACCTGTCTACAAGAGTTTCCTCATGAGCCTCTGTCCTCGGCCAGAA
ATAGATGAGATCTTCACTTCTTACCATGCTAAGGCCAAACCCTACATGACGAAGGAGCAC
CTGACCAAATTCATCAACCAGAAACAGCGGGACTCCCGGCTTAACTCCCTGCTGTTCCCG
CCAGCACGGCCTGACCAGGTGCAGGGCCTCATCGACAAGTATGAGCCCAGTGGCATCAAT
GCACAGAGGGGCCAGCTGTCACCTGAAGGCATGGTCTGGTTTCTCTGTGGGCCAGAGAAC
AGCGTGCTGGCCCAGGACAAGCTGCTGCTCCACCACGACATGACGCAGCCACTCAATCAT
TACTTCATCAACTCGTCCCACAACACCTACCTGACAGCCGGCCAGTTCTCAGGCCTCTCC
TCGGCTGAGATGTACCGCCAGGTGCTGCTCTCTGGCTGCCGTTGCGTGGAGCTAGACTGC
TGGAAGGGGAAACCCCCTGACGAGGAGCCCATTATCACCCATGGCTTCACCATGACCACA
GACATCTTCTTCAAAGAAGCAATTGAGGCTATTGCAGAAAGCGCCTTTAAGACCTCCCCC
TATCCCATCATCCTGTCGTTTGAGAACCATGTGGACTCACCCCGCCAGCAGGCTAAGATG
GCTGAGTATTGCCGGACGATCTTTGGGGATATGCTGCTCACAGAGCCCCTGGAAAAGTTC
CCACTAAAACCAGGTGTCCCCCTGCCCAGCCCTGAGGATCTCAGGGGCAAGATCCTCATC
AAGAACAAGAAGAACCAGTTTTCTGGCCCCACCTCCTCCAGTAAGGATACTGGTGGGGAG
GCTGAGGGCAGCAGCCCACCCAGTGCCCCTGCAGGTGAGGGCACAGTGTGGGCTGGCGAG
GAAGGGACTGAGCTGGAGGAGGAGGAGGTGGAAGAGGAAGAGGAGGAGGAGTCAGGAAAC
CTGGATGAAGAAGAGATTAAGAAGATGCAGTCGGATGAGGGCACAGCGGGCCTGGAAGTG
ACGGCTTATGAGGAGATGTCCAGCCTAGTCAATTACATCCAGCCCACCAAGTTCGTCTCC
TTTGAGTTCTCTGCCCAAAAGAACCGAAGTTATGTCATCTCGTCCTTCACAGAGCTCAAG
GCATATGACCTGCTCTCCAAGGCCTCGGTGCAGTTTGTGGACTACAACAAGCGCCAGATG
AGCCGCATTTACCCCAAGGGAACCCGCATGGACTCCTCCAACTACATGCCCCAGATGTTC
TGGAATGCTGGATGCCAGATGGTTGCCCTCAACTTCCAGACGATGGACTTGCCCATGCAG
CAGAACATGGCAGTATTTGAGTTCAACGGGCAGAGCGGCTACCTCCTCAAGCATGAGTTC
ATGCGCCGGCCGGACAAGCAGTTCAACCCCTTCTCAGTGGACCGCATCGACGTGGTGGTG
GCCACCACCCTTTCCATTACGGTGATCTCTGGGCAGTTCCTGTCAGAACGCAGCGTGCGC
ACCTATGTAGAAGTGGAGCTGTTTGGCCTTCCTGGGGACCCCAAGAGGCGCTATCGAACT
AAGCTGTCACCCAGTACTAACTCCATCAATCCTGTCTGGAAGGAGGAGCCCTTTGTCTTT
GAGAAGATCTTGATGCCTGAGCTGGCCTCCCTCAGAGTGGCTGTGATGGAGGAAGGCAAC
AAGTTTCTTGGACACCGCATCATCCCCATCAATGCCCTAAATTCTGGGTACCACCACCTG
TGCCTGCACAGTGAGAGCAACATGCCCCTCACCATGCCTGCGCTCTTCATCTTCCTGGAG
ATGAAGGACTACATACCTGGTGCTTGGGCAGATCTCACTGTGGCCCTCGCCAACCCCATT
AAGTTCTTCAGTGCCCATGACACGAAGTCTGTGAAGCTCAAGGAGGCCATGGGAGGTCTG
CCTGAGAAGCCCTTCCCACTGGCGAGTCCAGTTGCCAGCCAGGTCAATGGGGCGTTGGCC
CCAACGAGCAATGGGTCACCAGCAGCCAGGGCCGGGGCCAGGGAAGAGGCTATGAAAGAA
GCTGCGGAGCCGCGGACCGCCAGCCTGGAGGAGCTCCGGGAGCTAAAGGGCGTGGTGAAG
CTGCAGCGGCGGCACGAGAAGGAGCTGCGAGAGTTGGAGCGGCGCGGAGCGCGGCGCTGG
GAGGAGCTGCTGCAGCGGGGCGCGGCGCAGCTGGCGGAGCTCGGGCCACCGGGCGTGGGG
GGCGTCGGGGCCTGCAAGCTCGGTCCCGGCAAGGGCTCTCGCAAGAAGAGGAGCCTGCCC
CGCGAGGAGAGCGCCGGAGCCGCGCCGGGCGAGGGCCCTGAGGGCGTGGACGGGCGCGTG
CGGGAGCTGAAAGACAGGCTGGAGCTGGAGCTGCTGCGGCAGGGCGAGGAGCAGTACGAG
TGCGTTCTGAAGCGCAAGGAGCAGCACGTGGCCGAGCAAATCTCCAAAATGATGGAGCTG
GCCAGAGAGAAACAGGCGGCAGAGCTGAAGGCCCTGAAGGAGACGTCGGAGAACGACACC
AAAGAGATGAAGAAAAAGCTGGAGACAAAGAGACTGGAGCGGATCCAGGGCATGACCAAA
GTCACCACAGACAAGATGGCCCAGGAGAGGTTGAAGAGAGAGATTAACAACTCCCACATC
CAGGAAGTAGTGCAGGTGATCAAGCAGATGACGGAGAACTTGGAGAGGCACCAGGAGAAG
CTGGAGGAGAAGCAGGCGGCTTGCCTGGAACAGATACGGGAGATGGAAAAGCAGTTCCAG
AAGGAGGCGCTGGCAGAGTACGAGGCCAGGATGAAGGGTCTGGAGGCAGAGGTGAAGGAG
TCGGTGAGGGCCTGCCTCAGGACCTGCTTTCCCTCCGAGGCCAAGGACAAGCCTGAGAGG
GCCTGCGAGTGCCCCCCAGAGCTGTGTGAGCAGGACCCACTCATAGCAAAGGCAGATGCC
CAGGAGAGCCGCCTCTGA
Enzyme 3 GenBank Gene ID NM_004573.2 Link Image
Enzyme 3 GeneCard ID PLCB2 Link Image
Enzyme 3 GenAtlas ID PLCB2 Link Image
Enzyme 3 HGNC ID HGNC:9055 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 15q15
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Park D, Jhon DY, Kriz R, Knopf J, Rhee SG: Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2. J Biol Chem. 1992 Aug 15;267(23):16048-55. [PubMed Link Image]
  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. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  4. Jezyk MR, Snyder JT, Gershberg S, Worthylake DK, Harden TK, Sondek J: Crystal structure of Rac1 bound to its effector phospholipase C-beta2. Nat Struct Mol Biol. 2006 Dec;13(12):1135-40. Epub 2006 Nov 19. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5460
Enzyme 4 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3
Enzyme 4 Synonyms
  1. Phosphoinositide phospholipase C-beta-3
  2. Phospholipase C-beta-3
  3. PLC-beta-3
Enzyme 4 Gene Name PLCB3
Enzyme 4 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3
MAGAQPGVHALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNME
VDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNF
MAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFS
ADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPY
LTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYL
GGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRC
VELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAK
QQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPDS
AGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGD
EGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPV
KFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYM
PQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIV
DGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEP
FDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLI
YTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQL
GSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRGH
KALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVED
TKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQF
KRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLE
EAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGLG
DGPLVACASNGHAPGSSGHLSGADSESQEENTQL
Enzyme 4 Number of Residues 1234
Enzyme 4 Molecular Weight 138797.7
Enzyme 4 Theoretical pI 5.66
Enzyme 4 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 4 General Function Involved in calcium ion binding
Enzyme 4 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes
Enzyme 4 Pathways
Enzyme 4 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 148745659 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q01970 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PLCB3_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >3705 bp
ATGGCGGGCGCCCAGCCCGGCGTCCACGCGCTGCAGTTGGAGCCGCCCACCGTGGTGGAG
ACCCTGCGGCGCGGGAGTAAGTTCATCAAATGGGACGAGGAGACCTCCAGTCGGAACCTG
GTGACCCTGCGTGTGGACCCCAATGGCTTCTTCTTGTACTGGACGGGCCCCAACATGGAG
GTGGACACACTGGACATCAGTTCCATCAGGGACACACGGACAGGCCGGTACGCCCGCCTG
CCCAAGGACCCCAAGATCCGGGAAGTTCTGGGCTTTGGGGGTCCCGATGCCCGGCTGGAG
GAGAAGCTGATGACGGTGGTGTCTGGGCCAGACCCGGTGAACACAGTGTTCTTGAACTTC
ATGGCCGTGCAGGATGACACAGCCAAGGTCTGGTCTGAGGAGCTATTCAAGCTGGCTATG
AACATCCTGGCTCAGAACGCCTCCCGGAACACCTTCCTGCGCAAAGCATACACGAAGCTG
AAGCTGCAGGTGAACCAGGATGGTCGGATCCCCGTCAAGAACATCCTGAAGATGTTCTCA
GCAGACAAGAAGCGGGTGGAGACTGCGCTGGAATCCTGTGGCCTCAAATTCAACCGGAGT
GAGTCCATCCGGCCTGATGAGTTTTCCTTGGAAATCTTTGAGCGGTTCCTGAACAAGCTG
TGTCTGCGGCCGGACATTGACAAGATCCTGCTGGAGATAGGCGCCAAGGGCAAGCCATAC
CTGACGCTGGAGCAGCTCATGGACTTCATCAACCAGAAGCAACGCGACCCGAGACTCAAC
GAAGTGCTGTACCCGCCCCTGCGGCCCTCCCAGGCCCGGCTGCTCATCGAAAAGTATGAG
CCCAACCAGCAGTTTCTGGAGCGAGACCAGATGTCCATGGAGGGCTTTAGCCGCTACCTG
GGAGGCGAGGAGAATGGCATCCTGCCCCTGGAAGCCCTGGATCTGAGCACGGACATGACC
CAGCCACTGAGTGCCTACTTCATCAACTCCTCGCATAACACCTATCTCACTGCGGGGCAG
CTGGCTGGGACCTCGTCGGTGGAGATGTACCGCCAGGCACTACTATGGGGCTGCCGCTGC
GTGGAGCTGGACGTGTGGAAGGGACGGCCGCCTGAGGAGGAACCCTTCATTACCCACGGC
TTCACCATGACCACAGAGGTGCCTCTGCGCGACGTGCTGGAGGCCATTGCCGAGACTGCC
TTCAAGACCTCGCCCTACCCCGTCATCCTCTCCTTCGAGAACCATGTGGACTCGGCAAAG
CAACAGGCAAAGATGGCTGAGTACTGCCGCTCCATCTTTGGAGACGCGCTACTCATCGAG
CCTCTGGACAAGTACCCGCTGGCCCCAGGCGTTCCCCTGCCCAGCCCCCAGGACCTGATG
GGCCGTATCCTGGTGAAGAACAAGAAGCGGCACCGACCCAGCGCAGGTGGCCCAGACAGC
GCCGGGCGCAAGCGGCCCCTGGAGCAGAGCAATTCTGCCCTGAGCGAGAGCTCCGCGGCC
ACCGAGCCCTCCTCCCCGCAGCTGGGGTCTCCCAGCTCTGACAGCTGCCCAGGCCTGAGC
AATGGGGAGGAGGTAGGGCTTGAGAAGCCCAGCCTGGAGCCTCAGAAGTCTCTGGGTGAC
GAGGGCCTGAACCGAGGCCCCTATGTTCTTGGACCTGCTGACCGTGAGGATGAGGAGGAA
GATGAGGAAGAGGAGGAACAGACAGACCCCAAAAAGCCAACTACAGATGAGGGCACAGCC
AGCAGCGAGGTGAATGCCACTGAGGAGATGTCCACGCTTGTCAACTACATCGAACCTGTC
AAGTTCAAGTCCTTTGAGGCTGCTCGAAAGAGGAACAAATGCTTCGAGATGTCGTCCTTT
GTGGAGACCAAGGCCATGGAGCAACTGACCAAGAGCCCCATGGAGTTTGTGGAATACAAC
AAGCAGCAGCTCAGCCGCATCTACCCCAAGGGCACCCGCGTGGACTCCTCCAACTACATG
CCCCAGCTCTTCTGGAACGTAGGGTGCCAGCTTGTTGCGCTCAACTTCCAGACCCTCGAT
GTGGCGATGCAGCTCAACGCGGGCGTTTTTGAGTACAACGGGCGCAGCGGGTACCTGCTC
AAGCCGGAGTTCATGCGGCGGCCGGACAAGTCCTTCGACCCCTTCACTGAGGTCATCGTG
GATGGCATCGTGGCCAATGCCTTGCGGGTCAAGGTGATCTCAGGGCAGTTCCTGTCCGAC
AGGAAGGTGGGCATCTACGTGGAGGTGGACATGTTTGGCCTCCCTGTTGATACGCGGCGC
AAGTACCGCACCCGGACCTCTCAGGGGAACTCGTTCAACCCCGTGTGGGACGAAGAGCCC
TTCGACTTCCCCAAGGTGGTGCTGCCCACGCTGGCTTCACTTCGCATTGCAGCCTTTGAG
GAGGGGGGTAAATTCGTAGGGCACCGGATCCTGCCTGTCTCTGCCATCCGCTCCGGATAC
CACTACGTCTGCCTGCGGAACGAGGCCAACCAACCGCTGTGCCTGCCGGCCCTGCTCATC
TACACCGAAGCCTCGGACTACATTCCTGACGACCACCAGGACTATGCGGAGGCCCTGATC
AACCCCATTAAGCACGTCAGCCTGATGGACCAGAGGGCCCGGCAGCTGGCCGCCCTCATT
GGGGAGAGTGAGGCTCAGGCTGGCCAAGAGACGTGCCAGGACACCCAGTCTCAGCAGCTG
GGGTCTCAGCCGTCCTCAAACCCCACCCCCAGCCCACTGGATGCCTCCCCCCGCCGGCCC
CCTGGCCCCACCACCTCCCCTGCCAGCACCTCCCTCAGCAGCCCAGGGCAGCGTGATGAT
CTCATCGCCAGCATCCTCTCAGAGGTGGCCCCCACCCCGCTGGATGAGCTCCGAGGTCAC
AAGGCTCTGGTCAAGCTCCGGAGCCGGCAAGAGCGAGACCTGCGGGAGCTGCGCAAGAAG
CATCAGCGGAAGGCAGTCACCCTCACCCGCCGCCTGCTGGATGGCCTGGCTCAGGCACAG
GCTGAGGGCAGGTGCCGGCTGCGGCCAGGTGCCCTAGGTGGGGCCGCTGATGTGGAGGAC
ACGAAGGAGGGGGAGGACGAGGCAAAGCGGTATCAGGAGTTCCAGAACAGACAGGTGCAG
AGCCTGCTGGAGCTGCGGGAGGCCCAGGTGGACGCAGAGGCCCAGCGGAGGCTGGAACAC
CTGAGACAGGCTCTGCAGCGGCTCAGGGAGGTCGTCCTTGATGCAAACACAACTCAGTTC
AAGAGGCTGAAAGAGATGAACGAGAGGGAGAAGAAGGAGCTGCAGAAGATCCTGGACAGA
AAGCGCCATAACAGCATCTCGGAGGCCAAGATGAGGGACAAGCATAAGAAGGAGGCGGAA
CTGACGGAGATTAACCGTCGGCACATCACTGAGTCAGTCAACTCCATCCGTCGGCTGGAG
GAGGCCCAGAAGCAGCGGCATGACCGTCTTGTGGCTGGGCAGCAGCAGGTCCTGCAACAG
CTGGCAGAAGAGGAGCCCAAGCTGCTGGCCCAGCTGGCCCAGGAGTGTCAGGAGCAGCGG
GCGAGGCTCCCCCAGGAGATCCGCCGGAGCCTGCTGGGCGAGATGCCAGAGGGGCTGGGG
GACGGGCCTCTGGTGGCCTGTGCCAGCAACGGTCACGCACCCGGGAGCAGCGGGCACCTG
TCGGGCGCTGACTCGGAGAGCCAGGAGGAGAACACGCAGCTCTGA
Enzyme 4 GenBank Gene ID BC142681 Link Image
Enzyme 4 GeneCard ID PLCB3 Link Image
Enzyme 4 GenAtlas ID PLCB3 Link Image
Enzyme 4 HGNC ID HGNC:9056 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 11q13
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Mazuruk K, Schoen TJ, Chader GJ, Rodriguez IR: Structural organization and expression of the human phosphatidylinositol-specific phospholipase C beta-3 gene. Biochem Biophys Res Commun. 1995 Jul 6;212(1):190-5. [PubMed Link Image]
  2. Lagercrantz J, Carson E, Phelan C, Grimmond S, Rosen A, Dare E, Nordenskjold M, Hayward NK, Larsson C, Weber G: Genomic organization and complete cDNA sequence of the human phosphoinositide-specific phospholipase C beta 3 gene (PLCB3). Genomics. 1995 Apr 10;26(3):467-72. [PubMed Link Image]
  3. 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. Carozzi AJ, Kriz RW, Webster C, Parker PJ: Identification, purification and characterization of a novel phosphatidylinositol-specific phospholipase C, a third member of the beta subfamily. Eur J Biochem. 1992 Dec 1;210(2):521-9. [PubMed Link Image]
  5. 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]
  6. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  7. 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]
  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]
  9. 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]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5462
Enzyme 5 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2
Enzyme 5 Synonyms
  1. Phosphoinositide phospholipase C-gamma-2
  2. Phospholipase C-IV
  3. PLC-IV
  4. Phospholipase C-gamma-2
  5. PLC-gamma-2
Enzyme 5 Gene Name PLCG2
Enzyme 5 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2
MSTTVNVDSLAEYEKSQIKRALELGTVMTVFSFRKSTPERRTVQVIMETRQVAWSKTADK
IEGFLDIMEIKEIRPGKNSKDFERAKAVRQKEDCCFTILYGTQFVLSTLSLAADSKEDAV
NWLSGLKILHQEAMNASTPTIIESWLRKQIYSVDQTRRNSISLRELKTILPLINFKVSSA
KFLKDKFVEIGAHKDELSFEQFHLFYKKLMFEQQKSILDEFKKDSSVFILGNTDRPDASA
VYLHDFQRFLIHEQQEHWAQDLNKVRERMTKFIDDTMRETAEPFLFVDEFLTYLFSRENS
IWDEKYDAVDMQDMNNPLSHYWISSSHNTYLTGDQLRSESSPEAYIRCLRMGCRCIELDC
WDGPDGKPVIYHGWTRTTKIKFDDVVQAIKDHAFVTSSFPVILSIEEHCSVEQQRHMAKA
FKEVFGDLLLTKPTEASADQLPSPSQLREKIIIKHKKLGPRGDVDVNMEDKKDEHKQQGE
LYMWDSIDQKWTRHYCAIADAKLSFSDDIEQTMEEEVPQDIPPTELHFGEKWFHKKVEKR
TSAEKLLQEYCMETGGKDGTFLVRESETFPNDYTLSFWRSGRVQHCRIRSTMEGGTLKYY
LTDNLTFSSIYALIQHYRETHLRCAEFELRLTDPVPNPNPHESKPWYYDSLSRGEAEDML
MRIPRDGAFLIRKREGSDSYAITFRARGKVKHCRINRDGRHFVLGTSAYFESLVELVSYY
EKHSLYRKMRLRYPVTPELLERYNMERDINSLYDVSRMYVDPSEINPSMPQRTVKALYDY
KAKRSDELSFCRGALIHNVSKEPGGWWKGDYGTRIQQYFPSNYVEDISTADFEELEKQII
EDNPLGSLCRGILDLNTYNVVKAPQGKNQKSFVFILEPKQQGDPPVEFATDRVEELFEWF
QSIREITWKIDTKENNMKYWEKNQSIAIELSDLVVYCKPTSKTKDNLENPDFREIRSFVE
TKADSIIRQKPVDLLKYNQKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTADKY
MQMNHALFSLNGRTGYVLQPESMRTEKYDPMPPESQRKILMTLTVKVLGARHLPKLGRSI
ACPFVEVEICGAEYDNNKFKTTVVNDNGLSPIWAPTQEKVTFEIYDPNLAFLRFVVYEED
MFSDPNFLAHATYPIKAVKSGFRSVPLKNGYSEDIELASLLVFCEMRPVLESEEELYSSC
RQLRRRQEELNNQLFLYDTHQNLRNANRDALVKEFSVNENQLQLYQEKCNKRLREKRVSN
SKFYS
Enzyme 5 Number of Residues 1265
Enzyme 5 Molecular Weight 147868.7
Enzyme 5 Theoretical pI 6.60
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • molecular transducer activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • protein binding
  • signal transducer activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid catabolic process
  • phospholipid metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 5 General Function Involved in phosphoinositide phospholipase C activity
Enzyme 5 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling
Enzyme 5 Pathways
Enzyme 5 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 117320537 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P16885 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PLCG2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >3798 bp
ATGTCCACCACGGTCAATGTAGATTCCCTTGCGGAATATGAGAAGAGCCAGATCAAGAGA
GCCCTGGAGCTGGGGACGGTGATGACTGTGTTCAGCTTCCGCAAGTCCACCCCCGAGCGG
AGAACCGTCCAGGTGATCATGGAGACGCGGCAGGTGGCCTGGAGCAAGACCGCCGACAAG
ATCGAGGGCTTCTTGGATATCATGGAAATAAAAGAAATCCGCCCAGGGAAGAACTCCAAA
GATTTCGAGCGAGCAAAAGCAGTTCGCCAGAAAGAAGACTGCTGCTTCACCATCCTATAT
GGCACTCAGTTCGTCCTCAGCACGCTCAGCTTGGCAGCTGACTCTAAAGAGGATGCAGTT
AACTGGCTCTCTGGCTTGAAAATCTTACACCAGGAAGCGATGAATGCGTCCACGCCCACC
ATTATCGAGAGTTGGCTGAGAAAGCAGATATATTCTGTGGATCAAACCAGAAGAAACAGC
ATCAGTCTCCGAGAGTTGAAGACCATCTTGCCCCTGATCAACTTTAAAGTGAGCAGTGCC
AAGTTCCTTAAAGATAAGTTTGTGGAAATAGGAGCACACAAAGATGAGCTCAGCTTTGAA
CAGTTCCATCTCTTCTATAAAAAACTTATGTTTGAACAGCAAAAATCGATTCTCGATGAA
TTCAAAAAGGATTCGTCCGTGTTCATCCTGGGGAACACTGACAGGCCGGATGCCTCTGCT
GTTTACCTGCATGACTTCCAGAGGTTTCTCATACATGAACAGCAGGAGCATTGGGCTCAG
GATCTGAACAAAGTCCGTGAGCGGATGACAAAGTTCATTGATGACACCATGCGTGAAACT
GCTGAGCCTTTCTTGTTTGTGGATGAGTTCCTCACGTACCTGTTTTCACGAGAAAACAGC
ATCTGGGATGAGAAGTATGACGCGGTGGACATGCAGGACATGAACAACCCCCTGTCTCAT
TACTGGATCTCCTCGTCACATAACACGTACCTTACAGGTGACCAGCTGCGGAGCGAGTCG
TCCCCAGAAGCTTACATCCGCTGCCTGCGCATGGGCTGTCGCTGCATTGAACTGGACTGC
TGGGACGGGCCCGATGGGAAGCCGGTCATCTACCATGGCTGGACGCGGACTACCAAGATC
AAGTTTGACGACGTCGTGCAGGCCATCAAAGACCACGCCTTTGTTACCTCGAGCTTCCCA
GTGATCCTGTCCATCGAGGAGCACTGCAGCGTGGAGCAACAGCGTCACATGGCCAAGGCC
TTCAAGGAAGTATTTGGCGACCTGCTGTTGACGAAGCCCACGGAGGCCAGTGCTGACCAG
CTGCCCTCGCCCAGCCAGCTGCGGGAGAAGATCATCATCAAGCATAAGAAGCTGGGCCCC
CGAGGCGATGTGGATGTCAACATGGAGGACAAGAAGGACGAACACAAGCAACAGGGGGAG
CTGTACATGTGGGATTCCATTGACCAGAAATGGACTCGGCACTACTGCGCCATTGCCGAT
GCCAAGCTGTCCTTCAGTGATGACATTGAACAGACTATGGAGGAGGAAGTGCCCCAGGAT
ATACCCCCTACAGAACTACATTTTGGGGAGAAATGGTTCCACAAGAAGGTGGAGAAGAGG
ACGAGTGCCGAGAAGTTGCTGCAGGAATACTGCATGGAGACGGGGGGCAAGGATGGCACC
TTCCTGGTTCGGGAGAGCGAGACCTTCCCCAATGACTACACCCTGTCCTTCTGGCGGTCA
GGCCGGGTCCAGCACTGCCGGATCCGCTCCACCATGGAGGGCGGGACCCTGAAATACTAC
TTGACTGACAACCTCACCTTCAGCAGCATCTATGCCCTCATCCAGCACTACCGCGAGACG
CACCTGCGCTGCGCCGAGTTCGAGCTGCGGCTCACGGACCCTGTGCCCAACCCCAACCCC
CACGAGTCCAAGCCGTGGTACTATGACAGCCTGAGCCGCGGAGAGGCAGAGGACATGCTG
ATGAGGATTCCCCGGGACGGGGCCTTCCTGATCCGGAAGCGAGAGGGGAGCGACTCCTAT
GCCATCACCTTCAGGGCTAGGGGCAAGGTAAAGCATTGTCGCATCAACCGGGACGGCCGG
CACTTTGTGCTGGGGACCTCCGCCTATTTTGAGAGTCTGGTGGAGCTCGTCAGTTACTAC
GAGAAGCATTCACTCTACCGAAAGATGAGACTGCGCTACCCCGTGACCCCCGAGCTCCTG
GAGCGCTACAATATGGAAAGAGATATAAACTCCCTCTACGACGTCAGCAGAATGTATGTG
GATCCCAGTGAAATCAATCCGTCCATGCCTCAGAGAACCGTGAAAGCTCTGTATGACTAC
AAAGCCAAGCGAAGCGATGAGCTGAGCTTCTGCCGTGGTGCCCTCATCCACAATGTCTCC
AAGGAGCCCGGGGGCTGGTGGAAAGGAGACTATGGAACCAGGATCCAGCAGTACTTCCCA
TCCAACTACGTCGAGGACATCTCAACTGCAGACTTCGAGGAGCTAGAAAAGCAGATTATT
GAAGACAATCCCTTAGGGTCTCTTTGCAGAGGAATATTGGACCTCAATACCTATAACGTC
GTGAAAGCCCCTCAGGGAAAAAACCAGAAGTCCTTTGTCTTCATCCTGGAGCCCAAGCAG
CAGGGCGATCCTCCGGTGGAGTTTGCCACAGACAGGGTGGAGGAGCTCTTTGAGTGGTTT
CAGAGCATCCGAGAGATCACCTGGAAGATTGACACCAAGGAGAACAACATGAAGTACTGG
GAGAAGAACCAGTCCATCGCCATCGAGCTCTCTGACCTGGTTGTCTACTGCAAACCAACC
AGCAAAACCAAGGACAACTTAGAAAATCCTGACTTCCGAGAAATCCGCTCCTTTGTGGAG
ACGAAGGCTGACAGCATCATCAGACAGAAGCCCGTCGACCTCCTGAAGTACAATCAAAAG
GGCCTGACCCGCGTCTACCCAAAGGGACAAAGAGTTGACTCTTCAAACTACGACCCCTTC
CGCCTCTGGCTGTGCGGTTCTCAGATGGTGGCACTCAATTTCCAGACGGCAGATAAGTAC
ATGCAGATGAATCACGCATTGTTTTCTCTCAATGGGCGCACGGGCTACGTTCTGCAGCCT
GAGAGCATGAGGACAGAGAAATATGACCCGATGCCACCCGAGTCCCAGAGGAAGATCCTG
ATGACGCTGACAGTCAAGGTTCTCGGTGCTCGCCATCTCCCCAAACTTGGACGAAGTATT
GCCTGTCCCTTTGTAGAAGTGGAGATCTGTGGAGCCGAGTATGACAACAACAAGTTCAAG
ACGACGGTTGTGAATGATAATGGCCTCAGCCCTATCTGGGCTCCAACACAGGAGAAGGTG
ACATTTGAAATTTATGACCCAAACCTGGCATTTCTGCGCTTTGTGGTTTATGAAGAAGAT
ATGTTCAGCGATCCCAACTTTCTTGCTCATGCCACTTACCCCATTAAAGCAGTCAAATCA
GGATTCAGGTCCGTTCCTCTGAAGAATGGGTACAGCGAGGACATAGAGCTGGCTTCCCTC
CTGGTTTTCTGTGAGATGCGGCCAGTCCTGGAGAGCGAAGAGGAACTTTACTCCTCCTGT
CGCCAGCTGAGGAGGCGGCAAGAAGAACTGAACAACCAGCTCTTTCTGTATGACACACAC
CAGAACTTGCGCAATGCCAACCGGGATGCCCTGGTTAAAGAGTTCAGTGTTAATGAGAAC
CAGCTCCAGCTGTACCAGGAGAAATGCAACAAGAGGTTAAGAGAGAAGAGAGTCAGCAAC
AGCAAGTTTTACTCATAG
Enzyme 5 GenBank Gene ID NM_002661.2 Link Image
Enzyme 5 GeneCard ID PLCG2 Link Image
Enzyme 5 GenAtlas ID PLCG2 Link Image
Enzyme 5 HGNC ID HGNC:9066 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 16q24.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Ohta S, Matsui A, Nazawa Y, Kagawa Y: Complete cDNA encoding a putative phospholipase C from transformed human lymphocytes. FEBS Lett. 1988 Dec 19;242(1):31-5. [PubMed Link Image]
  2. Kemmer D, Podowski RM, Arenillas D, Lim J, Hodges E, Roth P, Sonnhammer EL, Hoog C, Wasserman WW: NovelFam3000--uncharacterized human protein domains conserved across model organisms. BMC Genomics. 2006 Mar 13;7:48. [PubMed Link Image]
  3. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [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. Ozdener F, Dangelmaier C, Ashby B, Kunapuli SP, Daniel JL: Activation of phospholipase Cgamma2 by tyrosine phosphorylation. Mol Pharmacol. 2002 Sep;62(3):672-9. [PubMed Link Image]
  6. Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC: Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. Anal Chem. 2004 May 15;76(10):2763-72. [PubMed Link Image]
  7. 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]
  8. 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5476
Enzyme 6 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1
Enzyme 6 Synonyms
  1. PLC-148
  2. Phosphoinositide phospholipase C-gamma-1
  3. Phospholipase C-II
  4. PLC-II
  5. Phospholipase C-gamma-1
  6. PLC-gamma-1
Enzyme 6 Gene Name PLCG1
Enzyme 6 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1
MAGAASPCANGCGPGAPSDAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQI
TWSRGADKIEGAIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTL
SLQATSEDEVNMWIKGLTWLMEDTLQAPTPLQIERWLRKQFYSVDRNREDRISAKDLKNM
LSQVNYRVPNMRFLRERLTDLEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLEASTLRA
GERPELCRVSLPEFQQFLLDYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDEFVT
FLFSKENSVWNSQLDAVCPDTMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMG
CRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIA
QQRNMAQYFKKVLGDTLLTKPVEISADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSMM
YSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEVSS
STELHSNEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFW
RNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQT
NAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQE
GQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNP
GFYVEANPMPTFKCAVKALFDYKAQREDELTFIKSAIIQNVEKQEGGWWRGDYGGKKQLW
FPSNYVEEMVNPVALEPEREHLDENSPLGDLLRGVLDVPACQIAIRPEGKNNRLFVFSIS
MASVAHWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKIMERRKKIALELSELVVYC
RPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDS
SNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMTGRHCGYVLQPSTMRDEAFDPFDKS
SLRGLEPCAISIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVW
PAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDL
ELASLLIKIDIFPAKENGDLSPFSGTSLRERGSDASGQLFHGRAREGSFESRYQQPFEDF
RISQEHLADHFDSRERRAPRRTRVNGDNRL
Enzyme 6 Number of Residues 1290
Enzyme 6 Molecular Weight 148530.8
Enzyme 6 Theoretical pI 5.91
Enzyme 6 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • molecular transducer activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • protein binding
  • signal transducer activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid catabolic process
  • phospholipid metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 6 General Function Involved in calcium ion binding
Enzyme 6 Specific Function PLC-gamma is a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase
Enzyme 6 Pathways
Enzyme 6 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 3336979 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P19174 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PLCG1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >3873 bp
ATGGCGGGCGCCGCGTCCCCTTGCGCCAACGGCTGCGGGCCCGGCGCGCCCTCGGACGCC
GAGGTGCTGCACCTCTGCCGCAGCCTCGAGGTGGGCACCGTCATGACTTTGTTCTACTCC
AAGAAGTCGCAGCGACCCGAGCGGAAGACCTTCCAGGTCAAGCTGGAGACGCGCCAGATC
ACGTGGAGCCGGGGCGCCGACAAGATCGAGGGGGCCATTGACATTCGTGAAATTAAGGAG
ATCCGCCCAGGGAAGACCTCACGGGACTTTGATCGCTATCAAGAGGACCCAGCTTTCCGG
CCGGACCAGTCACATTGCTTTGTCATTCTCTATGGAATGGAATTTCGCCTGAAAACGCTG
AGCCTGCAAGCCACATCTGAGGATGAAGTGAACATGTGGATCAAGGGCTTAACTTGGCTG
ATGGAGGATACATTGCAGGCACCCACACCCCTGCAGATTGAGAGGTGGCTCCGGAAGCAG
TTTTACTCAGTGGATCGGAATCGTGAGGATCGTATATCAGCCAAGGACCTGAAGAACATG
CTGTCCCAGGTCAACTACCGGGTCCCCAACATGCGCTTCCTCCGAGAGCGGCTGACGGAC
CTGGAGCAGCGCAGCGGGGACATCACCTACGGGCAGTTTGCTCAGCTGTACCGCAGCCTC
ATGTACAGCGCCCAGAAGACGATGGACCTCCCCTTCTTGGAAGCCAGTACTCTGAGGGCT
GGGGAGCGGCCGGAGCTTTGCCGAGTGTCCCTTCCTGAGTTCCAGCAGTTCCTTCTTGAC
TACCAGGGGGAGCTGTGGGCTGTTGATCGCCTCCAGGTGCAGGAGTTCATGCTCAGCTTC
CTCCGAGACCCCTTACGAGAGATCGAGGAGCCATACTTCTTCCTGGATGAGTTTGTCACC
TTCCTGTTCTCCAAAGAGAACAGTGTGTGGAACTCGCAGCTGGATGCAGTATGCCCGGAC
ACCATGAACAACCCTCTTTCCCACTACTGGATCTCCTCCTCGCACAACACGTACCTGACC
GGGGACCAGTTCTCCAGTGAGTCCTCCTTGGAAGCCTATGCTCGCTGCCTGCGGATGGGC
TGTCGCTGCATTGAGTTGGACTGCTGGGACGGCCCGGATGGGATGCCAGTTATTTACCAT
GGGCACACCCTTACCACCAAGATCAAGTTCTCAGATGTCCTGCACACCATCAAGGAGCAT
GCCTTTGTGGCCTCAGAGTACCCAGTCATCCTGTCCATTGAGGACCACTGCAGCATTGCC
CAGCAGAGAAACATGGCCCAATACTTCAAGAAGGTGCTGGGGGACACACTCCTCACCAAG
CCCGTGGAGATCTCTGCCGACGGGCTCCCCTCACCCAACCAGCTTAAGAGGAAGATCCTC
ATCAAGCACAAGAAGCTGGCTGAGGGCAGTGCCTACGAGGAGGTGCCTACATCCATGATG
TACTCTGAGAACGACATCAGCAACTCTATCAAGAATGGCATCCTCTACCTGGAGGACCCT
GTGAACCACGAATGGTATCCCCACTACTTTGTTCTGACCAGCAGCAAGATCTACTACTCT
GAGGAGACCAGCAGTGACCAGGGCAACGAGGATGAGGAGGAGCCCAAGGAGGTCAGCAGC
AGCACAGAGCTGCACTCCAATGAGAAGTGGTTCCATGGGAAGCTAGGGGCAGGGCGTGAC
GGGCGTCACATCGCTGAGCGCCTGCTTACTGAGTACTGCATCGAGACCGGAGCCCCTGAC
GGCTCCTTCCTCGTGCGAGAGAGTGAGACCTTCGTGGGCGACTACACGCTCTCTTTCTGG
CGGAACGGGAAAGTCCAGCACTGCCGTATCCACTCCCGGCAAGATGCTGGGACCCCCAAG
TTCTTCTTGACAGACAACCTCGTCTTTGACTCCCTCTATGACCTCATCACGCACTACCAG
CAGGTGCCCCTGCGCTGTAATGAGTTTGAGATGCGACTTTCAGAGCCTGTCCCACAGACC
AACGCCCACGAGAGCAAAGAGTGGTACCACGCGAGCCTGACCAGAGCACAGGCTGAGCAC
ATGCTAATGCGCGTCCCTCGTGATGGGGCCTTCCTGGTGCGGAAGCGGAATGAACCCAAC
TCATATGCCATCTCTTTCCGGGCTGAGGGCAAGATCAAGCATTGCCGTGTCCAGCAAGAG
GGCCAGACAGTGATGCTAGGGAACTCGGAGTTCGACAGCCTTGTTGACCTCATCAGCTAC
TATGAGAAACACCCGCTATACCGCAAGATGAAGCTGCGCTATCCCATCAACGAGGAGGCA
CTGGAGAAGATTGGCACAGCTGAGCCTGACTACGGGGCCCTGTATGAGGGACGCAACCCT
GGCTTCTATGTAGAGGCAAACCCTATGCCAACTTTCAAGTGTGCAGTCAAAGCCCTCTTT
GACTACAAGGCCCAGAGGGAGGACGAGCTGACCTTCATCAAGAGCGCCATCATCCAGAAT
GTGGAGAAGCAAGAGGGAGGCTGGTGGCGAGGGGACTACGGAGGGAAGAAGCAGCTGTGG
TTCCCATCAAACTACGTGGAAGAGATGGTCAACCCCGTGGCCCTGGAGCCGGAGAGGGAG
CACTTGGACGAGAACAGCCCCCTAGGGGACTTGCTGCGGGGGGTCTTGGATGTGCCGGCT
TGTCAGATTGCCATCCGTCCTGAGGGCAAGAACAACCGGCTCTTCGTCTTCTCCATCAGC
ATGGCGTCGGTGGCCCACTGGTCCCTGGATGTTGCTGCCGACTCACAGGAGGAGCTGCAG
GACTGGGTGAAAAAGATCCGTGAAGTGGCCCAGACAGCAGACGCCAGGCTCACTGAAGGG
AAGATAATGGAACGGAGGAAGAAGATTGCCCTGGAGCTCTCTGAACTTGTCGTCTACTGC
CGGCCTGTTCCCTTTGATGAAGAGAAGATTGGCACAGAACGTGCTTGCTACCGGGACATG
TCATCCTTCCCGGAAACCAAGGCTGAGAAATACGTGAACAAGGCCAAAGGCAAGAAGTTC
CTTCAGTACAATCGACTGCAGCTCTCCCGCATCTACCCCAAGGGCCAGCGACTGGATTCC
TCCAACTACGATCCTTTGCCCATGTGGATCTGTGGCAGTCAGCTTGTGGCCCTCAACTTC
CAGACCCCTGACAAGCCTATGCAGATGAACCAGGCCCTCTTCATGACGGGCAGGCACTGT
GGCTACGTGCTGCAGCCAAGCACCATGCGGGATGAGGCCTTCGACCCCTTTGACAAGAGC
AGCCTCCGCGGGCTGGAGCCATGTGCCATCTCTATTGAGGTGCTGGGGGCCCGACATCTG
CCAAAGAATGGCCGAGGCATTGTGTGTCCTTTTGTGGAGATTGAGGTGGCTGGAGCTGAG
TATGACAGCACCAAGCAGAAGACAGAGTTTGTGGTGGACAATGGACTCAACCCTGTATGG
CCAGCCAAGCCCTTCCACTTCCAGATCAGTAACCCTGAATTTGCCTTTCTGCGCTTCGTG
GTGTATGAGGAAGACATGTTTAGTGACCAGAATTTCCTGGCTCAGGCTACTTTCCCAGTA
AAAGGCCTGAAGACAGGATACAGAGCAGTGCCTTTGAAGAACAACTACAGTGAGGACCTG
GAGTTGGCCTCCCTGCTGATCAAGATTGACATTTTCCCTGCCAAGGAGAATGGTGACCTC
AGTCCCTTCAGTGGTACGTCCCTGCGGGAGCGGGGCTCAGATGCCTCAGGCCAGCTGTTT
CATGGCCGAGCCCGGGAAGGCTCCTTTGAATCCCGCTACCAGCAGCCGTTTGAGGACTTC
CGCATCTCCCAGGAGCATCTCGCAGACCATTTTGACAGTCGAGAACGAAGGGCCCCAAGA
AGGACTCGGGTCAATGGAGACAACCGCCTCTAG
Enzyme 6 GenBank Gene ID AL022394 Link Image
Enzyme 6 GeneCard ID PLCG1 Link Image
Enzyme 6 GenAtlas ID PLCG1 Link Image
Enzyme 6 HGNC ID HGNC:9065 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 20q12-q13.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Burgess WH, Dionne CA, Kaplow J, Mudd R, Friesel R, Zilberstein A, Schlessinger J, Jaye M: Characterization and cDNA cloning of phospholipase C-gamma, a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase. Mol Cell Biol. 1990 Sep;10(9):4770-7. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. 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. Zhang W, Sloan-Lancaster J, Kitchen J, Trible RP, Samelson LE: LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell. 1998 Jan 9;92(1):83-92. [PubMed Link Image]
  5. Lindholm CK, Gylfe E, Zhang W, Samelson LE, Welsh M: Requirement of the Src homology 2 domain protein Shb for T cell receptor-dependent activation of the interleukin-2 gene nuclear factor for activation of T cells element in Jurkat T cells. J Biol Chem. 1999 Sep 24;274(39):28050-7. [PubMed Link Image]
  6. Felschow DM, Civin CI, Hoehn GT: Characterization of the tyrosine kinase Tnk1 and its binding with phospholipase C-gamma1. Biochem Biophys Res Commun. 2000 Jun 24;273(1):294-301. [PubMed Link Image]
  7. Korkaya H, Jameel S, Gupta D, Tyagi S, Kumar R, Zafrullah M, Mazumdar M, Lal SK, Xiaofang L, Sehgal D, Das SR, Sahal D: The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK. J Biol Chem. 2001 Nov 9;276(45):42389-400. Epub 2001 Aug 22. [PubMed Link Image]
  8. Rebhun JF, Chen H, Quilliam LA: Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral. J Biol Chem. 2000 May 5;275(18):13406-10. [PubMed Link Image]
  9. Taguchi T, Kiyokawa N, Takenouch H, Matsui J, Tang WR, Nakajima H, Suzuki K, Shiozawa Y, Saito M, Katagiri YU, Takahashi T, Karasuyama H, Matsuo Y, Okita H, Fujimoto J: Deficiency of BLNK hampers PLC-gamma2 phosphorylation and Ca2+ influx induced by the pre-B-cell receptor in human pre-B cells. Immunology. 2004 Aug;112(4):575-82. [PubMed Link Image]
  10. 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]
  11. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  12. 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]
  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. 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]
  15. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  16. 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]
  17. 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]
  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. 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]
  20. Kohda D, Hatanaka H, Odaka M, Mandiyan V, Ullrich A, Schlessinger J, Inagaki F: Solution structure of the SH3 domain of phospholipase C-gamma. Cell. 1993 Mar 26;72(6):953-60. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5479
Enzyme 7 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1
Enzyme 7 Synonyms
  1. Phosphoinositide phospholipase C-delta-1
  2. Phospholipase C-III
  3. PLC-III
  4. Phospholipase C-delta-1
  5. PLC-delta-1
Enzyme 7 Gene Name PLCD1
Enzyme 7 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1
MDSGRDFLTLHGLQDDEDLQALLKGSQLLKVKSSSWRRERFYKLQEDCKTIWQESRKVMR
TPESQLFSIEDIQEVRMGHRTEGLEKFARDVPEDRCFSIVFKDQRNTLDLIAPSPADAQH
WVLGLHKIIHHSGSMDQRQKLQHWIHSCLRKADKNKDNKMSFKELQNFLKELNIQVDDSY
ARKIFRECDHSQTDSLEDEEIEAFYKMLTQRVEIDRTFAEAAGSGETLSVDQLVTFLQHQ
QREEAAGPALALSLIERYEPSETAKAQRQMTKDGFLMYLLSADGSAFSLAHRRVYQDMGQ
PLSHYLVSSSHNTYLLEDQLAGPSSTEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTF
TSKILFCDVLRAIRDYAFKASPYPVILSLENHCTLEQQRVMARHLHAILGPMLLNRPLDG
VTNSLPSPEQLKGKILLKGKKLGGLLPPGGEGGPEATVVSDEDEAAEMEDEAVRSRVQHK
PKEDKLRLAQELSDMVIYCKSVHFGGFSSPGTPGQAFYEMASFSENRALRLLQESGNGFV
RHNVGHLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYQGRFQDNGACG
YVLKPAFLRDPNGTFNPRALAQGPWWARKRLNIRVISGQQLPKVNKNKNSIVDPKVTVEI
HGVSRDVASRQTAVITNNGFNPWWDTEFAFEVVVPDLALIRFLVEDYDASSKNDFIGQST
IPLNSLKQGYRHVHLMSKNGDQHPSATLFVKISLQD
Enzyme 7 Number of Residues 756
Enzyme 7 Molecular Weight 85664.3
Enzyme 7 Theoretical pI 6.68
Enzyme 7 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 7 General Function Involved in calcium ion binding
Enzyme 7 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Essential for trophoblast and placental development
Enzyme 7 Pathways
Enzyme 7 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 37572274 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P51178 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PLCD1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2271 bp
ATGGACTCGGGCCGGGACTTCCTGACCCTGCACGGCCTACAGGATGATGAGGATCTACAG
GCGCTGCTGAAGGGCAGCCAGCTCCTGAAGGTGAAGTCCAGCTCATGGAGGAGAGAGCGC
TTCTACAAGTTGCAGGAGGACTGCAAGACCATCTGGCAGGAGTCCCGCAAGGTCATGCGG
ACCCCGGAGTCCCAGCTGTTCTCCATCGAGGACATTCAGGAGGTGCGAATGGGGCACCGC
ACGGAGGGTCTGGAGAAGTTCGCCCGTGATGTGCCCGAGGACCGCTGCTTCTCCATTGTC
TTCAAGGACCAGCGCAATACACTAGACCTCATCGCCCCATCGCCAGCTGATGCCCAGCAC
TGGGTGCTGGGGCTGCACAAGATCATCCACCACTCAGGCTCCATGGACCAGCGTCAGAAG
CTACAGCACTGGATTCACTCCTGCTTGCGAAAAGCTGACAAAAACAAGGACAACAAGATG
AGCTTCAAGGAGCTGCAGAACTTCCTGAAGGAGCTCAACATCCAGGTGGACGACAGCTAT
GCCCGGAAGATCTTCAGGGAGTGTGACCACTCCCAGACAGACTCCCTGGAGGACGAGGAG
ATTGAGGCCTTCTACAAGATGCTGACCCAGCGGGTGGAGATCGACCGCACCTTCGCCGAG
GCCGCGGGCTCAGGGGAGACTCTGTCGGTGGATCAGTTAGTGACGTTCCTGCAGCACCAG
CAGCGGGAGGAGGCGGCAGGGCCTGCGCTGGCCCTCTCCCTCATTGAGCGCTACGAGCCC
AGCGAGACTGCCAAGGCGCAGCGGCAGATGACCAAGGACGGCTTCCTCATGTACTTACTG
TCGGCTGACGGCAGCGCCTTCAGCCTGGCACACCGCCGTGTCTACCAGGACATGGGCCAG
CCACTTAGCCACTACCTGGTGTCCTCTTCACACAACACCTACCTGCTGGAGGACCAGCTA
GCCGGGCCCAGCAGCACTGAAGCCTACATCCGGGCACTGTGCAAAGGCTGCCGATGCCTG
GAGCTTGACTGCTGGGACGGGCCCAACCAGGAACCAATCATCTACCACGGCTATACTTTC
ACTTCCAAGATCCTCTTCTGCGATGTGCTCAGGGCCATCCGGGACTATGCCTTCAAGGCG
TCCCCCTACCCTGTCATCCTATCCCTGGAGAACCACTGCACACTGGAGCAGCAGCGCGTG
ATGGCGCGGCACCTGCATGCCATCCTGGGCCCCATGCTGTTGAACCGACCACTGGATGGG
GTCACCAACAGCCTGCCCTCCCCTGAGCAACTGAAGGGGAAGATCCTGCTGAAGGGGAAG
AAGCTCGGGGGGCTCCTGCCCCCTGGAGGGGAGGGTGGCCCTGAGGCCACTGTGGTGTCA
GACGAAGACGAGGCTGCTGAGATGGAGGATGAGGCAGTGAGGAGCCGTGTGCAGCACAAG
CCCAAGGAGGACAAGCTCAGGCTAGCACAGGAGCTCTCTGACATGGTCATTTACTGCAAG
AGTGTCCACTTTGGGGGCTTCTCCAGTCCTGGCACCCCTGGACAGGCCTTCTACGAGATG
GCGTCCTTCTCTGAGAACCGTGCCCTTCGACTGCTCCAAGAATCAGGAAACGGCTTTGTC
CGCCACAACGTGGGGCACCTGAGCAGAATCTACCCGGCTGGATGGAGAACAGACTCCTCC
AACTACAGCCCCGTGGAGATGTGGAATGGGGGCTGCCAGATCGTGGCCCTGAATTTCCAG
ACACCTGGGCCAGAGATGGACGTGTACCAGGGCCGCTTCCAGGACAACGGGGCCTGTGGG
TACGTGCTGAAGCCCGCCTTCCTGCGAGACCCCAACGGCACCTTTAACCCCCGCGCCCTG
GCTCAGGGGCCCTGGTGGGCACGGAAGCGGCTCAACATCAGGGTCATTTCGGGGCAGCAG
CTGCCAAAAGTCAACAAGAATAAGAATTCAATTGTGGACCCCAAAGTGACAGTGGAGATC
CATGGCGTGAGCCGGGACGTGGCCAGCCGCCAGACTGCTGTCATCACCAACAATGGTTTC
AACCCATGGTGGGACACGGAGTTTGCGTTTGAGGTAGTTGTGCCTGACCTTGCCCTCATC
CGCTTCTTGGTGGAAGATTATGATGCCTCCTCCAAGAATGACTTCATTGGCCAGAGTACC
ATCCCCTTGAACAGCCTCAAGCAAGGATACCGCCATGTCCACCTCATGTCTAAGAACGGG
GACCAGCATCCATCAGCCACCCTCTTTGTGAAGATCTCCCTCCAGGACTAG
Enzyme 7 GenBank Gene ID BC050382 Link Image
Enzyme 7 GeneCard ID PLCD1 Link Image
Enzyme 7 GenAtlas ID PLCD1 Link Image
Enzyme 7 HGNC ID HGNC:9060 Link Image
Enzyme 7 Chromosome Location 3
Enzyme 7 Locus 3p22-p21.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Cheng HF, Jiang MJ, Chen CL, Liu SM, Wong LP, Lomasney JW, King K: Cloning and identification of amino acid residues of human phospholipase C delta 1 essential for catalysis. J Biol Chem. 1995 Mar 10;270(10):5495-505. [PubMed Link Image]
  2. 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5829
Enzyme 8 Name N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
Enzyme 8 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class L protein
  2. PIG-L
Enzyme 8 Gene Name PIGL
Enzyme 8 Protein Sequence >N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
MEAMWLLCVALAVLAWGFLWVWDSSERMKSREQGGRLGAESRTLLVIAHPDDEAMFFAPT
VLGLARLRHWVYLLCFSAGNYYNQGETRKKELLQSCDVLGIPLSSVMIIDNRDFPDDPGM
QWDTEHVARVLLQHIEVNGINLVVTFDAGGVSGHSNHIALYAAVRALHSEGKLPKGCSVL
TLQSVNVLRKYISLLDLPLSLLHTQDVLFVLNSKEVAQAKKAMSCHRSQLLWFRRLYIIF
SRYMRINSLSFL
Enzyme 8 Number of Residues 252
Enzyme 8 Molecular Weight 28531.0
Enzyme 8 Theoretical pI 8.23
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Involved in N-acetylglucosaminylphosphatidylinositol de
Enzyme 8 Specific Function Involved in the second step of GPI biosynthesis. De-N- acetylation of N-acetylglucosaminyl-phosphatidylinositol
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate [RN:R03482 R05917]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 2-22
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 4239986 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9Y2B2 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PIGL_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >759 bp
ATGGAAGCAATGTGGCTCCTGTGTGTGGCGTTGGCGGTCTTGGCATGGGGCTTCCTCTGG
GTTTGGGACTCCTCAGAACGAATGAAGAGTCGGGAGCAGGGAGGACGGCTGGGAGCCGAA
AGCCGGACCCTGCTGGTCATAGCGCACCCTGACGATGAAGCCATGTTTTTTGCTCCCACA
GTGCTAGGCTTGGCCCGCCTAAGGCACTGGGTGTACCTGCTTTGCTTCTCTGCAGGAAAT
TACTACAATCAAGGAGAGACTCGTAAGAAAGAACTTTTGCAGAGCTGTGATGTTTTGGGG
ATTCCACTCTCCAGTGTAATGATTATTGACAACAGGGATTTCCCAGATGACCCAGGCATG
CAGTGGGACACAGAGCACGTGGCCAGAGTCCTCCTTCAGCACATAGAAGTGAATGGCATC
AATCTGGTGGTGACTTTCGATGCAGGGGGAGTAAGTGGCCACAGCAATCACATTGCTCTG
TATGCAGCTGTGAGGGCCCTGCACTCAGAAGGGAAGTTACCTAAAGGGTGCTCTGTGCTC
ACGCTTCAGTCTGTGAATGTGCTGCGCAAGTACATCTCCCTTCTGGATCTGCCCTTGTCT
CTGCTTCATACGCAGGATGTCCTCTTCGTGCTCAACAGCAAAGAAGTGGCACAGGCCAAG
AAAGCCATGTCCTGCCACCGCAGCCAGCTCCTCTGGTTCCGCCGCCTCTACATTATCTTC
TCCCGGTACATGAGAATCAACTCACTGAGCTTCCTCTGA
Enzyme 8 GenBank Gene ID AB017165 Link Image
Enzyme 8 GeneCard ID PIGL Link Image
Enzyme 8 GenAtlas ID PIGL Link Image
Enzyme 8 HGNC ID HGNC:8966 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 17p12-p11.2
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Watanabe R, Ohishi K, Maeda Y, Nakamura N, Kinoshita T: Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis. Biochem J. 1999 Apr 1;339 ( Pt 1):185-92. [PubMed Link Image]
  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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6228
Enzyme 9 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
Enzyme 9 Synonyms
  1. N-acetylglucosamyl transferase component GPI1
  2. Phosphatidylinositol-glycan biosynthesis class Q protein
  3. PIG-Q
Enzyme 9 Gene Name PIGQ
Enzyme 9 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
MVLKAFFPTCCVSTDSGLLVGRWVPEQSSAVVLAVLHFPFIPIQVKQLLAQVRQASQVGV
AVLGTWCHCRQEPEESLGRFLESLGAVFPHEPWLRLCRERGGTFWSCEATHRQAPTAPGA
PGEDQVMLIFYDQRQVLLSQLHLPTVLPDRQAGATTASTGGLAAVFDTVARSEVLFRSDR
FDEGPVRLSHWQSEGVEASILAELARRASGPICLLLASLLSLVSAVSACRVFKLWPLSFL
GSKLSTCEQLRHRLEHLTLIFSTRKAENPAQLMRKANTVASVLLDVALGLMLLSWLHGRS
RIGHLADALVPVADHVAEELQHLLQWLMGAPAGLKMNRALDQVLGRFFLYHIHLWISYIH
LMSPFVEHILWHVGLSACLGLTVALSLLSDIIALLTFHIYCFYVYGARLYCLKIHGLSSL
WRLFRGKKWNVLRQRVDSCSYDLDQLFIGTLLFTILLFLLPTTALYYLVFTLLRLLVVAV
QGLIHLLVDLINSLPLYSLGLRLCRPYRLADKPTALQPRGAHLPPPQLWLPPQALLGRPV
PQAVPWGAHLPLEAERGQAGLRELLARLAPPHGHSQPSALPGWHQLSWRMSCALWTLLCA
PEHGRPCYHTLGLEVIGSEQMWGWPARLAALHHWHCLPWDPLPTCCGHHGGEHSNPRCPE
HCPMPTLCTQVQRVRPPQQPQVEGWSPWGLPSGSALAVGVEGPCQDEPPSPRHPLAPSAE
QHPASGGLKQSLTPVPSGPGPSLPEPHGVYLRMFPGEVAL
Enzyme 9 Number of Residues 760
Enzyme 9 Molecular Weight 84081.4
Enzyme 9 Theoretical pI 8.08
Enzyme 9 GO Classification
Function
  • UDP-glycosyltransferase activity
  • acetylglucosaminyltransferase activity
  • catalytic activity
  • phosphatidylinositol N-acetylglucosaminyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 9 General Function Involved in phosphatidylinositol N-acetylglucosaminyltransferase activity
Enzyme 9 Specific Function Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol [RN:R02654 R05916]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • 278-298 349-371 378-400 446-468 475-497
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 22538453 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9BRB3 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PIGQ_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >2283 bp
ATGGTGCTCAAGGCCTTCTTCCCCACGTGCTGCGTCTCGACGGACAGCGGGCTGCTGGTG
GGACGGTGGGTGCCGGAGCAGAGCAGCGCCGTGGTCCTGGCGGTCCTGCACTTTCCCTTC
ATCCCCATCCAGGTCAAGCAGCTCCTGGCCCAGGTGCGGCAGGCCAGCCAGGTGGGCGTG
GCCGTGCTGGGCACCTGGTGCCACTGCCGGCAGGAGCCCGAGGAGAGCCTGGGCCGCTTC
CTGGAGAGCCTGGGTGCTGTCTTCCCCCATGAGCCCTGGCTGCGGCTGTGCCGGGAGAGA
GGCGGCACGTTCTGGAGCTGCGAGGCCACCCACCGGCAAGCGCCCACTGCCCCCGGTGCC
CCTGGTGAGGACCAGGTCATGCTCATCTTCTATGACCAGCGCCAGGTGTTGCTGTCACAG
CTACACCTGCCCACCGTCCTGCCCGACCGCCAGGCTGGAGCCACCACTGCCAGCACGGGG
GGCCTGGCTGCCGTCTTCGACACGGTAGCACGCAGTGAGGTGCTCTTCCGCAGTGACCGC
TTTGATGAGGGCCCCGTGCGGCTGAGCCACTGGCAGTCGGAGGGCGTGGAGGCCAGCATC
CTCGCGGAGCTGGCCAGGCGAGCCTCGGGACCCATTTGCCTGCTGTTGGCCAGCCTGCTG
TCGCTGGTCTCAGCTGTCAGTGCCTGCCGAGTGTTCAAGCTCTGGCCCCTGTCCTTCCTC
GGGAGCAAACTCTCCACGTGCGAACAGCTCCGGCACCGGCTGGAGCACCTCACGCTAATC
TTCAGTACACGGAAGGCGGAGAACCCTGCCCAGCTGATGAGGAAGGCCAACACGGTGGCC
TCTGTGCTGCTGGACGTGGCCCTGGGCCTCATGCTGCTGTCCTGGCTCCACGGGAGAAGC
CGCATCGGGCATCTGGCCGACGCCCTCGTTCCTGTGGCTGACCACGTGGCCGAGGAGCTC
CAGCATCTGCTGCAGTGGCTGATGGGTGCTCCCGCCGGGCTCAAGATGAACCGTGCACTG
GACCAGGTGCTGGGCCGCTTCTTCCTCTACCACATCCACCTGTGGATCAGCTACATCCAC
CTCATGTCCCCCTTCGTGGAGCACATCCTTTGGCACGTGGGCCTCTCGGCCTGCCTGGGC
CTGACGGTGGCCCTGTCCCTCCTCTCGGACATTATCGCCCTCCTCACCTTCCACATCTAC
TGCTTTTACGTCTATGGAGCCAGGCTGTACTGCCTGAAGATCCATGGCCTGTCCTCACTG
TGGCGTCTGTTCCGGGGGAAGAAGTGGAACGTTCTGCGCCAGCGCGTGGACTCCTGTTCC
TATGACCTGGACCAGCTGTTCATCGGGACTCTGCTCTTCACCATCCTGCTCTTCCTCCTG
CCTACCACAGCCCTGTACTACCTGGTGTTCACCCTGCTCCGGCTCCTGGTGGTCGCCGTG
CAGGGCCTGATCCATCTGCTCGTGGACCTCATCAACTCCCTGCCGCTGTACTCACTGGGT
CTTCGGCTCTGCCGGCCCTACAGGCTGGCGGATAAACCCACTGCCCTACAGCCGCGTGGT
GCACACCTACCGCCTCCCCAGCTGTGGCTGCCACCCCAAGCACTCCTGGGGCGCCCTGTG
CCGCAAGCTGTTCCTTGGGGAGCTCATCTACCCCTGGAGGCAGAGAGGGGACAAGCAGGA
CTGAGGGAACTGCTGGCTCGCCTGGCACCACCACACGGCCACAGCCAGCCATCTGCTCTG
CCAGGGTGGCACCAGCTCAGCTGGCGCATGTCCTGTGCTTTGTGGACGCTGCTGTGTGCT
CCTGAACACGGCAGGCCCTGCTATCACACCTTGGGCTTGGAGGTCATTGGGAGTGAGCAG
ATGTGGGGGTGGCCAGCCAGGCTGGCCGCACTCCATCACTGGCACTGCCTGCCTTGGGAC
CCGCTTCCCACCTGCTGCGGTCACCATGGTGGCGAGCACAGCAACCCCAGGTGTCCAGAG
CACTGCCCCATGCCCACCCTGTGTACCCAGGTCCAGAGGGTCCGTCCACCACAGCAGCCC
CAGGTGGAGGGCTGGTCTCCCTGGGGGCTCCCCAGTGGCTCTGCCCTGGCTGTGGGGGTG
GAGGGACCTTGCCAGGATGAACCCCCCAGTCCCAGGCACCCTCTAGCTCCCTCAGCCGAA
CAGCACCCTGCATCTGGGGGATTGAAGCAGTCGCTGACCCCCGTCCCCAGCGGGCCCGGG
CCCTCACTCCCTGAACCACACGGGGTTTATTTGCGGATGTTCCCTGGAGAGGTCGCTTTG
TGA
Enzyme 9 GenBank Gene ID NM_148920.1 Link Image
Enzyme 9 GeneCard ID PIGQ Link Image
Enzyme 9 GenAtlas ID PIGQ Link Image
Enzyme 9 HGNC ID HGNC:14135 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 16p13.3
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Tiede A, Schubert J, Nischan C, Jensen I, Westfall B, Taron CH, Orlean P, Schmidt RE: Human and mouse Gpi1p homologues restore glycosylphosphatidylinositol membrane anchor biosynthesis in yeast mutants. Biochem J. 1998 Sep 15;334 ( Pt 3):609-16. [PubMed Link Image]
  2. Watanabe R, Inoue N, Westfall B, Taron CH, Orlean P, Takeda J, Kinoshita T: The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1. EMBO J. 1998 Feb 16;17(4):877-85. [PubMed Link Image]
  3. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  4. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [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. Watanabe R, Murakami Y, Marmor MD, Inoue N, Maeda Y, Hino J, Kangawa K, Julius M, Kinoshita T: Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2. EMBO J. 2000 Aug 15;19(16):4402-11. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6229
Enzyme 10 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
Enzyme 10 Synonyms
  1. GlcNAc-PI synthesis protein
  2. Phosphatidylinositol-glycan biosynthesis class A protein
  3. PIG-A
Enzyme 10 Gene Name PIGA
Enzyme 10 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
MACRGGAGNGHRASATLSRVSPGSLYTCRTRTHNICMVSDFFYPNMGGVESHIYQLSQCL
IERGHKVIIVTHAYGNRKGIRYLTSGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRE
RVTIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNH
IICVSYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPFRRHDSITIVVVSRLVYRKGI
DLLSGIIPELCQKYPDLNFIIGGEGPKRIILEEVRERYQLHDRVRLLGALEHKDVRNVLV
QGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEPSVKSLCEGLE
KAIFQLKSGTLPAPENIHNIVKTFYTWRNVAERTEKVYDRVSVEAVLPMDKRLDRLISHC
GPVTGYIFALLAVFNFLFLIFLRWMTPDSIIDVAIDATGPRGAWTNNYSHSKRGGENNEI
SETR
Enzyme 10 Number of Residues 484
Enzyme 10 Molecular Weight 54126.1
Enzyme 10 Theoretical pI 8.41
Enzyme 10 GO Classification
Function
Process
  • GPI anchor biosynthetic process
  • biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
Enzyme 10 General Function Involved in biosynthetic process
Enzyme 10 Specific Function Necessary for the synthesis of N-acetylglucosaminyl- phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol [RN:R02654 R05916]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • 422-442
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 23398601 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P37287 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PIGA_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1455 bp
ATGGCCTGTAGAGGAGGAGCTGGGAATGGCCACCGTGCCTCAGCTACACTCTCTCGGGTT
AGCCCTGGAAGTCTTTACACATGTAGAACCCGTACCCATAATATATGCATGGTATCTGAC
TTTTTCTACCCAAATATGGGAGGCGTGGAAAGCCACATTTACCAGCTCTCTCAGTGCCTG
ATTGAAAGAGGGCATAAGGTTATAATTGTCACCCATGCTTATGGAAATCGAAAAGGCATC
CGTTACCTCACCAGTGGCCTCAAAGTCTATTACTTGCCTCTGAAAGTCATGTACAACCAG
TCTACAGCCACGACCCTCTTTCACAGTCTGCCATTGCTCAGGTACATATTTGTTCGGGAG
AGAGTCACGATAATCCATTCACATAGTTCTTTTTCTGCTATGGCCCATGATGCTCTCTTC
CACGCCAAGACAATGGGGCTTCAGACAGTCTTCACGGACCATTCCCTTTTTGGATTTGCT
GATGTCAGCTCGGTGCTTACAAACAAGCTTCTAACCGTGTCTCTTTGTGATACAAACCAC
ATCATTTGTGTGTCTTATACTAGTAAGGAAAATACTGTACTAAGAGCAGCACTGAATCCT
GAAATAGTGTCCGTCATTCCTAATGCTGTAGATCCTACTGACTTCACTCCAGACCCATTT
AGAAGGCATGATAGTATAACTATTGTTGTTGTCAGCAGACTTGTTTACAGAAAAGGGATC
GATTTGCTTAGTGGTATAATACCTGAACTCTGTCAGAAATATCCAGATTTAAATTTCATA
ATTGGAGGAGAGGGACCAAAGAGAATCATTTTGGAAGAAGTTCGGGAAAGATACCAGCTG
CATGACAGGGTGCGTCTTTTGGGAGCTTTAGAACACAAGGATGTTAGAAATGTCTTAGTT
CAAGGACATATTTTTCTGAATACCTCCCTTACTGAAGCATTCTGCATGGCGATCGTGGAA
GCAGCCAGTTGTGGTTTACAGGTTGTAAGTACCAGAGTTGGTGGAATTCCTGAGGTGCTT
CCAGAAAACCTTATTATTTTATGTGAGCCTTCAGTAAAATCTTTGTGTGAAGGATTGGAA
AAGGCTATTTTCCAACTGAAGTCAGGGACATTGCCAGCTCCAGAAAACATCCATAACATA
GTAAAGACTTTCTACACCTGGAGGAATGTTGCAGAAAGAACTGAAAAGGTATATGACCGG
GTATCAGTGGAAGCTGTGTTGCCAATGGACAAACGACTGGACAGACTTATTTCTCACTGC
GGCCCAGTAACAGGCTACATCTTTGCTTTGTTGGCAGTTTTCAACTTCCTCTTCCTCATT
TTCTTGAGATGGATGACTCCAGATTCTATCATTGATGTTGCAATAGATGCCACTGGGCCA
CGGGGTGCCTGGACTAATAACTATTCTCACAGTAAAAGAGGGGGTGAGAATAATGAGATA
TCTGAAACCAGGTAG
Enzyme 10 GenBank Gene ID BC038236 Link Image
Enzyme 10 GeneCard ID PIGA Link Image
Enzyme 10 GenAtlas ID PIGA Link Image
Enzyme 10 HGNC ID HGNC:8957 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Miyata T, Takeda J, Iida Y, Yamada N, Inoue N, Takahashi M, Maeda K, Kitani T, Kinoshita T: The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis. Science. 1993 Feb 26;259(5099):1318-20. [PubMed Link Image]
  2. Bessler M, Hillmen P, Longo L, Luzzatto L, Mason PJ: Genomic organization of the X-linked gene (PIG-A) that is mutated in paroxysmal nocturnal haemoglobinuria and of a related autosomal pseudogene mapped to 12q21. Hum Mol Genet. 1994 May;3(5):751-7. [PubMed Link Image]
  3. Iida Y, Takeda J, Miyata T, Inoue N, Nishimura J, Kitani T, Maeda K, Kinoshita T: Characterization of genomic PIG-A gene: a gene for glycosylphosphatidylinositol-anchor biosynthesis and paroxysmal nocturnal hemoglobinuria. Blood. 1994 Jun 1;83(11):3126-31. [PubMed Link Image]
  4. Yu J, Nagarajan S, Ueda E, Knez JJ, Petersen RB, Medof ME: Characterization of alternatively spliced PIG-A transcripts in normal and paroxysmal nocturnal hemoglobinuria cells. Braz J Med Biol Res. 1994 Feb;27(2):195-201. [PubMed Link Image]
  5. 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. Takeda J, Miyata T, Kawagoe K, Iida Y, Endo Y, Fujita T, Takahashi M, Kitani T, Kinoshita T: Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria. Cell. 1993 May 21;73(4):703-11. [PubMed Link Image]
  7. Murakami Y, Siripanyaphinyo U, Hong Y, Tashima Y, Maeda Y, Kinoshita T: The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component. Mol Biol Cell. 2005 Nov;16(11):5236-46. Epub 2005 Sep 14. [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. Bessler M, Mason PJ, Hillmen P, Miyata T, Yamada N, Takeda J, Luzzatto L, Kinoshita T: Paroxysmal nocturnal haemoglobinuria (PNH) is caused by somatic mutations in the PIG-A gene. EMBO J. 1994 Jan 1;13(1):110-7. [PubMed Link Image]
  10. Ware RE, Rosse WF, Howard TA: Mutations within the Piga gene in patients with paroxysmal nocturnal hemoglobinuria. Blood. 1994 May 1;83(9):2418-22. [PubMed Link Image]
  11. Nafa K, Bessler M, Castro-Malaspina H, Jhanwar S, Luzzatto L: The spectrum of somatic mutations in the PIG-A gene in paroxysmal nocturnal hemoglobinuria includes large deletions and small duplications. Blood Cells Mol Dis. 1998 Sep;24(3):370-84. [PubMed Link Image]
  12. Yoon JH, Cho HI, Park SS, Chang YH, Kim BK: Mutation analysis of the PIG-A gene in Korean patients with paroxysmal nocturnal haemoglobinuria. J Clin Pathol. 2002 Jun;55(6):410-3. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6230
Enzyme 11 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
Enzyme 11 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class H protein
  2. PIG-H
Enzyme 11 Gene Name PIGH
Enzyme 11 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
MEDERSFSDICGGRLALQRRYYSPSCREFCLSCPRLSLRSLTAVTCTVWLAAYGLFTLCE
NSMILSAAIFITLLGLLGYLHFVKIDQETLLIIDSLGIQMTSSYASGKESTTFIEMGKVK
DIVINEAIYMQKVIYYLCILLKDPVEPHGISQVVPVFQSAKPRLDCLIEVYRSCQEILAH
QKATSTSP
Enzyme 11 Number of Residues 188
Enzyme 11 Molecular Weight 21080.4
Enzyme 11 Theoretical pI 6.72
Enzyme 11 GO Classification Not Available
Enzyme 11 General Function Involved in phosphatidylinositol N-acetylglucosaminyltr
Enzyme 11 Specific Function Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol [RN:R02654 R05916]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 189054281 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q14442 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name PIGH_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >567 bp
ATGGAGGATGAGCGGAGCTTTTCGGATATCTGCGGCGGCCGCCTGGCGCTGCAGCGCCGC
TACTACTCCCCGTCCTGCCGGGAATTCTGCCTCAGCTGCCCTCGGCTCTCGCTGCGTTCG
CTCACCGCTGTCACCTGCACGGTGTGGCTGGCGGCCTACGGACTCTTCACCCTCTGCGAG
AACAGCATGATCCTCTCTGCTGCCATCTTCATCACCCTCTTAGGTCTGCTTGGTTATCTC
CATTTTGTGAAGATTGATCAGGAGACTCTGTTAATCATTGATTCCCTTGGCATTCAGATG
ACTTCATCTTATGCTTCAGGCAAAGAAAGCACTACCTTCATAGAAATGGGCAAGGTCAAG
GATATTGTCATCAATGAGGCCATTTACATGCAGAAGGTGATTTACTACCTCTGCATCTTA
TTGAAAGATCCAGTGGAACCACATGGGATATCCCAAGTAGTACCCGTCTTCCAGAGTGCC
AAGCCCCGGCTGGACTGCTTGATTGAAGTATACAGGAGCTGCCAGGAGATCCTGGCACAC
CAGAAAGCCACATCAACAAGCCCATGA
Enzyme 11 GenBank Gene ID AK314108 Link Image
Enzyme 11 GeneCard ID PIGH Link Image
Enzyme 11 GenAtlas ID PIGH Link Image
Enzyme 11 HGNC ID HGNC:8964 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 14q24.1
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Kamitani T, Chang HM, Rollins C, Waneck GL, Yeh ET: Correction of the class H defect in glycosylphosphatidylinositol anchor biosynthesis in Ltk- cells by a human cDNA clone. J Biol Chem. 1993 Oct 5;268(28):20733-6. [PubMed Link Image]
  2. 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. Watanabe R, Inoue N, Westfall B, Taron CH, Orlean P, Takeda J, Kinoshita T: The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1. EMBO J. 1998 Feb 16;17(4):877-85. [PubMed Link Image]
  5. 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]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6232
Enzyme 12 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
Enzyme 12 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class C protein
  2. PIG-C
Enzyme 12 Gene Name PIGC
Enzyme 12 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
MYAQPVTNTKEVKWQKVLYERQPFPDNYVDRRFLEELRKNIHARKYQYWAVVFESSVVIQ
QLCSVCVFVVIWWYMDEGLLAPHWLLGTGLASSLIGYVLFDLIDGGEGRKKSGQTRWADL
KSALVFITFTYGFSPVLKTLTESVSTDTIYAMSVFMLLGHLIFFDYGANAAIVSSTLSLN
MAIFASVCLASRLPRSLHAFIMVTFAIQIFALWPMLQKKLKACTPRSYVGVTLLFAFSAV
GGLLSISAVGAVLFALLLMSISCLCPFYLIRLQLFKENIHGPWDEAEIKEDLSRFLS
Enzyme 12 Number of Residues 297
Enzyme 12 Molecular Weight 33582.2
Enzyme 12 Theoretical pI 8.55
Enzyme 12 GO Classification
Function
  • UDP-glycosyltransferase activity
  • acetylglucosaminyltransferase activity
  • catalytic activity
  • phosphatidylinositol N-acetylglucosaminyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 12 General Function Involved in phosphatidylinositol N-acetylglucosaminyltransferase activity
Enzyme 12 Specific Function Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol [RN:R02654 R05916]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 51-71 80-100 154-174 239-259
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 2547042 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q92535 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name PIGC_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >894 bp
ATGTATGCTCAACCTGTGACTAACACCAAGGAGGTCAAGTGGCAGAAGGTCTTGTATGAG
CGACAGCCCTTTCCTGATAACTATGTGGACCGGCGATTCCTGGAAGAGCTCCGGAAAAAC
ATCCATGCTCGGAAATACCAATATTGGGCTGTGGTATTTGAGTCCAGTGTGGTGATCCAG
CAGCTGTGCAGTGTTTGTGTTTTTGTGGTTATCTGGTGGTATATGGATGAGGGTCTTCTG
GCCCCCCATTGGCTTTTAGGGACTGGCCTGGCTTCTTCACTGATTGGGTATGTTTTGTTT
GATCTCATTGATGGAGGTGAAGGGCGGAAGAAGAGTGGGCAGACCCGGTGGGCTGACCTG
AAGAGTGCCCTAGTCTTCATTACTTTCACTTATGGGTTTTCACCAGTGCTGAAGACCCTT
ACAGAGTCTGTCAGCACTGACACCATCTATGCCATGTCAGTCTTCATGCTGTTAGGCCAT
CTCATCTTTTTTGACTATGGTGCCAATGCTGCCATTGTATCCAGCACACTATCCTTGAAC
ATGGCCATCTTTGCTTCTGTATGCTTGGCATCACGTCTTCCCCGGTCCCTGCATGCCTTC
ATCATGGTGACATTTGCCATTCAGATTTTTGCCCTGTGGCCCATGTTGCAGAAGAAACTA
AAGGCATGTACTCCCCGGAGCTATGTGGGGGTCACACTGCTTTTTGCATTTTCAGCCGTG
GGAGGCCTACTGTCCATTAGTGCTGTGGGAGCCGTACTCTTTGCCCTTCTGCTGATGTCT
ATCTCATGTCTGTGTTCATTCTACCTCATTCGCTTGCAGCTTTTTAAAGAAAACATTCAT
GGGCCTTGGGATGAAGCTGAAATCAAGGAAGACTTGTCCAGGTTCCTCAGTTAA
Enzyme 12 GenBank Gene ID AB000360 Link Image
Enzyme 12 GeneCard ID PIGC Link Image
Enzyme 12 GenAtlas ID PIGC Link Image
Enzyme 12 HGNC ID HGNC:8960 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 1q23-q25
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Inoue N, Watanabe R, Takeda J, Kinoshita T: PIG-C, one of the three human genes involved in the first step of glycosylphosphatidylinositol biosynthesis is a homologue of Saccharomyces cerevisiae GPI2. Biochem Biophys Res Commun. 1996 Sep 4;226(1):193-9. [PubMed Link Image]
  2. Hong Y, Ohishi K, Inoue N, Endo Y, Fujita T, Takeda J, Kinoshita T: Structures and chromosomal localizations of the glycosylphosphatidylinositol synthesis gene PIGC and its pseudogene PIGCP1. Genomics. 1997 Sep 15;44(3):347-9. [PubMed Link Image]
  3. 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]
  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 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6427
Enzyme 13 Name Probable phospholipid-transporting ATPase IG
Enzyme 13 Synonyms
  1. ATPase IQ
  2. ATPase class VI type 11C
Enzyme 13 Gene Name ATP11C
Enzyme 13 Protein Sequence >Probable phospholipid-transporting ATPase IG
MQMVPSLPPASECAGEEKRVGTRTVFVGNHPVSETEAYIAQRFCDNRIVSSKYTLWNFLP
KNLFEQFRRIANFYFLIIFLVQVTVDTPTSPVTSGLPLFFVITVTAIKQGYEDCLRHRAD
NEVNKSTVYIIENAKRVRKESEKIKVGDVVEVQADETFPCDLILLSSCTTDGTCYVTTAS
LDGESNCKTHYAVRDTIALCTAESIDTLRAAIECEQPQPDLYKFVGRINIYSNSLEAVAR
SLGPENLLLKGATLKNTEKIYGVAVYTGMETKMALNYQGKSQKRSAVEKSINAFLIVYLF
ILLTKAAVCTTLKYVWQSTPYNDEPWYNQKTQKERETLKVLKMFTDFLSFMVLFNFIIPV
SMYVTVEMQKFLGSFFISWDKDFYDEEINEGALVNTSDLNEELGQVDYVFTDKTGTLTEN
SMEFIECCIDGHKYKGVTQEVDGLSQTDGTLTYFDKVDKNREELFLRALCLCHTVEIKTN
DAVDGATESAELTYISSSPDEIALVKGAKRYGFTFLGNRNGYMRVENQRKEIEEYELLHT
LNFDAVRRRMSVIVKTQEGDILLFCKGADSAVFPRVQNHEIELTKVHVERNAMDGYRTLC
VAFKEIAPDDYERINRQLIEAKMALQDREEKMEKVFDDIETNMNLIGATAVEDKLQDQAA
ETIEALHAAGLKVWVLTGDKMETAKSTCYACRLFQTNTELLELTTKTIEESERKEDRLHE
LLIEYRKKLLHEFPKSTRSFKKAWTEHQEYGLIIDGSTLSLILNSSQDSSSNNYKSIFLQ
ICMKCTAVLCCRMAPLQKAQIVRMVKNLKGSPITLSIGDGANDVSMILESHVGIGIKGKE
GRQAARNSDYSVPKFKHLKKLLLAHGHLYYVRIAHLVQYFFYKNLCFILPQFLYQFFCGF
SQQPLYDAAYLTMYNICFTSLPILAYSLLEQHINIDTLTSDPRLYMKISGNAMLQLGPFL
YWTFLAAFEGTVFFFGTYFLFQTASLEENGKVYGNWTFGTIVFTVLVFTVTLKLALDTRF
WTWINHFVIWGSLAFYVFFSFFWGGIIWPFLKQQRMYFVFAQMLSSVSTWLAIILLIFIS
LFPEILLIVLKNVRRRSARRNLSCRRASDSLSARPSVRPLLLRTFSDESNVL
Enzyme 13 Number of Residues 1132
Enzyme 13 Molecular Weight 129476.0
Enzyme 13 Theoretical pI 6.63
Enzyme 13 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • ion binding
  • ion transmembrane transporter activity
  • lipid transporter activity
  • magnesium ion binding
  • metal ion binding
  • nucleoside binding
  • phospholipid transporter activity
  • phospholipid-translocating ATPase activity
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • substrate-specific transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • cellular nitrogen compound metabolic process
  • establishment of localization
  • lipid transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phospholipid transport
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 13 General Function Involved in ATP binding
Enzyme 13 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions
  • ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • 67-85 87-107 291-311 347-367 880-900 909-929 956-976 996-1016 1027-1047 1070-1090
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 39573513 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q8NB49 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name AT11C_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >3399 bp
ATGCAGATGGTCCCATCTCTCCCTCCAGCCTCTGAGTGTGCTGGAGAAGAGAAACGAGTT
GGCACACGCACAGTGTTTGTTGGCAATCATCCAGTTTCGGAAACAGAAGCTTACATTGCA
CAAAGATTTTGTGATAATAGAATAGTCTCATCTAAGTATACACTTTGGAATTTTCTCCCA
AAGAATCTGTTTGAACAGTTTAGAAGAATTGCAAATTTTTATTTTCTCATAATCTTCCTT
GTACAGGTCACAGTAGACACACCAACTAGCCCAGTTACCAGTGGACTTCCACTTTTCTTT
GTTATAACTGTTACAGCCATCAAGCAGGGATATGAGGATTGGCTGAGACACAGAGCTGAC
AATGAAGTCAACAAAAGCACTGTTTACATTATTGAAAATGCAAAGCGAGTGAGAAAAGAA
AGTGAAAAAATCAAGGTTGGTGATGTAGTAGAAGTACAGGCAGATGAAACCTTTCCCTGT
GATCTTATTCTTCTATCATCTTGCACCACTGATGGAACCTGTTATGTCACTACAGCCAGT
CTTGATGGGGAATCCAATTGCAAGACACATTATGCAGTACGTGATACCATTGCACTGTGT
ACAGCAGAATCCATCGATACCCTCCGAGCAGCAATTGAATGTGAACAGCCTCAACCTGAC
CTCTACAAATTTGTTGGGCGAATCAATATCTACAGTAATAGTCTTGAGGCTGTTGCCAGG
TCTTTGGGACCTGAAAATCTCTTGCTGAAAGGAGCTACGCTAAAAAATACCGAGAAGATA
TATGGAGTTGCTGTTTACACTGGAATGGAAACCAAAATGGCTTTGAACTACCAAGGGAAA
TCTCAGAAACGTTCTGCTGTTGAAAAATCTATTAATGCTTTCCTGATTGTATATTTATTT
ATCTTACTGACCAAAGCTGCAGTATGCACTACTCTAAAGTATGTTTGGCAAAGTACCCCA
TACAATGATGAACCTTGGTATAACCAAAAGACTCAGAAAGAGCGAGAGACCTTGAAGGTT
TTAAAAATGTTCACCGACTTCCTATCATTTATGGTTCTATTCAACTTTATCATTCCTGTC
TCCATGTACGTCACAGTAGAAATGCAGAAATTCTTGGGCTCCTTCTTCATCTCATGGGAT
AAGGACTTTTATGATGAAGAAATTAATGAAGGAGCCCTGGTTAACACATCAGACCTTAAT
GAAGAACTTGGTCAGGTGGATTATGTATTTACAGATAAGACTGGAACACTCACTGAAAAC
AGCATGGAATTCATTGAATGCTGCATAGATGGCCACAAATATAAAGGTGTAACTCAAGAG
GTTGATGGATTATCTCAAACTGATGGAACTTTAACATATTTTGACAAAGTAGATAAGAAT
CGAGAAGAGCTGTTTCTACGTGCCTTGTGTTTATGTCATACTGTAGAAATCAAAACAAAC
GATGCTGTTGATGGAGCTACAGAATCAGCTGAATTAACCTATATCTCCTCTTCACCAGAT
GAAATAGCTTTGGTGAAAGGAGCTAAAAGGTACGGGTTCACATTTTTAGGAAATCGAAAT
GGATATATGAGAGTAGAGAACCAAAGAAAAGAAATAGAAGAATATGAACTTCTTCACACC
TTAAACTTTGATGCTGTCCGGCGACGTATGAGTGTAATTGTGAAGACTCAAGAAGGAGAC
ATACTTCTCTTTTGTAAAGGAGCAGACTCGGCAGTTTTTCCCAGAGTGCAAAATCATGAA
ATTGAGTTAACTAAAGTCCATGTGGAACGTAATGCAATGGATGGGTATCGGACACTCTGT
GTAGCCTTCAAAGAAATTGCTCCAGATGATTATGAAAGAATTAACAGACAGCTCATAGAG
GCAAAAATGGCCTTACAAGACAGAGAAGAAAAAATGGAAAAAGTTTTCGATGATATTGAG
ACAAACATGAATTTAATTGGAGCCACTGCAGTTGAAGACAAGCTACAAGATCAAGCTGCA
GAGACCATTGAAGCTCTGCATGCAGCAGGCCTGAAAGTCTGGGTGCTCACTGGGGACAAG
ATGGAGACAGCTAAATCCACATGCTATGCCTGCCGCCTTTTCCAGACCAACACTGAGCTC
TTAGAACTAACCACAAAAACCATTGAAGAAAGTGAAAGGAAAGAAGATCGATTACATGAA
TTATTGATAGAATATCGCAAGAAATTGCTGCATGAGTTTCCTAAAAGTACTAGAAGCTTT
AAAAAAGCATGGACAGAACATCAGGAATATGGATTAATCATAGATGGCTCCACATTGTCA
CTCATACTAAATTCTAGTCAAGACTCTAGTTCAAACAATTACAAAAGCATTTTCCTACAA
ATATGTATGAAGTGTACTGCAGTGCTCTGCTGTCGGATGGCACCATTACAGAAAGCCCAG
ATTGTCAGAATGGTGAAGAATTTAAAAGGCAGCCCAATAACTCTGTCGATAGGTGATGGT
GCCAATGATGTTAGTATGATCTTGGAATCCCATGTGGGAATAGGTATTAAAGGCAAAGAA
GGTCGCCAAGCAGCTAGGAATAGCGATTATTCTGTTCCAAAGTTTAAACACTTAAAGAAA
CTGCTGTTGGCTCATGGACATCTATATTATGTGAGAATAGCACACCTTGTACAGTACTTC
TTCTATAAGAACCTTTGTTTCATTTTGCCACAGTTTTTGTACCAGTTCTTCTGTGGATTC
TCACAACAGCCACTGTATGATGCTGCTTACCTTACAATGTACAATATCTGCTTCACATCC
TTGCCCATCCTGGCCTATAGTCTACTGGAACAGCACATCAACATTGACACTCTGACCTCA
GATCCCCGATTGTATATGAAAATTTCTGGCAATGCCATGCTACAGTTGGGCCCCTTCTTA
TATTGGACATTTCTGGCTGCCTTTGAAGGGACAGTGTTCTTCTTTGGGACTTACTTTCTT
TTTCAGACTGCATCCCTAGAAGAAAATGGAAAGGTATACGGAAACTGGACTTTTGGAACC
ATTGTTTTTACAGTCTTAGTATTCACTGTAACCCTGAAGCTTGCCTTGGATACCCGATTC
TGGACGTGGATAAATCACTTTGTGATTTGGGGTTCTTTAGCCTTCTATGTATTTTTCTCA
TTCTTCTGGGGAGGAATTATTTGGCCTTTTCTCAAGCAACAGAGAATGTATTTTGTATTT
GCCCAAATGCTGTCTTCTGTATCCACATGGTTGGCTATAATTCTTCTAATATTTATCAGC
CTGTTCCCTGAGATTCTTCTGATAGTATTAAAGAATGTAAGAAGAAGAAGTGCCAGGAGA
AATCTGAGCTGTAGAAGGGCATCTGACTCATTATCCGCCAGACCTTCAGTCAGACCTCTT
CTTTTACGAACATTCTCAGACGAATCTAATGTATTGTAA
Enzyme 13 GenBank Gene ID AJ580093 Link Image
Enzyme 13 GeneCard ID ATP11C Link Image
Enzyme 13 GenAtlas ID ATP11C Link Image
Enzyme 13 HGNC ID HGNC:13554 Link Image
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Andrew Nesbit M, Bowl MR, Harding B, Schlessinger D, Whyte MP, Thakker RV: X-linked hypoparathyroidism region on Xq27 is evolutionarily conserved with regions on 3q26 and 13q34 and contains a novel P-type ATPase. Genomics. 2004 Dec;84(6):1060-70. [PubMed Link Image]
  2. 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]
  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. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 6428
Enzyme 14 Name Probable phospholipid-transporting ATPase IH
Enzyme 14 Synonyms
  1. ATPase IS
  2. ATPase class VI type 11A
Enzyme 14 Gene Name ATP11A
Enzyme 14 Protein Sequence >Probable phospholipid-transporting ATPase IH
MDCSLVRTLVHRYCAGEENWVDSRTIYVGHREPPPGAEAYIPQRYPDNRIVSSKYTFWNF
IPKNLFEQFRRVANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHK
ADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTT
ASLDGESSHKTHYAVQDTKGFHTEEDIGGLHATIECEQPQPDLYKFVGRINVYSDLNDPV
VRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNAFLIVY
LCILISKALINTVLKYMWQSEPFRDEPWYNQKTESERQRNLFLKAFTDFLAFMVLFNYII
PVSMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLT
ENNMEFKECCIEGHVYVPHVICNGQVLPESSGIDMIDSSPSVNGREREELFFRALCLCHT
VQVKDDDSVDGPRKSPDGGKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEILNREN
HIERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPRVIEGKVDQIRARVER
NAVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATA
VEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLLELTTKRIEE
QSLHDVLFELSKTVLRHSGSLTRDNLSGLSADMQDYGLIIDGAALSLIMKPREDGSSGNY
RELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEHPITLAIGDGANDVSMILEAHVGI
GVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLY
QFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALL
RWRVFIYWTLLGLFDALVFFFGAYFVFENTTVTSNGQIFGNWTFGTLVFTVMVFTVTLKL
ALDTHYWTWINHFVIWGSLLFYVVFSLLWGGVIWPFLNYQRMYYVFIQMLSSGPAWLAIV
LLVTISLLPDVLKKVLCRQLWPTATERVQTKSQCLSVEQSTIFMLSQTSSSLSF
Enzyme 14 Number of Residues 1134
Enzyme 14 Molecular Weight 129754.6
Enzyme 14 Theoretical pI 6.58
Enzyme 14 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • ion binding
  • ion transmembrane transporter activity
  • lipid transporter activity
  • magnesium ion binding
  • metal ion binding
  • nucleoside binding
  • phospholipid transporter activity
  • phospholipid-translocating ATPase activity
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • substrate-specific transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • cellular nitrogen compound metabolic process
  • establishment of localization
  • lipid transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phospholipid transport
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 14 General Function Involved in ATP binding
Enzyme 14 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions
  • ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • 62-82 89-110 297-318 350-372 882-902 915-934 965-986 1001-1023 1030-1050 1069-1093
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 150421684 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P98196 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name AT11A_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >3405 bp
ATGGACTGCAGCCTCGTGCGGACGCTCGTGCACAGATACTGTGCAGGAGAAGAGAATTGG
GTGGACAGCAGGACCATCTACGTGGGACACAGGGAGCCACCTCCGGGCGCAGAGGCCTAC
ATCCCACAGAGATACCCAGACAACAGGATCGTCTCGTCCAAGTACACATTTTGGAACTTT
ATACCCAAGAATTTATTTGAACAATTCAGAAGAGTAGCCAACTTTTATTTCCTTATCATA
TTTCTGGTGCAGTTGATTATTGATACACCCACAAGTCCAGTGACAAGCGGACTTCCACTC
TTCTTTGTCATTACTGTGACGGCTATCAAACAGGGTTATGAAGACTGGCTTCGACATAAA
GCAGACAATGCCATGAACCAGTGTCCTGTTCATTTCATTCAGCACGGCAAGCTCGTTCGG
AAACAAAGTCGAAAGCTGCGAGTTGGGGACATTGTCATGGTTAAGGAGGACGAGACCTTT
CCCTGCGACTTGATCTTCCTTTCCAGCAACCGGGGAGATGGGACGTGCCACGTCACCACC
GCCAGCTTGGATGGAGAATCCAGCCATAAAACGCATTACGCGGTCCAGGACACCAAAGGC
TTCCACACAGAGGAGGATATCGGCGGACTTCACGCCACCATCGAGTGTGAGCAGCCCCAG
CCCGACCTCTACAAGTTCGTGGGTCGCATCAACGTTTACAGTGACCTGAATGACCCCGTG
GTGAGGCCCTTAGGATCGGAAAACCTGCTGCTTAGAGGAGCTACACTGAAGAACACTGAG
AAAATCTTTGGTGTGGCTATTTACACGGGAATGGAAACCAAGATGGCATTAAATTATCAA
TCAAAATCTCAGAAGCGATCTGCCGTGGAAAAATCGATGAATGCGTTCCTCATTGTGTAT
CTCTGCATTCTGATCAGCAAAGCCCTGATAAACACTGTGCTGAAATACATGTGGCAGAGT
GAGCCCTTTCGGGATGAGCCGTGGTATAATCAGAAAACGGAGTCGGAAAGGCAGAGGAAT
CTGTTCCTCAAGGCATTCACGGACTTCCTGGCCTTCATGGTCCTCTTTAACTACATCATC
CCTGTGTCCATGTACGTCACGGTCGAGATGCAGAAGTTCCTCGGCTCTTACTTCATCACC
TGGGACGAAGACATGTTTGACGAGGAGACTGGCGAGGGGCCTCTGGTGAACACGTCGGAC
CTCAATGAAGAGCTGGGACAGGTGGAGTACATCTTCACAGACAAGACCGGCACCCTCACG
GAAAACAACATGGAGTTCAAGGAGTGCTGCATCGAAGGCCATGTCTACGTGCCCCACGTC
ATCTGCAACGGGCAGGTCCTCCCAGAGTCGTCAGGAATCGACATGATTGACTCGTCCCCC
AGCGTCAACGGGAGGGAGCGCGAGGAGCTGTTTTTCCGGGCCCTCTGTCTCTGCCACACC
GTCCAGGTGAAAGACGATGACAGCGTAGACGGCCCCAGGAAATCGCCGGACGGGGGGAAA
TCCTGTGTGTACATCTCATCCTCGCCCGACGAGGTGGCGCTGGTCGAAGGTGTCCAGAGA
CTTGGCTTTACCTACCTAAGGCTGAAGGACAATTACATGGAGATATTAAACAGGGAGAAC
CACATCGAAAGGTTTGAATTGCTGGAAATTTTGAGTTTTGACTCAGTCAGAAGGAGAATG
AGTGTAATTGTAAAATCTGCTACAGGAGAAATTTATCTGTTTTGCAAAGGAGCAGATTCT
TCGATATTCCCCCGAGTGATAGAAGGCAAAGTTGACCAGATCCGAGCCAGAGTGGAGCGT
AACGCAGTGGAGGGGCTCCGAACTTTGTGTGTTGCTTATAAAAGGCTGATCCAAGAAGAA
TATGAAGGCATTTGTAAGCTGCTGCAGGCTGCCAAAGTGGCCCTTCAAGATCGAGAGAAA
AAGTTAGCAGAAGCCTATGAGCAAATAGAGAAAGATCTTACTCTGCTTGGTGCTACAGCT
GTTGAGGACCGGCTGCAGGAGAAAGCTGCAGACACCATCGAGGCCCTGCAGAAGGCCGGG
ATCAAAGTCTGGGTTCTCACGGGAGACAAGATGGAGACGGCCGCGGCCACGTGCTACGCC
TGCAAGCTCTTCCGCAGGAACACGCAGCTGCTGGAGCTGACCACCAAGAGGATCGAGGAG
CAGAGCCTGCACGACGTCCTGTTCGAGCTGAGCAAGACGGTCCTGCGCCACAGCGGGAGC
CTGACCAGAGACAACCTGTCCGGACTTTCAGCAGATATGCAGGACTACGGTTTAATTATC
GACGGAGCTGCACTGTCTCTGATAATGAAGCCTCGAGAAGACGGGAGTTCCGGCAACTAC
AGGGAGCTCTTCCTGGAAATCTGCCGGAGCTGCAGCGCGGTGCTCTGCTGCCGCATGGCG
CCCTTGCAGAAGGCTCAGATTGTTAAATTAATCAAATTTTCAAAAGAGCACCCAATCACG
TTAGCAATTGGCGATGGTGCAAATGATGTCAGCATGATTCTGGAAGCGCACGTGGGCATA
GGTGTCATCGGCAAGGAAGGCCGCCAGGCTGCCAGGAACAGCGACTATGCAATCCCAAAG
TTTAAGCATTTGAAGAAGATGCTGCTTGTTCACGGGCATTTTTATTACATTAGGATCTCT
GAGCTCGTGCAGTACTTCTTCTATAAGAACGTCTGCTTCATCTTCCCTCAGTTTTTATAC
CAGTTCTTCTGTGGGTTTTCACAACAGACTTTGTACGACACCGCGTATCTGACCCTCTAC
AACATCAGCTTCACCTCCCTCCCCATCCTCCTGTACAGCCTCATGGAGCAGCATGTTGGC
ATTGACGTGCTCAAGAGAGACCCGACCCTGTACAGGGACGTCGCCAAGAATGCCCTGCTG
CGCTGGCGCGTGTTCATCTACTGGACGCTCCTGGGACTGTTTGACGCACTGGTGTTCTTC
TTTGGTGCTTATTTCGTGTTTGAAAATACAACTGTGACAAGCAACGGGCAGATATTTGGA
AACTGGACGTTTGGAACGCTGGTATTCACCGTGATGGTGTTCACAGTTACACTAAAGCTT
GCATTGGACACACACTACTGGACTTGGATCAACCATTTTGTCATCTGGGGGTCGCTGCTG
TTCTACGTTGTCTTTTCGCTTCTCTGGGGAGGAGTGATCTGGCCGTTCCTCAACTACCAG
AGGATGTACTACGTGTTCATCCAGATGCTGTCCAGCGGGCCCGCCTGGCTGGCCATCGTG
CTGCTGGTGACCATCAGCCTCCTTCCCGACGTCCTCAAGAAAGTCCTGTGCCGGCAGCTG
TGGCCAACAGCAACAGAGAGAGTCCAGACTAAGAGCCAGTGCCTTTCTGTCGAGCAGTCA
ACCATCTTTATGCTTTCTCAGACTTCCAGCAGCCTGAGTTTCTGA
Enzyme 14 GenBank Gene ID NM_015205.2 Link Image
Enzyme 14 GeneCard ID ATP11A Link Image
Enzyme 14 GenAtlas ID ATP11A Link Image
Enzyme 14 HGNC ID HGNC:13552 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 13q34
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. 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]
  2. Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 6439
Enzyme 15 Name Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta isoform
Enzyme 15 Synonyms
  1. PI3-kinase subunit delta
  2. PI3K-delta
  3. PtdIns-3-kinase subunit delta
  4. Phosphatidylinositol-4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta
  5. PtdIns-3-kinase subunit p110-delta
Enzyme 15 Gene Name PIK3CD
Enzyme 15 Protein Sequence >Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta isoform
MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFH
MLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLL
IGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGP
GTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYT
LQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPR
AKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSS
SEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAW
ANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAP
HPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQE
HFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSL
RKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSV
ALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMR
QEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKN
GDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLN
KSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIM
IRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYC
ERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFN
EALRESWKTKVNWLAHNVSKDNRQ
Enzyme 15 Number of Residues 1044
Enzyme 15 Molecular Weight 119478.1
Enzyme 15 Theoretical pI 7.18
Enzyme 15 GO Classification
Function
  • 1-phosphatidylinositol-3-kinase activity
  • binding
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • kinase activity
  • lipid kinase activity
  • phosphatidylinositol-4,5-bisphosphate 3-kinase activity
  • phosphoinositide 3-kinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biological regulation
  • glycerophospholipid metabolic process
  • intracellular signal transduction
  • metabolic process
  • organophosphate metabolic process
  • phosphoinositide metabolic process
  • phosphoinositide phosphorylation
  • phosphoinositide-mediated signaling
  • phospholipid metabolic process
  • regulation of biological process
  • regulation of cellular process
  • second-messenger-mediated signaling
  • signal transduction
Component
  • macromolecular complex
  • phosphoinositide 3-kinase complex
  • protein complex
Enzyme 15 General Function Involved in binding
Enzyme 15 Specific Function ATP + 1-phosphatidyl-1D-myo-inositol 4,5- bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5- trisphosphate
Enzyme 15 Pathways
Enzyme 15 Reactions
  • ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate [RN:R04545]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 37496959 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID O00329 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name PK3CD_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >3135 bp
ATGCCCCCTGGGGTGGACTGCCCCATGGAATTCTGGACCAAGGAGGAGAATCAGAGCGTT
GTGGTTGACTTCCTGCTGCCCACAGGGGTCTACCTGAACTTCCCTGTGTCCCGCAATGCC
AACCTCAGCACCATCAAGCAGCTGCTGTGGCACCGCGCCCAGTATGAGCCGCTCTTCCAC
ATGCTCAGTGGCCCCGAGGCCTATGTGTTCACCTGCATCAACCAGACAGCGGAGCAGCAA
GAGCTGGAGGACGAGCAACGGCGTCTGTGTGACGTGCAGCCCTTCCTGCCCGTCCTGCGC
CTGGTGGCCCGTGAGGGCGACCGCGTGAAGAAGCTCATCAACTCACAGATCAGCCTCCTC
ATCGGCAAAGGCCTCCACGAGTTTGACTCCTTGTGCGACCCAGAAGTGAACGACTTTCGC
GCCAAGATGTGCCAATTCTGCGAGGAGGCGGCCGCCCGCCGGCAGCAGCTGGGCTGGGAG
GCCTGGCTGCAGTACAGTTTCCCCCTGCAGCTGGAGCCCTCGGCTCAAACCTGGGGGCCT
GGTACCCTGCGGCTCCCGAACCGGGCCCTTCTGGTCAACGTTAAGTTTGAGGGCAGCGAG
GAGAGCTTCACCTTCCAGGTGTCCACCAAGGACGTGCCGCTGGCGCTGATGGCCTGTGCC
CTGCGGAAGAAGGCCACAGTGTTCCGGCAGCCGCTGGTGGAGCAGCCGGAAGACTACACG
CTGCAGGTGAACGGCAGGCATGAGTACCTGTATGGCAGCTACCCGCTCTGCCAGTTCCAG
TACATCTGCAGCTGCCTGCACAGTGGGTTGACCCCTCACCTGACCATGGTCCATTCCTCC
TCCATCCTCGCCATGCGGGATGAGCAGAGCAACCCTGCCCCCCAGGTCCAGAAACCGCGT
GCCAAACCACCTCCCATTCCTGCGAAGAAGCCTTCCTCTGTGTCCCTGTGGTCCCTGGAG
CAGCCGTTCCGCATCGAGCTCATCCAGGGCAGCAAAGTGAACGCCGACGAGCGGATGAAG
CTGGTGGTGCAGGCCGGGCTTTTCCACGGCAACGAGATGCTGTGCAAGACGGTGTCCAGC
TCGGAGGTGAGCGTGTGCTCGGAGCCCGTGTGGAAGCAGCGGCTGGAGTTCGACATCAAC
ATCTGCGACCTGCCCCGCATGGCCCGTCTCTGCTTTGCGCTGTACGCCGTGATCGAGAAA
GCCAAGAAGGCTCGCTCCACCAAGAAGAAGTCCAAGAAGGCGGACTGCCCCATTGCCTGG
GCCAACCTCATGCTGTTTGACTACAAGGACCAGCTTAAGACCGGGGAACGCTGCCTCTAC
ATGTGGCCCTCCGTCCCAGATGAGAAGGGCGAGCTGCTGAACCCCACGGGCACTGTGCGC
AGTAACCCCAACACGGATAGCGCCGCTGCCCTGCTCATCTGCCTGCCCGAGGTGGCCCCG
CACCCCGTGTACTACCCCGCCCTGGAGAAGATCTTGGAGCTGGGGCGACACAGCGAGTGT
GTGCATGTCACCGAGGAGGAGCAGCTGCAGCTGCGGGAAATCCTGGAGCGGCGGGGGTCT
GGGGAGCTGTATGAGCACGAGAAGGACCTGGTGTGGAAGCTGCGGCATGAAGTCCAGGAG
CACTTCCCGGAGGCGCTAGCCCGGCTGCTGCTGGTCACCAAGTGGAACAAGCATGAGGAT
GTGGCCCAGATGCTCTACCTGCTGTGCTCCTGGCCGGAGCTGCCCGTCCTGAGCGCCCTG
GAGCTGCTAGACTTCAGCTTCCCCGATTGCCACGTAGGCTCCTTCGCCATCAAGTCGCTG
CGGAAACTGACGGACGATGAGCTGTTCCAGTACCTGCTGCAGCTGGTGCAGGTGCTCAAG
TACGAGTCCTACCTGGACTGCGAGCTGACCAAATTCCTGCTGGACCGGGCCCTGGCCAAC
CGCAAGATCGGCCACTTCCTTTTCTGGCACCTCCGCTCCGAGATGCACGTGCCGTCGGTG
GCCCTGCGCTTCGGCCTCATCCTGGAGGCCTACTGCAGGGGCAGCACCCACCACATGAAG
GTGCTGATGAAGCAGGGGGAAGCACTGAGCAAACTGAAGGCCCTGAATGACTTCGTCAAG
CTGAGCTCTCAGAAGACCCCCAAGCCCCAGACCAAGGAGCTGATGCACTTGTGCATGCGG
CAGGAGGCCTACCTAGAGGCCCTCTCCCACCTGCAGTCCCCACTCGACCCCAGCACCCTG
CTGGCTGAAGTCTGCGTGGAGCAGTGCACCTTCATGGACTCCAAGATGAAGCCCCTGTGG
ATCATGTACAGCAACGAGGAGGCAGGCAGCGGCGGCAGCGTGGGCATCATCTTTAAGAAC
GGGGATGACCTCCGGCAGGACATGCTGACCCTGCAGATGATCCAGCTCATGGACGTCCTG
TGGAAGCAGGAGGGGCTGGACCTGAGGATGACCCCCTATGGCTGCCTCCCCACCGGGGAC
CGCACAGGCCTCATTGAGGTGGTACTCCGTTCAGACACCATCGCCAACATCCAACTCAAC
AAGAGCAACATGGCAGCCACAGCCGCCTTCAACAAGGATGCCCTGCTCAACTGGCTGAAG
TCCAAGAACCCGGGGGAGGCCCTGGATCGAGCCATTGAGGAGTTCACCCTCTCCTGTGCT
GGCTATTGTGTGGCCACATATGTGCTGGGCATTGGCGATCGGCACAGCGACAACATCATG
ATCCGAGAGAGTGGGCAGCTGTTCCACATTGATTTTGGCCACTTTCTGGGGAATTTCAAG
ACCAAGTTTGGAATCAACCGCGAGCGTGTCCCATTCATCCTCACCTACGACTTTGTCCAT
GTGATTCAGCAGGGGAAGACTAATAATAGTGAGAAATTTGAACGGTTCCGGGGCTACTGT
GAAAGGGCCTACACCATCCTGCGGCGCCACGGGCTTCTCTTCCTCCACCTCTTTGCCCTG
ATGCGGGCGGCAGGCCTGCCTGAGCTCAGCTGCTCCAAAGACATCCAGTATCTCAAGGAC
TCCCTGGCACTGGGGAAAACAGAGGAGGAGGCACTGAAGCACTTCCGAGTGAAGTTTAAC
GAAGCCCTCCGTGAGAGCTGGAAAACCAAAGTGAACTGGCTGGCCCACAACGTGTCCAAA
GACAACAGGCAGTAG
Enzyme 15 GenBank Gene ID Y10055 Link Image
Enzyme 15 GeneCard ID PIK3CD Link Image
Enzyme 15 GenAtlas ID PIK3CD Link Image
Enzyme 15 HGNC ID HGNC:8977 Link Image
Enzyme 15 Chromosome Location 1
Enzyme 15 Locus 1p36.2
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Vanhaesebroeck B, Welham MJ, Kotani K, Stein R, Warne PH, Zvelebil MJ, Higashi K, Volinia S, Downward J, Waterfield MD: P110delta, a novel phosphoinositide 3-kinase in leukocytes. Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4330-5. [PubMed Link Image]
  2. Chantry D, Vojtek A, Kashishian A, Holtzman DA, Wood C, Gray PW, Cooper JA, Hoekstra MF: p110delta, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes. J Biol Chem. 1997 Aug 1;272(31):19236-41. [PubMed Link Image]
  3. 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]
  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. Vanhaesebroeck B, Higashi K, Raven C, Welham M, Anderson S, Brennan P, Ward SG, Waterfield MD: Autophosphorylation of p110delta phosphoinositide 3-kinase: a new paradigm for the regulation of lipid kinases in vitro and in vivo. EMBO J. 1999 Mar 1;18(5):1292-302. [PubMed Link Image]
  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. 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]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 6465
Enzyme 16 Name Probable phospholipid-transporting ATPase VA
Enzyme 16 Synonyms
  1. ATPase class V type 10A
  2. Aminophospholipid translocase VA
Enzyme 16 Gene Name ATP10A
Enzyme 16 Protein Sequence >Probable phospholipid-transporting ATPase VA
MEREPAGTEEPGPPGRRRRREGRTRTVRSNLLPPPGAEDPAAGAAKGERRRRRGCAQHLA
DNRLKTTKYTLLSFLPKNLFEQFHRPANVYFVFIALLNFVPAVNAFQPGLALAPVLFILA
ITAFRDLWEDYSRHRSDHKINHLGCLVFSREEKKYVNRFWKEIHVGDFVRLRCNEIFPAD
ILLLSSSDPDGLCHIETANLDGETNLKRRQVVRGFSELVSEFNPLTFTSVIECEKPNNDL
SRFRGCIIHDNGKKAGLYKENLLLRGCTLRNTDAVVGIVIYAGHETKALLNNSGPRYKRS
KLERQMNCDVLWCVLLLVCMSLFSAVGHGLWIWRYQEKKSLFYVPKSDGSSLSPVTAAVY
SFLTMIIVLQVLIPISLYVSIEIVKACQVYFINQDMQLYDEETDSQLQCRALNITEDLGQ
IQYIFSDKTGTLTENKMVFRRCTVSGVEYSHDANAQRLARYQEADSEEEEVVPRGGSVSQ
RGSIGSHQSVRVVHRTQSTKSHRRTGSRAEAKRASMLSKHTAFSSPMEKDITPDPKLLEK
VSECDKSLAVARHQEHLLAHLSPELSDVFDFFIALTICNTVVVTSPDQPRTKVRVRFELK
SPVKTIEDFLRRFTPSCLTSGCSSIGSLAANKSSHKLGSSFPSTPSSDGMLLRLEERLGQ
PTSAIASNGYSSQADNWASELAQEQESERELRYEAESPDEAALVYAARAYNCVLVERLHD
QVSVELPHLGRLTFELLHTLGFDSVRKRMSVVIRHPLTDEINVYTKGADSVVMDLLQPCS
SVDARGRHQKKIRSKTQNYLNVYAAEGLRTLCIAKRVLSKEEYACWLQSHLEAESSLENS
EELLFQSAIRLETNLHLLGATGIEDRLQDGVPETISKLRQAGLQIWVLTGDKQETAVNIA
YACKLLDHDEEVITLNATSQEACAALLDQCLCYVQSRGLQRAPEKTKGKVSMRFSSLCPP
STSTASGRRPSLVIDGRSLAYALEKNLEDKFLFLAKQCRSVLCCRSTPLQKSMVVKLVRS
KLKAMTLAIGDGANDVSMIQVADVGVGISGQEGMQAVMASDFAVPKFRYLERLLILHGHW
CYSRLANMVLYFFYKNTMFVGLLFWFQFFCGFSASTMIDQWYLIFFNLLFSSLPPLVTGV
LDRDVPANVLLTNPQLYKSGQNMEEYRPRTFWFNMADAAFQSLVCFSIPYLAYYDSNVDL
FTWGTPIVTIALLTFLLHLGIETKTWTWLNWITCGFSVLLFFTVALIYNASCATCYPPSN
PYWTMQALLGDPVFYLTCLMTPVAALLPRLFFRSLQGRVFPTQLQLARQLTRKSPRRCSA
PKETFAQGRLPKDSGTEHSSGRTVKTSVPLSQPSWHTQQPVCSLEASGEPSTVDMSMPVR
EHTLLEGLSAPAPMSSAPGEAVLRSPGGCPEESKVRAASTGRVTPLSSLFSLPTFSLLNW
ISSWSLVSRLGSVLQFSRTEQLADGQAGRGLPVQPHSGRSGLQGPDHRLLIGASSRRSQ
Enzyme 16 Number of Residues 1499
Enzyme 16 Molecular Weight 167686.6
Enzyme 16 Theoretical pI 8.43
Enzyme 16 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • ion binding
  • ion transmembrane transporter activity
  • lipid transporter activity
  • magnesium ion binding
  • metal ion binding
  • nucleoside binding
  • phospholipid transporter activity
  • phospholipid-translocating ATPase activity
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • substrate-specific transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • cellular nitrogen compound metabolic process
  • establishment of localization
  • lipid transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phospholipid transport
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 16 General Function Involved in ATP binding
Enzyme 16 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions
  • ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • 87-106 111-128 310-332 363-384 1088-1108 1120-1140 1171-1192 1200-1222 1229-1249 1268-1292
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 14424433 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID O60312 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name AT10A_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >4500 bp
ATGGAGCGGGAGCCGGCGGGGACCGAGGAGCCCGGGCCTCCGGGACGGCGGAGGCGCCGA
GAGGGCAGGACGCGCACGGTGCGCTCCAACCTGCTGCCGCCCCCGGGCGCCGAGGACCCT
GCGGCTGGCGCGGCCAAGGGCGAGCGGCGACGGCGGCGCGGGTGTGCCCAGCACCTGGCC
GACAACCGGCTCAAGACTACCAAGTACACGCTGCTGTCCTTCCTGCCCAAGAACCTGTTC
GAGCAGTTCCACCGCCCGGCCAACGTGTACTTTGTCTTCATCGCGCTGCTCAACTTCGTG
CCGGCGGTGAACGCCTTCCAGCCCGGCCTGGCACTGGCGCCGGTGCTCTTCATCCTGGCC
ATCACGGCCTTCAGGGACCTGTGGGAGGACTACAGCCGCCACCGCTCCGACCACAAGATC
AACCACCTGGGCTGCCTGGTCTTCAGCAGGGAAGAAAAGAAATACGTGAACCGATTCTGG
AAAGAAATCCACGTGGGAGACTTTGTGCGTCTTCGCTGCAACGAAATCTTCCCTGCGGAC
ATTCTGCTGCTCTCCTCCAGTGACCCCGACGGGCTATGCCACATCGAGACCGCCAACCTG
GATGGAGAGACCAACCTGAAGCGGCGGCAGGTGGTCCGCGGCTTCTCGGAGCTTGTCTCC
GAATTCAATCCTTTGACGTTCACCAGCGTGATCGAATGCGAGAAGCCAAACAACGACCTG
AGTAGGTTTCGCGGCTGCATCATACATGACAACGGGAAAAAGGCCGGGCTGTATAAAGAA
AACCTGCTGCTGAGGGGCTGCACCCTTAGGAACACGGACGCAGTCGTCGGCATTGTCATC
TACGCAGGACATGAAACCAAGGCTCTGCTGAACAACAGTGGGCCCCGCTACAAGCGCAGC
AAGCTGGAGAGGCAGATGAACTGCGACGTGCTCTGGTGTGTCCTGCTCCTTGTTTGCATG
TCTCTGTTTTCAGCAGTCGGACATGGACTGTGGATATGGCGGTATCAAGAGAAGAAGTCA
TTATTTTATGTCCCCAAGTCTGATGGAAGCTCCTTATCCCCAGTCACAGCTGCAGTTTAC
TCATTTTTAACAATGATAATAGTTCTGCAGGTTTTGATCCCAATTTCCTTATACGTTTCC
ATTGAAATTGTTAAAGCATGCCAAGTGTACTTCATTAACCAGGACATGCAGTTGTATGAC
GAAGAAACAGACTCGCAGCTGCAGTGCCGAGCTCTGAACATCACGGAAGACTTAGGACAG
ATACAGTACATTTTCTCAGATAAAACTGGCACTTTGACAGAGAATAAGATGGTTTTCCGA
AGATGCACTGTGTCTGGTGTAGAATATTCTCATGATGCAAATGCGCAGCGTCTGGCCAGG
TACCAAGAGGCAGACTCGGAGGAGGAGGAGGTGGTGCCCAGAGGGGGCTCGGTGTCCCAG
CGCGGCAGCATCGGCAGCCACCAGAGTGTCCGGGTGGTGCACAGAACCCAGAGCACCAAG
TCCCACCGGCGCACGGGCAGCCGGGCCGAGGCCAAGAGGGCCAGCATGCTGTCCAAGCAC
ACGGCCTTCAGCAGCCCCATGGAGAAGGATATCACGCCCGACCCAAAGCTGCTGGAGAAG
GTGAGTGAGTGTGACAAGAGCCTAGCCGTGGCGAGGCATCAGGAGCACCTGCTGGCCCAC
CTCTCGCCTGAGCTGTCTGACGTCTTTGATTTCTTCATCGCACTCACCATCTGCAACACA
GTCGTCGTCACGTCCCCGGATCAGCCACGAACAAAGGTGAGGGTGAGGTTTGAGCTGAAG
TCCCCGGTGAAGACGATAGAAGACTTCCTGCGGAGGTTCACACCCAGCTGCCTGACCTCA
GGCTGCAGCAGCATCGGGAGCCTGGCCGCCAACAAGTCCAGCCACAAGTTGGGCTCCAGC
TTCCCGTCCACCCCGTCCAGCGACGGCATGCTTCTCAGGCTGGAGGAGAGGCTGGGCCAG
CCCACCTCGGCCATCGCCAGCAACGGCTACAGCAGCCAGGCGGACAACTGGGCCTCGGAG
CTTGCTCAGGAGCAGGAGTCAGAGCGCGAGCTGCGGTACGAGGCGGAGAGCCCGGATGAG
GCCGCACTGGTGTATGCGGCCAGAGCCTACAACTGCGTGCTTGTGGAGCGGCTGCACGAC
CAAGTGTCAGTGGAGCTGCCCCACCTGGGCAGGCTCACCTTCGAGCTCCTGCACACACTG
GGTTTCGATTCCGTCCGCAAGAGGATGTCAGTGGTGATCCGGCACCCGCTTACCGATGAG
ATCAACGTCTACACCAAGGGGGCCGACTCAGTGGTCATGGATCTCCTGCAGCCCTGCTCT
TCAGTTGACGCCAGAGGGAGGCATCAAAAAAAGATTCGGAGCAAAACTCAGAATTACCTC
AACGTGTATGCGGCGGAAGGCCTGCGCACCTTGTGCATCGCCAAGAGAGTTCTGAGTAAA
GAAGAGTATGCCTGCTGGTTGCAAAGCCACCTAGAAGCCGAATCCTCCCTGGAAAACAGC
GAGGAGCTCCTCTTCCAGTCTGCCATTCGCCTGGAGACCAACCTGCACTTGTTAGGTGCC
ACTGGGATTGAAGACCGCCTGCAGGACGGAGTCCCTGAAACTATTTCTAAATTGCGTCAA
GCGGGCCTGCAGATTTGGGTTCTCACTGGTGACAAACAAGAAACAGCTGTCAACATTGCA
TATGCCTGCAAACTGCTGGACCACGACGAGGAGGTCATCACCCTGAATGCCACCTCCCAG
GAGGCGTGTGCAGCCCTGCTAGACCAGTGCCTATGCTACGTGCAGTCCAGAGGCCTCCAG
AGAGCCCCTGAGAAGACCAAGGGCAAAGTGAGCATGAGGTTCTCCTCTCTCTGCCCACCC
TCCACGTCCACTGCCTCTGGCCGCAGACCCAGCCTCGTGATCGATGGGAGAAGCCTGGCC
TACGCTCTCGAGAAAAACCTGGAGGACAAATTCCTCTTCCTTGCCAAGCAGTGCCGCTCC
GTCCTCTGCTGTCGGTCGACGCCTCTGCAGAAGAGCATGGTGGTGAAGCTGGTGCGGAGC
AAGCTCAAGGCCATGACCCTGGCCATAGGTGATGGAGCCAATGATGTCAGCATGATCCAG
GTGGCAGATGTGGGTGTGGGAATCTCCGGCCAGGAGGGTATGCAGGCAGTGATGGCCAGC
GACTTTGCAGTGCCGAAATTCCGATACCTGGAGAGGCTCTTGATTCTTCACGGGCATTGG
TGCTACTCCCGACTTGCCAACATGGTGCTGTACTTCTTCTACAAAAACACAATGTTCGTG
GGCCTCCTGTTTTGGTTCCAGTTTTTCTGTGGCTTCTCTGCATCTACCATGATTGACCAG
TGGTATCTAATCTTCTTTAATCTGCTCTTCTCGTCACTTCCCCCGCTCGTGACTGGGGTG
CTGGACAGGGATGTGCCAGCCAATGTGCTGCTGACCAACCCGCAGCTCTACAAGAGTGGC
CAGAACATGGAGGAATACCGGCCACGAACGTTCTGGTTTAACATGGCCGACGCCGCCTTC
CAGAGCCTGGTTTGCTTTTCCATTCCTTACCTGGCCTACTATGACTCGAACGTGGACCTG
TTTACCTGGGGGACCCCTATTGTGACAATCGCGCTGCTCACTTTCCTGCTCCACCTGGGC
ATTGAAACCAAAACCTGGACCTGGCTCAACTGGATAACGTGTGGCTTCAGTGTCCTTTTG
TTTTTCACCGTGGCTTTGATTTACAATGCGTCTTGTGCCACGTGCTATCCTCCGTCCAAC
CCTTACTGGACTATGCAAGCCTTACTGGGTGACCCAGTGTTTTACTTGACTTGCCTGATG
ACGCCTGTCGCTGCACTGCTGCCCAGATTGTTTTTCAGATCCCTCCAGGGGAGGGTTTTC
CCCACACAACTTCAGCTGGCACGTCAGTTGACCAGGAAGTCCCCCAGGAGATGCAGTGCT
CCCAAAGAGACCTTTGCTCAGGGACGCCTCCCGAAGGACTCGGGAACCGAGCACTCATCA
GGGAGGACAGTCAAGACCTCTGTGCCCCTGTCCCAGCCTTCTTGGCACACACAGCAGCCG
GTCTGCTCCCTGGAGGCCAGCGGGGAGCCCAGCACAGTGGACATGAGCATGCCAGTGAGG
GAGCACACCCTGCTGGAGGGGCTGAGCGCACCGGCCCCCATGTCCTCTGCGCCAGGGGAG
GCTGTCCTGAGGAGTCCAGGAGGGTGTCCTGAGGAGTCCAAGGTGAGAGCTGCCAGCACC
GGCAGGGTGACCCCCCTGTCTTCCCTCTTCAGCCTGCCTACCTTCAGCTTACTCAACTGG
ATTTCCTCCTGGTCGCTGGTCAGCAGGCTGGGGAGTGTCTTACAGTTCTCCCGGACGGAG
CAGCTTGCAGATGGACAAGCGGGACGTGGACTTCCTGTCCAGCCCCACTCAGGCCGATCA
GGACTTCAAGGGCCAGACCACAGACTACTTATAGGAGCATCTTCAAGGCGGTCACAGTGA
Enzyme 16 GenBank Gene ID NM_024490.3 Link Image
Enzyme 16 GeneCard ID ATP10A Link Image
Enzyme 16 GenAtlas ID ATP10A Link Image
Enzyme 16 HGNC ID HGNC:13542 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 15q11.2
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Meguro M, Kashiwagi A, Mitsuya K, Nakao M, Kondo I, Saitoh S, Oshimura M: A novel maternally expressed gene, ATP10C, encodes a putative aminophospholipid translocase associated with Angelman syndrome. Nat Genet. 2001 May;28(1):19-20. [PubMed Link Image]
  2. Herzing LB, Kim SJ, Cook EH Jr, Ledbetter DH: The human aminophospholipid-transporting ATPase gene ATP10C maps adjacent to UBE3A and exhibits similar imprinted expression. Am J Hum Genet. 2001 Jun;68(6):1501-5. Epub 2001 May 11. [PubMed Link Image]
  3. 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, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 6488
Enzyme 17 Name Probable phospholipid-transporting ATPase IC
Enzyme 17 Synonyms
  1. ATPase class I type 8B member 1
  2. Familial intrahepatic cholestasis type 1
Enzyme 17 Gene Name ATP8B1
Enzyme 17 Protein Sequence >Probable phospholipid-transporting ATPase IC
MSTERDSETTFDEDSQPNDEVVPYSDDETEDELDDQGSAVEPEQNRVNREAEENREPFRK
ECTWQVKANDRKYHEQPHFMNTKFLCIKESKYANNAIKTYKYNAFTFIPMNLFEQFKRAA
NLYFLALLILQAVPQISTLAWYTTLVPLLVVLGVTAIKDLVDDVARHKMDKEINNRTCEV
IKDGRFKVAKWKEIQVGDVIRLKKNDFVPADILLLSSSEPNSLCYVETAELDGETNLKFK
MSLEITDQYLQREDTLATFDGFIECEEPNNRLDKFTGTLFWRNTSFPLDADKILLRGCVI
RNTDFCHGLVIFAGADTKIMKNSGKTRFKRTKIDYLMNYMVYTIFVVLILLSAGLAIGHA
YWEAQVGNSSWYLYDGEDDTPSYRGFLIFWGYIIVLNTMVPISLYVSVEVIRLGQSHFIN
WDLQMYYAEKDTPAKARTTTLNEQLGQIHYIFSDKTGTLTQNIMTFKKCCINGQIYGDHR
DASQHNHNKIEQVDFSWNTYADGKLAFYDHYLIEQIQSGKEPEVRQFFFLLAVCHTVMVD
RTDGQLNYQAASPDEGALVNAARNFGFAFLARTQNTITISELGTERTYNVLAILDFNSDR
KRMSIIVRTPEGNIKLYCKGADTVIYERLHRMNPTKQETQDALDIFANETLRTLCLCYKE
IEEKEFTEWNKKFMAASVASTNRDEALDKVYEEIEKDLILLGATAIEDKLQDGVPETISK
LAKADIKIWVLTGDKKETAENIGFACELLTEDTTICYGEDINSLLHARMENQRNRGGVYA
KFAPPVQESFFPPGGNRALIITGSWLNEILLEKKTKRNKILKLKFPRTEEERRMRTQSKR
RLEAKKEQRQKNFVDLACECSAVICCRVTPKQKAMVVDLVKRYKKAITLAIGDGANDVNM
IKTAHIGVGISGQEGMQAVMSSDYSFAQFRYLQRLLLVHGRWSYIRMCKFLRYFFYKNFA
FTLVHFWYSFFNGYSAQTAYEDWFITLYNVLYTSLPVLLMGLLDQDVSDKLSLRFPGLYI
VGQRDLLFNYKRFFVSLLHGVLTSMILFFIPLGAYLQTVGQDGEAPSDYQSFAVTIASAL
VITVNFQIGLDTSYWTFVNAFSIFGSIALYFGIMFDFHSAGIHVLFPSAFQFTGTASNAL
RQPYIWLTIILAVAVCLLPVVAIRFLSMTIWPSESDKIQKHRKRLKAEEQWQRRQQVFRR
GVSTRRSAYAFSHQRGYADLISSGRSIRKKRSPLDAIVADGTAEYRRTGDS
Enzyme 17 Number of Residues 1251
Enzyme 17 Molecular Weight 143694.1
Enzyme 17 Theoretical pI 7.16
Enzyme 17 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • ion binding
  • ion transmembrane transporter activity
  • lipid transporter activity
  • magnesium ion binding
  • metal ion binding
  • nucleoside binding
  • phospholipid transporter activity
  • phospholipid-translocating ATPase activity
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • substrate-specific transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • cellular nitrogen compound metabolic process
  • establishment of localization
  • lipid transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phospholipid transport
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 17 General Function Involved in ATP binding
Enzyme 17 Specific Function May play a role in the transport of aminophospholipids from the outer to the inner leaflet of various membranes and the maintenance of asymmetric distribution of phospholipids in the canicular membrane. May have a role in transport of bile acids into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions
  • ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • 109-130 137-156 341-362 390-411 950-970 983-1002 1033-1054 1069-1091 1098-1118 1139-1163
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 5031697 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID O43520 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name AT8B1_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >3756 bp
ATGAGTACAGAAAGAGACTCAGAAACGACATTTGACGAGGATTCTCAGCCTAATGACGAA
GTGGTTCCCTACAGTGATGATGAAACAGAAGATGAACTTGATGACCAGGGGTCTGCTGTT
GAACCAGAACAAAACCGAGTCAACAGGGAAGCAGAGGAGAACCGGGAGCCATTCAGAAAA
GAATGTACATGGCAAGTCAAAGCAAACGATCGCAAGTACCACGAACAACCTCACTTTATG
AACACAAAATTCTTGTGTATTAAGGAGAGTAAATATGCGAATAATGCAATTAAAACATAC
AAGTACAACGCATTTACCTTTATACCAATGAATCTGTTTGAGCAGTTTAAGAGAGCAGCC
AATTTATATTTCCTGGCTCTTCTTATCTTACAGGCAGTTCCTCAAATCTCTACCCTGGCT
TGGTACACCACACTAGTGCCCCTGCTTGTGGTGCTGGGCGTCACTGCAATCAAAGACCTG
GTGGACGATGTGGCTCGCCATAAAATGGATAAGGAAATCAACAATAGGACGTGTGAAGTC
ATTAAGGATGGCAGGTTCAAAGTTGCTAAGTGGAAAGAAATTCAAGTTGGAGACGTCATT
CGTCTGAAAAAAAATGATTTTGTTCCAGCTGACATTCTCCTGCTGTCTAGCTCTGAGCCT
AACAGCCTCTGCTATGTGGAAACAGCAGAACTGGATGGAGAAACCAATTTAAAATTTAAG
ATGTCACTTGAAATCACAGACCAGTACCTCCAAAGAGAAGATACATTGGCTACATTTGAT
GGTTTTATTGAATGTGAAGAACCCAATAACAGACTAGATAAGTTTACAGGAACACTATTT
TGGAGAAACACAAGTTTTCCTTTGGATGCTGATAAAATTTTGTTACGTGGCTGTGTAATT
AGGAACACCGATTTCTGCCACGGCTTAGTCATTTTTGCAGGTGCTGACACTAAAATAATG
AAGAATAGTGGGAAAACCAGATTTAAAAGAACTAAAATTGATTACTTGATGAACTACATG
GTTTACACGATCTTTGTTGTTCTTATTCTGCTTTCTGCTGGTCTTGCCATCGGCCATGCT
TATTGGGAAGCACAGGTGGGCAATTCCTCTTGGTACCTCTATGATGGAGAAGACGATACA
CCCTCCTACCGTGGATTCCTCATTTTCTGGGGCTATATCATTGTTCTCAACACCATGGTA
CCCATCTCTCTCTATGTCAGCGTGGAAGTGATTCGTCTTGGACAGAGTCACTTCATCAAC
TGGGACCTGCAAATGTACTATGCTGAGAAGGACACACCCGCAAAAGCTAGAACCACCACA
CTCAATGAACAGCTCGGGCAGATCCATTATATCTTCTCTGATAAGACGGGGACACTCACA
CAAAATATCATGACCTTTAAAAAGTGCTGTATCAACGGGCAGATATATGGGGACCATCGG
GATGCCTCTCAACACAACCACAACAAAATAGAGCAAGTTGATTTTAGCTGGAATACATAT
GCTGATGGGAAGCTTGCATTTTATGACCACTATCTTATTGAGCAAATCCAGTCAGGGAAA
GAGCCAGAAGTACGACAGTTCTTCTTCTTGCTCGCAGTTTGCCACACAGTCATGGTGGAT
AGGACTGATGGTCAGCTCAACTACCAGGCAGCCTCTCCCGATGAAGGTGCCCTGGTAAAC
GCTGCCAGGAACTTTGGCTTTGCCTTCCTCGCCAGGACCCAGAACACCATCACCATCAGT
GAACTGGGCACTGAAAGGACTTACAATGTTCTTGCCATTTTGGACTTCAACAGTGACCGG
AAGCGAATGTCTATCATTGTAAGAACCCCAGAAGGCAATATCAAGCTTTACTGTAAAGGT
GCTGACACTGTTATTTATGAACGGTTACATCGAATGAATCCTACTAAGCAAGAAACACAG
GATGCCCTGGATATCTTTGCAAATGAAACTCTTAGAACCCTATGCCTTTGCTACAAGGAA
ATTGAAGAAAAAGAATTTACAGAATGGAATAAAAAGTTTATGGCTGCCAGTGTGGCCTCC
ACCAACCGGGACGAAGCTCTGGATAAAGTATATGAGGAGATTGAAAAAGACTTAATTCTC
CTGGGAGCTACAGCTATTGAAGACAAGCTACAGGATGGAGTTCCAGAAACCATTTCAAAA
CTTGCAAAAGCTGACATTAAGATCTGGGTGCTTACTGGAGACAAAAAGGAAACTGCTGAA
AATATAGGATTTGCTTGTGAACTTCTGACTGAAGACACCACCATCTGCTATGGGGAGGAT
ATTAATTCTCTTCTTCATGCAAGGATGGAAAACCAGAGGAATAGAGGTGGCGTCTACGCA
AAGTTTGCACCTCCTGTGCAGGAATCTTTTTTTCCACCCGGTGGAAACCGTGCCTTAATC
ATCACTGGTTCTTGGTTGAATGAAATTCTTCTCGAGAAAAAGACCAAGAGAAATAAGATT
CTGAAGCTGAAGTTCCCAAGAACAGAAGAAGAAAGACGGATGCGGACCCAAAGTAAAAGG
AGGCTAGAAGCTAAGAAAGAGCAGCGGCAGAAAAACTTTGTGGACCTGGCCTGCGAGTGC
AGCGCAGTCATCTGCTGCCGCGTCACCCCCAAGCAGAAGGCCATGGTGGTGGACCTGGTG
AAGAGGTACAAGAAAGCCATCACGCTGGCCATCGGAGATGGGGCCAATGACGTGAACATG
ATCAAAACTGCCCACATTGGCGTTGGAATAAGTGGACAAGAAGGAATGCAAGCTGTCATG
TCGAGTGACTATTCCTTTGCTCAGTTCCGATATCTGCAGAGGCTACTGCTGGTGCATGGC
CGATGGTCTTACATAAGGATGTGCAAGTTCCTACGATACTTCTTTTACAAAAACTTTGCC
TTTACTTTGGTTCATTTCTGGTACTCCTTCTTCAATGGCTACTCTGCGCAGACTGCATAC
GAGGATTGGTTCATCACCCTCTACAACGTGCTGTACACCAGCCTGCCCGTGCTCCTCATG
GGGCTGCTCGACCAGGATGTGAGTGACAAACTGAGCCTCCGATTCCCTGGGTTATACATA
GTGGGACAAAGAGACTTACTATTCAACTATAAGAGATTCTTTGTAAGCTTGTTGCATGGG
GTCCTAACATCGATGATCCTCTTCTTCATACCTCTTGGAGCTTATCTGCAAACCGTAGGG
CAGGATGGAGAGGCACCTTCCGACTACCAGTCTTTTGCCGTCACCATTGCCTCTGCTCTT
GTAATAACAGTCAATTTCCAGATTGGCTTGGATACTTCTTATTGGACTTTTGTGAATGCT
TTTTCAATTTTTGGAAGCATTGCACTTTATTTTGGCATCATGTTTGACTTTCATAGTGCT
GGAATACATGTTCTCTTTCCATCTGCATTTCAATTTACAGGCACAGCTTCAAACGCTCTG
AGACAGCCATACATTTGGTTAACTATCATCCTGACTGTTGCTGTGTGCTTACTACCCGTC
GTTGCCATTCGATTCCTGTCAATGACCATCTGGCCATCAGAAAGTGATAAGATCCAGAAG
CATCGCAAGCGGTTGAAGGCGGAGGAGCAGTGGCAGCGACGGCAGCAGGTGTTCCGCCGG
GGCGTGTCAACGCGGCGCTCGGCCTACGCCTTCTCGCACCAGCGGGGCTACGCGGACCTC
ATCTCCTCCGGGCGCAGCATCCGCAAGAAGCGCTCGCCGCTTGATGCCATCGTGGCGGAT
GGCACCGCGGAGTACAGGCGCACCGGGGACAGCTGA
Enzyme 17 GenBank Gene ID NM_005603.4 Link Image
Enzyme 17 GeneCard ID ATP8B1 Link Image
Enzyme 17 GenAtlas ID ATP8B1 Link Image
Enzyme 17 HGNC ID HGNC:3706 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 18q21-q22|18q21.31
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Bull LN, van Eijk MJ, Pawlikowska L, DeYoung JA, Juijn JA, Liao M, Klomp LW, Lomri N, Berger R, Scharschmidt BF, Knisely AS, Houwen RH, Freimer NB: A gene encoding a P-type ATPase mutated in two forms of hereditary cholestasis. Nat Genet. 1998 Mar;18(3):219-24. [PubMed Link Image]
  2. Nusbaum C, Zody MC, Borowsky ML, Kamal M, Kodira CD, Taylor TD, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Abouelleil A, Allen NR, Anderson S, Bloom T, Bugalter B, Butler J, Cook A, DeCaprio D, Engels R, Garber M, Gnirke A, Hafez N, Hall JL, Norman CH, Itoh T, Jaffe DB, Kuroki Y, Lehoczky J, Lui A, Macdonald P, Mauceli E, Mikkelsen TS, Naylor JW, Nicol R, Nguyen C, Noguchi H, O'Leary SB, O'Neill K, Piqani B, Smith CL, Talamas JA, Topham K, Totoki Y, Toyoda A, Wain HM, Young SK, Zeng Q, Zimmer AR, Fujiyama A, Hattori M, Birren BW, Sakaki Y, Lander ES: DNA sequence and analysis of human chromosome 18. Nature. 2005 Sep 22;437(7058):551-5. [PubMed Link Image]
  3. Halleck MS, Pradhan D, Blackman C, Berkes C, Williamson P, Schlegel RA: Multiple members of a third subfamily of P-type ATPases identified by genomic sequences and ESTs. Genome Res. 1998 Apr;8(4):354-61. [PubMed Link Image]
  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. 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]
  6. Tygstrup N, Steig BA, Juijn JA, Bull LN, Houwen RH: Recurrent familial intrahepatic cholestasis in the Faeroe Islands. Phenotypic heterogeneity but genetic homogeneity. Hepatology. 1999 Feb;29(2):506-8. [PubMed Link Image]
  7. Klomp LW, Bull LN, Knisely AS, van Der Doelen MA, Juijn JA, Berger R, Forget S, Nielsen IM, Eiberg H, Houwen RH: A missense mutation in FIC1 is associated with greenland familial cholestasis. Hepatology. 2000 Dec;32(6):1337-41. [PubMed Link Image]
  8. Klomp LW, Vargas JC, van Mil SW, Pawlikowska L, Strautnieks SS, van Eijk MJ, Juijn JA, Pabon-Pena C, Smith LB, DeYoung JA, Byrne JA, Gombert J, van der Brugge G, Berger R, Jankowska I, Pawlowska J, Villa E, Knisely AS, Thompson RJ, Freimer NB, Houwen RH, Bull LN: Characterization of mutations in ATP8B1 associated with hereditary cholestasis. Hepatology. 2004 Jul;40(1):27-38. [PubMed Link Image]
  9. Painter JN, Savander M, Ropponen A, Nupponen N, Riikonen S, Ylikorkala O, Lehesjoki AE, Aittomaki K: Sequence variation in the ATP8B1 gene and intrahepatic cholestasis of pregnancy. Eur J Hum Genet. 2005 Apr;13(4):435-9. [PubMed Link Image]
  10. Mullenbach R, Bennett A, Tetlow N, Patel N, Hamilton G, Cheng F, Chambers J, Howard R, Taylor-Robinson SD, Williamson C: ATP8B1 mutations in British cases with intrahepatic cholestasis of pregnancy. Gut. 2005 Jun;54(6):829-34. [PubMed Link Image]
  11. 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 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6504
Enzyme 18 Name Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform
Enzyme 18 Synonyms
  1. PI3-kinase subunit beta
  2. PI3K-beta
  3. PtdIns-3-kinase subunit beta
  4. Phosphatidylinositol-4,5-bisphosphate 3-kinase 110 kDa catalytic subunit beta
  5. PtdIns-3-kinase subunit p110-beta
Enzyme 18 Gene Name PIK3CB
Enzyme 18 Protein Sequence >Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform
MCFSFIMPPAMADILDIWAVDSQIASDGSIPVDFLLPTGIYIQLEVPREATISYIKQMLW
KQVHNYPMFNLLMDIDSYMFACVNQTAVYEELEDETRRLCDVRPFLPVLKLVTRSCDPGE
KLDSKIGVLIGKGLHEFDSLKDPEVNEFRRKMRKFSEEKILSLVGLSWMDWLKQTYPPEH
EPSIPENLEDKLYGGKLIVAVHFENCQDVFSFQVSPNMNPIKVNELAIQKRLTIHGKEDE
VSPYDYVLQVSGRVEYVFGDHPLIQFQYIRNCVMNRALPHFILVECCKIKKMYEQEMIAI
EAAINRNSSNLPLPLPPKKTRIISHVWENNNPFQIVLVKGNKLNTEETVKVHVRAGLFHG
TELLCKTIVSSEVSGKNDHIWNEPLEFDINICDLPRMARLCFAVYAVLDKVKTKKSTKTI
NPSKYQTIRKAGKVHYPVAWVNTMVFDFKGQLRTGDIILHSWSSFPDELEEMLNPMGTVQ
TNPYTENATALHVKFPENKKQPYYYPPFDKIIEKAAEIASSDSANVSSRGGKKFLPVLKE
ILDRDPLSQLCENEMDLIWTLRQDCREIFPQSLPKLLLSIKWNKLEDVAQLQALLQIWPK
LPPREALELLDFNYPDQYVREYAVGCLRQMSDEELSQYLLQLVQVLKYEPFLDCALSRFL
LERALGNRRIGQFLFWHLRSEVHIPAVSVQFGVILEAYCRGSVGHMKVLSKQVEALNKLK
TLNSLIKLNAVKLNRAKGKEAMHTCLKQSAYREALSDLQSPLNPCVILSELYVEKCKYMD
SKMKPLWLVYNNKVFGEDSVGVIFKNGDDLRQDMLTLQMLRLMDLLWKEAGLDLRMLPYG
CLATGDRSGLIEVVSTSETIADIQLNSSNVAAAAAFNKDALLNWLKEYNSGDDLDRAIEE
FTLSCAGYCVASYVLGIGDRHSDNIMVKKTGQLFHIDFGHILGNFKSKFGIKRERVPFIL
TYDFIHVIQQGKTGNTEKFGRFRQCCEDAYLILRRHGNLFITLFALMLTAGLPELTSVKD
IQYLKDSLALGKSEEEALKQFKQKFDEALRESWTTKVNWMAHTVRKDYRS
Enzyme 18 Number of Residues 1070
Enzyme 18 Molecular Weight 122761.2
Enzyme 18 Theoretical pI 7.09
Enzyme 18 GO Classification
Function
  • 1-phosphatidylinositol-3-kinase activity
  • binding
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • kinase activity
  • lipid kinase activity
  • phosphatidylinositol-4,5-bisphosphate 3-kinase activity
  • phosphoinositide 3-kinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biological regulation
  • glycerophospholipid metabolic process
  • intracellular signal transduction
  • metabolic process
  • organophosphate metabolic process
  • phosphoinositide metabolic process
  • phosphoinositide phosphorylation
  • phosphoinositide-mediated signaling
  • phospholipid metabolic process
  • regulation of biological process
  • regulation of cellular process
  • second-messenger-mediated signaling
  • signal transduction
Component
  • macromolecular complex
  • phosphoinositide 3-kinase complex
  • protein complex
Enzyme 18 General Function Involved in binding
Enzyme 18 Specific Function Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2 with a preference for PtdIns(4,5)P2
Enzyme 18 Pathways
Enzyme 18 Reactions
  • ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate [RN:R04545]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein Not Available
Enzyme 18 UniProtKB/Swiss-Prot ID P42338 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PK3CB_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >3213 bp
ATGTGCTTCAGTTTCATAATGCCTCCTGCTATGGCAGACATCCTTGACATCTGGGCGGTG
GATTCACAGATAGCATCTGATGGCTCCATACCTGTGGATTTCCTTTTGCCCACTGGGATT
TATATCCAGTTGGAGGTACCTCGGGAAGCTACCATTTCTTATATTAAGCAGATGTTATGG
AAGCAAGTTCACAATTACCCAATGTTCAACCTCCTTATGGATATTGACTCCTATATGTTT
GCATGTGTGAATCAGACTGCTGTATATGAGGAGCTTGAAGATGAAACACGAAGACTCTGT
GATGTCAGACCTTTTCTTCCAGTTCTCAAATTAGTGACAAGAAGTTGTGACCCAGGGGAA
AAATTAGACTCAAAAATTGGAGTCCTTATAGGAAAAGGTCTGCATGAATTTGATTCCTTG
AAGGATCCTGAAGTAAATGAATTTCGAAGAAAAATGCGCAAATTCAGCGAGGAAAAAATC
CTGTCACTTGTGGGATTGTCTTGGATGGACTGGCTAAAACAAACATATCCACCAGAGCAT
GAACCATCCATCCCTGAAAACTTAGAAGATAAACTTTATGGGGGAAAGCTCATCGTAGCT
GTTCATTTTGAAAACTGCCAGGACGTGTTTAGCTTTCAAGTGTCTCCTAATATGAATCCT
ATCAAAGTAAATGAATTGGCAATCCAAAAACGTTTGACTATTCATGGGAAGGAAGATGAA
GTTAGCCCCTATGATTATGTGTTGCAAGTCAGCGGGAGAGTAGAATATGTTTTTGGTGAT
CATCCACTAATTCAGTTCCAGTATATCCGGAACTGTGTGATGAACAGAGCCCTGCCCCAT
TTTATACTTGTGGAATGCTGCAAGATCAAGAAAATGTATGAACAAGAAATGATTGCCATA
GAGGCTGCCATAAATCGAAATTCATCTAATCTTCCTCTTCCATTACCACCAAAGAAAACA
CGAATTATTTCTCATGTTTGGGAAAATAACAACCCTTTCCAAATTGTCTTGGTTAAGGGA
AATAAACTTAACACAGAGGAAACTGTAAAAGTTCATGTCAGGGCTGGTCTTTTTCATGGT
ACTGAGCTCCTGTGTAAAACCATCGTAAGCTCAGAGGTATCAGGGAAAAATGATCATATT
TGGAATGAACCACTGGAATTTGATATTAATATTTGTGACTTACCAAGAATGGCTCGATTA
TGTTTTGCTGTTTATGCAGTTTTGGATAAAGTAAAAACGAAGAAATCAACGAAAACTATT
AATCCCTCTAAATATCAGACCATCAGGAAAGCTGGAAAAGTGCATTATCCTGTAGCGTGG
GTAAATACGATGGTTTTTGACTTTAAAGGACAATTGAGAACTGGAGACATAATATTACAC
AGCTGGTCTTCATTTCCTGATGAACTCGAAGAAATGTTGAATCCAATGGGAACTGTTCAA
ACAAATCCATATACTGAAAATGCAACAGCTTTGCATGTTAAATTTCCAGAGAATAAAAAA
CAACCTTATTATTACCCTCCCTTCGATAAGATTATTGAAAAGGCAGCTGAGATTGCAAGC
AGTGATAGTGCTAATGTGTCAAGTCGAGGTGGAAAAAAGTTTCTTCCTGTATTGAAAGAA
ATCTTGGACAGGGATCCCTTGTCTCAACTGTGTGAAAATGAAATGGATCTTATTTGGACT
TTGCGACAAGACTGCCGAGAGATTTTCCCACAATCACTGCCAAAATTACTGCTGTCAATC
AAGTGGAATAAACTTGAGGATGTTGCTCAGCTTCAGGCGCTGCTTCAGATTTGGCCTAAA
CTGCCCCCCCGGGAGGCCCTAGAGCTTCTGGATTTCAACTATCCAGACCAGTACGTTCGA
GAATATGCTGTAGGCTGCCTGCGACAGATGAGTGATGAAGAACTTTCTCAATATCTTTTA
CAACTGGTGCAAGTGTTAAAATATGAGCCTTTTCTTGATTGTGCCCTCTCTAGATTCCTA
TTAGAAAGAGCACTTGGTAATCGGAGGATAGGGCAGTTTCTATTTTGGCATCTTAGGTCA
GAAGTGCACATTCCTGCTGTCTCAGTACAATTTGGTGTCATCCTTGAAGCATACTGCCGG
GGAAGTGTGGGGCACATGAAAGTGCTTTCTAAGCAGGTTGAAGCACTCAATAAGTTAAAA
ACTTTAAATAGTTTAATCAAACTGAATGCCGTGAAGTTAAACAGAGCCAAAGGGAAGGAG
GCCATGCATACCTGTTTAAAACAGAGTGCTTACCGGGAAGCCCTCTCTGACCTGCAGTCA
CCCCTGAACCCATGTGTTATCCTCTCAGAACTCTATGTTGAAAAGTGCAAATACATGGAT
TCCAAAATGAAGCCTTTGTGGCTGGTATACAATAACAAGGTATTTGGTGAGGATTCAGTT
GGAGTGATTTTTAAAAATGGTGATGATTTACGACAGGATATGTTGACACTCCAAATGTTG
CGCTTGATGGATTTACTCTGGAAAGAAGCTGGTTTGGATCTTCGGATGTTGCCTTATGGC
TGTTTAGCAACAGGAGATCGCTCTGGCCTCATTGAAGTTGTGAGCACCTCTGAAACAATT
GCTGACATTCAGCTGAACAGTAGCAATGTGGCTGCTGCAGCAGCCTTCAACAAAGATGCC
CTTCTGAACTGGCTTAAAGAATACAACTCTGGGGATGACCTGGACCGAGCCATTGAGGAA
TTTACACTGTCCTGTGCTGGCTACTGTGTAGCTTCTTATGTCCTTGGGATTGGTGACAGA
CATAGTGACAACATCATGGTCAAAAAAACTGGCCAGCTCTTCCACATTGACTTTGGACAT
ATTCTTGGAAATTTCAAATCTAAGTTTGGCATTAAAAGGGAGCGAGTGCCTTTTATTCTT
ACCTATGATTTCATCCATGTCATTCAACAAGGAAAAACAGGAAATACAGAAAAGTTTGGC
CGGTTCCGCCAGTGTTGTGAGGATGCATATCTGATTTTACGACGGCATGGGAATCTCTTC
ATCACTCTCTTTGCGCTGATGTTGACTGCAGGGCTTCCTGAACTCACATCAGTCAAAGAT
ATACAGTATCTTAAGGACTCTCTTGCATTAGGGAAGAGTGAAGAAGAAGCACTCAAACAG
TTTAAGCAAAAATTTGATGAGGCGCTCAGGGAAAGCTGGACTACTAAAGTGAACTGGATG
GCCCACACAGTTCGGAAAGACTACAGATCTTAA
Enzyme 18 GenBank Gene ID S67334 Link Image
Enzyme 18 GeneCard ID PIK3CB Link Image
Enzyme 18 GenAtlas ID PIK3CB Link Image
Enzyme 18 HGNC ID HGNC:8976 Link Image
Enzyme 18 Chromosome Location 3
Enzyme 18 Locus 3q22.3
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Hu P, Mondino A, Skolnik EY, Schlessinger J: Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85. Mol Cell Biol. 1993 Dec;13(12):7677-88. [PubMed Link Image]
  2. Kossila M, Sinkovic M, Karkkainen P, Laukkanen MO, Miettinen R, Rissanen J, Kekalainen P, Kuusisto J, Yla-Herttuala S, Laakso M: Gene encoding the catalytic subunit p110beta of human phosphatidylinositol 3-kinase: cloning, genomic structure, and screening for variants in patients with type 2 diabetes. Diabetes. 2000 Oct;49(10):1740-3. [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 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 6516
Enzyme 19 Name Probable phospholipid-transporting ATPase IIA
Enzyme 19 Synonyms
  1. ATPase class II type 9A
Enzyme 19 Gene Name ATP9A
Enzyme 19 Protein Sequence >Probable phospholipid-transporting ATPase IIA
MTDNIPLQPVRQKKRMDSRPRAGCCEWLRCCGGGEARPRTVWLGHPEKRDQRYPRNVINN
QKYNFFTFLPGVLFNQFKYFFNLYFLLLACSQFVPEMRLGALYTYWVPLGFVLAVTVIRE
AVEEIRCYVRDKEVNSQVYSRLTARGTVKVKSSNIQVGDLIIVEKNQRVPADMIFLRTSE
KNGSCFLRTDQLDGETDWKLRLPVACTQRLPTAADLLQIRSYVYAEEPNIDIHNFVGTFT
REDSDPPISESLSIENTLWAGTVVASGTVVGVVLYTGRELRSVMNTSNPRSKIGLFDLEV
NCLTKILFGALVVVSLVMVALQHFAGRWYLQIIRFLLLFSNIIPISLRVNLDMGKIVYSW
VIRRDSKIPGTVVRSSTIPEQLGRISYLLTDKTGTLTQNEMIFKRLHLGTVAYGLDSMDE
VQSHIFSIYTQQSQDPPAQKGPTLTTKVRRTMSSRVHEAVKAIALCHNVTPVYESNGVTD
QAEAEKQYEDSCRVYQASSPDEVALVQWTESVGLTLVGRDQSSMQLRTPGDQILNFTILQ
IFPFTYESKRMGIIVRDESTGEITFYMKGADVVMAGIVQYNDWLEEECGNMAREGLRVLV
VAKKSLAEEQYQDFEARYVQAKLSVHDRSLKVATVIESLEMEMELLCLTGVEDQLQADVR
PTLETLRNAGIKVWMLTGDKLETATCTAKNAHLVTRNQDIHVFRLVTNRGEAHLELNAFR
RKHDCALVISGDSLEVCLKYYEYEFMELACQCPAVVCCRCAPTQKAQIVRLLQERTGKLT
CAVGDGGNDVSMIQESDCGVGVEGKEGKQASLAADFSITQFKHLGRLLMVHGRNSYKRSA
ALSQFVIHRSLCISTMQAVFSSVFYFASVPLYQGFLIIGYSTIYTMFPVFSLVLDKDVKS
EVAMLYPELYKDLLKGRPLSYKTFLIWVLISIYQGSTIMYGALLLFESEFVHIVAISFTS
LILTELLMVALTIQTWHWLMTVAELLSLACYIASLVFLHEFIDVYFIATLSFLWKVSVIT
LVSCLPLYVLKYLRRRFSPPSYSKLTS
Enzyme 19 Number of Residues 1047
Enzyme 19 Molecular Weight 118581.5
Enzyme 19 Theoretical pI 7.81
Enzyme 19 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • ion binding
  • ion transmembrane transporter activity
  • lipid transporter activity
  • magnesium ion binding
  • metal ion binding
  • nucleoside binding
  • phospholipid transporter activity
  • phospholipid-translocating ATPase activity
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • substrate-specific transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • cellular nitrogen compound metabolic process
  • establishment of localization
  • lipid transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phospholipid transport
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 19 General Function Involved in ATP binding
Enzyme 19 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions
  • ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • 70-91 97-119 304-325 333-354 842-862 875-893 924-942 950-972 979-999 1007-1030
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 65301139 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID O75110 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name ATP9A_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >3144 bp
ATGACGGACAACATCCCGCTGCAGCCGGTGCGCCAGAAGAAGCGGATGGACAGCAGGCCC
CGCGCCGGGTGCTGCGAGTGGCTGAGATGCTGCGGTGGAGGGGAGGCCAGGCCCCGCACT
GTCTGGCTGGGGCACCCCGAGAAGAGAGACCAGAGGTATCCTCGGAATGTCATCAACAAT
CAGAAGTACAATTTCTTCACCTTTCTTCCTGGGGTGCTGTTCAACCAGTTCAAATACTTT
TTCAACCTCTATTTCTTACTTCTTGCCTGCTCTCAGTTTGTTCCCGAAATGAGACTTGGT
GCACTCTATACCTACTGGGTTCCCCTGGGCTTCGTGCTGGCCGTCACTGTCATCCGTGAG
GCGGTGGAGGAGATCCGATGCTACGTGCGGGACAAGGAAGTCAACTCCCAGGTCTACAGC
CGGCTCACAGCACGAGGCACAGTGAAGGTGAAGAGTTCTAACATCCAAGTTGGAGACCTT
ATCATCGTTGAAAAGAACCAGCGGGTCCCTGCCGACATGATCTTCCTGAGGACATCAGAA
AAAAACGGGTCATGCTTCTTGCGGACGGATCAGCTGGATGGGGAGACGGACTGGAAGCTG
CGGCTTCCCGTGGCCTGCACGCAGAGGCTCCCCACGGCCGCCGACCTTCTTCAGATTCGA
TCGTATGTGTACGCAGAAGAGCCAAATATTGACATTCACAACTTCGTGGGAACTTTTACC
CGAGAAGACAGCGACCCCCCGATCAGCGAGAGCCTGAGCATAGAGAACACGCTGTGGGCT
GGCACTGTGGTCGCATCAGGTACTGTTGTGGGTGTTGTTCTTTACACTGGCAGAGAACTC
CGGAGTGTCATGAATACCTCAAATCCCCGAAGTAAGATCGGCCTGTTCGACTTGGAAGTG
AACTGCCTCACCAAGATCCTCTTTGGTGCCCTGGTGGTGGTCTCGCTGGTCATGGTTGCC
CTTCAGCACTTTGCAGGCCGTTGGTACCTGCAGATCATCCGCTTCCTCCTCTTGTTTTCC
AACATCATCCCCATTAGTTTGCGCGTGAACCTGGACATGGGCAAGATCGTGTACAGCTGG
GTGATTCGAAGGGACTCGAAAATCCCCGGGACCGTGGTTCGCTCCAGCACGATTCCTGAG
CAGCTGGGCAGGATTTCGTACTTACTCACAGACAAGACAGGCACTCTTACCCAGAACGAG
ATGATTTTCAAACGGCTCCATCTCGGAACAGTAGCCTACGGCCTCGACTCAATGGACGAA
GTACAAAGCCACATTTTCAGCATTTACACCCAGCAATCCCAGGACCCACCGGCTCAGAAG
GGCCCAACGCTCACCACTAAGGTCCGGCGGACCATGAGCAGCCGCGTGCACGAAGCCGTG
AAGGCCATCGCGCTCTGCCACAACGTGACTCCCGTGTATGAGTCCAACGGTGTGACTGAT
CAGGCTGAGGCCGAGAAGCAGTACGAAGACTCCTGCCGCGTATACCAGGCATCCAGCCCC
GATGAGGTGGCCCTGGTACAGTGGACGGAAAGTGTGGGCTTAACCCTGGTGGGCCGAGAC
CAGTCTTCCATGCAGCTGAGGACCCCTGGCGACCAGATCCTGAACTTCACCATCCTACAG
ATCTTCCCTTTCACCTATGAAAGCAAACGTATGGGCATCATCGTGCGGGATGAATCAACT
GGAGAAATTACGTTTTACATGAAGGGAGCAGATGTGGTCATGGCTGGCATTGTGCAGTAC
AATGACTGGTTGGAGGAAGAGTGTGGCAACATGGCCCGAGAAGGGCTGCGGGTGCTCGTG
GTGGCAAAGAAGTCTCTTGCAGAGGAGCAGTATCAGGACTTTGAAGCCCGCTACGTCCAG
GCCAAGCTGAGTGTGCACGACCGCTCCCTCAAAGTGGCCACGGTGATCGAGAGCCTGGAG
ATGGAGATGGAACTGCTGTGCCTGACGGGCGTGGAGGACCAGCTGCAGGCAGATGTGCGG
CCCACGCTGGAGACCCTGAGGAATGCTGGCATCAAGGTTTGGATGCTGACAGGGGACAAG
CTGGAGACAGCTACGTGCACAGCGAAGAATGCACATCTGGTGACCAGAAACCAAGACATC
CACGTTTTTCGGCTGGTGACCAACCGCGGGGAGGCTCACCTCGAGCTGAACGCCTTCCGC
AGGAAGCATGATTGTGCCCTGGTCATCTCGGGAGACTCCCTGGAGGTTTGCCTCAAGTAC
TATGAGTACGAGTTCATGGAGCTGGCCTGCCAGTGCCCGGCCGTAGTCTGCTGCCGATGT
GCCCCCACCCAGAAGGCCCAGATCGTGCGCCTGCTTCAGGAGCGCACGGGCAAGCTCACC
TGTGCAGTAGGGGACGGAGGCAATGACGTCAGCATGATTCAGGAATCTGACTGCGGCGTG
GGAGTGGAAGGAAAGGAAGGAAAACAGGCTTCGTTGGCTGCAGACTTCTCCATCACTCAA
TTTAAGCATCTTGGCCGGTTGCTTATGGTGCATGGCCGGAACAGCTACAAGCGGTCAGCC
GCCCTCAGCCAGTTCGTGATTCACAGGAGCCTCTGTATCAGCACCATGCAGGCTGTCTTT
TCCTCCGTGTTTTACTTTGCCTCCGTCCCTCTCTATCAAGGATTCCTCATCATTGGGTAC
TCCACAATTTACACCATGTTTCCTGTGTTTTCTCTGGTCCTGGACAAAGATGTCAAATCG
GAAGTTGCCATGCTGTATCCTGAGCTCTACAAGGATCTTCTCAAGGGACGGCCGTTGTCC
TACAAGACATTCTTAATATGGGTTTTGATTAGCATCTATCAAGGGAGCACCATCATGTAC
GGGGCGCTGCTGCTGTTTGAGTCGGAGTTCGTGCACATCGTGGCCATCTCCTTCACCTCG
CTGATCCTCACCGAGCTGCTCATGGTGGCGCTGACCATCCAGACCTGGCACTGGCTCATG
ACAGTGGCGGAGCTGCTCAGCCTGGCCTGCTACATCGCCTCCCTGGTGTTCTTACACGAG
TTCATCGATGTGTACTTCATCGCCACCTTGTCATTCTTGTGGAAAGTCTCCGTCATCACT
CTGGTCAGCTGCCTCCCCCTCTATGTCCTCAAGTACCTGCGAAGACGGTTCTCTCCCCCC
AGCTACTCAAAGCTCACATCATAG
Enzyme 19 GenBank Gene ID NM_006045.1 Link Image
Enzyme 19 GeneCard ID ATP9A Link Image
Enzyme 19 GenAtlas ID ATP9A Link Image
Enzyme 19 HGNC ID HGNC:13540 Link Image
Enzyme 19 Chromosome Location 2
Enzyme 19 Locus 20q13.2
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  2. Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Jun 30;5(3):169-76. [PubMed Link Image]
  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]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 6532
Enzyme 20 Name Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
Enzyme 20 Synonyms
  1. PI3-kinase subunit alpha
  2. PI3K-alpha
  3. PtdIns-3-kinase subunit alpha
  4. Phosphatidylinositol-4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha
  5. PtdIns-3-kinase subunit p110-alpha
Enzyme 20 Gene Name PIK3CA
Enzyme 20 Protein Sequence >Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
MPPRPSSGELWGIHLMPPRILVECLLPNGMIVTLECLREATLITIKHELFKEARKYPLHQ
LLQDESSYIFVSVTQEAEREEFFDETRRLCDLRLFQPFLKVIEPVGNREEKILNREIGFA
IGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKH
IYNKLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLK
LCVLEYQGKYILKVCGCDEYFLEKYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPMD
CFTMPSYSRRISTATPYMNGETSTKSLWVINSALRIKILCATYVNVNIRDIDKIYVRTGI
YHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHC
PLAWGNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNPNKETPCLELEFDWF
SSVVKFPDMSVIEEHANWSVSREAGFSYSHAGLSNRLARDNELRENDKEQLKAISTRDPL
SEITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMYCLVKDWPPIKPEQAME
LLDCNYPDPMVRGFAVRCLEKYLTDDKLSQYLIQLVQVLKYEQYLDNLLVRFLLKKALTN
QRIGHFFFWHLKSEMHNKTVSQRFGLLLESYCRACGMYLKHLNRQVEAMEKLINLTDILK
QEKKDETQKVQMKFLVEQMRRPDFMDALQGFLSPLNPAHQLGNLRLEECRIMSSAKRPLW
LNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLS
IGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRS
CAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDF
LIVISKGAQECTKTREFERFQEMCYKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIA
YIRKTLALDKTEQEALEYFMKQMNDAHHGGWTTKMDWIFHTIKQHALN
Enzyme 20 Number of Residues 1068
Enzyme 20 Molecular Weight 124283.0
Enzyme 20 Theoretical pI 7.23
Enzyme 20 GO Classification
Function
  • 1-phosphatidylinositol-3-kinase activity
  • binding
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • kinase activity
  • lipid kinase activity
  • phosphatidylinositol-4,5-bisphosphate 3-kinase activity
  • phosphoinositide 3-kinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biological regulation
  • glycerophospholipid metabolic process
  • intracellular signal transduction
  • metabolic process
  • organophosphate metabolic process
  • phosphoinositide metabolic process
  • phosphoinositide phosphorylation
  • phosphoinositide-mediated signaling
  • phospholipid metabolic process
  • regulation of biological process
  • regulation of cellular process
  • second-messenger-mediated signaling
  • signal transduction
Component
  • macromolecular complex
  • phosphoinositide 3-kinase complex
  • protein complex
Enzyme 20 General Function Involved in binding
Enzyme 20 Specific Function Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2 with a preference for PtdIns(4,5)P2
Enzyme 20 Pathways
Enzyme 20 Reactions
  • ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate [RN:R04545]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 472991 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P42336 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name PK3CA_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >3207 bp
ATGCCTCCAAGACCATCATCAGGTGAACTGTGGGGCATCCACTTGATGCCCCCAAGAATC
CTAGTGGAATGTTTACTACCAAATGGAATGATAGTGACTTTAGAATGCCTCCGTGAGGCT
ACATTAGTAACTATAAAGCATGAACTATTTAAAGAAGCAAGAAAATACCCTCTCCATCAA
CTTCTTCAAGATGAATCTTCTTACATTTTCGTAAGTGTTACCCAAGAAGCAGAAAGGGAA
GAATTTTTTGATGAAACAAGACGACTTTGTGATCTTCGGCTTTTTCAACCATTTTTAAAA
GTAATTGAACCAGTAGGCAACCGTGAAGAAAAGATCCTCAATCGAGAAATTGGTTTTGCT
ATCGGCATGCCAGTGTGCGAATTTGATATGGTTAAAGATCCTGAAGTACAGGACTTCCGA
AGAAATATTCTTAATGTTTGTAAAGAAGCTGTGGATCTTAGGGATCTTAATTCACCTCAT
AGTAGAGCAATGTATGTCTATCCGCCACATGTAGAATCTTCACCAGAGCTGCCAAAGCAC
ATATATAATAAATTGGATAGAGGCCAAATAATAGTGGTGATTTGGGTAATAGTTTCTCCA
AATAATGACAAGCAGAAGTATACTCTGAAAATCAACCATGACTGTGTGCCAGAACAAGTA
ATTGCTGAAGCAATCAGGAAAAAAACTAGAAGTATGTTGCTATCATCTGAACAATTAAAA
CTCTGTGTTTTAGAATATCAGGGCAAGTACATTTTAAAAGTGTGTGGATGTGATGAATAC
TTCCTAGAAAAATATCCTCTGAGTCAGTATAAGTATATAAGAAGCTGTATAATGCTTGGG
AGGATGCCCAATTTGAAGATGATGGCTAAAGAAAGCCTTTATTCTCAACTGCCAATGGAC
TGTTTTACAATGCCATCTTATTCCAGACGCATTTCCACAGCTACACCATATATGAATGGA
GAAACATCTACAAAATCCCTTTGGGTTATAAATAGAGCACTCAGAATAAAAATTCTTTGT
GCAACCTACGTGAATCTAAATATTCGAGACATTGACAAGATTTATGTTCGAACAGGTATC
TACCATGGAGGAGAACCCTTATGTGACAATGTGAACACTCAAAGAGTACCTTGTTCCAAT
CCCAGGTGGAATGAATGGCTGAATTATGATATATACATTCCTGATCTTCCTCGTGCTGCT
CGACTTTGCCTTTCCATTTGCTCTGTTAAAGGCCGAAAGGGTGCTAAAGAGGAACACTGT
CCATTGGCATGGGGAAATATAAACTTGTTTGATTACACAGACACTCTAGTATCTGGAAAA
ATGGCTTTGAATCTTTGGCCAGTACCTCATGGATTAGAAGATTTGCTGAACCCTATTGGT
GTTACTGGATCAAATCCAAATAAAGAAACTCCATGCTTAGAGTTGGAGTTTGACTGGTTC
AGCAGTGTGGTAAAGTTCCCAGATATGTCAGTGATTGAAGAGCATGCCAATTGGTCTGTA
TCCCGAGAAGCAGGATTTAGCTATTCCCACGCAGGACTGAGTAACAGACTAGCTAGAGAC
AATGAATTAAGGGAAAATGACAAAGAACAGCTCAAAGCAATTTCTACACGAGATCCTCTC
TCTGAAATCACTGAGCAGGAGAAAGATTTTCTATGGAGTCACAGACACTATTGTGTAACT
ATCCCCGAAATTCTACCCAAATTGCTTCTGTCTGTTAAATGGAATTCTAGAGATGAAGTA
GCCCAGATGTATTGCTTGGTAAAAGATTGGCCTCCAATCAAACCTGAACAGGCTATGGAA
CTTCTGGACTGTAATTACCCAGATCCTATGGTTCGAGGTTTTGCTGTTCGGTGCTTGGAA
AAATATTTAACAGATGACAAACTTTCTCAGTATTTAATTCAGCTAGTACAGGTCCTAAAA
TATGAACAATATTTGGATAACTTGCTTGTGAGATTTTTACTGAAGAAAGCATTGACTAAT
CAAAGGATTGGGCACTTTTTCTTTTGGCATTTAAAATCTGAGATGCACAATAAAACAGTT
AGCCAGAGGTTTGGCCTGCTTTTGGAGTCCTATTGTCGTGCATGTGGGATGTATTTGAAG
CACCTGAATAGGCAAGTCGAGGCAATGGAAAAGCTCATTAACTTAACTGACATTCTCAAA
CAGGAGAGGAAGGATGAAACACAAAAGGTACAGATGAAGTTTTTAGTTGAGCAAATGAGG
CGACCAGATTTCATGGATGCCCTACAGGGCTTGCTGTCTCCTCTAAACCCTGCTCATCAA
CTAGGAAACCTCAGGCTTAAAGAGTGTCGAATTATGTCTTCTGCAAAAAGGCCACTGTGG
TTGAATTGGGAGAACCCAGACATCATGTCAGAGTTACTGTTTCAGAACAATGAGATCATC
TTTAAAAATGGGGATGATTTACGGCAAGATATGCTAACACTTCAAATTATTCGTATTATG
GAAAATATCTGGCAAAATCAAGGTCTTGATCTTCGAATGTTACCTTATGGTTGTCTGTCA
ATCGGTGACTGTGTGGGACTTATTGAGGTGGTGCGAAATTCTCACACTATTATGCAAATT
CAGTGCAAAGGCGGCTTGAAAGGTGCACTGCAGTTCAACAGCCACACACTACATCAGTGG
CTCAAAGACAAGAACAAAGGAGAAATATATGATGCAGCCATTGACCTGTTTACACGTTCA
TGTGCTGGATACTGTGTAGCTACCTTCATTTTGGGAATTGGAGATCGTCACAATAGTAAC
ATCATGGTGAAAGACGATGGACAACTGTTTCATATAGATTTTGGACACTTTTTGGATCAC
AAGAAGAAAAAATTTGGTTATAAACGAGAACGTGTGCCATTTGTTTTGACACAGGATTTC
TTAATAGTGATTAGTAAAGGAGCCCAAGAATGCACAAAGACAAGAGAATTTGAGAGGTTT
CAGGAGATGTGTTACAAGGCTTATCTAGCTATTCGACAGCATGCCAATCTCTTCATAAAT
CTTTTCTCAATGATGCTTGGCTCTGGAATGCCAGAACTACAATCTTTTGATGACATTGCA
TACATTCGAAAGACCCTAGCCTTAGATAAAACTGAGCAAGAGGCTTTGGAGTATTTCATG
AAACAAATGAATGATGCACATCATGGTGGCTGGACAACAAAAATGGATTGGATCTTCCAC
ACAATTAAACAGCATGCATTGAACTGA
Enzyme 20 GenBank Gene ID Z29090 Link Image
Enzyme 20 GeneCard ID PIK3CA Link Image
Enzyme 20 GenAtlas ID PIK3CA Link Image
Enzyme 20 HGNC ID HGNC:8975 Link Image
Enzyme 20 Chromosome Location 3
Enzyme 20 Locus 3q26.3
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Volinia S, Hiles I, Ormondroyd E, Nizetic D, Antonacci R, Rocchi M, Waterfield MD: Molecular cloning, cDNA sequence, and chromosomal localization of the human phosphatidylinositol 3-kinase p110 alpha (PIK3CA) gene. Genomics. 1994 Dec;24(3):472-7. [PubMed Link Image]
  2. Stirdivant SM, Ahern J, Conroy RR, Barnett SF, Ledder LM, Oliff A, Heimbrook DC: Cloning and mutagenesis of the p110 alpha subunit of human phosphoinositide 3'-hydroxykinase. Bioorg Med Chem. 1997 Jan;5(1):65-74. [PubMed Link Image]
  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. Broderick DK, Di C, Parrett TJ, Samuels YR, Cummins JM, McLendon RE, Fults DW, Velculescu VE, Bigner DD, Yan H: Mutations of PIK3CA in anaplastic oligodendrogliomas, high-grade astrocytomas, and medulloblastomas. Cancer Res. 2004 Aug 1;64(15):5048-50. [PubMed Link Image]
  5. Campbell IG, Russell SE, Choong DY, Montgomery KG, Ciavarella ML, Hooi CS, Cristiano BE, Pearson RB, Phillips WA: Mutation of the PIK3CA gene in ovarian and breast cancer. Cancer Res. 2004 Nov 1;64(21):7678-81. [PubMed Link Image]
  6. Samuels Y, Wang Z, Bardelli A, Silliman N, Ptak J, Szabo S, Yan H, Gazdar A, Powell SM, Riggins GJ, Willson JK, Markowitz S, Kinzler KW, Vogelstein B, Velculescu VE: High frequency of mutations of the PIK3CA gene in human cancers. Science. 2004 Apr 23;304(5670):554. Epub 2004 Mar 11. [PubMed Link Image]
  7. Hartmann C, Bartels G, Gehlhaar C, Holtkamp N, von Deimling A: PIK3CA mutations in glioblastoma multiforme. Acta Neuropathol. 2005 Jun;109(6):639-42. Epub 2005 May 28. [PubMed Link Image]
  8. Li VS, Wong CW, Chan TL, Chan AS, Zhao W, Chu KM, So S, Chen X, Yuen ST, Leung SY: Mutations of PIK3CA in gastric adenocarcinoma. BMC Cancer. 2005 Mar 23;5:29. [PubMed Link Image]
  9. Ikenoue T, Kanai F, Hikiba Y, Obata T, Tanaka Y, Imamura J, Ohta M, Jazag A, Guleng B, Tateishi K, Asaoka Y, Matsumura M, Kawabe T, Omata M: Functional analysis of PIK3CA gene mutations in human colorectal cancer. Cancer Res. 2005 Jun 1;65(11):4562-7. [PubMed Link Image]
  10. Oda K, Stokoe D, Taketani Y, McCormick F: High frequency of coexistent mutations of PIK3CA and PTEN genes in endometrial carcinoma. Cancer Res. 2005 Dec 1;65(23):10669-73. [PubMed Link Image]
  11. Velho S, Oliveira C, Ferreira A, Ferreira AC, Suriano G, Schwartz S Jr, Duval A, Carneiro F, Machado JC, Hamelin R, Seruca R: The prevalence of PIK3CA mutations in gastric and colon cancer. Eur J Cancer. 2005 Jul;41(11):1649-54. [PubMed Link Image]
  12. Wang Y, Helland A, Holm R, Kristensen GB, Borresen-Dale AL: PIK3CA mutations in advanced ovarian carcinomas. Hum Mutat. 2005 Mar;25(3):322. [PubMed Link Image]
  13. Lee JW, Soung YH, Kim SY, Lee HW, Park WS, Nam SW, Kim SH, Lee JY, Yoo NJ, Lee SH: PIK3CA gene is frequently mutated in breast carcinomas and hepatocellular carcinomas. Oncogene. 2005 Feb 17;24(8):1477-80. [PubMed Link Image]
  14. Qiu W, Schonleben F, Li X, Ho DJ, Close LG, Manolidis S, Bennett BP, Su GH: PIK3CA mutations in head and neck squamous cell carcinoma. Clin Cancer Res. 2006 Mar 1;12(5):1441-6. [PubMed Link Image]
  15. Or YY, Hui AB, To KF, Lam CN, Lo KW: PIK3CA mutations in nasopharyngeal carcinoma. Int J Cancer. 2006 Feb 15;118(4):1065-7. [PubMed Link Image]
  16. Buttitta F, Felicioni L, Barassi F, Martella C, Paolizzi D, Fresu G, Salvatore S, Cuccurullo F, Mezzetti A, Campani D, Marchetti A: PIK3CA mutation and histological type in breast carcinoma: high frequency of mutations in lobular carcinoma. J Pathol. 2006 Feb;208(3):350-5. [PubMed Link Image]
  17. Bader AG, Kang S, Vogt PK: Cancer-specific mutations in PIK3CA are oncogenic in vivo. Proc Natl Acad Sci U S A. 2006 Jan 31;103(5):1475-9. Epub 2006 Jan 23. [PubMed Link Image]
  18. Hafner C, Lopez-Knowles E, Luis NM, Toll A, Baselga E, Fernandez-Casado A, Hernandez S, Ribe A, Mentzel T, Stoehr R, Hofstaedter F, Landthaler M, Vogt T, Pujol RM, Hartmann A, Real FX: Oncogenic PIK3CA mutations occur in epidermal nevi and seborrheic keratoses with a characteristic mutation pattern. Proc Natl Acad Sci U S A. 2007 Aug 14;104(33):13450-4. Epub 2007 Aug 2. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 6535
Enzyme 21 Name Probable phospholipid-transporting ATPase VD
Enzyme 21 Synonyms
  1. ATPase class V type 10D
Enzyme 21 Gene Name ATP10D
Enzyme 21 Protein Sequence >Probable phospholipid-transporting ATPase VD
MTEALQWARYHWRRLIRGATRDDDSGPYNYSSLLACGRKSSQTPKLSGRHRIVVPHIQPF
KDEYEKFSGAYVNNRIRTTKYTLLNFVPRNLFEQFHRAANLYFLFLVVLNWVPLVEAFQK
EITMLPLVVVLTIIAIKDGLEDYRKYKIDKQINNLITKVYSRKEKKYIDRCWKDVTVGDF
IRLSCNEVIPADMVLLFSTDPDGICHIETSGLDGESNLKQRQVVRGYAEQDSEVDPEKFS
SRIECESPNNDLSRFRGFLEHSNKERVGLSKENLLLRGCTIRNTEAVVGIVVYAGHETKA
MLNNSGPRYKRSKLERRANTDVLWCVMLLVIMCLTGAVGHGIWLSRYEKMHFFNVPEPDG
HIISPLLAGFYMFWTMIILLQVLIPISLYVSIEIVKLGQIYFIQSDVDFYNEKMDSIVQC
RALNIAEDLGQIQYLFSDKTGTLTENKMVFRRCSVAGFDYCHEENARRLESYQEAVSEDE
DFIDTVSGSLSNMAKPRAPSCRTVHNGPLGNKPSNHLAGSSFTLGSGEGASEVPHSRQAA
FSSPIETDVVPDTRLLDKFSQITPRLFMPLDETIQNPPMETLYIIDFFIALAICNTVVVS
APNQPRQKIRHPSLGGLPIKSLEEIKSLFQRWSVRRSSSPSLNSGKEPSSGVPNAFVSRL
PLFSRMKPASPVEEEVSQVCESPQCSSSSACCTETEKQHGDAGLLNGKAESLPGQPLACN
LCYEAESPDEAALVYAARAYQCTLRSRTPEQVMVDFAALGPLTFQLLHILPFDSVRKRMS
VVVRHPLSNQVVVYTKGADSVIMELLSVASPDGASLEKQQMIVREKTQKHLDDYAKQGLR
TLCIAKKVMSDTEYAEWLRNHFLAETSIDNREELLLESAMRLENKLTLLGATGIEDRLQE
GVPESIEALHKAGIKIWMLTGDKQETAVNIAYACKLLEPDDKLFILNTQSKDACGMLMST
ILKELQKKTQALPEQVSLSEDLLQPPVPRDSGLRAGLIITGKTLEFALQESLQKQFLELT
SWCQAVVCCRATPLQKSEVVKLVRSHLQVMTLAIGDGANDVSMIQVADIGIGVSGQEGMQ
AVMASDFAVSQFKHLSKLLLVHGHWCYTRLSNMILYFFYKNVAYVNLLFWYQFFCGFSGT
SMTDYWVLIFFNLLFTSAPPVIYGVLEKDVSAETLMQLPELYRSGQKSEAYLPHTFWITL
LDAFYQSLVCFFVPYFTYQGSDTDIFAFGNPLNTAALFIVLLHLVIESKSLTWIHLLVII
GSILSYFLFAIVFGAMCVTCNPPSNPYWIMQEHMLDPVFYLVCILTTSIALLPRFVYRVL
QGSLFPSPILRAKHFDRLTPEERTKALKKWRGAGKMNQVTSKYANQSAGKSGRRPMPGPS
AVFAMKSASSCAIEQGNLSLCETALDQGYSETKAFEMAGPSKGKES
Enzyme 21 Number of Residues 1426
Enzyme 21 Molecular Weight 160272.3
Enzyme 21 Theoretical pI 7.15
Enzyme 21 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • ion binding
  • ion transmembrane transporter activity
  • lipid transporter activity
  • magnesium ion binding
  • metal ion binding
  • nucleoside binding
  • phospholipid transporter activity
  • phospholipid-translocating ATPase activity
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • substrate-specific transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • cellular nitrogen compound metabolic process
  • establishment of localization
  • lipid transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phospholipid transport
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 21 General Function Involved in ATP binding
Enzyme 21 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions
  • ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 98-118 122-142 322-342 366-386 1114-1134 1146-1166 1196-1216 1225-1245 1253-1273 1293-1313
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 222352161 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q9P241 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name AT10D_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >4281 bp
ATGACTGAGGCTCTCCAATGGGCCAGATATCACTGGCGACGGCTGATCAGAGGTGCAACC
AGGGATGATGATTCAGGGCCATACAACTATTCCTCGTTGCTCGCCTGTGGGCGCAAGTCC
TCTCAGACCCCTAAACTGTCAGGAAGGCACCGGATTGTTGTTCCCCACATCCAGCCCTTC
AAGGATGAGTATGAGAAGTTCTCCGGAGCCTATGTGAACAATCGAATACGAACAACAAAG
TACACACTTCTGAATTTTGTGCCAAGAAATTTATTTGAACAATTTCACAGAGCTGCCAAT
TTATATTTCCTGTTCCTAGTTGTCCTGAACTGGGTACCTTTGGTAGAAGCCTTCCAAAAG
GAAATCACCATGTTGCCTCTGGTGGTGGTCCTTACAATTATCGCAATTAAAGATGGCCTG
GAAGATTATCGGAAATACAAAATTGACAAACAGATCAATAATTTAATAACTAAAGTTTAT
AGTAGGAAAGAGAAAAAATACATTGACCGATGCTGGAAAGACGTTACTGTTGGGGACTTT
ATTCGCCTCTCCTGCAACGAGGTCATCCCTGCAGACATGGTACTACTCTTTTCCACTGAT
CCAGATGGAATCTGTCACATTGAGACTTCTGGTCTTGATGGAGAGAGCAATTTAAAACAG
AGGCAGGTGGTTCGGGGATATGCAGAACAGGACTCTGAAGTTGATCCTGAGAAGTTTTCC
AGTAGGATAGAATGTGAAAGCCCAAACAATGACCTCAGCAGATTCCGAGGCTTCCTAGAA
CATTCCAACAAAGAACGCGTGGGTCTCAGTAAAGAAAATTTGTTGCTTAGAGGATGCACC
ATTAGAAACACAGAGGCTGTTGTGGGCATTGTGGTTTATGCAGGCCATGAAACCAAAGCA
ATGCTGAACAACAGTGGGCCACGGTATAAGCGCAGCAAATTAGAAAGAAGAGCAAACACA
GATGTCCTCTGGTGTGTCATGCTTCTGGTCATAATGTGCTTAACTGGCGCAGTAGGTCAT
GGAATCTGGCTGAGCAGGTATGAAAAGATGCATTTTTTCAATGTTCCCGAGCCTGATGGA
CATATCATATCACCACTGTTGGCAGGATTTTATATGTTTTGGACCATGATCATTTTGTTA
CAGGTCTTGATTCCTATTTCTCTCTATGTTTCCATCGAAATTGTGAAGCTTGGACAAATA
TATTTCATTCAAAGTGATGTGGATTTCTACAATGAAAAAATGGATTCTATTGTTCAGTGC
CGAGCCCTGAACATCGCCGAGGATCTGGGACAGATTCAGTACCTCTTTTCCGATAAGACA
GGAACCCTCACTGAGAATAAGATGGTTTTTCGAAGATGTAGTGTGGCAGGATTTGATTAC
TGCCATGAAGAAAATGCCAGGAGGTTGGAGTCCTATCAGGAAGCTGTCTCTGAAGATGAA
GATTTTATAGACACAGTCAGTGGTTCCCTCAGCAATATGGCAAAACCGAGAGCCCCCAGC
TGCAGGACAGTTCATAATGGGCCTTTGGGAAATAAGCCCTCAAATCATCTTGCTGGGAGC
TCTTTTACTCTAGGAAGTGGAGAAGGAGCCAGTGAAGTGCCTCATTCCAGACAGGCTGCT
TTCAGTAGCCCCATTGAAACAGACGTGGTACCAGACACCAGGCTTTTAGACAAATTTAGT
CAGATTACACCTCGGCTCTTTATGCCACTAGATGAGACCATCCAAAATCCACCAATGGAA
ACTTTGTACATTATCGACTTTTTCATTGCATTGGCAATTTGCAACACAGTAGTGGTTTCT
GCTCCTAACCAACCCCGACAAAAGATCAGACACCCTTCACTGGGGGGGTTGCCCATTAAG
TCTTTGGAAGAGATTAAAAGTCTTTTCCAGAGATGGTCTGTCCGAAGATCAAGTTCTCCA
TCGCTTAACAGTGGGAAAGAGCCATCTTCTGGAGTTCCAAACGCCTTTGTGAGCAGACTC
CCTCTCTTTAGTCGAATGAAACCAGCTTCACCTGTGGAGGAAGAGGTCTCCCAGGTGTGT
GAGAGCCCCCAGTGCTCCAGTAGCTCAGCTTGCTGCACAGAAACAGAGAAACAACACGGT
GATGCAGGCCTCCTGAATGGCAAGGCAGAGTCCCTCCCTGGACAGCCATTGGCCTGCAAC
CTGTGTTATGAGGCCGAGAGCCCAGACGAAGCGGCCTTAGTGTATGCCGCCAGGGCTTAC
CAATGCACTTTACGGTCTCGGACACCAGAGCAGGTCATGGTGGACTTTGCTGCTTTGGGA
CCATTAACATTTCAACTCCTACACATCCTGCCCTTTGACTCAGTAAGAAAAAGAATGTCT
GTTGTGGTCCGACACCCTCTTTCCAATCAAGTTGTGGTGTATACGAAAGGCGCTGATTCT
GTGATCATGGAGTTACTGTCGGTGGCTTCCCCAGATGGAGCAAGTCTGGAGAAACAACAG
ATGATAGTAAGGGAGAAAACCCAGAAGCACTTGGATGACTATGCCAAACAAGGCCTTCGT
ACTTTATGTATAGCAAAGAAGGTCATGAGTGACACTGAATATGCAGAGTGGCTGAGGAAT
CATTTTTTAGCTGAAACCAGCATTGACAACAGGGAAGAATTACTACTTGAATCTGCCATG
AGGTTGGAGAACAAACTTACATTACTTGGTGCTACTGGCATTGAAGACCGTCTGCAGGAG
GGAGTCCCTGAATCTATAGAAGCTCTTCACAAAGCGGGCATCAAGATCTGGATGCTGACA
GGGGACAAGCAGGAGACAGCTGTCAACATAGCTTATGCATGCAAACTACTGGAGCCAGAT
GACAAGCTTTTTATCCTCAATACCCAAAGTAAAGATGCCTGTGGGATGCTGATGAGCACA
ATTTTGAAAGAACTTCAGAAGAAAACTCAAGCCCTGCCAGAGCAAGTGTCATTAAGTGAA
GATTTACTTCAGCCTCCTGTCCCCCGGGACTCAGGGTTACGAGCTGGACTCATTATCACT
GGGAAGACCCTGGAGTTTGCCCTGCAAGAAAGTCTGCAAAAGCAGTTCCTGGAACTGACA
TCTTGGTGTCAAGCTGTGGTCTGCTGCCGAGCCACACCGCTGCAGAAAAGTGAAGTGGTG
AAATTGGTCCGCAGCCATCTCCAGGTGATGACCCTTGCTATTGGTGATGGTGCCAATGAT
GTTAGCATGATACAAGTGGCAGACATTGGGATAGGGGTCTCAGGTCAAGAAGGCATGCAG
GCTGTGATGGCCAGTGACTTTGCCGTTTCTCAGTTCAAACATCTCAGCAAGCTCCTTCTT
GTCCATGGACACTGGTGTTATACACGGCTTTCCAACATGATTCTCTATTTTTTCTATAAG
AATGTGGCCTATGTGAACCTCCTTTTCTGGTACCAGTTCTTTTGTGGATTTTCAGGAACA
TCCATGACTGATTACTGGGTTTTGATCTTCTTCAACCTCCTCTTCACATCTGCCCCTCCT
GTCATTTATGGTGTTTTGGAGAAAGATGTGTCTGCAGAGACCCTCATGCAACTGCCTGAA
CTTTACAGAAGTGGTCAGAAATCAGAGGCATACTTACCCCATACCTTCTGGATCACCTTA
TTGGATGCTTTTTATCAAAGCCTGGTCTGCTTCTTTGTGCCTTATTTTACCTACCAGGGC
TCAGATACTGACATCTTTGCATTTGGAAACCCCCTGAACACAGCCGCTCTGTTCATCGTT
CTCCTCCATCTGGTCATTGAAAGCAAGAGTTTGACTTGGATTCACTTGCTGGTCATCATT
GGTAGCATCTTGTCTTATTTTTTATTTGCCATAGTTTTTGGAGCCATGTGTGTAACTTGC
AACCCACCATCCAACCCTTACTGGATTATGCAGGAGCACATGCTGGATCCAGTATTCTAC
TTAGTTTGTATCCTCACGACGTCCATTGCTCTTCTGCCCAGGTTTGTATACAGAGTTCTT
CAGGGATCCCTGTTTCCATCTCCAATTCTGAGAGCTAAGCACTTTGACAGACTAACTCCA
GAGGAGAGGACTAAAGCTCTCAAGAAGTGGAGAGGGGCTGGAAAGATGAATCAAGTGACA
TCAAAGTATGCTAACCAATCAGCTGGCAAGTCAGGAAGAAGACCCATGCCTGGCCCTTCT
GCTGTATTTGCAATGAAGTCAGCAAGTTCCTGTGCTATTGAGCAAGGAAACTTATCTCTG
TGTGAAACTGCTTTAGATCAAGGCTACTCTGAAACTAAGGCCTTTGAGATGGCTGGACCC
TCCAAAGGTAAAGAAAGCTAG
Enzyme 21 GenBank Gene ID NM_020453.3 Link Image
Enzyme 21 GeneCard ID ATP10D Link Image
Enzyme 21 GenAtlas ID ATP10D Link Image
Enzyme 21 HGNC ID HGNC:13549 Link Image
Enzyme 21 Chromosome Location 4
Enzyme 21 Locus 4p12
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Flamant S, Pescher P, Lemercier B, Clement-Ziza M, Kepes F, Fellous M, Milon G, Marchal G, Besmond C: Characterization of a putative type IV aminophospholipid transporter P-type ATPase. Mamm Genome. 2003 Jan;14(1):21-30. [PubMed Link Image]
  2. 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]
  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. Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 6543
Enzyme 22 Name Probable phospholipid-transporting ATPase IB
Enzyme 22 Synonyms
  1. ATPase class I type 8A member 2
  2. ML-1
Enzyme 22 Gene Name ATP8A2
Enzyme 22 Protein Sequence >Probable phospholipid-transporting ATPase IB
MSRATSVGDQLEAPARTIYLNQPHLNKFRDNQISTAKYSVLTFLPRFLYEQIRRAANAFF
LFIALLQQIPDVSPTGRYTTLVPLIIILTIAGIKEIVEDFKRHKADNAVNKKKTIVLRNG
MWHTIMWKEVAVGDIVKVVNGQYLPADVVLLSSSEPQAMCYVETANLDGETNLKIRQGLS
HTADMQTREVLMKLSGTIECEGPNRHLYDFTGNLNLDGKSLVALGPDQILLRGTQLRNTQ
WVFGIVVYTGHDTKLMQNSTKAPLKRSNVEKVTNVQILVLFGILLVMALVSSAGALYWNR
SHGEKNWYIKKMDTTSDNFGYNLLTFIILYNNLIPISLLVTLEVVKYTQALFINWDTDMY
YIGNDTPAMARTSNLNEELGQVKYLFSDKTGTLTCNIMNFKKCSIAGVTYGHFPELAREP
SSDDFCRMPPPCSDSCDFDDPRLLKNIEDRHPTAPCIQEFLTLLAVCHTVVPEKDGDNII
YQASSPDEAALVKGAKKLGFVFTARTPFSVIIEAMGQEQTFGILNVLEFSSDRKRMSVIV
RTPSGRLRLYCKGADNVIFERLSKDSKYMEETLCHLEYFATEGLRTLCVAYADLSENEYE
EWLKVYQEASTILKDRAQRLEECYEIIEKNLLLLGATAIEDRLQAGVPETIATLLKAEIK
IWVLTGDKQETAINIGYSCRLVSQNMALILLKEDSLDATRAAITQHCTDLGNLLGKENDV
ALIIDGHTLKYALSFEVRRSFLDLALSCKAVICCRVSPLQKSEIVDVVKKRVKAITLAIG
DGANDVGMIQTAHVGVGISGNEGMQATNNSDYAIAQFSYLEKLLLVHGAWSYNRVTKCIL
YCFYKNVVLYIIELWFAFVNGFSGQILFERWCIGLYNVIFTALPPFTLGIFERSCTQESM
LRFPQLYKITQNGEGFNTKVFWGHCINALVHSLILFWFPMKALEHDTVLTSGHATDYLFV
GNIVYTYVVVTVCLKAGLETTAWTKFSHLAVWGSMLTWLVFFGIYSTIWPTIPIAPDMRG
QATMVLSSAHFWLGLFLVPTACLIEDVAWRAAKHTCKKTLLEEVQELETKSRVLGKAVLR
DSNGKRLNERDRLIKRLGRKTPPTLFRGSSLQQGVPHGYAFSQEEHGAVSQEEVIRAYDT
TKKKSRKK
Enzyme 22 Number of Residues 1148
Enzyme 22 Molecular Weight 129240.4
Enzyme 22 Theoretical pI 7.84
Enzyme 22 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • ion binding
  • ion transmembrane transporter activity
  • lipid transporter activity
  • magnesium ion binding
  • metal ion binding
  • nucleoside binding
  • phospholipid transporter activity
  • phospholipid-translocating ATPase activity
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • substrate-specific transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • cellular nitrogen compound metabolic process
  • establishment of localization
  • lipid transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phospholipid transport
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 22 General Function Involved in ATP binding
Enzyme 22 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions
  • ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 45-66 72-94 277-298 324-345 838-858 871-890 921-942 957-979 986-1006 1025-1049
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 117168245 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q9NTI2 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name AT8A2_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >3567 bp
ATGCTGAACGGCGCAGGCCTGGACAAAGCTCTTAAGATGTCCCTGCCGCGGAGGTCGAGG
ATCCGCTCGTCCGTGGGACCTGTTCGTTCTTCTTTGGGCTATAAGAAGGCAGAGGATGAG
ATGTCCCGGGCCACGTCTGTTGGAGACCAGCTGGAGGCACCCGCCCGCACCATTTACCTC
AACCAACCGCATCTCAACAAATTCCGCGACAACCAGATCAGTACGGCCAAGTACAGCGTG
TTGACATTTCTACCTCGATTCTTGTATGAGCAGATTAGAAGAGCTGCTAATGCCTTCTTT
CTCTTCATTGCCTTATTACAGCAAATTCCAGATGTATCTCCAACAGGAAGATATACCACC
CTGGTGCCATTGATCATTATTTTAACAATTGCAGGCATCAAAGAGATTGTAGAAGATTTT
AAGCGACACAAGGCAGACAATGCAGTTAACAAAAAGAAAACAATAGTGTTAAGAAATGGT
ATGTGGCATACCATTATGTGGAAAGAGGTGGCAGTGGGAGACATTGTGAAGGTCGTCAAT
GGGCAGTATCTTCCAGCAGATGTGGTCCTGCTGTCATCCAGTGAACCTCAGGCAATGTGT
TATGTTGAAACAGCTAATCTGGATGGGGAGACGAACCTTAAAATACGTCAGGGTTTGAGT
CACACTGCTGACATGCAAACACGTGAAGTTCTGATGAAGTTATCTGGAACTATAGAGTGT
GAAGGGCCCAACCGCCACCTCTATGACTTCACTGGAAACTTGAACTTAGATGGGAAAAGC
CTTGTTGCCCTTGGGCCTGACCAGATCTTATTAAGAGGTACACAGCTTAGAAATACTCAG
TGGGTCTTTGGCATAGTTGTTTATACTGGACACGACACCAAACTCATGCAGAATTCAACC
AAAGCGCCTCTCAAGAGATCAAATGTTGAGAAGGTGACTAACGTGCAGATCCTGGTGTTG
TTTGGCATCCTCTTGGTCATGGCCTTGGTGAGCTCGGCGGGGGCCCTGTACTGGAACAGG
TCTCATGGTGAAAAGAACTGGTACATCAAGAAGATGGACACCACCTCAGATAATTTTGGA
TACAACCTACTGACGTTCATCATCTTATACAACAATCTTATTCCCATCAGTCTGTTGGTG
ACTCTTGAGGTTGTGAAGTATACTCAAGCCCTTTTCATAAACTGGGACACAGATATGTAT
TATATAGGAAATGACACTCCTGCCATGGCCAGGACATCAAACCTTAATGAAGAGCTTGGG
CAGGTGAAATATCTCTTTTCTGACAAGACTGGAACGCTTACATGCAATATCATGAACTTT
AAGAAGTGCAGCATTGCCGGAGTAACCTATGGTCACTTCCCAGAATTGGCAAGAGAGCCG
TCTTCAGATGACTTCTGTCGGATGCCTCCTCCCTGTAGTGATTCCTGTGACTTTGATGAC
CCCAGGCTGTTGAAGAACATTGAGGATCGCCATCCCACAGCCCCTTGCATTCAGGAGTTC
CTCACCCTTCTGGCCGTGTGCCACACGGTTGTTCCTGAGAAGGATGGAGATAACATCATC
TACCAGGCCTCTTCCCCAGATGAAGCTGCTTTGGTGAAAGGAGCTAAAAAGCTGGGCTTT
GTCTTCACAGCCAGAACACCATTCTCAGTCATCATAGAAGCGATGGGACAGGAACAAACA
TTCGGAATCCTTAATGTCCTGGAATTTTCTAGTGACAGAAAAAGAATGTCTGTAATTGTT
CGAACTCCTTCAGGACGACTTCGGCTTTACTGTAAAGGGGCTGATAATGTGATTTTTGAG
AGACTTTCAAAAGACTCAAAATATATGGAGGAAACATTATGCCATCTGGAATACTTTGCC
ACGGAAGGCTTGCGGACTCTCTGTGTGGCTTATGCTGATCTCTCTGAGAATGAGTATGAG
GAGTGGCTGAAAGTCTATCAGGAAGCCAGCACCATATTGAAGGACAGAGCTCAACGGTTG
GAAGAGTGTTACGAGATCATTGAGAAGAATTTGCTGCTACTTGGAGCCACAGCCATAGAA
GATCGCCTTCAAGCAGGAGTTCCAGAAACCATCGCAACACTGTTGAAGGCAGAAATTAAA
ATATGGGTGTTGACAGGAGACAAACAAGAAACTGCGATTAATATAGGGTATTCCTGCCGA
TTGGTATCGCAGAATATGGCCCTTATCCTATTGAAGGAGGACTCTTTGGATGCCACAAGG
GCAGCCATTACTCAGCACTGCACTGACCTTGGGAATTTGCTGGGCAAGGAAAATGACGTG
GCCCTGATCATCGATGGCCACACCCTGAAGTACGCGCTCTCCTTCGAAGTCCGGAGGAGT
TTCCTGGATTTGGCACTCTCGTGCAAAGCGGTCATATGCTGCAGAGTGTCTCCTCTGCAG
AAGTCTGAGATAGTGGATGTGGTGAAGAAGCGGGTGAAGGCCATCACCCTCGCCATCGGA
GACGGCGCCAACGATGTCGGGATGATCCAGACAGCCCACGTGGGTGTGGGAATCAGTGGG
AATGAAGGCATGCAGGCCACCAACAACTCGGATTACGCCATCGCACAGTTTTCCTACTTA
GAGAAGCTTCTGTTGGTTCATGGAGCCTGGAGCTACAACCGGGTGACCAAGTGCATCTTG
TACTGCTTCTATAAGAACGTGGTCCTGTATATTATTGAGCTTTGGTTCGCCTTTGTTAAT
GGATTTTCTGGGCAGATTTTATTTGAACGTTGGTGCATCGGCCTGTACAATGTGATTTTC
ACCGCTTTGCCGCCCTTCACTCTGGGAATCTTTGAGAGGTCTTGCACTCAGGAGAGCATG
CTCAGGTTTCCCCAGCTCTACAAAATCACCCAGAATGGCGAAGGCTTCAACACAAAGGTT
TTCTGGGGTCACTGCATCAACGCCTTGGTCCACTCCCTCATCCTCTTCTGGTTTCCCATG
AAAGCTCTGGAGCATGATACTGTGTTGACAAGTGGTCATGCTACCGACTATTTATTTGTT
GGAAATATTGTTTACACATATGTTGTTGTTACTGTTTGTCTGAAAGCTGGTTTGGAGACC
ACAGCTTGGACTAAATTCAGTCATCTGGCTGTCTGGGGAAGCATGCTGACCTGGCTGGTG
TTTTTTGGCATCTACTCGACCATCTGGCCCACCATTCCCATTGCTCCAGATATGAGAGGA
CAGGCAACTATGGTCCTGAGCTCCGCACACTTCTGGTTGGGATTATTTCTGGTTCCTACT
GCCTGTTTGATTGAAGATGTGGCATGGAGAGCAGCCAAGCACACCTGCAAAAAGACATTG
CTGGAGGAGGTGCAGGAGCTGGAAACCAAGTCTCGAGTCCTGGGAAAAGCGGTGCTGCGG
GATAGCAATGGAAAGAGGCTGAACGAGCGCGACCGCCTGATCAAGAGGCTGGGCCGGAAG
ACGCCCCCGACGCTGTTCCGGGGCAGCTCCCTGCAGCAGGGCGTCCCGCATGGGTATGCT
TTTTCTCAAGAAGAACACGGAGCTGTTAGTCAGGAAGAAGTCATCCGTGCTTATGACACC
ACCAAAAAGAAATCCAGGAAGAAATAA
Enzyme 22 GenBank Gene ID NM_016529 Link Image
Enzyme 22 GeneCard ID ATP8A2 Link Image
Enzyme 22 GenAtlas ID ATP8A2 Link Image
Enzyme 22 HGNC ID HGNC:13533 Link Image
Enzyme 22 Chromosome Location 1
Enzyme 22 Locus 13q12
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. 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]
  2. Sun XL, Li D, Fang J, Noyes I, Casto B, Theil K, Shuler C, Milo GE: Changes in levels of normal ML-1 gene transcripts associated with the conversion of human nontumorigenic to tumorigenic phenotypes. Gene Expr. 1999;8(2):129-39. [PubMed Link Image]
  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]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 6655
Enzyme 23 Name Probable phospholipid-transporting ATPase IA
Enzyme 23 Synonyms
  1. ATPase class I type 8A member 1
  2. Chromaffin granule ATPase II
Enzyme 23 Gene Name ATP8A1
Enzyme 23 Protein Sequence >Probable phospholipid-transporting ATPase IA
MPTMRRTVSEIRSRAEGYEKTDDVSEKTSLADQEEVRTIFINQPQLTKFCNNHVSTAKYN
IITFLPRFLYSQFRRAANSFFLFIALLQQIPDVSPTGRYTTLVPLLFILAVAAIKEIIED
IKRHKADNAVNKKQTQVLRNGAWEIVHWEKVAVGEIVKVTNGEHLPADLISLSSSEPQAM
CYIETSNLDGETNLKIRQGLPATSDIKDVDSLMRISGRIECESPNRHLYDFVGNIRLDGH
GTVPLGADQILLRGAQLRNTQWVHGIVVYTGHDTKLMQNSTSPPLKLSNVERITNVQILI
LFCILIAMSLVCSVGSAIWNRRHSGKDWYLNLNYGGASNFGLNFLTFIILFNNLIPISLL
VTLEVVKFTQAYFINWDLDMHYEPTDTAAMARTSNLNEELGQVKYIFSDKTGTLTCNVMQ
FKKCTIAGVAYGHVPEPEDYGCSPDEWQNSQFGDEKTFSDSSLLENLQNNHPTAPIICEF
LTMMAVCHTAVPEREGDKIIYQAASPDEGALVRAAKQLNFVFTGRTPDSVIIDSLGQEER
YELLNVLEFTSARKRMSVIVRTPSGKLRLYCKGADTVIYDRLAETSKYKEITLKHLEQFA
TEGLRTLCFAVAEISESDFQEWRAVYQRASTSVQNRLLKLEESYELIEKNLQLLGATAIE
DKLQDQVPETIETLMKADIKIWILTGDKQETAINIGHSCKLLKKNMGMIVINEGSLDGTR
ETLSRHCTTLGDALRKENDFALIIDGKTLKYALTFGVRQYFLDLALSCKAVICCRVSPLQ
KSEVVEMVKKQVKVVTLAIGDGANDVSMIQTAHVGVGISGNEGLQAANSSDYSIAQFKYL
KNLLMIHGAWNYNRVSKCILYCFYKNIVLYIIEIWFAFVNGFSGQILFERWCIGLYNVMF
TAMPPLTLGIFERSCRKENMLKYPELYKTSQNALDFNTKVFWVHCLNGLFHSVILFWFPL
KALQYGTAFGNGKTSDYLLLGNFVYTFVVITVCLKAGLETSYWTWFSHIAIWGSIALWVV
FFGIYSSLWPAIPMAPDMSGEAAMLFSSGVFWMGLLFIPVASLLLDVVYKVIKRTAFKTL
VDEVQELEAKSQDPGAVVLGKSLTERAQLLKNVFKKNHVNLYRSESLQQNLLHGYAFSQD
ENGIVSQSEVIRAYDTTKQRPDEW
Enzyme 23 Number of Residues 1164
Enzyme 23 Molecular Weight 131368.2
Enzyme 23 Theoretical pI 6.83
Enzyme 23 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • ion binding
  • ion transmembrane transporter activity
  • lipid transporter activity
  • magnesium ion binding
  • metal ion binding
  • nucleoside binding
  • phospholipid transporter activity
  • phospholipid-translocating ATPase activity
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • substrate-specific transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • cellular nitrogen compound metabolic process
  • establishment of localization
  • lipid transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phospholipid transport
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 23 General Function Involved in ATP binding
Enzyme 23 Specific Function May play a role in the transport of aminophospholipids from the outer to the inner leaflet of various membranes and the maintenance of asymmetric distribution of phospholipids, mainly in secretory vesicles
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions
  • ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 66-86 93-115 298-319 345-366 858-878 891-910 941-962 977-999 1006-1026 1045-1070
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein Not Available
Enzyme 23 UniProtKB/Swiss-Prot ID Q9Y2Q0 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name AT8A1_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >3492 bp
ATGCCCACCATGCGGAGGACCGTGTCGGAGATCCGCTCGCGCGCCGAAGGTTATGAGAAG
ACAGATGATGTTTCAGAGAAGACCTCACTGGCTGACCAGGAGGAAGTAAGGACTATTTTC
ATCAACCAGCCCCAGCTGACAAAATTCTGCAATAACCATGTCAGCACTGCAAAATACAAC
ATAATCACATTCCTTCCAAGATTTCTCTACTCTCAGTTCAGAAGAGCTGCTAATTCATTT
TTTCTCTTTATTGCACTGCTGCAGCAAATACCTGATGTGTCACCAACAGGTCGTTATACA
ACACTGGTTCCTCTCTTATTTATTTTAGCTGTGGCAGCTATCAAAGAGATAATAGAAGAT
ATTAAACGACATAAAGCTGATAATGCAGTGAACAAGAAACAAACGCAAGTTTTGAGAAAT
GGTGCTTGGGAAATTGTCCACTGGGAAAAGGTGGCAGTAGGGGAGATAGTGAAAGTGACC
AATGGGGAACATCTCCCAGCAGATCTCATCAGTCTGTCCTCAAGTGAGCCCCAAGCCATG
TGCTACATTGAAACATCCAACTTAGATGGTGAAACAAACTTGAAAATTAGACAGGGCTTA
CCAGCAACATCAGATATCAAAGACGTTGACAGTTTGATGAGGATTTCTGGCAGAATTGAG
TGTGAAAGTCCAAACAGACATCTCTACGATTTTGTTGGAAACATAAGGCTTGATGGACAT
GGCACCGTTCCACTGGGAGCAGATCAGATTCTTCTTCGAGGAGCTCAGTTGAGAAATACA
CAGTGGGTTCATGGAATAGTTGTCTACACTGGACATGACACCAAGCTGATGCAGAATTCA
ACAAGTCCACCACTTAAGCTCTCAAATGTGGAACGGATTACAAATGTACAAATTTTGATT
TTATTTTGTATCTTAATTGCCATGTCTCTTGTCTGTTCTGTGGGCTCAGCCATTTGGAAT
CGAAGGCATTCTGGAAAAGACTGGTATCTCAATCTAAACTATGGTGGCGCTAGTAATTTT
GGACTGAATTTCTTGACCTTCATCATCCTTTTCAACAATCTCATTCCTATCAGCTTATTG
GTTACATTAGAAGTTGTGAAATTTACCCAGGCATACTTCATAAATTGGGATCTTGACATG
CACTATGAACCCACAGACACTGCTGCTATGGCTCGAACATCTAATCTGAATGAGGAACTT
GGCCAGGTTAAATACATATTTTCTGACAAAACTGGTACTCTGACATGCAATGTAATGCAG
TTTAAGAAGTGCACCATAGCGGGAGTTGCTTATGGCCATGTCCCTGAACCTGAGGATTAT
GGCTGCTCTCCTGATGAATGGCAGAACTCACAGTTTGGAGATGAAAAAACATTTAGTGAT
TCATCATTGCTGGAAAATCTCCAAAATAATCATCCAACTGCACCTATAATATGTGAATTT
CTTACAATGATGGCAGTCTGTCACACAGCAGTGCCAGAGCGAGAAGGTGACAAGATTATT
TATCAAGCAGCATCTCCAGATGAGGGAGCATTGGTCAGAGCAGCCAAGCAATTGAATTTT
GTTTTCACTGGAAGAACACCCGACTCGGTGATTATAGATTCACTGGGGCAGGAAGAAAGA
TATGAATTGCTCAATGTCTTGGAGTTTACCAGTGCTAGGAAAAGAATGTCAGTGATTGTT
CGCACTCCATCTGGAAAGTTACGACTCTACTGCAAAGGAGCTGACACTGTAATTTATGAT
CGACTGGCAGAGACGTCAAAATACAAAGAAATTACCCTAAAACATTTAGAGCAGTTTGCT
ACAGAAGGGTTAAGAACTTTATGTTTTGCTGTGGCTGAGATTTCAGAGAGCGACTTTCAG
GAGTGGCGAGCAGTCTATCAGCGAGCATCTACATCTGTGCAGAACAGGCTACTCAAACTC
GAAGAGAGTTATGAGTTGATTGAAAAGAATCTTCAGCTACTTGGAGCAACAGCCATTGAG
GATAAATTACAAGATCAAGTGCCTGAAACCATAGAAACGCTAATGAAAGCAGACATCAAA
ATCTGGATCCTTACAGGGGACAAGCAAGAAACTGCCATTAACATCGGACACTCCTGCAAA
CTGTTGAAGAAGAACATGGGAATGATTGTTATAAATGAAGGCTCTCTTGATGGAACAAGG
GAAACTCTCAGTCGTCACTGTACTACCCTTGGTGATGCTCTCCGGAAAGAGAATGATTTT
GCTCTTATAATTGATGGGAAAACCCTCAAATATGCCTTAACCTTTGGAGTACGACAGTAT
TTCCTGGACTTAGCTTTGTCATGCAAAGCTGTCATTTGCTGTCGGGTTTCTCCTCTTCAA
AAATCTGAAGTTGTTGAGATGGTTAAGAAACAAGTCAAAGTCGTAACGCTTGCAATCGGT
GATGGAGCAAATGATGTCAGCATGATACAGACAGCGCACGTTGGTGTTGGTATCAGTGGC
AATGAAGGCCTGCAGGCAGCTAATTCCTCTGACTACTCCATAGCTCAGTTCAAATATTTG
AAGAATTTACTGATGATTCATGGTGCCTGGAACTATAACAGAGTCTCCAAGTGCATCTTA
TACTGCTTCTACAAGAATATAGTGCTCTATATTATCGAGATCTGGTTTGCCTTTGTTAAT
GGCTTTTCTGGACAGATCCTCTTTGAAAGATGGTGTATAGGTCTCTATAACGTGATGTTT
ACAGCAATGCCTCCTTTAACTCTTGGAATATTTGAGAGATCATGCAGAAAAGAGAACATG
TTGAAGTACCCTGAATTATACAAAACATCTCAGAATGCCCTGGACTTCAACACCAAGGTT
TTCTGGGTTCATTGTTTAAATGGCCTCTTCCACTCAGTTATTCTGTTTTGGTTTCCACTA
AAAGCCCTTCAGTATGGTACTGCATTTGGAAATGGGAAAACCTCGGATTATCTGCTACTG
GGAAACTTTGTGTACACTTTTGTGGTGATAACTGTGTGTTTGAAAGCTGGATTGGAGACA
TCATATTGGACATGGTTCAGCCACATAGCGATATGGGGGAGCATCGCACTCTGGGTGGTG
TTTTTTGGAATCTACTCATCTCTGTGGCCTGCCATTCCGATGGCCCCTGATATGTCAGGA
GAGGCAGCCATGTTGTTCAGTTCTGGAGTCTTTTGGATGGGCTTGTTATTCATCCCTGTG
GCATCTCTGCTCCTTGATGTGGTGTACAAGGTTATCAAGAGGACTGCTTTTAAAACATTG
GTCGATGAAGTTCAGGAGCTGGAGGCAAAATCTCAAGACCCAGGAGCAGTTGTACTTGGA
AAAAGCCTGACCGAGAGGGCGCAACTGCTCAAGAACGTCTTTAAGAAGAACCACGTGAAC
TTGTACCGCTCTGAATCCTTGCAACAAAATCTGCTCCATGGGTATGCGTTCTCTCAAGAT
GAAAATGGAATCGTTTCACAGTCTGAAGTGATAAGAGCATATGATACCACGAAACAGAGG
CCCGACGAATGG
Enzyme 23 GenBank Gene ID AF067820 Link Image
Enzyme 23 GeneCard ID ATP8A1 Link Image
Enzyme 23 GenAtlas ID ATP8A1 Link Image
Enzyme 23 HGNC ID HGNC:13531 Link Image
Enzyme 23 Chromosome Location 4
Enzyme 23 Locus 4p13
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Mouro I, Halleck MS, Schlegel RA, Mattei MG, Williamson P, Zachowski A, Devaux P, Cartron JP, Colin Y: Cloning, expression, and chromosomal mapping of a human ATPase II gene, member of the third subfamily of P-type ATPases and orthologous to the presumed bovine and murine aminophospholipid translocase. Biochem Biophys Res Commun. 1999 Apr 13;257(2):333-9. [PubMed Link Image]
  2. 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]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 6688
Enzyme 24 Name Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
Enzyme 24 Synonyms
  1. PI3-kinase subunit gamma
  2. PI3K-gamma
  3. PtdIns-3-kinase subunit gamma
  4. Phosphatidylinositol-4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma
  5. PtdIns-3-kinase subunit p110-gamma
  6. p120-PI3K
Enzyme 24 Gene Name PIK3CG
Enzyme 24 Protein Sequence >Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
MELENYKQPVVLREDNCRRRRRMKPRSAAASLSSMELIPIEFVLPTSQRKCKSPETALLH
VAGHGNVEQMKAQVWLRALETSVAADFYHRLGPHHFLLLYQKKGQWYEIYDKYQVVQTLD
CLRYWKATHRSPGQIHLVQRHPPSEESQAFQRQLTALIGYDVTDVSNVHDDELEFTRRGL
VTPRMAEVASRDPKLYAMHPWVTSKPLPEYLWKKIANNCIFIVIHRSTTSQTIKVSPDDT
PGAILQSFFTKMAKKKSLMDIPESQSEQDFVLRVCGRDEYLVGETPIKNFQWVRHCLKNG
EEIHVVLDTPPDPALDEVRKEEWPLVDDCTGVTGYHEQLTIHGKDHESVFTVSLWDCDRK
FRVKIRGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNVWLEFSIKI
KDLPKGALLNLQIYCGKAPALSSKASAESPSSESKGKVQLLYYVNLLLIDHRFLLRRGEY
VLHMWQISGKGEDQGSFNADKLTSATNPDKENSMSISILLDNYCHPIALPKHQPTPDPEG
DRVRAEMPNQLRKQLEAIIATDPLNPLTAEDKELLWHFRYESLKHPKAYPKLFSSVKWGQ
QEIVAKTYQLLARREVWDQSALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYL
LQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLRSEIAQSRHYQQRFAVILEAY
LRGCGTAMLHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLP
ESFRVPYDPGLKAGALAIEKCKVMASKKKPLWLEFKCADPTALSNETIGIIFKHGDDLRQ
DMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTVGNTG
AFKDEVLNHWLKEKSPTEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNL
FHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSPHFQKFQDICVKAYLAL
RHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKNEEDAKKYFLDQIEVCRDKGW
TVQFNWFLHLVLGIKQGEKHSA
Enzyme 24 Number of Residues 1102
Enzyme 24 Molecular Weight 126452.6
Enzyme 24 Theoretical pI 7.53
Enzyme 24 GO Classification
Function
  • 1-phosphatidylinositol-3-kinase activity
  • binding
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • kinase activity
  • lipid kinase activity
  • phosphoinositide 3-kinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biological regulation
  • glycerophospholipid metabolic process
  • intracellular signal transduction
  • metabolic process
  • organophosphate metabolic process
  • phosphoinositide metabolic process
  • phosphoinositide phosphorylation
  • phosphoinositide-mediated signaling
  • phospholipid metabolic process
  • regulation of biological process
  • regulation of cellular process
  • second-messenger-mediated signaling
  • signal transduction
Component
  • macromolecular complex
  • phosphoinositide 3-kinase complex
  • protein complex
Enzyme 24 General Function Involved in binding
Enzyme 24 Specific Function 3-phosphorylates the cellular phosphoinositide PtdIns- 4,5-biphosphate (PtdIns(4,5)P2) to produce PtdIns-3, 4,5- triiphosphate (PtdIns(3,4,5)P3). Links G-protein coupled receptor activation to the secondary messenger PtdIns(3,4,5)P3 production
Enzyme 24 Pathways
Enzyme 24 Reactions
  • ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate [RN:R04545]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 1507822 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P48736 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PK3CG_HUMAN Link Image
Enzyme 24 PDB ID 1E8Z Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >3306 bp
ATGGAGCTGGAGAACTATAAACAGCCCGTGGTGCTGAGAGAGGACAACTGCCGAAGGCGC
CGGAGGATGAAGCCGCGCAGTGCTGCCAGCCTGTCCTCCATGGAGCTCATCCCCATCGAG
TTCGTGCTGCCCACCAGCCAGCGCAAATGCAAGAGCCCCGAAACGGCGCTGCTGCACGTG
GCCGGCCACGGCAACGTGGAGCAGATGAAGGCCCAGGTGTGGCTGCGAGCGCTGGAGACC
AGCGTGGCGGCGGACTTCTACCACCGGCTGGGACCGCATCACTTCCTCCTGCTCTATCAG
AAGAAGGGGCAGTGGTACGAGATCTACGACAAGTACCAGGTGGTGCAGACTCTGGACTGC
CTGCGCTACTGGAAGGCCACGCACCGGAGCCCGGGCCAGATCCACCTGGTGCAGCGGCAC
CCGCCCTCCGAGGAGTCCCAAGCCTTCCAGCGGCAGCTCACGGCGCTGATTGGCTATGAC
GTCACTGACGTCAGCAACGTGCACGACGATGAGCTGGAGTTCACGCGCCGTGGCTTGGTG
ACCCCGCGCATGGCGGAGGTGGCCAGCCGCGACCCCAAGCTCTACGCCATGCACCCGTGG
GTGACGTCCAAGCCCCTCCCGGAGTACCTGTGGAAGAAGATTGCCAACAACTGCATCTTC
ATCGTCATTCACCGCAGCACCACCAGCCAGACCATTAAGGTCTCACCCGACGACACCCCC
GGCGCCATCCTGCAGAGCTTCTTCACCAAGATGGCCAAGAAGAAATCTCTGATGGATATT
CCCGAAAGCCAAAGCGAACAGGATTTTGTGCTGCGCGTCTGTGGCCGGGATGAGTACCTG
GTGGGCGAAACGCCCATCAAAAACTTCCAGTGGGTGAGGCACTGCCTCAAGAACGGAGAA
GAGATTCACGTGGTACTGGACACGCCTCCAGACCCGGCCCTAGACGAGGTGAGGAAGGAA
GAGTGGCCGCTGGTGGACGACTGCACGGGAGTCACCGGCTACCATGAGCAGCTTACCATC
CACGGCAAGGACCACGAGAGTGTGTTCACCGTGTCCCTGTGGGACTGCGACCGCAAGTTC
AGGGTCAAGATCAGAGGCATTGATATCCCCGTCCTGCCTCGGAACACCGACCTCACAGTT
TTTGTAGAGGCAAACATCCAGCATGGGCAACAAGTCCTTTGCCAAAGGAGAACCAGCCCC
AAACCCTTCACAGAGGAGGTGCTGTGGAATGTGTGGCTTGAGTTCAGTATCAAAATCAAA
GACTTGCCCAAAGGGGCTCTACTGAACCTCCAGATCTACTGCGGTAAAGCTCCAGCACTG
TCCAGCAAGGCCTCTGCAGAGTCCCCCAGTTCTGAGTCCAAGGGCAAAGTTCGGCTTCTC
TATTATGTGAACCTGCTGCTGATAGACCACCGTTTCCTCCTGCGCCGTGGAGAATACGTC
CTCCACATGTGGCAGATATCTGGGAAGGGAGAAGACCAAGGAAGCTTCAATGCTGACAAA
CTCACGTCTGCAACTAACCCAGACAAGGAGAACTCAATGTCCATCTCCATTCTTCTGGAC
AATTACTGCCACCCGATAGCCCTGCCTAAGCATCAGCCCACCCCTGACCCGGAAGGGGAC
CGGGTTCGAGCAGAAATGCCCAACCAGCTTCGCAAGCAATTGGAGGCGATCATAGCCACT
GATCCACTTAACCCTCTCACAGCAGAGGACAAAGAATTGCTCTGGCATTTTAGATACGAA
AGCCTTAAGCACCCAAAAGCATATCCTAAGCTATTTAGTTCAGTGAAATGGGGACAGCAA
GAAATTGTGGCCAAAACATACCAATTGTTGGCCAGAAGGGAAGTCTGGGATCAAAGTGCT
TTGGATGTTGGGTTAACAATGCAGCTCCTGGACTGCAACTTCTCAGATGAAAATGTAAGA
GCCATTGCAGTTCAGAAACTGGAGAGCTTGGAGGACGATGATGTTCTGCATTACCTTCTA
CAATTGGTCCAGGCTGTGAAATTTGAACCATACCATGATAGCGCCCTTGCCAGATTTCTG
CTGAAGCGTGGTTTAAGAAACAAAAGAATTGGTCACTTTTTGTTTTGGTTCTTGAGAAGT
GAGATAGCCCAGTCCAGACACTATCAGCAGAGGTTCGCTGTGATTCTGGAAGCCTATCTG
AGGGGCTGTGGCACAGCCATGCTGCACGACTTTACCCAACAAGTCCAAGTAATCGAGATG
TTACAAAAAGTCACCCTTGATATTAAATCGCTCTCTGCTGAAAAGTATGACGTCAGTTCC
CAAGTTATTTCACAACTTAAACAAAAGCTTGAAAACCTGCAGAATTCTCAACTCCCCGAA
AGCTTTAGAGTTCCATATGATCCTGGACTGAAAGCAGGAGCGCTGGCAATTGAAAAATGT
AAAGTAATGGCCTCCAAGAAAAAACCACTATGGCTTGAGTTTAAATGTGCCGATCCTACA
GCCCTATCAAATGAAACAATTGGAATTATCTTTAAACATGGTGATGATCTGCGCCAAGAC
ATGCTTATTTTACAGATTCTACGAATCATGGAGTCTATTTGGGAGACTGAATCTTTGGAT
CTATGCCTCCTGCCATATGGTTGCATTTCAACTGGTGACAAAATAGGAATGATCGAGATT
GTGAAAGACGCCACGACAATTGCCAAAATTCAGCAAAGCACAGTGGGCAACACGGGAGCA
TTTAAAGATGAAGTCCTGAATCACTGGCTCAAAGAAAAATCCCCTACTGAAGAAAAGTTT
CAGGCAGCAGTGGAGAGATTTGTTTATTCCTGTGCAGGCTACTGTGTGGCAACCTTTGTT
CTTGGAATAGGCGACAGACACAATGACAATATTATGATCACCGAGACAGGAAACCTATTT
CATATTGACTTCGGGCACATTCTTGGGAATTACAAAAGTTTCCTGGGCATTAATAAAGAG
AGAGTGCCATTTGTGCTAACCCCTGACTTCCTCTTTGTGATGGGAACTTCTGGAAAGAAG
ACAAGCCCACACTTCCAGAAATTTCAGGACATCTGTGTTAAGGCTTATCTAGCCCTTCGT
CATCACACAAACCTACTGATCATCCTGTTCTCCATGATGCTGATGACAGGAATGCCCCAG
TTAACAAGCAAAGAAGACATTGAATATATCCGGGATGCCCTCACAGTGGGGAAAAATGAG
GAGGATGCTAAAAAGTATTTTCTTGATCAGATCGAAGTTTGCAGAGACAAAGGATGGACT
GTGCAGTTTAATTGGTTTCTACATCTTGTTCTTGGCATCAAACAAGGAGAGAAACATTCA
GCCTAA
Enzyme 24 GenBank Gene ID X83368 Link Image
Enzyme 24 GeneCard ID PIK3CG Link Image
Enzyme 24 GenAtlas ID PIK3CG Link Image
Enzyme 24 HGNC ID HGNC:8978 Link Image
Enzyme 24 Chromosome Location 7
Enzyme 24 Locus 7q22.3
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Stoyanov B, Volinia S, Hanck T, Rubio I, Loubtchenkov M, Malek D, Stoyanova S, Vanhaesebroeck B, Dhand R, Nurnberg B, et al.: Cloning and characterization of a G protein-activated human phosphoinositide-3 kinase. Science. 1995 Aug 4;269(5224):690-3. [PubMed Link Image]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  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. Suire S, Coadwell J, Ferguson GJ, Davidson K, Hawkins P, Stephens L: p84, a new Gbetagamma-activated regulatory subunit of the type IB phosphoinositide 3-kinase p110gamma. Curr Biol. 2005 Mar 29;15(6):566-70. [PubMed Link Image]
  5. Walker EH, Perisic O, Ried C, Stephens L, Williams RL: Structural insights into phosphoinositide 3-kinase catalysis and signalling. Nature. 1999 Nov 18;402(6759):313-20. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 6759
Enzyme 25 Name Probable phospholipid-transporting ATPase IM
Enzyme 25 Synonyms
  1. ATPase class I type 8B member 4
Enzyme 25 Gene Name ATP8B4
Enzyme 25 Protein Sequence >Probable phospholipid-transporting ATPase IM
MFCSEKKLREVERIVKANDREYNEKFQYADNRIHTSKYNILTFLPINLFEQFQRVANAYF
LCLLILQLIPEISSLTWFTTIVPLVLVITMTAVKDATDDYFRHKSDNQVNNRQSEVLINS
KLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRHALS
VTSELGADISRLAGFDGIVVCEVPNNKLDKFMGILSWKDSKHSLNNEKIILRGCILRNTS
WCFGMVIFAGPDTKLMQNSGKTKFKRTSIDRLMNTLVLWIFGFLICLGIILAIGNSIWES
QTGDQFRTFLFWNEGEKSSVFSGFLTFWSYIIILNTVVPISLYVSVEVIRLGHSYFINWD
RKMYYSRKAIPAVARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKRCSINGRIYGEVHDD
LDQKTEITQEKEPVDFSVKSQADREFQFFDHHLMESIKMGDPKVHEFLRLLALCHTVMSE
ENSAGELIYQVQSPDEGALVTAARNFGFIFKSRTPETITIEELGTLVTYQLLAFLDFNNT
RKRMSVIVRNPEGQIKLYSKGADTILFEKLHPSNEVLLSLTSDHLSEFAGEGLRTLAIAY
RDLDDKYFKEWHKMLEDANAATEERDERIAGLYEEIERDLMLLGATAVEDKLQEGVIETV
TSLSLANIKIWVLTGDKQETAINIGYACNMLTDDMNDVFVIAGNNAVEVREELRKAKQNL
FGQNRNFSNGHVVCEKKQQLELDSIVEETITGDYALIINGHSLAHALESDVKNDLLELAC
MCKTVICCRVTPLQKAQVVELVKKYRNAVTLAIGDGANDVSMIKSAHIGVGISGQEGLQA
VLASDYSFAQFRYLQRLLLVHGRWSYFRMCKFLCYFFYKNFAFTLVHFWFGFFCGFSAQT
VYDQWFITLFNIVYTSLPVLAMGIFDQDVSDQNSVDCPQLYKPGQLNLLFNKRKFFICVL
HGIYTSLVLFFIPYGAFYNVAGEDGQHIADYQSFAVTMATSLVIVVSVQIALDTSYWTFI
NHVFIWGSIAIYFSILFTMHSNGIFGIFPNQFPFVGNARHSLTQKCIWLVILLTTVASVM
PVVAFRFLKVDLYPTLSDQIRRWQKAQKKARPPSSRRPRTRRSSSRRSGYAFAHQEGYGE
LITSGKNMRAKNPPPTSGLEKTHYNSTSWIENLCKKTTDTVSSFSQDKTVKL
Enzyme 25 Number of Residues 1192
Enzyme 25 Molecular Weight 135867.0
Enzyme 25 Theoretical pI 6.99
Enzyme 25 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • ion binding
  • ion transmembrane transporter activity
  • lipid transporter activity
  • magnesium ion binding
  • metal ion binding
  • nucleoside binding
  • phospholipid transporter activity
  • phospholipid-translocating ATPase activity
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • substrate-specific transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • cellular nitrogen compound metabolic process
  • establishment of localization
  • lipid transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phospholipid transport
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 25 General Function Involved in ATP binding
Enzyme 25 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions
  • ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • 45-66 73-92 277-298 328-349 872-892 905-924 955-976 991-1013 1020-1040 1061-1085
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 50083277 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q8TF62 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name AT8B4_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >3579 bp
ATGTTCTGCAGTGAAAAGAAATTGCGTGAAGTGGAACGGATAGTGAAAGCCAATGACCGT
GAATATAATGAAAAGTTCCAGTATGCGGATAATCGTATCCACACATCGAAATATAATATT
CTCACCTTCTTGCCAATTAATTTATTTGAACAGTTCCAAAGAGTGGCAAATGCCTATTTT
CTTTGCCTTCTGATTTTACAGCTAATTCCAGAAATTTCCTCCTTGACCTGGTTTACCACC
ATTGTGCCTTTGGTCCTGGTGATAACTATGACAGCTGTCAAAGATGCCACAGATGACTAT
TTTCGCCACAAGAGTGATAATCAAGTGAATAATCGGCAGTCTGAAGTGCTCATCAACAGC
AAACTGCAGAATGAAAAATGGATGAATGTCAAAGTGGGAGACATCATTAAATTAGAAAAT
AACCAATTTGTTGCTGCTGATTTACTTCTCCTATCAAGTAGTGAGCCACATGGTCTCTGT
TATGTTGAAACTGCTGAGCTTGATGGGGAAACGAACCTAAAAGTCCGCCATGCACTATCA
GTTACTTCAGAACTTGGAGCAGATATCAGCAGACTTGCAGGGTTTGATGGGATTGTTGTC
TGTGAGGTGCCTAACAACAAGTTAGATAAATTCATGGGAATCCTTTCTTGGAAAGACAGC
AAGCATTCCCTCAACAATGAGAAGATAATCCTGAGAGGCTGCATCCTGAGAAATACCAGC
TGGTGTTTTGGAATGGTTATTTTTGCAGGTCCTGACACTAAACTAATGCAGAATAGTGGT
AAGACAAAGTTTAAAAGGACAAGCATTGATAGATTGATGAATACTCTAGTACTATGGATT
TTTGGGTTTCTGATATGCTTGGGAATTATTCTTGCAATAGGAAATTCAATCTGGGAGAGT
CAAACTGGGGACCAATTCAGAACTTTCCTCTTTTGGAATGAAGGAGAGAAGAGCTCTGTG
TTCTCCGGATTCTTAACATTCTGGTCATATATTATTATTCTCAATACAGTTGTACCCATT
TCCTTATATGTGAGTGTGGAAGTAATTCGTCTAGGACACAGTTATTTTATAAACTGGGAC
CGGAAGATGTATTATTCTCGAAAAGCAATACCTGCAGTGGCTCGAACGACCACGCTCAAT
GAGGAACTGGGGCAGATTGAGTACATTTTCTCCGACAAAACGGGTACCCTCACTCAAAAC
ATCATGACCTTTAAAAGATGTTCCATTAATGGGAGAATCTATGGTGAAGTACATGATGAC
CTGGATCAGAAGACAGAAATAACTCAGGAAAAAGAGCCTGTGGATTTCTCAGTCAAATCT
CAAGCGGATAGAGAATTTCAGTTCTTTGACCACCATCTGATGGAATCCATTAAAATGGGT
GATCCCAAAGTTCATGAATTCCTTAGGTTACTTGCTCTCTGCCACACTGTAATGTCAGAA
GAGAATAGCGCAGGAGAGCTGATTTACCAAGTTCAGTCACCTGATGAAGGGGCTCTAGTG
ACTGCCGCTAGAAATTTTGGGTTCATTTTTAAATCCCGGACCCCAGAGACCATAACAATA
GAAGAATTGGGAACACTAGTTACTTATCAATTACTTGCCTTTTTGGATTTCAACAACACC
AGAAAAAGGATGTCTGTCATAGTTCGAAACCCAGAAGGACAGATAAAGCTTTATTCCAAA
GGAGCAGATACTATTCTGTTTGAAAAACTTCATCCTTCCAATGAAGTCCTTTTGTCTTTG
ACGTCAGACCACCTCAGTGAATTTGCAGGGGAAGGCCTTCGGACCTTGGCCATCGCATAC
AGAGACCTGGATGACAAGTACTTTAAAGAGTGGCATAAGATGCTTGAAGATGCGAATGCT
GCCACAGAAGAGAGGGATGAACGAATAGCTGGGCTATATGAAGAAATTGAAAGAGATTTG
ATGCTACTAGGTGCCACTGCTGTAGAAGATAAGTTACAGGAGGGTGTTATTGAAACAGTT
ACAAGTTTATCACTAGCCAATATTAAGATCTGGGTCCTAACAGGAGACAAACAAGAAACT
GCCATCAACATCGGTTATGCCTGCAACATGCTGACTGACGACATGAATGATGTGTTTGTG
ATAGCAGGGAATAATGCTGTGGAAGTGAGAGAAGAACTCAGGAAAGCAAAACAAAATTTG
TTTGGACAAAACAGAAATTTTTCCAATGGCCATGTAGTTTGTGAAAAAAAGCAGCAGCTG
GAGTTGGATTCTATTGTAGAAGAAACCATAACAGGAGATTATGCCTTAATCATAAATGGC
CACAGTTTGGCTCATGCCCTAGAAAGTGATGTCAAGAATGATCTCCTAGAACTTGCTTGC
ATGTGTAAGACTGTAATTTGCTGCAGGGTCACTCCACTCCAGAAAGCCCAAGTGGTAGAG
CTGGTGAAGAAGTACAGAAATGCTGTTACTTTGGCCATTGGTGATGGAGCCAATGATGTC
AGCATGATTAAAAGTGCTCACATTGGTGTTGGCATCAGCGGCCAGGAAGGATTGCAAGCA
GTCTTAGCCAGCGACTATTCATTTGCACAGTTTAGATATCTCCAAAGGCTTCTCCTTGTT
CATGGAAGGTGGTCTTATTTCCGAATGTGCAAATTCTTATGCTATTTCTTCTATAAGAAT
TTTGCATTTACACTTGTGCATTTCTGGTTTGGTTTCTTCTGTGGTTTCTCAGCCCAGACT
GTTTATGACCAGTGGTTCATCACCCTTTTTAACATTGTTTACACATCACTGCCTGTTTTA
GCCATGGGGATTTTTGACCAGGATGTGAGTGACCAGAACAGCGTGGACTGTCCCCAGCTC
TACAAACCAGGACAGCTGAATCTGCTTTTTAACAAGCGTAAATTTTTCATTTGCGTGTTG
CATGGAATCTACACCTCATTAGTCCTTTTCTTCATCCCCTATGGGGCCTTTTACAACGTG
GCTGGAGAAGATGGGCAACATATTGCTGACTACCAGTCCTTTGCAGTTACCATGGCCACA
TCTTTGGTCATTGTGGTCAGTGTGCAGATAGCCTTGGATACCAGTTACTGGACTTTCATT
AATCACGTCTTCATCTGGGGGAGCATTGCCATTTATTTCTCCATTTTATTTACAATGCAC
AGTAATGGCATCTTTGGCATCTTCCCAAACCAGTTTCCATTTGTTGGTAATGCACGACAT
TCCCTGACCCAGAAGTGCATCTGGCTTGTAATTCTCTTAACAACAGTGGCTTCAGTTATG
CCAGTGGTGGCATTCAGATTTTTGAAGGTGGATTTATACCCAACCCTGAGTGATCAGATC
CGCCGGTGGCAGAAGGCTCAAAAGAAGGCAAGGCCTCCAAGTAGCCGAAGGCCTCGGACC
CGCAGGTCAAGCTCAAGAAGGTCTGGATATGCTTTTGCTCACCAAGAAGGCTATGGAGAG
CTTATCACATCTGGAAAAAATATGCGAGCTAAAAATCCACCCCCAACATCAGGGCTGGAA
AAGACACATTATAATAGCACTAGCTGGATTGAAAATTTATGTAAGAAAACCACAGACACC
GTGAGCAGCTTTAGCCAGGATAAAACAGTGAAACTGTGA
Enzyme 25 GenBank Gene ID NM_024837.2 Link Image
Enzyme 25 GeneCard ID ATP8B4 Link Image
Enzyme 25 GenAtlas ID ATP8B4 Link Image
Enzyme 25 HGNC ID HGNC:13536 Link Image
Enzyme 25 Chromosome Location 1
Enzyme 25 Locus 15q21.2
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed Link Image]
  2. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [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]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 6781
Enzyme 26 Name Probable phospholipid-transporting ATPase IF
Enzyme 26 Synonyms
  1. ATPase IR
  2. ATPase class VI type 11B
Enzyme 26 Gene Name ATP11B
Enzyme 26 Protein Sequence >Probable phospholipid-transporting ATPase IF
MWRWIRQQLGFDPPHQSDTRTIYVANRFPQNGLYTPQKFIDNRIISSKYTVWNFVPKNLF
EQFRRVANFYFLIIFLVQLMIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHNSDNEVN
GAPVYVVRSGGLVKTRSKNIRVGDIVRIAKDEIFPADLVLLSSDRLDGSCHVTTASLDGE
TNLKTHVAVPETALLQTVANLDTLVAVIECQQPEADLYRFMGRMIITQQMEEIVRPLGPE
SLLLRGARLKNTKEIFGVAVYTGMETKMALNYKSKSQKRSAVEKSMNTFLIIYLVILISE
AVISTILKYTWQAEEKWDEPWYNQKTEHQRNSSKILRFISDFLAFLVLYNFIIPISLYVT
VEMQKFLGSFFIGWDLDLYHEESDQKAQVNTSDLNEELGQVEYVFTDKTGTLTENEMQFR
ECSINGMKYQEINGRLVPEGPTPDSSEGNLSYLSSLSHLNNLSHLTTSSSFRTSPENETE
LIKEHDLFFKAVSLCHTVQISNVQTDCTGDGPWQSNLAPSQLEYYASSPDEKALVEAAAR
IGIVFIGNSEETMEVKTLGKLERYKLLHILEFDSDRRRMSVIVQAPSGEKLLFAKGAESS
ILPKCIGGEIEKTRIHVDEFALKGLRTLCIAYRKFTSKEYEEIDKRIFEARTALQQREEK
LAAVFQFIEKDLILLGATAVEDRLQDKVRETIEALRMAGIKVWVLTGDKHETAVSVSLSC
GHFHRTMNILELINQKSDSECAEQLRQLARRITEDHVIQHGLVVDGTSLSLALREHEKLF
MEVCRNCSAVLCCRMAPLQKAKVIRLIKISPEKPITLAVGDGANDVSMIQEAHVGIGIMG
KEGRQAARNSDYAIARFKFLSKLLFVHGHFYYIRIATLVQYFFYKNVCFITPQFLYQFYC
LFSQQTLYDSVYLTLYNICFTSLPILIYSLLEQHVDPHVLQNKPTLYRDISKNRLLSIKT
FLYWTILGFSHAFIFFFGSYLLIGKDTSLLGNGQMFGNWTFGTLVFTVMVITVTVKMALE
THFWTWINHLVTWGSIIFYFVFSLFYGGILWPFLGSQNMYFVFIQLLSSGSAWFAIILMV
VTCLFLDIIKKVFDRHLHPTSTEKAQLTETNAGIKCLDSMCCFPEGEAACASVGRMLERV
IGRCSPTHISRSWSASDPFYTNDRSILTLSTMDSSTC
Enzyme 26 Number of Residues 1177
Enzyme 26 Molecular Weight 134188.6
Enzyme 26 Theoretical pI 6.95
Enzyme 26 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • ion binding
  • ion transmembrane transporter activity
  • lipid transporter activity
  • magnesium ion binding
  • metal ion binding
  • nucleoside binding
  • phospholipid transporter activity
  • phospholipid-translocating ATPase activity
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • substrate-specific transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • cellular nitrogen compound metabolic process
  • establishment of localization
  • lipid transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phospholipid transport
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 26 General Function Involved in ATP binding
Enzyme 26 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions
  • ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • 56-77 83-104 290-311 342-359 877-898 911-930 961-982 998-1020 1026-1047 1066-1090
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 62632750 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q9Y2G3 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name AT11B_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >3534 bp
ATGTGGCGCTGGATCCGGCAGCAGCTGGGTTTTGACCCACCACATCAGAGTGACACAAGA
ACCATCTACGTAGCCAACAGGTTTCCTCAGAATGGCCTTTACACACCTCAGAAATTTATA
GATAACAGGATCATTTCATCTAAGTACACTGTGTGGAATTTTGTTCCAAAAAATTTATTT
GAACAGTTCAGAAGAGTGGCAAACTTTTATTTTCTTATTATATTTTTGGTTCAGCTTATG
ATTGATACACCTACCAGTCCAGTTACCAGTGGACTTCCATTATTCTTTGTGATAACAGTA
ACTGCCATAAAGCAGGGATATGAAGATTGGTTACGGCATAACTCAGATAATGAAGTAAAT
GGAGCTCCTGTTTATGTTGTTCGAAGTGGTGGCCTTGTAAAAACTAGATCAAAAAACATT
CGGGTGGGTGATATTGTTCGAATAGCCAAAGATGAAATTTTTCCTGCAGACTTGGTGCTT
CTGTCCTCAGATCGACTGGATGGTTCCTGTCACGTTACAACTGCTAGTTTGGACGGAGAA
ACTAACCTGAAGACACATGTGGCAGTTCCAGAAACAGCATTATTACAAACAGTTGCCAAT
TTGGACACTCTAGTAGCTGTAATAGAATGCCAGCAACCAGAAGCAGACTTATACAGATTC
ATGGGACGAATGATCATAACCCAACAAATGGAAGAAATTGTAAGACCTCTGGGGCCGGAG
AGTCTCCTGCTTCGTGGAGCCAGATTAAAAAACACAAAAGAAATTTTTGGTGTTGCGGTA
TACACTGGAATGGAAACTAAGATGGCATTAAATTACAAGAGCAAATCACAGAAACGATCT
GCAGTAGAAAAGTCAATGAATACATTTTTGATAATTTATCTAGTAATTCTTATATCTGAA
GCTGTCATCAGCACTATCTTGAAGTATACATGGCAAGCTGAAGAAAAATGGGATGAACCT
TGGTATAACCAAAAAACAGAACATCAAAGAAATAGCAGTAAGATTCTGAGATTTATTTCA
GACTTCCTTGCTTTTTTGGTTCTCTACAATTTCATCATTCCAATTTCATTATATGTGACA
GTCGAAATGCAGAAATTTCTTGGATCATTTTTTATTGGCTGGGATCTTGATCTGTATCAT
GAAGAATCAGATCAGAAAGCTCAAGTCAATACTTCCGATCTGAATGAAGAGCTTGGACAG
GTAGAGTACGTGTTTACAGATAAAACTGGTACACTGACAGAAAATGAGATGCAGTTTCGG
GAATGTTCAATTAATGGCATGAAATACCAAGAAATTAATGGTAGACTTGTACCCGAAGGA
CCAACACCAGACTCTTCAGAAGGAAACTTATCTTATCTTAGTAGTTTATCCCATCTTAAC
AACTTATCCCATCTTACAACCAGTTCCTCTTTCAGAACCAGTCCTGAAAATGAAACTGAA
CTAATTAAAGAACATGATCTCTTCTTTAAAGCAGTCAGTCTCTGTCACACTGTACAGATT
AGCAATGTTCAAACTGACTGCACTGGTGATGGTCCCTGGCAATCCAACCTGGCACCATCG
CAGTTGGAGTACTATGCATCTTCACCAGATGAAAAGGCTCTAGTAGAAGCTGCTGCAAGG
ATTGGTATTGTGTTTATTGGCAATTCTGAAGAAACTATGGAGGTTAAAACTCTTGGAAAA
CTGGAACGGTACAAACTGCTTCATATTCTGGAATTTGATTCAGATCGTAGGAGAATGAGT
GTAATTGTTCAGGCACCTTCAGGTGAGAAGTTATTATTTGCTAAAGGAGCTGAGTCATCA
ATTCTCCCTAAATGTATAGGTGGAGAAATAGAAAAAACCAGAATTCATGTAGATGAATTT
GCTTTGAAAGGGCTAAGAACTCTGTGTATAGCATATAGAAAATTTACATCAAAAGAGTAT
GAGGAAATAGATAAACGCATATTTGAAGCCAGGACTGCCTTGCAGCAGCGGGAAGAGAAA
TTGGCAGCTGTTTTCCAGTTCATAGAGAAAGACCTGATATTACTTGGAGCCACAGCAGTA
GAAGACAGACTACAAGATAAAGTTCGAGAAACTATTGAAGCATTGAGAATGGCTGGTATC
AAAGTATGGGTACTTACTGGGGATAAACATGAAACAGCTGTTAGTGTGAGTTTATCATGT
GGCCATTTTCATAGAACCATGAACATCCTTGAACTTATAAACCAGAAATCAGACAGCGAG
TGTGCTGAACAATTGAGGCAGCTTGCCAGAAGAATTACAGAGGATCATGTGATTCAGCAT
GGGCTGGTAGTGGATGGGACCAGCCTATCTCTTGCACTCAGGGAGCATGAAAAACTATTT
ATGGAAGTTTGCAGAAATTGTTCAGCTGTATTATGCTGTCGTATGGCTCCACTGCAGAAA
GCAAAAGTAATAAGACTAATAAAAATATCACCTGAGAAACCTATAACATTGGCTGTTGGT
GATGGTGCTAATGACGTAAGCATGATACAAGAAGCCCATGTTGGCATAGGAATCATGGGT
AAAGAAGGAAGACAGGCTGCAAGAAACAGTGACTATGCAATAGCCAGATTTAAGTTCCTC
TCCAAATTGCTTTTTGTTCATGGTCATTTTTATTATATTAGAATAGCTACCCTTGTACAG
TATTTTTTTTATAAGAATGTGTGCTTTATCACACCCCAGTTTTTATATCAGTTCTACTGT
TTGTTTTCTCAGCAAACATTGTATGACAGCGTGTACCTGACTTTATACAATATTTGTTTT
ACTTCCCTACCTATTCTGATATATAGTCTTTTGGAACAGCATGTAGACCCTCATGTGTTA
CAAAATAAGCCCACCCTTTATCGAGACATTAGTAAAAACCGCCTCTTAAGTATTAAAACA
TTTCTTTATTGGACCATCCTGGGCTTCAGTCATGCCTTTATTTTCTTTTTTGGATCCTAT
TTACTAATAGGGAAAGATACATCTCTGCTTGGAAATGGCCAGATGTTTGGAAACTGGACA
TTTGGCACTTTGGTCTTCACAGTCATGGTTATTACAGTCACAGTAAAGATGGCTCTGGAA
ACTCATTTTTGGACTTGGATCAACCATCTCGTTACCTGGGGATCTATTATATTTTATTTT
GTATTTTCCTTGTTTTATGGAGGGATTCTCTGGCCATTTTTGGGCTCCCAGAATATGTAT
TTTGTGTTTATTCAGCTCCTGTCAAGTGGTTCTGCTTGGTTTGCCATAATCCTCATGGTT
GTTACATGTCTATTTCTTGATATCATAAAGAAGGTCTTTGACCGACACCTCCACCCTACA
AGTACTGAAAAGGCACAGCTTACTGAAACAAATGCAGGTATCAAGTGCTTGGACTCCATG
TGCTGTTTCCCGGAAGGAGAAGCAGCGTGTGCATCTGTTGGAAGAATGCTGGAACGAGTT
ATAGGAAGATGTAGTCCAACCCACATCAGCAGATCATGGAGTGCATCGGATCCTTTCTAT
ACCAACGACAGGAGCATCTTGACTCTCTCCACAATGGACTCATCTACTTGTTAA
Enzyme 26 GenBank Gene ID NM_014616.1 Link Image
Enzyme 26 GeneCard ID ATP11B Link Image
Enzyme 26 GenAtlas ID ATP11B Link Image
Enzyme 26 HGNC ID HGNC:13553 Link Image
Enzyme 26 Chromosome Location 3
Enzyme 26 Locus 3q27
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Halleck MS, Lawler JF JR, Blackshaw S, Gao L, Nagarajan P, Hacker C, Pyle S, Newman JT, Nakanishi Y, Ando H, Weinstock D, Williamson P, Schlegel RA: Differential expression of putative transbilayer amphipath transporters. Physiol Genomics. 1999 Nov 11;1(3):139-50. [PubMed Link Image]
  2. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, 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, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [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. Halleck MS, Schlegel RA, Williamson PL: Reanalysis of ATP11B, a type IV P-type ATPase. J Biol Chem. 2002 Mar 22;277(12):9736-40. Epub 2002 Jan 14. [PubMed Link Image]
  5. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Feb 26;6(1):63-70. [PubMed Link Image]
  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]
  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]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 6785
Enzyme 27 Name Probable phospholipid-transporting ATPase IK
Enzyme 27 Synonyms
  1. ATPase class I type 8B member 3
Enzyme 27 Gene Name ATP8B3
Enzyme 27 Protein Sequence >Probable phospholipid-transporting ATPase IK
MGTGPAQTPRSTRAGPEPSPAPPGPGDTGDSDVTQEGSGPAGIRGGETVIRAGMGDSPGR
GAPERRHKAQPGRARKYEWRPEGPTSMGSLGQREDLQDEDRNSAFTWKVQANNRAYNGQF
KEKVILCWQRKKYKTNVIRTAKYNFYSFLPLNLYEQFHRVSNLFFLIIIILQSIPDISTL
PWFSLSTPMVCLLFIRATRDLVDDMGRHKSDRAINNRPCQILMGKSFKQKKWQDLCVGDV
VCLRKDNIVPADMLLLASTEPSSLCYVETVDIDGETNLKFRQALMVTHKELATIKKMASF
QGTVTCEAPNSRMHHFVGCLEWNDKKYSLDIGNLLLRGCRIRNTDTCYGLVIYAGFDTKI
MKNCGKIHLKRTKLDLLMNKLVVVIFISVVLVCLVLAFGFGFSVKEFKDHHYYLSGVHGS
SVAAESFFVFWSFLILLSVTIPMSMFILSEFIYLGNSVFIDWDVQMYYKPQDVPAKARST
SLNDHLGQVEYIFSDKTGTLTQNILTFNKCCISGRVYGPDSEATTRPKENPYLWNKFADG
KLLFHNAALLHLVRTNGDEAVREFWRLLAICHTVMVRESPRERPDQLLYQAASPDEGALV
TAARNFGYVFLSRTQDTVTIMELGEERVYQVLAIMDFNSTRKRMSVLVRKPEGAICLYTK
GADTVIFERLHRRGAMEFATEEALAAFAQETLRTLCLAYREVAEDIYEDWQQRHQEASLL
LQNRAQALQQLLGATAIEDRLQDGVPETIKCLKKSNIKIWVLTGDKQETAVNIGFACELL
SENMLILEEKEISRILETYWENSNNLLTRESLSQVKLALVINGDFLDKLLVSLRKEPRAL
AQNVNMDEAWQELGQSRRDFLYARRLSLLCRRFGLPLAAPPAQDSRARRSSEVLQERAFV
DLASKCQAVICCRVTPKQKALIVALVKKYHQVVTLAIGDGANDINMIKTADVGVGLAGQE
GMQAVQNSDFVLGQFCFLQRLLLVHGRWSYVRICKFLRYFFYKSMASMMVQVWFACYNGF
TGQPLYEGWFLALFNLLYSTLPVLYIGLFEQDVSAEQSLEKPELYVVGQKDELFNYWVFV
QAIAHGVTTSLVNFFMTLWISRDTAGPASFSDHQSFAVVVALSCLLSITMEVILIIKYWT
ALCVATILLSLGFYAIMTTTTQSFWLFRVSPTTFPFLYADLSVMSSPSILLVVLLSVSIN
TFPVLALRVIFPALKELRAKEEKVEEGPSEEIFTMEPLPHVHRESRARRSSYAFSHREGY
ANLITQGTILRRGPGVSSDIASESLDPSDEEAASSPKESQ
Enzyme 27 Number of Residues 1300
Enzyme 27 Molecular Weight 146750.9
Enzyme 27 Theoretical pI 7.96
Enzyme 27 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • ion binding
  • ion transmembrane transporter activity
  • lipid transporter activity
  • magnesium ion binding
  • metal ion binding
  • nucleoside binding
  • phospholipid transporter activity
  • phospholipid-translocating ATPase activity
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • substrate-specific transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • cellular nitrogen compound metabolic process
  • establishment of localization
  • lipid transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phospholipid transport
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 27 General Function Involved in ATP binding
Enzyme 27 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions
  • ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • 150-171 178-197 382-403 431-452 996-1016 1029-1048 1079-1100 1113-1135 1142-1162 1183-1207
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 44888835 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID O60423 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name AT8B3_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >3903 bp
ATGGGCACTGGCCCCGCTCAGACTCCCAGGAGCACCAGAGCTGGCCCTGAGCCAAGCCCT
GCCCCACCAGGACCTGGGGACACGGGTGACTCAGACGTGACTCAGGAAGGCTCAGGTCCT
GCTGGCATCCGCGGAGGTGAGACGGTGATCAGAGCTGGGATGGGAGACTCCCCAGGCAGA
GGGGCACCTGAGAGGAGGCACAAGGCCCAGCCTGGCCGGGCTAGGAAGTATGAATGGAGA
CCAGAAGGCCCCACCAGCATGGGCAGCCTCGGCCAGAGAGAAGATCTCCAAGATGAGGAC
AGGAACTCAGCATTCACCTGGAAGGTCCAGGCCAACAACCGTGCCTACAACGGGCAGTTC
AAGGAGAAGGTGATCCTGTGCTGGCAAAGGAAGAAATACAAGACCAATGTCATCCGCACG
GCCAAGTACAACTTCTACTCGTTCCTGCCGCTGAACCTGTACGAGCAGTTCCACCGCGTG
TCCAACCTGTTCTTCCTCATCATCATCATCCTGCAGAGCATTCCCGACATCTCCACGCTG
CCCTGGTTCTCGCTCAGTACCCCTATGGTCTGCCTCCTCTTCATCCGTGCCACCCGGGAC
CTGGTGGACGACATGGGGAGACACAAGAGTGACAGAGCCATCAACAACAGACCCTGCCAG
ATTCTGATGGGGAAGAGCTTCAAGCAGAAGAAATGGCAGGATCTGTGCGTGGGGGATGTG
GTCTGTCTCCGCAAGGACAACATCGTCCCAGCCGACATGCTCTTGCTGGCCAGCACGGAG
CCCAGCAGCCTGTGCTATGTGGAGACGGTGGACATTGACGGGGAGACCAACTTGAAGTTC
AGACAGGCCCTGATGGTCACCCACAAAGAACTGGCCACTATAAAGAAGATGGCGTCCTTT
CAAGGCACAGTGACGTGTGAGGCGCCTAACAGTCGGATGCACCACTTCGTGGGGTGCCTG
GAATGGAATGACAAGAAATACTCCCTGGACATTGGCAACCTCCTCCTCCGAGGCTGCAGG
ATTCGCAACACAGACACCTGCTATGGACTGGTCATTTATGCTGGTTTTGACACAAAAATT
ATGAAGAACTGTGGCAAGATCCATTTGAAGAGAACCAAGCTGGACCTCCTGATGAACAAG
CTGGTGGTTGTGATCTTCATCTCCGTGGTGCTTGTCTGCCTGGTGTTGGCCTTCGGCTTC
GGTTTCTCAGTCAAAGAATTCAAAGACCACCACTACTACCTCTCGGGGGTGCATGGGAGC
AGCGTGGCCGCAGAGTCCTTCTTCGTCTTCTGGAGCTTCCTCATCCTGCTCAGCGTCACC
ATCCCGATGTCCATGTTCATCCTGTCCGAGTTCATCTACCTGGGGAACAGCGTCTTCATC
GACTGGGACGTGCAGATGTACTACAAGCCGCAGGACGTGCCTGCCAAGGCCCGCAGCACC
AGCCTCAACGACCACCTGGGCCAGGTGGAATACATCTTCTCGGACAAGACGGGCACGCTC
ACGCAGAACATCTTGACCTTCAACAAGTGCTGCATCAGCGGCCGCGTCTATGGGCCGGAT
TCAGAGGCCACGACCCGACCTAAGGAGAACCCCTACCTCTGGAACAAGTTCGCCGACGGG
AAGCTGCTCTTCCACAATGCGGCCCTGCTGCACCTCGTGCGGACCAACGGGGACGAGGCC
GTGCGGGAGTTCTGGCGCCTGCTGGCCATCTGCCACACGGTGATGGTGCGGGAGAGCCCC
CGTGAGCGCCCAGACCAGCTGTTGTACCAGGCGGCCTCCCCCGACGAGGGGGCGCTGGTC
ACCGCAGCCCGGAACTTCGGCTACGTGTTCCTGTCCCGCACCCAGGACACCGTCACGATC
ATGGAGCTGGGGGAGGAACGGGTCTACCAGGTCCTGGCCATAATGGACTTCAACAGCACG
CGCAAACGGATGTCGGTGCTGGTTCGAAAGCCAGAGGGCGCCATCTGCCTGTACACCAAG
GGCGCCGACACGGTCATCTTCGAACGCTTGCACAGGAGGGGGGCAATGGAATTTGCCACA
GAGGAGGCCTTGGCTGCCTTTGCCCAGGAGACCCTGCGGACACTGTGCCTGGCCTACAGG
GAGGTGGCTGAGGACATTTACGAGGACTGGCAGCAGCGCCACCAGGAGGCCAGCCTCCTG
CTGCAGAACCGGGCACAGGCCCTGCAACAGCTGCTGGGAGCCACAGCCATCGAGGACAGA
CTCCAGGACGGTGTCCCTGAAACCATCAAATGTCTCAAGAAGAGCAACATCAAAATATGG
GTGCTCACCGGGGACAAGCAGGAAACGGCTGTGAACATCGGCTTCGCCTGCGAGCTGCTG
TCAGAGAATATGCTCATTCTGGAGGAGAAGGAGATTAGCCGCATCCTGGAGACCTACTGG
GAAAACAGTAACAACCTTCTAACCAGGGAGTCCCTGTCGCAGGTCAAGCTGGCCTTGGTC
ATTAACGGAGACTTCCTGGACAAACTGCTGGTGTCCCTGCGGAAGGAGCCGCGCGCCCTG
GCGCAGAACGTGAACATGGACGAGGCGTGGCAGGAGCTCGGCCAGTCCAGGAGGGATTTC
CTCTACGCCAGGCGCCTGTCCCTGCTGTGCCGGAGGTTCGGGCTCCCGCTGGCTGCACCG
CCAGCCCAGGACTCCAGAGCCCGCCGTAGCTCCGAGGTGCTGCAGGAGCGCGCCTTCGTG
GACCTGGCGTCCAAGTGCCAGGCGGTCATCTGCTGCCGCGTGACGCCCAAGCAGAAGGCC
CTGATCGTGGCCCTGGTCAAGAAGTACCACCAGGTGGTGACCCTGGCCATCGGGGACGGT
GCCAACGACATCAACATGATCAAGACCGCGGACGTGGGCGTGGGGCTGGCGGGCCAGGAG
GGCATGCAGGCAGTTCAGAACAGCGACTTCGTGCTCGGCCAGTTCTGCTTCCTGCAGCGC
CTCCTGCTGGTGCACGGCCGCTGGTCCTACGTGCGGATCTGCAAGTTCCTGCGCTACTTC
TTCTACAAGAGCATGGCCAGCATGATGGTGCAGGTCTGGTTTGCCTGCTACAACGGCTTC
ACCGGCCAGCCCCTGTATGAAGGATGGTTCCTGGCTCTTTTCAACCTCCTGTACAGCACC
CTGCCAGTTCTCTACATTGGGCTCTTTGAGCAGGACGTGAGCGCAGAGCAGAGCCTGGAG
AAGCCGGAGCTGTACGTGGTGGGGCAGAAGGACGAGCTCTTCAACTACTGGGTCTTCGTC
CAAGCCATCGCCCATGGTGTGACCACCTCTCTGGTCAACTTCTTCATGACACTGTGGATC
AGCCGCGACACGGCGGGACCCGCCAGCTTCAGCGACCACCAGTCCTTTGCGGTCGTGGTG
GCCCTGTCTTGCCTGCTGTCCATCACCATGGAGGTCATTCTTATCATCAAGTACTGGACC
GCCCTGTGCGTGGCGACCATCCTCCTCAGCCTTGGTTTCTACGCCATCATGACTACCACC
ACCCAGAGCTTCTGGCTCTTCAGAGTATCCCCCACGACCTTCCCGTTTCTGTATGCCGAC
CTCAGCGTGATGTCCTCTCCCTCCATCCTGCTGGTGGTCCTGCTGAGTGTGTCCATAAAC
ACCTTCCCTGTCCTGGCCCTCCGAGTCATCTTCCCAGCCCTCAAGGAGCTACGTGCCAAG
GAGGAGAAGGTGGAGGAGGGCCCCAGCGAGGAGATTTTCACCATGGAGCCCTTGCCTCAT
GTACACCGGGAGTCTCGTGCCCGCCGTTCCAGCTATGCTTTCTCCCACCGTGAGGGATAT
GCAAACCTCATCACTCAGGGCACAATTCTGCGGAGGGGACCAGGGGTCAGCAGTGACATA
GCATCTGAATCCCTAGACCCATCTGATGAAGAGGCAGCTTCGAGCCCAAAAGAGTCACAG
TGA
Enzyme 27 GenBank Gene ID NM_138813.2 Link Image
Enzyme 27 GeneCard ID ATP8B3 Link Image
Enzyme 27 GenAtlas ID ATP8B3 Link Image
Enzyme 27 HGNC ID HGNC:13535 Link Image
Enzyme 27 Chromosome Location 1
Enzyme 27 Locus 19p13.3
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. 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]
  2. 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]
  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]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 6866
Enzyme 28 Name Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Enzyme 28 Synonyms
  1. Mutated in multiple advanced cancers 1
  2. Phosphatase and tensin homolog
Enzyme 28 Gene Name PTEN
Enzyme 28 Protein Sequence >Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSK
HKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVA
AIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSY
LLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMY
FEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEI
DSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEAS
SSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV
Enzyme 28 Number of Residues 403
Enzyme 28 Molecular Weight 47165.9
Enzyme 28 Theoretical pI 6.33
Enzyme 28 GO Classification
Function
  • PDZ domain binding
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • phosphatase activity
  • phosphatidylinositol bisphosphate phosphatase activity
  • phosphatidylinositol trisphosphate phosphatase activity
  • phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity
  • phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity
  • phosphoprotein phosphatase activity
  • phosphoric ester hydrolase activity
  • protein binding
  • protein domain specific binding
  • protein tyrosine phosphatase activity
  • protein tyrosine/serine/threonine phosphatase activity
Process
  • alcohol metabolic process
  • biological regulation
  • cellular metabolic process
  • dephosphorylation
  • glycerophospholipid metabolic process
  • inositol metabolic process
  • inositol phosphate dephosphorylation
  • metabolic process
  • negative regulation of cell migration
  • negative regulation of cell proliferation
  • negative regulation of cell-matrix adhesion
  • negative regulation of focal adhesion assembly
  • negative regulation of intracellular protein kinase cascade
  • negative regulation of protein kinase B signaling cascade
  • negative regulation of signal transduction
  • organophosphate metabolic process
  • phosphate metabolic process
  • phosphoinositide dephosphorylation
  • phosphoinositide metabolic process
  • phospholipid metabolic process
  • phosphorus metabolic process
  • polyol metabolic process
  • posttranscriptional regulation of gene expression
  • protein amino acid dephosphorylation
  • regulation of biological process
  • regulation of cell adhesion
  • regulation of cell communication
  • regulation of cell migration
  • regulation of cell motility
  • regulation of cell proliferation
  • regulation of cell-matrix adhesion
  • regulation of cell-substrate adhesion
  • regulation of cellular process
  • regulation of gene expression
  • regulation of locomotion
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of protein stability
  • regulation of signal transduction
  • small molecule metabolic process
Component
Enzyme 28 General Function Involved in magnesium ion binding
Enzyme 28 Specific Function Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine- phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3- phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K- AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability
Enzyme 28 Pathways
Enzyme 28 Reactions
  • phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate [RN:R04513]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein Not Available
Enzyme 28 UniProtKB/Swiss-Prot ID P60484 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name PTEN_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1212 bp
ATGACAGCCATCATCAAAGAGATCGTTAGCAGAAACAAAAGGAGATATCAAGAGGATGGA
TTCGACTTAGACTTGACCTATATTTATCCAAACATTATTGCTATGGGATTTCCTGCAGAA
AGACTTGAAGGCGTATACAGGAACAATATTGATGATGTAGTAAGGTTTTTGGATTCAAAG
CATAAAAACCATTACAAGATATACAATCTTTGTGCTGAAAGACATTATGACACCGCCAAA
TTTAATTGCAGAGTTGCACAATATCCTTTTGAAGACCATAACCCACCACAGCTAGAACTT
ATCAAACCCTTTTGTGAAGATCTTGACCAATGGCTAAGTGAAGATGACAATCATGTTGCA
GCAATTCACTGTAAAGCTGGAAAGGGACGAACTGGTGTAATGATATGTGCATATTTATTA
CATCGGGGCAAATTTTTAAAGGCACAAGAGGCCCTAGATTTCTATGGGGAAGTAAGGACC
AGAGACAAAAAGGGAGTAACTATTCCCAGTCAGAGGCGCTATGTGTATTATTATAGCTAC
CTGTTAAAGAATCATCTGGATTATAGACCAGTGGCACTGTTGTTTCACAAGATGATGTTT
GAAACTATTCCAATGTTCAGTGGCGGAACTTGCAATCCTCAGTTTGTGGTCTGCCAGCTA
AAGGTGAAGATATATTCCTCCAATTCAGGACCCACACGACGGGAAGACAAGTTCATGTAC
TTTGAGTTCCCTCAGCCGTTACCTGTGTGTGGTGATATCAAAGTAGAGTTCTTCCACAAA
CAGAACAAGATGCTAAAAAAGGACAAAATGTTTCACTTTTGGGTAAATACATTCTTCATA
CCAGGACCAGAGGAAACCTCAGAAAAAGTAGAAAATGGAAGTCTATGTGATCAAGAAATC
GATAGCATTTGCAGTATAGAGCGTGCAGATAATGACAAGGAATATCTAGTACTTACTTTA
ACAAAAAATGATCTTGACAAAGCAAATAAAGACAAAGCCAACCGATACTTTTCTCCAAAT
TTTAAGGTGAAGCTGTACTTCACAAAAACAGTAGAGGAGCCGTCAAATCCAGAGGCTAGC
AGTTCAACTTCTGTAACACCAGATGTTAGTGACAATGAACCTGATCATTATAGATATTCT
GACACCACTGACTCTGATCCAGAGAATGAACCTTTTGATGAAGATCAGCATACACAAATT
ACAAAAGTCTGA
Enzyme 28 GenBank Gene ID U96180 Link Image
Enzyme 28 GeneCard ID PTEN Link Image
Enzyme 28 GenAtlas ID PTEN Link Image
Enzyme 28 HGNC ID HGNC:9588 Link Image
Enzyme 28 Chromosome Location 1
Enzyme 28 Locus 10q23.3
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Li DM, Sun H: TEP1, encoded by a candidate tumor suppressor locus, is a novel protein tyrosine phosphatase regulated by transforming growth factor beta. Cancer Res. 1997 Jun 1;57(11):2124-9. [PubMed Link Image]
  2. Steck PA, Pershouse MA, Jasser SA, Yung WK, Lin H, Ligon AH, Langford LA, Baumgard ML, Hattier T, Davis T, Frye C, Hu R, Swedlund B, Teng DH, Tavtigian SV: Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers. Nat Genet. 1997 Apr;15(4):356-62. [PubMed Link Image]
  3. Li J, Yen C, Liaw D, Podsypanina K, Bose S, Wang SI, Puc J, Miliaresis C, Rodgers L, McCombie R, Bigner SH, Giovanella BC, Ittmann M, Tycko B, Hibshoosh H, Wigler MH, Parsons R: PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science. 1997 Mar 28;275(5308):1943-7. [PubMed Link Image]
  4. Hamilton JA, Stewart LM, Ajayi L, Gray IC, Gray NE, Roberts KG, Watson GJ, Kaisary AV, Snary D: The expression profile for the tumour suppressor gene PTEN and associated polymorphic markers. Br J Cancer. 2000 May;82(10):1671-6. [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. Myers MP, Stolarov JP, Eng C, Li J, Wang SI, Wigler MH, Parsons R, Tonks NK: P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase. Proc Natl Acad Sci U S A. 1997 Aug 19;94(17):9052-7. [PubMed Link Image]
  8. Maehama T, Dixon JE: The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem. 1998 May 29;273(22):13375-8. [PubMed Link Image]
  9. Myers MP, Pass I, Batty IH, Van der Kaay J, Stolarov JP, Hemmings BA, Wigler MH, Downes CP, Tonks NK: The lipid phosphatase activity of PTEN is critical for its tumor supressor function. Proc Natl Acad Sci U S A. 1998 Nov 10;95(23):13513-8. [PubMed Link Image]
  10. Tamura M, Gu J, Matsumoto K, Aota S, Parsons R, Yamada KM: Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN. Science. 1998 Jun 5;280(5369):1614-7. [PubMed Link Image]
  11. Georgescu MM, Kirsch KH, Akagi T, Shishido T, Hanafusa H: The tumor-suppressor activity of PTEN is regulated by its carboxyl-terminal region. Proc Natl Acad Sci U S A. 1999 Aug 31;96(18):10182-7. [PubMed Link Image]
  12. Adey NB, Huang L, Ormonde PA, Baumgard ML, Pero R, Byreddy DV, Tavtigian SV, Bartel PL: Threonine phosphorylation of the MMAC1/PTEN PDZ binding domain both inhibits and stimulates PDZ binding. Cancer Res. 2000 Jan 1;60(1):35-7. [PubMed Link Image]
  13. Wu Y, Dowbenko D, Spencer S, Laura R, Lee J, Gu Q, Lasky LA: Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase. J Biol Chem. 2000 Jul 14;275(28):21477-85. [PubMed Link Image]
  14. Wu X, Hepner K, Castelino-Prabhu S, Do D, Kaye MB, Yuan XJ, Wood J, Ross C, Sawyers CL, Whang YE: Evidence for regulation of the PTEN tumor suppressor by a membrane-localized multi-PDZ domain containing scaffold protein MAGI-2. Proc Natl Acad Sci U S A. 2000 Apr 11;97(8):4233-8. [PubMed Link Image]
  15. Vazquez F, Grossman SR, Takahashi Y, Rokas MV, Nakamura N, Sellers WR: Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex. J Biol Chem. 2001 Dec 28;276(52):48627-30. Epub 2001 Nov 13. [PubMed Link Image]
  16. Miller SJ, Lou DY, Seldin DC, Lane WS, Neel BG: Direct identification of PTEN phosphorylation sites. FEBS Lett. 2002 Sep 25;528(1-3):145-53. [PubMed Link Image]
  17. Valiente M, Andres-Pons A, Gomar B, Torres J, Gil A, Tapparel C, Antonarakis SE, Pulido R: Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases. J Biol Chem. 2005 Aug 12;280(32):28936-43. Epub 2005 Jun 10. [PubMed Link Image]
  18. Wang X, Trotman LC, Koppie T, Alimonti A, Chen Z, Gao Z, Wang J, Erdjument-Bromage H, Tempst P, Cordon-Cardo C, Pandolfi PP, Jiang X: NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN. Cell. 2007 Jan 12;128(1):129-39. [PubMed Link Image]
  19. Song MS, Salmena L, Carracedo A, Egia A, Lo-Coco F, Teruya-Feldstein J, Pandolfi PP: The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network. Nature. 2008 Oct 9;455(7214):813-7. Epub 2008 Aug 20. [PubMed Link Image]
  20. Yim EK, Peng G, Dai H, Hu R, Li K, Lu Y, Mills GB, Meric-Bernstam F, Hennessy BT, Craven RJ, Lin SY: Rak functions as a tumor suppressor by regulating PTEN protein stability and function. Cancer Cell. 2009 Apr 7;15(4):304-14. [PubMed Link Image]
  21. 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]
  22. Mund T, Pelham HR: Regulation of PTEN/Akt and MAP kinase signaling pathways by the ubiquitin ligase activators Ndfip1 and Ndfip2. Proc Natl Acad Sci U S A. 2010 Jun 22;107(25):11429-34. Epub 2010 Jun 7. [PubMed Link Image]
  23. Lee JO, Yang H, Georgescu MM, Di Cristofano A, Maehama T, Shi Y, Dixon JE, Pandolfi P, Pavletich NP: Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Cell. 1999 Oct 29;99(3):323-34. [PubMed Link Image]
  24. Tsou HC, Teng DH, Ping XL, Brancolini V, Davis T, Hu R, Xie XX, Gruener AC, Schrager CA, Christiano AM, Eng C, Steck P, Ott J, Tavtigian SV, Peacocke M: The role of MMAC1 mutations in early-onset breast cancer: causative in association with Cowden syndrome and excluded in BRCA1-negative cases. Am J Hum Genet. 1997 Nov;61(5):1036-43. [PubMed Link Image]
  25. Lynch ED, Ostermeyer EA, Lee MK, Arena JF, Ji H, Dann J, Swisshelm K, Suchard D, MacLeod PM, Kvinnsland S, Gjertsen BT, Heimdal K, Lubs H, Moller P, King MC: Inherited mutations in PTEN that are associated with breast cancer, cowden disease, and juvenile polyposis. Am J Hum Genet. 1997 Dec;61(6):1254-60. [PubMed Link Image]
  26. Wang SI, Puc J, Li J, Bruce JN, Cairns P, Sidransky D, Parsons R: Somatic mutations of PTEN in glioblastoma multiforme. Cancer Res. 1997 Oct 1;57(19):4183-6. [PubMed Link Image]
  27. Nelen MR, van Staveren WC, Peeters EA, Hassel MB, Gorlin RJ, Hamm H, Lindboe CF, Fryns JP, Sijmons RH, Woods DG, Mariman EC, Padberg GW, Kremer H: Germline mutations in the PTEN/MMAC1 gene in patients with Cowden disease. Hum Mol Genet. 1997 Aug;6(8):1383-7. [PubMed Link Image]
  28. Liaw D, Marsh DJ, Li J, Dahia PL, Wang SI, Zheng Z, Bose S, Call KM, Tsou HC, Peacocke M, Eng C, Parsons R: Germline mutations of the PTEN gene in Cowden disease, an inherited breast and thyroid cancer syndrome. Nat Genet. 1997 May;16(1):64-7. [PubMed Link Image]
  29. Marsh DJ, Dahia PL, Zheng Z, Liaw D, Parsons R, Gorlin RJ, Eng C: Germline mutations in PTEN are present in Bannayan-Zonana syndrome. Nat Genet. 1997 Aug;16(4):333-4. [PubMed Link Image]
  30. Maxwell GL, Risinger JI, Gumbs C, Shaw H, Bentley RC, Barrett JC, Berchuck A, Futreal PA: Mutation of the PTEN tumor suppressor gene in endometrial hyperplasias. Cancer Res. 1998 Jun 15;58(12):2500-3. [PubMed Link Image]
  31. Chi SG, Kim HJ, Park BJ, Min HJ, Park JH, Kim YW, Dong SH, Kim BH, Lee JI, Chang YW, Chang R, Kim WK, Yang MH: Mutational abrogation of the PTEN/MMAC1 gene in gastrointestinal polyps in patients with Cowden disease. Gastroenterology. 1998 Nov;115(5):1084-9. [PubMed Link Image]
  32. Tsou HC, Ping XL, Xie XX, Gruener AC, Zhang H, Nini R, Swisshelm K, Sybert V, Diamond TM, Sutphen R, Peacocke M: The genetic basis of Cowden's syndrome: three novel mutations in PTEN/MMAC1/TEP1. Hum Genet. 1998 Apr;102(4):467-73. [PubMed Link Image]
  33. Marsh DJ, Coulon V, Lunetta KL, Rocca-Serra P, Dahia PL, Zheng Z, Liaw D, Caron S, Duboue B, Lin AY, Richardson AL, Bonnetblanc JM, Bressieux JM, Cabarrot-Moreau A, Chompret A, Demange L, Eeles RA, Yahanda AM, Fearon ER, Fricker JP, Gorlin RJ, Hodgson SV, Huson S, Lacombe D, Eng C, et al.: Mutation spectrum and genotype-phenotype analyses in Cowden disease and Bannayan-Zonana syndrome, two hamartoma syndromes with germline PTEN mutation. Hum Mol Genet. 1998 Mar;7(3):507-15. [PubMed Link Image]
  34. Scala S, Bruni P, Lo Muzio L, Mignogna M, Viglietto G, Fusco A: Novel mutation of the PTEN gene in an Italian Cowden's disease kindred. Int J Oncol. 1998 Oct;13(4):665-8. [PubMed Link Image]
  35. Marsh DJ, Dahia PL, Caron S, Kum JB, Frayling IM, Tomlinson IP, Hughes KS, Eeles RA, Hodgson SV, Murday VA, Houlston R, Eng C: Germline PTEN mutations in Cowden syndrome-like families. J Med Genet. 1998 Nov;35(11):881-5. [PubMed Link Image]
  36. Olschwang S, Serova-Sinilnikova OM, Lenoir GM, Thomas G: PTEN germ-line mutations in juvenile polyposis coli. Nat Genet. 1998 Jan;18(1):12-4. [PubMed Link Image]
  37. Kurose K, Araki T, Matsunaka T, Takada Y, Emi M: Variant manifestation of Cowden disease in Japan: hamartomatous polyposis of the digestive tract with mutation of the PTEN gene. Am J Hum Genet. 1999 Jan;64(1):308-10. [PubMed Link Image]
  38. Sutphen R, Diamond TM, Minton SE, Peacocke M, Tsou HC, Root AW: Severe Lhermitte-Duclos disease with unique germline mutation of PTEN. Am J Med Genet. 1999 Feb 12;82(4):290-3. [PubMed Link Image]
  39. Nelen MR, Kremer H, Konings IB, Schoute F, van Essen AJ, Koch R, Woods CG, Fryns JP, Hamel B, Hoefsloot LH, Peeters EA, Padberg GW: Novel PTEN mutations in patients with Cowden disease: absence of clear genotype-phenotype correlations. Eur J Hum Genet. 1999 Apr;7(3):267-73. [PubMed Link Image]
  40. Marsh DJ, Kum JB, Lunetta KL, Bennett MJ, Gorlin RJ, Ahmed SF, Bodurtha J, Crowe C, Curtis MA, Dasouki M, Dunn T, Feit H, Geraghty MT, Graham JM Jr, Hodgson SV, Hunter A, Korf BR, Manchester D, Miesfeldt S, Murday VA, Nathanson KL, Parisi M, Pober B, Romano C, Eng C, et al.: PTEN mutation spectrum and genotype-phenotype correlations in Bannayan-Riley-Ruvalcaba syndrome suggest a single entity with Cowden syndrome. Hum Mol Genet. 1999 Aug;8(8):1461-72. [PubMed Link Image]
  41. Han SY, Kato H, Kato S, Suzuki T, Shibata H, Ishii S, Shiiba K, Matsuno S, Kanamaru R, Ishioka C: Functional evaluation of PTEN missense mutations using in vitro phosphoinositide phosphatase assay. Cancer Res. 2000 Jun 15;60(12):3147-51. [PubMed Link Image]
  42. De Vivo I, Gertig DM, Nagase S, Hankinson SE, O'Brien R, Speizer FE, Parsons R, Hunter DJ: Novel germline mutations in the PTEN tumour suppressor gene found in women with multiple cancers. J Med Genet. 2000 May;37(5):336-41. [PubMed Link Image]
  43. Celebi JT, Shendrik I, Silvers DN, Peacocke M: Identification of PTEN mutations in metastatic melanoma specimens. J Med Genet. 2000 Sep;37(9):653-7. [PubMed Link Image]
  44. Weng LP, Brown JL, Eng C: PTEN coordinates G(1) arrest by down-regulating cyclin D1 via its protein phosphatase activity and up-regulating p27 via its lipid phosphatase activity in a breast cancer model. Hum Mol Genet. 2001 Mar 15;10(6):599-604. [PubMed Link Image]
  45. Reardon W, Zhou XP, Eng C: A novel germline mutation of the PTEN gene in a patient with macrocephaly, ventricular dilatation, and features of VATER association. J Med Genet. 2001 Dec;38(12):820-3. [PubMed Link Image]
  46. Marsh DJ, Theodosopoulos G, Howell V, Richardson AL, Benn DE, Proos AL, Eng C, Robinson BG: Rapid mutation scanning of genes associated with familial cancer syndromes using denaturing high-performance liquid chromatography. Neoplasia. 2001 May-Jun;3(3):236-44. [PubMed Link Image]
  47. Staal FJ, van der Luijt RB, Baert MR, van Drunen J, van Bakel H, Peters E, de Valk I, van Amstel HK, Taphoorn MJ, Jansen GH, van Veelen CW, Burgering B, Staal GE: A novel germline mutation of PTEN associated with brain tumours of multiple lineages. Br J Cancer. 2002 May 20;86(10):1586-91. [PubMed Link Image]
  48. Poetsch M, Lorenz G, Kleist B: Detection of new PTEN/MMAC1 mutations in head and neck squamous cell carcinomas with loss of chromosome 10. Cancer Genet Cytogenet. 2002 Jan 1;132(1):20-4. [PubMed Link Image]
  49. Smith JM, Kirk EP, Theodosopoulos G, Marshall GM, Walker J, Rogers M, Field M, Brereton JJ, Marsh DJ: Germline mutation of the tumour suppressor PTEN in Proteus syndrome. J Med Genet. 2002 Dec;39(12):937-40. [PubMed Link Image]
  50. Butler MG, Dasouki MJ, Zhou XP, Talebizadeh Z, Brown M, Takahashi TN, Miles JH, Wang CH, Stratton R, Pilarski R, Eng C: Subset of individuals with autism spectrum disorders and extreme macrocephaly associated with germline PTEN tumour suppressor gene mutations. J Med Genet. 2005 Apr;42(4):318-21. [PubMed Link Image]
  51. Balciuniene J, Feng N, Iyadurai K, Hirsch B, Charnas L, Bill BR, Easterday MC, Staaf J, Oseth L, Czapansky-Beilman D, Avramopoulos D, Thomas GH, Borg A, Valle D, Schimmenti LA, Selleck SB: Recurrent 10q22-q23 deletions: a genomic disorder on 10q associated with cognitive and behavioral abnormalities. Am J Hum Genet. 2007 May;80(5):938-47. Epub 2007 Mar 20. [PubMed Link Image]
  52. Tekin M, Hismi BO, Fitoz S, Yalcinkaya F, Ekim M, Kansu A, Ertem M, Deda G, Tutar E, Arsan S, Zhou XP, Pilarski R, Eng C, Akar N: A germline PTEN mutation with manifestations of prenatal onset and verrucous epidermal nevus. Am J Med Genet A. 2006 Jul 1;140(13):1472-5. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 7009
Enzyme 29 Name Phosphatidylinositol transfer protein beta isoform
Enzyme 29 Synonyms
  1. PI-TP-beta
  2. PtdIns transfer protein beta
  3. PtdInsTP beta
Enzyme 29 Gene Name PITPNB
Enzyme 29 Protein Sequence >Phosphatidylinositol transfer protein beta isoform
MVLIKEFRVVLPCSVQEYQVGQLYSVAEASKNETGGGEGIEVLKNEPYEKDGEKGQYTHK
IYHLKSKVPAFVRMIAPEGSLVFHEKAWNAYPYCRTIVTNEYMKDDFFIKIETWHKPDLG
TLENVHGLDPNTWKTVEIVHIDIADRSQVEPADYKADEDPALFQSVKTKRGPLGPNWKKE
LANSPDCPQMCAYKLVTIKFKWWGLQSKVENFIQKQEKRIFTNFHRQLFCWIDKWIDLTM
EDIRRMEDETQKELETMRKRGSVRGTSAADV
Enzyme 29 Number of Residues 271
Enzyme 29 Molecular Weight 31539.9
Enzyme 29 Theoretical pI 6.87
Enzyme 29 GO Classification
Function
Process
  • establishment of localization
  • transport
Component
  • cell part
  • intracellular
Enzyme 29 General Function Involved in transport
Enzyme 29 Specific Function Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 6572213 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P48739 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name PIPNB_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >816 bp
ATGGTGCTGATCAAGGAATTCCGTGTGGTTTTGCCATGTTCTGTTCAGGAGTATCAGGTT
GGGCAGCTTTACTCTGTTGCAGAAGCTAGTAAGAATGAGACTGGTGGTGGAGAAGGAATT
GAAGTCTTAAAGAATGAACCTTATGAGAAGGATGGAGAAAAGGGACAGTATACGCACAAA
ATTTATCACCTAAAGAGCAAAGTGCCTGCATTCGTGAGGATGATTGCTCCCGAGGGCTCC
TTGGTGTTTCATGAGAAAGCCTGGAATGCGTACCCCTACTGTAGAACAATTGTAACGAAT
GAATATATGAAAGATGATTTCTTCATTAAAATCGAAACATGGCACAAACCAGACTTGGGA
ACATTAGAAAATGTACATGGTTTAGATCCAAACACATGGAAAACTGTTGAAATTGTCCAT
ATAGATATTGCAGATAGAAGTCAAGTTGAACCAGCAGACTACAAAGCTGATGAAGACCCA
GCATTATTCCAGTCAGTCAAGACCAAGAGAGGCCCTTTGGGACCCAACTGGAAGAAGGAG
CTGGCAAACAGCCCTGACTGTCCCCAGATGTGTGCCTATAAGCTGGTGACCATCAAATTC
AAGTGGTGGGGACTGCAAAGCAAAGTAGAAAACTTCATTCAAAAGCAAGAAAAACGGATA
TTTACAAACTTCCATCGCCAGCTTTTTTGTTGGATTGACAAGTGGATCGATCTCACGATG
GAAGACATTAGGAGAATGGAAGACGAGACTCAGAAAGAACTAGAAACAATGCGTAAGAGG
GGTTCCGTTCGAGGCACGTCGGCTGCTGATGTCTAG
Enzyme 29 GenBank Gene ID AL031591 Link Image
Enzyme 29 GeneCard ID PITPNB Link Image
Enzyme 29 GenAtlas ID PITPNB Link Image
Enzyme 29 HGNC ID HGNC:9002 Link Image
Enzyme 29 Chromosome Location 2
Enzyme 29 Locus 22q12.1
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Tanaka S, Yamashita S, Hosaka K: Cloning and expression of human cDNA encoding phosphatidylinositol transfer protein beta. Biochim Biophys Acta. 1995 Dec 7;1259(3):199-202. [PubMed Link Image]
  2. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  3. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  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. 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]
  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 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 7222
Enzyme 30 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-2
Enzyme 30 Synonyms
  1. Phosphoinositide phospholipase C-eta-2
  2. Phosphoinositide phospholipase C-like 4
  3. PLC-L4
  4. Phospholipase C-like protein 4
  5. Phospholipase C-eta-2
  6. PLC-eta2
Enzyme 30 Gene Name PLCH2
Enzyme 30 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-2
MSGPWPSPDSRTKGTVAWLAEVLLWVGGSVVLSSEWQLGPLVERCMGAMQEGMQMVKLRG
GSKGLVRFYYLDEHRSCIRWRPSRKNEKAKISIDSIQEVSEGRQSEVFQRYPDGSFDPNC
CFSIYHGSHRESLDLVSTSSEVARTWVTGLRYLMAGISDEDSLARRQRTRDQWLKQTFDE
ADKNGDGSLSIGEVLQLLHKLNVNLPRQRVKQMFREADTDDHQGTLGFEEFCAFYKMMST
RRDLYLLMLTYSNHKDHLDAASLQRFLQVEQKMAGVTLESCQDIIEQFEPCPENKSKGLL
GIDGFTNYTRSPAGDIFNPEHHHVHQDMTQPLSHYFITSSHNTYLVGDQLMSQSRVDMYA
WVLQAGCRCVEVDCWDGPDGEPIVHHGYTLTSKILFKDVIETINKYAFIKNEYPVILSIE
NHCSVIQQKKMAQYLTDILGDKLDLSSVSSEDATTLPSPQMLKGKILVKGKKLPANISED
AEEGEVSDEDSADEIDDDCKLLNGDASTNRKRVENTAKRKLDSLIKESKIRDCEDPNNFS
VSTLSPSGKLGRKSKAEEDVESGEDAGASRRNGRLVVGSFSRRKKKGSKLKKAASVEEGD
EGQDSPGGQSRGATRQKKTMKLSRALSDLVKYTKSVATHDIEMEAASSWQVSSFSETKAH
QILQQKPAQYLRFNQQQLSRIYPSSYRVDSSNYNPQPFWNAGCQMVALNYQSEGRMLQLN
RAKFSANGGCGYVLKPGCMCQGVFNPNSEDPLPGQLKKQLVLRIISGQQLPKPRDSMLGD
RGEIIDPFVEVEIIGLPVDCSREQTRVVDDNGFNPTWEETLVFMVHMPEIALVRFLVWDH
DPIGRDFIGQRTLAFSSMMPGYRHVYLEGMEEASIFVHVAVSDISGKVKQALGLKGLFLR
GPKPGSLDSHAAGRPPARPSVSQRILRRTASAPTKSQKPGRRGFPELVLGTRDTGSKGVA
DDVVPPGPGPAPEAPAQEGPGSGSPRDTRPLSTQRPLPPLCSLETIAEEPAPGPGPPPPA
AVPTSSSQGRPPYPTGPGANVASPLEDTEEPRDSRPRPCNGEGAGGAYERAPGSQTDGRS
QPRTLGHLPVIRRVKSEGQVPTEPLGGWRPLAAPFPAPAVYSDATGSDPLWQRLEPCGHR
DSVSSSSSMSSSDTVIDLSLPSLGLGRSRENLAGAHMGRLPPRPHSASAARPDLPPVTKS
KSNPNLRATGQRPPIPDELQPRSLAPRMAGLPFRPPWGCLSLVGVQDCPVAAKSKSLGDL
TADDFAPSFEGGSRRLSHSLGLPGGTRRVSGPGVRRDTLTEQLRWLTVFQQAGDITSPTS
LGPAGEGVAGGPGFVRRSSSRSHSRVRAIASRARQAQERQQRLQGLGRQGPPEEERGTPE
GACSVGHEGSVDAPAPSKGALGPASAAAENLVLLRL
Enzyme 30 Number of Residues 1416
Enzyme 30 Molecular Weight 154667.0
Enzyme 30 Theoretical pI 7.89
Enzyme 30 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 30 General Function Involved in calcium ion binding
Enzyme 30 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This phospholipase activity is very sensitive to calcium. May be important for formation and maintenance of the neuronal network in the postnatal brain
Enzyme 30 Pathways
Enzyme 30 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein Not Available
Enzyme 30 UniProtKB/Swiss-Prot ID O75038 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name PLCH2_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >4251 bp
ATGTCTGGTCCATGGCCCTCCCCCGACAGCCGGACCAAGGGAACGGTGGCCTGGCTGGCG
GAGGTACTCCTCTGGGTTGGAGGGAGTGTGGTGCTGTCTTCAGAGTGGCAGCTCGGCCCC
CTGGTGGAGCGGTGCATGGGTGCCATGCAAGAGGGGATGCAGATGGTGAAGCTGCGTGGC
GGCTCCAAGGGCCTGGTCCGCTTCTACTACCTGGACGAGCACCGCTCCTGCATCCGCTGG
AGGCCCTCACGCAAGAACGAGAAGGCCAAGATCTCCATCGACTCCATCCAGGAGGTGAGT
GAGGGGCGGCAGTCGGAGGTCTTCCAGCGCTACCCTGACGGCAGCTTCGACCCCAACTGC
TGCTTCAGCATCTACCACGGCAGCCACCGCGAGTCGCTGGACCTGGTCTCCACCAGCAGC
GAGGTGGCGCGCACCTGGGTCACTGGCCTGCGCTACCTCATGGCCGGCATCAGCGACGAG
GACAGCCTGGCTCGCCGCCAGCGCACCAGGGACCAGTGGCTGAAGCAGACGTTTGACGAG
GCCGACAAGAACGGGGATGGCAGCCTGAGCATTGGCGAGGTCCTGCAGCTGCTGCACAAG
CTCAACGTGAACCTGCCCCGGCAGAGGGTGAAGCAGATGTTCAGGGAAGCGGACACGGAT
GACCACCAAGGGACGCTGGGTTTTGAAGAGTTCTGTGCCTTCTACAAGATGATGTCCACC
CGCCGGGACCTCTACCTGCTCATGCTGACCTACAGCAACCACAAGGACCACCTGGATGCC
GCCAGCCTGCAGCGCTTCCTGCAGGTGGAGCAGAAGATGGCGGGTGTGACCCTCGAGAGC
TGCCAGGACATCATCGAGCAGTTTGAGCCATGCCCAGAAAACAAGAGTAAGGGGCTGCTG
GGCATTGATGGCTTCACCAACTACACCAGGAGCCCTGCTGGTGACATCTTCAACCCTGAG
CACCACCATGTGCACCAGGACATGACGCAGCCGCTGAGCCACTACTTCATCACCTCGTCC
CACAACACCTACCTCGTGGGTGACCAGCTCATGTCCCAGTCACGGGTGGACATGTATGCT
TGGGTCCTGCAGGCTGGCTGCCGCTGCGTGGAGGTGGACTGCTGGGATGGGCCCGACGGG
GAGCCCATTGTGCACCATGGCTACACTCTGACTTCCAAGATCCTCTTCAAAGACGTCATT
GAAACCATCAACAAATATGCCTTCATCAAGAATGAGTACCCAGTGATCCTGTCCATCGAA
AACCACTGCAGTGTCATCCAGCAGAAGAAAATGGCCCAGTATCTGACTGACATCCTTGGG
GACAAGCTGGACCTGTCATCAGTGAGCAGTGAAGATGCCACCACACTCCCCTCTCCACAG
ATGCTCAAGGGCAAGATCCTCGTGAAGGGGAAGAAGCTCCCAGCCAACATCAGCGAGGAT
GCGGAGGAAGGCGAGGTGTCTGATGAGGACAGTGCTGATGAGATTGACGATGACTGCAAG
CTCCTCAATGGGGATGCATCCACCAATCGAAAGCGTGTAGAAAACACTGCTAAGAGGAAA
CTGGATTCCCTCATCAAAGAGTCGAAGATTCGGGACTGTGAGGACCCCAACAACTTCTCC
GTCTCCACACTGTCCCCATCTGGAAAGCTCGGACGCAAGAGCAAGGCTGAAGAGGACGTG
GAGTCTGGGGAGGATGCCGGGGCCAGCAGACGCAATGGCCGCCTCGTCGTGGGAAGCTTC
TCCAGGCGCAAGAAGAAGGGCAGCAAGCTGAAGAAGGCGGCCAGCGTGGAGGAGGGAGAT
GAGGGTCAGGACTCCCCGGGAGGCCAGAGCCGAGGGGCGACCCGGCAGAAGAAGACCATG
AAGCTGTCCCGGGCCCTCTCTGACCTGGTGAAGTACACCAAGTCCGTGGCCACCCACGAC
ATAGAGATGGAGGCGGCGTCCAGCTGGCAGGTGTCGTCCTTCAGCGAGACCAAGGCCCAC
CAGATTCTGCAGCAGAAGCCGGCGCAGTACCTACGCTTCAACCAGCAGCAGCTCTCCCGC
ATCTACCCCTCCTCCTACCGTGTGGACTCCAGCAACTACAACCCGCAGCCCTTCTGGAAC
GCCGGCTGCCAAATGGTTGCCCTGAACTACCAGTCAGAGGGGCGGATGCTGCAGCTGAAC
CGAGCCAAGTTCAGCGCCAACGGTGGCTGCGGCTACGTACTCAAGCCTGGGTGCATGTGC
CAGGGCGTGTTCAACCCCAACTCGGAGGACCCCCTGCCCGGGCAGCTCAAGAAGCAGCTG
GTGCTCCGGATCATCAGTGGCCAGCAGCTTCCCAAGCCGCGCGACTCCATGCTGGGGGAC
CGTGGGGAGATCATCGACCCCTTTGTGGAGGTGGAGATCATTGGGCTCCCTGTGGACTGC
AGCAGGGAGCAGACCCGCGTGGTGGACGACAACGGGTTCAACCCCACCTGGGAGGAGACC
CTGGTTTTCATGGTGCACATGCCGGAGATCGCGCTGGTCCGCTTCCTCGTCTGGGACCAC
GATCCCATTGGGCGTGACTTCATTGGCCAGAGGACGCTGGCCTTCAGCAGCATGATGCCA
GGCTACAGACACGTGTACCTAGAAGGGATGGAAGAGGCCTCCATCTTCGTGCATGTGGCT
GTCAGTGACATCAGCGGTAAGGTCAAGCAGGCTCTGGGCCTAAAAGGCCTCTTCCTCCGA
GGCCCAAAGCCCGGCTCGCTGGACAGTCATGCTGCTGGGCGGCCCCCGGCCCGGCCCTCC
GTTAGCCAGCGGATCCTGCGGCGCACGGCCAGCGCCCCGACCAAGAGCCAGAAGCCGGGC
CGCAGGGGCTTCCCGGAGCTGGTCCTGGGTACACGGGACACAGGCTCCAAGGGGGTGGCA
GACGATGTGGTGCCCCCCGGGCCCGGACCTGCTCCGGAAGCCCCAGCCCAGGAGGGGCCC
GGCAGCGGCAGCCCCCGAGACACCCGCCCCCTCTCCACGCAGCGGCCACTCCCCCCACTG
TGCAGCCTGGAAACCATCGCTGAGGAGCCCGCCCCAGGCCCTGGTCCCCCGCCACCAGCG
GCTGTCCCCACCAGCTCTTCTCAGGGACGGCCCCCATACCCCACAGGACCCGGAGCCAAT
GTGGCAAGCCCCCTAGAGGACACTGAGGAGCCCCGAGACAGCAGGCCTCGGCCGTGCAAC
GGCGAGGGCGCCGGCGGGGCATACGAGAGGGCCCCCGGCAGCCAGACGGACGGCAGGAGC
CAGCCCCGGACCCTGGGCCACCTGCCCGTGATTAGAAGGGTGAAGAGTGAGGGGCAGGTG
CCCACGGAGCCCCTGGGAGGGTGGCGGCCCCTGGCCGCTCCCTTTCCAGCTCCTGCCGTG
TACTCCGATGCCACGGGCAGTGACCCGCTGTGGCAGCGGCTGGAGCCATGTGGCCACCGA
GACAGCGTTTCCTCCTCCTCCAGCATGTCATCCAGCGACACTGTCATTGACCTCTCCCTG
CCCAGCCTGGGCCTGGGCCGCAGCCGTGAGAACCTCGCTGGAGCCCACATGGGACGCCTG
CCCCCCAGGCCCCACTCGGCTTCGGCTGCCCGCCCAGACCTGCCACCTGTGACCAAGAGC
AAATCCAACCCCAACCTTCGGGCTACAGGCCAGCGGCCTCCCATACCTGACGAACTGCAG
CCCAGGTCCCTGGCCCCAAGGATGGCTGGCCTCCCCTTCCGGCCTCCCTGGGGCTGCCTT
TCCCTGGTGGGCGTGCAGGACTGCCCCGTGGCTGCCAAGTCCAAGAGCCTGGGCGACCTC
ACTGCTGATGACTTTGCCCCTAGCTTTGAGGGCGGCTCCCGCAGACTGAGCCACAGCCTG
GGCCTCCCGGGAGGGACACGGCGGGTGTCGGGGCCAGGGGTGAGACGGGACACCCTGACA
GAGCAGCTGCGCTGGCTCACTGTCTTCCAGCAGGCAGGAGACATCACGTCACCCACCAGC
CTGGGCCCGGCTGGGGAGGGGGTGGCAGGGGGCCCTGGTTTTGTGCGGCGCTCCTCCTCC
CGCAGCCACAGCCGCGTGCGTGCCATTGCCAGCCGGGCCCGCCAGGCCCAGGAGCGGCAG
CAGAGACTGCAGGGCCTGGGCCGGCAGGGACCCCCAGAAGAGGAGCGGGGCACCCCCGAG
GGCGCCTGCTCCGTGGGCCACGAGGGCAGTGTGGATGCACCAGCACCCTCCAAGGGAGCC
CTCGGGCCAGCATCCGCGGCTGCTGAAAACCTGGTCCTGCTCCGCCTCTGA
Enzyme 30 GenBank Gene ID DQ176850 Link Image
Enzyme 30 GeneCard ID PLCH2 Link Image
Enzyme 30 GenAtlas ID PLCH2 Link Image
Enzyme 30 HGNC ID HGNC:29037 Link Image
Enzyme 30 Chromosome Location 1
Enzyme 30 Locus 1p36.32
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Zhou Y, Wing MR, Sondek J, Harden TK: Molecular cloning and characterization of PLC-eta2. Biochem J. 2005 Nov 1;391(Pt 3):667-76. [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. 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]
  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 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 7395
Enzyme 31 Name Phospholipid scramblase 1
Enzyme 31 Synonyms
  1. PL scramblase 1
  2. Ca(2+)-dependent phospholipid scramblase 1
  3. Erythrocyte phospholipid scramblase
  4. MmTRA1b
Enzyme 31 Gene Name PLSCR1
Enzyme 31 Protein Sequence >Phospholipid scramblase 1
MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAG
FPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVL
TGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLR
CSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCC
GDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLI
DFMFFESTGSQEQKSGVW
Enzyme 31 Number of Residues 318
Enzyme 31 Molecular Weight 35048.8
Enzyme 31 Theoretical pI 4.57
Enzyme 31 GO Classification Not Available
Enzyme 31 General Function Involved in calcium ion binding
Enzyme 31 Specific Function May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes. May contribute to cytokine-regulated cell proliferation and differentiation
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • 289-305
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 3510297 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID O15162 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name PLS1_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >957 bp
ATGGACAAACAAAACTCACAGATGAATGCTTCTCACCCGGAAACAAACTTGCCAGTTGGG
TATCCTCCTCAGTATCCACCGACAGCATTCCAAGGACCTCCAGGATATAGTGGCTACCCT
GGGCCCCAGGTCAGCTACCCACCCCCACCAGCCGGCCATTCAGGTCCTGGCCCAGCTGGC
TTTCCTGTCCCAAATCAGCCAGTGTATAATCAGCCAGTATATAATCAGCCAGTTGGAGCT
GCAGGGGTACCATGGATGCCAGCGCCACAGCCTCCATTAAACTGTCCACCTGGATTAGAA
TATTTAAGTCAGATAGATCAGATACTGATTCATCAGCAAATTGAACTTCTGGAAGTTTTA
ACAGGTTTTGAAACTAATAACAAATATGAAATTAAGAACAGCTTTGGACAGAGGGTTTAC
TTTGCAGCGGAAGATACTGATTGCTGTACCCGAAATTGCTGTGGGCCATCTAGACCTTTT
ACCTTGAGGATTATTGATAATATGGGTCAAGAAGTCATAACTCTGGAGAGACCACTAAGA
TGTAGCAGCTGTTGTTGTCCCTGCTGCCTTCAGGAGATAGAAATCCAAGCTCCTCCTGGT
GTACCAATAGGTTATGTTATTCAGACTTGGCACCCATGTCTACCAAAGTTTACAATTCAA
AATGAGAAAAGAGAGGATGTACTAAAAATAAGTGGTCCATGTGTTGTGTGCAGCTGTTGT
GGAGATGTTGATTTTGAGATTAAATCTCTTGATGAACAGTGTGTGGTTGGCAAAATTTCC
AAGCACTGGACTGGAATTTTGAGAGAGGCATTTACAGACGCTGATAACTTTGGAATCCAG
TTCCCTTTAGACCTTGATGTTAAAATGAAAGCTGTAATGATTGGTGCCTGTTTCCTCATT
GACTTCATGTTTTTTGAAAGCACTGGCAGCCAGGAACAAAAATCAGGAGTGTGGTAG
Enzyme 31 GenBank Gene ID AB006746 Link Image
Enzyme 31 GeneCard ID PLSCR1 Link Image
Enzyme 31 GenAtlas ID PLSCR1 Link Image
Enzyme 31 HGNC ID HGNC:9092 Link Image
Enzyme 31 Chromosome Location 3
Enzyme 31 Locus 3q23
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Zhou Q, Zhao J, Stout JG, Luhm RA, Wiedmer T, Sims PJ: Molecular cloning of human plasma membrane phospholipid scramblase. A protein mediating transbilayer movement of plasma membrane phospholipids. J Biol Chem. 1997 Jul 18;272(29):18240-4. [PubMed Link Image]
  2. Kasukabe T, Kobayashi H, Kaneko Y, Okabe-Kado J, Honma Y: Identity of human normal counterpart (MmTRA1b) of mouse leukemogenesis-associated gene (MmTRA1a) product as plasma membrane phospholipid scramblase and chromosome mapping of the human MmTRA1b/phospholipid scramblase gene. Biochem Biophys Res Commun. 1998 Aug 19;249(2):449-55. [PubMed Link Image]
  3. Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed Link Image]
  4. 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. Basse F, Stout JG, Sims PJ, Wiedmer T: Isolation of an erythrocyte membrane protein that mediates Ca2+-dependent transbilayer movement of phospholipid. J Biol Chem. 1996 Jul 19;271(29):17205-10. [PubMed Link Image]
  7. Frasch SC, Henson PM, Kailey JM, Richter DA, Janes MS, Fadok VA, Bratton DL: Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cdelta. J Biol Chem. 2000 Jul 28;275(30):23065-73. [PubMed Link Image]
  8. Sun J, Zhao J, Schwartz MA, Wang JY, Wiedmer T, Sims PJ: c-Abl tyrosine kinase binds and phosphorylates phospholipid scramblase 1. J Biol Chem. 2001 Aug 3;276(31):28984-90. Epub 2001 Jun 4. [PubMed Link Image]
  9. Zhao J, Zhou Q, Wiedmer T, Sims PJ: Palmitoylation of phospholipid scramblase is required for normal function in promoting Ca2+-activated transbilayer movement of membrane phospholipids. Biochemistry. 1998 May 5;37(18):6361-6. [PubMed Link Image]
  10. Zhou Q, Sims PJ, Wiedmer T: Identity of a conserved motif in phospholipid scramblase that is required for Ca2+-accelerated transbilayer movement of membrane phospholipids. Biochemistry. 1998 Feb 24;37(8):2356-60. [PubMed Link Image]
  11. Dong B, Zhou Q, Zhao J, Zhou A, Harty RN, Bose S, Banerjee A, Slee R, Guenther J, Williams BR, Wiedmer T, Sims PJ, Silverman RH: Phospholipid scramblase 1 potentiates the antiviral activity of interferon. J Virol. 2004 Sep;78(17):8983-93. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 7675
Enzyme 32 Name Phosphatidylserine synthase 1
Enzyme 32 Synonyms
  1. PSS-1
  2. PtdSer synthase 1
  3. Serine-exchange enzyme I
Enzyme 32 Gene Name PTDSS1
Enzyme 32 Protein Sequence >Phosphatidylserine synthase 1
MASCVGSRTLSKDDVNYKMHFRMINEQQVEDITIDFFYRPHTITLLSFTIVSLMYFAFTR
DDSVPEDNIWRGILSVIFFFLIISVLAFPNGPFTRPHPALWRMVFGLSVLYFLFLVFLLF
LNFEQVKSLMYWLDPNLRYATREADVMEYAVNCHVITWERIISHFDIFAFGHFWGWAMKA
LLIRSYGLCWTISITWELTELFFMHLLPNFAECWWDQVILDILLCNGGGIWLGMVVCRFL
EMRTYHWASFKDIHTTTGKIKRAVLQFTPASWTYVRWFDPKSSFQRVAGVYLFMIIWQLT
ELNTFFLKHIFVFQASHPLSWGRILFIGGITAPTVRQYYAYLTDTQCKRVGTQCWVFGVI
GFLEAIVCIKFGQDLFSKTQILYVVLWLLCVAFTTFLCLYGMIWYAEHYGHREKTYSECE
DGTYSPEISWHHRKGTKGSEDSPPKHAGNNESHSSRRRNRHSKSKVTNGVGKK
Enzyme 32 Number of Residues 473
Enzyme 32 Molecular Weight 55527.2
Enzyme 32 Theoretical pI 8.52
Enzyme 32 GO Classification
Function
Process
  • glycerophospholipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phosphatidylserine biosynthetic process
  • phosphatidylserine metabolic process
  • phospholipid metabolic process
Component
Enzyme 32 General Function Involved in phosphatidylserine biosynthetic process
Enzyme 32 Specific Function Catalyzes a base-exchange reaction in which the polar head group of phosphatidylcholine is replaced by L-serine
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • 36-56 73-93 103-123 161-181 187-207 217-237 287-307 310-330 356-376 384-404
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein Not Available
Enzyme 32 UniProtKB/Swiss-Prot ID P48651 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name PTSS1_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >1422 bp
ATGGCGTCCTGCGTGGGGAGCCGGACCCTAAGCAAGGATGATGTGAACTACAAAATGCAT
TTCCGGATGATCAACGAGCAGCAAGTGGAGGACATCACCATTGACTTCTTCTACCGGCCG
CATACCATCACCCTGCTCAGCTTCACCATCGTCAGCCTCATGTACTTCGCCTTTACCAGG
GATGACTCTGTTCCAGAAGACAACATCTGGAGAGGCATCCTCTCTGTTATTTTCTTCTTT
CTTATCATCAGTGTGTTAGCTTTCCCCAATGGTCCGTTCACTCGACCTCATCCAGCCTTA
TGGCGAATGGTTTTTGGACTCAGTGTGCTCTACTTCCTGTTCCTGGTATTCCTACTCTTC
CTGAATTTCGAGCAGGTTAAATCTCTAATGTATTGGCTAGATCCAAATCTTCGATACGCC
ACAAGGGAAGCAGATGTCATGGAGTATGCTGTGAACTGCCATGTGATCACCTGGGAGAGG
ATTATCAGCCACTTTGATATTTTTGCATTTGGACATTTCTGGGGCTGGGCCATGAAGGCC
TTGCTGATCCGTAGTTACGGTCTCTGCTGGACAATCAGTATTACCTGGGAGCTGACTGAG
CTCTTCTTCATGCATCTCCTCCCCAATTTTGCCGAGTGCTGGTGGGATCAAGTCATTCTG
GACATCCTGTTGTGCAATGGCGGTGGCATTTGGCTGGGCATGGTCGTTTGCCGGTTTTTA
GAGATGAGGACTTACCACTGGGCAAGCTTCAAGGACATTCATACCACCACCGGGAAGATC
AAGAGAGCTGTTCTGCAGTTCACTCCTGCTAGCTGGACCTATGTTCGATGGTTTGACCCC
AAATCTTCTTTTCAGAGAGTAGCTGGAGTGTACCTTTTCATGATCATCTGGCAGCTGACT
GAGTTGAATACCTTCTTCTTGAAGCATATCTTTGTGTTCCAAGCCAGTCATCCATTAAGT
TGGGGTAGAATTCTCTTTATTGGTGGCATCACAGCTCCCACAGTGAGACAGTACTACGCT
TACCTCACCGACACACAGTGCAAGCGCGTAGGAACACAATGCTGGGTGTTTGGGGTCATT
GGTTTCCTGGAGGCCATTGTTTGCATAAAATTTGGACAAGATCTCTTCTCTAAGACCCAA
ATACTCTATGTTGTGCTTTGGCTTCTTTGCGTGGCTTTCACCACTTTCCTCTGTCTGTAC
GGCATGATTTGGTATGCAGAACACTATGGTCACCGAGAAAAGACCTACTCGGAGTGTGAA
GATGGCACCTACAGTCCAGAGATCTCCTGGCATCACAGGAAAGGGACAAAAGGTTCTGAA
GACAGCCCACCCAAGCATGCAGGCAACAACGAAAGCCATTCTTCCAGGAGAAGGAATCGG
CATTCCAAGTCAAAAGTCACCAATGGCGTTGGAAAGAAATGA
Enzyme 32 GenBank Gene ID D14694 Link Image
Enzyme 32 GeneCard ID PTDSS1 Link Image
Enzyme 32 GenAtlas ID PTDSS1 Link Image
Enzyme 32 HGNC ID HGNC:9587 Link Image
Enzyme 32 Chromosome Location 8
Enzyme 32 Locus 8q22
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed Link Image]
  2. 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]
  3. 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]
  4. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  5. 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]
  6. 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]
  7. 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]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 7740
Enzyme 33 Name Phosphatidylserine decarboxylase proenzyme
Enzyme 33 Synonyms
  1. Phosphatidylserine decarboxylase alpha chain
  2. Phosphatidylserine decarboxylase beta chain
Enzyme 33 Gene Name PISD
Enzyme 33 Protein Sequence >Phosphatidylserine decarboxylase proenzyme
MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARKIHTAPART
MFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWEVALYKSVPTRLLS
RAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPV
CGLHSISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKN
QLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCH
NERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNRE
GVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL
Enzyme 33 Number of Residues 408
Enzyme 33 Molecular Weight 46572.2
Enzyme 33 Theoretical pI 9.80
Enzyme 33 GO Classification
Function
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
  • phosphatidylserine decarboxylase activity
Process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid biosynthetic process
  • phospholipid metabolic process
Component
Enzyme 33 General Function Involved in phosphatidylserine decarboxylase activity
Enzyme 33 Specific Function Phosphatidyl-L-serine = phosphatidylethanolamine + CO(2)
Enzyme 33 Pathways
Enzyme 33 Reactions
  • phosphatidyl-L-serine = phosphatidylethanolamine + CO2 [RN:R02055]
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 13489112 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q9UG56 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name PISD_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >1128 bp
ATGATGTGTCAGTCAGAGGCGCGGCAAGGACCAGAGCTCCGCGCGGCGAAATGGTTGCAC
TTCCCCCAGCTGGCCCTGAGGCGGAGGCTGGGGCAGCTGAGCTGCATGTCCAGACCCGCT
CTGAAACTGCGCTCCTGGCCCTTGACCGTCCTCTACTACCTCCTGCCCTTCGGCGCCCTC
AGACCGCTCAGCCGGGTGGGATGGAGGCCCGTAAGCAGGGTGGCTTTGTACAAGTCAGTG
CCAACGCGCTTGCTGTCACGGGCCTGGGGTCGCCTCAATCAGGTGGAGCTGCCACACTGG
CTGCGCAGGCCCGTCTACAGCCTGTACATCTGGACGTTTGGGGTGAACATGAAAGAGGCC
GCTGTGGAGGACCTGCATCACTACCGCAACCTCAGCGAGTTCTTCCGGCGCAAGCTGAAG
CCGCAGGCCCGGCCTGTCTGTGGCCTGCACAGCGTGATTAGCCCATCGGATGGAAGGATC
CTCAACTTTGGGCAGGTGAAGAACTGTGAGGTGGAGCAGGTAAAGGGGGTCACCTACTCC
CTGGAGTCGTTCCTGGGCCCGCGTATGTGCACAGAGGACCTGCCCTTCCCACCAGCCGCG
TCGTGTGACTCCTTCAAGAACCAGCTGGTCACCCGGGAAGGGAATGAGCTCTATCACTGT
GTCATCTACCTGGCCCCTGGGGACTACCACTGCTTCCACTCCCCCACCGACTGGACTGTG
TCCCACCGGCGCCACTTCCCAGGCTCCCTGATGTCAGTGAACCCTGGCATGGCTCGCTGG
ATCAAAGAGCTCTTCTGCCATAACGAGCGGGTGGTCCTGACGGGGGACTGGAAACATGGC
TTCTTCTCACTGACAGCTGTGGGGGCCACCAACGTGGGCTCCATTCGCATCTACTTTGAC
CGGGACCTGCACACAAACAGCCCAAGGCACAGCAAGGGCTCCTACAATGACTTCAGCTTC
GTGACGCACACCAATAGAGAGGGCGTCCCCATGCGTAAGGGCGAGCACCTGGGCGAGTTC
AACCTGGGCTCCACCATCGTGCTCATCTTCGAGGCCCCCAAGGACTTCAATTTCCAGCTG
AAAACAGGACAGAAAATCCGCTTTGGGGAAGCCCTGGGCTCGCTCTAG
Enzyme 33 GenBank Gene ID NM_014338 Link Image
Enzyme 33 GeneCard ID PISD Link Image
Enzyme 33 GenAtlas ID PISD Link Image
Enzyme 33 HGNC ID HGNC:8999 Link Image
Enzyme 33 Chromosome Location 2
Enzyme 33 Locus 22q12.2
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  2. 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]
  3. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  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 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 8021
Enzyme 34 Name Phosphatidylinositol transfer protein alpha isoform
Enzyme 34 Synonyms
  1. PI-TP-alpha
  2. PtdIns transfer protein alpha
  3. PtdInsTP alpha
Enzyme 34 Gene Name PITPNA
Enzyme 34 Protein Sequence >Phosphatidylinositol transfer protein alpha isoform
MVLLKEYRVILPVSVDEYQVGQLYSVAEASKNETGGGEGVEVLVNEPYEKDGEKGQYTHK
IYHLQSKVPTFVRMLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLG
TQENVHKLEPEAWKHVEAVYIDIADRSQVLSKDYKAEEDPAKFKSIKTGRGPLGPNWKQE
LVNQKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQERRLFTNFHRQLFCWLDKWVDLTM
DDIRRMEEETKRQLDEMRQKDPVKGMTADD
Enzyme 34 Number of Residues 270
Enzyme 34 Molecular Weight 31806.2
Enzyme 34 Theoretical pI 6.52
Enzyme 34 GO Classification
Function
Process
  • establishment of localization
  • transport
Component
  • cell part
  • intracellular
Enzyme 34 General Function Involved in phosphatidylcholine transmembrane transport
Enzyme 34 Specific Function Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions Not Available
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 28175608 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q00169 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name PIPNA_HUMAN Link Image
Enzyme 34 PDB ID 1T27 Link Image
Enzyme 34 PDB File Show
Enzyme 34 3D Structure
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >813 bp
ATGGTGCTGCTCAAGGAGTATCGAGTAATCCTGCCTGTGTCTGTAGATGAGTATCAAGTG
GGGCAGCTGTATTCTGTGGCTGAGGCCAGTAAAAATGAAACGGGTGGTGGCGAAGGCGTG
GAGGTCCTGGTGAATGAGCCCTACGAGAAGGACGGTGAGAAAGGCCAGTACACACATAAG
ATCTACCACCTGCAGAGCAAAGTACCCACGTTTGTTCGAATGCTGGCCCCAGAGGGAGCC
CTGAATATACACGAGAAAGCCTGGAATGCTTACCCCTACTGCAGAACCGTTATTACAAAT
GAGTACATGAAAGAAGACTTTCTGATTAAAATTGAAACCTGGCACAAACCAGATCTTGGC
ACGCAGGAGAATGTGCATAAGCTGGAGCCTGAGGCGTGGAAACACGTGGAAGCCGTATAT
ATAGACATTGCAGATCGAAGCCAAGTGCTCAGCAAGGATTACAAGGCAGAGGAAGACCCA
GCAAAATTTAAATCTATCAAAACAGGCCGAGGACCCTTGGGCCCCAATTGGAAGCAAGAG
CTTGTAAACCAGAAGGACTGCCCATATATGTGTGCATACAAACTGGTGACCGTCAAGTTC
AAGTGGTGGGGCCTGCAGAACAAAGTGGAGAACTTCATCCATAAGCAAGAGAGGCGTCTG
TTTACAAACTTCCACAGGCAGCTGTTCTGTTGGCTCGATAAGTGGGTTGACCTGACCATG
GACGACATTCGAAGGATGGAAGAAGAGACGAAGAGACAGCTGGATGAAATGAGACAAAAG
GACCCAGTGAAAGGAATGACAGCAGATGACTAA
Enzyme 34 GenBank Gene ID BC045108 Link Image
Enzyme 34 GeneCard ID PITPNA Link Image
Enzyme 34 GenAtlas ID Not Available
Enzyme 34 HGNC ID Not Available
Enzyme 34 Chromosome Location 1
Enzyme 34 Locus 17p13.3
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Dickeson SK, Helmkamp GM Jr, Yarbrough LR: Sequence of a human cDNA encoding phosphatidylinositol transfer protein and occurrence of a related sequence in widely divergent eukaryotes. Gene. 1994 May 16;142(2):301-5. [PubMed Link Image]
  2. 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]
  3. 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]
  4. 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 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 8048
Enzyme 35 Name Phospholipid transfer protein
Enzyme 35 Synonyms
  1. Lipid transfer protein II
Enzyme 35 Gene Name PLTP
Enzyme 35 Protein Sequence >Phospholipid transfer protein
MALFGALFLALLAGAHAEFPGCKIRVTSKALELVKQEGLRFLEQELETITIPDLRGKEGH
FYYNISEVKVTELQLTSSELDFQPQQELMLQITNASLGLRFRRQLLYWFFYDGGYINASA
EGVSIRTGLELSRDPAGRMKVSNVSCQASVSRMHAAFGGTFKKVYDFLSTFITSGMRFLL
NQQICPVLYHAGTVLLNSLLDTVPVRSSVDELVGIDYSLMKDPVASTSNLDMDFRGAFFP
LTERNWSLPNRAVEPQLQEEERMVYVAFSEFFFDSAMESYFRAGALQLLLVGDKVPHDLD
MLLRATYFGSIVLLSPAVIDSPLKLELRVLAPPRCTIKPSGTTISVTASVTIALVPPDQP
EVQLSSMTMDARLSAKMALRGKALRTQLDLRRFRIYSNHSALESLALIPLQAPLKTMLQI
GVMPMLNERTWRGVQIPLPEGINFVHEVVTNHAGFLTIGADLHFAKGLREVIEKNRPADV
RASTAPTPSTAAV
Enzyme 35 Number of Residues 493
Enzyme 35 Molecular Weight 54738.8
Enzyme 35 Theoretical pI 7.01
Enzyme 35 GO Classification
Function
  • binding
  • lipid binding
Process
Component
Enzyme 35 General Function Involved in lipid binding
Enzyme 35 Specific Function Converts HDL into larger and smaller particles. May play a key role in extracellular phospholipid transport and modulation of hdl particles
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • 1-17
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 18143452 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID P55058 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name PLTP_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >1482 bp
ATGGCCCTCTTCGGGGCCCTCTTCCTAGCGCTGCTGGCAGGCGCACATGCAGAGTTCCCA
GGCTGCAAGATCCGCGTCACCTCCAAGGCGCTGGAGCTGGTGAAGCAGGAGGGGCTGCGC
TTTCTGGAGCAAGAGCTGGAGACTATCACCATTCCGGACCTGCGGGGCAAAGAAGGCCAC
TTCTACTACAACATCTCTGAGGTGAAGGTCACAGAGCTGCAACTGACATCTTCCGAGCTC
GATTTCCAGCCACAGCAGGAGCTGATGCTTCAAATCACCAATGCCTCCTTGGGGCTGCGC
TTCCGGAGACAGCTGCTCTACTGGTTCTTCTATGATGGGGGCTACATCAACGCCTCAGCT
GAGGGTGTGTCCATCCGCACTGGTCTGGAGCTCTCCCGGGATCCCGCTGGACGGATGAAA
GTGTCCAATGTCTCCTGCCAGGCCTCTGTCTCCAGAATGCACGCGGCCTTCGGGGGAACC
TTCAAGAAGGTGTATGATTTTCTCTCCACGTTCATCACCTCAGGGATGCGCTTCCTCCTC
AACCAGCAGATCTGCCCTGTCCTCTACCACGCAGGGACGGTCCTGCTCAACTCCCTCCTG
GACACCGTGCCTGTGCGCAGTTCTGTGGACGAGCTTGTTGGCATTGACTATTCCCTCATG
AAGGATCCTGTGGCTTCCACCAGCAACCTGGACATGGACTTCCGGGGGGCCTTCTTCCCC
CTGACTGAGAGGAACTGGAGCCTCCCCAACCGGGCAGTGGAGCCCCAGCTGCAGGAGGAA
GAGCGGATGGTGTATGTGGCCTTCTCTGAGTTCTTCTTCGACTCTGCCATGGAGAGCTAC
TTCCGGGCGGGGGCCCTGCAGCTGTTGCTGGTGGGGGACAAGGTGCCCCACGACCTGGAC
ATGCTGCTGAGGGCCACCTACTTTGGGAGCATTGTCCTGCTGAGCCCAGCAGTGATTGAC
TCCCCATTGAAGCTGGAGCTGCGGGTCCTGGCCCCACCGCGCTGCACCATCAAGCCCTCT
GGCACCACCATCTCTGTCACTGCTAGCGTCACCATTGCCCTGGTCCCACCAGACCAGCCT
GAGGTCCAGCTGTCCAGCATGACTATGGACGCCCGTCTCAGCGCCAAGATGGCTCTCCGG
GGGAAGGCCCTGCGCACGCAGCTGGACCTGCGCAGGTTCCGAATCTATTCCAACCATTCT
GCACTGGAGTCGCTGGCTCTGATCCCATTACAGGCCCCTCTGAAGACCATGCTGCAGATT
GGGGTGATGCCCATGCTCAATGAGCGGACCTGGCGTGGGGTGCAGATCCCACTACCTGAG
GGCATCAACTTTGTGCATGAGGTGGTGACGAACCATGCGGGATTCCTCACCATCGGGGCT
GATCTCCACTTTGCCAAAGGGCTGCGAGAGGTGATTGAGAAGAACCGGCCTGCTGATGTC
AGGGCGTCCACTGCCCCCACACCGTCCACAGCAGCTGTCTGA
Enzyme 35 GenBank Gene ID AB076694 Link Image
Enzyme 35 GeneCard ID PLTP Link Image
Enzyme 35 GenAtlas ID PLTP Link Image
Enzyme 35 HGNC ID HGNC:9093 Link Image
Enzyme 35 Chromosome Location 2
Enzyme 35 Locus 20q13.12
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Day JR, Albers JJ, Lofton-Day CE, Gilbert TL, Ching AF, Grant FJ, O'Hara PJ, Marcovina SM, Adolphson JL: Complete cDNA encoding human phospholipid transfer protein from human endothelial cells. J Biol Chem. 1994 Mar 25;269(12):9388-91. [PubMed Link Image]
  2. 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. Qu SJ, Fan HZ, Kilinc C, Pownall HJ: Role of cysteine residues in human plasma phospholipid transfer protein. J Protein Chem. 1999 Feb;18(2):193-8. [PubMed Link Image]
  6. 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]
  7. 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]
  8. 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]
  9. Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 8469
Enzyme 36 Name GPI mannosyltransferase 1
Enzyme 36 Synonyms
  1. GPI mannosyltransferase I
  2. GPI-MT-I
  3. Phosphatidylinositol-glycan biosynthesis class M protein
  4. PIG-M
Enzyme 36 Gene Name PIGM
Enzyme 36 Protein Sequence >GPI mannosyltransferase 1
MGSTKHWGEWLLNLKVAPAGVFGVAFLARVALVFYGVFQDRTLHVRYTDIDYQVFTDAAR
FVTEGRSPYLRATYRYTPLLGWLLTPNIYLSELFGKFLFISCDLLTAFLLYRLLLLKGLG
RRQACGYCVFWLLNPLPMAVSSRGNADSIVASLVLMVLYLIKKRLVACAAVFYGFAVHMK
IYPVTYILPITLHLLPDRDNDKSLRQFRYTFQACLYELLKRLCNRAVLLFVAVAGLTFFA
LSFGFYYEYGWEFLEHTYFYHLTRRDIRHNFSPYFYMLYLTAESKWSFSLGIAAFLPQLI
LLSAVSFAYYRDLVFCCFLHTSIFVTFNKVCTSQYFLWYLCLLPLVMPLVRMPWKRAVVL
LMLWFIGQAMWLAPAYVLEFQGKNTFLFIWLAGLFFLLINCSILIQIISHYKEEPLTERI
KYD
Enzyme 36 Number of Residues 423
Enzyme 36 Molecular Weight 49459.2
Enzyme 36 Theoretical pI 9.31
Enzyme 36 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
  • organelle membrane
Enzyme 36 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 36 Specific Function Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • 18-38 80-100 139-161 170-190 226-246 288-308 315-337 339-350 358-378 385-405
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 11414879 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q9H3S5 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name PIGM_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >1272 bp
ATGGGCTCCACCAAGCACTGGGGCGAATGGCTCCTGAACTTGAAGGTGGCTCCAGCCGGC
GTCTTTGGTGTGGCCTTTCTAGCCAGAGTCGCCCTGGTTTTCTATGGCGTCTTCCAGGAC
CGGACCCTGCACGTGAGGTATACGGACATCGACTACCAGGTCTTCACCGACGCCGCGCGC
TTCGTCACGGAGGGGCGCTCGCCTTACCTGAGAGCCACGTACCGTTACACCCCGCTGCTG
GGTTGGCTCCTCACTCCCAACATCTACCTCAGCGAGCTCTTTGGAAAGTTTCTCTTCATC
AGCTGCGACCTCCTCACCGCTTTCCTCTTATACCGCCTGCTGCTGCTGAAGGGGCTGGGG
CGCCGCCAGGCTTGTGGCTACTGTGTCTTTTGGCTTCTTAACCCCCTGCCTATGGCAGTA
TCCAGCCGCGGTAATGCGGACTCTATTGTCGCCTCCCTGGTCCTGATGGTCCTCTACTTG
ATAAAGAAAAGACTCGTCGCGTGTGCAGCTGTATTCTATGGTTTCGCGGTGCATATGAAG
ATATATCCAGTGACTTACATCCTTCCCATAACCCTCCACCTGCTTCCAGATCGCGACAAT
GACAAAAGCCTCCGTCAATTCCGGTACACTTTCCAGGCTTGTTTGTACGAGCTCCTGAAA
AGGCTGTGTAATCGGGCTGTGCTGCTGTTTGTAGCAGTTGCTGGACTCACGTTTTTTGCC
CTGAGCTTTGGTTTTTACTATGAGTACGGCTGGGAATTTTTGGAACACACCTACTTTTAT
CACCTGACTAGGCGGGATATCCGTCACAACTTTTCTCCGTACTTCTACATGCTGTATTTG
ACTGCAGAGAGCAAGTGGAGTTTTTCCCTGGGAATTGCTGCATTCCTGCCACAGCTCATC
TTGCTTTCAGCTGTGTCTTTCGCCTATTACAGAGACCTCGTTTTTTGTTGTTTTCTTCAT
ACGTCCATTTTTGTGACTTTTAACAAAGTCTGCACCTCCCAGTACTTTCTTTGGTACCTC
TGCTTACTGCCTCTTGTGATGCCACTAGTCAGAATGCCTTGGAAAAGAGCTGTAGTTCTC
CTAATGTTATGGTTTATAGGGCAGGCCATGTGGCTGGCTCCTGCCTATGTTCTAGAGTTT
CAAGGAAAGAACACCTTTCTGTTTATTTGGTTAGCTGGTTTGTTCTTTCTTCTTATCAAT
TGTTCCATCCTGATTCAAATTATTTCCCATTACAAAGAAGAACCCCTGACAGAGAGAATC
AAATATGACTAG
Enzyme 36 GenBank Gene ID AB028127 Link Image
Enzyme 36 GeneCard ID PIGM Link Image
Enzyme 36 GenAtlas ID PIGM Link Image
Enzyme 36 HGNC ID HGNC:18858 Link Image
Enzyme 36 Chromosome Location 1
Enzyme 36 Locus 1q23.2
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Maeda Y, Watanabe R, Harris CL, Hong Y, Ohishi K, Kinoshita K, Kinoshita T: PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER. EMBO J. 2001 Jan 15;20(1-2):250-61. [PubMed Link Image]
  2. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed Link Image]
  3. 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]
  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. Almeida AM, Murakami Y, Layton DM, Hillmen P, Sellick GS, Maeda Y, Richards S, Patterson S, Kotsianidis I, Mollica L, Crawford DH, Baker A, Ferguson M, Roberts I, Houlston R, Kinoshita T, Karadimitris A: Hypomorphic promoter mutation in PIGM causes inherited glycosylphosphatidylinositol deficiency. Nat Med. 2006 Jul;12(7):846-51. Epub 2006 Jun 11. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 8475
Enzyme 37 Name Phosphatidylserine synthase 2
Enzyme 37 Synonyms
  1. PSS-2
  2. PtdSer synthase 2
  3. Serine-exchange enzyme II
Enzyme 37 Gene Name PTDSS2
Enzyme 37 Protein Sequence >Phosphatidylserine synthase 2
MRRGERRDAGGPRPESPVPAGRASLEEPPDGPSAGQATGPGEGRRSTESEVYDDGTNTFF
WRAHTLTVLFILTCTLGYVTLLEETPQDTAYNTKRGIVASILVFLCFGVTQAKDGPFSRP
HPAYWRFWLCVSVVYELFLIFILFQTVQDGRQFLKYVDPKLGVPLPERDYGGNCLIYDPD
NETDPFHNIWDKLDGFVPAHFLGWYLKTLMIRDWWMCMIISVMFEFLEYSLEHQLPNFSE
CWWDHWIMDVLVCNGLGIYCGMKTLEWLSLKTYKWQGLWNIPTYKGKMKRIAFQFTPYSW
VRFEWKPASSLRRWLAVCGIILVFLLAELNTFYLKFVLWMPPEHYLVLLRLVFFVNVGGV
AMREIYDFMDDPKPHKKLGPQAWLVAAITATELLIVVKYDPHTLTLSLPFYISQCWTLGS
VLALTWTVWRFFLRDITLRYKETRWQKWQNKDDQGSTVGNGDQHPLGLDEDLLGPGVAEG
EGAPTPN
Enzyme 37 Number of Residues 487
Enzyme 37 Molecular Weight 56252.5
Enzyme 37 Theoretical pI 6.19
Enzyme 37 GO Classification
Function
Process
  • glycerophospholipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phosphatidylserine biosynthetic process
  • phosphatidylserine metabolic process
  • phospholipid metabolic process
Component
Enzyme 37 General Function Involved in phosphatidylserine biosynthetic process
Enzyme 37 Specific Function Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine is replaced by L-serine
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions Not Available
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • 63-83 97-117 127-147 242-262 314-334 336-356 377-397 404-424
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 21740008 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q9BVG9 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name PTSS2_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >1464 bp
ATGCGGAGGGGCGAGCGCAGGGACGCCGGAGGTCCGCGGCCCGAGTCCCCGGTGCCCGCG
GGCAGGGCCTCGCTGGAGGAGCCGCCTGACGGGCCGTCTGCCGGCCAAGCCACCGGGCCG
GGCGAGGGCCGCCGCAGCACCGAGTCCGAGGTCTACGACGACGGCACCAACACCTTCTTC
TGGCGAGCCCACACCTTAACCGTGCTCTTCATCCTCACCTGTACGCTTGGCTATGTGACG
CTGCTGGAGGAAACACCTCAGGACACGGCCTACAACACCAAGAGAGGTATTGTGGCCAGT
ATTTTGGTTTTCTTATGTTTTGGAGTCACACAAGCTAAAGACGGGCCATTTTCCAGACCT
CATCCAGCTTACTGGAGGTTTTGGCTCTGCGTGAGTGTGGTCTACGAGCTGTTTCTCATC
TTTATACTCTTCCAGACTGTCCAGGACGGCCGGCAGTTTCTAAAGTATGTTGACCCCAAG
CTGGGAGTCCCACTGCCAGAGAGAGACTACGGGGGAAACTGCCTCATCTACGACCCAGAC
AATGAGACTGACCCCTTTCACAACATCTGGGACAAGTTGGATGGCTTTGTTCCCGCGCAC
TTTCTTGGCTGGTACCTGAAGACCCTGATGATCCGAGACTGGTGGATGTGCATGATCATC
AGCGTGATGTTCGAGTTCCTGGAGTACAGCCTGGAGCACCAGCTGCCCAACTTCAGCGAG
TGCTGGTGGGATCACTGGATCATGGACGTGCTCGTCTGCAACGGGCTGGGCATCTACTGC
GGCATGAAGACCCTTGAGTGGCTGTCCCTGAAGACGTACAAGTGGCAGGGCCTCTGGAAC
ATTCCGACCTACAAGGGCAAGATGAAGAGGATCGCCTTCCAGTTCACGCCGTACAGCTGG
GTTCGCTTCGAGTGGAAGCCGGCCTCCAGCCTGCGTCGCTGGCTGGCCGTGTGCGGCATC
ATCCTGGTGTTCCTGTTGGCAGAACTGAACACGTTCTACCTGAAGTTTGTGCTGTGGATG
CCCCCGGAGCACTACCTGGTCCTCCTGCGGCTCGTCTTCTTCGTGAACGTGGGTGGCGTG
GCCATGCGTGAGATCTACGACTTCATGGATGACCCGAAGCCCCACAAGAAGCTGGGCCCG
CAGGCCTGGCTGGTGGCGGCCATCACGGCCACGGAGCTGCTCATCGTGGTGAAGTACGAC
CCCCACACGCTCACCCTGTCCCTGCCCTTCTACATCTCCCAGTGCTGGACCCTCGGCTCC
GTCCTGGCGCTCACCTGGACCGTCTGGCGCTTCTTCCTGCGGGACATCACATTGAGGTAC
AAGGAGACCCGGTGGCAGAAGTGGCAGAACAAGGATGACCAGGGCAGCACCGTCGGCAAC
GGGGACCAGCACCCACTGGGGCTGGACGAAGACCTGCTGGGGCCTGGGGTGGCCGAGGGC
GAGGGAGCACCAACTCCAAACTGA
Enzyme 37 GenBank Gene ID AL834357 Link Image
Enzyme 37 GeneCard ID PTDSS2 Link Image
Enzyme 37 GenAtlas ID PTDSS2 Link Image
Enzyme 37 HGNC ID HGNC:15463 Link Image
Enzyme 37 Chromosome Location 1
Enzyme 37 Locus 11p15.5
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 8495
Enzyme 38 Name Phosphatidylinositol-glycan biosynthesis class W protein
Enzyme 38 Synonyms
  1. PIG-W
Enzyme 38 Gene Name PIGW
Enzyme 38 Protein Sequence >Phosphatidylinositol-glycan biosynthesis class W protein
MSEKQMKEAFVSNLNGTTVLEITQGLCFPAFCILCRGFLIIFSQYLCSFSPTWKTRFLTD
FVVLIVPMVATLTIWASFILLELLGVIIFGAGLLYQIYRRRTCYARLPFLKILEKFLNIS
LESEYNPAISCFRVITSAFTAIAILAVDFPLFPRRFAKTELYGTGAMDFGVGGFVFGSAM
VCLEVRRRKYMEGSKLHYFTNSLYSVWPLVFLGIGRLAIIKSIGYQEHLTEYGVHWNFFF
TIIVVKLITPLLLIIFPLNKSWIIALGITVLYQLALDFTSLKRLILYGTDGSGTRVGLLN
ANREGIISTLGYVAIHMAGVQTGLYMHKNRSHIKDLIKVACFLLLAAISLFISLYVVQVN
VEAVSRRMANLAFCIWIVASSLILLSSLLLGDIILSFAKFLIKGALVPCSWKLIQSPVTN
KKHSESLVPEAERMEPSLCLITALNRKQLIFFLLSNITTGLINLMVDTLHSSTLWALFVV
NLYMFSNCLIVYVLYLQDKTVQFW
Enzyme 38 Number of Residues 504
Enzyme 38 Molecular Weight 56881.3
Enzyme 38 Theoretical pI 9.44
Enzyme 38 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
  • organelle membrane
Enzyme 38 General Function Involved in transferase activity, transferring acyl groups
Enzyme 38 Specific Function Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI- anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually removed soon after the attachment of GPIs to proteins
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions Not Available
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • 22-42 74-94 132-152 163-183 203-223 238-258 261-281 306-326 339-359 371-391 449-469 474-494
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 31339065 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID Q7Z7B1 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name PIGW_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >1515 bp
ATGTCTGAAAAGCAGATGAAGGAAGCTTTTGTCAGTAACCTCAATGGAACCACCGTGCTG
GAAATCACCCAGGGATTGTGCTTTCCTGCATTCTGTATCCTGTGCAGAGGGTTCCTGATC
ATTTTCTCACAGTACTTGTGTTCTTTTTCACCTACCTGGAAAACTAGATTCCTCACTGAC
TTTGTTGTCCTAATAGTTCCCATGGTAGCCACTTTGACCATTTGGGCTTCATTTATCCTC
CTTGAGCTTCTCGGTGTAATTATCTTTGGGGCAGGGCTGTTGTATCAAATATACCGAAGG
AGGACCTGCTATGCCAGACTGCCTTTCCTAAAAATCCTTGAAAAATTCTTGAACATCAGT
CTAGAATCAGAATACAATCCAGCCATCTCCTGTTTCCGTGTAATTACCAGTGCGTTTACT
GCTATTGCTATTTTGGCTGTGGACTTCCCACTTTTTCCCAGAAGATTTGCCAAAACTGAG
CTCTATGGGACAGGAGCAATGGATTTTGGAGTAGGTGGCTTTGTTTTTGGGTCTGCAATG
GTTTGTCTAGAGGTCAGGAGGAGAAAATATATGGAAGGGTCCAAATTGCATTACTTTACA
AACTCATTGTACTCTGTTTGGCCATTAGTCTTCCTAGGAATCGGACGATTAGCCATTATA
AAATCAATAGGCTATCAGGAACATTTAACAGAGTATGGAGTTCACTGGAACTTTTTCTTT
ACCATAATAGTTGTGAAATTGATAACACCACTGCTGTTGATTATTTTTCCCCTAAATAAG
TCCTGGATTATTGCCCTCGGCATTACTGTATTATACCAGCTAGCCCTTGACTTTACCTCA
CTGAAGAGGTTAATATTATATGGCACTGATGGTAGTGGCACACGGGTTGGTCTATTAAAT
GCCAACCGCGAAGGAATAATCTCTACCCTGGGGTATGTGGCAATACACATGGCTGGTGTG
CAAACAGGGTTATATATGCATAAGAACCGATCACATATCAAAGACTTGATAAAAGTAGCC
TGTTTTCTTTTACTGGCAGCTATTAGCCTCTTCATATCTCTTTACGTAGTTCAAGTAAAT
GTAGAAGCAGTATCTCGAAGAATGGCAAATTTAGCCTTTTGTATTTGGATAGTTGCTTCT
AGCCTGATCCTTCTTAGTAGTTTATTACTGGGTGATATAATTTTGAGTTTTGCCAAATTT
CTAATTAAAGGAGCTCTAGTACCATGTTCTTGGAAACTTATCCAGTCACCTGTTACAAAT
AAAAAGCATTCAGAATCTCTAGTCCCTGAAGCCGAAAGAATGGAACCCAGTCTTTGTTTA
ATCACAGCTCTAAACAGAAAACAGTTAATATTTTTCTTGCTGTCAAATATAACAACTGGC
CTGATCAACCTGATGGTAGATACATTACACAGCAGTACCTTGTGGGCCTTATTTGTGGTC
AATCTCTATATGTTTTCCAACTGTTTAATTGTATATGTACTATATTTGCAAGATAAGACT
GTACAATTTTGGTGA
Enzyme 38 GenBank Gene ID AB097818 Link Image
Enzyme 38 GeneCard ID PIGW Link Image
Enzyme 38 GenAtlas ID PIGW Link Image
Enzyme 38 HGNC ID HGNC:23213 Link Image
Enzyme 38 Chromosome Location 1
Enzyme 38 Locus 17q12
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Murakami Y, Siripanyapinyo U, Hong Y, Kang JY, Ishihara S, Nakakuma H, Maeda Y, Kinoshita T: PIG-W is critical for inositol acylation but not for flipping of glycosylphosphatidylinositol-anchor. Mol Biol Cell. 2003 Oct;14(10):4285-95. Epub 2003 Jun 13. [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. 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 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 8621
Enzyme 39 Name Phosphatidylinositol-glycan biosynthesis class X protein
Enzyme 39 Synonyms
  1. PIG-X
Enzyme 39 Gene Name PIGX
Enzyme 39 Protein Sequence >Phosphatidylinositol-glycan biosynthesis class X protein
MAARVAAVRAAAWLLLGAATGLTRGPAAAFTAARSDAGIRAMCSEIILRQEVLKDGFHRD
LLIKVKFGESIEDLHTCRLLIKQDIPAGLYVDPYELASLRERNITEAVMVSENFDIEAPN
YLSKESEVLIYARRDSQCIDCFQAFLPVHCRYHRPHSEDGEASIVVNNPDLLMFCDQEFP
ILKCWAHSEVAAPCALENEDICQWNKMKYKSVYKNVILQVPVGLTVHTSLVCSVTLLITI
LCSTLILVAVFKYGHFSL
Enzyme 39 Number of Residues 258
Enzyme 39 Molecular Weight 28788.1
Enzyme 39 Theoretical pI 6.30
Enzyme 39 GO Classification
Function
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • membrane
  • organelle membrane
Enzyme 39 General Function Involved in GPI anchor biosynthetic process
Enzyme 39 Specific Function Essential component of glycosylphosphatidylinositol- mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the mannosyltransferase PIGM
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions Not Available
Enzyme 39 Pfam Domain Function Not Available
Enzyme 39 Signals
  • 1-21
Enzyme 39 Transmembrane Regions
  • 231-251
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 261490706 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q8TBF5 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name PIGX_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >777 bp
CTGGCGGCTCGGGTGGCGGCGGTTCGGGCGGCCGCCTGGCTGCTCCTCGGGGCGGCGACC
GGGCTCACGCGCGGGCCCGCCGCGGCCTTCACCGCCGCGCGCTCTGACGCCGGCATAAGG
GCCATGTGTTCTGAAATTATTTTGAGGCAAGAAGTTTTGAAAGATGGTTTCCACAGAGAC
CTTTTAATCAAAGTGAAGTTTGGGGAAAGCATTGAGGACTTGCACACCTGCCGTCTCTTA
ATTAAACAGGACATTCCTGCAGGACTTTATGTGGATCCGTATGAGTTGGCTTCATTACGA
GAGAGAAACATAACAGAGGCAGTGATGGTTTCAGAAAATTTTGATATAGAGGCCCCTAAC
TATTTGTCCAAGGAGTCTGAAGTTCTCATTTATGCCAGACGAGATTCACAGTGCATTGAC
TGTTTTCAAGCCTTTTTGCCTGTGCACTGCCGCTATCATCGGCCGCACAGTGAAGATGGA
GAAGCCTCGATTGTGGTCAATAACCCAGATTTGTTGATGTTTTGTGACCAAGAGTTCCCG
ATTTTGAAATGCTGGGCTCACTCAGAAGTGGCAGCCCCTTGTGCTTTGGAGAATGAGGAT
ATCTGCCAATGGAACAAGATGAAGTATAAATCAGTATATAAGAATGTGATTCTACAAGTT
CCAGTGGGACTGACTGTACATACCTCTCTAGTATGTTCTGTGACTCTGCTCATTACAATC
CTGTGCTCTACATTGATCCTTGTAGCAGTTTTCAAATATGGCCATTTTTCCCTATAA
Enzyme 39 GenBank Gene ID NM_017861.3 Link Image
Enzyme 39 GeneCard ID PIGX Link Image
Enzyme 39 GenAtlas ID PIGX Link Image
Enzyme 39 HGNC ID HGNC:26046 Link Image
Enzyme 39 Chromosome Location 3
Enzyme 39 Locus 3q29
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, 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, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  2. 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]
  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. Ashida H, Hong Y, Murakami Y, Shishioh N, Sugimoto N, Kim YU, Maeda Y, Kinoshita T: Mammalian PIG-X and yeast Pbn1p are the essential components of glycosylphosphatidylinositol-mannosyltransferase I. Mol Biol Cell. 2005 Mar;16(3):1439-48. Epub 2005 Jan 5. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 8625
Enzyme 40 Name GPI mannosyltransferase 4
Enzyme 40 Synonyms
  1. GPI mannosyltransferase IV
  2. GPI-MT-IV
  3. Phosphatidylinositol-glycan biosynthesis class Z protein
  4. PIG-Z
  5. SMP3 homolog
  6. hSMP3
Enzyme 40 Gene Name PIGZ
Enzyme 40 Protein Sequence >GPI mannosyltransferase 4
MQICGSSVASVAAGTSFQVLGPVCWQQLDLKMAVRVLWGGLSLLRVLWCLLPQTGYVHPD
EFFQSPEVMAEDILGVQAARPWEFYPSSSCRSVLFPLLISGSTFWLLRLWEELGPWPGLV
SGYALLVGPRLLLTALSFALDGAVYHLAPPMGADRWNALALLSGSYVTLVFYTRTFSNTI
EGLLFTWLLVLVSSHVTWGPTRKEPAPGPRWRSWLLGGIVAAGFFNRPTFLAFAVVPLYL
WGTRGATNPGLKSLTREALVLLPGATLTAAVFVATDSWYFSSPATSRNLVLTPVNFLHYN
LNPQNLARHGTHARLTHLAVNGFLLFGVLHAQALQAAWQQLQVGLQASAQMGLLRALGAR
SLLSSPRSYLLLLYFMPLALLSAFSHQEARFLIPLLVPLVLLCSPQTQPVPWKGTVVLFN
ALGALLFGCLHQGGLVPGLEYLEQVVHAPVLPSTPTHYTLLFTHTYMPPRHLLHLPGLGA
PVEVVDMGGTEDWALCQTLKSFTRQPACQVAGGPWLCRLFVVTPGTTRRAVEKCSFPFKN
ETLLFPHLTLEDPPALSSLLSGAWRDHLSLHIVELGEET
Enzyme 40 Number of Residues 579
Enzyme 40 Molecular Weight 63472.6
Enzyme 40 Theoretical pI 8.28
Enzyme 40 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 40 General Function Involved in transferase activity, transferring glycosyl groups
Enzyme 40 Specific Function Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to some trimannosyl-GPIs during GPI precursor assembly. The presence of a fourth mannose in GPI is facultative and only scarcely detected, suggesting that it only exists in some tissues
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • 131-151 156-173 180-200 216-236 258-278 369-389 391-411 416-436
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 30581137 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID Q86VD9 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name PIGZ_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >1740 bp
ATGCAGATCTGTGGATCCAGCGTAGCATCTGTAGCAGCTGGGACATCATTCCAGGTTTTG
GGCCCGGTGTGTTGGCAACAACTGGATCTGAAGATGGCAGTCAGGGTGCTTTGGGGTGGT
CTCAGCCTGCTCCGAGTGCTGTGGTGTCTCCTTCCGCAGACGGGCTATGTGCACCCAGAT
GAGTTCTTCCAGTCCCCTGAGGTGATGGCAGAGGACATCCTGGGCGTTCAGGCCGCGCGG
CCCTGGGAGTTTTACCCCAGCAGCTCCTGCCGCTCGGTGCTCTTCCCCCTGCTGATCTCT
GGTTCCACCTTCTGGCTGCTCAGGCTCTGGGAGGAGCTGGGGCCGTGGCCTGGCCTGGTG
AGCGGCTATGCGCTGCTGGTGGGGCCTCGACTCCTCCTCACTGCCCTTTCCTTTGCTCTG
GACGGGGCCGTGTACCACCTGGCCCCGCCGATGGGGGCGGATCGCTGGAACGCCCTGGCC
CTGCTGTCTGGTTCCTACGTCACCCTGGTCTTCTACACAAGGACCTTCTCCAACACCATT
GAGGGACTCCTCTTCACGTGGCTGCTGGTGCTGGTATCCTCCCATGTAACGTGGGGCCCT
ACACGCAAGGAGCCGGCGCCGGGTCCACGGTGGCGCAGCTGGCTTCTTGGAGGCATTGTG
GCTGCTGGCTTCTTCAACCGGCCCACCTTTCTGGCCTTTGCTGTGGTCCCCCTCTACCTC
TGGGGCACTCGTGGAGCCACAAACCCTGGTTTGAAGTCTCTGACCCGGGAGGCCCTGGTG
CTGCTCCCTGGGGCAGCCCTCACAGCAGCGGTGTTTGTGGCCACGGACAGCTGGTATTTC
TCCAGCCCCGCTACATCCAGGAACCTTGTCCTGACACCTGTCAACTTCTTGCACTACAAC
CTGAATCCCCAAAACCTGGCGAGACATGGCACGCACGCGCGGCTCACTCACCTGGCAGTC
AACGGCTTCCTGCTCTTCGGGGTGCTGCATGCCCAGGCCCTGCAGGCTGCGTGGCAACGG
CTGCAAGTCGGCCTCCAGGCCTCTGCACAAATGGGCCTCCTGAGGGCACTGGGTGCCCGG
AGCCTGCTGTCCAGCCCCAGGTCCTATCTCCTTCTCCTCTACTTCATGCCTCTGGCCCTG
CTATCTGCCTTTAGCCACCAGGAGGCTCGGTTCCTGATTCCCCTCCTGGTCCCCCTGGTC
CTGCTTTGTAGTCCACAGACGCAGCCTGTGCCTTGGAAGGGCACTGTGGTCCTCTTCAAC
GCCCTCGGTGCCCTCCTCTTCGGCTGCCTGCATCAGGGGGGCCTGGTGCCTGGCCTGGAG
TACCTGGAGCAGGTGGTCCATGCCCCTGTGCTCCCAAGCACACCCACCCACTACACACTC
CTCTTCACTCACACCTACATGCCCCCCCGGCACCTCCTACACCTCCCAGGCCTGGGGGCA
CCAGTGGAGGTGGTGGACATGGGGGGGACTGAGGACTGGGCCCTGTGCCAAACCCTGAAA
AGCTTCACCAGACAACCAGCCTGCCAAGTGGCTGGTGGGCCATGGCTCTGCCGCCTCTTT
GTGGTAACCCCTGGCACCACCAGGCGTGCCGTGGAGAAGTGCAGCTTCCCCTTCAAGAAT
GAAACACTTTTATTTCCCCATCTGACCCTGGAGGATCCACCAGCCCTGTCCTCCTTGCTG
AGTGGGGCTTGGAGGGACCACCTCAGTCTTCACATTGTGGAGCTGGGGGAAGAAACCTGA
Enzyme 40 GenBank Gene ID NM_025163.2 Link Image
Enzyme 40 GeneCard ID PIGZ Link Image
Enzyme 40 GenAtlas ID PIGZ Link Image
Enzyme 40 HGNC ID HGNC:30596 Link Image
Enzyme 40 Chromosome Location 3
Enzyme 40 Locus 3q29
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  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]
  2. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, 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, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [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. Taron BW, Colussi PA, Wiedman JM, Orlean P, Taron CH: Human Smp3p adds a fourth mannose to yeast and human glycosylphosphatidylinositol precursors in vivo. J Biol Chem. 2004 Aug 20;279(34):36083-92. Epub 2004 Jun 18. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 8839
Enzyme 41 Name Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2
Enzyme 41 Synonyms
  1. Inositol polyphosphate phosphatase-like protein 1
  2. INPPL-1
  3. Protein 51C
  4. SH2 domain-containing inositol-5'-phosphatase 2
  5. SH2 domain-containing inositol phosphatase 2
  6. SHIP-2
Enzyme 41 Gene Name INPPL1
Enzyme 41 Protein Sequence >Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2
MASACGAPGPGGALGSQAPSWYHRDLSRAAAEELLARAGRDGSFLVRDSESVAGAFALCV
LYQKHVHTYRILPDGEDFLAVQTSQGVPVRRFQTLGELIGLYAQPNQGLVCALLLPVEGE
REPDPPDDRDASDGEDEKPPLPPRSGSTSISAPTGPSSPLPAPETPTAPAAESAPNGLST
VSHDYLKGSYGLDLEAVRGGASHLPHLTRTLATSCRRLHSEVDKVLSGLEILSKVFDQQS
SPMVTRLLQQQNLPQTGEQELESLVLKLSVLKDFLSGIQKKALKALQDMSSTAPPAPQPS
TRKAKTIPVQAFEVKLDVTLGDLTKIGKSQKFTLSVDVEGGRLVLLRRQRDSQEDWTTFT
HDRIRQLIKSQRVQNKLGVVFEKEKDRTQRKDFIFVSARKREAFCQLLQLMKNKHSKQDE
PDMISVFIGTWNMGSVPPPKNVTSWFTSKGLGKTLDEVTVTIPHDIYVFGTQENSVGDRE
WLDLLRGGLKELTDLDYRPIAMQSLWNIKVAVLVKPEHENRISHVSTSSVKTGIANTLGN
KGAVGVSFMFNGTSFGFVNCHLTSGNEKTARRNQNYLDILRLLSLGDRQLNAFDISLRFT
HLFWFGDLNYRLDMDIQEILNYISRKEFEPLLRVDQLNLEREKHKVFLRFSEEEISFPPT
YRYERGSRDTYAWHKQKPTGVRTNVPSWCDRILWKSYPETHIICNSYGCTDDIVTSDHSP
VFGTFEVGVTSQFISKKGLSKTSDQAYIEFESIEAIVKTASRTKFFIEFYSTCLEEYKKS
FENDAQSSDNINFLKVQWSSRQLPTLKPILADIEYLQDQHLLLTVKSMDGYESYGECVVA
LKSMIGSTAQQFLTFLSHRGEETGNIRGSMKVRVPTERLGTRERLYEWISIDKDEAGAKS
KAPSVSRGSQEPRSGSRKPAFTEASCPLSRLFEEPEKPPPTGRPPAPPRAAPREEPLTPR
LKPEGAPEPEGVAAPPPKNSFNNPAYYVLEGVPHQLLPPEPPSPARAPVPSATKNKVAIT
VPAPQLGHHRHPRVGEGSSSDEESGGTLPPPDFPPPPLPDSAIFLPPSLDPLPGPVVRGR
GGAEARGPPPPKAHPRPPLPPGPSPASTFLGEVASGDDRSCSVLQMAKTLSEVDYAPAGP
ARSALLPGPLELQPPRGLPSDYGRPLSFPPPRIRESIQEDLAEEAPCLQGGRASGLGEAG
MSAWLRAIGLERYEEGLVHNGWDDLEFLSDITEEDLEEAGVQDPAHKRLLLDTLQLSK
Enzyme 41 Number of Residues 1258
Enzyme 41 Molecular Weight 138597.5
Enzyme 41 Theoretical pI 6.49
Enzyme 41 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphatase activity
  • phosphoric ester hydrolase activity
  • protein binding
Process
Component
Enzyme 41 General Function Involved in inositol or phosphatidylinositol phosphatase activity
Enzyme 41 Specific Function Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol- 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling. Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6
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 222136583 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID O15357 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name SHIP2_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >3777 bp
ATGGCCTCGGCCTGCGGGGCGCCGGGCCCGGGGGGCGCCCTGGGCAGCCAGGCCCCCTCC
TGGTACCACCGCGACCTGAGCCGGGCGGCCGCGGAGGAGCTGCTGGCCCGGGCGGGCCGC
GATGGCAGCTTCCTGGTCCGAGACAGCGAGAGCGTGGCGGGGGCCTTCGCGCTCTGCGTC
CTGTATCAGAAGCATGTGCACACGTATCGCATTCTGCCTGATGGAGAAGATTTCTTGGCT
GTGCAGACCTCGCAGGGTGTGCCTGTGCGCCGCTTCCAGACCCTGGGTGAGCTCATCGGC
CTGTACGCCCAGCCCAACCAGGGCCTTGTGTGCGCCCTGCTTCTTCCTGTAGAGGGTGAG
CGAGAGCCGGACCCACCGGATGACCGGGATGCCTCAGATGGGGAGGATGAGAAGCCCCCG
CTGCCCCCGCGCTCTGGCTCCACCAGCATTTCTGCCCCCACTGGGCCCAGCAGTCCCCTG
CCAGCTCCTGAGACTCCCACAGCTCCAGCTGCTGAGAGTGCTCCCAATGGGCTGAGCACC
GTCTCGCACGACTACCTGAAAGGCAGCTATGGGCTGGACCTGGAAGCTGTGAGGGGTGGA
GCCAGCCACCTGCCCCACCTCACCCGTACCCTCGCTACCTCATGCCGGAGGCTGCACAGT
GAGGTGGACAAGGTCCTGTCAGGCCTGGAGATCCTGTCCAAGGTGTTTGACCAGCAGAGC
TCGCCCATGGTGACCCGCCTTTTGCAGCAGCAGAACCTGCCACAGACAGGGGAGCAGGAA
CTAGAGAGCCTGGTGCTGAAGCTGTCAGTGCTAAAGGACTTCCTGTCAGGCATCCAGAAG
AAGGCCCTGAAGGCCCTACAGGACATGAGCTCCACAGCACCCCCAGCTCCGCAGCCATCC
ACACGTAAGGCCAAGACCATCCCCGTGCAGGCCTTTGAGGTGAAGCTAGATGTGACCCTG
GGTGACCTGACCAAGATTGGGAAGTCACAGAAGTTCACGCTGAGCGTGGATGTGGAGGGT
GGGCGGCTGGTGCTGCTGCGGAGACAGCGGGACTCCCAGGAGGACTGGACCACCTTCACG
CACGACCGCATCCGCCAGCTCATTAAGTCCCAGCGTGTCCAGAACAAGCTGGGTGTTGTG
TTTGAGAAGGAGAAGGACCGGACTCAGCGCAAGGACTTCATCTTTGTCAGTGCCCGGAAG
CGGGAGGCCTTCTGCCAGCTGTTGCAGCTCATGAAGAACAAGCACTCCAAGCAGGACGAG
CCCGACATGATCTCAGTCTTCATAGGCACCTGGAACATGGGAAGTGTACCACCTCCAAAA
AACGTGACATCCTGGTTCACATCGAAGGGTCTGGGGAAGACCCTGGACGAGGTCACAGTG
ACCATACCCCATGACATCTATGTCTTTGGGACCCAGGAGAACTCAGTGGGCGACCGCGAG
TGGCTGGACCTACTGCGCGGGGGCCTCAAGGAGCTTACGGATCTGGATTACCGCCCGATT
GCCATGCAATCACTGTGGAATATCAAGGTGGCAGTGCTGGTCAAGCCAGAGCACGAGAAC
CGTATCAGCCATGTCAGTACGTCCAGTGTGAAGACTGGCATCGCCAACACCCTGGGGAAC
AAGGGGGCTGTGGGCGTCTCCTTCATGTTTAATGGCACCTCATTTGGCTTTGTGAATTGT
CACCTCACCTCGGGAAATGAGAAGACGGCTCGGAGGAACCAAAACTACTTGGACATCCTG
CGGCTGCTCTCGCTGGGCGACCGGCAGCTCAATGCCTTTGACATCTCTCTGCGTTTCACA
CACCTCTTCTGGTTTGGGGACCTCAACTACCGCCTGGACATGGATATCCAGGAGATCCTG
AACTACATCAGCAGGAAAGAGTTTGAGCCCCTCCTCAGGGTGGACCAGCTCAACCTGGAG
CGGGAGAAGCACAAGGTCTTCCTTCGATTCAGTGAGGAGGAGATCTCCTTCCCACCCACC
TACCGCTATGAGCGGGGTTCCCGGGACACATATGCCTGGCACAAGCAGAAGCCAACTGGG
GTCCGGACCAATGTGCCCTCATGGTGTGACCGGATTCTGTGGAAATCCTACCCTGAAACT
CACATCATCTGCAATTCTTATGGTTGCACTGATGACATCGTCACCAGCGACCATTCCCCC
GTGTTTGGGACATTTGAGGTTGGAGTTACCTCCCAGTTCATCTCCAAGAAAGGGCTCTCA
AAGACTTCAGACCAGGCCTACATTGAGTTTGAGAGCATCGAGGCCATTGTGAAGACAGCC
AGCCGCACCAAGTTCTTCATCGAGTTCTACTCTACCTGCCTGGAGGAATACAAGAAGAGC
TTTGAGAATGATGCCCAGAGCAGTGACAACATCAACTTCCTCAAAGTGCAGTGGTCTTCA
CGCCAGCTGCCCACGCTCAAACCAATTCTGGCTGATATCGAGTACCTGCAGGACCAGCAC
CTCCTGCTCACAGTCAAGTCCATGGATGGCTATGAATCCTATGGGGAGTGTGTGGTTGCA
CTCAAATCCATGATCGGCAGCACGGCCCAACAGTTCCTGACCTTCCTATCCCACCGTGGC
GAGGAGACAGGCAATATCAGAGGCTCCATGAAGGTGCGGGTGCCCACGGAGCGCCTGGGC
ACCCGTGAGCGGCTCTACGAGTGGATCAGCATTGATAAGGATGAGGCAGGAGCAAAGAGC
AAAGCCCCCTCTGTGTCCCGAGGGAGCCAGGAGCCCAGGTCAGGGAGCCGCAAGCCAGCC
TTCACAGAGGCCTCCTGCCCGCTCTCCAGGTTATTTGAAGAACCAGAGAAACCGCCACCA
ACGGGGAGGCCCCCAGCCCCACCCCGAGCAGCTCCCCGGGAGGAGCCCTTGACCCCCAGG
TTGAAGCCAGAGGGAGCTCCTGAACCAGAAGGGGTGGCGGCCCCCCCACCCAAGAACAGC
TTCAATAACCCTGCCTACTACGTCCTTGAAGGGGTCCCGCACCAGCTGCTGCCCCCGGAG
CCACCCTCGCCTGCCAGGGCCCCTGTCCCATCTGCCACCAAGAACAAAGTGGCCATTACA
GTGCCTGCTCCACAGCTTGGGCACCACCGGCACCCTCGTGTGGGAGAGGGGAGTTCTTCA
GATGAGGAGTCTGGAGGCACACTGCCCCCTCCAGACTTTCCACCTCCACCACTGCCGGAC
TCAGCCATCTTCCTGCCCCCCAGCCTGGATCCTTTACCAGGGCCAGTGGTCCGGGGCCGT
GGTGGGGCTGAGGCCCGTGGCCCACCACCTCCCAAGGCCCATCCAAGGCCTCCACTGCCC
CCAGGCCCCTCACCAGCCAGCACTTTCCTGGGGGAAGTGGCCAGTGGGGATGACCGGTCC
TGCTCGGTGCTGCAGATGGCCAAGACGCTGAGCGAGGTGGACTATGCCCCTGCTGGGCCT
GCACGCTCAGCGCTCCTCCCAGGCCCCCTGGAGCTGCAGCCCCCCCGGGGACTGCCCTCG
GACTATGGCCGGCCCCTCAGCTTCCCTCCACCCCGCATCCGGGAGAGCATCCAGGAAGAC
CTGGCAGAGGAGGCTCCGTGCCTGCAGGGCGGGCGGGCCAGCGGGCTGGGCGAGGCAGGC
ATGAGTGCCTGGCTGCGGGCCATCGGCTTGGAGCGCTATGAGGAGGGCCTGGTGCATAAT
GGCTGGGACGACCTGGAGTTTCTCAGTGACATCACCGAGGAGGACTTGGAGGAGGCTGGG
GTGCAGGACCCGGCTCACAAGCGCCTCCTTCTGGACACCCTGCAGCTCAGCAAGTGA
Enzyme 41 GenBank Gene ID NM_001567.3 Link Image
Enzyme 41 GeneCard ID INPPL1 Link Image
Enzyme 41 GenAtlas ID INPPL1 Link Image
Enzyme 41 HGNC ID HGNC:6080 Link Image
Enzyme 41 Chromosome Location 1
Enzyme 41 Locus 11q23
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Hejna JA, Saito H, Merkens LS, Tittle TV, Jakobs PM, Whitney MA, Grompe M, Friedberg AS, Moses RE: Cloning and characterization of a human cDNA (INPPL1) sharing homology with inositol polyphosphate phosphatases. Genomics. 1995 Sep 1;29(1):285-7. [PubMed Link Image]
  2. Pesesse X, Deleu S, De Smedt F, Drayer L, Erneux C: Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP. Biochem Biophys Res Commun. 1997 Oct 29;239(3):697-700. [PubMed Link Image]
  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. 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. Habib T, Hejna JA, Moses RE, Decker SJ: Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein. J Biol Chem. 1998 Jul 17;273(29):18605-9. [PubMed Link Image]
  6. Wisniewski D, Strife A, Swendeman S, Erdjument-Bromage H, Geromanos S, Kavanaugh WM, Tempst P, Clarkson B: A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells. Blood. 1999 Apr 15;93(8):2707-20. [PubMed Link Image]
  7. Bruhns P, Vely F, Malbec O, Fridman WH, Vivier E, Daeron M: Molecular basis of the recruitment of the SH2 domain-containing inositol 5-phosphatases SHIP1 and SHIP2 by fcgamma RIIB. J Biol Chem. 2000 Dec 1;275(48):37357-64. [PubMed Link Image]
  8. Pesesse X, Dewaste V, De Smedt F, Laffargue M, Giuriato S, Moreau C, Payrastre B, Erneux C: The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor (EGF) receptor and dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated COS-7 cells. J Biol Chem. 2001 Jul 27;276(30):28348-55. Epub 2001 May 10. [PubMed Link Image]
  9. Dyson JM, O'Malley CJ, Becanovic J, Munday AD, Berndt MC, Coghill ID, Nandurkar HH, Ooms LM, Mitchell CA: The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. J Cell Biol. 2001 Dec 10;155(6):1065-79. Epub 2001 Dec 10. [PubMed Link Image]
  10. Prasad N, Topping RS, Decker SJ: SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas) adapter protein and regulates cellular adhesion and spreading. Mol Cell Biol. 2001 Feb;21(4):1416-28. [PubMed Link Image]
  11. Steen H, Kuster B, Fernandez M, Pandey A, Mann M: Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway. J Biol Chem. 2002 Jan 11;277(2):1031-9. Epub 2001 Oct 30. [PubMed Link Image]
  12. Prasad N, Topping RS, Decker SJ: Src family tyrosine kinases regulate adhesion-dependent tyrosine phosphorylation of 5'-inositol phosphatase SHIP2 during cell attachment and spreading on collagen I. J Cell Sci. 2002 Oct 1;115(Pt 19):3807-15. [PubMed Link Image]
  13. Vandenbroere I, Paternotte N, Dumont JE, Erneux C, Pirson I: The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2. Biochem Biophys Res Commun. 2003 Jan 10;300(2):494-500. [PubMed Link Image]
  14. Dyson JM, Munday AD, Kong AM, Huysmans RD, Matzaris M, Layton MJ, Nandurkar HH, Berndt MC, Mitchell CA: SHIP-2 forms a tetrameric complex with filamin, actin, and GPIb-IX-V: localization of SHIP-2 to the activated platelet actin cytoskeleton. Blood. 2003 Aug 1;102(3):940-8. Epub 2003 Apr 3. [PubMed Link Image]
  15. Pengal RA, Ganesan LP, Fang H, Marsh CB, Anderson CL, Tridandapani S: SHIP-2 inositol phosphatase is inducibly expressed in human monocytes and serves to regulate Fcgamma receptor-mediated signaling. J Biol Chem. 2003 Jun 20;278(25):22657-63. Epub 2003 Apr 10. [PubMed Link Image]
  16. 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]
  17. Vandeput F, Backers K, Villeret V, Pesesse X, Erneux C: The influence of anionic lipids on SHIP2 phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase activity. Cell Signal. 2006 Dec;18(12):2193-9. Epub 2006 May 23. [PubMed Link Image]
  18. Paternotte N, Zhang J, Vandenbroere I, Backers K, Blero D, Kioka N, Vanderwinden JM, Pirson I, Erneux C: SHIP2 interaction with the cytoskeletal protein Vinexin. FEBS J. 2005 Dec;272(23):6052-66. [PubMed Link Image]
  19. Prasad NK, Decker SJ: SH2-containing 5'-inositol phosphatase, SHIP2, regulates cytoskeleton organization and ligand-dependent down-regulation of the epidermal growth factor receptor. J Biol Chem. 2005 Apr 1;280(13):13129-36. Epub 2005 Jan 24. [PubMed Link Image]
  20. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  21. 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]
  22. Koch A, Mancini A, El Bounkari O, Tamura T: The SH2-domian-containing inositol 5-phosphatase (SHIP)-2 binds to c-Met directly via tyrosine residue 1356 and involves hepatocyte growth factor (HGF)-induced lamellipodium formation, cell scattering and cell spreading. Oncogene. 2005 May 12;24(21):3436-47. [PubMed Link Image]
  23. 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]
  24. 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]
  25. Raaijmakers JH, Deneubourg L, Rehmann H, de Koning J, Zhang Z, Krugmann S, Erneux C, Bos JL: The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase SHIP2 in a SAM domain-dependent manner. Cell Signal. 2007 Jun;19(6):1249-57. Epub 2007 Jan 20. [PubMed Link Image]
  26. Zhuang G, Hunter S, Hwang Y, Chen J: Regulation of EphA2 receptor endocytosis by SHIP2 lipid phosphatase via phosphatidylinositol 3-Kinase-dependent Rac1 activation. J Biol Chem. 2007 Jan 26;282(4):2683-94. Epub 2006 Nov 29. [PubMed Link Image]
  27. Artemenko Y, Gagnon A, Ibrahim S, Sorisky A: Regulation of PDGF-stimulated SHIP2 tyrosine phosphorylation and association with Shc in 3T3-L1 preadipocytes. J Cell Physiol. 2007 Jun;211(3):598-607. [PubMed Link Image]
  28. Marion E, Kaisaki PJ, Pouillon V, Gueydan C, Levy JC, Bodson A, Krzentowski G, Daubresse JC, Mockel J, Behrends J, Servais G, Szpirer C, Kruys V, Gauguier D, Schurmans S: The gene INPPL1, encoding the lipid phosphatase SHIP2, is a candidate for type 2 diabetes in rat and man. Diabetes. 2002 Jul;51(7):2012-7. [PubMed Link Image]
  29. Kaisaki PJ, Delepine M, Woon PY, Sebag-Montefiore L, Wilder SP, Menzel S, Vionnet N, Marion E, Riveline JP, Charpentier G, Schurmans S, Levy JC, Lathrop M, Farrall M, Gauguier D: Polymorphisms in type II SH2 domain-containing inositol 5-phosphatase (INPPL1, SHIP2) are associated with physiological abnormalities of the metabolic syndrome. Diabetes. 2004 Jul;53(7):1900-4. [PubMed Link Image]
  30. Kagawa S, Sasaoka T, Yaguchi S, Ishihara H, Tsuneki H, Murakami S, Fukui K, Wada T, Kobayashi S, Kimura I, Kobayashi M: Impact of SRC homology 2-containing inositol 5'-phosphatase 2 gene polymorphisms detected in a Japanese population on insulin signaling. J Clin Endocrinol Metab. 2005 May;90(5):2911-9. Epub 2005 Feb 1. [PubMed Link Image]
  31. Marcano AC, Burke B, Gungadoo J, Wallace C, Kaisaki PJ, Woon PY, Farrall M, Clayton D, Brown M, Dominiczak A, Connell JM, Webster J, Lathrop M, Caulfield M, Samani N, Gauguier D, Munroe PB: Genetic association analysis of inositol polyphosphate phosphatase-like 1 (INPPL1, SHIP2) variants with essential hypertension. J Med Genet. 2007 Sep;44(9):603-5. Epub 2007 Jun 8. [PubMed Link Image]
  32. 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]
  33. 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]
  34. 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]
  35. 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]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 9375
Enzyme 42 Name Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1
Enzyme 42 Synonyms
  1. Inositol polyphosphate-5-phosphatase of 145 kDa
  2. SIP-145
  3. SH2 domain-containing inositol-5'-phosphatase 1
  4. SH2 domain-containing inositol phosphatase 1
  5. SHIP-1
  6. p150Ship
  7. hp51CN
Enzyme 42 Gene Name INPP5D
Enzyme 42 Protein Sequence >Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1
MVPCWNHGNITRSKAEELLSRTGKDGSFLVRASESISRAYALCVLYRNCVYTYRILPNED
DKFTVQASEGVSMRFFTKLDQLIEFYKKENMGLVTHLQYPVPLEEEDTGDDPEEDTVESV
VSPPELPPRNIPLTASSCEAKEVPFSNENPRATETSRPSLSETLFQRLQSMDTSGLPEEH
LKAIQDYLSTQLAQDSEFVKTGSSSLPHLKKLTTLLCKELYGEVIRTLPSLESLQRLFDQ
QLSPGLRPRPQVPGEANPINMVSKLSQLTSLLSSIEDKVKALLHEGPESPHRPSLIPPVT
FEVKAESLGIPQKMQLKVDVESGKLIIKKSKDGSEDKFYSHKKILQLIKSQKFLNKLVIL
VETEKEKILRKEYVFADSKKREGFCQLLQQMKNKHSEQPEPDMITIFIGTWNMGNAPPPK
KITSWFLSKGQGKTRDDSADYIPHDIYVIGTQEDPLSEKEWLEILKHSLQEITSVTFKTV
AIHTLWNIRIVVLAKPEHENRISHICTDNVKTGIANTLGNKGAVGVSFMFNGTSLGFVNS
HLTSGSEKKLRRNQNYMNILRFLALGDKKLSPFNITHRFTHLFWFGDLNYRVDLPTWEAE
TIIQKIKQQQYADLLSHDQLLTERREQKVFLHFEEEEITFAPTYRFERLTRDKYAYTKQK
ATGMKYNLPSWCDRVLWKSYPLVHVVCQSYGSTSDIMTSDHSPVFATFEAGVTSQFVSKN
GPGTVDSQGQIEFLRCYATLKTKSQTKFYLEFHSSCLESFVKSQEGENEEGSEGELVVKF
GETLPKLKPIISDPEYLLDQHILISIKSSDSDESYGEGCIALRLEATETQLPIYTPLTHH
GELTGHFQGEIKLQTSQGKTREKLYDFVKTERDESSGPKTLKSLTSHDPMKQWEVTSRAP
PCSGSSITEIINPNYMGVGPFGPPMPLHVKQTLSPDQQPTAWSYDQPPKDSPLGPCRGES
PPTPPGQPPISPKKFLPSTANRGLPPRTQESRPSDLGKNAGDTLPQEDLPLTKPEMFENP
LYGSLSSFPKPAPRKDQESPKMPRKEPPPCPEPGILSPSIVLTKAQEADRGEGPGKQVPA
PRLRSFTCSSSAEGRAAGGDKSQGKPKTPVSSQAPVPAKRPIKPSRSEINQQTPPTPTPR
PPLPVKSPAVLHLQHSKGRDYRDNTELPHHGKHRPEEGPPGPLGRTAMQ
Enzyme 42 Number of Residues 1189
Enzyme 42 Molecular Weight 133291.4
Enzyme 42 Theoretical pI 7.64
Enzyme 42 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphatase activity
  • phosphoric ester hydrolase activity
  • protein binding
Process
Component
Enzyme 42 General Function Involved in inositol or phosphatidylinositol phosphatase activity
Enzyme 42 Specific Function Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol- 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity. Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions 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 64085167 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q92835 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name SHIP1_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >3570 bp
ATGGTCCCCTGCTGGAACCATGGCAACATCACCCGCTCCAAGGCGGAGGAGCTGCTTTCC
AGGACAGGCAAGGACGGGAGCTTCCTCGTGCGTGCCAGCGAGTCCATCTCCCGGGCATAC
GCGCTCTGCGTGCTGTATCGGAATTGCGTTTACACTTACAGAATTCTGCCCAATGAAGAT
GATAAATTCACTGTTCAGGCATCCGAAGGCGTCTCCATGAGGTTCTTCACCAAGCTGGAC
CAGCTCATCGAGTTTTACAAGAAGGAAAACATGGGGCTGGTGACCCATCTGCAATACCCT
GTGCCGCTGGAGGAAGAGGACACAGGCGACGACCCTGAGGAGGACACAGTAGAAAGTGTC
GTGTCTCCACCCGAGCTGCCCCCAAGAAACATCCCGCTGACTGCCAGCTCCTGTGAGGCC
AAGGAGGTTCCTTTTTCAAACGAGAATCCCCGAGCGACCGAGACCAGCCGGCCGAGCCTC
TCCGAGACATTGTTCCAGCGACTGCAAAGCATGGACACCAGTGGGCTTCCAGAAGAGCAT
CTTAAGGCCATCCAAGATTATTTAAGCACTCAGCTCGCCCAGGACTCTGAATTTGTGAAG
ACAGGGTCCAGCAGTCTTCCTCACCTGAAGAAACTGACCACACTGCTCTGCAAGGAGCTC
TATGGAGAAGTCATCCGGACCCTCCCATCCCTGGAGTCTCTGCAGAGGTTATTTGACCAG
CAGCTCTCCCCGGGCCTCCGTCCACGTCCTCAGGTTCCTGGTGAGGCCAATCCCATCAAC
ATGGTGTCCAAGCTCAGCCAACTGACAAGCCTGTTGTCATCCATTGAAGACAAGGTCAAG
GCCTTGCTGCACGAGGGTCCTGAGTCTCCGCACCGGCCCTCCCTTATCCCTCCAGTCACC
TTTGAGGTGAAGGCAGAGTCTCTGGGGATTCCTCAGAAAATGCAGCTCAAAGTCGACGTT
GAGTCTGGGAAACTGATCATTAAGAAGTCCAAGGATGGTTCTGAGGACAAGTTCTACAGC
CACAAGAAAATCCTGCAGCTCATTAAGTCACAGAAATTTCTGAATAAGTTGGTGATCTTG
GTGGAAACAGAGAAGGAGAAGATCCTGCGGAAGGAATATGTTTTTGCTGACTCCAAAAAG
AGAGAAGGCTTCTGCCAGCTCCTGCAGCAGATGAAGAACAAGCACTCAGAGCAGCCGGAG
CCCGACATGATCACCATCTTCATCGGCACCTGGAACATGGGTAACGCCCCCCCTCCCAAG
AAGATCACGTCCTGGTTTCTCTCCAAGGGGCAGGGAAAGACGCGGGACGACTCTGCGGAC
TACATCCCCCATGACATTTACGTGATCGGCACCCAAGAGGACCCCCTGAGTGAGAAGGAG
TGGCTGGAGATCCTCAAACACTCCCTGCAAGAAATCACCAGTGTGACTTTTAAAACAGTC
GCCATCCACACGCTCTGGAACATCCGCATCGTGGTGCTGGCCAAGCCTGAGCACGAGAAC
CGGATCAGCCACATCTGTACTGACAACGTGAAGACAGGCATTGCAAACACACTGGGGAAC
AAGGGAGCCGTGGGGGTGTCGTTCATGTTCAATGGAACCTCCTTAGGGTTCGTCAACAGC
CACTTGACTTCAGGAAGTGAAAAGAAACTCAGGCGAAACCAAAACTATATGAACATTCTC
CGGTTCCTGGCCCTGGGCGACAAGAAGCTGAGTCCCTTTAACATCACTCACCGCTTCACG
CACCTCTTCTGGTTTGGGGATCTTAACTACCGTGTGGATCTGCCTACCTGGGAGGCAGAA
ACCATCATCCAGAAAATCAAGCAGCAGCAGTACGCAGACCTCCTGTCCCACGACCAGCTG
CTCACAGAGAGGAGGGAGCAGAAGGTCTTCCTACACTTCGAGGAGGAAGAAATCACGTTT
GCCCCAACCTACCGTTTTGAGAGACTGACTCGGGACAAATACGCCTACACCAAGCAGAAA
GCGACAGGGATGAAGTACAACTTGCCTTCCTGGTGTGACCGAGTCCTCTGGAAGTCTTAT
CCCCTGGTGCACGTGGTGTGTCAGTCTTATGGCAGTACCAGCGACATCATGACGAGTGAC
CACAGCCCTGTCTTTGCCACATTTGAGGCAGGAGTCACTTCCCAGTTTGTCTCCAAGAAC
GGTCCCGGGACTGTTGACAGCCAAGGACAGATTGAGTTTCTCAGGTGCTATGCCACATTG
AAGACCAAGTCCCAGACCAAATTCTACCTGGAGTTCCACTCGAGCTGCTTGGAGAGTTTT
GTCAAGAGTCAGGAAGGAGAAAATGAAGAAGGAAGTGAGGGGGAGCTGGTGGTGAAGTTT
GGTGAGACTCTTCCAAAGCTGAAGCCCATTATCTCTGACCCTGAGTACCTGCTAGACCAG
CACATCCTCATCAGCATCAAGTCCTCTGACAGCGACGAATCCTATGGCGAGGGCTGCATT
GCCCTTCGGTTAGAGGCCACAGAAACGCAGCTGCCCATCTACACGCCTCTCACCCACCAT
GGGGAGTTGACAGGCCACTTCCAGGGGGAGATCAAGCTGCAGACCTCTCAGGGCAAGACG
AGGGAGAAGCTCTATGACTTTGTGAAGACGGAGCGTGATGAATCCAGTGGGCCAAAGACC
CTGAAGAGCCTCACCAGCCACGACCCCATGAAGCAGTGGGAAGTCACTAGCAGGGCCCCT
CCGTGCAGTGGCTCCAGCATCACTGAAATCATCAACCCCAACTACATGGGAGTGGGGCCC
TTTGGGCCACCAATGCCCCTGCACGTGAAGCAGACCTTGTCCCCTGACCAGCAGCCCACA
GCCTGGAGCTACGACCAGCCGCCCAAGGACTCCCCGCTGGGGCCCTGCAGGGGAGAAAGT
CCTCCGACACCTCCCGGCCAGCCGCCCATATCACCCAAGAAGTTTTTACCCTCAACAGCA
AACCGGGGTCTCCCTCCCAGGACACAGGAGTCAAGGCCCAGTGACCTGGGGAAGAACGCA
GGGGACACGCTGCCTCAGGAGGACCTGCCGCTGACGAAGCCCGAGATGTTTGAGAACCCC
CTGTATGGGTCCCTGAGTTCCTTCCCTAAGCCTGCTCCCAGGAAGGACCAGGAATCCCCC
AAAATGCCGCGGAAGGAACCCCCGCCCTGCCCGGAACCCGGCATCTTGTCGCCCAGCATC
GTGCTCACCAAAGCCCAGGAGGCTGATCGCGGCGAGGGGCCCGGCAAGCAGGTGCCCGCG
CCCCGGCTGCGCTCCTTCACGTGCTCATCCTCTGCCGAGGGCAGGGCGGCCGGCGGGGAC
AAGAGCCAAGGGAAGCCCAAGACCCCGGTCAGCTCCCAGGCCCCGGTGCCGGCCAAGAGG
CCCATCAAGCCTTCCAGATCGGAAATCAACCAGCAGACCCCGCCCACCCCGACGCCGCGG
CCGCCGCTGCCAGTCAAGAGCCCGGCGGTGCTGCACCTCCAGCACTCCAAGGGCCGCGAC
TACCGCGACAACACCGAGCTCCCGCATCACGGCAAGCACCGGCCGGAGGAGGGGCCACCA
GGGCCTCTAGGCAGGACTGCCATGCAGTGA
Enzyme 42 GenBank Gene ID NM_001017915.1 Link Image
Enzyme 42 GeneCard ID INPP5D Link Image
Enzyme 42 GenAtlas ID INPP5D Link Image
Enzyme 42 HGNC ID HGNC:6079 Link Image
Enzyme 42 Chromosome Location 2
Enzyme 42 Locus 2q37.1
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Drayer AL, Pesesse X, De Smedt F, Woscholski R, Parker P, Erneux C: Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase. Biochem Biophys Res Commun. 1996 Aug 5;225(1):243-9. [PubMed Link Image]
  2. Ware MD, Rosten P, Damen JE, Liu L, Humphries RK, Krystal G: Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation. Blood. 1996 Oct 15;88(8):2833-40. [PubMed Link Image]
  3. Kavanaugh WM, Pot DA, Chin SM, Deuter-Reinhard M, Jefferson AB, Norris FA, Masiarz FR, Cousens LS, Majerus PW, Williams LT: Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2. Curr Biol. 1996 Apr 1;6(4):438-45. [PubMed Link Image]
  4. Geier SJ, Algate PA, Carlberg K, Flowers D, Friedman C, Trask B, Rohrschneider LR: The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood. Blood. 1997 Mar 15;89(6):1876-85. [PubMed Link Image]
  5. Odai H, Sasaki K, Iwamatsu A, Nakamoto T, Ueno H, Yamagata T, Mitani K, Yazaki Y, Hirai H: Purification and molecular cloning of SH2- and SH3-containing inositol polyphosphate-5-phosphatase, which is involved in the signaling pathway of granulocyte-macrophage colony-stimulating factor, erythropoietin, and Bcr-Abl. Blood. 1997 Apr 15;89(8):2745-56. [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. Mikhalap SV, Shlapatska LM, Berdova AG, Law CL, Clark EA, Sidorenko SP: CDw150 associates with src-homology 2-containing inositol phosphatase and modulates CD95-mediated apoptosis. J Immunol. 1999 May 15;162(10):5719-27. [PubMed Link Image]
  8. Dunant NM, Wisniewski D, Strife A, Clarkson B, Resh MD: The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells. Cell Signal. 2000 May;12(5):317-26. [PubMed Link Image]
  9. Freeburn RW, Wright KL, Burgess SJ, Astoul E, Cantrell DA, Ward SG: Evidence that SHIP-1 contributes to phosphatidylinositol 3,4,5-trisphosphate metabolism in T lymphocytes and can regulate novel phosphoinositide 3-kinase effectors. J Immunol. 2002 Nov 15;169(10):5441-50. [PubMed Link Image]
  10. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  11. Vaillancourt M, Levasseur S, Tremblay ML, Marois L, Rollet-Labelle E, Naccache PH: The Src homology 2-containing inositol 5-phosphatase 1 (SHIP1) is involved in CD32a signaling in human neutrophils. Cell Signal. 2006 Nov;18(11):2022-32. Epub 2006 Apr 3. [PubMed Link Image]
  12. 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]
  13. 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]
  14. Luo JM, Yoshida H, Komura S, Ohishi N, Pan L, Shigeno K, Hanamura I, Miura K, Iida S, Ueda R, Naoe T, Akao Y, Ohno R, Ohnishi K: Possible dominant-negative mutation of the SHIP gene in acute myeloid leukemia. Leukemia. 2003 Jan;17(1):1-8. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 9581
Enzyme 43 Name Phosphatidylinositol 3-kinase catalytic subunit type 3
Enzyme 43 Synonyms
  1. PI3-kinase type 3
  2. PI3K type 3
  3. PtdIns-3-kinase type 3
  4. Phosphatidylinositol 3-kinase p100 subunit
  5. Phosphoinositide-3-kinase class 3
  6. hVps34
Enzyme 43 Gene Name PIK3C3
Enzyme 43 Protein Sequence >Phosphatidylinositol 3-kinase catalytic subunit type 3
MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVT
CQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAV
PVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTK
AHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDG
DESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIV
SYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDV
EDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKK
DSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLI
SRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRS
LLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVK
IRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRK
ENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAE
VMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLN
KEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVK
KVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK
Enzyme 43 Number of Residues 887
Enzyme 43 Molecular Weight 101548.6
Enzyme 43 Theoretical pI 6.79
Enzyme 43 GO Classification
Function
  • 1-phosphatidylinositol-3-kinase activity
  • binding
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • kinase activity
  • lipid kinase activity
  • phosphoinositide 3-kinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biological regulation
  • glycerophospholipid metabolic process
  • intracellular signal transduction
  • metabolic process
  • organophosphate metabolic process
  • phosphoinositide metabolic process
  • phosphoinositide phosphorylation
  • phosphoinositide-mediated signaling
  • phospholipid metabolic process
  • regulation of biological process
  • regulation of cellular process
  • second-messenger-mediated signaling
  • signal transduction
Component
  • macromolecular complex
  • phosphoinositide 3-kinase complex
  • protein complex
Enzyme 43 General Function Involved in binding
Enzyme 43 Specific Function Catalytic subunit of the PI3K complex. Involved in the transport of lysosomal enzyme precursors to lysosomes
Enzyme 43 Pathways
Enzyme 43 Reactions
  • ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate [RN:R03362]
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 987948 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID Q8NEB9 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name PK3C3_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >2664 bp
ATGGGGGAAGCAGAGAAGTTTCACTACATCTATAGTTGTGACCTGGATATCAACGTCCAG
CTTAAGATAGGAAGCTTGGAAGGGAAGAGAGAACAAAAGAGTTATAACGCTGTCCTGGAA
GACCCAATGTTGAAGTTCTCAGGACTATATCAAGAGACATGCTCTGATCTTTATGTTACT
TGTCAAGTTTTTGCAGAAGGGAAGCCTTCGGCCTTGCCAGTGAGAACATCCTACAAAGCA
TTTAGTACAAGATGGAACTGGAATGAATGGCTGAAACTACCAGTAAAATACCCTGACCTG
CCCAGGAATGCCCAAGTGGCCCTCACCATATGGGATGTGTATGGTCCCGGAAAAGCAGTG
CCTGTAGGAGGAACAACGGTTTCGCTCTTTGGAAAATACGGCATGTCTCGCCAAGGGATG
CATGACTTGAAAGTCTGGCCTAATGTAGAAGCAGATGGATCAGAACCCACAAATACTCCT
GGCAGAACAAGTAGCACTCTCTCAGAAGATCAGATGAGCCGTCTTGCCAAGCTCACCAAA
GCTCATCGACAAGGACACATGGTGAAAGTAGATTGGCTGGATAGATTGACATTTAGAGAA
ATAGAAATGATAAATGAGAGTGTGAAACGAAGTTCTAATTTCATGTACCTGATGGGTGGA
TTTCGATGTGTCAAGTGTGATGATAAGGAATATGGTATTGTTTATTATGAAAAGGACGGT
GATGAATCATCTCCAATTTTAACAAGTTTTGAATTAGTGAAAGTTCCTGACCCCCAGATG
TCCCTGGAGAATTTAGTTGAGAGCAAACACCACAACCTTCCCCGGAGTTTAAGAAGTGGA
CCTTCTGACCACGATCTGAAACCCTATCCTTCCCCGAGAGATCAGTTAAAAAATATTGTG
AGTTATCCTCCATCCAAGCCACCCACATATGAAGAACAAGATCTTGTTTGGGAGTTTAGA
TATTATCTTACGAATCAAGATAAAGCCTTGACCAAAATCCTGACATCTGTTATTTGGGAT
CTACCTCAGGGGGCCAAACAGGCCTTGGCACTTCTGGGGAAATGGAACCCGATGGATGTA
GAGGACTCCTTGGAGCTGATATCCTCTCATTACACCAACCCAACTGTGAGGCGTTATGCT
GTTGCCCGGTTGCGACAGGCCGATGATGAGGATTTGTTGATGTACCTATCACAATTGGTC
CAGGCTCTCAAATATGAAAATTTTGATGATATAAAGAATGGATTGGAACCTACCAAGAAG
GATAGTCAGAGTTCAGTGTCAGGAAATGTGTCAAATTCTGGAATAAATTCTGCAGAAATA
GATAGCTCCCAAATTATAACCAGCCCCCTTCCTTCAGTCTCTTCACCTCCTCCTGCATCA
AAAACAAAAGAAGTTCCAGATGGCGAAAATCTGGAACAAGATCTCTGTACCTTCTTGATA
TCGAGAGCCTCCAAAAACTCAACACTGGCTAATTATTTATACTGGTATGTGATAGTGGAA
TGTGAAGATCAAGATACTCAGCAGAGAGATCCAAAGACCCATGAGATGTACTTGAACGTA
ATGAGAAGATTCAGCCAAGCATTGTTGAAGGGTGATAAGTCTGTCAGAGTTATGCGTTCT
TTGCTGGCTGCACAACAGACATTTGTAGATCGGTTGGTGCATCTAATGAAGGCAGTACAA
CGCGAAAGTGGAAATCGTAAGAAAAAGAATGAGAGACTACAGGCATTGCTTGGAGATAAT
GAAAAGATGAATTTGTCAGATGTGGAACTTATCCCGTTGCCTTTAGAACCCCAAGTGAAA
ATTAGAGGAATAATTCCGGAAACAGCTACACTGTTTAAAAGTGCCCTTATGCCTGCACAG
TTGTTTTTTAAGACGGAAGATGGAGGCAAATATCCAGTTATATTTAAGCATGGAGATGAT
TTACGTCAAGATCAACTTATTCTTCAAATCATTTCACTCATGGACAAGCTGTTACGGAAA
GAAAATCTGGACTTGAAATTGACACCTTATAAGGTGTTAGCCACCAGTACAAAACATGGC
TTCATGCAGTTTATCCAGTCAGTTCCTGTGGCTGAAGTTCTTGATACAGAGGGAAGCATT
CAGAACTTTTTTAGAAAATATGCACCAAGTGAGAATGGGCCAAATGGGATTAGTGCTGAG
GTCATGGACACTTACGTTAAAAGCTGTGCTGGATATTGCGTGATCACCTATATACTTGGA
GTTGGAGACAGGCACCTGGATAACCTTGTGCTAACAAAAACAGGCAAACTCTTCCACATA
GACTTTGGATATATTTTGGGTCGGGATCCAAAGCCTCTTCCTCCACCAATGAAGCTGAAT
AAAGAAATGGTAGAAGGAATGGGGGGCACACAGAGTGAGCAGTACCAAGAGTTCCGTAAA
CAGTGTTACACGGCTTTCCTCCACCTGCGGAGGTATTCTAATCTGATTTTGAACTTGTTT
TCCTTGATGGTTGATCCAAACATTCCAGATATTGCACTTGAACCAGATAAAACTGTGAAA
AAGGTTCAGGATAAATTCCGCTTAGACCTGTCGGATGAAGAGGCTGTGCATTACATGCAG
AGTCTGATTGATGAGAGTGTCCATGCTCTTTTTGCTGCAGTGGTGGAACAGATTCACAAG
TTTGCCCAGTACTGGAGAAAATGA
Enzyme 43 GenBank Gene ID Z46973 Link Image
Enzyme 43 GeneCard ID PIK3C3 Link Image
Enzyme 43 GenAtlas ID PIK3C3 Link Image
Enzyme 43 HGNC ID HGNC:8974 Link Image
Enzyme 43 Chromosome Location 1
Enzyme 43 Locus 18q12.3
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Volinia S, Dhand R, Vanhaesebroeck B, MacDougall LK, Stein R, Zvelebil MJ, Domin J, Panaretou C, Waterfield MD: A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system. EMBO J. 1995 Jul 17;14(14):3339-48. [PubMed Link Image]
  2. 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]
  3. 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]
  4. Sun Q, Fan W, Chen K, Ding X, Chen S, Zhong Q: Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase. Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19211-6. Epub 2008 Dec 2. [PubMed Link Image]
  5. 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]
  6. Matsunaga K, Saitoh T, Tabata K, Omori H, Satoh T, Kurotori N, Maejima I, Shirahama-Noda K, Ichimura T, Isobe T, Akira S, Noda T, Yoshimori T: Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages. Nat Cell Biol. 2009 Apr;11(4):385-96. Epub 2009 Mar 8. [PubMed Link Image]
  7. 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]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 10045
Enzyme 44 Name PI-PLC X domain-containing protein 2
Enzyme 44 Synonyms Not Available
Enzyme 44 Gene Name PLCXD2
Enzyme 44 Protein Sequence >PI-PLC X domain-containing protein 2
MLAVRKARRKLRMGTICSPNPSGTKTSSEVCNADWMASLPPHLHNLPLSNLAIPGSHDSF
SYWVDEKSPVGPDQTQAIKRLARISLVKKLMKKWSVTQNLTFREQLEAGIRYFDLRVSSK
PGDADQEIYFIHGLFGIKVWDGLMEIDSFLTQHPQEIIFLDFNHFYAMDETHHKCLVLRI
QEAFGNKLCPACSVESLTLRTLWEKNCQVLIFYHCPFYKQYPFLWPGKKIPAPWANTTSV
RKLILFLETTLSERASRGSFHVSQAILTPRVKTIARGLVGGLKNTLVHSNRWNSHGPSLL
SQERS
Enzyme 44 Number of Residues 305
Enzyme 44 Molecular Weight 34776.9
Enzyme 44 Theoretical pI 9.94
Enzyme 44 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • signaling
  • signaling pathway
Component
Enzyme 44 General Function Involved in phosphoric diester hydrolase activity
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 297515471 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID Q0VAA5 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name PLCX2_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >918 bp
ATGCTAGCAGTTAGGAAGGCCAGGAGGAAACTCAGGATGGGGACCATCTGCTCCCCCAAC
CCCAGCGGGACAAAGACATCATCGGAGGTCTGCAATGCCGACTGGATGGCCTCGCTCCCC
CCTCACCTCCACAACCTCCCCCTTTCCAATCTGGCAATCCCAGGCTCACATGATTCATTC
AGCTACTGGGTGGATGAAAAGTCCCCAGTGGGGCCTGACCAAACCCAAGCTATCAAACGC
CTCGCCAGGATCTCCTTGGTGAAGAAGCTAATGAAGAAGTGGTCTGTGACTCAGAACCTG
ACATTTCGAGAACAGCTGGAAGCTGGGATCCGCTACTTTGACCTGCGTGTGTCTTCCAAA
CCAGGGGATGCCGACCAGGAGATCTACTTCATCCATGGGCTTTTTGGCATCAAGGTCTGG
GATGGGCTGATGGAAATTGACTCGTTTCTTACACAGCACCCCCAGGAGATTATCTTCCTG
GATTTCAACCACTTCTATGCCATGGATGAGACCCATCACAAATGCCTGGTTCTGCGGATC
CAGGAGGCCTTTGGAAACAAGCTGTGCCCAGCCTGCAGTGTGGAAAGTTTGACGCTGCGA
ACTCTGTGGGAGAAGAACTGCCAGGTTCTTATTTTCTACCACTGTCCCTTCTACAAGCAG
TACCCCTTCCTGTGGCCAGGAAAGAAGATTCCAGCGCCCTGGGCAAACACCACAAGTGTG
CGCAAACTAATCCTCTTCTTGGAGACCACTCTGAGTGAGCGGGCCTCACGGGGCTCCTTC
CATGTCTCCCAAGCGATCCTCACCCCCAGAGTGAAGACCATTGCCCGGGGCTTGGTTGGG
GGCCTCAAGAACACGCTGGTTCATAGCAATCGCTGGAACAGCCATGGGCCATCCCTGCTG
AGTCAGGAAAGAAGCTGA
Enzyme 44 GenBank Gene ID NM_001185106.1 Link Image
Enzyme 44 GeneCard ID PLCXD2 Link Image
Enzyme 44 GenAtlas ID PLCXD2 Link Image
Enzyme 44 HGNC ID HGNC:26462 Link Image
Enzyme 44 Chromosome Location 3
Enzyme 44 Locus 3q13.2
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 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]
  2. 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]
  3. 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 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 10047
Enzyme 45 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
Enzyme 45 Synonyms
  1. hPLCD4
  2. Phosphoinositide phospholipase C-delta-4
  3. Phospholipase C-delta-4
  4. PLC-delta-4
Enzyme 45 Gene Name PLCD4
Enzyme 45 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
MASLLQDQLTTDQDLLLMQEGMPMRKVRSKSWKKLRYFRLQNDGMTVWHARQARGSAKPS
FSISDVETIRNGHDSELLRSLAEELPLEQGFTIVFHGRRSNLDLMANSVEEAQIWMRGLQ
LLVDLVTSMDHQERLDQWLSDWFQRGDKNQDGKMSFQEVQRLLHLMNVEMDQEYAFSLFQ
AADTSQSGTLEGEEFVQFYKALTKRAEVQELFESFSADGQKLTLLEFLDFLQEEQKERDC
TSELALELIDRYEPSDSGKLRHVLSMDGFLSYLCSKDGDIFNPACLPIYQDMTQPLNHYF
ICSSHNTYLVGDQLCGQSSVEGYIRALKRGCRCVEVDVWDGPSGEPVVYHGHTLTSRILF
KDVVATVAQYAFQTSDYPVILSLETHCSWEQQQTMARHLTEILGEQLLSTTLDGVLPTQL
PSPEELRRKILVKGKKLTLEEDLEYEEEEAEPELEESELALESQFETEPEPQEQNLQNKD
KKKKSKPILCPALSSLVIYLKSVSFRSFTHSKEHYHFYEISSFSETKAKRLIKEAGNEFV
QHNTWQLSRVYPSGLRTDSSNYNPQELWNAGCQMVAMNMQTAGLEMDICDGHFRQNGGCG
YVLKPDFLRDIQSSFHPEKPISPFKAQTLLIQVISGQQLPKVDKTKEGSIVDPLVKVQIF
GVRLDTARQETNYVENNGFNPYWGQTLCFRVLVPELAMLRFVVMDYDWKSRNDFIGQYTL
PWTCMQQGYRHIHLLSKDGISLRPASIFVYICIQEGLEGDES
Enzyme 45 Number of Residues 762
Enzyme 45 Molecular Weight 87584.5
Enzyme 45 Theoretical pI 4.85
Enzyme 45 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 45 General Function Involved in calcium ion binding
Enzyme 45 Specific Function Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Required for acrosome reaction in sperm during fertilization, probably by acting as an important enzyme for intracellular Ca(2+) mobilization in the zona pellucida- induced acrosome reaction. May play a role in cell growth. Modulates the liver regeneration in cooperation with nuclear PKC. Overexpression upregulates the Erk signaling pathway and proliferation
Enzyme 45 Pathways
Enzyme 45 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 62897967 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID Q9BRC7 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name PLCD4_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >2289 bp
ATGGCGTCCCTGCTGCAAGACCAGCTGACCACTGATCAGGACTTGCTGCTGATGCAGGAA
GGCATGCCGATGCGCAAGGTGAGGTCCAAAAGCTGGAAGAAGCTAAGATACTTCAGACTT
CAGAATGACGGCATGACAGTCTGGCATGCACGGCAGGCCAGGGGCAGTGCCAAGCCCAGC
TTCTCAATCTCTGATGTGGAGACAATACGTAATGGCCATGATTCCGAGTTGCTGCGTAGC
CTGGCAGAGGAGCTCCCCCTGGAGCAGGGCTTCACCATTGTCTTCCATGGCCACCGCTCC
AACCTGGACCTGATGGCCAACAGTGTTGAGGAGGCCCAGATATGGATGCGAGGGCTCCAG
CTGTTGGTGGATCTTGTCACCAGCATGGACCATCAGGAGCGCCTGGACCAATGGCTGAGC
GATTGGTTTCAACGTGGAGACAAAAATCAGGATGGTAAGATGAGTTTCCAAGAAGTTCAG
CGGTTATTGCACCTAATGAATGTGGAAATGGACCAAGAATATGCCTTCAGTCTTTTTCAG
GCAGCAGACACGTCCCAGTCTGGAACCCTGGAAGGAGAAGAATTCGTACAGTTCTATAAG
GCATTGACTAAACGTGCTGAGGTGCAGGAACTGTTTGAAAGTTTTTCAGCTGATGGGCAG
AAGCTGACTCTGCTGGAATTTTTGGATTTCCTCCAAGAGGAGCAGAAGGAGAGAGACTGC
ACCTCTGAGCTTGCTCTGGAACTCATTGACCGCTATGAACCTTCAGACAGTGGCAAACTG
CGGCATGTGCTGAGTATGGATGGCTTCCTCAGCTACCTCTGCTCTAAGGATGGAGACATC
TTCAACCCAGCCTGCCTCCCCATCTATCAGGATATGACTCAACCCCTGAACCACTACTTC
ATCTGCTCTTCTCATAACACCTACCTAGTGGGGGACCAGCTTTGCGGCCAGAGCAGCGTC
GAGGGATATATACGGGCCCTGAAGCGGGGGTGCCGCTGCGTGGAGGTGGATGTATGGGAT
GGACCTAGCGGGGAACCTGTCGTTTACCACGGACACACCCTGACCTCCCGCATCCTGTTC
AAAGATGTCGTGGCCACAGTAGCACAGTATGCCTTCCAGACATCAGACTACCCAGTCATC
TTGTCCCTGGAGACCCACTGCAGCTGGGAGCAGCAGCAGACCATGGCCCGTCATCTGACT
GAGATCCTGGGGGAGCAGCTGCTGAGCACCACCTTGGATGGGGTGCTGCCCACTCAGCTG
CCCTCGCCTGAGGAGCTTCGGAGGAAGATCCTGGTGAAGGGGAAGAAGTTAACACTTGAG
GAAGACCTGGAATATGAGGAAGAGGAAGCAGAACCTGAGTTGGAAGAGTCAGAATTGGCG
CTGGAGTCCCAGTTTGAGACTGAGCCTGAGCCCCAGGAGCAGAACCTTCAGAATAAGGAC
AAAAAGAAGAAATCCAAGCCCATCTTGTGTCCAGCCCTCTCTTCCCTGGTTATCTACTTG
AAGTCTGTCTCATTCCGCAGCTTCACACATTCAAAGGAGCACTACCACTTCTACGAGATA
TCATCTTTCTCTGAAACCAAGGCCAAGCGCCTCATCAAGGAGGCTGGCAATGAGTTTGTG
CAGCACAATACTTGGCAGTTAAGCCGTGTGTATCCCAGCGGCCTGAGGACAGACTCTTCC
AACTACAACCCCCAGGAACTCTGGAATGCAGGCTGCCAGATGGTGGCCATGAATATGCAG
ACTGCAGGGCTTGAAATGGACATCTGTGATGGGCATTTCCGCCAGAATGGCGGCTGTGGC
TATGTGCTGAAGCCAGACTTCCTGCGTGATATCCAGAGTTCTTTCCACCCTGAGAAGCCC
ATCAGCCCTTTCAAAGCCCAGACTCTCTTAATCCAGGTGATCAGCGGTCAGCAACTCCCC
AAAGTGGACAAGACCAAAGAGGGGTCCATTGTGGATCCACTGGTGAAAGTGCAGATCTTT
GGCGTTCGTCTAGACACAGCACGGCAGGAGACCAACTATGTGGAGAACAATGGTTTTAAT
CCATACTGGGGGCAGACACTATGTTTCCGGGTGCTGGTGCCTGAACTTGCCATGCTGCGT
TTTGTGGTAATGGATTATGACTGGAAATCCCGAAATGACTTTATTGGTCAGTACACCCTG
CCTTGGACCTGCATGCAACAAGGTTACCGCCACATTCACCTGCTGTCCAAAGATGGCATC
AGCCTCCGCCCAGCTTCCATCTTTGTGTATATCTGCATCCAGGAAGGCCTGGAGGGGGAT
GAGTCCTGA
Enzyme 45 GenBank Gene ID AK223203 Link Image
Enzyme 45 GeneCard ID PLCD4 Link Image
Enzyme 45 GenAtlas ID PLCD4 Link Image
Enzyme 45 HGNC ID HGNC:9062 Link Image
Enzyme 45 Chromosome Location 2
Enzyme 45 Locus 2q35
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Leung DW, Tompkins C, Brewer J, Ball A, Coon M, Morris V, Waggoner D, Singer JW: Phospholipase C delta-4 overexpression upregulates ErbB1/2 expression, Erk signaling pathway, and proliferation in MCF-7 cells. Mol Cancer. 2004 May 13;3:15. [PubMed Link Image]
  2. 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]
  3. Kim H, Suh PG, Ryu SH, Park SH: Assignment of the human PLC delta4 gene (PLCD4) to human chromosome band 2q35 by fluorescence in situ hybridization. Cytogenet Cell Genet. 1999;87(3-4):254-5. [PubMed Link Image]
  4. Landreville S, Coulombe S, Carrier P, Gelb MH, Guerin SL, Salesse C: Expression of phospholipases A2 and C in human corneal epithelial cells. Invest Ophthalmol Vis Sci. 2004 Nov;45(11):3997-4003. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 10048
Enzyme 46 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-1
Enzyme 46 Synonyms
  1. Phosphoinositide phospholipase C-eta-1
  2. Phospholipase C-eta-1
  3. PLC-eta-1
  4. Phospholipase C-like protein 3
  5. PLC-L3
Enzyme 46 Gene Name PLCH1
Enzyme 46 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-1
MADLEVYKNLSPEKVERCMSVMQSGTQMIKLKRGTKGLVRLFYLDEHRTRLRWRPSRKSE
KAKILIDSIYKVTEGRQSEIFHRQAEGNFDPSCCFTIYHGNHMESLDLITSNPEEARTWI
TGLKYLMAGISDEDSLAKRQRTHDQWVKQTFEEADKNGDGLLNIEEIHQLMHKLNVNLPR
RKVRQMFQEADTDENQGTLTFEEFCVFYKMMSLRRDLYLLLLSYSDKKDHLTVEELAQFL
KVEQKMNNVTTDYCLDIIKKFEVSEENKVKNVLGIEGFTNFMRSPACDIFNPLHHEVYQD
MDQPLCNYYIASSHNTYLTGDQLLSQSKVDMYARVLQEGCRCVEVDCWDGPDGEPVVHHG
YTLTSKILFRDVVETINKHAFVKNEFPVILSIENHCSIQQQRKIAQYLKGIFGDKLDLSS
VDTGECKQLPSPQSLKGKILVKGKKLPYHLGDDAEEGEVSDEDSADEIEDECKFKLHYSN
GTTEHQVESFIRKKLESLLKESQIRDKEDPDSFTVRALLKATHEGLNAHLKQSPDVKESG
KKSHGRSLMTNFGKHKKTTKSRSKSYSTDDEEDTQQSTGKEGGQLYRLGRRRKTMKLCRE
LSDLVVYTNSVAAQDIVDDGTTGNVLSFSETRAHQVVQQKSEQFMIYNQKQLTRIYPSAY
RIDSSNFNPLPYWNAGCQLVALNYQSEGRMMQLNRAKFKANGNCGYVLKPQQMCKGTFNP
FSGDPLPANPKKQLILKVISGQQLPKPPDSMFGDRGEIIDPFVEVEIIGLPVDCCKDQTR
VVDDNGFNPVWEETLTFTVHMPEIALVRFLVWDHDPIGRDFVGQRTVTFSSLVPGYRHVY
LEGLTEASIFVHITINEIYGKWSPLILNPSYTILHFLGATKNRQLQGLKGLFNKNPRHSS
SENNSHYVRKRSIGDRILRRTASAPAKGRKKSKMGFQEMVEIKDSVSEATRDQDGVLRRT
TRSLQARPVSMPVDRNLLGALSLPVSETAKDIEGKENSLAEDKDGRRKGKASIKDPHFLN
FNKKLSSSSSALLHKDTSQGDTIVSTAHMSVTGEQLGMSSPRGGRTTSNATSNCQENPCP
SKSLSPKQHLAPDPVVNPTQDLHGVKIKEKGNPEDFVEGKSILSGSVLSHSNLEIKNLEG
NRGKGRAATSFSLSDVSMLCSDIPDLHSTAILQESVISHLIDNVTLTNENEPGSSISALI
GQFDETNNQALTVVSHLHNTSVMSGHCPLPSLGLKMPIKHGFCKGKSKSSFLCSSPELIA
LSSSETTKHATNTVYETTCTPISKTKPDDDLSSKAKTAALESNLPGSPNTSRGWLPKSPT
KGEDWETLKSCSPASSPDLTLEDVIADPTLCFNSGESSLVEIDGESENLSLTTCEYRREG
TSQLASPLKLKYNQGVVEHFQRGLRNGYCKETLRPSVPEIFNNIQDVKTQSISYLAYQGA
GFVHNHFSDSDAKMFQTCVPQQSSAQDMHVPVPKQLAHLPLPALKLPSPCKSKSLGDLTS
EDIACNFESKYQCISKSFVTTGIRDKKGVTVKTKSLEPIDALTEQLRKLVSFDQEDNCQV
LYSKQDANQLPRALVRKLSSRSQSRVRNIASRAKEKQEANKQKVPNPSNGAGVVLRNKPS
APTPAVNRHSTGSYIAGYLKNTKGGGLEGRGIPEGACTALHYGHVDQFCSDNSVLQTEPS
SDDKPEIYFLLRL
Enzyme 46 Number of Residues 1693
Enzyme 46 Molecular Weight 189221.5
Enzyme 46 Theoretical pI 7.79
Enzyme 46 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 46 General Function Involved in calcium ion binding
Enzyme 46 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by calcium-activated phosphatidylinositol-specific phospholipase C enzymes
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 195972871 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID Q4KWH8 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name PLCH1_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >5082 bp
ATGGCAGACCTTGAAGTGTATAAAAACTTAAGTCCAGAAAAAGTTGAAAGATGCATGAGT
GTGATGCAGTCCGGGACACAGATGATCAAGCTGAAACGTGGAACCAAAGGGCTTGTCCGC
CTCTTTTACCTGGATGAGCACCGGACACGCCTCCGATGGCGACCCTCTAGGAAGAGTGAG
AAGGCAAAAATACTTATTGATTCCATTTACAAAGTGACTGAGGGCCGGCAGTCTGAAATA
TTCCACAGACAAGCTGAGGGGAACTTCGACCCCAGCTGCTGCTTCACCATCTACCATGGC
AACCACATGGAGTCCCTGGACCTCATCACCTCCAACCCCGAGGAGGCCCGCACCTGGATC
ACAGGCCTCAAGTACCTGATGGCTGGCATCAGTGATGAAGACTCCCTTGCCAAAAGGCAG
AGGACCCATGACCAATGGGTGAAGCAGACCTTTGAGGAAGCTGATAAGAATGGTGACGGC
TTGCTGAATATTGAAGAGATACATCAGCTGATGCATAAACTGAATGTTAATCTGCCCCGA
AGAAAAGTCAGACAAATGTTTCAGGAAGCCGACACAGATGAGAATCAGGGAACTTTGACA
TTTGAAGAGTTCTGTGTTTTTTACAAAATGATGTCTTTGAGACGAGACCTTTATTTGTTA
CTTTTGAGCTACAGTGACAAGAAAGATCACCTAACTGTGGAAGAACTGGCTCAGTTTTTG
AAGGTGGAGCAAAAGATGAATAATGTGACAACGGACTATTGTCTTGACATCATAAAGAAG
TTTGAAGTTTCAGAAGAAAATAAGGTGAAAAATGTTCTTGGCATAGAAGGCTTCACGAAC
TTCATGCGTAGTCCTGCCTGTGACATATTTAACCCATTGCACCATGAAGTGTACCAAGAC
ATGGATCAGCCCCTCTGCAACTACTACATTGCTTCCTCTCACAATACATACCTGACTGGA
GACCAGCTCCTTTCTCAGTCCAAAGTGGATATGTATGCACGGGTGCTGCAAGAGGGCTGT
CGCTGTGTGGAAGTTGACTGTTGGGATGGCCCAGATGGAGAGCCAGTAGTACATCATGGT
TACACTCTCACTTCAAAAATTCTCTTCAGAGATGTTGTGGAGACCATCAACAAGCATGCC
TTTGTGAAGAATGAGTTTCCTGTTATATTGTCTATCGAGAATCACTGCAGTATCCAGCAG
CAAAGGAAGATTGCTCAGTACCTGAAAGGAATATTCGGAGACAAACTGGACCTGTCATCT
GTTGATACAGGGGAGTGCAAGCAGCTTCCAAGCCCTCAAAGTTTGAAAGGCAAAATTCTA
GTGAAGGGTAAGAAGTTGCCTTATCACCTTGGGGATGATGCAGAGGAAGGGGAAGTTTCT
GATGAGGACAGTGCAGATGAAATTGAAGACGAGTGCAAATTCAAGCTCCATTATAGTAAT
GGGACCACTGAGCATCAGGTGGAATCTTTCATAAGGAAAAAACTGGAGTCACTGTTAAAA
GAATCTCAAATTCGAGATAAAGAAGATCCTGATAGTTTCACAGTGCGGGCACTACTGAAG
GCCACGCATGAAGGCTTAAATGCACACCTGAAGCAGAGTCCAGATGTAAAGGAAAGTGGA
AAGAAATCACATGGACGATCCCTCATGACCAACTTTGGAAAACATAAGAAAACTACAAAA
TCACGGTCTAAATCTTACAGTACTGATGATGAGGAAGACACACAGCAGAGTACTGGCAAG
GAGGGTGGCCAGCTGTACAGATTGGGTCGCCGAAGGAAAACCATGAAGCTCTGCCGAGAA
CTCTCTGATTTGGTTGTGTACACAAACTCCGTGGCCGCTCAGGACATTGTGGATGACGGA
ACCACAGGAAATGTGTTATCATTCAGTGAAACAAGAGCACATCAGGTTGTTCAGCAAAAA
TCAGAGCAGTTCATGATTTATAATCAAAAGCAACTCACGAGGATTTACCCCTCTGCCTAC
CGCATTGATTCCAGTAACTTCAACCCTCTCCCCTACTGGAACGCAGGCTGCCAGCTAGTG
GCACTGAATTATCAATCTGAAGGACGAATGATGCAGTTAAACCGAGCCAAATTCAAGGCA
AATGGCAATTGTGGCTATGTCCTCAAACCCCAGCAAATGTGCAAAGGTACTTTCAACCCT
TTCTCTGGTGACCCTCTTCCTGCCAACCCCAAAAAGCAGCTCATCCTGAAAGTTATCAGT
GGACAGCAACTCCCCAAACCTCCAGACTCCATGTTTGGAGATCGAGGCGAGATCATTGAC
CCTTTTGTTGAAGTTGAAATTATTGGATTGCCAGTAGATTGTTGTAAAGATCAAACCCGT
GTGGTAGATGACAATGGATTTAACCCTGTGTGGGAAGAAACACTGACATTTACAGTACAC
ATGCCAGAAATAGCTTTGGTTCGGTTCCTTGTGTGGGATCACGATCCCATTGGACGAGAC
TTTGTTGGACAAAGAACTGTGACCTTCAGCAGCTTAGTGCCTGGCTACCGGCATGTCTAT
TTGGAAGGACTGACAGAAGCATCCATATTTGTACACATAACCATCAATGAAATCTATGGA
AAGTGGAGCCCTTTAATACTCAACCCCAGTTATACTATATTGCACTTTCTAGGAGCTACA
AAGAACAGACAACTCCAGGGTCTGAAGGGACTGTTCAATAAGAATCCTAGGCACAGTTCT
TCAGAAAACAATTCCCATTATGTACGGAAGCGATCCATTGGAGATAGAATTCTGCGACGC
ACAGCTAGCGCCCCAGCCAAAGGCAGGAAAAAGAGCAAAATGGGCTTCCAAGAAATGGTG
GAGATAAAGGATTCTGTGTCCGAGGCCACAAGAGATCAAGATGGCGTGCTGAGGAGGACC
ACACGCAGTTTGCAAGCACGCCCTGTCTCTATGCCTGTTGACAGAAACCTTCTGGGAGCT
TTGTCGCTGCCTGTATCTGAAACAGCAAAAGACATTGAAGGAAAAGAAAACTCTCTAGCA
GAAGATAAAGATGGCAGAAGAAAAGGGAAAGCAAGTATAAAAGATCCACATTTTCTAAAT
TTCAACAAAAAGTTATCATCCTCCTCCAGTGCTCTGCTCCACAAAGATACCAGCCAAGGG
GACACCATTGTATCTACTGCCCACATGTCAGTCACAGGAGAACAGCTGGGCATGTCAAGT
CCTAGGGGTGGGAGAACCACATCAAATGCCACAAGCAATTGCCAGGAAAACCCCTGTCCC
AGCAAGTCTCTCTCCCCAAAGCAGCATTTGGCTCCCGATCCTGTAGTTAACCCCACACAA
GATCTGCATGGTGTGAAAATCAAGGAAAAGGGTAATCCTGAGGACTTTGTGGAAGGGAAA
AGCATCTTGTCAGGAAGCGTCCTTTCTCATAGCAACCTAGAAATTAAGAACCTGGAAGGT
AATAGGGGTAAGGGCCGAGCTGCAACATCCTTTTCTTTGTCAGACGTCTCCATGCTCTGT
TCTGACATACCTGACCTACATTCAACTGCAATTCTGCAGGAGAGTGTAATTTCCCATCTT
ATTGACAATGTCACTTTAACAAATGAGAATGAGCCGGGCAGTTCCATCTCAGCCCTGATT
GGCCAGTTTGATGAGACCAACAATCAGGCTCTCACAGTTGTTTCTCATCTTCATAATACC
AGTGTGATGTCAGGCCATTGTCCCTTGCCTAGCCTGGGCCTAAAAATGCCCATCAAGCAT
GGTTTTTGCAAGGGAAAATCCAAGTCTTCCTTCCTGTGCTCATCTCCGGAGCTGATAGCA
CTCTCGAGTTCTGAGACCACCAAACATGCAACGAACACAGTTTATGAAACTACCTGCACT
CCCATCTCTAAAACCAAACCAGATGATGACCTTTCTAGTAAGGCCAAGACAGCGGCCTTA
GAAAGCAACCTGCCTGGATCCCCTAATACTTCTCGTGGCTGGTTACCAAAAAGTCCTACC
AAGGGAGAAGACTGGGAAACACTGAAGAGCTGCAGCCCTGCCTCTTCCCCTGATTTGACC
CTGGAGGATGTAATAGCTGATCCCACTCTCTGTTTCAATTCTGGGGAGAGCAGCCTTGTG
GAAATTGATGGAGAATCAGAAAATCTTTCTCTAACAACCTGTGAATATAGGAGAGAGGGC
ACAAGTCAACTTGCTTCTCCTTTAAAACTCAAGTACAATCAGGGTGTGGTAGAACACTTT
CAAAGAGGTTTGAGAAACGGCTACTGTAAAGAGACCCTCCGCCCTTCTGTCCCTGAAATA
TTCAACAATATTCAAGATGTCAAAACTCAAAGTATTTCTTATCTAGCCTATCAGGGTGCT
GGCTTTGTGCATAATCATTTCTCAGATTCAGATGCAAAAATGTTCCAGACCTGTGTGCCC
CAGCAATCTAGTGCTCAAGATATGCATGTCCCTGTACCCAAGCAGTTGGCACATCTTCCT
TTGCCTGCTCTGAAACTGCCTAGTCCTTGCAAATCCAAAAGTCTGGGGGACTTAACATCA
GAGGACATTGCCTGCAATTTTGAGAGCAAGTACCAGTGTATTAGTAAGAGTTTTGTTACA
ACTGGCATTAGAGACAAGAAGGGCGTGACTGTGAAGACAAAGTCGTTAGAGCCTATAGAT
GCCCTGACCGAGCAGCTTCGGAAGCTTGTGTCCTTTGACCAGGAAGACAACTGCCAAGTG
CTATATTCAAAGCAGGATGCCAATCAGCTCCCCCGGGCACTGGTCAGGAAGTTGTCATCC
AGAAGTCAGAGCAGAGTGCGCAATATTGCTAGTCGTGCCAAGGAGAAACAGGAAGCCAAC
AAGCAGAAAGTTCCAAACCCCAGCAATGGGGCAGGAGTGGTTCTTAGAAACAAACCCTCA
GCACCCACCCCTGCAGTGAATCGCCACTCCACCGGCTCCTACATCGCAGGCTACCTGAAG
AACACGAAAGGGGGTGGCCTTGAAGGCCGGGGCATCCCAGAGGGGGCATGCACGGCTCTT
CACTATGGCCACGTTGACCAGTTTTGTTCAGATAATTCTGTTTTGCAGACTGAGCCAAGC
AGTGATGATAAACCAGAAATTTATTTTCTTTTGAGACTGTGA
Enzyme 46 GenBank Gene ID NM_001130960.1 Link Image
Enzyme 46 GeneCard ID PLCH1 Link Image
Enzyme 46 GenAtlas ID PLCH1 Link Image
Enzyme 46 HGNC ID HGNC:29185 Link Image
Enzyme 46 Chromosome Location 3
Enzyme 46 Locus 3q25.31
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Hwang JI, Oh YS, Shin KJ, Kim H, Ryu SH, Suh PG: Molecular cloning and characterization of a novel phospholipase C, PLC-eta. Biochem J. 2005 Jul 1;389(Pt 1):181-6. [PubMed Link Image]
  2. 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]
  3. Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed Link Image]
  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. 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]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 10049
Enzyme 47 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1
Enzyme 47 Synonyms
  1. Pancreas-enriched phospholipase C
  2. Phosphoinositide phospholipase C-epsilon-1
  3. Phospholipase C-epsilon-1
  4. PLC-epsilon-1
Enzyme 47 Gene Name PLCE1
Enzyme 47 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1
MTSEEMTASVLIPVTQRKVVSAQSAADESSEKVSDINISKAHTVRRSGETSHTISQLNKL
KEEPSGSNLPKILSIAREKIVSDENSNEKCWEKIMPDSAKNLNINCNNILRNHQHGLPQR
QFYEMYNSVAEEDLCLETGIPSPLERKVFPGIQLELDRPSMGISPLGNQSVIIETGRAHP
DSRRAVFHFHYEVDRRMSDTFCTLSENLILDDCGNCVPLPGGEEKQKKNYVAYTCKLMEL
AKNCDNKNEQLQCDHCDTLNDKYFCFEGSCEKVDMVYSGDSFCRKDFTDSQAAKTFLSHF
EDFPDNCDDVEEDAFKSKKERSTLLVRRFCKNDREVKKSVYTGTRAIVRTLPSGHIGLTA
WSYIDQKRNGPLLPCGRVMEPPSTVEIRQDGSQRLSEAQWYPIYNAVRREETENTVGSLL
HFLTKLPASETAHGRISVGPCLKQCVRDTVCEYRATLQRTSISQYITGSLLEATTSLGAR
SGLLSTFGGSTGRMMLKERQPGPSVANSNALPSSSAGISKELIDLQPLIQFPEEVASILM
EQEQTIYRRVLPVDYLCFLTRDLGTPECQSSLPCLKASISASILTTQNGEHNALEDLVMR
FNEVSSWVTWLILTAGSMEEKREVFSYLVHVAKCCWNMGNYNAVMEFLAGLRSRKVLKMW
QFMDQSDIETMRSLKDAMAQHESSCEYRKVVTRALHIPGCKVVPFCGVFLKELCEVLDGA
SGLMKLCPRYNSQEETLEFVADYSGQDNFLQRVGQNGLKNSEKESTVNSIFQVIRSCNRS
LETDEEDSPSEGNSSRKSSLKDKSRWQFIIGDLLDSDNDIFEQSKEYDSHGSEDSQKAFD
HGTELIPWYVLSIQADVHQFLLQGATVIHYDQDTHLSARCFLQLQPDNSTLTWVKPTTAS
PASSKAKLGVLNNTAEPGKFPLLGNAGLSSLTEGVLDLFAVKAVYMGHPGIDIHTVCVQN
KLGSMFLSETGVTLLYGLQTTDNRLLHFVAPKHTAKMLFSGLLELTRAVRKMRKFPDQRQ
QWLRKQYVSLYQEDGRYEGPTLAHAVELFGGRRWSARNPSPGTSAKNAEKPNMQRNNTLG
ISTTKKKKKILMRGESGEVTDDEMATRKAKMHKECRSRSGSDPQDINEQEESEVNAIANP
PNPLPSRRAHSLTTAGSPNLAAGTSSPIRPVSSPVLSSSNKSPSSAWSSSSWHGRIKGGM
KGFQSFMVSDSNMSFVEFVELFKSFSVRSRKDLKDLFDVYAVPCNRSGSESAPLYTNLTI
DENTSDLQPDLDLLTRNVSDLGLFIKSKQQLSDNQRQISDAIAAASIVTNGTGIESTSLG
IFGVGILQLNDFLVNCQGEHCTYDEILSIIQKFEPSISMCHQGLMSFEGFARFLMDKENF
ASKNDESQENIKELQLPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLQGCRSVELDC
WDGDDGMPIIYHGHTLTTKIPFKEVVEAIDRSAFINSDLPIIISIENHCSLPQQRKMAEI
FKTVFGEKLVTKFLFETDFSDDPMLPSPDQLRKKVLLKNKKLKAHQTPVDILKQKAHQLA
SMQVQAYNGGNANPRPANNEEEEDEEDEYDYDYESLSDDNILEDRPENKSCNDKLQFEYN
EEIPKRIKKADNSACNKGKVYDMELGEEFYLDQNKKESRQIAPELSDLVIYCQAVKFPGL
STLNASGSSRGKERKSRKSIFGNNPGRMSPGETASFNKTSGKSSCEGIRQTWEESSSPLN
PTTSLSAIIRTPKCYHISSLNENAAKRLCRRYSQKLTQHTACQLLRTYPAATRIDSSNPN
PLMFWLHGIQLVALNYQTDDLPLHLNAAMFEANGGCGYVLKPPVLWDKNCPMYQKFSPLE
RDLDSMDPAVYSLTIVSGQNVCPSNSMGSPCIEVDVLGMPLDSCHFRTKPIHRNTLNPMW
NEQFLFHVHFEDLVFLRFAVVENNSSAVTAQRIIPLKALKRGYRHLQLRNLHNEVLEISS
LFINSRRMEENSSGNTMSASSMFNTEERKCLQTHRVTVHGVPGPEPFTVFTINGGTKAKQ
LLQQILTNEQDIKPVTTDYFLMEEKYFISKEKNECRKQPFQRAIGPEEEIMQILSSWFPE
EGYMGRIVLKTQQENLEEKNIVQDDKEVILSSEEESFFVQVHDVSPEQPRTVIKAPRVST
AQDVIQQTLCKAKYSYSILSNPNPSDYVLLEEVVKDTTNKKTTTPKSSQRVLLDQECVFQ
AQSKWKGAGKFILKLKEQVQASREDKKKGISFASELKKLTKSTKQPRGLTSPSQLLTSES
IQTKEEKPVGGLSSSDTMDYRQ
Enzyme 47 Number of Residues 2302
Enzyme 47 Molecular Weight 258712.3
Enzyme 47 Theoretical pI 6.44
Enzyme 47 GO Classification
Function
  • GTPase regulator activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • nucleoside-triphosphatase regulator activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signal transduction
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 47 General Function Involved in calcium ion binding
Enzyme 47 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. PLCE1 is a bifunctional enzyme which also regulates small GTPases of the Ras superfamily through its Ras guanine- exchange factor (RasGEF) activity. As an effector of heterotrimeric and small G-protein, it may play a role in cell survival, cell growth, actin organization and T-cell activation
Enzyme 47 Pathways
Enzyme 47 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 117168250 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID Q9P212 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name PLCE1_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >6909 bp
ATGACTTCTGAAGAAATGACAGCTTCTGTTCTCATACCTGTGACTCAGAGAAAAGTGGTT
TCTGCCCAGTCGGCTGCAGATGAAAGTAGTGAAAAGGTCTCAGACATCAATATTTCAAAA
GCACATACTGTCAGACGAAGTGGGGAGACTTCTCATACCATCTCACAACTGAACAAACTT
AAAGAAGAACCTTCTGGAAGCAACTTGCCAAAGATTCTCTCAATAGCGAGGGAGAAAATA
GTGAGTGATGAGAACAGTAATGAAAAATGTTGGGAGAAAATCATGCCAGATTCTGCGAAA
AACCTTAACATTAACTGCAACAACATATTGAGAAACCATCAGCATGGCCTTCCTCAGAGA
CAATTTTATGAAATGTACAACTCTGTTGCTGAGGAAGACTTGTGTTTAGAAACTGGAATT
CCTTCTCCACTGGAAAGAAAGGTGTTCCCTGGAATTCAACTGGAACTAGACAGACCTTCC
ATGGGCATTAGTCCTTTAGGAAATCAGTCAGTGATCATAGAGACAGGCAGAGCACACCCT
GACAGCAGAAGGGCAGTATTTCATTTTCATTATGAAGTTGACAGAAGAATGTCAGACACT
TTCTGTACCCTATCAGAAAACTTAATTTTAGACGATTGTGGAAATTGTGTACCACTACCT
GGGGGTGAGGAGAAGCAAAAGAAAAACTATGTGGCATATACCTGTAAACTGATGGAATTG
GCCAAAAATTGTGATAATAAGAATGAGCAGCTGCAGTGTGATCATTGTGACACCTTGAAT
GATAAATACTTTTGCTTTGAAGGCTCTTGTGAGAAGGTTGACATGGTATATTCAGGTGAT
AGCTTTTGTAGGAAAGACTTTACTGACAGTCAAGCTGCCAAGACCTTTTTGAGCCATTTT
GAGGACTTCCCTGATAATTGTGATGATGTAGAAGAAGACGCTTTTAAAAGCAAAAAGGAG
CGATCCACTTTGTTAGTCAGGAGATTCTGTAAAAATGACAGAGAAGTTAAGAAATCTGTG
TATACTGGAACAAGAGCAATTGTGAGAACTCTGCCTTCTGGCCACATTGGGCTGACTGCA
TGGAGTTACATAGATCAGAAGAGAAATGGTCCCTTACTGCCTTGTGGGAGAGTAATGGAA
CCCCCGTCAACAGTGGAGATAAGGCAAGATGGGAGCCAACGTCTGTCAGAAGCCCAGTGG
TATCCTATCTACAATGCAGTGAGAAGAGAAGAAACAGAAAATACAGTTGGATCTCTACTC
CATTTCCTCACCAAGCTCCCAGCCTCCGAGACAGCCCATGGAAGGATAAGCGTTGGTCCA
TGCTTAAAGCAATGTGTCCGAGACACTGTATGTGAGTATCGCGCCACCCTCCAAAGGACT
TCAATATCGCAGTACATCACCGGTTCTCTCCTAGAAGCAACCACGTCTTTGGGAGCAAGA
AGTGGCCTTCTCAGTACTTTTGGAGGATCCACTGGACGAATGATGCTGAAAGAACGCCAG
CCAGGCCCCTCTGTGGCCAATTCCAATGCCCTCCCTTCAAGTTCAGCTGGGATCAGCAAG
GAGCTGATCGATCTGCAGCCTCTCATCCAGTTCCCAGAGGAAGTCGCCAGCATCCTGATG
GAGCAAGAGCAGACTATTTACCGCAGGGTCTTGCCAGTCGACTACCTTTGCTTCTTAACA
CGGGACTTGGGCACTCCTGAATGCCAGAGCTCCTTGCCCTGCCTCAAAGCATCCATCTCA
GCGTCGATTCTTACCACTCAGAATGGAGAGCACAATGCCCTTGAAGATCTGGTGATGAGG
TTTAATGAGGTGAGCTCCTGGGTGACATGGCTGATCCTCACGGCAGGCTCCATGGAGGAG
AAGCGAGAAGTCTTTTCATATTTGGTGCATGTGGCCAAATGCTGCTGGAACATGGGCAAC
TACAACGCTGTCATGGAGTTCTTGGCTGGCCTCAGGTCAAGAAAAGTTTTAAAAATGTGG
CAGTTCATGGACCAGTCTGATATTGAGACCATGAGGAGCCTGAAGGATGCTATGGCCCAG
CATGAGTCCTCTTGTGAGTACAGAAAGGTGGTGACACGTGCCCTGCACATCCCTGGCTGT
AAGGTGGTTCCATTCTGTGGGGTGTTTCTGAAGGAGCTCTGTGAAGTGCTTGACGGCGCC
TCCGGTCTCATGAAGCTTTGCCCGCGGTACAATTCCCAAGAAGAAACTTTAGAGTTTGTA
GCAGATTACAGTGGACAAGATAATTTCTTACAACGAGTGGGACAAAATGGCTTAAAGAAT
TCGGAGAAGGAGTCCACTGTCAACAGCATCTTTCAGGTCATCCGGAGCTGCAATCGAAGT
CTGGAGACAGACGAGGAGGACAGCCCCAGTGAAGGAAACAGCTCCAGGAAAAGCTCCTTG
AAGGATAAAAGCCGATGGCAGTTTATAATTGGAGATTTGTTGGATTCAGACAATGACATC
TTTGAGCAATCCAAAGAATACGACTCTCATGGTTCAGAGGACTCACAGAAGGCCTTCGAC
CATGGGACGGAGCTCATCCCTTGGTACGTGCTGTCCATCCAAGCCGATGTGCACCAGTTC
CTGCTGCAGGGGGCCACGGTCATCCACTACGACCAGGACACACACCTCTCTGCCCGCTGC
TTCCTCCAGCTTCAGCCCGACAATAGCACCTTGACCTGGGTAAAGCCCACAACTGCCTCC
CCAGCCAGCAGTAAAGCAAAACTTGGTGTACTTAATAACACAGCTGAGCCTGGAAAATTC
CCACTACTGGGTAATGCTGGATTAAGTAGCCTGACGGAAGGGGTCTTGGATCTTTTTGCA
GTGAAGGCTGTATACATGGGCCACCCTGGCATTGATATACACACTGTGTGTGTTCAGAAC
AAACTGGGTAGCATGTTCCTGTCAGAGACTGGTGTGACATTGCTCTATGGGCTTCAGACC
ACAGACAACAGATTATTGCACTTCGTGGCACCAAAGCACACAGCTAAAATGCTCTTCAGC
GGATTATTGGAACTCACTAGAGCTGTGAGAAAGATGAGGAAATTCCCTGACCAAAGACAG
CAGTGGCTGCGGAAACAGTACGTCAGCCTTTATCAGGAGGATGGACGGTATGAAGGCCCA
ACTTTGGCTCACGCTGTGGAGTTGTTTGGTGGCAGACGGTGGAGTGCTCGAAACCCCAGC
CCCGGAACATCAGCAAAGAATGCTGAGAAGCCCAATATGCAGAGAAACAATACCCTGGGC
ATAAGCACTACCAAGAAAAAGAAGAAAATCCTCATGAGGGGTGAGAGTGGAGAGGTAACT
GACGATGAGATGGCAACCCGAAAGGCCAAGATGCACAAAGAGTGTCGAAGCCGGAGTGGT
TCTGATCCTCAAGACATTAATGAACAAGAAGAATCAGAGGTGAATGCCATCGCTAACCCT
CCAAACCCCCTCCCTTCCAGAAGAGCCCACTCTTTGACCACAGCTGGGTCCCCCAACTTG
GCTGCCGGGACGTCATCTCCCATCAGGCCAGTGTCCTCCCCTGTGCTGTCTTCTTCAAAC
AAGAGCCCATCCAGTGCTTGGAGCAGTAGTAGCTGGCACGGGCGGATCAAAGGCGGCATG
AAGGGATTTCAGAGCTTCATGGTTTCAGATAGCAACATGAGTTTTGTTGAATTTGTTGAG
CTGTTCAAATCATTCAGTGTCAGGAGCCGCAAGGACCTGAAGGATCTGTTTGATGTCTAT
GCAGTGCCCTGCAACCGATCTGGCTCCGAGTCAGCCCCACTCTACACCAACCTGACAATT
GATGAAAACACCAGCGATCTTCAGCCTGACCTAGATCTGTTGACCAGAAATGTCTCGGAT
TTGGGGTTGTTCATTAAGAGTAAACAGCAGCTATCGGACAACCAGAGGCAGATATCTGAT
GCCATTGCTGCTGCAAGCATTGTGACAAATGGCACTGGGATTGAGAGCACATCTCTGGGC
ATTTTTGGGGTGGGCATACTTCAGCTCAACGATTTCCTCGTGAATTGCCAAGGAGAACAC
TGCACTTATGATGAAATCCTCAGCATCATCCAGAAGTTCGAGCCTAGCATCAGTATGTGT
CATCAGGGACTAATGTCATTTGAAGGGTTTGCCAGGTTTCTGATGGATAAAGAAAATTTT
GCCTCAAAAAATGATGAGTCACAGGAGAACATTAAAGAACTGCAGCTACCCCTCTCATAC
TATTACATCGAATCTTCGCACAATACCTACCTCACGGGCCATCAGCTCAAAGGAGAATCC
TCGGTAGAACTCTACAGCCAGGTCCTTTTGCAAGGCTGTCGAAGTGTAGAATTGGACTGC
TGGGACGGAGACGATGGGATGCCCATCATTTATCATGGACATACGCTGACAACCAAGATC
CCCTTCAAGGAAGTGGTTGAAGCCATTGATCGCAGTGCCTTCATCAACTCTGACCTGCCA
ATCATCATATCGATTGAGAACCACTGTTCATTGCCTCAGCAACGAAAAATGGCAGAAATT
TTCAAGACTGTGTTTGGAGAAAAGCTGGTGACTAAATTCTTATTTGAGACTGATTTCTCA
GATGATCCAATGCTTCCTTCACCTGACCAACTCAGAAAGAAAGTTCTTCTTAAAAACAAG
AAGCTAAAAGCCCATCAGACGCCAGTGGATATCTTAAAGCAAAAGGCTCATCAGTTAGCA
TCTATGCAAGTGCAGGCTTATAATGGTGGGAATGCCAACCCCCGACCTGCCAATAATGAG
GAAGAGGAAGATGAGGAGGACGAATATGATTATGACTATGAATCCCTTTCTGATGACAAC
ATTCTGGAAGACAGACCTGAAAATAAATCATGTAATGACAAGCTTCAGTTTGAATATAAT
GAAGAAATCCCAAAGAGGATAAAGAAAGCAGATAACTCTGCTTGCAACAAAGGAAAGGTT
TATGATATGGAACTGGGAGAAGAATTTTATCTTGATCAGAATAAAAAGGAAAGCAGACAG
ATTGCACCAGAGCTTTCTGACCTTGTAATCTATTGTCAAGCAGTAAAATTTCCAGGACTG
TCAACTCTAAATGCATCTGGCTCTAGCAGAGGAAAAGAAAGGAAAAGCAGGAAGTCCATT
TTTGGCAACAATCCGGGCAGAATGAGCCCAGGGGAGACAGCATCATTTAACAAAACATCT
GGAAAAAGTTCCTGTGAAGGCATTCGACAGACCTGGGAGGAATCTTCTTCCCCTCTCAAC
CCAACCACGTCCCTCAGTGCTATCATTAGAACTCCCAAATGTTATCATATCTCGTCGCTG
AATGAAAATGCCGCCAAACGTCTGTGTCGCAGGTATTCTCAGAAACTGACCCAGCACACC
GCCTGTCAGCTGCTGAGAACTTACCCTGCTGCCACCCGCATCGACTCTTCCAACCCGAAC
CCCCTCATGTTCTGGCTCCATGGGATACAGCTTGTGGCACTCAACTACCAGACTGATGAT
CTCCCTTTACATTTAAATGCTGCAATGTTTGAGGCAAATGGTGGTTGTGGTTATGTATTG
AAACCTCCAGTTCTGTGGGACAAGAACTGCCCCATGTATCAGAAGTTTTCTCCACTAGAA
AGAGATCTGGACAGCATGGATCCTGCAGTCTATTCTTTAACTATTGTCTCTGGTCAGAAT
GTGTGCCCCAGTAATAGCATGGGAAGCCCGTGCATTGAAGTCGACGTCCTGGGCATGCCT
CTGGACAGCTGCCATTTCCGCACAAAGCCCATCCATCGAAACACCCTGAACCCCATGTGG
AACGAGCAGTTTCTGTTCCACGTTCACTTCGAAGATCTTGTATTTCTTCGTTTTGCAGTT
GTGGAAAACAATAGTTCAGCGGTAACTGCTCAGAGAATCATTCCACTGAAAGCTTTAAAA
CGAGGATATCGACATCTTCAGCTGCGAAACCTTCACAATGAAGTCTTGGAGATTTCTAGT
TTATTCATTAACAGCAGAAGGATGGAAGAAAATTCCTCTGGCAATACCATGTCAGCCTCT
TCGATGTTTAATACAGAAGAAAGAAAATGTTTGCAGACTCACAGAGTCACGGTGCATGGG
GTCCCAGGGCCAGAGCCCTTTACCGTTTTCACTATTAATGGAGGCACCAAGGCAAAGCAG
CTTCTGCAGCAAATTCTGACAAATGAACAAGACATCAAACCTGTTACCACAGACTATTTT
TTGATGGAAGAAAAATATTTTATATCTAAAGAAAAGAATGAATGTAGGAAACAACCATTC
CAGAGAGCCATTGGTCCAGAAGAGGAGATCATGCAAATTTTAAGCAGCTGGTTTCCAGAA
GAGGGATACATGGGCAGGATTGTCTTAAAAACCCAGCAGGAAAACCTAGAAGAGAAAAAC
ATTGTTCAAGATGACAAAGAGGTGATCTTGAGCTCAGAGGAGGAGAGTTTCTTTGTCCAA
GTGCATGATGTTTCTCCAGAGCAACCTCGAACAGTCATCAAAGCACCCCGCGTCAGCACT
GCACAGGATGTCATTCAGCAGACCTTATGCAAAGCCAAATATTCCTACAGCATCCTGAGC
AACCCCAATCCAAGCGACTATGTGCTTTTGGAAGAGGTGGTGAAAGACACTACCAACAAG
AAGACTACCACACCAAAGTCCTCTCAGCGGGTCCTTCTGGATCAGGAGTGTGTGTTTCAA
GCCCAAAGCAAGTGGAAAGGTGCAGGAAAATTCATCCTTAAGCTAAAGGAGCAGGTGCAG
GCATCTCGAGAAGATAAAAAGAAAGGCATTTCTTTCGCAAGTGAACTCAAGAAGCTCACC
AAGTCAACTAAACAGCCCCGAGGACTTACATCACCTTCTCAGCTCTTGACCTCAGAAAGT
ATCCAAACCAAGGAGGAGAAACCTGTGGGTGGCTTGTCCTCCAGTGACACAATGGATTAC
CGACAGTGA
Enzyme 47 GenBank Gene ID NM_016341.3 Link Image
Enzyme 47 GeneCard ID PLCE1 Link Image
Enzyme 47 GenAtlas ID PLCE1 Link Image
Enzyme 47 HGNC ID HGNC:17175 Link Image
Enzyme 47 Chromosome Location 1
Enzyme 47 Locus 10q23
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. Song C, Hu CD, Masago M, Kariyai K, Yamawaki-Kataoka Y, Shibatohge M, Wu D, Satoh T, Kataoka T: Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras. J Biol Chem. 2001 Jan 26;276(4):2752-7. Epub 2000 Oct 5. [PubMed Link Image]
  2. Lopez I, Mak EC, Ding J, Hamm HE, Lomasney JW: A novel bifunctional phospholipase c that is regulated by Galpha 12 and stimulates the Ras/mitogen-activated protein kinase pathway. J Biol Chem. 2001 Jan 26;276(4):2758-65. Epub 2000 Oct 5. [PubMed Link Image]
  3. Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed Link Image]
  4. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [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. 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]
  7. Jin TG, Satoh T, Liao Y, Song C, Gao X, Kariya K, Hu CD, Kataoka T: Role of the CDC25 homology domain of phospholipase Cepsilon in amplification of Rap1-dependent signaling. J Biol Chem. 2001 Aug 10;276(32):30301-7. Epub 2001 Jun 6. [PubMed Link Image]
  8. Schmidt M, Evellin S, Weernink PA, von Dorp F, Rehmann H, Lomasney JW, Jakobs KH: A new phospholipase-C-calcium signalling pathway mediated by cyclic AMP and a Rap GTPase. Nat Cell Biol. 2001 Nov;3(11):1020-4. [PubMed Link Image]
  9. Evellin S, Nolte J, Tysack K, vom Dorp F, Thiel M, Weernink PA, Jakobs KH, Webb EJ, Lomasney JW, Schmidt M: Stimulation of phospholipase C-epsilon by the M3 muscarinic acetylcholine receptor mediated by cyclic AMP and the GTPase Rap2B. J Biol Chem. 2002 May 10;277(19):16805-13. Epub 2002 Mar 4. [PubMed Link Image]
  10. Song C, Satoh T, Edamatsu H, Wu D, Tadano M, Gao X, Kataoka T: Differential roles of Ras and Rap1 in growth factor-dependent activation of phospholipase C epsilon. Oncogene. 2002 Nov 21;21(53):8105-13. [PubMed Link Image]
  11. Czyzyk J, Brogdon JL, Badou A, Henegariu O, Preston Hurlburt P, Flavell R, Bottomly K: Activation of CD4 T cells by Raf-independent effectors of Ras. Proc Natl Acad Sci U S A. 2003 May 13;100(10):6003-8. Epub 2003 Apr 29. [PubMed Link Image]
  12. vom Dorp F, Sari AY, Sanders H, Keiper M, Oude Weernink PA, Jakobs KH, Schmidt M: Inhibition of phospholipase C-epsilon by Gi-coupled receptors. Cell Signal. 2004 Aug;16(8):921-8. [PubMed Link Image]
  13. Wang H, Oestreich EA, Maekawa N, Bullard TA, Vikstrom KL, Dirksen RT, Kelley GG, Blaxall BC, Smrcka AV: Phospholipase C epsilon modulates beta-adrenergic receptor-dependent cardiac contraction and inhibits cardiac hypertrophy. Circ Res. 2005 Dec 9;97(12):1305-13. Epub 2005 Nov 17. [PubMed Link Image]
  14. Sorli SC, Bunney TD, Sugden PH, Paterson HF, Katan M: Signaling properties and expression in normal and tumor tissues of two phospholipase C epsilon splice variants. Oncogene. 2005 Jan 6;24(1):90-100. [PubMed Link Image]
  15. Ada-Nguema AS, Xenias H, Hofman JM, Wiggins CH, Sheetz MP, Keely PJ: The small GTPase R-Ras regulates organization of actin and drives membrane protrusions through the activity of PLCepsilon. J Cell Sci. 2006 Apr 1;119(Pt 7):1307-19. Epub 2006 Mar 14. [PubMed Link Image]
  16. Bunney TD, Harris R, Gandarillas NL, Josephs MB, Roe SM, Sorli SC, Paterson HF, Rodrigues-Lima F, Esposito D, Ponting CP, Gierschik P, Pearl LH, Driscoll PC, Katan M: Structural and mechanistic insights into ras association domains of phospholipase C epsilon. Mol Cell. 2006 Feb 17;21(4):495-507. [PubMed Link Image]
  17. Hinkes B, Wiggins RC, Gbadegesin R, Vlangos CN, Seelow D, Nurnberg G, Garg P, Verma R, Chaib H, Hoskins BE, Ashraf S, Becker C, Hennies HC, Goyal M, Wharram BL, Schachter AD, Mudumana S, Drummond I, Kerjaschki D, Waldherr R, Dietrich A, Ozaltin F, Bakkaloglu A, Cleper R, Basel-Vanagaite L, Pohl M, Griebel M, Tsygin AN, Soylu A, Muller D, Sorli CS, Bunney TD, Katan M, Liu J, Attanasio M, O'toole JF, Hasselbacher K, Mucha B, Otto EA, Airik R, Kispert A, Kelley GG, Smrcka AV, Gudermann T, Holzman LB, Nurnberg P, Hildebrandt F: Positional cloning uncovers mutations in PLCE1 responsible for a nephrotic syndrome variant that may be reversible. Nat Genet. 2006 Dec;38(12):1397-405. Epub 2006 Nov 5. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 10050
Enzyme 48 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
Enzyme 48 Synonyms
  1. Phosphoinositide phospholipase C-delta-3
  2. Phospholipase C-delta-3
  3. PLC-delta-3
Enzyme 48 Gene Name PLCD3
Enzyme 48 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
MLCGRWRRCRRPPEEPPVAAQVAAQVAAPVALPSPPTPSDGGTKRPGLRALKKMGLTEDE
DVRAMLRGSRLRKIRSRTWHKERLYRLQEDGLSVWFQRRIPRAPSQHIFFVQHIEAVREG
HQSEGLRRFGGAFAPARCLTIAFKGRRKNLDLAAPTAEEAQRWVRGLTKLRARLDAMSQR
ERLDHWIHSYLHRADSNQDSKMSFKEIKSLLRMVNVDMNDMYAYLLFKECDHSNNDRLEG
AEIEEFLRRLLKRPELEEIFHQYSGEDRVLSAPELLEFLEDQGEEGATLARAQQLIQTYE
LNETAKQHELMTLDGFMMYLLSPEGAALDNTHTCVFQDMNQPLAHYFISSSHNTYLTDSQ
IGGPSSTEAYVRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVVQAVRDHAFT
LSPYPVILSLENHCGLEQQAAMARHLCTILGDMLVTQALDSPNPEELPSPEQLKGRVLVK
GKKLPAARSEDGRALSDREEEEEDDEEEEEEVEAAAQRRLAKQISPELSALAVYCHATRL
RTLHPAPNAPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQ
EMWNSGCQLVALNFQTPGYEMDLNAGRFLVNGQCGYVLKPACLRQPDSTFDPEYPGPPRT
TLSIQVLTAQQLPKLNAEKPHSIVDPLVRIEIHGVPADCARQETDYVLNNGFNPRWGQTL
QFQLRAPELALVRFVVEDYDATSPNDFVGQFTLPLSSLKQGYRHIHLLSKDGASLSPATL
FIQIRIQRS
Enzyme 48 Number of Residues 789
Enzyme 48 Molecular Weight 89257.5
Enzyme 48 Theoretical pI 6.97
Enzyme 48 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 48 General Function Involved in calcium ion binding
Enzyme 48 Specific Function Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow
Enzyme 48 Pathways
Enzyme 48 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
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 Q8N3E9 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name PLCD3_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >2370 bp
ATGCTGTGCGGCCGCTGGAGGCGTTGCCGCCGCCCGCCCGAGGAGCCCCCGGTGGCCGCC
CAGGTCGCAGCCCAAGTCGCGGCGCCGGTCGCTCTCCCGTCCCCGCCGACTCCCTCCGAT
GGCGGCACCAAGAGGCCCGGGCTGCGGGCGCTGAAGAAGATGGGCCTGACGGAGGACGAG
GACGTGCGCGCCATGCTGCGGGGCTCCCGGCTCCGCAAGATCCGCTCGCGCACGTGGCAC
AAGGAGCGGCTGTACCGGCTGCAGGAGGACGGCCTGAGCGTGTGGTTCCAGCGGCGCATC
CCGCGTGCGCCATCGCAGCACATCTTCTTCGTGCAGCACATCGAGGCGGTCCGCGAGGGC
CACCAGTCCGAGGGCCTGCGGCGCTTCGGGGGTGCCTTCGCGCCAGCGCGCTGCCTCACC
ATCGCCTTCAAGGGCCGCCGCAAGAACCTGGACCTGGCGGCGCCCACGGCTGAGGAAGCG
CAGCGCTGGGTGCGCGGTCTGACCAAGCTCCGCGCGCGCCTGGACGCCATGAGCCAGCGC
GAGCGGCTAGACCACTGGATCCACTCCTATCTGCACCGGGCTGACTCCAACCAGGACAGC
AAGATGAGCTTCAAGGAGATCAAGAGCCTGCTGAGAATGGTCAACGTGGACATGAACGAC
ATGTACGCCTACCTCCTCTTCAAGGAGTGTGACCACTCCAACAACGACCGTCTAGAGGGG
GCTGAGATCGAGGAGTTCCTGCGGCGGCTGCTGAAGCGGCCGGAGCTGGAGGAGATCTTC
CATCAGTACTCGGGCGAGGACCGCGTGCTGAGTGCCCCTGAGCTGCTGGAGTTCCTGGAG
GACCAGGGCGAGGAGGGCGCCACACTGGCCCGCGCCCAGCAGCTCATTCAGACCTATGAG
CTCAACGAGACAGCCAAGCAGCATGAGCTGATGACACTGGATGGCTTCATGATGTACCTG
TTGTCGCCGGAGGGGGCTGCCTTGGACAACACCCACACGTGTGTGTTCCAGGACATGAAC
CAGCCCCTTGCCCACTACTTCATCTCTTCCTCCCACAACACCTATCTGACTGACTCCCAG
ATCGGGGGGCCCAGCAGCACCGAGGCCTATGTTAGGGCCTTTGCCCAGGGATGCCGCTGC
GTGGAGCTGGACTGCTGGGAGGGGCCAGGAGGGGAGCCCGTCATCTATCATGGCCATACC
CTCACCTCCAAGATTCTCTTCCGGGACGTGGTCCAAGCCGTGCGCGACCATGCCTTCACG
CTGTCCCCTTACCCTGTCATCCTATCCCTGGAGAACCACTGCGGGCTGGAGCAGCAGGCT
GCCATGGCCCGCCACCTCTGCACCATCCTGGGGGACATGCTGGTGACACAGGCGCTGGAC
TCCCCAAATCCCGAGGAGCTGCCATCCCCAGAGCAGCTGAAGGGCCGGGTCCTGGTGAAG
GGAAAGAAGTTGCCCGCTGCTCGGAGCGAGGATGGCCGGGCTCTGTCGGATCGGGAGGAG
GAGGAGGAGGATGACGAGGAGGAAGAAGAGGAGGTGGAGGCTGCAGCGCAGAGGCGGCTG
GCCAAGCAGATCTCCCCGGAGCTGTCGGCCCTGGCTGTGTACTGCCACGCCACCCGCCTG
CGGACCCTGCACCCTGCCCCCAACGCCCCACAACCCTGCCAGGTCAGCTCCCTCAGCGAG
CGCAAAGCCAAGAAACTCATTCGGGAGGCAGGGAACAGCTTTGTCAGGCACAATGCCCGC
CAGCTGACCCGCGTGTACCCGCTGGGGCTGCGGATGAACTCAGCCAACTACAGTCCCCAG
GAGATGTGGAACTCGGGCTGTCAGCTGGTGGCCTTGAACTTCCAGACGCCAGGCTACGAG
ATGGACCTCAATGCCGGGCGCTTCCTAGTCAATGGGCAGTGTGGCTACGTCCTAAAACCT
GCCTGCCTGCGGCAACCTGACTCGACCTTTGACCCCGAGTACCCAGGACCTCCCAGAACC
ACTCTCAGCATCCAGGTGCTGACTGCACAGCAGCTGCCCAAGCTGAATGCCGAGAAGCCA
CACTCCATTGTGGACCCCCTGGTGCGCATTGAGATCCATGGGGTGCCCGCAGACTGTGCC
CGGCAGGAGACTGACTACGTGCTCAACAATGGCTTCAACCCCCGCTGGGGGCAGACCCTG
CAGTTCCAGCTGCGGGCTCCGGAGCTGGCACTGGTCCGGTTTGTGGTGGAAGATTATGAC
GCCACCTCCCCCAATGACTTTGTGGGCCAGTTTACACTGCCTCTTAGCAGCCTAAAGCAA
GGGTACCGCCACATACACCTGCTTTCCAAGGACGGGGCCTCACTGTCACCAGCCACGCTC
TTCATCCAAATCCGCATCCAGCGCTCCTGA
Enzyme 48 GenBank Gene ID AK074240 Link Image
Enzyme 48 GeneCard ID PLCD3 Link Image
Enzyme 48 GenAtlas ID PLCD3 Link Image
Enzyme 48 HGNC ID HGNC:9061 Link Image
Enzyme 48 Chromosome Location 1
Enzyme 48 Locus 17q21.31
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 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]
  2. 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]
  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. Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed Link Image]
  5. Pawelczyk T, Matecki A: Expression, purification and kinetic properties of human recombinant phospholipase C delta 3. Acta Biochim Pol. 1997;44(2):221-9. [PubMed Link Image]
  6. Ghosh S, Pawelczyk T, Lowenstein JM: Phospholipase C isoforms delta 1 and delta 3 from human fibroblasts. High-yield expression in Escherichia coli, simple purification, and properties. Protein Expr Purif. 1997 Mar;9(2):262-78. [PubMed Link Image]
  7. Pawelczyk T, Matecki A: Localization of phospholipase C delta3 in the cell and regulation of its activity by phospholipids and calcium. Eur J Biochem. 1998 Oct 1;257(1):169-77. [PubMed Link Image]
  8. Kim H, Suh PG, Ryu SH, Park SH: Assignment of the human PLC delta3 gene (PLCD3) to human chromosome band 17q21 by fluorescence in situ hybridization. Cytogenet Cell Genet. 1999;87(3-4):209-10. [PubMed Link Image]
  9. Pawelczyk T, Matecki A: Phospholipase C-delta3 binds with high specificity to phosphatidylinositol 4,5-bisphosphate and phosphatidic acid in bilayer membranes. Eur J Biochem. 1999 Jun;262(2):291-8. [PubMed Link Image]
  10. Lin FG, Cheng HF, Lee IF, Kao HJ, Loh SH, Lee WH: Downregulation of phospholipase C delta3 by cAMP and calcium. Biochem Biophys Res Commun. 2001 Aug 17;286(2):274-80. [PubMed Link Image]
  11. Ananthanarayanan B, Das S, Rhee SG, Murray D, Cho W: Membrane targeting of C2 domains of phospholipase C-delta isoforms. J Biol Chem. 2002 Feb 1;277(5):3568-75. Epub 2001 Nov 12. [PubMed Link Image]
  12. Landreville S, Coulombe S, Carrier P, Gelb MH, Guerin SL, Salesse C: Expression of phospholipases A2 and C in human corneal epithelial cells. Invest Ophthalmol Vis Sci. 2004 Nov;45(11):3997-4003. [PubMed Link Image]
  13. 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]
  14. Naito Y, Okada M, Yagisawa H: Phospholipase C isoforms are localized at the cleavage furrow during cytokinesis. J Biochem. 2006 Dec;140(6):785-91. Epub 2006 Oct 14. [PubMed Link Image]
  15. 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 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 12915
Enzyme 49 Name Phospholipid scramblase 2
Enzyme 49 Synonyms
  1. PL scramblase 2
  2. Ca(2+)-dependent phospholipid scramblase 2
Enzyme 49 Gene Name PLSCR2
Enzyme 49 Protein Sequence >Phospholipid scramblase 2
MPAPPPPLNCPPGLEYLSQIDMILIHQQIELLEVLFSFESSNMYEIKNSFGQRIYFAAED
TNFCIRNCCGRSRPFTLRITDNVGREVITLERPLRCNCCCCPCCLQEIEIQAPPGVPVGY
VTQTWHPCLTKFTIKNQKREDVLKISGPCIVCSCIAGVDFEITSLDEQIVVGRISKHWSG
FLREAFTDADNFGIQFPRDLDVKMKAVMIGACFLIDYMFFERTR
Enzyme 49 Number of Residues 224
Enzyme 49 Molecular Weight 25522.5
Enzyme 49 Theoretical pI 5.34
Enzyme 49 GO Classification Not Available
Enzyme 49 General Function Involved in calcium ion binding
Enzyme 49 Specific Function May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions Not Available
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • 204-220
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 9651165 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q9NRY7 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name PLS2_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >675 bp
ATGCCAGCACCACCACCACCATTAAACTGTCCGCCAGGATTGGAATACTTAAGTCAGATA
GATATGATACTAATTCATCAGCAAATTGAACTTCTGGAAGTTCTATTCAGTTTTGAAAGT
AGTAACATGTATGAAATCAAGAACAGCTTTGGGCAGAGGATTTATTTTGCAGCAGAAGAT
ACTAATTTCTGTATCCGAAATTGCTGTGGGCGGTCTAGACCTTTTACCTTGAGGATTACT
GATAATGTGGGTCGAGAAGTCATAACTCTGGAAAGACCACTAAGATGTAACTGTTGTTGT
TGCCCCTGCTGCCTTCAGGAGATAGAAATCCAAGCTCCTCCTGGTGTACCAGTAGGTTAT
GTTACTCAGACCTGGCACCCATGTCTAACAAAGTTTACAATTAAAAATCAGAAAAGAGAG
GATGTACTAAAAATTAGTGGTCCATGTATCGTGTGCAGCTGTATTGCGGGTGTTGATTTT
GAGATTACATCTCTTGATGAACAAATTGTGGTTGGCAGGATTTCTAAGCACTGGTCTGGG
TTTTTAAGAGAGGCATTTACTGATGCTGACAACTTTGGAATCCAATTCCCTAGAGACCTT
GATGTTAAAATGAAAGCCGTGATGATTGGTGCCTGTTTCCTCATTGACTACATGTTTTTT
GAAAGAACTAGGTAA
Enzyme 49 GenBank Gene ID AF159441 Link Image
Enzyme 49 GeneCard ID PLSCR2 Link Image
Enzyme 49 GenAtlas ID PLSCR2 Link Image
Enzyme 49 HGNC ID HGNC:16494 Link Image
Enzyme 49 Chromosome Location 3
Enzyme 49 Locus 3q24
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed Link Image]
  2. 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 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 12916
Enzyme 50 Name Phospholipid scramblase 3
Enzyme 50 Synonyms
  1. PL scramblase 3
  2. Ca(2+)-dependent phospholipid scramblase 3
Enzyme 50 Gene Name PLSCR3
Enzyme 50 Protein Sequence >Phospholipid scramblase 3
MAGYLPPKGYAPSPPPPYPVTPGYPEPALHPGPGQAPVPAQVPAPAPGFALFPSPGPVAL
GSAAPFLPLPGVPSGLEFLVQIDQILIHQKAERVETFLGWETCNRYELRSGAGQPLGQAA
EESNCCARLCCGARRPLRVRLADPGDREVLRLLRPLHCGCSCCPCGLQEMEVQAPPGTTI
GHVLQTWHPFLPKFSIQDADRQTVLRVVGPCWTCGCGTDTNFEVKTRDESRSVGRISKQW
GGLVREALTDADDFGLQFPLDLDVRVKAVLLGATFLIDYMFFEKRGGAGPSAVTS
Enzyme 50 Number of Residues 295
Enzyme 50 Molecular Weight 31648.1
Enzyme 50 Theoretical pI 6.63
Enzyme 50 GO Classification Not Available
Enzyme 50 General Function Involved in calcium ion binding
Enzyme 50 Specific Function May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • 266-282
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 31543417 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID Q9NRY6 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name PLS3_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >888 bp
ATGGCAGGCTACTTGCCCCCCAAAGGCTACGCCCCTTCGCCCCCACCTCCCTACCCTGTC
ACCCCTGGGTACCCGGAGCCGGCGCTACATCCTGGGCCCGGGCAGGCGCCAGTGCCCGCC
CAGGTACCTGCCCCAGCTCCCGGCTTCGCCCTCTTCCCCTCGCCTGGCCCCGTGGCCTTG
GGGTCTGCTGCCCCCTTCTTGCCACTGCCAGGGGTGCCTTCTGGCCTCGAATTCCTGGTG
CAGATTGATCAGATTTTGATTCACCAGAAGGCTGAGCGAGTGGAAACGTTCCTAGGCTGG
GAGACCTGTAATCGGTATGAACTGCGCTCTGGGGCCGGGCAGCCCCTGGGTCAGGCGGCC
GAGGAGAGCAACTGCTGCGCCCGTCTGTGCTGTGGCGCCCGCCGGCCGCTGCGTGTCCGC
CTGGCCGACCCCGGGGACCGTGAGGTGCTGCGTTTGCTCCGCCCGCTGCACTGTGGCTGC
AGCTGCTGCCCCTGTGGCCTCCAGGAGATGGAAGTACAGGCTCCACCAGGCACCACCATT
GGCCACGTGCTACAGACCTGGCATCCCTTCCTCCCCAAGTTCTCCATCCAGGATGCCGAT
CGCCAGACAGTCTTGCGAGTGGTGGGGCCCTGCTGGACCTGTGGCTGTGGCACAGACACC
AACTTTGAGGTGAAGACTCGGGATGAATCCCGCAGTGTGGGCCGCATCAGCAAGCAGTGG
GGGGGCCTGGTCCGAGAAGCCCTCACAGATGCAGATGACTTTGGCCTACAGTTCCCGCTG
GACCTGGATGTGAGGGTGAAGGCTGTGCTGCTGGGAGCCACATTCCTCATTGACTACATG
TTCTTTGAGAAGCGAGGAGGCGCTGGGCCCTCTGCCGTCACCAGTTAG
Enzyme 50 GenBank Gene ID NM_020360.2 Link Image
Enzyme 50 GeneCard ID PLSCR3 Link Image
Enzyme 50 GenAtlas ID PLSCR3 Link Image
Enzyme 50 HGNC ID HGNC:16495 Link Image
Enzyme 50 Chromosome Location 1
Enzyme 50 Locus 17p13.1
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References
  1. Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed Link Image]
  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. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [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. Shibata H, Suzuki H, Kakiuchi T, Inuzuka T, Yoshida H, Mizuno T, Maki M: Identification of Alix-type and Non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants. J Biol Chem. 2008 Apr 11;283(15):9623-32. Epub 2008 Feb 6. [PubMed Link Image]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 12917
Enzyme 51 Name Phospholipid scramblase 4
Enzyme 51 Synonyms
  1. PL scramblase 4
  2. Ca(2+)-dependent phospholipid scramblase 4
  3. Cell growth-inhibiting gene 43 protein
  4. TRA1
Enzyme 51 Gene Name PLSCR4
Enzyme 51 Protein Sequence >Phospholipid scramblase 4
MSGVVPTAPEQPAGEMENQTKPPDPRPDAPPEYNSHFLPGPPGTAVPPPTGYPGGLPMGY
YSPQQPSTFPLYQPVGGIHPVRYQPGKYPMPNQSVPITWMPGPTPMANCPPGLEYLVQLD
NIHVLQHFEPLEMMTCFETNNRYDIKNNSDQMVYIVTEDTDDFTRNAYRTLRPFVLRVTD
CMGREIMTMQRPFRCTCCCFCCPSARQELEVQCPPGVTIGFVAEHWNLCRAVYSIQNEKK
ENVMRVRGPCSTYGCGSDSVFEVKSLDGISNIGSIIRKWNGLLSAMADADHFDIHFPLDL
DVKMKAMIFGACFLIDFMYFERSPPQRSR
Enzyme 51 Number of Residues 329
Enzyme 51 Molecular Weight 37005.2
Enzyme 51 Theoretical pI 5.62
Enzyme 51 GO Classification Not Available
Enzyme 51 General Function Involved in calcium ion binding
Enzyme 51 Specific Function May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions Not Available
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • 304-320
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 9622872 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID Q9NRQ2 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name PLS4_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >990 bp
ATGTCAGGTGTGGTACCCACAGCCCCTGAACAGCCTGCAGGTGAAATGGAAAATCAAACA
AAACCACCAGATCCAAGGCCTGATGCTCCTCCTGAATACAGTTCTCATTTTTTACCAGGA
CCCCCTGGAACAGCTGTCCCTCCACCTACTGGCTACCCAGGAGGCTTGCCTATGGGATAC
TACAGTCCACAGCAACCCAGTACCTTCCCTTTGTACCAGCCAGTTGGTGGTATCCATCCT
GTCCGGTATCAGCCTGGCAAATATCCTATGCCAAATCAGTCTGTTCCAATAACATGGATG
CCAGGGCCAACTCCTATGGCAAACTGCCCTCCTGGTCTGGAATACTTAGTTCAGTTGGAC
AACATACATGTTCTTCAGCATTTTGAGCCTCTGGAAATGATGACATGTTTTGAAACTAAT
AATAGATATGATATTAAAAACAACTCAGACCAGATGGTTTACGTTGTAACCGAAGACACA
GATGACTTTACCAGGAATGCCTATCGGACACTAAGGCCCTTCGTCCTCCGGGTCACTGAT
TGTATGGGCCGAGAAATCATGACAATGCAGAGACCCTTCAGATGCACCTGCTGTTGCTTC
TGTTGCCCCTCTGCCAGACAAGAGCTGGAGGTGCAGTGTCCTCCTGGTGTCACCATTGGC
TTTGTTGCGGAACATTGGAACCTGTGCAGGGCGGTGTACAGCATCCAAAATGAGAAGAAA
GAAAATGTGATGAGAGTTCGTGGGCCATGCTCAACCTATGGCTGTGGTTCAGATTCTGTT
TTTGAGGTCAAATCCCTTGATGGCATATCCAACATCGGCAGTATTATCCGGAAGTGGAAT
GGTTTGTTATCAGCAATGGCAGATGCTGACCATTTTGACATTCACTTCCCACTAGACCTG
GATGTGAAGATGAAAGCCATGATTTTTGGAGCTTGCTTCCTCATTGACTTCATGTATTTT
GAAAGATCTCCACCACAACGTTCAAGATAG
Enzyme 51 GenBank Gene ID AF199023 Link Image
Enzyme 51 GeneCard ID PLSCR4 Link Image
Enzyme 51 GenAtlas ID PLSCR4 Link Image
Enzyme 51 HGNC ID HGNC:16497 Link Image
Enzyme 51 Chromosome Location 3
Enzyme 51 Locus 3q24
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 General References
  1. Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed Link Image]
  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]
  5. Shibata H, Suzuki H, Kakiuchi T, Inuzuka T, Yoshida H, Mizuno T, Maki M: Identification of Alix-type and Non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants. J Biol Chem. 2008 Apr 11;283(15):9623-32. Epub 2008 Feb 6. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 12918
Enzyme 52 Name Phospholipid scramblase family member 5
Enzyme 52 Synonyms Not Available
Enzyme 52 Gene Name PLSCR5
Enzyme 52 Protein Sequence >Phospholipid scramblase family member 5
MASKDAQNQRRGLPGFLPGAPDPDQSLPASSNPGNQAWQLSLPLPSSFLPTVSLPPGLEY
LSQLDLIIIHQQVELLGMILGTETSNKYEIKNSLGQRIYFAVEESICFNRTFCSTLRSCT
LRITDNSGREVITVNRPLRCNSCWCPCYLQELEIQAPPGTIVGYVTQKWDPFLPKFTIQN
ANKEDILKIVGPCVTCGCFGDVDFEVKTINEKLTIGKISKYWSGFVNDVFTNADNFGIHV
PADLDVTVKAAMIGACFLFDFMFFEHSLAGL
Enzyme 52 Number of Residues 271
Enzyme 52 Molecular Weight 30026.2
Enzyme 52 Theoretical pI 4.90
Enzyme 52 GO Classification Not Available
Enzyme 52 General Function Not Available
Enzyme 52 Specific Function Not Available
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions Not Available
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 146229354 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID A0PG75 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name PLS5_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >816 bp
ATGGCCTCTAAAGATGCCCAGAACCAAAGAAGAGGTCTGCCTGGTTTTCTTCCTGGAGCT
CCAGACCCAGACCAAAGCCTTCCTGCCTCTTCCAATCCAGGGAACCAAGCATGGCAGCTG
AGTCTCCCTCTGCCAAGCAGTTTCCTGCCAACAGTCAGTCTCCCTCCTGGTCTAGAATAT
TTAAGCCAGTTAGACCTGATAATTATACACCAGCAGGTGGAGCTGCTTGGAATGATACTT
GGTACTGAGACCTCCAACAAATATGAGATTAAAAACAGCTTGGGACAAAGAATTTACTTT
GCAGTGGAGGAAAGCATCTGCTTCAATCGTACTTTCTGTTCCACTCTGCGATCTTGCACC
CTGAGGATCACAGATAACTCAGGTCGAGAGGTCATTACAGTGAACAGGCCCTTGAGATGT
AACAGCTGCTGGTGCCCTTGCTACCTACAAGAGTTAGAAATCCAAGCCCCTCCTGGTACT
ATAGTTGGTTACGTTACGCAGAAGTGGGACCCCTTTCTGCCTAAATTCACAATCCAAAAT
GCAAACAAAGAAGATATTTTGAAAATTGTTGGTCCTTGTGTGACATGTGGCTGTTTTGGC
GATGTGGATTTTGAGGTGAAAACCATTAATGAAAAGCTTACAATTGGGAAGATTTCAAAG
TACTGGTCAGGATTTGTAAATGATGTCTTCACAAATGCTGACAATTTCGGAATTCATGTT
CCTGCAGATCTAGATGTAACAGTCAAAGCAGCAATGATCGGTGCCTGTTTTCTCTTTGAT
TTTATGTTCTTTGAACATTCACTGGCTGGATTATAA
Enzyme 52 GenBank Gene ID NM_001085420.1 Link Image
Enzyme 52 GeneCard ID PLSCR5 Link Image
Enzyme 52 GenAtlas ID PLSCR5 Link Image
Enzyme 52 HGNC ID HGNC:19952 Link Image
Enzyme 52 Chromosome Location 3
Enzyme 52 Locus 3q24
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References
  1. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, 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, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 12919
Enzyme 53 Name Probable phospholipid-transporting ATPase VB
Enzyme 53 Synonyms
  1. ATPase class V type 10B
Enzyme 53 Gene Name ATP10B
Enzyme 53 Protein Sequence >Probable phospholipid-transporting ATPase VB
MALSVDSSWHRWQWRVRDGFPHCPSETTPLLSPEKGRQSYNLTQQRVVFPNNSIFHQDWE
EVSRRYPGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITML
PLAIVLFVIMIKDGMEDFKRHRFDKAINCSNIRIYERKEQTYVQKCWKDVRVGDFIQMKC
NEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEVQFEPELFHNTIVC
EKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNS
GPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSFLPS
ALGGFYMFLTMIILLQVLIPISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNI
AEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQENAKRLETPKELDSDGEEWTQY
QCLSFSARWAQDPATMRSQKGAQPLRRSQSARVPIQGHYRQRSMGHRESSQPPVAFSSSI
EKDVTPDKNLLTKVRDAALWLETLSDSRPAKASLSTTSSIADFFLALTICNSVMVSTTTE
PRQRVTIKPSSKALGTSLEKIQQLFQKLKLLSLSQSFSSTAPSDTDLGESLGANVATTDS
DERDDASVCSGGDSTDDGGYRSSMWDQGDILESGSGTSLEEALEAPATDLARPEFCYEAE
SPDEAALVHAAHAYSFTLVSRTPEQVTVRLPQGTCLTFSLLCTLGFDSVRKRMSVVVRHP
LTGEIVVYTKGADSVIMDLLEDPACVPDINMEKKLRKIRARTQKHLDLYARDGLRTLCIA
KKVVSEEDFRRWASFRREAEASLDNRDELLMETAQHLENQLTLLGATGIEDRLQEGVPDT
IATLREAGIQLWVLTGDKQETAVNIAHSCRLLNQTDTVYTINTENQETCESILNCALEEL
KQFRELQKPDRKLFGFRLPSKTPSITSEAVVPEAGLVIDGKTLNAIFQGKLEKKFLELTQ
YCRSVLCCRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAADIGIGISGQEGMQA
VMSSDFAITRFKHLKKLLLVHGHWCYSRLARMVVYYLYKNVCYVNLLFWYQFFCGFSSST
MIDYWQMIFFNLFFTSLPPLVFGVLDKDISAETLLALPELYKSGQNSECYNLSTFWISMV
DAFYQSLICFFIPYLAYKGSDIDVFTFGTPINTISLTTILLHQAMEMKTWTIFHGVVLLG
SFLMYFLVSLLYNATCVICNSPTNPYWVMEGQLSNPTFYLVCFLTPVVALLPRYFFLSLQ
GTCGKSLISKAQKIDKLPPDKRNLEIQSWRSRQRPAPVPEVARPTHHPVSSITGQDFSAS
TPKSSNPPKRKHVEESVLHEQRCGTECMRDDSCSGDSSAQLSSGEHLLGPNRIMAYSRGQ
TDMCRCSKRSSHRRSQSSLTI
Enzyme 53 Number of Residues 1461
Enzyme 53 Molecular Weight 165388.9
Enzyme 53 Theoretical pI 6.87
Enzyme 53 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • ion binding
  • ion transmembrane transporter activity
  • lipid transporter activity
  • magnesium ion binding
  • metal ion binding
  • nucleoside binding
  • phospholipid transporter activity
  • phospholipid-translocating ATPase activity
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • substrate-specific transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • cellular nitrogen compound metabolic process
  • establishment of localization
  • lipid transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phospholipid transport
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 53 General Function Involved in ATP binding
Enzyme 53 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 53 Pathways Not Available
Enzyme 53 Reactions
  • ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • 83-104 111-132 317-338 369-390 1112-1132 1145-1164 1195-1216 1224-1246 1253-1273 1292-1316
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein 149944474 Link Image
Enzyme 53 UniProtKB/Swiss-Prot ID O94823 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name AT10B_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence >4386 bp
ATGGCCCTCTCAGTGGACTCATCGTGGCATCGGTGGCAGTGGAGAGTCAGAGATGGCTTC
CCCCATTGTCCATCGGAAACCACACCGCTGCTCTCTCCAGAGAAAGGGAGACAGAGCTAC
AACTTGACACAGCAGCGGGTCGTGTTCCCCAACAACAGCATATTCCATCAAGATTGGGAA
GAGGTCTCCAGGAGATACCCTGGCAACAGAACCTGCACAACCAAATACACCCTCTTCACC
TTCCTGCCCCGGAATCTCTTTGAGCAATTTCATAGATGGGCTAACCTCTATTTCCTGTTC
CTGGTGATTTTGAACTGGATGCCCTCCATGGAAGTCTTCCACAGAGAAATCACCATGTTA
CCATTGGCCATTGTCCTGTTCGTCATCATGATCAAGGATGGCATGGAGGACTTCAAGAGA
CACCGCTTTGATAAAGCAATAAACTGCTCCAACATTCGAATTTATGAAAGAAAAGAGCAG
ACCTATGTGCAGAAGTGCTGGAAGGATGTGCGCGTGGGAGACTTCATCCAAATGAAATGC
AATGAGATTGTCCCAGCAGACATACTCCTCCTTTTTTCCTCTGACCCCAATGGGATATGC
CATCTGGAAACTGCCAGCTTGGATGGAGAGACAAACCTCAAGCAAAGATGTGTCGTGAAG
GGCTTCTCACAGCAGGAGGTACAGTTCGAACCAGAGCTTTTCCACAATACCATCGTGTGT
GAGAAACCCAACAACCACCTCAACAAATTTAAGGGTTATATGGAGCATCCTGACCAGACC
AGGACTGGCTTTGGCTGTGAGAGTCTTCTGCTTCGAGGCTGCACCATCAGAAACACCGAG
ATGGCTGTTGGCATTGTCATCTATGCAGGCCATGAGACGAAAGCCATGCTGAACAACAGT
GGCCCCCGGTACAAACGCAGCAAGATTGAGCGGCGCATGAATATAGACATCTTCTTCTGC
ATTGGGATCCTCATCCTCATGTGCCTTATTGGAGCTGTAGGTCACAGCATCTGGAATGGG
ACCTTTGAAGAACACCCTCCCTTCGATGTGCCAGATGCCAATGGCAGCTTCCTTCCCAGT
GCCCTTGGGGGCTTCTACATGTTCCTCACAATGATCATCCTGCTCCAGGTGCTGATCCCC
ATCTCTTTGTATGTCTCCATTGAGCTGGTGAAGCTCGGGCAAGTGTTCTTCTTGAGCAAT
GACCTTGACCTGTATGATGAAGAGACCGATTTATCCATTCAATGTCGAGCCCTCAACATC
GCAGAGGACTTGGGCCAGATCCAGTACATCTTCTCCGATAAGACGGGGACCCTGACAGAG
AACAAGATGGTGTTCCGACGTTGCACCATCATGGGCAGCGAGTATTCTCACCAAGAAAAT
GCTAAGCGACTGGAGACCCCAAAGGAGCTGGACTCAGATGGTGAAGAGTGGACCCAATAC
CAATGCCTGTCCTTCTCGGCTAGATGGGCCCAGGATCCAGCAACTATGAGAAGCCAAAAA
GGTGCTCAGCCTCTGAGGAGGAGCCAGAGTGCCCGGGTGCCCATCCAGGGCCACTACCGG
CAAAGGTCTATGGGGCACCGTGAAAGCTCACAGCCTCCTGTGGCCTTCAGCAGCTCCATA
GAAAAAGATGTAACTCCAGATAAAAACCTACTGACCAAGGTTCGAGATGCTGCCCTGTGG
TTGGAGACCTTGTCAGACAGCAGACCTGCCAAGGCTTCCCTCTCCACCACCTCCTCCATT
GCTGATTTCTTCCTTGCCTTAACCATCTGCAACTCTGTCATGGTGTCCACAACCACCGAG
CCCAGGCAGAGGGTCACCATCAAACCCTCAAGCAAGGCTCTGGGGACGTCCCTGGAGAAG
ATTCAGCAGCTCTTCCAGAAGTTGAAGCTATTGAGCCTCAGCCAGTCATTCTCATCCACT
GCACCCTCTGACACAGACCTCGGGGAGAGCTTAGGGGCCAACGTGGCCACCACAGACTCG
GATGAGAGAGATGATGCATCTGTGTGCAGTGGAGGTGACTCCACTGATGACGGTGGCTAC
AGGAGCAGCATGTGGGACCAGGGCGACATCCTGGAGTCTGGGTCAGGCACTTCCTTGGAG
GAGGCATTGGAGGCCCCAGCCACAGACCTGGCCAGGCCTGAGTTCTGTTACGAGGCTGAG
AGCCCTGATGAGGCCGCCCTGGTGCACGCTGCCCATGCCTACAGCTTCACACTAGTGTCC
CGGACACCTGAGCAGGTGACTGTGCGCCTGCCCCAGGGCACCTGCCTCACCTTCAGCCTC
CTCTGCACCCTGGGCTTTGACTCTGTCAGGAAGAGAATGTCTGTGGTTGTGAGGCACCCA
CTGACTGGCGAGATTGTTGTCTACACCAAGGGTGCTGACTCGGTCATCATGGACCTGCTG
GAAGACCCAGCCTGCGTACCTGACATTAATATGGAAAAGAAGCTGAGAAAAATCCGAGCC
CGGACCCAAAAGCATCTAGACTTGTATGCAAGAGATGGCCTGCGCACACTATGCATTGCC
AAGAAGGTTGTAAGCGAAGAGGACTTCCGGAGATGGGCCAGTTTCCGGCGTGAGGCTGAG
GCATCCCTCGACAACCGAGATGAGCTTCTCATGGAAACTGCACAGCATCTGGAGAATCAA
CTCACCTTACTTGGAGCCACTGGGATCGAAGACCGGCTGCAGGAAGGAGTTCCAGATACG
ATTGCCACTCTGCGGGAGGCTGGGATCCAGCTCTGGGTCCTGACTGGAGATAAGCAGGAG
ACAGCGGTCAACATTGCCCATTCCTGCAGACTGTTAAATCAGACCGACACTGTTTATACC
ATCAATACAGAGAATCAGGAGACCTGTGAATCCATCCTCAATTGTGCATTGGAAGAGCTA
AAGCAATTTCGTGAACTACAGAAGCCAGACCGCAAGCTCTTTGGATTCCGCTTACCTTCC
AAGACACCATCCATCACCTCAGAAGCTGTGGTTCCAGAAGCTGGATTGGTCATCGATGGG
AAGACATTGAATGCCATCTTCCAGGGAAAGCTAGAGAAGAAGTTTCTGGAATTGACCCAG
TATTGTCGGTCCGTCCTGTGCTGCCGCTCCACGCCACTCCAGAAGAGTATGATAGTCAAG
CTGGTGCGAGACAAGTTGCGCGTCATGACCCTTTCCATAGGTGATGGAGCAAATGATGTA
AGCATGATTCAAGCTGCTGATATTGGAATTGGAATATCTGGACAGGAAGGCATGCAGGCT
GTCATGTCCAGCGACTTTGCCATCACCCGCTTTAAGCATCTCAAGAAGTTGCTGCTCGTG
CATGGCCACTGGTGTTACTCGCGCCTGGCCAGGATGGTGGTGTACTACCTCTACAAGAAC
GTGTGCTACGTCAACCTGCTCTTCTGGTATCAGTTCTTCTGTGGTTTCTCCAGCTCCACC
ATGATTGATTACTGGCAGATGATATTCTTCAATCTCTTCTTTACCTCCTTGCCTCCTCTT
GTCTTTGGAGTCCTTGACAAAGACATCTCTGCAGAAACACTCCTGGCATTGCCTGAGCTA
TACAAGAGTGGCCAGAACTCTGAGTGCTATAACCTGTCGACTTTCTGGATTTCTATGGTG
GATGCATTCTACCAGAGCCTCATCTGTTTCTTTATCCCTTACCTGGCCTATAAGGGCTCT
GATATAGATGTCTTTACCTTTGGGACACCAATCAACACCATCTCCCTCACCACAATCCTT
TTGCACCAGGCAATGGAAATGAAGACATGGACCATTTTCCACGGAGTCGTGCTCCTCGGC
AGCTTCCTGATGTACTTTCTGGTATCCCTCCTGTACAATGCCACCTGCGTCATCTGCAAC
AGCCCCACCAATCCCTATTGGGTGATGGAAGGCCAGCTCTCAAACCCCACTTTCTACCTC
GTCTGCTTTCTCACACCAGTTGTTGCTCTTCTCCCAAGATACTTTTTCCTGTCTCTGCAA
GGAACTTGTGGGAAGTCTCTAATCTCAAAAGCTCAGAAAATTGACAAACTCCCCCCAGAC
AAAAGAAACCTGGAAATCCAGAGTTGGAGAAGCAGACAGAGGCCTGCCCCTGTCCCCGAA
GTGGCTCGACCAACTCACCACCCAGTGTCATCTATCACAGGACAGGACTTCAGTGCCAGC
ACCCCAAAGAGCTCTAACCCTCCCAAGAGGAAGCATGTGGAAGAGTCAGTACTCCACGAA
CAGAGATGTGGCACGGAGTGCATGAGGGATGACTCATGCTCAGGGGACTCCTCAGCTCAA
CTCTCATCCGGGGAGCACCTGCTGGGACCTAACAGGATAATGGCCTACTCAAGAGGACAG
ACTGATATGTGCCGGTGCTCAAAGAGGAGCAGCCATCGCCGATCCCAGAGTTCACTGACC
ATATGA
Enzyme 53 GenBank Gene ID NM_025153.2 Link Image
Enzyme 53 GeneCard ID ATP10B Link Image
Enzyme 53 GenAtlas ID ATP10B Link Image
Enzyme 53 HGNC ID HGNC:13543 Link Image
Enzyme 53 Chromosome Location 5
Enzyme 53 Locus 5q34
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 General References
  1. Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Oct 30;5(5):277-86. [PubMed Link Image]
  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. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed Link Image]
Enzyme 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 12920
Enzyme 54 Name Probable phospholipid-transporting ATPase ID
Enzyme 54 Synonyms
  1. ATPase class I type 8B member 2
Enzyme 54 Gene Name ATP8B2
Enzyme 54 Protein Sequence >Probable phospholipid-transporting ATPase ID
MTVPKEMPEKWARAQAPPSWSRKKPSWGTEEERRARANDREYNEKFQYASNCIKTSKYNI
LTFLPVNLFEQFQEVANTYFLFLLILQLIPQISSLSWFTTIVPLVLVLTITAVKDATDDY
FRHKSDNQVNNRQSQVLINGILQQEQWMNVCVGDIIKLENNQFVAADLLLLSSSEPHGLC
YIETAELDGETNMKVRQAIPVTSELGDISKLAKFDGEVICEPPNNKLDKFSGTLYWKENK
FPLSNQNMLLRGCVLRNTEWCFGLVIFAGPDTKLMQNSGRTKFKRTSIDRLMNTLVLWIF
GFLVCMGVILAIGNAIWEHEVGMRFQVYLPWDEAVDSAFFSGFLSFWSYIIILNTVVPIS
LYVSVEVIRLGHSYFINWDKKMFCMKKRTPAEARTTTLNEELGQVEYIFSDKTGTLTQNI
MVFNKCSINGHSYGDVFDVLGHKAELGERPEPVDFSFNPLADKKFLFWDPSLLEAVKIGD
PHTHEFFRLLSLCHTVMSEEKNEGELYYKAQSPDEGALVTAARNFGFVFRSRTPKTITVH
EMGTAITYQLLAILDFNNIRKRMSVIVRNPEGKIRLYCKGADTILLDRLHHSTQELLNTT
MDHLNEYAGEGLRTLVLAYKDLDEEYYEEWAERRLQASLAQDSREDRLASIYEEVENNMM
LLGATAIEDKLQQGVPETIALLTLANIKIWVLTGDKQETAVNIGYSCKMLTDDMTEVFIV
TGHTVLEVREELRKAREKMMDSSRSVGNGFTYQDKLSSSKLTSVLEAVAGEYALVINGHS
LAHALEADMELEFLETACACKAVICCRVTPLQKAQVVELVKKYKKAVTLAIGDGANDVSM
IKTAHIGVGISGQEGIQAVLASDYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFA
FTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGVFDQDVPEQRSMEYPKLYE
PGQLNLLFNKREFFICIAQGIYTSVLMFFIPYGVFADATRDDGTQLADYQSFAVTVATSL
VIVVSVQIGLDTGYWTAINHFFIWGSLAVYFAILFAMHSNGLFDMFPNQFRFVGNAQNTL
AQPTVWLTIVLTTVVCIMPVVAFRFLRLNLKPDLSDTVRYTQLVRKKQKAQHRCMRRVGR
TGSRRSGYAFSHQEGFGELIMSGKNMRLSSLALSSFTTRSSSSWIESLRRKKSDSASSPS
GGADKPLKG
Enzyme 54 Number of Residues 1209
Enzyme 54 Molecular Weight 137439.1
Enzyme 54 Theoretical pI 6.99
Enzyme 54 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • ion binding
  • ion transmembrane transporter activity
  • lipid transporter activity
  • magnesium ion binding
  • metal ion binding
  • nucleoside binding
  • phospholipid transporter activity
  • phospholipid-translocating ATPase activity
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • substrate-specific transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • cellular nitrogen compound metabolic process
  • establishment of localization
  • lipid transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phospholipid transport
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 54 General Function Involved in ATP binding
Enzyme 54 Specific Function ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)
Enzyme 54 Pathways Not Available
Enzyme 54 Reactions
  • ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • 65-86 93-112 296-317 347-368 890-910 923-942 973-994 1009-1031 1038-1058 1079-1103
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein 40316837 Link Image
Enzyme 54 UniProtKB/Swiss-Prot ID P98198 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name AT8B2_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence >3672 bp
ATGGATACCTTGAGAGCTGTTCCCCTTTTTTCAATATCTGGCCTCTTCTCCTTTCCCTAC
AGGGTCTCCCATGGGATTGCTGGGATCTTGCTGGGTGAGATGGCAGTGTGTGCAAAAAAG
CGCCCCCCAGAAGAAGAAAGGAGGGCGCGGGCTAATGACCGAGAATACAATGAGAAATTC
CAGTATGCGAGTAACTGCATCAAGACCTCCAAGTACAATATTCTCACCTTCCTGCCTGTC
AACCTCTTTGAGCAGTTCCAGGAAGTTGCCAACACTTACTTCCTGTTCCTCCTCATTCTG
CAGTTGATCCCCCAGATCTCTTCCCTGTCCTGGTTCACCACCATTGTGCCTTTGGTTCTT
GTCCTCACCATCACAGCTGTTAAAGATGCCACTGATGACTATTTCCGCCACAAGAGCGAT
AACCAGGTGAATAACCGCCAGTCTCAGGTGCTGATCAATGGAATCCTCCAGCAGGAGCAG
TGGATGAATGTCTGTGTTGGTGATATTATCAAGCTAGAAAATAACCAGTTTGTGGCGGCG
GATCTCCTCCTCCTTTCCAGCAGTGAGCCCCATGGGCTGTGTTACATAGAGACAGCAGAA
CTTGATGGCGAGACCAACATGAAAGTACGTCAGGCGATTCCAGTCACCTCAGAATTGGGA
GACATCAGTAAGCTTGCCAAGTTTGACGGTGAAGTGATCTGTGAACCTCCCAACAACAAA
CTGGACAAATTCAGCGGAACCCTCTACTGGAAGGAAAATAAGTTCCCTCTGAGCAACCAG
AACATGCTGCTGCGGGGCTGTGTGCTGCGAAACACCGAGTGGTGCTTCGGGCTGGTCATC
TTTGCAGGTCCCGACACTAAGCTGATGCAAAACAGCGGCAGAACAAAGTTCAAAAGAACG
AGTATCGATCGCCTAATGAATACCCTGGTGCTCTGGATTTTTGGATTCCTGGTTTGCATG
GGGGTGATCCTGGCCATTGGCAATGCCATCTGGGAGCACGAGGTGGGGATGCGTTTCCAG
GTCTACCTGCCGTGGGATGAGGCAGTGGACAGTGCCTTCTTCTCTGGCTTCCTCTCCTTC
TGGTCCTACATCATCATCCTCAACACCGTTGTGCCCATTTCACTCTATGTCAGTGTGGAG
GTCATCCGTCTGGGCCACAGCTACTTCATCAACTGGGATAAGAAGATGTTCTGCATGAAG
AAGCGGACGCCTGCAGAAGCCCGCACCACCACCCTAAACGAGGAGCTGGGCCAGGTGGAG
TACATCTTCTCCGACAAGACGGGCACCCTCACCCAGAACATCATGGTTTTCAACAAGTGC
TCCATCAATGGCCACAGCTATGGTGATGTGTTTGACGTCCTGGGACACAAAGCTGAATTG
GGAGAGAGGCCTGAACCTGTTGACTTCTCCTTCAATCCTCTGGCTGACAAGAAGTTCTTA
TTTTGGGACCCCAGCCTGCTGGAGGCTGTCAAGATCGGGGACCCCCACACGCATGAGTTC
TTCCGCCTCCTTTCCCTGTGTCATACTGTCATGTCAGAAGAAAAGAACGAAGGAGAGCTG
TACTACAAAGCTCAGTCCCCAGATGAGGGGGCCCTGGTCACCGCAGCCAGGAACTTTGGT
TTTGTTTTCCGCTCTCGCACCCCCAAAACAATCACCGTCCATGAGATGGGCACAGCCATC
ACCTACCAGCTGCTGGCCATCCTGGACTTCAACAACATCCGCAAGCGGATGTCGGTCATA
GTGCGGAATCCAGAGGGGAAGATCCGACTCTACTGCAAAGGGGCTGACACTATCCTACTG
GACAGACTGCACCACTCCACTCAAGAGCTGCTCAACACCACCATGGACCACCTTAATGAG
TACGCAGGGGAAGGGCTGAGGACCCTGGTGCTGGCCTACAAGGATCTGGATGAAGAGTAC
TACGAGGAGTGGGCTGAGCGACGCCTCCAGGCCAGCCTGGCCCAGGACAGCCGGGAGGAC
AGGCTGGCTAGCATCTATGAGGAGGTTGAGAACAACATGATGCTGCTGGGTGCAACGGCC
ATTGAGGACAAACTTCAGCAAGGGGTTCCAGAGACCATTGCCCTCCTGACACTGGCCAAC
ATCAAGATTTGGGTGCTAACCGGAGACAAGCAAGAGACGGCTGTGAACATCGGCTATTCC
TGCAAGATGCTGACGGATGACATGACTGAGGTTTTCATAGTCACTGGCCATACTGTCCTG
GAGGTGCGGGAGGAGCTCAGGAAAGCCCGGGAGAAGATGATGGACTCATCCCGCTCCGTA
GGCAACGGCTTCACCTATCAGGACAAGCTTTCTTCTTCCAAGCTAACTTCTGTCCTGGAG
GCCGTTGCTGGGGAGTACGCCCTGGTCATAAATGGTCACAGCCTGGCCCACGCACTGGAG
GCAGACATGGAGCTGGAGTTTCTGGAGACAGCGTGTGCCTGCAAAGCTGTCATCTGCTGC
CGGGTGACCCCCTTGCAGAAGGCACAGGTGGTAGAACTGGTCAAGAAGTACAAGAAGGCT
GTGACGCTTGCCATTGGAGACGGAGCCAATGATGTCAGCATGATCAAAACGGCTCACATT
GGTGTGGGGATCAGTGGGCAGGAAGGGATCCAGGCTGTCTTGGCCTCCGATTACTCCTTC
TCCCAGTTCAAGTTCCTGCAGCGCCTCCTGCTGGTGCATGGGCGCTGGTCCTACCTGCGA
ATGTGCAAGTTTCTTTGCTATTTCTTCTACAAAAACTTTGCTTTCACCATGGTCCACTTC
TGGTTTGGCTTCTTCTGTGGCTTCTCAGCCCAGACCGTCTATGACCAGTATTTCATCACC
CTGTATAACATCGTGTACACCTCCCTGCCAGTCCTGGCTATGGGGGTCTTTGATCAGGAT
GTCCCCGAGCAGCGGAGCATGGAGTACCCTAAGCTGTATGAGCCGGGCCAGCTGAACCTT
CTCTTCAACAAGCGGGAGTTCTTCATCTGCATCGCCCAGGGCATCTACACCTCCGTGCTC
ATGTTCTTCATTCCCTATGGGGTGTTTGCTGATGCCACCCGGGATGATGGCACTCAGCTG
GCTGACTACCAGTCCTTTGCAGTCACTGTGGCCACATCCTTGGTCATTGTGGTTAGCGTG
CAGATTGGGCTCGACACAGGCTACTGGACGGCCATCAACCACTTCTTCATCTGGGGAAGC
CTTGCTGTTTACTTTGCCATCCTCTTTGCCATGCACAGCAATGGGCTCTTCGACATGTTT
CCCAACCAGTTCCGGTTTGTGGGGAATGCCCAGAACACCTTGGCCCAGCCCACGGTGTGG
CTGACCATTGTGCTCACCACAGTCGTCTGCATCATGCCCGTGGTTGCCTTCCGATTCCTC
AGGCTCAACCTGAAGCCGGATCTCTCCGACACGGTCCGCTACACACAGCTCGTGAGGAAG
AAGCAGAAGGCCCAGCACCGCTGCATGCGGCGGGTTGGCCGCACTGGCTCCCGGCGCTCC
GGCTATGCCTTCTCCCATCAGGAGGGCTTCGGGGAGCTCATCATGTCTGGCAAGAACATG
CGGCTGAGCTCTCTCGCGCTCTCCAGCTTCACCACCCGCTCCAGCTCCAGCTGGATTGAG
AGCCTGCGCAGGAAGAAGAGTGACAGTGCCAGTAGCCCCAGTGGCGGTGCCGACAAGCCC
CTCAAGGGCTGA
Enzyme 54 GenBank Gene ID Not Available
Enzyme 54 GeneCard ID ATP8B2 Link Image
Enzyme 54 GenAtlas ID ATP8B2 Link Image
Enzyme 54 HGNC ID HGNC:13534 Link Image
Enzyme 54 Chromosome Location 1
Enzyme 54 Locus 1q21.3
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References
  1. Harris MJ, Arias IM: FIC1, a P-type ATPase linked to cholestatic liver disease, has homologues (ATP8B2 and ATP8B3) expressed throughout the body. Biochim Biophys Acta. 2003 Jul 21;1633(2):127-31. [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. 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]
  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. Hirosawa M, Nagase T, Ishikawa K, Kikuno R, Nomura N, Ohara O: Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain. DNA Res. 1999 Oct 29;6(5):329-36. [PubMed Link Image]
  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]
  7. 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]
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 12929
Enzyme 55 Name Phospholipase A1 member A
Enzyme 55 Synonyms
  1. Phosphatidylserine-specific phospholipase A1
  2. PS-PLA1
Enzyme 55 Gene Name PLA1A
Enzyme 55 Protein Sequence >Phospholipase A1 member A
MPPGPWESCFWVGGLILWLSVGSSGDAPPTPQPKCADFQSANLFEGTDLKVQFLLFVPSN
PSCGQLVEGSSDLQNSGFNATLGTKLIIHGFRVLGTKPSWIDTFIRTLLRATNANVIAVD
WIYGSTGVYFSAVKNVIKLSLEISLFLNKLLVLGVSESSIHIIGVSLGAHVGGMVGQLFG
GQLGQITGLDPAGPEYTRASVEERLDAGDALFVEAIHTDTDNLGIRIPVGHVDYFVNGGQ
DQPGCPTFFYAGYSYLICDHMRAVHLYISALENSCPLMAFPCASYKAFLAGRCLDCFNPF
LLSCPRIGLVEQGGVKIEPLPKEVKVYLLTTSSAPYCMHHSLVEFHLKELRNKDTNIEVT
FLSSNITSSSKITIPKQQRYGKGIIAHATPQCQINQVKFKFQSSNRVWKKDRTTIIGKFC
TALLPVNDREKMVCLPEPVNLQASVTVSCDLKIACV
Enzyme 55 Number of Residues 456
Enzyme 55 Molecular Weight 49715.0
Enzyme 55 Theoretical pI 7.40
Enzyme 55 GO Classification
Function
  • catalytic activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 55 General Function Involved in catalytic activity
Enzyme 55 Specific Function Hydrolyzes the ester bond at the sn-1 position of glycerophospholipids and produces 2-acyl lysophospholipids. Hydrolyzes phosphatidylserine (PS) in the form of liposomes and 1- acyl-2 lysophosphatidylserine (lyso-PS), but not triolein, phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidic acid (PA) or phosphatidylinositol (PI). Isoform 2 hydrolyzes lyso-PS but not PS. Hydrolysis of lyso-PS in peritoneal mast cells activated by receptors for IgE leads to stimulate histamine production
Enzyme 55 Pathways Not Available
Enzyme 55 Reactions Not Available
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • 1-25
Enzyme 55 Transmembrane Regions
  • None
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 4090960 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID Q53H76 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name PLA1A_HUMAN Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >1371 bp
ATGCCCCCAGGTCCCTGGGAGAGCTGCTTCTGGGTGGGGGGCCTCATTTTGTGGCTCAGC
GTTGGAAGTTCAGGGGATGCACCTCCTACCCCACAGCCAAAGTGCGCTGACTTCCAGAGC
GCCAACCTTTTTGAAGGCACCGATCTCAAAGTCCAGTTTCTCCTCTTTGTCCCTTCGAAT
CCTAGCTGTGGGCAGCTAGTAGAAGGAAGCAGTGACCTCCAAAACTCTGGGTTCAATGCC
ACTCTGGGAACCAAACTAATTATCCATGGATTCAGGGTTTTAGGAACAAAGCCTTCCTGG
ATTGACACATTTATTAGAACCCTTCTGCGTGCAACGAATGCTAATGTGATTGCCGTGGAC
TGGATTTATGGGTCTACAGGAGTCTACTTCTCAGCTGTGAAAAATGTGATTAAGTTGAGC
CTCGAGATCTCCCTTTTCCTCAATAAACTCCTGGTGCTGGGTGTGTCGGAATCCTCAATC
CACATCATTGGTGTTAGCCTGGGGGCCCACGTTGGGGGCATGGTGGGACAGCTCTTCGGA
GGCCAGCTGGGACAGATCACAGGCCTGGACCCCGCTGGACCTGAGTACACCAGGGCCAGT
GTGGAAGAGCGCTTGGATGCTGGAGATGCCCTCTTCGTGGAAGCCATCCACACAGACACC
GACAATTTGGGTATTCGGATTCCCGTTGGACATGTGGACTACTTCGTCAACGGAGGCCAA
GACCAACCTGGCTGCCCCACCTTCTTTTACGCAGGTTATAGTTATCTGATCTGTGATCAC
ATGAGGGCTGTGCACCTCTACATCAGCGCCCTGGAGAATTCCTGTCCACTGATGGCCTTT
CCCTGTGCCAGCTACAAGGCCTTCCTTGCTGGACGCTGTCTGGATTGCTTTAACCCTTTT
CTGCTTTCCTGCCCAAGGATAGGACTGGTGGAACAAGGTGGTGTCAAGATAGAGCCGCTC
CCCAAGGAAGTGAAAGTCTACCTCCTGACTACTTCCAGTGCTCCGTACTGCATGCATCAC
AGCCTCGTGGAGTTTCACTTGAAGGAACTGAGAAACAAGGACACCAACATCGAGGTTACC
TTCCTTAGCAGTAACATCACCTCTTCATCTAAGATCACCATACCTAAGCAGCAACGCTAT
GGGAAAGGAATCATAGCCCATGCCACCCCACAATGCCAGATAAACCAAGTGAAATTCAAG
TTTCAGTCTTCCAACCGAGTTTGGAAAAAAGACCGGACTACCATTATTGGGAAGTTCTGC
ACTGCCCTTTTGCCTGTCAATGACAGAGAAAAGATGGTCTGCTTACCTGAACCAGTGAAC
TTACAAGCAAGTGTGACTGTTTCCTGTGACCTGAAGATAGCCTGTGTGTAG
Enzyme 55 GenBank Gene ID AF035268 Link Image
Enzyme 55 GeneCard ID PLA1A Link Image
Enzyme 55 GenAtlas ID PLA1A Link Image
Enzyme 55 HGNC ID HGNC:17661 Link Image
Enzyme 55 Chromosome Location 3
Enzyme 55 Locus 3q13.13-q13.2
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References
  1. van Groningen JJ, Egmond MR, Bloemers HP, Swart GW: nmd, a novel gene differentially expressed in human melanoma cell lines, encodes a new atypical member of the enzyme family of lipases. FEBS Lett. 1997 Mar 3;404(1):82-6. [PubMed Link Image]
  2. Nagai Y, Aoki J, Sato T, Amano K, Matsuda Y, Arai H, Inoue K: An alternative splicing form of phosphatidylserine-specific phospholipase A1 that exhibits lysophosphatidylserine-specific lysophospholipase activity in humans. J Biol Chem. 1999 Apr 16;274(16):11053-9. [PubMed Link Image]
  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. Wang J, Wen XY, Stewart AK, Hegele RA: Polymorphisms in the gene encoding phosphatidylserine-specific phospholipase A1 ( PSPLA1). J Hum Genet. 2002;47(11):611-3. [PubMed Link Image]
Enzyme 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 12930
Enzyme 56 Name Serum deprivation-response protein
Enzyme 56 Synonyms
  1. Cavin-2
  2. PS-p68
  3. Phosphatidylserine-binding protein
Enzyme 56 Gene Name SDPR
Enzyme 56 Protein Sequence >Serum deprivation-response protein
MGEDAAQAEKFQHPGSDMRQEKPSSPSPMPSSTPSPSLNLGNTEEAIRDNSQVNAVTVLT
LLDKLVNMLDAVQENQHKMEQRQISLEGSVKGIQNDLTKLSKYQASTSNTVSKLLEKSRK
VSAHTRAVKERMDRQCAQVKRLENNHAQLLRRNHFKVLIFQEENEIPASVFVKQPVSGAV
EGKEELPDENKSLEETLHTVDLSSDDDLPHDEEALEDSAEEKVEESRAEKIKRSSLKKVD
SLKKAFSRQNIEKKMNKLGTKIVSVERREKIKKSLTSNHQKISSGKSSPFKVSPLTFGRK
KVREGESHAENETKSEDLPSSEQMPNDQEEESFAEGHSEASLASALVEGEIAEEAAEKAT
SRGSNSGMDSNIDLTIVEDEEEESVALEQAQKVRYEGSYALTSEEAERSDGDPVQPAVLQ
VHQTS
Enzyme 56 Number of Residues 425
Enzyme 56 Molecular Weight 47172.8
Enzyme 56 Theoretical pI 4.88
Enzyme 56 GO Classification Not Available
Enzyme 56 General Function Involved in phosphatidylserine binding
Enzyme 56 Specific Function May play a role in targeting PRKCA to caveolae
Enzyme 56 Pathways Not Available
Enzyme 56 Reactions Not Available
Enzyme 56 Pfam Domain Function Not Available
Enzyme 56 Signals
  • None
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein 4336416 Link Image
Enzyme 56 UniProtKB/Swiss-Prot ID O95810 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name SDPR_HUMAN Link Image
Enzyme 56 PDB ID Not Available
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence >1278 bp
ATGGGAGAGGACGCTGCACAGGCCGAAAAGTTCCAGCACCCTGGGTCTGACATGCGGCAG
GAAAAGCCCTCGAGCCCCAGCCCGATGCCTTCCTCCACACCAAGCCCCAGCCTGAACCTA
GGGAACACAGAGGAGGCCATCCGGGACAACTCACAGGTGAACGCAGTCACGGTGCTCACG
CTCCTGGACAAGCTGGTGAACATGCTAGACGCTGTGCAGGAGAACCAGCACAAGATGGAG
CAGCGACAGATCAGTTTGGAGGGCTCCGTGAAGGGCATCCAGAATGACCTCACCAAGCTC
TCCAAGTACCAGGCCTCCACCAGCAACACGGTGAGCAAGCTGCTGGAGAAGTCCCGCAAG
GTCAGCGCCCACACGCGCGCGGTCAAAGAGCGCATGGATAGGCAGTGCGCACAGGTGAAG
CGGCTGGAGAACAACCACGCCCAGCTCCTCCGACGCAACCATTTCAAAGTGCTCATCTTC
CAGGAGGAAAATGAGATCCCTGCCAGCGTGTTTGTGAAACAGCCCGTTTCCGGTGCCGTG
GAAGGGAAGGAGGAGCTTCCGGATGAAAACAAATCCCTGGAGGAAACCCTGCACACCGTG
GACCTCTCCTCAGATGATGATTTGCCCCACGATGAGGAGGCCCTGGAAGACAGTGCCGAG
GAAAAGGTGGAAGAAAGTAGGGCAGAGAAAATAAAAAGATCCAGCCTGAAGAAAGTGGAT
AGCCTCAAGAAAGCATTTTCTCGCCAGAACATCGAGAAAAAGATGAACAAGCTGGGGACA
AAGATCGTATCTGTAGAGAGGAGAGAGAAGATTAAGAAATCTCTCACGTCAAATCACCAG
AAAATATCCTCAGGAAAAAGCTCCCCCTTCAAGGTTTCTCCCCTCACTTTCGGGCGGAAG
AAAGTCCGAGAGGGAGAAAGCCATGCAGAAAATGAGACCAAGTCAGAAGACCTGCCTAGC
AGTGAGCAGATGCCAAATGACCAGGAAGAGGAGTCCTTTGCAGAGGGTCATTCCGAAGCG
TCCCTCGCCAGCGCTCTGGTGGAAGGGGAAATTGCAGAGGAGGCTGCTGAGAAGGCGACC
TCCAGGGGGAGTAACTCGGGGATGGACAGCAACATCGACTTGACTATTGTGGAAGATGAA
GAGGAGGAGTCAGTGGCCCTGGAACAGGCACAGAAGGTACGCTATGAGGGTAGCTACGCG
CTAACATCCGAGGAGGCGGAGCGCTCCGATGGGGACCCCGTGCAGCCCGCCGTGCTCCAG
GTGCACCAGACCTCCTGA
Enzyme 56 GenBank Gene ID AF085481 Link Image
Enzyme 56 GeneCard ID SDPR Link Image
Enzyme 56 GenAtlas ID SDPR Link Image
Enzyme 56 HGNC ID HGNC:10690 Link Image
Enzyme 56 Chromosome Location 2
Enzyme 56 Locus 2q32-q33
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 General References
  1. Gustincich S, Vatta P, Goruppi S, Wolf M, Saccone S, Della Valle G, Baggiolini M, Schneider C: The human serum deprivation response gene (SDPR) maps to 2q32-q33 and codes for a phosphatidylserine-binding protein. Genomics. 1999 Apr 1;57(1):120-9. [PubMed Link Image]
  2. 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]
  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. Burgener R, Wolf M, Ganz T, Baggiolini M: Purification and characterization of a major phosphatidylserine-binding phosphoprotein from human platelets. Biochem J. 1990 Aug 1;269(3):729-34. [PubMed Link Image]
  5. 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]
  6. Carrascal M, Ovelleiro D, Casas V, Gay M, Abian J: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. J Proteome Res. 2008 Dec;7(12):5167-76. [PubMed Link Image]
  7. Ogata T, Ueyama T, Isodono K, Tagawa M, Takehara N, Kawashima T, Harada K, Takahashi T, Shioi T, Matsubara H, Oh H: MURC, a muscle-restricted coiled-coil protein that modulates the Rho/ROCK pathway, induces cardiac dysfunction and conduction disturbance. Mol Cell Biol. 2008 May;28(10):3424-36. Epub 2008 Mar 10. [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]
  9. 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]
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 12947
Enzyme 57 Name GPI mannosyltransferase 3
Enzyme 57 Synonyms
  1. GPI mannosyltransferase III
  2. GPI-MT-III
  3. Phosphatidylinositol-glycan biosynthesis class B protein
  4. PIG-B
Enzyme 57 Gene Name PIGB
Enzyme 57 Protein Sequence >GPI mannosyltransferase 3
MRRPLSKCGMEPGGGDASLTLHGLQNRSHGKIKLRKRKSTLYFNTQEKSARRRGDLLGEN
IYLLLFTIALRILNCFLVQTSFVPDEYWQSLEVSHHMVFNYGYLTWEWTERLRSYTYPLI
FASIYKILHLLGKDSVQLLIWIPRLAQALLSAVADVRLYSLMKQLENQEVARWVFFCQLC
SWFTWYCCTRTLTNTMETVLTIIALFYYPLEGSKSMNSVKYSSLVALAFIIRPTAVILWT
PLLFRHFCQEPRKLDLILHHFLPVGFVTLSLSLMIDRIFFGQWTLVQFNFLKFNVLQNWG
TFYGSHPWHWYFSQGFPVILGTHLPFFIHGCYLAPKRYRILLVTVLWTLLVYSMLSHKEF
RFIYPVLPFCMVFCGYSLTHLKTWKKPALSFLFLSNLFLALYTGLVHQRGTLDVMSHIQK
VCYNNPNKSSASIFIMMPCHSTPYYSHVHCPLPMRFLQCPPDLTGKSHYLDEADVFYLNP
LNWLHREFHDDASLPTHLITFSILEEEISAFLISSNYKRTAVFFHTHLPEGRIGSHIYVY
ERKLKGKFNMKMKF
Enzyme 57 Number of Residues 554
Enzyme 57 Molecular Weight 65055.9
Enzyme 57 Theoretical pI 9.57
Enzyme 57 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 57 General Function Involved in transferase activity, transferring glycosyl groups
Enzyme 57 Specific Function Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-GlcN-acyl-PI during GPI precursor assembly
Enzyme 57 Pathways Not Available
Enzyme 57 Reactions Not Available
Enzyme 57 Pfam Domain Function
Enzyme 57 Signals
  • None
Enzyme 57 Transmembrane Regions
  • 63-83 136-156 192-212 224-244 255-275 315-335 340-360 362-382 387-407
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein 62898221 Link Image
Enzyme 57 UniProtKB/Swiss-Prot ID Q92521 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name PIGB_HUMAN Link Image
Enzyme 57 PDB ID Not Available
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence >1665 bp
ATGAGGAGGCCCCTAAGCAAGTGCGGAATGGAGCCGGGGGGCGGAGATGCCAGCCTCACT
TTGCATGGTCTCCAGAACCGCTCCCACGGCAAGATAAAGCTGCGAAAGAGAAAGTCTACC
TTGTACTTCAACACCCAGGAGAAGAGCGCCAGGCGCCGCGGGGATCTTCTTGGAGAAAAT
ATTTATCTGCTCTTGTTTACCATAGCTTTACGAATATTAAACTGCTTTTTAGTGCAGACA
AGTTTTGTTCCAGATGAATACTGGCAGTCTCTTGAAGTTTCACATCACATGGTTTTCAAT
TATGGTTATTTGACTTGGGAATGGACAGAGAGACTGAGGAGTTACACTTATCCCTTAATC
TTTGCAAGCATTTACAAGATTCTTCATCTTTTAGGGAAAGATAGTGTTCAGTTGCTGATT
TGGATTCCTAGACTTGCCCAAGCACTTCTGTCTGCTGTAGCAGATGTGAGACTTTACTCA
TTAATGAAGCAACTAGAAAATCAGGAAGTGGCAAGATGGGTGTTTTTTTGCCAGTTGTGC
TCCTGGTTCACATGGTATTGCTGTACCAGAACCCTTACAAACACCATGGAAATTGTTCTC
ACTATAATTGCTCTTTTCTACTATCCTTTGGAAGGTTCAAAGTCTATGAACAGTGTCAAA
TACTCATCCCTGGTGGCACTTGCCTTCATAATTCGTCCCACAGCTGTCATTCTGTGGACA
CCTTTGCTCTTCAGACATTTCTGTCAAGAACCAAGAAAGCTTGATCTTATTCTACATCAT
TTTTTACCTGTAGGCTTTGTTACTTTGAGTTTGTCTCTGATGATTGATCGTATTTTTTTT
GGCCAATGGACTCTGGTTCAATTTAATTTTTTGAAATTTAACGTGCTGCAGAACTTGGGA
ACATTTTATGGTTCTCATCCATGGCACTGGTACTTCAGTCAAGGATTTCCAGTTATCTTG
GGTACTCACTTACCCTTCTTTATTCATGGCTGCTATCTAGCACCAAAGAGATACCGGATA
CTTTTGGTGACTGTGCTGTGGACACTGCTTGTTTATAGCATGTTGAGCCACAAAGAATTC
AGGTTTATTTATCCAGTTTTACCATTCTGTATGGTGTTCTGTGGATACTCATTAACCCAC
CTGAAAACATGGAAGAAACCAGCTCTAAGTTTCCTGTTTTTATCAAATTTGTTCCTCGCC
CTTTATACTGGTTTAGTTCATCAACGAGGTACTCTTGATGTCATGAGTCATATTCAAAAA
GTTTGTTACAACAATCCCAATAAATCTTCAGCTTCAATATTTATAATGATGCCTTGCCAC
TCTACTCCTTATTACAGCCATGTTCACTGCCCACTTCCCATGAGATTTCTCCAGTGCCCG
CCAGACCTGACTGGAAAAAGTCATTATCTTGATGAAGCAGATGTATTTTACCTAAATCCC
TTAAACTGGTTACATAGAGAGTTTCATGATGATGCATCATTGCCTACTCACTTGATCACC
TTCAGCATTTTGGAAGAGGAAATAAGCGCTTTCCTAATTTCAAGCAATTATAAAAGAACT
GCTGTTTTCTTCCACACTCACTTGCCAGAGGGTCGAATTGGAAGTCACATATATGTCTAT
GAACGGAAGTTAAAAGGGAAATTCAACATGAAGATGAAATTCTGA
Enzyme 57 GenBank Gene ID AK223330 Link Image
Enzyme 57 GeneCard ID PIGB Link Image
Enzyme 57 GenAtlas ID PIGB Link Image
Enzyme 57 HGNC ID HGNC:8959 Link Image
Enzyme 57 Chromosome Location 1
Enzyme 57 Locus 15q21-q22
Enzyme 57 SNPs SNPJam Report Link Image
Enzyme 57 General References
  1. Takahashi M, Inoue N, Ohishi K, Maeda Y, Nakamura N, Endo Y, Fujita T, Takeda J, Kinoshita T: PIG-B, a membrane protein of the endoplasmic reticulum with a large lumenal domain, is involved in transferring the third mannose of the GPI anchor. EMBO J. 1996 Aug 15;15(16):4254-61. [PubMed Link Image]
  2. 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]
  3. Mohney RP, Knez JJ, Ravi L, Sevlever D, Rosenberry TL, Hirose S, Medof ME: Glycoinositol phospholipid anchor-defective K562 mutants with biochemical lesions distinct from those in Thy-1- murine lymphoma mutants. J Biol Chem. 1994 Mar 4;269(9):6536-42. [PubMed Link Image]
Enzyme 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 12948
Enzyme 58 Name Phosphatidylinositol-glycan biosynthesis class F protein
Enzyme 58 Synonyms
  1. PIG-F
  2. GPI11 homolog
Enzyme 58 Gene Name PIGF
Enzyme 58 Protein Sequence >Phosphatidylinositol-glycan biosynthesis class F protein
MKDNDIKRLLYTHLLCIFSIILSVFIPSLFLENFSILETHLTWLCICSGFVTAVNLVLYL
VVKPNTSSKRSSLSHKVTGFLKCCIYFLMSCFSFHVIFVLYGAPLIELALETFLFAVILS
TFTTVPCLCLLGPNLKAWLRVFSRNGVTSIWENSLQITTISSFVGAWLGALPIPLDWERP
WQVWPISCTLGATFGYVAGLVISPLWIYWNRKQLTYKNN
Enzyme 58 Number of Residues 219
Enzyme 58 Molecular Weight 24889.3
Enzyme 58 Theoretical pI 8.64
Enzyme 58 GO Classification
Function
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
  • organelle membrane
Enzyme 58 General Function Involved in GPI anchor biosynthetic process
Enzyme 58 Specific Function Involved in GPI-anchor biosynthesis through the transfer of ethanolamine phosphate to the third mannose of GPI
Enzyme 58 Pathways Not Available
Enzyme 58 Reactions Not Available
Enzyme 58 Pfam Domain Function
Enzyme 58 Signals
  • None
Enzyme 58 Transmembrane Regions
  • 11-31 42-62 86-106 113-133 155-175 189-209
Enzyme 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein 4505797 Link Image
Enzyme 58 UniProtKB/Swiss-Prot ID Q07326 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name PIGF_HUMAN Link Image
Enzyme 58 PDB ID Not Available
Enzyme 58 Cellular Location Not Available
Enzyme 58 Gene Sequence >660 bp
ATGAAAGATAACGATATCAAGAGACTACTGTATACCCATCTTTTATGCATATTTTCAATT
ATCCTAAGTGTCTTCATTCCATCACTCTTCTTGGAGAACTTCTCAATATTGGAAACACAC
TTGACATGGTTGTGCATCTGTTCTGGTTTTGTAACTGCTGTCAATCTAGTACTATATTTA
GTAGTGAAACCAAATACATCCTCTAAAAGAAGTTCATTATCACACAAGGTAACTGGATTT
TTGAAATGCTGTATCTACTTTCTTATGTCTTGTTTCTCCTTTCATGTAATTTTTGTTCTG
TATGGAGCACCACTGATAGAGTTGGCATTGGAAACATTTTTATTTGCAGTTATTTTGTCT
ACTTTTACTACTGTGCCTTGCTTATGTTTGTTAGGACCAAACCTCAAAGCATGGCTAAGA
GTGTTCAGTAGAAATGGAGTTACATCCATATGGGAGAATAGTCTCCAGATCACTACAATT
TCTAGCTTTGTAGGAGCATGGCTTGGAGCACTTCCTATTCCACTGGATTGGGAAAGACCA
TGGCAGGTATGGCCCATCTCCTGTACGCTTGGAGCGACCTTTGGCTACGTGGCTGGCCTT
GTTATTTCACCACTCTGGATATACTGGAATAGAAAGCAACTTACATACAAGAACAATTAA
Enzyme 58 GenBank Gene ID NM_002643.3 Link Image
Enzyme 58 GeneCard ID PIGF Link Image
Enzyme 58 GenAtlas ID PIGF Link Image
Enzyme 58 HGNC ID HGNC:8962 Link Image
Enzyme 58 Chromosome Location 2
Enzyme 58 Locus 2p21-p16
Enzyme 58 SNPs SNPJam Report Link Image
Enzyme 58 General References
  1. Inoue N, Kinoshita T, Orii T, Takeda J: Cloning of a human gene, PIG-F, a component of glycosylphosphatidylinositol anchor biosynthesis, by a novel expression cloning strategy. J Biol Chem. 1993 Apr 5;268(10):6882-5. [PubMed Link Image]
  2. 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]
  3. Shishioh N, Hong Y, Ohishi K, Ashida H, Maeda Y, Kinoshita T: GPI7 is the second partner of PIG-F and involved in modification of glycosylphosphatidylinositol. J Biol Chem. 2005 Mar 11;280(10):9728-34. Epub 2005 Jan 4. [PubMed Link Image]
Enzyme 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 12949
Enzyme 59 Name GPI ethanolamine phosphate transferase 2
Enzyme 59 Synonyms
  1. GPI7 homolog
  2. hGPI7
  3. Phosphatidylinositol-glycan biosynthesis class G protein
  4. PIG-G
Enzyme 59 Gene Name PIGG
Enzyme 59 Protein Sequence >GPI ethanolamine phosphate transferase 2
MRLGSGTFATCCVAIEVLGIAVFLRGFFPAPVRSSARAEHGAEPPAPEPSAGASSNWTTL
PPPLFSKVVIVLIDALRDDFVFGSKGVKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIK
ALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGT
TSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMD
SVLMKIHTSLQSKERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP
GDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLLFPVVEGRPMREQLRFLHLNTVQLSK
LLQENVPSYEKDPGFEQFKMSERLHGNWIRLYLEEKHSEVLFNLGSKVLRQYLDALKTLS
LSLSAQVAQYDIYSMMVGTVVVLEVLTLLLLSVPQALRRKAELEVPLSSPGFSLLFYLVI
LVLSAVHVIVCTSAESSCYFCGLSWLAAGGVMVLASALLCVIVSVLTNVLVGGNTPRKNP
MHPSSRWSELDLLILLGTAGHVLSLGASSFVEEEHQTWYFLVNTLCLALSQETYRNYFLG
DDGEPPCGLCVEQGHDGATAAWQDGPGCDVLERDKGHGSPSTSEVLRGREKWMVLASPWL
ILACCRLLRSLNQTGVQWAHRPDLGHWLTSSDHKAELSVLAALSLLVVFVLVQRGCSPVS
KAALALGLLGVYCYRAAIGSVRFPWRPDSKDISKGIIEARFVYVFVLGILFTGTKDLLKS
QVIAADFKLKTVGLWEIYSGLVLLAALLFRPHNLPVLAFSLLIQTLMTKFIWKPLRHDAA
EITVMHYWFGQAFFYFQGNSNNIATVDISAGFVGLDTYVEIPAVLLTAFGTYAGPVLWAS
HLVHFLSSETRSGSALSHACFCYALICSIPVFTYIVLVTSLRYHLFIWSVFSPKLLYEGM
HLLITAAVCVFFTAMDQTRLTQS
Enzyme 59 Number of Residues 983
Enzyme 59 Molecular Weight 108171.7
Enzyme 59 Theoretical pI 7.15
Enzyme 59 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 59 General Function Involved in catalytic activity
Enzyme 59 Specific Function Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose
Enzyme 59 Pathways Not Available
Enzyme 59 Reactions Not Available
Enzyme 59 Pfam Domain Function
Enzyme 59 Signals
  • None
Enzyme 59 Transmembrane Regions
  • 432-452 471-491 506-526 552-572 699-719 721-741 752-772 789-809 812-832 879-899 919-939 955-975
Enzyme 59 Essentiality Not Available
Enzyme 59 GenBank ID Protein 58430451 Link Image
Enzyme 59 UniProtKB/Swiss-Prot ID Q5H8A4 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name PIGG_HUMAN Link Image
Enzyme 59 PDB ID Not Available
Enzyme 59 Cellular Location Not Available
Enzyme 59 Gene Sequence >2952 bp
ATGCGGCTGGGCTCCGGGACTTTCGCTACCTGTTGCGTAGCGATCGAGGTGCTAGGGATC
GCGGTCTTCCTTCGGGGATTCTTCCCGGCTCCCGTTCGTTCCTCTGCCAGAGCGGAACAC
GGAGCGGAGCCCCCAGCGCCCGAACCCTCGGCTGGAGCCAGTTCTAACTGGACCACGCTG
CCACCACCTCTCTTCAGTAAAGTTGTTATTGTTCTGATAGATGCCTTGAGAGATGATTTT
GTGTTTGGGTCAAAGGGTGTGAAATTTATGCCCTACACAACTTACCTTGTGGAAAAAGGA
GCATCTCACAGTTTTGTGGCTGAAGCAAAGCCACCTACAGTTACTATGCCTCGAATCAAG
GCATTGATGACGGGGAGCCTTCCTGGCTTTGTCGACGTCATCAGGAACCTCAATTCTCCT
GCACTGCTGGAAGACAGTGTGATAAGACAAGCAAAAGCAGCTGGAAAAAGAATAGTCTTT
TATGGAGATGAAACCTGGGTTAAATTATTCCCAAAGCATTTTGTGGAATATGATGGAACA
ACCTCATTTTTCGTGTCAGATTACACAGAGGTGGATAATAATGTCACGAGGCATTTGGAT
AAAGTATTAAAAAGAGGAGATTGGGACATATTAATCCTCCACTACCTGGGGCTGGACCAC
ATTGGCCACATTTCAGGGCCCAACAGCCCCCTGATTGGGCAGAAGCTGAGCGAGATGGAC
AGCGTGCTGATGAAGATCCACACCTCACTGCAGTCGAAGGAGAGAGAGACGCCTTTACCC
AATTTGCTGGTTCTTTGTGGTGACCATGGCATGTCTGAAACAGGAAGTCACGGGGCCTCC
TCCACCGAGGAGGTGAATACACCTCTGATTTTAATCAGTTCTGCGTTTGAAAGGAAACCC
GGTGATATCCGACATCCAAAGCACGTCCAACAGACGGATGTGGCTGCGACACTGGCGATA
GCACTTGGCTTACCGATTCCAAAAGACAGTGTAGGGAGCCTCCTATTCCCAGTTGTGGAA
GGAAGACCAATGAGAGAGCAGTTGAGATTTTTACATTTGAATACAGTGCAGCTTAGTAAA
CTGTTGCAAGAGAATGTGCCGTCATATGAAAAAGATCCTGGGTTTGAGCAGTTTAAAATG
TCAGAAAGATTGCATGGGAACTGGATCAGACTGTACTTGGAGGAAAAGCATTCAGAAGTC
CTATTCAACCTGGGCTCCAAGGTTCTCAGGCAGTACCTGGATGCTCTGAAGACGCTGAGC
TTGTCCCTGAGTGCACAAGTGGCCCAGTACGACATCTATTCGATGATGGTGGGGACTGTC
GTGGTTTTGGAGGTTCTCACCCTGCTCCTGCTCAGCGTCCCACAGGCACTGCGCAGAAAG
GCTGAGCTGGAAGTCCCACTGTCATCTCCTGGGTTTTCTCTGCTCTTTTATTTGGTGATC
CTGGTTCTTTCGGCCGTTCACGTCATTGTGTGCACCTCAGCTGAAAGTTCGTGCTACTTC
TGTGGCCTCTCGTGGCTGGCGGCAGGTGGGGTGATGGTGCTGGCCTCGGCGCTGCTGTGT
GTGATTGTGTCTGTTCTGACCAACGTGCTCGTGGGTGGAAACACCCCAAGGAAGAACCCC
ATGCATCCCAGCTCAAGGTGGTCAGAGCTAGACCTTCTTATTCTGTTGGGGACGGCGGGC
CACGTCTTGAGCCTGGGCGCCAGCAGCTTCGTGGAGGAGGAGCACCAGACCTGGTACTTC
CTTGTGAACACCCTGTGTCTAGCTCTGAGCCAAGAAACCTACAGAAACTACTTTCTGGGA
GATGACGGTGAGCCTCCGTGTGGCCTCTGTGTGGAACAAGGGCATGACGGGGCCACAGCA
GCGTGGCAGGACGGGCCTGGCTGTGATGTCCTGGAGCGAGACAAAGGCCACGGAAGCCCC
TCTACCTCCGAAGTGCTCAGAGGCCGCGAGAAGTGGATGGTGCTGGCCAGTCCGTGGCTA
ATACTGGCCTGCTGCCGGCTGCTGCGCTCCCTAAACCAGACAGGTGTGCAGTGGGCTCAC
CGGCCTGACCTCGGCCACTGGCTCACCAGCTCTGACCACAAAGCCGAGCTCTCTGTCCTG
GCTGCCCTCTCCCTCCTCGTAGTTTTTGTGCTGGTGCAGAGGGGGTGCTCCCCTGTGTCC
AAGGCTGCCCTGGCGCTGGGGCTGCTGGGCGTCTACTGCTACCGGGCGGCCATCGGGAGT
GTCCGGTTCCCGTGGCGGCCGGACAGCAAGGACATTTCCAAGGGTATTATTGAAGCTCGT
TTTGTTTATGTCTTTGTCCTTGGCATTCTGTTCACGGGCACCAAAGACTTACTTAAATCT
CAAGTCATTGCTGCAGACTTCAAACTCAAGACTGTAGGTTTATGGGAGATATATAGTGGA
TTAGTTCTTCTGGCAGCCTTGCTCTTTAGACCACATAATCTTCCGGTCTTAGCATTTAGC
CTCTTGATTCAGACTCTAATGACTAAATTCATCTGGAAGCCCCTGAGACACGATGCAGCT
GAGATTACTGTGATGCATTATTGGTTTGGTCAAGCATTCTTCTATTTTCAGGGCAACTCC
AACAACATTGCCACCGTGGACATCTCCGCAGGCTTCGTGGGCTTAGACACCTACGTGGAA
ATCCCAGCCGTGCTCCTGACAGCGTTTGGGACGTACGCAGGGCCTGTGCTGTGGGCCAGC
CACTTAGTGCACTTCCTGAGCTCAGAAACACGCAGTGGTTCAGCACTGAGTCATGCTTGC
TTCTGCTACGCACTGATTTGTTCTATTCCAGTTTTCACGTACATCGTTTTGGTGACATCT
CTGCGTTATCATTTATTTATATGGAGTGTATTTTCTCCAAAACTTCTCTACGAGGGAATG
CACCTGCTCATTACAGCTGCTGTCTGTGTATTCTTCACGGCAATGGATCAAACCAGACTC
ACACAGTCTTAG
Enzyme 59 GenBank Gene ID AB162713 Link Image
Enzyme 59 GeneCard ID PIGG Link Image
Enzyme 59 GenAtlas ID PIGG Link Image
Enzyme 59 HGNC ID HGNC:25985 Link Image
Enzyme 59 Chromosome Location 4
Enzyme 59 Locus 4p16.3
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 General References
  1. Shishioh N, Hong Y, Ohishi K, Ashida H, Maeda Y, Kinoshita T: GPI7 is the second partner of PIG-F and involved in modification of glycosylphosphatidylinositol. J Biol Chem. 2005 Mar 11;280(10):9728-34. Epub 2005 Jan 4. [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. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [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]
Enzyme 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 12950
Enzyme 60 Name GPI ethanolamine phosphate transferase 1
Enzyme 60 Synonyms
  1. MCD4 homolog
  2. Phosphatidylinositol-glycan biosynthesis class N protein
  3. PIG-N
Enzyme 60 Gene Name PIGN
Enzyme 60 Protein Sequence >GPI ethanolamine phosphate transferase 1
MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALY
ELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENP
VEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFD
NVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKE
IVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQ
FDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILPVDYLNNTDLFKAESM
FTNAVQILEQFKVKMTQKKEVTLPFLFTPFKLLSDSKQFNILRKARSYIKHRKFDEVVSL
CKELIHLALKGLSYYHTYDRFFLGVNVVIGFVGWISYASLLIIKSHSNLIKGVSKEVKKP
SHLLPCSFVAIGILVAFFLLIQACPWTYYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYP
LSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFLTRLWTRAKMTSLSWTFFSL
LLAVFPLMPVVGRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKEELLVHLLQVLST
VLSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLVVPLLSSPVLFQRLFSILLSLMST
YLLLSTGYEALFPLVLSCLMFVWINIEQETLQQSGVCCKQKLTSIQFSYNTDITQFRQLY
LDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFV
LVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGSWLDIGTSISHYVIVMS
MTIFLVFLNGLAQLLTTKKLRLCGKPKSHFM
Enzyme 60 Number of Residues 931
Enzyme 60 Molecular Weight 105809.2
Enzyme 60 Theoretical pI 8.87
Enzyme 60 GO Classification
Function
  • catalytic activity
  • transferase activity
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • membrane
  • organelle membrane
Enzyme 60 General Function Involved in catalytic activity
Enzyme 60 Specific Function Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor
Enzyme 60 Pathways Not Available
Enzyme 60 Reactions Not Available
Enzyme 60 Pfam Domain Function
Enzyme 60 Signals
  • None
Enzyme 60 Transmembrane Regions
  • 2-24 443-463 483-503 509-529 544-564 566-586 592-612 619-639 650-670 686-706 724-744 787-807 825-845 859-879 895-915
Enzyme 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein 4206155 Link Image
Enzyme 60 UniProtKB/Swiss-Prot ID O95427 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name PIGN_HUMAN Link Image
Enzyme 60 PDB ID Not Available
Enzyme 60 Cellular Location Not Available
Enzyme 60 Gene Sequence >2796 bp
ATGCTGCTGTTCTTTACTTTGGGATTGCTTATACATTTTGTGTTCTTCGCCTCCATCTTT
GACATTTATTTTACATCTCCTTTGGTTCATGGAATGACTCCTCAGTTTACACCATTGCCT
CCTCCAGCGAGAAGATTAGTGTTGTTTGTTGCTGATGGCCTTCGAGCAGATGCACTTTAC
GAATTAGATGAAAATGGAAACTCTAGAGCACCGTTTATTAGGAATATCATAATGCATGAA
GGCAGCTGGGGCATATCTCATACACGTGTGCCAACAGAATCTCGGCCAGGTCATGTAGCT
CTGATAGCTGGGTTTTATGAAGATGTCAGTGCAGTTGCCAAAGGATGGAAGGAAAATCCT
GTAGAGTTTGATTCTCTTTTTAATGAAAGTAAATACACATGGAGCTGGGGAAGCCCAGAT
ATCCTGCCTATGTTTGCCAAAGGTGCTAGTGGAGACCACGTTTATACATATAGTTATGAT
GCTAAAAGAGAGGATTTTGGTGCTCAAGATGCAACAAAACTGGATACGTGGGTTTTTGAT
AATGTTAAGGACTTCTTTCATCATGCCAGAAACAACCAGTCTTTGTTTTCTAAAATAAAT
GAAGAGAAAATAGTTTTTTTCTTACATTTATTAGGAATAGATACAAACGGACATGCTCAT
CGACCATCCTCGAGAGACTACAAGCACAATATTAAAAAAGTTGATGATGGAGTTAAAGAA
ATCGTGTCTATGTTTAACCACTTCTATGGAAATGATGGGAAAACAACATTTATCTTTACC
TCTGACCATGGAATGACAGACTGGGGTTCCCATGGGGCTGGTCATCCTTCAGAGACTTTA
ACTCCTTTAGTCACTTGGGGAGCTGGAATCAAGTATCCCCAAAGAGTATCAGCTCAGCAA
TTTGATGATGCATTTTTGAAAGAGTGGAGATTGGAGAATTGGAAGAGGCTAGATGTCAAT
CAGGCTGATATTGCACCATTGATGACTTCCCTTATTGGAGTTCCCTTTCCTCTTAACTCA
GTGGGAATCCTTCCTGTGGATTATCTTAACAACACTGATCTCTTCAAAGCAGAGAGCATG
TTTACAAATGCAGTACAGATTCTTGAACAGTTCAAGGTGAAAATGACTCAGAAGAAAGAA
GTTACTTTACCATTTTTGTTTACACCATTTAAACTGCTTTCTGATTCCAAACAGTTCAAC
ATTTTAAGAAAAGCAAGATCTTATATAAAACACAGAAAGTTTGATGAAGTGGTCTCCCTT
TGCAAGGAGCTAATTCATCTTGCATTGAAAGGATTGTCCTATTATCACACATATGACAGA
TTCTTTTTGGGCGTCAATGTTGTTATTGGTTTTGTGGGATGGATATCTTATGCCTCTTTG
TTGATCATCAAGTCTCATTCCAACCTTATAAAAGGTGTTAGTAAAGAAGTGAAGAAACCA
AGCCATCTCCTGCCTTGTAGTTTTGTAGCTATTGGCATTTTAGTAGCATTTTTTCTGCTG
ATTCAAGCCTGTCCCTGGACATATTATGTATATGGTTTGTTGCCACTGCCAATATGGTAT
GCGGTTCTAAGAGAATTTCAAGTTATTCAGGACCTTGTTGTATCAGTGTTGACCTATCCT
CTGAGCCATTTTGTTGGGTACCTGTTAGCCTTTACCCTGGGAATTGAAGTATTAGTTCTC
AGTTTTTTCTACCGCTATATGCTTACCGCTGGACTTACTGCCTTTGCAGCTTGGCCATTT
CTCACTCGGCTGTGGACTCGAGCAAAGATGACCTCACTGAGTTGGACTTTCTTCTCTTTG
CTCCTGGCAGTGTTCCCACTGATGCCGGTTGTAGGTCGAAAGCCAGACATCTCTCTAGTG
ATGGGTGCAGGCTTGCTGGTTCTTCTGTTATCCCTGTGTGTTGTAACATCTCTCATGAAA
AGAAAAGATAGCTTTATAAAGGAAGAGCTATTGGTACATCTGTTACAGGTGCTGAGCACA
GTGCTCTCCATGTATGTTGTGTATAGCACTCAGAGTAGTTTACTCAGGAAGCAAGGACTG
CCTCTCATGAATCAAATTATTAGCTGGGCAACATTAGCCTCTTCCTTGGTTGTGCCACTA
CTGAGTTCTCCAGTTCTCTTTCAGCGATTGTTCAGCATACTTCTTTCATTGATGTCAACC
TACCTACTTCTAAGCACAGGGTATGAAGCTCTCTTTCCACTAGTGTTGTCTTGTTTGATG
TTTGTCTGGATAAACATAGAACAAGAAACTCTACAACAATCTGGTGTTTGCTGTAAACAA
AAGCTCACCAGTATCCAGTTCTCTTATAATACTGATATAACTCAGTTTCGACAGCTATAT
CTGGATGACATCCGTAGGGCCTTTTTCCTTGTTTTCTTCTTAGTGACAGCATTTTTTGGA
ACTGGAAATATAGCTTCTATTAACAGCTTTGATCTTGCCTCTGTCTATTGCTTTCTGACT
GTGTTCAGTCCTTTTATGATGGGAGCCCTGATGATGTGGAAGATTTTAATCCCCTTTGTT
CTTGTTATGTGTGCTTTTGAAGCAGTTCAGTTGACTACTCAGTTATCGTCAAAAAGCCTT
TTTCTCATTGTTCTCGTCATATCAGACATTATGGCTTTGCATTTTTTCTTCTTGGTCAAG
GATTATGGCAGCTGGCTTGATATTGGGACAAGCATCAGCCACTATGTGATTGTCATGTCC
ATGACCATCTTTTTGGTGTTCCTCAATGGCCTGGCCCAGCTGCTCACAACGAAGAAACTC
AGACTATGTGGCAAACCCAAAAGTCACTTCATGTGA
Enzyme 60 GenBank Gene ID AF109219 Link Image
Enzyme 60 GeneCard ID PIGN Link Image
Enzyme 60 GenAtlas ID PIGN Link Image
Enzyme 60 HGNC ID HGNC:8967 Link Image
Enzyme 60 Chromosome Location 1
Enzyme 60 Locus 18q21.33
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 General References
  1. Gaynor EC, Mondesert G, Grimme SJ, Reed SI, Orlean P, Emr SD: MCD4 encodes a conserved endoplasmic reticulum membrane protein essential for glycosylphosphatidylinositol anchor synthesis in yeast. Mol Biol Cell. 1999 Mar;10(3):627-48. [PubMed Link Image]
  2. 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]
  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]
Enzyme 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 12951
Enzyme 61 Name GPI ethanolamine phosphate transferase 3
Enzyme 61 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class O protein
  2. PIG-O
Enzyme 61 Gene Name PIGO
Enzyme 61 Protein Sequence >GPI ethanolamine phosphate transferase 3
MQKASVLLFLAWVCFLFYAGIALFTSGFLLTRLELTNHSSCQEPPGPGSLPWGSQGKPGA
CWMASRFSRVVLVLIDALRFDFAQPQHSHVPREPPVSLPFLGKLSSLQRILEIQPHHARL
YRSQVDPPTTTMQRLKALTTGSLPTFIDAGSNFASHAIVEDNLIKQLTSAGRRVVFMGDD
TWKDLFPGAFSKAFFFPSFNVRDLDTVDNGILEHLYPTMDSGEWDVLIAHFLGVDHCGHK
HGPHHPEMAKKLSQMDQVIQGLVERLENDTLLVVAGDHGMTTNGDHGGDSELEVSAALFL
YSPTAVFPSTPPEEPEVIPQVSLVPTLALLLGLPIPFGNIGEVMAELFSGGEDSQPHSSA
LAQASALHLNAQQVSRFLHTYSAATQDLQAKELHQLQNLFSKASADYQWLLQSPKGAEAT
LPTVIAELQQFLRGARAMCIESWARFSLVRMAGGTALLAASCFICLLASQWAISPGFPFC
PLLLTPVAWGLVGAIAYAGLLGTIELKLDLVLLGAVAAVSSFLPFLWKAWAGWGSKRPLA
TLFPIPGPVLLLLLFRLAVFFSDSFVVAEARATPFLLGSFILLLVVQLHWEGQLLPPKLL
TMPRLGTSATTNPPRHNGAYALRLGIGLLLCTRLAGLFHRCPEETPVCHSSPWLSPLASM
VGGRAKNLWYGACVAALVALLAAVRLWLRRYGNLKSPEPPMLFVRWGLPLMALGTAAYWA
LASGADEAPPRLRVLVSGASMVLPRAVAGLAASGLALLLWKPVTVLVKAGAGAPRTRTVL
TPFSGPPTSQADLDYVVPQIYRHMQEEFRGRLERTKSQGPLTVAAYQLGSVYSAAMVTAL
TLLAFPLLLLHAERISLVFLLLFLQSFLLLHLLAAGIPVTTPGPFTVPWQAVSAWALMAT
QTFYSTGHQPVFPAIHWHAAFVGFPEGHGSCTWLPALLVGANTFASHLLFAVGCPLLLLW
PFLCESQGLRKRQQPPGNEADARVRPEEEEEPLMEMRLRDAPQHFYAALLQLGLKYLFIL
GIQILACALAASILRRHLMVWKVFAPKFIFEAVGFIVSSVGLLLGIALVMRVDGAVSSWF
RQLFLAQQR
Enzyme 61 Number of Residues 1089
Enzyme 61 Molecular Weight 118697.6
Enzyme 61 Theoretical pI 8.18
Enzyme 61 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 61 General Function Involved in catalytic activity
Enzyme 61 Specific Function Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI third mannose which links the GPI-anchor to the C-terminus of the proteins by an amide bond
Enzyme 61 Pathways Not Available
Enzyme 61 Reactions Not Available
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • 4-24 457-477 482-502 510-530 541-561 575-595 668-688 701-721 747-767 830-850 857-877 944-964 1014-1034 1048-1068
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein 23397648 Link Image
Enzyme 61 UniProtKB/Swiss-Prot ID Q8TEQ8 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name PIGO_HUMAN Link Image
Enzyme 61 PDB ID Not Available
Enzyme 61 Cellular Location Not Available
Enzyme 61 Gene Sequence >3270 bp
ATGCAGAAAGCCTCAGTGTTGCTCTTCCTGGCCTGGGTCTGCTTCCTCTTCTACGCTGGC
ATTGCCCTCTTCACCAGTGGCTTCCTGCTCACCCGTTTGGAGCTCACCAACCATAGCAGC
TGCCAAGAGCCCCCAGGCCCTGGGTCCCTGCCATGGGGGAGCCAAGGGAAACCTGGGGCC
TGCTGGATGGCTTCCCGATTTTCGCGGGTTGTGTTGGTGCTGATAGATGCTCTGCGATTT
GACTTCGCCCAGCCCCAGCATTCACACGTGCCTAGAGAGCCTCCTGTCTCCCTACCCTTC
CTGGGCAAACTAAGCTCCTTGCAGAGGATCCTGGAGATTCAGCCCCACCATGCCCGGCTC
TACCGATCTCAGGTTGACCCTCCTACCACCACCATGCAGCGCCTCAAGGCCCTCACCACT
GGCTCACTGCCTACCTTTATTGATGCTGGTAGTAACTTCGCCAGCCACGCCATAGTGGAA
GACAATCTCATTAAGCAGCTCACCAGTGCAGGAAGGCGTGTAGTCTTCATGGGAGATGAT
ACCTGGAAAGACCTTTTCCCTGGTGCTTTCTCCAAAGCTTTCTTCTTCCCATCCTTCAAT
GTCAGAGACCTAGACACAGTGGACAATGGCATCCTGGAACACCTCTACCCCACCATGGAC
AGTGGTGAATGGGACGTGCTGATTGCTCACTTCCTGGGTGTGGACCACTGTGGCCACAAG
CATGGCCCTCACCACCCTGAAATGGCCAAGAAACTTAGCCAGATGGACCAGGTGATCCAG
GGACTTGTGGAGCGTCTGGAGAATGACACACTGCTGGTAGTGGCTGGGGACCATGGGATG
ACCACAAATGGAGACCATGGAGGGGACAGTGAGCTGGAGGTCTCAGCTGCTCTCTTTCTG
TATAGCCCCACAGCAGTCTTCCCCAGCACCCCACCAGAGGAGCCAGAGGTGATTCCTCAA
GTTAGCCTTGTGCCCACGCTGGCCCTGCTGCTGGGCCTGCCCATCCCATTTGGGAATATC
GGGGAAGTGATGGCTGAGCTATTCTCAGGGGGTGAGGACTCCCAGCCCCACTCCTCTGCT
TTAGCCCAAGCCTCAGCTCTCCATCTCAATGCTCAGCAGGTGTCCCGATTTCTTCATACC
TACTCAGCTGCTACTCAGGACCTTCAAGCTAAGGAGCTTCATCAGCTGCAGAACCTCTTC
TCCAAGGCCTCTGCTGACTACCAGTGGCTTCTCCAGAGCCCCAAGGGGGCTGAGGCGACA
CTGCCGACTGTGATTGCTGAGCTGCAGCAGTTCCTGCGGGGAGCTCGGGCCATGTGCATC
GAGTCTTGGGCTCGTTTCTCTCTGGTCCGCATGGCGGGGGGTACTGCTCTCTTGGCTGCT
TCCTGCTTTATCTGCCTGCTGGCATCTCAGTGGGCAATATCCCCAGGCTTTCCATTCTGC
CCTCTACTCCTGACACCTGTGGCCTGGGGCCTGGTTGGGGCCATAGCGTATGCTGGACTC
CTGGGAACTATTGAGCTGAAGCTAGATCTAGTGCTTCTAGGGGCTGTGGCTGCAGTGAGC
TCATTCCTCCCTTTTCTGTGGAAAGCCTGGGCTGGCTGGGGGTCCAAGAGGCCCCTGGCA
ACCCTGTTTCCCATCCCTGGGCCCGTCCTGTTACTCCTGCTGTTTCGCTTGGCTGTGTTC
TTCTCTGATAGTTTTGTTGTAGCTGAGGCCAGGGCCACCCCCTTCCTTTTGGGCTCATTC
ATCCTGCTCCTGGTTGTCCAGCTTCACTGGGAGGGCCAGCTGCTTCCACCTAAGCTACTC
ACAATGCCCCGCCTTGGCACTTCAGCCACAACAAACCCCCCACGGCACAATGGTGCATAT
GCCCTGAGGCTTGGAATTGGGTTGCTTTTATGTACAAGGCTAGCTGGGCTTTTTCATCGT
TGCCCTGAAGAGACACCTGTTTGCCACTCCTCTCCCTGGCTGAGTCCTCTGGCATCCATG
GTGGGTGGTCGAGCCAAGAATTTGTGGTATGGAGCTTGTGTGGCGGCGCTGGTGGCCCTG
TTAGCTGCCGTGCGCTTGTGGCTTCGCCGCTATGGTAATCTCAAGAGCCCCGAGCCACCC
ATGCTCTTTGTGCGCTGGGGACTGCCCCTAATGGCATTGGGTACTGCTGCCTACTGGGCA
TTGGCGTCGGGGGCAGATGAGGCTCCCCCCCGTCTCCGGGTCCTGGTCTCTGGGGCATCC
ATGGTGCTGCCTCGGGCTGTAGCAGGGCTGGCTGCTTCAGGGCTCGCGCTGCTGCTCTGG
AAGCCTGTGACAGTGCTGGTGAAGGCTGGGGCAGGCGCTCCAAGGACCAGGACTGTCCTC
ACTCCCTTCTCAGGCCCCCCCACTTCTCAAGCTGACTTGGATTATGTGGTCCCTCAAATC
TACCGACACATGCAGGAGGAGTTCCGGGGCCGGTTAGAGAGGACCAAATCTCAGGGTCCC
CTGACTGTGGCTGCTTATCAGTTGGGGAGTGTCTACTCAGCTGCTATGGTCACAGCCCTC
ACCCTGTTGGCCTTCCCACTTCTGCTGTTGCATGCGGAGCGCATCAGCCTTGTGTTCCTG
CTTCTGTTTCTGCAGAGCTTCCTTCTCCTACATCTGCTTGCTGCTGGGATACCCGTCACC
ACCCCTGGTCCTTTTACTGTGCCATGGCAGGCAGTCTCGGCTTGGGCCCTCATGGCCACA
CAGACCTTCTACTCCACAGGCCACCAGCCTGTCTTTCCAGCCATCCATTGGCATGCAGCC
TTCGTGGGATTCCCAGAGGGTCATGGCTCCTGTACTTGGCTGCCTGCTTTGCTAGTGGGA
GCCAACACCTTTGCCTCCCACCTCCTCTTTGCAGTAGGTTGCCCACTGCTCCTGCTCTGG
CCTTTCCTGTGTGAGAGTCAAGGGCTGCGGAAGAGACAGCAGCCCCCAGGGAATGAAGCT
GATGCCAGAGTCAGACCCGAGGAGGAAGAGGAGCCACTGATGGAGATGCGGCTCCGGGAT
GCGCCTCAGCACTTCTATGCAGCACTGCTGCAGCTGGGCCTCAAGTACCTCTTTATCCTT
GGTATTCAGATTCTGGCCTGTGCCTTGGCAGCCTCCATCCTTCGCAGGCATCTCATGGTC
TGGAAAGTGTTTGCCCCTAAGTTCATATTTGAGGCTGTGGGCTTCATTGTGAGCAGCGTG
GGACTTCTCCTGGGCATAGCTTTGGTGATGAGAGTGGATGGTGCTGTGAGCTCCTGGTTC
AGGCAGCTATTTCTGGCCCAGCAGAGGTAG
Enzyme 61 GenBank Gene ID NM_032634.2 Link Image
Enzyme 61 GeneCard ID PIGO Link Image
Enzyme 61 GenAtlas ID PIGO Link Image
Enzyme 61 HGNC ID HGNC:23215 Link Image
Enzyme 61 Chromosome Location 9
Enzyme 61 Locus 9p13.3
Enzyme 61 SNPs SNPJam Report Link Image
Enzyme 61 General References
  1. 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]
  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. 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]
  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. 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]
  6. 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 61 Metabolite References Not Available
Enzyme 62 [top]
Enzyme 62 ID 12952
Enzyme 62 Name GPI transamidase component PIG-S
Enzyme 62 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class S protein
Enzyme 62 Gene Name PIGS
Enzyme 62 Protein Sequence >GPI transamidase component PIG-S
MAAAGAAATHLEVARGKRAALFFAAVAIVLGLPLWWKTTETYRASLPYSQISGLNALQLR
LMVPVTVVFTRESVPLDDQEKLPFTVVHEREIPLKYKMKIKCRFQKAYRRALDHEEEALS
SGSVQEAEAMLDEPQEQAEGSLTVYVISEHSSLLPQDMMSYIGPKRTAVVRGIMHREAFN
IIGRRIVQVAQAMSLTEDVLAAALADHLPEDKWSAEKRRPLKSSLGYEITFSLLNPDPKS
HDVYWDIEGAVRRYVQPFLNALGAAGNFSVDSQILYYAMLGVNPRFDSASSSYYLDMHSL
PHVINPVESRLGSSAASLYPVLNFLLYVPELAHSPLYIQDKDGAPVATNAFHSPRWGGIM
VYNVDSKTYNASVLPVRVEVDMVRVMEVFLAQLRLLFGIAQPQLPPKCLLSGPTSEGLMT
WELDRLLWARSVENLATATTTLTSLAQLLGKISNIVIKDDVASEVYKAVAAVQKSAEELA
SGHLASAFVASQEAVTSSELAFFDPSLLHLLYFPDDQKFAIYIPLFLPMAVPILLSLVKI
FLETRKSWRKPEKTD
Enzyme 62 Number of Residues 555
Enzyme 62 Molecular Weight 61655.5
Enzyme 62 Theoretical pI 6.46
Enzyme 62 GO Classification Not Available
Enzyme 62 General Function Involved in protein binding
Enzyme 62 Specific Function Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates
Enzyme 62 Pathways Not Available
Enzyme 62 Reactions Not Available
Enzyme 62 Pfam Domain Function
Enzyme 62 Signals
  • None
Enzyme 62 Transmembrane Regions
  • 19-39 521-541
Enzyme 62 Essentiality Not Available
Enzyme 62 GenBank ID Protein 14456613 Link Image
Enzyme 62 UniProtKB/Swiss-Prot ID Q96S52 Link Image
Enzyme 62 UniProtKB/Swiss-Prot Entry Name PIGS_HUMAN Link Image
Enzyme 62 PDB ID Not Available
Enzyme 62 Cellular Location Not Available
Enzyme 62 Gene Sequence >1668 bp
ATGGCGGCCGCCGGGGCTGCGGCTACACACCTAGAGGTGGCCCGGGGCAAGCGCGCCGCC
CTCTTCTTCGCTGCGGTGGCCATCGTGCTGGGGCTACCGCTCTGGTGGAAGACCACGGAG
ACCTACCGGGCCTCGTTGCCTTACTCCCAGATCAGTGGCCTGAATGCCCTTCAGCTCCGC
CTCATGGTGCCTGTCACTGTCGTGTTTACGCGGGAGTCAGTGCCCCTGGACGACCAGGAG
AAGCTGCCCTTCACCGTTGTGCATGAAAGAGAGATTCCTCTGAAATACAAAATGAAAATC
AAATGCCGTTTCCAGAAGGCCTATCGGAGGGCTTTGGACCATGAGGAGGAGGCCCTGTCA
TCGGGCAGTGTGCAAGAGGCAGAAGCCATGTTAGATGAGCCTCAGGAACAAGCGGAGGGC
TCCCTGACTGTGTACGTGATATCTGAACACTCCTCACTTCTTCCCCAGGACATGATGAGC
TACATTGGGCCCAAGAGGACAGCAGTGGTGCGGGGGATAATGCACCGGGAGGCCTTTAAC
ATCATTGGCCGCCGCATAGTCCAGGTGGCCCAGGCCATGTCTTTGACTGAGGATGTGCTT
GCTGCTGCTCTGGCTGACCACCTTCCAGAGGACAAGTGGAGCGCTGAGAAGAGGCGGCCT
CTCAAGTCCAGCTTGGGCTATGAGATCACCTTCAGTTTACTCAACCCAGACCCCAAGTCC
CATGATGTCTACTGGGACATTGAGGGGGCTGTCCGGCGCTATGTGCAACCTTTCCTGAAT
GCCCTCGGTGCCGCTGGCAACTTCTCTGTGGACTCTCAGATTCTTTACTATGCAATGTTG
GGGGTGAATCCCCGCTTTGACTCAGCTTCCTCCAGCTACTATTTGGACATGCACAGCCTC
CCCCATGTCATCAACCCAGTGGAGTCCCGGCTGGGATCCAGTGCTGCCTCCTTGTACCCT
GTGCTCAACTTTCTACTCTACGTGCCTGAGCTTGCACACTCACCGCTGTACATTCAGGAC
AAGGATGGCGCTCCAGTGGCCACCAATGCCTTCCATAGTCCCCGCTGGGGTGGCATTATG
GTATATAATGTTGACTCCAAAACCTATAATGCCTCAGTGCTGCCAGTGAGAGTCGAGGTG
GACATGGTGCGAGTGATGGAGGTGTTCCTGGCACAGTTGCGGTTGCTCTTTGGGATTGCT
CAGCCCCAGCTGCCTCCAAAATGCCTGCTTTCAGGGCCTACGAGTGAAGGGCTAATGACC
TGGGAGCTAGACCGGCTGCTCTGGGCTCGGTCAGTGGAGAACCTGGCCACAGCCACCACC
ACCCTTACCTCCCTGGCGCAGCTTCTGGGCAAGATCAGCAACATTGTCATTAAGGACGAC
GTGGCATCTGAGGTGTACAAGGCTGTAGCTGCCGTCCAGAAGTCGGCAGAAGAGTTGGCG
TCTGGGCACCTGGCATCTGCCTTTGTCGCCAGCCAGGAAGCTGTGACATCCTCTGAGCTT
GCCTTCTTTGACCCGTCACTCCTCCACCTCCTTTATTTCCCTGATGACCAGAAGTTTGCC
ATCTACATCCCACTCTTCCTGCCTATGGCTGTGCCCATCCTCCTGTCCCTGGTCAAGATC
TTCCTGGAGACCCGCAAGTCCTGGAGAAAGCCTGAGAAGACAGACTGA
Enzyme 62 GenBank Gene ID AB057723 Link Image
Enzyme 62 GeneCard ID PIGS Link Image
Enzyme 62 GenAtlas ID PIGS Link Image
Enzyme 62 HGNC ID HGNC:14937 Link Image
Enzyme 62 Chromosome Location 1
Enzyme 62 Locus 17p13.2
Enzyme 62 SNPs SNPJam Report Link Image
Enzyme 62 General References
  1. Ohishi K, Inoue N, Kinoshita T: PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. EMBO J. 2001 Aug 1;20(15):4088-98. [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. 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. 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 62 Metabolite References Not Available
Enzyme 63 [top]
Enzyme 63 ID 12953
Enzyme 63 Name GPI transamidase component PIG-T
Enzyme 63 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class T protein
Enzyme 63 Gene Name PIGT
Enzyme 63 Protein Sequence >GPI transamidase component PIG-T
MAAAMPLALLVLLLLGPGGWCLAEPPRDSLREELVITPLPSGDVAATFQFRTRWDSELQR
EGVSHYRLFPKALGQLISKYSLRELHLSFTQGFWRTRYWGPPFLQAPSGAELWVWFQDTV
TDVDKSWKELSNVLSGIFCASLNFIDSTNTVTPTASFKPLGLANDTDHYFLRYAVLPREV
VCTENLTPWKKLLPCSSKAGLSVLLKADRLFHTSYHSQAVHIRPVCRNARCTSISWELRQ
TLSVVFDAFITGQGKKDWSLFRMFSRTLTEPCPLASESRVYVDITTYNQDNETLEVHPPP
TTTYQDVILGTRKTYAIYDLLDTAMINNSRNLNIQLKWKRPPENEAPPVPFLHAQRYVSG
YGLQKGELSTLLYNTHPYRAFPVLLLDTVPWYLRLYVHTLTITSKGKENKPSYIHYQPAQ
DRLQPHLLEMLIQLPANSVTKVSIQFERALLKWTEYTPDPNHGFYVSPSVLSALVPSMVA
AKPVDWEESPLFNSLFPVSDGSNYFVRLYTEPLLVNLPTPDFSMPYNVICLTCTVVAVCY
GSFYNLLTRTFHIEEPRTGGLAKRLANLIRRARGVPPL
Enzyme 63 Number of Residues 578
Enzyme 63 Molecular Weight 65699.0
Enzyme 63 Theoretical pI 8.49
Enzyme 63 GO Classification
Function
Process
Component
  • GPI-anchor transamidase complex
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • macromolecular complex
  • membrane part
  • protein complex
Enzyme 63 General Function Involved in protein binding
Enzyme 63 Specific Function Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates
Enzyme 63 Pathways Not Available
Enzyme 63 Reactions Not Available
Enzyme 63 Pfam Domain Function
Enzyme 63 Signals
  • 1-21
Enzyme 63 Transmembrane Regions
  • 528-548
Enzyme 63 Essentiality Not Available
Enzyme 63 GenBank ID Protein 14456615 Link Image
Enzyme 63 UniProtKB/Swiss-Prot ID Q969N2 Link Image
Enzyme 63 UniProtKB/Swiss-Prot Entry Name PIGT_HUMAN Link Image
Enzyme 63 PDB ID Not Available
Enzyme 63 Cellular Location Not Available
Enzyme 63 Gene Sequence >1737 bp
ATGGCGGCGGCTATGCCGCTTGCTCTGCTCGTCCTGTTGCTCCTGGGGCCCGGCGGCTGG
TGCCTTGCAGAACCCCCACGCGACAGCCTGCGGGAGGAACTTGTCATCACCCCGCTGCCT
TCCGGGGACGTAGCCGCCACATTCCAGTTCCGCACGCGCTGGGATTCGGAGCTTCAGCGG
GAAGGAGTGTCCCATTACAGGCTCTTTCCCAAAGCCCTGGGGCAGCTGATCTCCAAGTAT
TCTCTACGGGAGCTGCACCTGTCATTCACACAAGGCTTTTGGAGGACCCGATACTGGGGG
CCACCCTTCCTGCAGGCCCCATCAGGTGCAGAGCTGTGGGTCTGGTTCCAAGACACTGTC
ACTGATGTGGATAAATCTTGGAAGGAGCTCAGTAATGTCCTCTCAGGGATCTTCTGCGCC
TCTCTCAACTTCATCGACTCCACCAACACAGTCACTCCCACTGCCTCCTTCAAACCCCTG
GGTCTGGCCAATGACACTGACCACTACTTTCTGCGCTATGCTGTGCTGCCGCGGGAGGTG
GTCTGCACCGAAAACCTCACCCCCTGGAAGAAGCTCTTGCCCTGTAGTTCCAAGGCAGGC
CTCTCTGTGCTGCTGAAGGCAGATCGCTTGTTCCACACCAGCTACCACTCCCAGGCAGTG
CATATCCGCCCTGTTTGCAGAAATGCACGCTGTACTAGCATCTCCTGGGAGCTGAGGCAG
ACCCTGTCAGTTGTATTTGATGCCTTCATCACGGGGCAGGGAAAGAAAGACTGGTCCCTC
TTCCGGATGTTCTCCCGAACCCTCACGGAGCCCTGCCCCCTGGCTTCAGAGAGCCGAGTC
TATGTGGACATCACCACCTACAACCAGGACAACGAGACATTAGAGGTGCACCCACCCCCG
ACCACTACATATCAGGACGTCATCCTAGGCACTCGGAAGACCTATGCCATCTATGACTTG
CTTGACACCGCCATGATCAACAACTCTCGAAACCTCAACATCCAGCTCAAGTGGAAGAGA
CCCCCAGAGAATGAGGCCCCCCCAGTGCCCTTCCTGCATGCCCAGCGGTACGTGAGTGGC
TATGGGCTGCAGAAGGGGGAGCTGAGCACACTGCTGTACAACACCCACCCATACCGGGCC
TTCCCGGTGCTGCTGCTGGACACCGTACCCTGGTATCTGCGGCTGTATGTGCACACCCTC
ACCATCACCTCCAAGGGCAAGGAGAACAAACCAAGTTACATCCACTACCAGCCTGCCCAG
GACCGGCTGCAACCCCACCTCCTGGAGATGCTGATTCAGCTGCCGGCCAACTCAGTCACC
AAGGTTTCCATCCAGTTTGAGCGGGCGCTGCTGAAGTGGACCGAGTACACGCCAGATCCT
AACCATGGCTTCTATGTCAGCCCATCTGTCCTCAGCGCCCTTGTGCCCAGCATGGTAGCA
GCCAAGCCAGTGGACTGGGAAGAGAGTCCCCTCTTCAACAGCCTGTTCCCAGTCTCTGAT
GGCTCTAACTACTTTGTGCGGCTCTACACGGAGCCGCTGCTGGTGAACCTGCCGACACCG
GACTTCAGCATGCCCTACAACGTGATCTGCCTCACGTGCACTGTGGTGGCCGTGTGCTAT
GGCTCCTTCTACAATCTCCTCACCCGAACCTTCCACATCGAGGAGCCCCGCACAGGTGGC
CTGGCCAAGCGGCTGGCCAACCTTATCCGGCGCGCCCGAGGTGTCCCCCCACTCTGA
Enzyme 63 GenBank Gene ID AB057724 Link Image
Enzyme 63 GeneCard ID PIGT Link Image
Enzyme 63 GenAtlas ID PIGT Link Image
Enzyme 63 HGNC ID HGNC:14938 Link Image
Enzyme 63 Chromosome Location 2
Enzyme 63 Locus 20q12-q13.12
Enzyme 63 SNPs SNPJam Report Link Image
Enzyme 63 General References
  1. Ohishi K, Inoue N, Kinoshita T: PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. EMBO J. 2001 Aug 1;20(15):4088-98. [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. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [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. 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]
  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. 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]
  8. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed Link Image]
  9. Ohishi K, Nagamune K, Maeda Y, Kinoshita T: Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge. J Biol Chem. 2003 Apr 18;278(16):13959-67. Epub 2003 Feb 11. [PubMed Link Image]
  10. 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 63 Metabolite References Not Available
Enzyme 64 [top]
Enzyme 64 ID 12954
Enzyme 64 Name Phosphatidylinositol glycan anchor biosynthesis class U protein
Enzyme 64 Synonyms
  1. Cell division cycle protein 91-like 1
  2. Protein CDC91-like 1
  3. GPI transamidase component PIG-U
Enzyme 64 Gene Name PIGU
Enzyme 64 Protein Sequence >Phosphatidylinositol glycan anchor biosynthesis class U protein
MAAPLVLVLVVAVTVRAALFRSSLAEFISERVEVVSPLSSWKRVVEGLSLLDLGVSPYSG
AVFHETPLIIYLFHFLIDYAELVFMITDALTAIALYFAIQDFNKVVFKKQKLLLELDQYA
PDVAELIRTPMEMRYIPLKVALFYLLNPYTILSCVAKSTCAINNTLIAFFILTTIKGSAF
LSAIFLALATYQSLYPLTLFVPGLLYLLQRQYIPVKMKSKAFWIFSWEYAMMYVGSLVVI
ICLSFFLLSSWDFIPAVYGFILSVPDLTPNIGLFWYFFAEMFEHFSLFFVCVFQINVFFY
TIPLAIKLKEHPIFFMFIQIAVIAIFKSYPTVGDVALYMAFFPVWNHLYRFLRNIFVLTC
IIIVCSLLFPVLWHLWIYAGSANSNFFYAITLTFNVGQILLISDYFYAFLRREYYLTHGL
YLTAKDGTEAMLVLK
Enzyme 64 Number of Residues 435
Enzyme 64 Molecular Weight 50051.2
Enzyme 64 Theoretical pI 7.82
Enzyme 64 GO Classification
Function
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
  • organelle membrane
Enzyme 64 General Function Involved in GPI anchor biosynthetic process
Enzyme 64 Specific Function Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI
Enzyme 64 Pathways Not Available
Enzyme 64 Reactions Not Available
Enzyme 64 Pfam Domain Function
Enzyme 64 Signals
  • None
Enzyme 64 Transmembrane Regions
  • 66-86 166-186 188-208 237-257 259-279 286-306 313-333 355-375 386-406
Enzyme 64 Essentiality Not Available
Enzyme 64 GenBank ID Protein 27372217 Link Image
Enzyme 64 UniProtKB/Swiss-Prot ID Q9H490 Link Image
Enzyme 64 UniProtKB/Swiss-Prot Entry Name PIGU_HUMAN Link Image
Enzyme 64 PDB ID Not Available
Enzyme 64 Cellular Location Not Available
Enzyme 64 Gene Sequence >1308 bp
ATGGCGGCTCCCTTGGTCCTGGTGCTGGTGGTGGCTGTGACAGTGCGGGCGGCCTTGTTC
CGCTCCAGTCTGGCCGAGTTCATTTCCGAGCGGGTGGAGGTGGTGTCCCCACTGAGCTCT
TGGAAGAGAGTGGTTGAAGGCCTTTCACTGTTGGACTTGGGAGTATCTCCGTATTCTGGA
GCAGTATTTCATGAAACTCCATTAATAATATACCTCTTTCATTTCCTAATTGACTATGCT
GAATTGGTGTTTATGATAACTGATGCACTCACTGCTATTGCCCTGTATTTTGCAATCCAG
GACTTCAATAAAGTTGTGTTTAAAAAGCAGAAACTCCTCCTAGAACTGGACCAGTATGCC
CCAGATGTGGCCGAACTCATCCGGACCCCTATGGAAATGCGTTACATCCCTTTGAAAGTG
GCCCTGTTCTATCTCTTAAATCCTTACACGATTTTGTCTTGTGTTGCCAAGTCTACCTGT
GCCATCAACAACACCCTCATTGCTTTCTTCATTTTGACTACGATAAAAGGCAGTGCTTTC
CTCAGTGCTATTTTTCTTGCCTTAGCGACATACCAGTCTCTGTACCCACTCACCTTGTTT
GTCCCAGGACTCCTCTATCTCCTCCAGCGGCAGTACATACCTGTGAAAATGAAGAGCAAA
GCCTTCTGGATCTTTTCTTGGGAGTATGCCATGATGTATGTGGGAAGCCTAGTGGTAATC
ATTTGCCTCTCCTTCTTCCTTCTCAGCTCTTGGGATTTCATCCCCGCAGTCTATGGCTTT
ATACTTTCTGTTCCAGATCTCACTCCAAACATTGGTCTTTTCTGGTACTTCTTTGCAGAG
ATGTTTGAGCACTTCAGCCTCTTCTTTGTATGTGTGTTTCAGATCAACGTCTTCTTCTAC
ACCATCCCCTTAGCCATAAAGCTAAAGGAGCACCCCATCTTCTTCATGTTTATCCAGATC
GCTGTCATCGCCATCTTTAAGTCCTACCCGACAGTGGGGGACGTGGCGCTCTACATGGCC
TTCTTCCCCGTGTGGAACCATCTCTACAGATTCCTGAGAAACATCTTTGTCCTCACCTGC
ATCATCATCGTCTGTTCCCTGCTCTTCCCTGTCCTGTGGCACCTCTGGATTTATGCAGGA
AGTGCCAACTCTAATTTCTTTTATGCCATCACACTGACCTTCAACGTTGGGCAGATCCTG
CTCATCTCTGATTACTTCTATGCCTTCCTGCGGCGGGAGTACTACCTCACACATGGCCTC
TACTTGACCGCCAAGGATGGCACAGAGGCCATGCTCGTGCTCAAGTAG
Enzyme 64 GenBank Gene ID AB086842 Link Image
Enzyme 64 GeneCard ID PIGU Link Image
Enzyme 64 GenAtlas ID PIGU Link Image
Enzyme 64 HGNC ID HGNC:15791 Link Image
Enzyme 64 Chromosome Location 2
Enzyme 64 Locus 20q11.22
Enzyme 64 SNPs SNPJam Report Link Image
Enzyme 64 General References
  1. Hong Y, Ohishi K, Kang JY, Tanaka S, Inoue N, Nishimura J, Maeda Y, Kinoshita T: Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins. Mol Biol Cell. 2003 May;14(5):1780-9. Epub 2003 Jan 26. [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. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  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 64 Metabolite References Not Available
Enzyme 65 [top]
Enzyme 65 ID 12955
Enzyme 65 Name GPI mannosyltransferase 2
Enzyme 65 Synonyms
  1. GPI mannosyltransferase II
  2. GPI-MT-II
  3. Phosphatidylinositol-glycan biosynthesis class V protein
  4. PIG-V
Enzyme 65 Gene Name PIGV
Enzyme 65 Protein Sequence >GPI mannosyltransferase 2
MWPQDPSRKEVLRFAVSCRILTLMLQALFNAIIPDHHAEAFSPPRLAPSGFVDQLVEGLL
GGLSHWDAEHFLFIAEHGYLYEHNFAFFPGFPLALLVGTELLRPLRGLLSLRSCLLISVA
SLNFLFFMLAAVALHDLGCLVLHCPHQSFYAALLFCLSPANVFLAAGYSEALFALLTFSA
MGQLERGRVWTSVLLFAFATGVRSNGLVSVGFLMHSQCQGFFSSLTMLNPLRQLFKLMAS
LFLSVFTLGLPFALFQYYAYTQFCLPGSARPIPEPLVQLAVDKGYRIAEGNEPPWCFWDV
PLIYSYIQDVYWNVGFLKYYELKQVPNFLLAAPVAILVAWATWTYVTTHPWLCLTLGLQR
SKNNKTLEKPDLGFLSPQVFVYVVHAAVLLLFGGLCMHVQVLTRFLGSSTPIMYWFPAHL
LQDQEPLLRSLKTVPWKPLAEDSPPGQKVPRNPIMGLLYHWKTCSPVTRYILGYFLTYWL
LGLLLHCNFLPWT
Enzyme 65 Number of Residues 493
Enzyme 65 Molecular Weight 55712.1
Enzyme 65 Theoretical pI 8.03
Enzyme 65 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
  • organelle membrane
Enzyme 65 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 65 Specific Function Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly
Enzyme 65 Pathways Not Available
Enzyme 65 Reactions Not Available
Enzyme 65 Pfam Domain Function Not Available
Enzyme 65 Signals
  • None
Enzyme 65 Transmembrane Regions
  • 14-34 78-98 114-134 137-157 162-182 193-213 235-255 328-348 379-399 470-490
Enzyme 65 Essentiality Not Available
Enzyme 65 GenBank ID Protein 7020604 Link Image
Enzyme 65 UniProtKB/Swiss-Prot ID Q9NUD9 Link Image
Enzyme 65 UniProtKB/Swiss-Prot Entry Name PIGV_HUMAN Link Image
Enzyme 65 PDB ID Not Available
Enzyme 65 Cellular Location Not Available
Enzyme 65 Gene Sequence >1482 bp
ATGTGGCCCCAGGACCCATCCCGGAAGGAGGTGCTGAGGTTTGCAGTCAGCTGCCGTATC
CTGACTCTGATGCTGCAGGCCCTCTTCAATGCCATCACCCCAGATCACCATGCAGAAGCC
TTCTCTCCTCCTCGCCTGGCCCCCTCAGGCTTTGTGGACCAACTCGTGGAAGGTCTTCTG
GGCGGCCTGTCTCACTGGGATGCTGAACACTTCTTGTTCATTGCTGAGCATGGCTACCTG
TATGAGCACAACTTTGCCTTCTTTCCTGGTTTCCCCTTGGCCCTGCTGGTGGGGACTGAA
CTGTTGAGACCCTTACGGGGGTTACTGAGTCTACGCAGTTGCCTGCTGATTTCGGTAGCA
TCACTCAATTTCTTGTTCTTCATGTTGGCTGCAGTTGCACTTCATGACCTGGGTTGTCTG
GTTTTGCACTGTCCCCACCAGTCCTTTTATGCAGCTCTGCTTTTCTGTCTCAGCCCTGCC
AATGTCTTCCTGGCAGCTGGTTACTCAGAAGCTTTGTTTGCCCTCCTGACATTCAGTGCC
ATGGGGCAGCTGGAGAGGGGCCGAGTCTGGACTAGTGTACTCCTCTTTGCCTTTGCCACT
GGGGTACGCTCCAACGGGCTGGTCAGTGTTGGCTTCCTCATGCATTCTCAATGCCAAGGC
TTTTTCTCTTCTCTAACGATGCTGAATCCTCTGAGACAGCTCTTTAAGCTGATGGCCTCT
CTGTTTCTGTCGGTGTTCACACTTGGCCTTCCCTTTGCCCTCTTTCAGTATTATGCCTAC
ACCCAATTCTGTCTGCCAGGCTCAGCCCGCCCCATTCCTGAGCCTTTGGTACAGTTAGCT
GTAGACAAGGGCTACCGGATTGCAGAGGGAAATGAACCGCCTTGGTGCTTCTGGGATGTT
CCACTAATATACAGCTATATCCAGGATGTCTACTGGAATGTTGGCTTTTTGAAATACTAT
GAGCTCAAGCAGGTGCCCAATTTTCTACTGGCTGCACCAGTGGCTATACTGGTTGCCTGG
GCAACTTGGACATACGTGACCACTCACCCTTGGCTCTGCCTTACACTTGGGCTGCAAAGG
AGCAAGAACAATAAGACCCTAGAGAAGCCCGATCTTGGATTCCTCAGTCCTCAGGTGTTT
GTGTACGTGGTCCACGCTGCAGTGCTGCTGCTGTTTGGAGGTCTGTGCATGCATGTTCAG
GTTCTCACCAGGTTTTTGGGCTCCTCCACTCCTATTATGTACTGGTTTCCAGCTCACTTG
CTTCAGGATCAAGAGCCGCTGTTGAGATCCTTAAAGACTGTGCCTTGGAAGCCTCTTGCA
GAGGACTCCCCACCAGGACAAAAGGTCCCCAGAAATCCTATCATGGGACTTTTGTATCAC
TGGAAAACCTGTTCTCCAGTCACACGATACATTCTAGGCTACTTCCTGACTTACTGGCTC
CTGGGACTACTCCTACATTGCAACTTCCTGCCTTGGACATGA
Enzyme 65 GenBank Gene ID AK000484 Link Image
Enzyme 65 GeneCard ID PIGV Link Image
Enzyme 65 GenAtlas ID PIGV Link Image
Enzyme 65 HGNC ID HGNC:26031 Link Image
Enzyme 65 Chromosome Location 1
Enzyme 65 Locus 1p36.11
Enzyme 65 SNPs SNPJam Report Link Image
Enzyme 65 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]
  2. 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]
  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. Fabre AL, Orlean P, Taron CH: Saccharomyces cerevisiae Ybr004c and its human homologue are required for addition of the second mannose during glycosylphosphatidylinositol precursor assembly. FEBS J. 2005 Mar;272(5):1160-8. [PubMed Link Image]
  5. Kang JY, Hong Y, Ashida H, Shishioh N, Murakami Y, Morita YS, Maeda Y, Kinoshita T: PIG-V involved in transferring the second mannose in glycosylphosphatidylinositol. J Biol Chem. 2005 Mar 11;280(10):9489-97. Epub 2004 Dec 28. [PubMed Link Image]
Enzyme 65 Metabolite References Not Available
Enzyme 66 [top]
Enzyme 66 ID 12956
Enzyme 66 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
Enzyme 66 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class Y protein
  2. PIG-Y
Enzyme 66 Gene Name PIGY
Enzyme 66 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
MFLSLPTLTVLIPLVSLAGLFYSASVEENFPQGCTSTASLCFYSLLLPITIPVYVFFHLW
TWMGIKLFRHN
Enzyme 66 Number of Residues 71
Enzyme 66 Molecular Weight 8057.5
Enzyme 66 Theoretical pI 7.41
Enzyme 66 GO Classification Not Available
Enzyme 66 General Function Involved in GPI anchor biosynthetic process
Enzyme 66 Specific Function Component of the GPI-GlcNAc transferase (GPI-GnT) complex in the endoplasmic reticulum, a complex that catalyzes transfer of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the first step in the production of GPI- anchors for cell surface proteins. May act by regulating the catalytic subunit PIGA
Enzyme 66 Pathways Not Available
Enzyme 66 Reactions Not Available
Enzyme 66 Pfam Domain Function Not Available
Enzyme 66 Signals
  • None
Enzyme 66 Transmembrane Regions
  • 4-26 45-65
Enzyme 66 Essentiality Not Available
Enzyme 66 GenBank ID Protein 75674192 Link Image
Enzyme 66 UniProtKB/Swiss-Prot ID Q3MUY2 Link Image
Enzyme 66 UniProtKB/Swiss-Prot Entry Name PIGY_HUMAN Link Image
Enzyme 66 PDB ID Not Available
Enzyme 66 Cellular Location Not Available
Enzyme 66 Gene Sequence >216 bp
ATGTTTCTGTCTCTTCCTACGTTGACTGTTCTTATTCCACTGGTTTCTTTAGCAGGACTG
TTCTACTCAGCCTCTGTGGAAGAAAACTTCCCACAGGGCTGCACTAGCACAGCCAGCCTT
TGCTTTTACAGCCTGCTCTTGCCTATTACCATACCAGTGTATGTATTCTTCCACCTTTGG
ACTTGGATGGGTATTAAACTCTTCAGGCATAATTGA
Enzyme 66 GenBank Gene ID AB206972 Link Image
Enzyme 66 GeneCard ID PIGY Link Image
Enzyme 66 GenAtlas ID PIGY Link Image
Enzyme 66 HGNC ID HGNC:28213 Link Image
Enzyme 66 Chromosome Location 4
Enzyme 66 Locus 4q22.1
Enzyme 66 SNPs SNPJam Report Link Image
Enzyme 66 General References
  1. Murakami Y, Siripanyaphinyo U, Hong Y, Tashima Y, Maeda Y, Kinoshita T: The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component. Mol Biol Cell. 2005 Nov;16(11):5236-46. Epub 2005 Sep 14. [PubMed Link Image]
  2. 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 66 Metabolite References Not Available
Enzyme 67 [top]
Enzyme 67 ID 12957
Enzyme 67 Name Cytoplasmic phosphatidylinositol transfer protein 1
Enzyme 67 Synonyms
  1. Mammalian rdgB homolog beta
  2. M-rdgB beta
  3. MrdgBbeta
  4. Retinal degeneration B homolog beta
  5. RdgBbeta
Enzyme 67 Gene Name PITPNC1
Enzyme 67 Protein Sequence >Cytoplasmic phosphatidylinositol transfer protein 1
MLLKEYRICMPLTVDEYKIGQLYMISKHSHEQSDRGEGVEVVQNEPFEDPHHGNGQFTEK
RVYLNSKLPSWARAVVPKIFYVTEKAWNYYPYTITEYTCSFLPKFSIHIETKYEDNKGSN
DTIFDNEAKDVEREVCFIDIACDEIPERYYKESEDPKHFKSEKTGRGQLREGWRDSHQPI
MCSYKLVTVKFEVWGLQTRVEQFVHKVVRDILLIGHRQAFAWVDEWYDMTMDDVREFERA
TQEATNKKIGIFPPAISISSIPLLPSSVRSAPSSAPSTPLSTDAPEFLSVPKDRPRKKSA
PETLTLPDPEKKATLNLPGMHSSDKPCRPKSE
Enzyme 67 Number of Residues 332
Enzyme 67 Molecular Weight 38373.2
Enzyme 67 Theoretical pI 6.36
Enzyme 67 GO Classification
Function
Process
  • establishment of localization
  • transport
Component
  • cell part
  • intracellular
Enzyme 67 General Function Involved in transport
Enzyme 67 Specific Function Phosphatidylinositol transfer proteins mediate the monomeric transport of lipids by shielding a lipid from the aqueous environment and binding the lipid in a hydrophobic cavity. Able to transfer phosphatidylinositol in vitro
Enzyme 67 Pathways Not Available
Enzyme 67 Reactions Not Available
Enzyme 67 Pfam Domain Function
Enzyme 67 Signals
  • None
Enzyme 67 Transmembrane Regions
  • None
Enzyme 67 Essentiality Not Available
Enzyme 67 GenBank ID Protein 6272656 Link Image
Enzyme 67 UniProtKB/Swiss-Prot ID Q9UKF7 Link Image
Enzyme 67 UniProtKB/Swiss-Prot Entry Name PITC1_HUMAN Link Image
Enzyme 67 PDB ID Not Available
Enzyme 67 Cellular Location Not Available
Enzyme 67 Gene Sequence >999 bp
ATGCTGCTGAAAGAGTACCGGATCTGCATGCCGCTCACCGTAGACGAGTACAAAATTGGA
CAGCTGTACATGATCAGCAAACACAGCCATGAACAGAGTGACCGGGGAGAAGGGGTGGAG
GTCGTCCAGAATGAGCCCTTTGAGGACCCTCACCATGGCAATGGGCAGTTCACCGAGAAG
CGGGTGTATCTCAACAGCAAACTGCCTAGTTGGGCTAGAGCTGTTGTCCCCAAAATATTT
TATGTGACAGAGAAGGCTTGGAACTATTATCCCTACACAATTACAGAATACACATGTTCC
TTTCTGCCGAAATTCTCCATTCATATAGAAACCAAGTATGAGGACAACAAAGGAAGCAAT
GACACCATTTTCGACAGTGAAGCCAAAGACGTGGAGAGAGAAGTTTGCTTTATTGATATT
GCCTGCGATGAAATTCCAGAGCGCTACTACAAAGAATCCGAGGATCCTAAGCACTTCAAG
TCAGAGAAGACAGGACGGGGACAGTTGAGGGAAGGCTGGAGAGATAGTCATCAGCCTATC
ATGTGCTCCTACAAGCTGGTGACTGTGAAGTCTGAGGTCTGGGGGCTTCAGACCAGAGTG
GAACAATTTGTACACAAGGTGGTCCGAGACATTCTGCTGATTGGACATAGACAGGCTTTT
GCATGGGTTGATGAGTGGTATGACATGACAATGGATGAAGTCCGAGAATTTGAACGAGCC
ACTCAGGAAGCCACCAACAAGAAAATCGGCATTTTCCCACCTGCAATTTCTATCTCCAGC
ATCCCCCTGCTGCCTTCTTCCGTCCGCAGTGCGCCTTCTAGTGCTCCATCCACCCCTCTC
TCCACAGACGCACCCGAATTTCTGTCCGTTCCCAAAGATCGGCCCCGGAAAAAGTCTGCC
CCAGAAACTCTCACACTTCCAGACCCTGAGAAAAAAGCCACCCTGAATTTACCCGGCATG
CACTCTTCAGATAAGCCATGTCGGCCCAAATCTGAGTAA
Enzyme 67 GenBank Gene ID AF171102 Link Image
Enzyme 67 GeneCard ID PITPNC1 Link Image
Enzyme 67 GenAtlas ID PITPNC1 Link Image
Enzyme 67 HGNC ID HGNC:21045 Link Image
Enzyme 67 Chromosome Location 1
Enzyme 67 Locus 17q24.2
Enzyme 67 SNPs SNPJam Report Link Image
Enzyme 67 General References
  1. Fullwood Y, dos Santos M, Hsuan JJ: Cloning and characterization of a novel human phosphatidylinositol transfer protein, rdgBbeta. J Biol Chem. 1999 Oct 29;274(44):31553-8. [PubMed Link Image]
  2. 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 67 Metabolite References Not Available
Enzyme 68 [top]
Enzyme 68 ID 12958
Enzyme 68 Name Membrane-associated phosphatidylinositol transfer protein 1
Enzyme 68 Synonyms
  1. Drosophila retinal degeneration B homolog
  2. Phosphatidylinositol transfer protein, membrane-associated 1
  3. PITPnm 1
  4. Pyk2 N-terminal domain-interacting receptor 2
  5. NIR-2
Enzyme 68 Gene Name PITPNM1
Enzyme 68 Protein Sequence >Membrane-associated phosphatidylinositol transfer protein 1
MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGSGQYTH
KVYHVGSHIPGWFRALLPKAALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGG
QQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDPRLYHSVKTGRGPLSDDWARTA
AQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWTELSMAD
IRALEEETARMLAQRMAKCNTGSEGSEAQPPGKPSTEARSAASNTGTPDGPEAPPGPDAS
PDASFGKQWSSSSRSSYSSQHGGAVSPQSLSEWRMQNIARDSENSSEEEFFDAHEGFSDS
EEVFPKEMTKWNSNDFIDAFASPVEAEGTPEPGAEAAKGIEDGAQAPRDSEGLDGAGELG
AEACAVHALFLILHSGNILDSGPGDANSKQADVQTLSSAFEAVTRIHFPEALGHVALRLV
PCPPICAAAYALVSNLSPYSHDGDSLSRSQDHIPLAALPLLATSSSRYQGAVATVIARTN
QAYSAFLRSPEGAGFCGQVALIGDGVGGILGFDALCHSANAGTGSRGSSRRGSMNNELLS
PEFGPVRDPLADGVEGLGRGSPEPSALPPQRIPSDMASPEPEGSQNSLQAAPATTSSWEP
RRASTAFCPPAASSEAPDGPSSTARLDFKVSGFFLFGSPLGLVLALRKTVMPALEAAQMR
PACEQIYNLFHAADPCASRLEPLLAPKFQAIAPLTVPRYQKFPLGDGSSLLLADTLQTHS
SLFLEELEMLVPSTPTSTSGAFWKGSELATDPPAQPAAPSTTSEVVKILERWWGTKRIDY
SLYCPEALTAFPTVTLPHLFHASYWESADVVAFILRQVIEKERPQLAECEEPSIYSPAFP
REKWQRKRTQVKIRNVTSNHRASDTVVCEGRPQVLSGRFMYGPLDVVTLTGEKVDVYIMT
QPLSGKWIHFGTEVTNSSGRLTFPVPPERALGIGVYPVRMVVRGDHTYAECCLTVVARGT
EAVVFSIDGSFTASVSIMGSDPKVRAGAVDVVRHWQDSGYLIVYVTGRPDMQKHRVVAWL
SQHNFPHGVVSFCDGLTHDPLRQKAMFLQSLVQEVELNIVAGYGSPKDVAVYAALGLSPS
QTYIVGRAVRKLQAQCQFLSDGYVAHLGQLEAGSHSHASSGPPRAALGKSSYGVAAPVDF
LRKQSQLLRSRGPSQAEREGPGTPPTTLARGKARSISLKLDSEE
Enzyme 68 Number of Residues 1244
Enzyme 68 Molecular Weight 134846.3
Enzyme 68 Theoretical pI 5.81
Enzyme 68 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • metal ion binding
Process
  • establishment of localization
  • transport
Component
  • cell part
  • intracellular
Enzyme 68 General Function Involved in metal ion binding
Enzyme 68 Specific Function Regulates RHOA activity, and plays a role in cytoskeleton remodeling. Necessary for normal completion of cytokinesis. Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus. Binds phosphatidyl inositol phosphates (in vitro). May catalyze the transfer of phosphatidylinositol and phosphatidylcholine between membranes. Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus. Required for protein export from the endoplasmic reticulum and the Golgi. Binds calcium ions
Enzyme 68 Pathways Not Available
Enzyme 68 Reactions Not Available
Enzyme 68 Pfam Domain Function
Enzyme 68 Signals
  • None
Enzyme 68 Transmembrane Regions
  • None
Enzyme 68 Essentiality Not Available
Enzyme 68 GenBank ID Protein 12667436 Link Image
Enzyme 68 UniProtKB/Swiss-Prot ID O00562 Link Image
Enzyme 68 UniProtKB/Swiss-Prot Entry Name PITM1_HUMAN Link Image
Enzyme 68 PDB ID Not Available
Enzyme 68 Cellular Location Not Available
Enzyme 68 Gene Sequence >3735 bp
ATGCTCATCAAGGAATACCACATTCTGCTGCCCATGAGCCTGGACGAGTACCAGGTGGCC
CAGCTCTACATGATCCAGAAAAAGAGCCGGGAGGAGTCTAGTGGTGAGGGCAGCGGCGTG
GAGATCCTGGCCAACCGGCCCTACACGGATGGGCCCGGGGGCAGCGGGCAATACACACAC
AAGGTGTACCACGTGGGCTCCCACATCCCAGGCTGGTTCCGGGCACTGCTGCCCAAGGCT
GCCCTGCAGGTAGAAGAGGAATCCTGGAATGCCTACCCCTACACCCGAACCCGGTACACC
TGCCCTTTCGTGGAGAAATTCTCCATTGAAATTGAGACCTATTACCTGCCTGATGGGGGG
CAGCAGCCAAACGTCTTCAACCTGAGCGGGGCCGAGAGGAGACAGCGCATCCTGGACACC
ATCGACATCGTGCGGGATGCAGTGGCCCCAGGCGAGTACAAAGCAGAAGAGGACCCCCGG
CTTTATCACTCGGTCAAGACGGGCCGAGGGCCACTGTCTGATGACTGGGCACGGACGGCG
GCACAGACGGGGCCCCTTATGTGTGCCTATAAGCTGTGCAAGGTTGAGTTCCGCTACTGG
GGCATGCAAGCCAAGATCGAGCAGTTCATCCATGATGTAGGTCTGCGTCGGGTGATGCTG
CGGGCCCACCGCCAGGCCTGGTGCTGGCAGGATGAGTGGACAGAGCTGAGCATGGCTGAC
ATCCGGGCACTGGAAGAGGAGACTGCTCGCATGCTGGCCCAGCGCATGGCCAAGTGCAAC
ACAGGCAGTGAGGGGTCCGAGGCCCAGCCCCCCGGGAAACCGAGCACCGAGGCCCGGTCT
GCGGCCAGCAACACTGGCACCCCCGATGGGCCTGAGGCCCCCCCAGGCCCAGATGCCTCC
CCCGATGCCAGCTTTGGGAAGCAGTGGTCCTCATCCTCCCGTTCCTCCTACTCATCCCAA
CATGGAGGGGCTGTGTCTCCCCAGAGCTTGTCTGAGTGGCGCATGCAGAACATTGCCCGA
GACTCTGAGAACAGCTCCGAGGAAGAGTTCTTTGATGCCCACGAAGGCTTCTCGGACAGT
GAGGAGGTCTTCCCCAAGGAGATGACCAAGTGGAACTCCAATGACTTCATTGATGCCTTT
GCCTCCCCAGTGGAGGCAGAGGGAACGCCAGAGCCTGGAGCCGAGGCAGCTAAAGGCATT
GAGGATGGGGCCCAAGCACCCAGGGACTCAGAGGGCCTGGATGGAGCCGGGGAGCTGGGG
GCTGAGGCATGCGCAGTCCACGCCCTCTTCCTTATCCTGCACAGCGGCAACATCCTGGAC
TCAGGCCCTGGAGACGCCAACTCCAAGCAGGCGGATGTGCAGACGCTGAGCTCCGCCTTC
GAGGCCGTCACCCGCATCCACTTCCCTGAGGCCTTGGGCCACGTGGCGCTGCGACTGGTG
CCCTGTCCACCCATCTGCGCCGCCGCCTATGCCCTTGTCTCCAACCTGAGCCCTTACAGC
CACGATGGGGACAGCCTGTCTCGCTCCCAAGACCACATTCCACTGGCTGCCCTGCCACTG
CTGGCCACCTCATCCTCCCGCTACCAGGGCGCCGTGGCCACCGTCATTGCCCGCACCAAC
CAGGCCTACTCAGCCTTCCTGCGCTCACCTGAGGGTGCCGGCTTCTGTGGGCAGGTCGCA
CTGATTGGAGATGGTGTTGGTGGCATCCTGGGCTTTGATGCACTCTGCCACAGTGCTAAC
GCGGGCACCGGGAGTCGGGGCAGCAGCCGCCGTGGGAGCATGAACAATGAGCTGCTCTCT
CCGGAGTTTGGCCCAGTGCGGGACCCCCTGGCAGATGGTGTGGAAGGCCTGGGTCGGGGC
AGCCCAGAACCCTCGGCCTTGCCTCCCCAGCGCATCCCCAGCGACATGGCCAGTCCTGAG
CCCGAGGGCTCTCAGAACAGCCTTCAGGCAGCCCCCGCAACCACCTCCTCCTGGGAGCCC
CGGCGGGCAAGCACGGCCTTCTGCCCACCCGCTGCCAGTTCCGAGGCACCTGACGGCCCC
AGCAGCACTGCCCGCCTTGACTTCAAGGTCTCTGGCTTCTTCCTCTTCGGCTCCCCACTG
GGCCTGGTGCTGGCTCTGCGCAAAACTGTGATGCCCGCCCTGGAGGCAGCCCAGATGCGC
CCAGCCTGTGAACAGATCTACAACCTCTTCCACGCGGCCGACCCCTGCGCCTCACGCCTC
GAGCCCCTGCTGGCCCCGAAGTTCCAGGCCATCGCCCCACTGACCGTGCCCCGCTACCAG
AAGTTCCCCCTGGGAGATGGCTCATCCCTGCTGCTGGCCGACACTCTGCAGACGCACTCC
AGCCTCTTTCTGGAGGAGCTGGAGATGCTGGTGCCCTCAACACCCACCTCTACTAGCGGT
GCCTTCTGGAAGGGCAGTGAGTTGGCCACTGACCCCCCGGCCCAGCCAGCCGCCCCCAGC
ACCACCAGTGAGGTGGTTAAGATCCTGGAGCGCTGGTGGGGGACCAAGCGGATCGACTAC
TCGCTGTACTGCCCCGAGGCGCTCACCGCCTTTCCCACCGTCACGCTGCCCCACCTCTTC
CACGCCAGCTACTGGGAGTCCGCCGACGTGGTGGCGTTCATCCTGCGCCAGGTGATCGAG
AAGGAGCGGCCACAGCTGGCGGAATGCGAGGAGCCGTCCATCTACAGCCCGGCCTTCCCC
AGGGAGAAGTGGCAGCGAAAACGCACGCAGGTCAAGATCCGGAACGTCACTTCCAACCAC
CGGGCGAGCGACACGGTGGTGTGCGAGGGGCCGCCCCAGGTGCTAAGCGGGCGCTTCATG
TACGGGCCCCTGGACGTCGTCACGCTCACTGGAGAGAAGGTGGATGTCTACATCATGACG
CAGCCGCTGTCGGGCAAGTGGATCCACTTTGGCACCGAAGTCACCAATAGCTCGGGCCGC
CTCACCTTCCCAGTTCCCCCAGAACGCGCGCTGGGCATTGGTGTCTACCCCGTGCGCATG
GTGGTCAGGGGCGACCACACCTATGCCGAATGCTGCCTGACTGTGGTGGCCCGCGGCACG
GAGGCTGTGGTCTTCAGCATCGACGGCTCCTTCACCGCCAGCGTCTCCATCATGGGCAGC
GACCCCAAGGTGCGAGCTGGCGCCGTGGACGTGGTCAGGCACTGGCAGGACTCCGGCTAC
CTGATCGTGTATGTCACAGGCCGGCCGGATATGCAGAAGCACCGCGTGGTGGCATGGCTG
TCGCAGCACAACTTCCCCCACGGCGTCGTCTCCTTCTGCGACGGCCTCACCCACGACCCA
CTACGCCAGAAGGCAATGTTTCTGCAGAGCCTGGTGCAGGAGGTAGAACTGAACATCGTG
GCCGGTTATGGGTCTCCCAAAGATGTGGCTGTATACGCGGCGCTGGGGCTGTCCCCGAGC
CAGACCTACATCGTGGGCCGTGCCGTGCGGAAGCTACAGGCGCAGTGCCAGTTCCTGTCA
GACGGCTATGTGGCCCACCTGGGCCAGCTGGAAGCGGGCTCGCACTCGCATGCCTCCTCG
GGACCCCCGAGAGCTGCCTTGGGCAAGAGCAGCTATGGTGTGGCTGCCCCCGTGGACTTC
CTGCGCAAACAGAGCCAGCTGCTTCGCTCGAGGGGCCCCAGCCAGGCGGAGCGTGAGGGC
CCGGGAACACCACCCACCACCCTGGCACGGGGCAAAGCACGGAGCATCAGCCTGAAGCTG
GACAGCGAGGAGTGA
Enzyme 68 GenBank Gene ID AF334584 Link Image
Enzyme 68 GeneCard ID PITPNM1 Link Image
Enzyme 68 GenAtlas ID PITPNM1 Link Image
Enzyme 68 HGNC ID HGNC:9003 Link Image
Enzyme 68 Chromosome Location 1
Enzyme 68 Locus 11q13
Enzyme 68 SNPs SNPJam Report Link Image
Enzyme 68 General References
  1. Rubboli F, Bulfone A, Bogni S, Marchitiello A, Zollo M, Borsani G, Ballabio A, Banfi S: A mammalian homologue of the Drosophila retinal degeneration B gene: implications for the evolution of phototransduction mechanisms. Genes Funct. 1997 Jun;1(3):205-13. [PubMed Link Image]
  2. Lev S, Hernandez J, Martinez R, Chen A, Plowman G, Schlessinger J: Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein. Mol Cell Biol. 1999 Mar;19(3):2278-88. [PubMed Link Image]
  3. Ocaka L, Spalluto C, Wilson DI, Hunt DM, Halford S: Chromosomal localization, genomic organization and evolution of the genes encoding human phosphatidylinositol transfer protein membrane-associated (PITPNM) 1, 2 and 3. Cytogenet Genome Res. 2005;108(4):293-302. [PubMed Link Image]
  4. 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]
  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. Litvak V, Shaul YD, Shulewitz M, Amarilio R, Carmon S, Lev S: Targeting of Nir2 to lipid droplets is regulated by a specific threonine residue within its PI-transfer domain. Curr Biol. 2002 Sep 3;12(17):1513-8. [PubMed Link Image]
  7. Tian D, Litvak V, Toledo-Rodriguez M, Carmon S, Lev S: Nir2, a novel regulator of cell morphogenesis. Mol Cell Biol. 2002 Apr;22(8):2650-62. [PubMed Link Image]
  8. Litvak V, Argov R, Dahan N, Ramachandran S, Amarilio R, Shainskaya A, Lev S: Mitotic phosphorylation of the peripheral Golgi protein Nir2 by Cdk1 provides a docking mechanism for Plk1 and affects cytokinesis completion. Mol Cell. 2004 May 7;14(3):319-30. [PubMed Link Image]
  9. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  10. Amarilio R, Ramachandran S, Sabanay H, Lev S: Differential regulation of endoplasmic reticulum structure through VAP-Nir protein interaction. J Biol Chem. 2005 Feb 18;280(7):5934-44. Epub 2004 Nov 15. [PubMed Link Image]
  11. Litvak V, Dahan N, Ramachandran S, Sabanay H, Lev S: Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function. Nat Cell Biol. 2005 Mar;7(3):225-34. Epub 2005 Feb 20. [PubMed Link Image]
  12. 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]
  13. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
Enzyme 68 Metabolite References Not Available
Enzyme 69 [top]
Enzyme 69 ID 12959
Enzyme 69 Name Membrane-associated phosphatidylinositol transfer protein 2
Enzyme 69 Synonyms
  1. Phosphatidylinositol transfer protein, membrane-associated 2
  2. PITPnm 2
  3. Pyk2 N-terminal domain-interacting receptor 3
  4. NIR-3
Enzyme 69 Gene Name PITPNM2
Enzyme 69 Protein Sequence >Membrane-associated phosphatidylinositol transfer protein 2
MIIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETYGEGSGVEILENRPYTDGPGGSGQYTH
KVYHVGMHIPSWFRSILPKAALRVVEESWNAYPYTRTRFTCPFVEKFSIDIETFYKTDAG
ENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDPKLFQSTKTQRGPLSENWIEEY
KKQVFPIMCAYKLCKVEFRYWGMQSKIERFIHDTGLRRVMVRAHRQAWCWQDEWYGLSME
NIRELEKEAQLMLSRKMAQFNEDGEEATELVKHEAVSDQTSGEPPEPSSSNGEPLVGRGL
KKQWSTSSKSSRSSKRGASPSRHSISEWRMQSIARDSDESSDDEFFDAHEDLSDTEEMFP
KDITKWSSNDLMDKIESPEPEDTQDGLYRQGAPEFRVASSVEQLNIIEDEVSQPLAAPPS
KIHVLLLVLHGGTILDTGAGDPSSKKGDANTIANVFDTVMRVHYPSALGRLAIRLVPCPP
VCSDAFALVSNLSPYSHDEGCLSSSQDHIPLAALPLLATSSPQYQEAVATVIQRANLAYG
DFIKSQEGMTFNGQVCLIGDCVGGILAFDALCYSNQPVSESQSSSRRGSVVSMQDNDLLS
PGILMNAAHCCGGGGGGGGGGGSSGGGGSSGGSSLESSRHLSRSNVDIPRSNGTEDPKRQ
LPRKRSDSSTYELDTIQQHQAFLSSLHASVLRTEPCSRHSSSSTMLDGTGALGRFDFEIT
DLFLFGCPLGLVLALRKTVIPALDVFQLRPACQQVYNLFHPADPSASRLEPLLERRFHAL
PPFSVPRYQRYPLGDGCSTLLADVLQTHNAAFQEHGAPSSPGTAPASRGFRRASEISIAS
QVSGMAESYTASSIAQKAPDALSHTPSVRRLSLLALPAPSPTTPGPHPPARKASPGLERA
PGLPELDIGEVAAKWWGQKRIDYALYCPDALTAFPTVALPHLFHASYWESTDVVSFLLRQ
VMRHDNSSILELDGKEVSVFTPSKPREKWQRKRTHVKLRNVTANHRINDALANEDGPQVL
TGRFMYGPLDMVTLTGEKVDVHIMTQPPSGEWLYLDTLVTNNSGRVSYTIPESHRLGVGV
YPIKMVVRGDHTFADSYITVLPKGTEFVVFSIDGSFAASVSIMGSDPKVRAGAVDVVRHW
QDLGYLIIYVTGRPDMQKQRVVAWLAQHNFPHGVVSFCDGLVHDPLRHKANFLKLLISEL
HLRVHAAYGSTKDVAVYSAISLSPMQIYIVGRPTKKLQQQCQFITDGYAAHLAQLKYSHR
ARPARNTATRMALRKGSFGLPGQGDFLRSRNHLLRTISAQPSGPSHRHERTQSQADGEQR
GQRSMSVAAGCWGRAMTGRLEPGAAAGPK
Enzyme 69 Number of Residues 1349
Enzyme 69 Molecular Weight 148931.9
Enzyme 69 Theoretical pI 7.17
Enzyme 69 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • metal ion binding
Process
  • establishment of localization
  • transport
Component
  • cell part
  • intracellular
Enzyme 69 General Function Involved in metal ion binding
Enzyme 69 Specific Function Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes (in vitro). Binds calcium ions
Enzyme 69 Pathways Not Available
Enzyme 69 Reactions Not Available
Enzyme 69 Pfam Domain Function
Enzyme 69 Signals
  • None
Enzyme 69 Transmembrane Regions
  • None
Enzyme 69 Essentiality Not Available
Enzyme 69 GenBank ID Protein 24308237 Link Image
Enzyme 69 UniProtKB/Swiss-Prot ID Q9BZ72 Link Image
Enzyme 69 UniProtKB/Swiss-Prot Entry Name PITM2_HUMAN Link Image
Enzyme 69 PDB ID Not Available
Enzyme 69 Cellular Location Not Available
Enzyme 69 Gene Sequence >4050 bp
ATGATTATAAAGGAATATCGGATTCCTCTGCCAATGACCGTGGAGGAGTACCGCATCGCC
CAGCTGTACATGATACAGAAGAAGAGCCGTAACGAGACATATGGCGAAGGCAGCGGCGTG
GAGATCCTGGAGAACCGGCCGTACACAGATGGCCCAGGCGGCTCTGGGCAGTACACACAC
AAGGTGTATCATGTGGGCATGCACATTCCCAGCTGGTTCCGCTCCATCCTGCCCAAGGCA
GCCCTGCGGGTGGTGGAGGAGTCTTGGAATGCCTACCCCTACACCCGAACCAGGTTCACC
TGTCCTTTCGTGGAGAAATTCTCCATCGACATTGAAACCTTTTATAAAACTGATGCTGGA
GAAAACCCCGACGTGTTCAACCTCTCTCCTGTGGAAAAGAACCAGCTGACAATCGACTTC
ATCGACATTGTCAAAGACCCTGTGCCCCACAACGAGTATAAGACAGAAGAGGACCCCAAG
CTGTTCCAGTCAACCAAGACCCAGCGGGGGCCCCTGTCCGAGAACTGGATCGAGGAGTAC
AAGAAGCAGGTCTTCCCCATCATGTGCGCATACAAGCTCTGCAAGGTGGAGTTCCGCTAC
TGGGGCATGCAGTCCAAGATCGAGAGGTTCATCCACGACACCGGACTACGGAGGGTGATG
GTGCGGGCTCACCGGCAGGCCTGGTGCTGGCAGGACGAGTGGTATGGGCTGAGCATGGAG
AACATCCGGGAGCTGGAGAAGGAGGCACAGCTCATGCTTTCCCGTAAGATGGCCCAGTTC
AATGAGGATGGTGAGGAGGCCACTGAGCTCGTCAAGCACGAAGCCGTCTCGGACCAGACC
TCTGGGGAGCCCCCGGAGCCCAGCAGCAGCAATGGGGAGCCCCTAGTGGGGCGCGGCCTC
AAGAAACAGTGGTCCACATCCTCCAAGTCGTCTCGGTCGTCCAAGCGGGGAGCGAGTCCT
TCCCGCCACAGCATCTCAGAGTGGAGGATGCAGAGTATTGCCAGGGACTCGGATGAGAGC
TCAGATGATGAGTTCTTCGATGCGCACGAGGACCTGTCCGACACAGAGGAAATGTTCCCC
AAGGACATCACCAAGTGGAGCTCCAATGACCTCATGGACAAGATCGAGAGCCCAGAGCCG
GAAGACACACAAGATGGTCTGTACCGCCAGGGTGCCCCTGAGTTCAGGGTGGCCTCCAGT
GTGGAGCAGCTGAACATCATAGAGGACGAGGTTAGCCAGCCGCTGGCTGCACCGCCCTCC
AAGATCCACGTGCTGCTACTGGTGCTGCACGGAGGCACCATCCTGGACACAGGCGCCGGG
GACCCCAGCTCCAAGAAGGGCGATGCTAACACCATCGCCAACGTGTTCGACACCGTCATG
CGCGTGCACTACCCCAGCGCCCTGGGCCGCCTTGCCATCCGCCTGGTGCCCTGCCCGCCC
GTCTGCTCTGACGCCTTTGCCCTGGTCTCCAACCTCAGCCCCTACAGCCATGACGAAGGC
TGTCTGTCCAGCAGTCAGGACCACATTCCCCTGGCTGCCCTCCCCCTGCTGGCCACCTCC
TCCCCCCAGTACCAGGAGGCAGTTGCCACAGTGATTCAGCGAGCCAACCTTGCCTATGGG
GACTTCATCAAGTCCCAGGAGGGCATGACCTTCAATGGGCAGGTCTGCCTGATTGGGGAC
TGCGTCGGGGGCATCCTGGCATTTGATGCCCTGTGCTACAGTAACCAGCCGGTGTCTGAG
AGTCAGAGCAGCAGCCGCCGGGGCAGCGTGGTCAGCATGCAGGACAATGACCTGCTGTCC
CCGGGCATCCTGATGAATGCAGCACACTGCTGCGGTGGTGGCGGTGGCGGCGGTGGCGGT
GGTGGCAGCAGTGGTGGTGGTGGCAGTAGTGGTGGCTCCAGCCTGGAGAGCAGTCGGCAC
CTGAGCCGAAGCAACGTCGACATCCCCCGCAGCAACGGCACTGAGGACCCCAAAAGGCAA
CTGCCCCGCAAGAGGAGCGACTCATCCACCTACGAGCTGGATACCATCCAGCAGCACCAG
GCCTTCCTGTCCAGCCTCCATGCCAGCGTGCTGAGGACTGAGCCCTGCTCACGCCATTCC
AGCAGCTCCACCATGCTGGATGGCACAGGTGCCCTGGGCAGGTTTGACTTTGAGATCACC
GACCTCTTCCTCTTCGGGTGCCCGCTGGGGCTGGTCCTGGCCTTGAGGAAGACTGTCATC
CCAGCCCTGGATGTTTTCCAGCTGCGGCCGGCCTGCCAGCAAGTCTACAACCTCTTCCAC
CCCGCGGACCCGTCAGCTTCACGCCTGGAGCCGCTGCTGGAACGGCGCTTTCACGCCCTG
CCGCCTTTCAGCGTCCCCCGCTACCAACGCTACCCGCTGGGGGATGGCTGCTCCACGCTG
CTGGCGGATGTGCTCCAGACCCACAATGCAGCCTTCCAAGAGCATGGCGCCCCCTCCTCG
CCGGGCACTGCCCCTGCCAGTCGTGGCTTCCGCCGAGCCAGTGAGATCAGCATCGCCAGC
CAGGTGTCAGGCATGGCTGAGAGCTACACGGCATCCAGCATCGCCCAGAAGGCCCCCGAT
GCGCTCAGCCATACCCCCAGCGTCAGGCGTCTGTCCCTGCTCGCCCTGCCCGCCCCCAGC
CCCACCACCCCTGGCCCCCACCCTCCAGCCAGGAAGGCAAGCCCTGGCCTGGAGAGGGCC
CCTGGCCTCCCTGAGCTGGACATTGGAGAAGTCGCTGCAAAGTGGTGGGGCCAGAAGCGG
ATCGACTACGCCCTGTACTGCCCTGACGCCCTCACGGCCTTCCCCACGGTGGCTCTGCCT
CACCTCTTCCACGCCAGCTACTGGGAGTCAACAGACGTGGTCTCCTTTCTGCTGAGACAG
GTCATGAGGCATGACAACTCCAGCATCTTGGAGCTGGATGGCAAGGAAGTGTCGGTGTTC
ACCCCCTCAAAGCCAAGGGAGAAGTGGCAGCGCAAGCGGACCCACGTGAAGCTGCGGAAC
GTGACGGCCAACCACCGGATCAATGATGCCCTTGCCAATGAGGACGGCCCCCAGGTTCTG
ACGGGCAGGTTCATGTATGGGCCCCTGGACATGGTCACCCTGACTGGGGAGAAGGTGGAT
GTGCACATCATGACCCAGCCGCCCTCAGGCGAGTGGCTCTACCTGGATACGCTGGTGACC
AACAACAGTGGGCGTGTCTCCTACACCATCCCTGAGTCGCACCGCCTGGGCGTGGGTGTC
TACCCTATCAAGATGGTGGTCAGGGGAGACCACACGTTTGCCGACAGCTACATCACCGTG
CTGCCCAAGGGCACAGAGTTCGTGGTCTTCAGCATCGACGGTTCCTTTGCCGCTAGCGTG
TCCATCATGGGCAGCGACCCCAAGGTGCGGGCCGGGGCCGTGGACGTGGTGCGGCACTGG
CAGGACCTGGGCTACCTCATCATCTACGTGACGGGCCGGCCCGACATGCAGAAGCAGCGG
GTGGTGGCGTGGCTGGCCCAGCACAACTTCCCCCATGGCGTGGTGTCCTTCTGTGACGGC
CTGGTGCATGACCCGCTGCGGCACAAGGCCAACTTCCTGAAGCTGCTCATCTCCGAGCTG
CACCTGCGCGTGCACGCGGCCTATGGCTCCACCAAGGACGTGGCGGTGTACAGCGCCATT
AGCCTGTCCCCCATGCAGATCTACATCGTGGGCCGGCCCACCAAGAAGCTGCAGCAGCAG
TGCCAGTTCATCACGGATGGCTACGCGGCCCACCTGGCGCAGCTGAAGTACAGCCACCGG
GCGCGGCCCGCTCGCAACACGGCCACCCGCATGGCGCTGCGCAAGGGCAGCTTCGGCCTG
CCCGGCCAGGGCGACTTTCTGCGCTCCCGGAACCACCTGCTTCGCACCATCTCGGCCCAG
CCCAGCGGGCCCAGCCACCGGCACGAGCGGACACAGAGCCAGGCGGATGGCGAGCAGCGG
GGCCAGCGCAGCATGAGTGTGGCGGCCGGCTGCTGGGGCCGCGCCATGACTGGCCGCCTG
GAGCCGGGGGCAGCCGCGGGCCCCAAGTAG
Enzyme 69 GenBank Gene ID NM_020845.2 Link Image
Enzyme 69 GeneCard ID PITPNM2 Link Image
Enzyme 69 GenAtlas ID PITPNM2 Link Image
Enzyme 69 HGNC ID HGNC:21044 Link Image
Enzyme 69 Chromosome Location 1
Enzyme 69 Locus 12q24.31
Enzyme 69 SNPs SNPJam Report Link Image
Enzyme 69 General References
  1. Lev S, Hernandez J, Martinez R, Chen A, Plowman G, Schlessinger J: Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein. Mol Cell Biol. 1999 Mar;19(3):2278-88. [PubMed Link Image]
  2. Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed Link Image]
Enzyme 69 Metabolite References Not Available
Enzyme 70 [top]
Enzyme 70 ID 12960
Enzyme 70 Name Membrane-associated phosphatidylinositol transfer protein 3
Enzyme 70 Synonyms
  1. Phosphatidylinositol transfer protein, membrane-associated 3
  2. PITPnm 3
  3. Pyk2 N-terminal domain-interacting receptor 1
  4. NIR-1
Enzyme 70 Gene Name PITPNM3
Enzyme 70 Protein Sequence >Membrane-associated phosphatidylinositol transfer protein 3
MAKAGRAGGPPPGGGAPWHLRNVLSDSVESSDDEFFDAREEMAEGKNAILIGMSQWNSND
LVEQIETMGKLDEHQGEGTAPCTSSILQEKQRELYRVSLRRQRFPAQGSIEIHEDSEEGC
PQRSCKTHVLLLVLHGGNILDTGAGDPSCKAADIHTFSSVLEKVTRAHFPAALGHILIKF
VPCPAICSEAFSLVSHLNPYSHDEGCLSSSQDHVPLAALPLLAISSPQYQDAVATVIERA
NQVYREFLKSSDGIGFSGQVCLIGDCVGGLLAFDAICYSAGPSGDSPASSSRKGSISSTQ
DTPVAVEEDCSLASSKRLSKSNIDISSGLEDEEPKRPLPRKQSDSSTYDCEAITQHHAFL
SSIHSSVLKDESETPAAGGPQLPEVSLGRFDFDVSDFFLFGSPLGLVLAMRRTVLPGLDG
FQVRPACSQVYSFFHCADPSASRLEPLLEPKFHLVPPVSVPRYQRFPLGDGQSLLLADAL
HTHSPLFLEGSSRDSPPLLDAPASPPQASRFQRPGRRMSEGSSHSESSESSDSMAPVGAS
RITAKWWGSKRIDYALYCPDVLTAFPTVALPHLFHASYWESTDVVAFILRQVMRYESVNI
KESARLDPAALSPANPREKWLRKRTQVKLRNVTANHRANDVIAAEDGPQVLVGRFMYGPL
DMVALTGEKVDILVMAEPSSGRWVHLDTEITNSSGRITYNVPRPRRLGVGVYPVKMVVRG
DQTCAMSYLTVLPRGMECVVFSIDGSFAASVSIMGSDPKVRPGAVDVVRHWQDLGYMILY
ITGRPDMQKQRVVSWLSQHNFPQGMIFFSDGLVHDPLRQKAIFLRNLMQECFIKISAAYG
STKDISVYSVLGLPASQIFIVGRPTKKYQTQCQFLSEGYAAHLAALEASHRSRPKKNNSR
MILRKGSFGLHAQPEFLRKRNHLRRTMSVQQPDPPAANPKPERAQSQPESDKDHERPLPA
LSWARGPPKFESVP
Enzyme 70 Number of Residues 974
Enzyme 70 Molecular Weight 106780.1
Enzyme 70 Theoretical pI 7.14
Enzyme 70 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • metal ion binding
Process
  • establishment of localization
  • transport
Component
  • cell part
  • intracellular
Enzyme 70 General Function Involved in metal ion binding
Enzyme 70 Specific Function Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes (in vitro). Binds calcium ions
Enzyme 70 Pathways Not Available
Enzyme 70 Reactions Not Available
Enzyme 70 Pfam Domain Function
Enzyme 70 Signals
  • None
Enzyme 70 Transmembrane Regions
  • None
Enzyme 70 Essentiality Not Available
Enzyme 70 GenBank ID Protein 190358515 Link Image
Enzyme 70 UniProtKB/Swiss-Prot ID Q9BZ71 Link Image
Enzyme 70 UniProtKB/Swiss-Prot Entry Name PITM3_HUMAN Link Image
Enzyme 70 PDB ID Not Available
Enzyme 70 Cellular Location Not Available
Enzyme 70 Gene Sequence >2925 bp
ATGGCCAAGGCGGGCCGTGCAGGTGGTCCTCCCCCGGGCGGCGGTGCCCCCTGGCACCTT
CGAAATGTCCTCAGTGACTCTGTGGAGAGCTCAGATGATGAATTCTTTGATGCCAGAGAG
GAGATGGCTGAAGGGAAGAATGCCATCCTCATTGGGATGAGCCAGTGGAACTCCAATGAC
CTCGTGGAGCAGATCGAGACCATGGGGAAACTGGACGAGCATCAAGGAGAAGGGACCGCG
CCGTGCACATCCAGCATCCTCCAGGAGAAGCAGCGAGAACTGTACCGGGTTTCCTTGAGA
AGACAGAGGTTCCCAGCCCAGGGAAGCATCGAGATCCACGAAGACAGCGAGGAAGGCTGC
CCGCAGCGCTCCTGCAAGACACATGTCCTCCTGCTGGTCCTGCATGGGGGAAACATCCTG
GACACGGGTGCCGGGGACCCGTCCTGCAAGGCAGCCGACATCCACACCTTCAGCTCCGTG
CTGGAGAAGGTCACACGAGCCCATTTCCCTGCTGCCCTGGGCCACATCCTCATCAAGTTC
GTCCCCTGTCCTGCCATCTGCTCTGAGGCTTTCTCGCTTGTCTCTCACCTGAACCCCTAC
AGCCACGATGAGGGCTGCCTCAGCAGCAGCCAGGACCACGTCCCTCTGGCCGCCCTTCCC
CTGTTGGCCATCTCCTCCCCGCAGTACCAGGATGCTGTCGCCACCGTCATCGAGCGAGCC
AACCAGGTCTACAGAGAGTTCCTGAAGTCCTCTGATGGGATTGGCTTCAGTGGGCAGGTG
TGTCTCATCGGGGACTGTGTGGGGGGCCTCCTGGCCTTCGATGCCATCTGCTACAGTGCG
GGGCCCTCAGGGGACAGCCCTGCCAGCAGCAGCCGGAAGGGGAGCATCAGCAGCACCCAG
GACACCCCAGTCGCGGTGGAGGAAGATTGCAGCCTGGCCAGCAGCAAGCGTCTCAGCAAA
AGCAACATTGACATCTCCAGTGGGTTGGAGGATGAGGAGCCCAAGAGGCCGTTGCCGCGG
AAACAGAGCGACTCCTCCACCTATGACTGCGAGGCCATCACCCAGCACCATGCCTTCCTC
TCAAGCATCCACTCCAGCGTGCTAAAGGATGAGTCTGAGACCCCGGCGGCTGGGGGGCCG
CAGCTCCCTGAGGTCAGCCTGGGCCGCTTTGACTTCGATGTGTCCGACTTCTTCCTCTTC
GGCTCGCCACTGGGCCTGGTCCTGGCCATGCGGAGGACGGTGCTGCCTGGGCTGGACGGC
TTCCAGGTGCGTCCTGCCTGCAGCCAGGTCTACAGCTTCTTCCATTGCGCAGACCCCTCT
GCCTCACGGCTCGAGCCACTGCTGGAGCCCAAGTTCCACCTGGTGCCGCCTGTCAGCGTG
CCTCGCTACCAGAGGTTCCCACTGGGCGATGGGCAGTCCCTCCTCCTCGCTGATGCCCTA
CACACCCACAGCCCCCTCTTCCTGGAGGGCAGCTCCCGGGACAGCCCGCCACTTCTGGAT
GCCCCTGCCTCGCCCCCTCAGGCCTCGAGGTTCCAGCGCCCAGGACGGAGGATGAGCGAG
GGGAGCTCCCACAGCGAGAGCTCGGAGTCCTCGGACAGCATGGCACCCGTGGGTGCCTCC
CGCATCACAGCCAAGTGGTGGGGAAGCAAGAGGATCGACTATGCCCTGTACTGCCCTGAT
GTCCTCACGGCCTTCCCCACCGTGGCCCTGCCCCACCTCTTCCACGCCAGTTACTGGGAG
TCCACAGACGTGGTGGCCTTCATCCTGAGACAGGTAATGCGCTATGAGAGCGTGAACATC
AAGGAAAGCGCCCGCCTGGACCCTGCAGCACTGAGTCCTGCCAACCCCCGGGAGAAGTGG
CTTCGTAAGCGGACTCAGGTCAAGCTGAGGAATGTCACGGCTAATCACCGGGCCAATGAT
GTGATTGCTGCTGAAGATGGCCCCCAGGTCCTGGTGGGGCGGTTCATGTACGGGCCCCTC
GACATGGTGGCTCTGACTGGAGAGAAGGTGGACATCCTAGTAATGGCAGAGCCATCCTCA
GGCCGCTGGGTACACCTGGACACAGAGATCACCAACAGCAGTGGTCGCATCACATACAAT
GTGCCGCGGCCCCGGCGCCTGGGGGTTGGTGTCTATCCTGTGAAGATGGTCGTCAGGGGC
GACCAGACCTGTGCCATGAGCTACCTCACGGTGTTGCCCAGGGGCATGGAGTGTGTAGTG
TTCAGCATTGATGGGTCCTTCGCGGCCAGCGTGTCTATCATGGGAAGCGACCCCAAGGTC
CGGCCGGGTGCAGTGGATGTTGTCCGGCACTGGCAGGACTTGGGCTACATGATCCTTTAC
ATCACGGGACGGCCGGACATGCAGAAGCAGCGGGTGGTGTCGTGGCTGTCCCAGCACAAC
TTCCCACAGGGCATGATCTTCTTCTCCGATGGGCTGGTGCATGACCCGCTGCGGCAGAAG
GCCATCTTCCTGCGCAACCTCATGCAGGAGTGCTTCATCAAAATCAGTGCGGCCTATGGC
TCCACGAAGGACATCTCTGTCTACAGCGTGCTGGGCCTGCCTGCCTCCCAGATCTTCATT
GTGGGCCGGCCCACCAAGAAGTACCAAACCCAGTGCCAGTTCCTGAGCGAGGGCTACGCC
GCACACCTGGCCGCGCTGGAGGCCAGCCACCGCTCACGCCCAAAGAAGAACAACTCGCGC
ATGATCCTGCGCAAGGGCAGCTTCGGGCTGCACGCGCAGCCAGAGTTCCTGCGGAAGCGC
AACCACCTGCGCAGAACCATGTCAGTGCAGCAGCCCGACCCGCCCGCCGCCAACCCCAAG
CCCGAGCGGGCCCAGAGCCAGCCCGAGTCGGACAAAGACCACGAGCGGCCGCTGCCGGCG
CTCAGCTGGGCGCGTGGGCCCCCCAAGTTCGAGTCGGTGCCCTGA
Enzyme 70 GenBank Gene ID NM_031220.3 Link Image
Enzyme 70 GeneCard ID PITPNM3 Link Image
Enzyme 70 GenAtlas ID PITPNM3 Link Image
Enzyme 70 HGNC ID HGNC:21043 Link Image
Enzyme 70 Chromosome Location 1
Enzyme 70 Locus 17p13
Enzyme 70 SNPs SNPJam Report Link Image
Enzyme 70 General References
  1. Lev S, Hernandez J, Martinez R, Chen A, Plowman G, Schlessinger J: Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein. Mol Cell Biol. 1999 Mar;19(3):2278-88. [PubMed Link Image]
  2. 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]
  3. 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]
  4. 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]
  5. Kohn L, Kadzhaev K, Burstedt MS, Haraldsson S, Hallberg B, Sandgren O, Golovleva I: Mutation in the PYK2-binding domain of PITPNM3 causes autosomal dominant cone dystrophy (CORD5) in two Swedish families. Eur J Hum Genet. 2007 Jun;15(6):664-71. Epub 2007 Mar 21. [PubMed Link Image]
Enzyme 70 Metabolite References Not Available
Enzyme 71 [top]
Enzyme 71 ID 12961
Enzyme 71 Name Pleckstrin homology domain-containing family A member 8
Enzyme 71 Synonyms
  1. PH domain-containing family A member 8
  2. Phosphatidylinositol-four-phosphate adapter protein 2
  3. FAPP-2
  4. Phosphoinositol 4-phosphate adapter protein 2
  5. hFAPP2
  6. Serologically defined breast cancer antigen NY-BR-86
Enzyme 71 Gene Name PLEKHA8
Enzyme 71 Protein Sequence >Pleckstrin homology domain-containing family A member 8
MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTR
MDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSEL
RLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSE
LLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELSTCENGSLNMEINGEEEILMKNK
NSLYLKSAEIDCSISSEENTDDNITVQGEIRKEDGMENLKNHDNNLTQSGSDSSCSPECL
WEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMD
LVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLT
EVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRATPSYEDFVAALTVKEGDHRKE
AFSIGMQRDLSLYLPAMKKQMAILDALYEVHGLESDEVV
Enzyme 71 Number of Residues 519
Enzyme 71 Molecular Weight 58306.0
Enzyme 71 Theoretical pI 4.89
Enzyme 71 GO Classification
Function
  • binding
  • glycolipid binding
  • glycolipid transporter activity
  • lipid binding
  • lipid transporter activity
  • substrate-specific transporter activity
  • transporter activity
Process
  • establishment of localization
  • glycolipid transport
  • lipid transport
  • transport
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 71 General Function Involved in glycolipid transporter activity
Enzyme 71 Specific Function Involved in TGN-to-plasma membrane transport and in the formation of post-Golgi constitutive carriers. May play a role in ensuring the coordination of the budding and the fission reactions
Enzyme 71 Pathways Not Available
Enzyme 71 Reactions Not Available
Enzyme 71 Pfam Domain Function
Enzyme 71 Signals
  • None
Enzyme 71 Transmembrane Regions
  • None
Enzyme 71 Essentiality Not Available
Enzyme 71 GenBank ID Protein 308153327 Link Image
Enzyme 71 UniProtKB/Swiss-Prot ID Q96JA3 Link Image
Enzyme 71 UniProtKB/Swiss-Prot Entry Name PKHA8_HUMAN Link Image
Enzyme 71 PDB ID Not Available
Enzyme 71 Cellular Location Not Available
Enzyme 71 Gene Sequence >1560 bp
ATGGAGGGGGTGCTGTACAAGTGGACCAACTATCTGAGCGGTTGGCAGCCTCGATGGTTC
CTTCTCTGTGGGGGAATATTGTCCTATTATGATTCTCCTGAAGATGCCTGGAAAGGTTGC
AAAGGGAGCATACAAATGGCAGTCTGTGAAATTCAAGTTCATTCTGTAGATAATACACGC
ATGGACCTGATAATCCCTGGGGAACAGTATTTCTACCTGAAGGCCAGAAGTGTGGCTGAA
AGACAGCGGTGGCTGGTGGCCCTGGGATCAGCCAAGGCTTGCCTGACTGACAGTAGGACC
CAGAAGGAGAAAGAGTTTGCTGAAAACACTGAAAACTTGAAAACCAAAATGTCAGAACTA
AGACTCTACTGTGACCTCCTTGTTCAGCAAGTAGATAAAACAAAAGAAGTGACCACAACT
GGTGTGTCCAATTCTGAGGAGGGAATTGATGTGGGAACTTTGCTGAAATCAACCTGTAAT
ACTTTTCTGAAGACCTTGGAAGAATGCATGCAGATCGCAAATGCAGCCTTCACCTCTGAG
CTGCTCTACCGCACTCCACCAGGATCACCTCAGCTGGCCATGCTCAAGTCCAGCAAGATG
AAACATCCTATTATACCAATTCATAATTCATTGGAAAGGCAAATGGAGTTGAGCACTTGT
GAAAATGGATCTTTAAATATGGAAATAAATGGTGAGGAAGAAATCCTAATGAAAAATAAG
AATTCCTTATATTTGAAATCTGCAGAGATAGACTGCAGCATATCAAGTGAGGAAAATACA
GATGATAATATAACAGTCCAAGGTGAAATAAGGAAGGAAGATGGAATGGAAAACCTGAAA
AATCATGACAATAACTTGACTCAGTCTGGATCAGACTCAAGTTGCTCTCCGGAATGCCTC
TGGGAGGAAGGCAAAGAAGTTATCCCAACTTTCTTTAGTACCATGAACACAAGCTTTAGT
GACATTGAACTTCTGGAAGACAGTGGCATTCCCACAGAAGCATTCTTGGCATCATGTTAT
GCTGTGGTTCCAGTATTAGACAAACTTGGCCCTACAGTGTTTGCTCCTGTTAAGATGGAT
CTTGTTGGAAATATTAAGAAAGTAAATCAGAAGTATATAACCAACAAAGAAGAGTTTACC
ACTCTCCAGAAGATAGTGCTGCACGAAGTGGAGGCGGATGTAGCCCAGGTTAGGAACTCA
GCGACTGAAGCCCTCTTGTGGCTGAAGAGAGGTCTCAAATTTTTGAAGGGATTTTTGACA
GAAGTGAAAAATGGGGAGAAGGATATCCAGACAGCCCTAAATAATGCATATGGTAAAACA
TTGCGGCAACACCATGGCTGGGTAGTTCGAGGGGTTTTTGCGTTAGCTTTAAGGGCAGCT
CCATCCTATGAAGATTTTGTGGCCGCGTTAACCGTAAAGGAAGGTGACCACCAGAAAGAA
GCTTTCAGTATTGGGATGCAGAGGGACCTCAGCCTTTACCTCCCTGCCATGGAGAAGCAG
CTGGCCATACTGGACACTTTATATGAGGTCCACGGGCTGGAATCTGATGAGGTGGTATGA
Enzyme 71 GenBank Gene ID NM_001197026.1 Link Image
Enzyme 71 GeneCard ID PLEKHA8 Link Image
Enzyme 71 GenAtlas ID PLEKHA8 Link Image
Enzyme 71 HGNC ID HGNC:30037 Link Image
Enzyme 71 Chromosome Location 7
Enzyme 71 Locus 7p21-p11.2
Enzyme 71 SNPs SNPJam Report Link Image
Enzyme 71 General References
  1. Dowler S, Currie RA, Campbell DG, Deak M, Kular G, Downes CP, Alessi DR: Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities. Biochem J. 2000 Oct 1;351(Pt 1):19-31. [PubMed Link Image]
  2. 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]
  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. Scanlan MJ, Gout I, Gordon CM, Williamson B, Stockert E, Gure AO, Jager D, Chen YT, Mackay A, O'Hare MJ, Old LJ: Humoral immunity to human breast cancer: antigen definition and quantitative analysis of mRNA expression. Cancer Immun. 2001 Mar 30;1:4. [PubMed Link Image]
  5. Godi A, Di Campli A, Konstantakopoulos A, Di Tullio G, Alessi DR, Kular GS, Daniele T, Marra P, Lucocq JM, De Matteis MA: FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P. Nat Cell Biol. 2004 May;6(5):393-404. Epub 2004 Apr 25. [PubMed Link Image]
  6. 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 71 Metabolite References Not Available
Enzyme 72 [top]
Enzyme 72 ID 12962
Enzyme 72 Name PI-PLC X domain-containing protein 1
Enzyme 72 Synonyms Not Available
Enzyme 72 Gene Name PLCXD1
Enzyme 72 Protein Sequence >PI-PLC X domain-containing protein 1
MGGQVSASNSFSRLHCRNANEDWMSALCPRLWDVPLHHLSIPGSHDTMTYCLNKKSPISH
EESRLLQLLNKALPCITRPVVLKWSVTQALDVTEQLDAGVRYLDLRIAHMLEGSEKNLHF
VHMVYTTALVEDTLTEISEWLERHPREVVILACRNFEGLSEDLHEYLVACIKNIFGDMLC
PRGEVPTLRQLWSRGQQVIVSYEDESSLRRHHELWPGVPYWWGNRVKTEALIRYLETMKS
CGRPGGLFVAGINLTENLQYVLAHPSESLEKMTLPNLPRLSAWVREQCPGPGSRCTNIIA
GDFIGADGFVSDVIALNQKLLWC
Enzyme 72 Number of Residues 323
Enzyme 72 Molecular Weight 36667.8
Enzyme 72 Theoretical pI 6.56
Enzyme 72 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • signaling
  • signaling pathway
Component
Enzyme 72 General Function Involved in phosphoric diester hydrolase activity
Enzyme 72 Specific Function Not Available
Enzyme 72 Pathways Not Available
Enzyme 72 Reactions Not Available
Enzyme 72 Pfam Domain Function
Enzyme 72 Signals
  • None
Enzyme 72 Transmembrane Regions
  • None
Enzyme 72 Essentiality Not Available
Enzyme 72 GenBank ID Protein 7023908 Link Image
Enzyme 72 UniProtKB/Swiss-Prot ID Q9NUJ7 Link Image
Enzyme 72 UniProtKB/Swiss-Prot Entry Name PLCX1_HUMAN Link Image
Enzyme 72 PDB ID Not Available
Enzyme 72 Cellular Location Not Available
Enzyme 72 Gene Sequence >972 bp
ATGGGTGGGCAGGTGAGCGCTTCCAACAGCTTCTCGAGGCTGCACTGCAGAAATGCCAAC
GAGGACTGGATGTCGGCACTGTGTCCCCGGCTCTGGGATGTGCCCCTCCACCACCTCTCC
ATCCCAGGGAGCCACGACACGATGACGTACTGCCTGAACAAGAAGTCCCCCATTTCTCAC
GAGGAGTCCCGGCTGCTGCAGCTGCTGAACAAGGCCTTGCCCTGCATCACGCGCCCTGTC
GTGCTGAAATGGTCCGTCACCCAGGCACTGGACGTCACAGAGCAGCTGGATGCCGGGGTG
CGGTACCTGGACCTGCGGATAGCCCACATGCTGGAGGGCTCGGAGAAGAACCTGCACTTT
GTCCATATGGTGTACACAACGGCGCTGGTGGAGGACACACTCACGGAAATCTCGGAGTGG
CTGGAGCGGCATCCACGCGAGGTGGTCATCCTGGCCTGCAGAAACTTCGAGGGGCTGAGC
GAGGACCTGCACGAGTACCTGGTCGCCTGTATCAAGAACATCTTCGGGGACATGCTGTGT
CCTCGTGGGGAGGTGCCGACACTGCGGCAGCTGTGGTCCCGGGGCCAACAGGTCATCGTC
TCCTATGAAGACGAGAGCTCCTTGCGCCGGCACCACGAGCTGTGGCCAGGAGTCCCCTAC
TGGTGGGGAAACAGGGTGAAGACCGAGGCCCTCATCCGATACCTGGAGACCATGAAGAGC
TGCGGCCGCCCAGGAGGGTTGTTCGTGGCCGGCATCAACCTCACGGAGAACCTGCAGTAC
GTTCTGGCGCACCCGTCCGAGTCCCTGGAGAAGATGACGCTGCCCAACCTTCCGCGGCTG
AGCGCGTGGGTCCGAGAGCAGTGCCCGGGGCCGGGTTCACGGTGCACCAACATCATCGCG
GGGGACTTCATCGGCGCAGACGGCTTCGTCAGTGACGTCATCGCGCTCAATCAGAAGCTG
CTGTGGTGCTGA
Enzyme 72 GenBank Gene ID AK002185 Link Image
Enzyme 72 GeneCard ID PLCXD1 Link Image
Enzyme 72 GenAtlas ID PLCXD1 Link Image
Enzyme 72 HGNC ID HGNC:23148 Link Image
Enzyme 72 Chromosome Location Not Available
Enzyme 72 Locus Not Available
Enzyme 72 SNPs SNPJam Report Link Image
Enzyme 72 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]
  2. Skaletsky H, Kuroda-Kawaguchi T, Minx PJ, Cordum HS, Hillier L, Brown LG, Repping S, Pyntikova T, Ali J, Bieri T, Chinwalla A, Delehaunty A, Delehaunty K, Du H, Fewell G, Fulton L, Fulton R, Graves T, Hou SF, Latrielle P, Leonard S, Mardis E, Maupin R, McPherson J, Miner T, Nash W, Nguyen C, Ozersky P, Pepin K, Rock S, Rohlfing T, Scott K, Schultz B, Strong C, Tin-Wollam A, Yang SP, Waterston RH, Wilson RK, Rozen S, Page DC: The male-specific region of the human Y chromosome is a mosaic of discrete sequence classes. Nature. 2003 Jun 19;423(6942):825-37. [PubMed Link Image]
  3. 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]
  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 72 Metabolite References Not Available
Enzyme 73 [top]
Enzyme 73 ID 12963
Enzyme 73 Name PI-PLC X domain-containing protein 3
Enzyme 73 Synonyms Not Available
Enzyme 73 Gene Name PLCXD3
Enzyme 73 Protein Sequence >PI-PLC X domain-containing protein 3
MASSQGKNELKLADWMATLPESMHSIPLTNLAIPGSHDSFSFYIDEASPVGPEQPETVQN
FVSVFGTVAKKLMRKWLATQTMNFTGQLGAGIRYFDLRISTKPRDPDNELYFAHGLFSAK
VNEGLEEINAFLTDHHKEVVFLDFNHFYGMQKYHHEKLVQMLKDIYGNKMCPAIFAQEVS
LKYLWEKDYQVLVFYHSPVALEVPFLWPGQMMPAPWANTTDPEKLIQFLQASITERRKKG
SFFISQVVLTPKASTVVKGVASGLRETITERALPAMMQWVRTQKPGESGINIVTADFVEL
GDFISTVIKLNYVFDEGEANT
Enzyme 73 Number of Residues 321
Enzyme 73 Molecular Weight 36312.5
Enzyme 73 Theoretical pI 6.24
Enzyme 73 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • signaling
  • signaling pathway
Component
Enzyme 73 General Function Involved in phosphoric diester hydrolase activity
Enzyme 73 Specific Function Not Available
Enzyme 73 Pathways Not Available
Enzyme 73 Reactions Not Available
Enzyme 73 Pfam Domain Function
Enzyme 73 Signals
  • None
Enzyme 73 Transmembrane Regions
  • None
Enzyme 73 Essentiality Not Available
Enzyme 73 GenBank ID Protein 53828920 Link Image
Enzyme 73 UniProtKB/Swiss-Prot ID Q63HM9 Link Image
Enzyme 73 UniProtKB/Swiss-Prot Entry Name PLCX3_HUMAN Link Image
Enzyme 73 PDB ID Not Available
Enzyme 73 Cellular Location Not Available
Enzyme 73 Gene Sequence >966 bp
ATGGCCTCGTCTCAGGGGAAAAACGAGCTGAAATTAGCCGACTGGATGGCAACTCTGCCG
GAGAGCATGCACAGCATCCCCCTCACCAATTTAGCCATTCCAGGGTCTCATGATTCCTTC
AGCTTCTACATTGATGAAGCCTCTCCAGTAGGTCCTGAGCAGCCAGAAACTGTCCAGAAT
TTTGTCTCTGTGTTTGGAACTGTGGCCAAAAAGCTCATGCGGAAATGGTTAGCCACTCAG
ACAATGAATTTTACTGGCCAGCTAGGAGCTGGAATTCGTTATTTTGATCTTCGAATTTCC
ACCAAGCCCAGAGACCCCGACAATGAACTCTATTTTGCTCATGGTTTGTTCAGTGCCAAA
GTCAATGAAGGCCTTGAGGAGATCAATGCATTCCTCACAGATCACCATAAGGAGGTAGTG
TTCTTGGACTTCAACCACTTTTATGGGATGCAGAAATATCACCATGAAAAACTGGTCCAA
ATGCTGAAAGACATCTATGGAAATAAAATGTGCCCAGCGATTTTTGCCCAGGAAGTTAGT
TTAAAGTACCTGTGGGAGAAGGACTATCAAGTGCTGGTCTTCTACCATAGTCCAGTGGCT
CTGGAAGTGCCCTTTCTCTGGCCTGGGCAGATGATGCCAGCACCCTGGGCCAACACCACA
GACCCCGAGAAACTGATCCAGTTTCTTCAAGCATCCATCACTGAGAGAAGAAAGAAGGGA
TCGTTTTTTATATCTCAGGTGGTGCTGACCCCCAAAGCTAGCACTGTGGTCAAAGGGGTG
GCAAGTGGCCTCAGAGAAACAATCACAGAAAGAGCTCTTCCTGCCATGATGCAGTGGGTC
CGCACGCAGAAGCCAGGAGAGAGTGGCATCAATATTGTCACTGCCGATTTTGTAGAACTT
GGTGACTTTATCAGCACTGTCATAAAGCTCAACTATGTCTTTGATGAAGGAGAAGCCAAC
ACTTGA
Enzyme 73 GenBank Gene ID NM_001005473.2 Link Image
Enzyme 73 GeneCard ID PLCXD3 Link Image
Enzyme 73 GenAtlas ID PLCXD3 Link Image
Enzyme 73 HGNC ID HGNC:31822 Link Image
Enzyme 73 Chromosome Location 5
Enzyme 73 Locus 5p13.1
Enzyme 73 SNPs SNPJam Report Link Image
Enzyme 73 General References
  1. 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]
  2. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed Link Image]
Enzyme 73 Metabolite References Not Available
Enzyme 74 [top]
Enzyme 74 ID 12964
Enzyme 74 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase zeta-1
Enzyme 74 Synonyms
  1. Phosphoinositide phospholipase C-zeta-1
  2. Phospholipase C-zeta-1
  3. PLC-zeta-1
  4. Testis-development protein NYD-SP27
Enzyme 74 Gene Name PLCZ1
Enzyme 74 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase zeta-1
MEMRWFLSKIQDDFRGGKINLEKTQRLLEKLDIRCSYIHVKQIFKDNDRLKQGRITIEEF
RAIYRIITHREEIIEIFNTYSENRKILLASNLAQFLTQEQYAAEMSKAIAFEIIQKYEPI
EEVRKAHQMSLEGFTRYMDSRECLLFKNECRKVYQDMTHPLNDYFISSSHNTYLVSDQLL
GPSDLWGYVSALVKGCRCLEIDCWDGAQNEPVVYHGYTLTSKLLFKTVIQAIHKYAFMTS
DYPVVLSLENHCSTAQQEVMADNLQATFGESLLSDMLDDFPDTLPSPEALKFKILVKNKK
IGTLKETHERKGSDKRGDNQDKETGVKKLPGVMLFKKKKTRKLKIALALSDLVIYTKAEK
FKSFQHSRLYQQFNENNSIGETQARKLSKLRVHEFIFHTRKFITRIYPKATRADSSNFNP
QEFWNIGCQMVALNFQTPGLPMDLQNGKFLDNGGSGYILKPHFLRESKSYFNPSNIKEGM
PITLTIRLISGIQLPLTHSSSNKGDSLVIIEVFGVPNDQMKQQTRVIKKNAFSPRWNETF
TFIIHVPELALIRFVVEGQGLIAGNEFLGQYTLPLLCMNKGYRRIPLFSRMGESLEPASL
FVYVWYVR
Enzyme 74 Number of Residues 608
Enzyme 74 Molecular Weight 70410.7
Enzyme 74 Theoretical pI 9.43
Enzyme 74 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 74 General Function Involved in calcium ion binding
Enzyme 74 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)- dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg- activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function
Enzyme 74 Pathways Not Available
Enzyme 74 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 74 Pfam Domain Function
Enzyme 74 Signals
  • None
Enzyme 74 Transmembrane Regions
  • None
Enzyme 74 Essentiality Not Available
Enzyme 74 GenBank ID Protein 25053795 Link Image
Enzyme 74 UniProtKB/Swiss-Prot ID Q86YW0 Link Image
Enzyme 74 UniProtKB/Swiss-Prot Entry Name PLCZ1_HUMAN Link Image
Enzyme 74 PDB ID Not Available
Enzyme 74 Cellular Location Not Available
Enzyme 74 Gene Sequence >1827 bp
ATGGAAATGAGATGGTTTTTGTCAAAGATTCAGGATGACTTCAGAGGTGGAAAAATTAAC
CTAGAAAAAACTCAGAGGTTACTTGAAAAATTAGATATTCGGTGCAGTTATATTCATGTG
AAACAGATTTTTAAGGACAATGACAGGCTGAAACAAGGAAGAATCACCATAGAAGAATTT
AGAGCAATTTATCGAATTATCACGCACAGAGAAGAAATTATTGAGATTTTCAACACATAT
TCTGAAAACCGGAAAATTCTTTTAGCAAGTAATCTGGCTCAATTTCTGACACAAGAACAA
TATGCAGCTGAGATGAGTAAAGCTATTGCTTTTGAGATCATTCAGAAATACGAGCCTATC
GAAGAAGTTAGGAAAGCACACCAAATGTCATTAGAAGGTTTTACAAGATACATGGATTCA
CGTGAATGTCTACTGTTTAAAAATGAATGTAGAAAAGTTTATCAAGATATGACTCATCCA
TTAAATGATTATTTTATTTCATCTTCACATAACACATATTTGGTATCTGATCAATTATTG
GGACCAAGTGACCTTTGGGGATATGTAAGTGCCCTTGTGAAAGGATGCCGTTGTTTGGAG
ATTGACTGCTGGGATGGAGCACAAAATGAACCTGTTGTATATCATGGCTACACACTCACA
AGCAAACTTCTGTTTAAAACTGTTATCCAAGCTATACACAAGTATGCATTCATGACATCT
GACTACCCAGTGGTGCTCTCTTTAGAAAATCACTGCTCCACTGCCCAACAAGAAGTAATG
GCAGACAATTTGCAGGCTACTTTTGGAGAGTCCTTGCTTTCTGATATGCTTGATGATTTT
CCTGATACTCTACCATCACCAGAGGCACTAAAATTCAAAATATTAGTTAAAAATAAGAAA
ATAGGAACCTTAAAGGAAACCCATGAAAGAAAAGGTTCTGATAAGCGTGGAGACAATCAA
GACAAGGAAACAGGGGTAAAAAAGTTACCTGGAGTAATGCTTTTCAAGAAAAAGAAGACC
AGGAAGCTAAAAATTGCTCTGGCCTTATCTGATCTTGTCATTTATACGAAAGCTGAGAAA
TTCAAAAGCTTTCAACATTCAAGATTATATCAGCAATTTAATGAAAATAATTCTATTGGG
GAGACACAAGCCCGAAAACTTTCAAAATTGCGAGTCCATGAGTTTATTTTTCACACCAGG
AAGTTCATTACCAGAATATATCCCAAAGCAACAAGAGCAGACTCTTCTAATTTTAATCCC
CAAGAATTTTGGAATATAGGTTGTCAAATGGTGGCTTTAAATTTCCAGACCCCTGGTCTG
CCCATGGATCTGCAAAATGGGAAATTTTTGGATAATGGTGGTTCTGGATATATTTTGAAA
CCACATTTCTTAAGAGAGAGTAAATCATACTTTAACCCAAGTAACATAAAAGAGGGTATG
CCAATTACACTTACAATAAGGCTCATCAGTGGTATCCAGTTGCCTCTTACTCATTCATCA
TCTAACAAAGGTGATTCATTAGTAATTATAGAAGTTTTTGGTGTTCCAAATGATCAAATG
AAGCAGCAGACTCGTGTAATTAAAAAAAATGCTTTTAGTCCAAGATGGAATGAAACATTC
ACATTTATTATTCATGTCCCAGAATTGGCATTGATACGTTTTGTTGTTGAAGGTCAAGGT
TTAATAGCAGGAAATGAATTTCTTGGGCAATATACTTTGCCACTTCTATGCATGAACAAA
GGTTATCGTCGTATTCCTCTGTTTTCCAGAATGGGTGAGAGCCTTGAGCCTGCTTCACTG
TTTGTTTATGTTTGGTACGTCAGATAA
Enzyme 74 GenBank Gene ID AF532185 Link Image
Enzyme 74 GeneCard ID PLCZ1 Link Image
Enzyme 74 GenAtlas ID PLCZ1 Link Image
Enzyme 74 HGNC ID HGNC:19218 Link Image
Enzyme 74 Chromosome Location 1
Enzyme 74 Locus 12p12.3
Enzyme 74 SNPs SNPJam Report Link Image
Enzyme 74 General References
  1. Cox LJ, Larman MG, Saunders CM, Hashimoto K, Swann K, Lai FA: Sperm phospholipase Czeta from humans and cynomolgus monkeys triggers Ca2+ oscillations, activation and development of mouse oocytes. Reproduction. 2002 Nov;124(5):611-23. [PubMed Link Image]
  2. Zhu H, Zhu JX, Lo PS, Li J, Leung KM, Rowlands DK, Tsang LL, Yu MK, Jiang JL, Lam SY, Chung YW, Zhou Z, Sha J, Chang Chan H: Rescue of defective pancreatic secretion in cystic-fibrosis cells by suppression of a novel isoform of phospholipase C. Lancet. 2003 Dec 20;362(9401):2059-65. [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. Rogers NT, Hobson E, Pickering S, Lai FA, Braude P, Swann K: Phospholipase Czeta causes Ca2+ oscillations and parthenogenetic activation of human oocytes. Reproduction. 2004 Dec;128(6):697-702. [PubMed Link Image]
Enzyme 74 Metabolite References Not Available
Enzyme 75 [top]
Enzyme 75 ID 12965
Enzyme 75 Name Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
Enzyme 75 Synonyms
  1. P-Rex1
  2. PtdIns(3,4,5)-dependent Rac exchanger 1
Enzyme 75 Gene Name PREX1
Enzyme 75 Protein Sequence >Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
MEAPSGSEPGGDGAGDCAHPDPRAPGAAAPSSGPGPCAAARESERQLRLRLCVLNEILGT
ERDYVGTLRFLQSAFLHRIRQNVADSVEKGLTEENVKVLFSNIEDILEVHKDFLAALEYC
LHPEPQSQHELGNVFLKFKDKFCVYEEYCSNHEKALRLLVELNKIPTVRAFLLSCMLLGG
RKTTDIPLEGYLLSPIQRICKYPLLLKELAKRTPGKHPDHPAVQSALQAMKTVCSNINET
KRQMEKLEALEQLQSHIEGWEGSNLTDICTQLLLQGTLLKISAGNIQERAFFLFDNLLVY
CKRKSRVTGSKKSTKRTKSINGSLYIFRGRINTEVMEVENVEDGTADYHSNGYTVTNGWK
IHNTAKNKWFVCMAKTAEEKQKWLDAIIREREQRESLKLGMERDAYVMIAEKGEKLYHMM
MNKKVNLIKDRRRKLSTVPKCFLGNEFVAWLLEIGEISKTEEGVNLGQALLENGIIHHVS
DKHQFKNEQVMYRFRYDDGTYKARSELEDIMSKGVRLYCRLHSLYTPVIKDRDYHLKTYK
SVLPGSKLVDWLLAQGDCQTREEAVALGVGLCNNGFMHHVLEKSEFRDESQYFRFHADEE
MEGTSSKNKQLRNDFKLVENILAKRLLILPQEEDYGFDIEEKNKAVVVKSVQRGSLAEVA
GLQVGRKIYSINEDLVFLRPFSEVESILNQSFCSRRPLRLLVATKAKEIIKIPDQPDTLC
FQIRGAAPPYVYAVGRGSEAMAAGLCAGQCILKVNGSNVMNDGAPEVLEHFQAFRSRREE
ALGLYQWIYHTHEDAQEARASQEASTEDPSGEQAQEEDQADSAFPLLSLGPRLSLCEDSP
MVTLTVDNVHLEHGVVYEYVSTAGVRCHVLEKIVEPRGCFGLTAKILEAFAANDSVFVEN
CRRLMALSSAIVTMPHFEFRNICDTKLESIGQRIACYQEFAAQLKSRVSPPFKQAPLEPH
PLCGLDFCPTNCHINLMEVSYPKTTPSVGRSFSIRFGRKPSLIGLDPEQGHLNPMSYTQH
CITTMAAPSWKCLPAAEGDPQGQGLHDGSFGPASGTLGQEDRGLSFLLKQEDREIQDAYL
QLFTKLDVALKEMKQYVTQINRLLSTITEPTSGGSCDASLAEEASSLPLVSEESEMDRSD
HGGIKKVCFKVAEEDQEDSGHDTMSYRDSYSECNSNRDSVLSYTSVRSNSSYLGSDEMGS
GDELPCDMRIPSDKQDKLHGCLEHLFNQVDSINALLKGPVMSRAFEETKHFPMNHSLQEF
KQKEECTIRGRSLIQISIQEDPWNLPNSIKTLVDNIQRYVEDGKNQLLLALLKCTDTELQ
LRRDAIFCQALVAAVCTFSKQLLAALGYRYNNNGEYEESSRDASRKWLEQVAATGVLLHC
QSLLSPATVKEERTMLEDIWVTLSELDNVTFSFKQLDENYVANTNVFYHIEGSRQALKVI
FYLDSYHFSKLPSRLEGGASLRLHTALFTKVLENVEGLPSPGSQAAEDLQQDINAQSLEK
VQQYYRKLRAFYLERSNLPTDASTTAVKIDQLIRPINALDELCRLMKSFVHPKPGAAGSV
GAGLIPISSELCYRLGACQMVMCGTGMQRSTLSVSLEQAAILARSHGLLPKCIMQATDIM
RKQGPRVEILAKNLRVKDQMPQGAPRLYRLCQPPVDGDL
Enzyme 75 Number of Residues 1659
Enzyme 75 Molecular Weight 186201.7
Enzyme 75 Theoretical pI 6.40
Enzyme 75 GO Classification
Function
  • GTPase regulator activity
  • Ras guanyl-nucleotide exchange factor activity
  • Rho guanyl-nucleotide exchange factor activity
  • binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • protein binding
  • small GTPase regulator activity
Process
  • biological regulation
  • intracellular signaling pathway
  • regulation of Ras protein signal transduction
  • regulation of Rho protein signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
Enzyme 75 General Function Involved in intracellular signaling pathway
Enzyme 75 Specific Function Functions as a RAC guanine nucleotide exchange factor (GEF), which activates the Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol-3,4,5-triphosphate and the beta gamma subunits of heterotrimeric G protein. May function downstream of heterotrimeric G proteins in neutrophils
Enzyme 75 Pathways Not Available
Enzyme 75 Reactions Not Available
Enzyme 75 Pfam Domain Function
Enzyme 75 Signals
  • None
Enzyme 75 Transmembrane Regions
  • None
Enzyme 75 Essentiality Not Available
Enzyme 75 GenBank ID Protein 34452732 Link Image
Enzyme 75 UniProtKB/Swiss-Prot ID Q8TCU6 Link Image
Enzyme 75 UniProtKB/Swiss-Prot Entry Name PREX1_HUMAN Link Image
Enzyme 75 PDB ID Not Available
Enzyme 75 Cellular Location Not Available
Enzyme 75 Gene Sequence >4980 bp
ATGGAGGCGCCCAGCGGCAGCGAGCCCGGCGGCGACGGGGCCGGGGACTGCGCCCACCCG
GACCCCCGGGCCCCTGGCGCCGCGGCGCCCAGCTCCGGCCCCGGCCCGTGCGCGGCCGCC
CGGGAGTCCGAGCGCCAGCTGCGCCTCCGCCTCTGCGTCCTCAACGAGATCTTGGGCACC
GAGAGGGACTACGTGGGCACCTTGCGCTTCTTGCAGTCGGCATTCCTGCATCGCATCCGG
CAGAACGTGGCCGACTCAGTGGAGAAGGGCCTCACGGAGGAGAATGTCAAGGTCCTGTTC
TCGAACATCGAAGACATCCTGGAAGTTCATAAGGATTTCTTGGCCGCCTTGGAGTATTGT
TTACACCCGGAGCCGCAGTCTCAGCATGAACTTGGGAATGTTTTCTTAAAATTCAAGGAC
AAGTTCTGCGTGTACGAGGAGTATTGCAGCAACCATGAGAAAGCCCTGAGGCTGCTGGTG
GAGCTGAACAAGATCCCTACCGTGCGCGCCTTCCTTTTGAGCTGCATGCTTCTGGGAGGC
CGGAAGACCACGGACATCCCTTTGGAAGGCTACCTGTTGTCTCCGATCCAGAGGATCTGC
AAGTACCCGCTCCTCCTTAAGGAGCTGGCCAAGAGGACTCCCGGCAAGCACCCAGACCAC
CCCGCGGTCCAGAGTGCCCTGCAGGCCATGAAGACCGTTTGCTCCAACATCAATGAGACC
AAGCGGCAGATGGAGAAGCTGGAAGCCCTGGAGCAGCTGCAGTCCCACATCGAAGGCTGG
GAGGGTTCCAACCTCACAGACATCTGCACTCAGCTCCTCCTGCAAGGGACTTTGTTAAAG
ATCTCTGCGGGCAACATCCAGGAAAGGGCCTTCTTCCTCTTCGACAACCTTCTCGTCTAC
TGCAAGCGGAAATCCAGGGTCACCGGGAGCAAGAAGTCCACCAAGAGGACCAAATCCATC
AACGGCTCCCTCTACATCTTCAGGGGTCGAATCAACACTGAAGTCATGGAGGTGGAGAAT
GTGGAAGATGGGACAGCGGATTACCATAGCAACGGCTATACCGTCACCAACGGCTGGAAG
ATCCACAACACGGCCAAGAATAAGTGGTTTGTCTGCATGGCCAAGACGGCAGAGGAGAAG
CAGAAGTGGCTGGATGCCATCATCCGCGAGCGGGAGCAGCGCGAGAGCCTGAAGCTGGGC
ATGGAGCGTGATGCCTACGTCATGATTGCGGAGAAGGGGGAGAAGCTGTACCACATGATG
ATGAACAAGAAGGTGAACCTCATCAAGGACCGCCGGAGAAAGCTGAGCACTGTCCCCAAG
TGCTTTCTTGGCAATGAGTTCGTTGCCTGGCTCCTAGAAATTGGTGAAATCAGCAAGACG
GAAGAAGGAGTCAACTTGGGCCAAGCCCTGTTGGAGAATGGCATCATCCACCATGTTTCC
GACAAGCACCAGTTCAAGAATGAGCAGGTGATGTATCGCTTCCGCTACGACGATGGCACC
TACAAGGCCCGAAGTGAGCTGGAGGACATCATGTCCAAGGGTGTGAGGCTTTACTGCCGT
CTTCACAGCCTCTACACCCCGGTGATCAAAGACCGTGATTACCACCTGAAGACCTACAAG
TCAGTGCTTCCCGGGAGCAAGCTGGTGGACTGGCTGCTGGCTCAGGGAGACTGCCAGACT
CGGGAGGAGGCAGTGGCGCTCGGCGTGGGTCTGTGCAACAATGGCTTCATGCACCACGTG
CTGGAGAAGAGCGAGTTCAGGGATGAGTCCCAGTACTTCCGCTTTCATGCTGACGAGGAG
ATGGAGGGGACCAGCAGCAAGAACAAACAGCTTCGCAACGACTTCAAGCTGGTGGAGAAC
ATTCTGGCCAAGCGCCTGCTGATCCTGCCCCAGGAGGAGGACTATGGCTTTGACATCGAG
GAGAAGAACAAGGCTGTGGTGGTGAAGTCCGTCCAGAGGGGCTCGCTGGCTGAGGTGGCT
GGCCTGCAGGTGGGGAGGAAGATCTACTCCATCAATGAGGACCTGGTGTTCCTGCGGCCG
TTTTCAGAGGTGGAGTCCATCCTCAACCAGTCCTTCTGCTCCCGCCGCCCTCTGCGCCTC
CTGGTGGCCACGAAGGCCAAAGAGATCATCAAAATCCCCGACCAGCCGGACACACTGTGC
TTCCAGATTCGTGGAGCTGCCCCACCGTACGTCTATGCTGTGGGGAGAGGCTCTGAGGCC
ATGGCTGCAGGGCTCTGTGCTGGTCAGTGCATTCTGAAGGTCAATGGCAGCAACGTGATG
AACGATGGTGCCCCTGAGGTCCTGGAGCACTTCCAGGCATTCCGGAGTCGGCGCGAAGAG
GCCCTGGGCCTGTACCAGTGGATCTACCACACCCATGAGGATGCCCAGGAAGCACGAGCC
AGTCAGGAGGCCTCCACTGAGGACCCCAGTGGCGAGCAGGCCCAGGAGGAAGACCAGGCT
GATTCAGCCTTCCCACTGCTGTCCCTGGGTCCCCGGCTGAGCCTGTGTGAGGACAGCCCC
ATGGTCACCCTGACTGTGGACAACGTGCACCTGGAACACGGCGTGGTGTATGAGTATGTG
AGCACGGCAGGCGTCAGGTGCCATGTGCTGGAGAAGATCGTGGAGCCCCGCGGCTGCTTC
GGCCTCACCGCCAAGATCCTCGAGGCCTTTGCTGCCAATGACAGCGTCTTCGTGGAGAAC
TGCAGGCGGCTCATGGCCCTGAGCAGCGCCATCGTGACCATGCCCCACTTTGAGTTCCGC
AACATCTGTGACACCAAGCTGGAGAGCATTGGCCAGAGGATTGCCTGCTACCAGGAGTTT
GCAGCCCAACTGAAGAGCAGGGTCAGCCCACCCTTCAAACAAGCCCCCCTGGAGCCCCAC
CCGCTGTGTGGCCTGGACTTCTGCCCCACCAATTGCCACATCAACCTCATGGAAGTGTCC
TACCCCAAGACCACCCCCTCAGTGGGCAGGTCCTTCAGCATCCGCTTTGGACGCAAACCC
TCCCTCATCGGCCTTGACCCGGAGCAAGGCCACCTGAACCCCATGTCGTACACCCAGCAC
TGCATCACCACCATGGCTGCTCCCTCCTGGAAGTGCTTGCCTGCTGCAGAGGGTGATCCC
CAAGGCCAGGGTCTCCATGATGGCAGCTTCGGGCCAGCCAGTGGGACCCTTGGTCAGGAA
GACCGGGGCCTCAGCTTCCTACTCAAGCAGGAGGACCGTGAGATCCAGGATGCCTACCTG
CAGCTCTTCACCAAGCTGGATGTGGCCCTGAAGGAGATGAAGCAATATGTCACCCAGATC
AACAGGCTGCTGTCCACCATCACAGAGCCCACCTCGGGTGGGTCCTGCGACGCATCCTTG
GCTGAGGAGGCCTCCTCCCTGCCCCTGGTCAGTGAAGAGAGCGAGATGGACAGGAGTGAC
CATGGGGGCATCAAGAAGGTGTGCTTCAAGGTGGCCGAGGAGGACCAGGAGGACTCAGGC
CACGACACCATGAGTTATCGCGACTCCTACAGCGAGTGTAACAGCAATCGAGACTCGGTC
CTGTCCTACACCAGCGTGAGAAGTAACAGCTCCTACTTGGGCAGCGACGAGATGGGGTCT
GGAGATGAGCTGCCCTGTGACATGCGGATCCCATCTGACAAGCAGGACAAGCTTCATGGC
TGCCTGGAGCACCTCTTTAACCAGGTGGACTCCATCAATGCTCTCCTCAAGGGGCCAGTC
ATGAGCCGGGCTTTCGAAGAGACCAAGCATTTCCCTATGAACCACAGCTTACAAGAGTTT
AAACAGAAAGAAGAGTGTACAATCCGTGGCCGGAGCCTGATCCAGATTAGCATCCAGGAG
GACCCCTGGAACCTCCCCAACTCCATCAAGACCCTGGTGGACAACATTCAGAGATATGTG
GAAGATGGGAAGAACCAGCTGCTCCTGGCCTTGCTGAAGTGCACAGACACGGAGCTGCAG
CTGCGCAGAGACGCGATCTTCTGCCAGGCCCTGGTGGCCGCCGTGTGCACCTTCTCCGAG
CAGCTGCTGGCGGCCCTGGGCTACCGCTACAACAACAATGGCGAGTACGAGGAGAGCAGC
CGCGACGCCAGCCGCAAGTGGCTGGAGCAGGTGGCGGCCACGGGCGTCCTGCTGCACTGC
CAGTCCCTGCTCTCGCCAGCCACAGTGAAGGAGGAACGGACCATGCTGGAGGACATCTGG
GTGACGCTGTCAGAGCTGGACAATGTCACCTTCTCCTTTAAGCAGCTGGACGAGAACTAT
GTGGCCAACACCAACGTCTTCTACCACATTGAGGGCAGCCGGCAGGCGCTGAAGGTCATC
TTCTACCTCGACAGCTACCACTTCTCCAAGCTGCCCTCCCGCCTGGAGGGTGGGGCCAGC
CTGAGGCTGCACACAGCGCTGTTCACGAAAGTGCTGGAGAACGTGGAGGGGCTGCCTTCT
CCAGGCAGCCAGGCCGCGGAGGATTTGCAGCAGGACATCAACGCGCAGTCCCTGGAGAAA
GTTCAGCAGTATTACCGCAAACTCAGGGCATTTTACCTGGAGCGGTCTAACCTGCCCACG
GATGCCAGCACCACGGCGGTAAAGATAGACCAGCTGATCCGCCCCATCAATGCCCTGGAT
GAGCTCTGCCGCCTCATGAAGTCCTTTGTCCACCCAAAGCCTGGTGCTGCTGGGAGTGTG
GGCGCCGGCCTCATCCCCATCTCCTCGGAGCTCTGCTACCGCCTGGGGGCCTGCCAGATG
GTCATGTGTGGCACAGGCATGCAGAGGAGCACCCTGAGCGTGTCCCTGGAGCAGGCGGCC
ATCTTGGCACGGAGCCACGGGTTGCTGCCCAAGTGCATCATGCAGGCCACGGACATCATG
CGGAAGCAGGGCCCAAGGGTGGAGATTCTGGCCAAAAACCTGCGAGTCAAGGACCAGATG
CCCCAGGGTGCTCCGCGCCTCTACCGCCTCTGCCAGCCGCCGGTGGATGGGGACCTCTGA
Enzyme 75 GenBank Gene ID NM_020820.3 Link Image
Enzyme 75 GeneCard ID PREX1 Link Image
Enzyme 75 GenAtlas ID PREX1 Link Image
Enzyme 75 HGNC ID HGNC:32594 Link Image
Enzyme 75 Chromosome Location 2
Enzyme 75 Locus 20q13.13
Enzyme 75 SNPs SNPJam Report Link Image
Enzyme 75 General References
  1. Welch HC, Coadwell WJ, Ellson CD, Ferguson GJ, Andrews SR, Erdjument-Bromage H, Tempst P, Hawkins PT, Stephens LR: P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac. Cell. 2002 Mar 22;108(6):809-21. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  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. Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [PubMed Link Image]
  5. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  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. 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]
  8. 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 75 Metabolite References Not Available
Enzyme 76 [top]
Enzyme 76 ID 12966
Enzyme 76 Name Transmembrane protein 55A
Enzyme 76 Synonyms
  1. PtdIns-4,5-P2 4-Ptase II
  2. Type II phosphatidylinositol 4,5-bisphosphate 4-phosphatase
Enzyme 76 Gene Name TMEM55A
Enzyme 76 Protein Sequence >Transmembrane protein 55A
MAADGVDERSPLLSASHSGNVTPTAPPYLQESSPRAELPPPYTAIASPDASGIPVINCRV
CQSLINLDGKLHQHVVKCTVCNEATPIKNPPTGKKYVRCPCNCLLICKDTSRRIGCPRPN
CRRIINLGPVMLISEEQPAQPALPIQPEGTRVVCGHCGNTFLWMELRFNTLAKCPHCKKI
SSVGSALPRRRCCAYITIGMICIFIGVGLTVGTPDFARRFRATYVSWAIAYLLGLICLIR
ACYWGAIRVSYPEHSFA
Enzyme 76 Number of Residues 257
Enzyme 76 Molecular Weight 28080.6
Enzyme 76 Theoretical pI 8.74
Enzyme 76 GO Classification Not Available
Enzyme 76 General Function Involved in hydrolase activity
Enzyme 76 Specific Function Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 4,5-bisphosphate. Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4- bisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3- monophosphate
Enzyme 76 Pathways Not Available
Enzyme 76 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate [RN:R08981]
Enzyme 76 Pfam Domain Function
Enzyme 76 Signals
  • None
Enzyme 76 Transmembrane Regions
  • 192-212 227-247
Enzyme 76 Essentiality Not Available
Enzyme 76 GenBank ID Protein 189054014 Link Image
Enzyme 76 UniProtKB/Swiss-Prot ID Q8N4L2 Link Image
Enzyme 76 UniProtKB/Swiss-Prot Entry Name TM55A_HUMAN Link Image
Enzyme 76 PDB ID Not Available
Enzyme 76 Cellular Location Not Available
Enzyme 76 Gene Sequence >774 bp
ATGGCTGCTGATGGGGTGGACGAACGCTCGCCTCTGCTGTCAGCATCCCACTCCGGAAAT
GTCACTCCCACCGCCCCACCGTACTTGCAAGAAAGCAGCCCCAGAGCGGAGCTCCCACCT
CCATATACAGCCATTGCCAGTCCAGACGCCAGTGGTATTCCAGTAATAAACTGCCGTGTG
TGCCAATCACTAATCAATTTGGATGGCAAGCTTCACCAGCATGTGGTTAAGTGCACAGTT
TGCAATGAAGCTACGCCAATCAAAAACCCCCCAACAGGCAAGAAATATGTTAGATGCCCT
TGTAATTGTCTTCTCATTTGTAAGGACACATCTCGGCGAATAGGATGCCCAAGACCCAAC
TGTAGACGGATAATTAACCTTGGCCCAGTAATGCTTATTTCTGAAGAACAACCAGCTCAG
CCTGCATTGCCAATCCAACCAGAAGGTACAAGGGTCGTGTGTGGGCACTGTGGAAACACA
TTCCTGTGGATGGAACTGAGGTTCAACACTCTGGCAAAATGCCCACACTGCAAAAAAATC
TCCTCAGTGGGTAGTGCACTTCCACGAAGACGCTGCTGTGCATATATTACCATTGGAATG
ATATGTATTTTCATTGGAGTTGGGTTAACTGTTGGCACCCCAGATTTTGCAAGGCGATTT
CGAGCAACCTATGTTTCTTGGGCAATTGCTTATCTCCTAGGATTGATCTGCCTTATCCGA
GCTTGTTATTGGGGAGCCATAAGAGTCAGTTATCCAGAACACAGTTTTGCATAA
Enzyme 76 GenBank Gene ID AK313783 Link Image
Enzyme 76 GeneCard ID TMEM55A Link Image
Enzyme 76 GenAtlas ID TMEM55A Link Image
Enzyme 76 HGNC ID HGNC:25452 Link Image
Enzyme 76 Chromosome Location 8
Enzyme 76 Locus 8q21.3
Enzyme 76 SNPs SNPJam Report Link Image
Enzyme 76 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]
  2. 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]
  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. Ungewickell A, Hugge C, Kisseleva M, Chang SC, Zou J, Feng Y, Galyov EE, Wilson M, Majerus PW: The identification and characterization of two phosphatidylinositol-4,5-bisphosphate 4-phosphatases. Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18854-9. Epub 2005 Dec 19. [PubMed Link Image]
Enzyme 76 Metabolite References Not Available
Enzyme 77 [top]
Enzyme 77 ID 12967
Enzyme 77 Name Transmembrane protein 55B
Enzyme 77 Synonyms
  1. PtdIns-4,5-P2 4-Ptase I
  2. Type I phosphatidylinositol 4,5-bisphosphate 4-phosphatase
Enzyme 77 Gene Name TMEM55B
Enzyme 77 Protein Sequence >Transmembrane protein 55B
MAADGERSPLLSEPIDGGAGGNGLVGPGGSGAGPGGGLTPSAPPYGAAFPPFPEGHPAVL
PGEDPPPYSPLTSPDSGSAPMITCRVCQSLINVEGKMHQHVVKCGVCNEATPIKNAPPGK
KYVRCPCNCLLICKVTSQRIACPRPYCKRIINLGPVHPGPLSPEPQPMGVRVICGHCKNT
FLWTEFTDRTLARCPHCRKVSSIGRRYPRKRCICCFLLGLLLAVTATGLAFGTWKHARRY
GGIYAAWAFVILLAVLCLGRALYWACMKVSHPVQNFS
Enzyme 77 Number of Residues 277
Enzyme 77 Molecular Weight 29469.3
Enzyme 77 Theoretical pI 9.01
Enzyme 77 GO Classification Not Available
Enzyme 77 General Function Involved in hydrolase activity
Enzyme 77 Specific Function Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 4,5-bisphosphate. Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4- bisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3- monophosphate
Enzyme 77 Pathways Not Available
Enzyme 77 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate [RN:R08981]
Enzyme 77 Pfam Domain Function
Enzyme 77 Signals
  • None
Enzyme 77 Transmembrane Regions
  • 212-232 242-262
Enzyme 77 Essentiality Not Available
Enzyme 77 GenBank ID Protein 189054212 Link Image
Enzyme 77 UniProtKB/Swiss-Prot ID Q86T03 Link Image
Enzyme 77 UniProtKB/Swiss-Prot Entry Name TM55B_HUMAN Link Image
Enzyme 77 PDB ID Not Available
Enzyme 77 Cellular Location Not Available
Enzyme 77 Gene Sequence >834 bp
ATGGCGGCAGATGGAGAGCGTTCCCCGCTGCTGTCTGAGCCCATCGACGGTGGCGCGGGC
GGCAACGGTTTAGTGGGGCCCGGCGGGAGTGGGGCTGGGCCCGGGGGAGGCCTGACCCCC
TCCGCACCACCGTACGGAGCCGCATTTCCCCCGTTTCCCGAGGGGCATCCAGCCGTGTTG
CCTGGGGAGGACCCACCCCCCTATTCACCCTTAACTAGCCCGGACAGTGGGAGTGCCCCT
ATGATCACCTGCCGAGTCTGCCAATCTCTCATCAACGTGGAAGGCAAGATGCATCAGCAT
GTAGTCAAATGTGGTGTCTGCAATGAAGCCACCCCAATCAAGAATGCACCCCCAGGGAAA
AAATATGTTCGATGCCCCTGTAACTGTCTCCTTATCTGCAAAGTGACATCCCAACGGATT
GCATGCCCTCGGCCCTACTGCAAAAGAATCATCAACCTGGGGCCTGTGCATCCCGGACCT
CTGAGTCCAGAACCCCAACCCATGGGTGTCAGGGTTATCTGTGGACATTGCAAGAATACT
TTTCTGTGGACAGAGTTCACAGACCGCACTTTGGCACGTTGTCCTCACTGCAGGAAAGTG
TCATCTATTGGGCGCAGATACCCACGTAAGAGATGTATCTGCTGCTTCTTGCTTGGCTTG
CTTTTGGCAGTCACTGCCACTGGCCTTGCCTTTGGCACATGGAAGCATGCACGGCGATAT
GGAGGCATCTATGCAGCCTGGGCATTTGTCATCCTGTTGGCTGTGCTGTGTTTGGGCCGG
GCTCTTTATTGGGCCTGTATGAAGGTCAGCCACCCTGTCCAGAACTTCTCCTGA
Enzyme 77 GenBank Gene ID AK314021 Link Image
Enzyme 77 GeneCard ID TMEM55B Link Image
Enzyme 77 GenAtlas ID TMEM55B Link Image
Enzyme 77 HGNC ID HGNC:19299 Link Image
Enzyme 77 Chromosome Location 1
Enzyme 77 Locus 14q11.2
Enzyme 77 SNPs SNPJam Report Link Image
Enzyme 77 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]
  2. 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]
  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. Ungewickell A, Hugge C, Kisseleva M, Chang SC, Zou J, Feng Y, Galyov EE, Wilson M, Majerus PW: The identification and characterization of two phosphatidylinositol-4,5-bisphosphate 4-phosphatases. Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18854-9. Epub 2005 Dec 19. [PubMed Link Image]
  5. 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 77 Metabolite References Not Available
Enzyme 78 [top]
Enzyme 78 ID 12968
Enzyme 78 Name Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase TPTE2
Enzyme 78 Synonyms
  1. Lipid phosphatase TPIP
  2. TPTE and PTEN homologous inositol lipid phosphatase
Enzyme 78 Gene Name TPTE2
Enzyme 78 Protein Sequence >Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase TPTE2
MNESPQTNEFKGTTEEAPAKESPHTSEFKGAALVSPISKSMLERLSKFEVEDAENVASYD
SKIKKIVHSIVSSFAFGIFGVFLVLLDVTLLLADLIFTDSKLYIPLEYRSISLAIGLFFL
MDVLLRVFVEGRQQYFSDLFNILDTAIIVIPLLVDVIYIFFDIKLLRNIPRWTHLVRLLR
LIILIRIFHLLHQKRQLEKLMRRLVSENKRRYTRDGFDLDLTYVTERIIAMSFPSSGRQS
FYRNPIEEVVRFLDKKHRNHYRVYNLCSERAYDPKHFHNRVSRIMIDDHNVPTLHEMVVF
TKEVNEWMAQDLENIVAIHCKGGKGRTGTMVCALLIASEIFLTAEESLYYFGERRTNKTH
SNKFQGVETPSQNRYVGYFAQVKHLYNWNLPPRRILFIKRFIIYSIRGDVCDLKVQVVME
KKVVFSSTSLGNCSILHDIETDKILINVYDGPPLYDDVKVQFFSSNLPKYYDNCPFFFWF
NTSFIQNNRLCLPRNELDNPHKQKAWKIYPPEFAVEILFGEK
Enzyme 78 Number of Residues 522
Enzyme 78 Molecular Weight 61111.3
Enzyme 78 Theoretical pI 8.86
Enzyme 78 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion channel activity
  • ion transmembrane transporter activity
  • phosphatase activity
  • phosphoprotein phosphatase activity
  • phosphoric ester hydrolase activity
  • protein tyrosine phosphatase activity
  • protein tyrosine/serine/threonine phosphatase activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • cellular metabolic process
  • dephosphorylation
  • establishment of localization
  • ion transport
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • protein amino acid dephosphorylation
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
Enzyme 78 General Function Involved in protein tyrosine/serine/threonine phosphatase activity
Enzyme 78 Specific Function Phosphatidylinositol 3,4,5-trisphosphate + H(2)O = phosphatidylinositol 4,5-bisphosphate + phosphate
Enzyme 78 Pathways
Enzyme 78 Reactions
  • phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate [RN:R04513]
Enzyme 78 Pfam Domain Function
Enzyme 78 Signals
  • None
Enzyme 78 Transmembrane Regions
  • 66-86 111-131 146-166
Enzyme 78 Essentiality Not Available
Enzyme 78 GenBank ID Protein 213972591 Link Image
Enzyme 78 UniProtKB/Swiss-Prot ID Q6XPS3 Link Image
Enzyme 78 UniProtKB/Swiss-Prot Entry Name TPTE2_HUMAN Link Image
Enzyme 78 PDB ID Not Available
Enzyme 78 Cellular Location Not Available
Enzyme 78 Gene Sequence >1569 bp
ATGAATGAAAGTCCACAGACAAACGAATTTAAAGGAACAACCGAGGAGGCACCTGCGAAA
GAAAGCCCACACACAAGTGAATTTAAAGGAGCAGCCCTGGTGTCACCTATCAGTAAAAGT
ATGTTAGAACGACTTTCCAAGTTTGAAGTTGAAGATGCTGAAAATGTTGCTTCATATGAC
AGCAAGATTAAGAAAATTGTGCATTCAATTGTATCATCCTTTGCATTTGGAATATTTGGA
GTTTTCCTGGTCTTACTGGATGTCACTCTCCTCCTTGCCGACCTAATTTTCACTGACAGC
AAACTTTATATTCCTTTGGAGTATCGTTCTATTTCTCTAGCTATTGGCTTATTTTTTCTC
ATGGATGTTCTTCTTCGAGTATTTGTAGAAGGGAGACAGCAGTATTTTTCTGACTTATTT
AACATTTTAGATACTGCCATTATTGTGATTCCTCTGCTGGTTGATGTCATTTACATTTTT
TTTGACATTAAGTTGCTTAGGAATATTCCCAGATGGACACATTTAGTTCGACTTCTACGA
CTTATTATTCTGATAAGAATTTTTCATCTGCTTCATCAAAAAAGACAACTTGAAAAGCTG
ATGAGAAGGCTGGTTTCAGAAAACAAAAGGCGATACACAAGGGATGGATTTGACCTAGAC
CTCACTTACGTTACAGAACGTATTATTGCTATGTCATTTCCATCTTCTGGAAGGCAGTCT
TTCTATAGAAATCCAATTGAGGAAGTTGTGCGGTTTCTAGATAAGAAACATCGAAACCAC
TATCGAGTCTACAATCTATGCAGTGAAAGAGCTTATGATCCTAAGCACTTCCATAATAGG
GTCAGTAGAATCATGATTGATGATCATAATGTCCCCACTCTACATGAGATGGTGGTTTTC
ACCAAGGAAGTAAATGAGTGGATGGCTCAAGATCTTGAAAACATCGTAGCGATTCACTGT
AAAGGAGGCAAAGGAAGAACCGGGACTATGGTTTGTGCCCTCCTTATTGCCTCCGAAATA
TTTTTAACTGCCGAGGAAAGCCTATATTATTTTGGAGAAAGGCGAACCAATAAAACCCAC
AGCAATAAATTTCAGGGAGTAGAAACTCCTTCTCAGAATAGATATGTTGGATATTTTGCA
CAAGTGAAACATCTCTACAACTGGAATCTCCCTCCAAGACGGATACTCTTTATAAAAAGA
TTCATTATTTATTCGATTCGTGGTGATGTATGTGATCTAAAAGTCCAAGTAGTAATGGAG
AAAAAGGTTGTCTTTTCCAGTACTTCATTAGGAAATTGTTCGATATTGCATGACATTGAA
ACAGACAAAATATTAATTAATGTATATGACGGTCCACCTCTGTATGATGATGTGAAAGTG
CAGTTTTTCTCTTCGAATCTTCCTAAATACTATGACAATTGTCCATTTTTCTTCTGGTTC
AACACGTCTTTTATTCAAAATAACAGGCTTTGTCTACCAAGAAATGAATTGGATAATCCA
CATAAACAAAAAGCATGGAAAATTTATCCACCAGAATTTGCTGTGGAGATACTTTTTGGC
GAGAAATGA
Enzyme 78 GenBank Gene ID NM_199254.2 Link Image
Enzyme 78 GeneCard ID TPTE2 Link Image
Enzyme 78 GenAtlas ID TPTE2 Link Image
Enzyme 78 HGNC ID HGNC:17299 Link Image
Enzyme 78 Chromosome Location 1
Enzyme 78 Locus 13q12.11
Enzyme 78 SNPs SNPJam Report Link Image
Enzyme 78 General References
  1. Walker SM, Downes CP, Leslie NR: TPIP: a novel phosphoinositide 3-phosphatase. Biochem J. 2001 Dec 1;360(Pt 2):277-83. [PubMed Link Image]
  2. Tapparel C, Reymond A, Girardet C, Guillou L, Lyle R, Lamon C, Hutter P, Antonarakis SE: The TPTE gene family: cellular expression, subcellular localization and alternative splicing. Gene. 2003 Dec 24;323:189-99. [PubMed Link Image]
  3. 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]
Enzyme 78 Metabolite References Not Available
Enzyme 79 [top]
Enzyme 79 ID 14039
Enzyme 79 Name Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1
Enzyme 79 Synonyms
  1. Centaurin-beta-1
  2. Cnt-b1
Enzyme 79 Gene Name ACAP1
Enzyme 79 Protein Sequence >Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1
MTVKLDFEECLKDSPRFRASIELVEAEVSELETRLEKLLKLGTGLLESGRHYLAASRAFV
VGICDLARLGPPEPMMAECLEKFTVSLNHKLDSHAELLDATQHTLQQQIQTLVKEGLRGF
REARRDFWRGAESLEAALTHNAEVPRRRAQEAEEAGAALRTARAGYRGRALDYALQINVI
EDKRKFDIMEFVLRLVEAQATHFQQGHEELSRLSQYRKELGAQLHQLVLNSAREKRDMEQ
RHVLLKQKELGGEEPEPSLREGPGGLVMEGHLFKRASNAFKTWSRRWFTIQSNQLVYQKK
YKDPVTVVVDDLRLCTVKLCPDSERRFCFEVVSTSKSCLLQADSERLLQLWVSAVQSSIA
SAFSQARLDDSPRGPGQGSGHLAIGSAATLGSGGMARGREPGGVGHVVAQVQSVDGNAQC
CDCREPAPEWASINLGVTLCIQCSGIHRSLGVHFSKVRSLTLDSWEPELVKLMCELGNVI
INQIYEARVEAMAVKKPGPSCSRQEKEAWIHAKYVEKKFLTKLPEIRGRRGGRGRPRGQP
PVPPKPSIRPRPGSLRSKPEPPSEDLGSLHPGALLFRASGHPPSLPTMADALAHGADVNW
VNGGQDNATPLIQATAANSLLACEFLLQNGANVNQADSAGRGPLHHATILGHTGLACLFL
KRGADLGARDSEGRDPLTIAMETANADIVTLLRLAKMREAEAAQGQAGDETYLDIFRDFS
LMASDDPEKLSRRSHDLHTL
Enzyme 79 Number of Residues 740
Enzyme 79 Molecular Weight 81535.1
Enzyme 79 Theoretical pI 7.70
Enzyme 79 GO Classification
Function
  • ARF GTPase activator activity
  • GTPase regulator activity
  • binding
  • catalytic activity
  • cation binding
  • enzyme regulator activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • nucleoside-triphosphatase regulator activity
  • phospholipase C activity
  • phospholipase activity
  • small GTPase regulator activity
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of ARF GTPase activity
  • regulation of GTP catabolic process
  • regulation of GTPase activity
  • regulation of Ras GTPase activity
  • regulation of biological process
  • regulation of cellular metabolic process
  • regulation of metabolic process
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • regulation of nucleotide catabolic process
  • regulation of nucleotide metabolic process
  • regulation of purine nucleotide catabolic process
  • signaling
  • signaling pathway
Component
Enzyme 79 General Function Involved in ARF GTPase activator activity
Enzyme 79 Specific Function GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface
Enzyme 79 Pathways Not Available
Enzyme 79 Reactions Not Available
Enzyme 79 Pfam Domain Function
Enzyme 79 Signals
  • None
Enzyme 79 Transmembrane Regions
  • None
Enzyme 79 Essentiality Not Available
Enzyme 79 GenBank ID Protein 17391289 Link Image
Enzyme 79 UniProtKB/Swiss-Prot ID Q15027 Link Image
Enzyme 79 UniProtKB/Swiss-Prot Entry Name ACAP1_HUMAN Link Image
Enzyme 79 PDB ID Not Available
Enzyme 79 Cellular Location Not Available
Enzyme 79 Gene Sequence >2223 bp
ATGACGGTCAAGCTGGATTTCGAGGAGTGTCTCAAGGACTCACCCCGTTTCCGAGCCTCT
ATTGAGCTGGTGGAAGCCGAAGTGTCAGAATTGGAGACCCGTCTGGAAAAGCTCCTGAAA
CTGGGCACTGGTCTCCTGGAAAGTGGGCGCCATTACCTTGCTGCCAGCCGCGCCTTCGTT
GTCGGCATTTGTGACCTGGCCCGCCTGGGTCCACCAGAGCCCATGATGGCGGAGTGTCTG
GAAAAATTCACCGTGAGCCTGAACCACAAGCTGGACAGCCATGCGGAGCTTCTAGATGCC
ACCCAACACACACTGCAGCAGCAGATCCAGACCCTGGTCAAGGAAGGTCTGCGGGGTTTC
CGAGAGGCTCGCCGGGATTTCTGGCGGGGGGCTGAGAGCCTGGAGGCTGCCCTGACCCAC
AACGCAGAGGTTCCCAGGCGCCGGGCCCAGGAGGCAGAAGAGGCAGGAGCTGCTTTGAGG
ACGGCTCGAGCTGGGTACCGGGGACGGGCACTGGATTATGCCCTGCAGATCAACGTGATT
GAGGACAAGAGGAAGTTTGACATCATGGAGTTTGTGCTGCGTTTGGTGGAGGCCCAGGCT
ACCCATTTCCAGCAGGGCCATGAGGAGCTGAGCCGGCTGTCCCAGTATCGAAAGGAGCTG
GGCGCCCAGTTGCACCAGCTGGTCTTGAATTCAGCACGAGAGAAGAGGGACATGGAGCAG
AGACACGTGCTGCTGAAACAGAAGGAGCTGGGTGGGGAGGAGCCAGAACCAAGCTTAAGA
GAGGGGCCTGGTGGCCTGGTGATGGAAGGACATCTCTTCAAACGGGCCAGCAACGCATTT
AAGACCTGGAGCAGACGCTGGTTCACCATTCAGAGCAACCAACTGGTTTACCAGAAGAAG
TACAAGGACCCTGTGACTGTGGTGGTGGATGACCTTCGTCTCTGCACAGTGAAACTCTGC
CCTGACTCAGAAAGGCGGTTCTGCTTTGAGGTGGTGTCCACCAGCAAGTCCTGCCTCCTC
CAGGCTGACTCAGAGCGCCTCCTGCAGCTGTGGGTCAGTGCTGTGCAGAGCAGCATTGCT
TCTGCCTTCAGTCAGGCTCGCCTTGATGACAGCCCCCGGGGTCCAGGCCAGGGCTCAGGA
CACCTGGCCATAGGCTCTGCTGCCACCCTGGGCTCTGGTGGAATGGCCAGGGGAAGGGAG
CCTGGGGGAGTCGGGCACGTGGTGGCCCAGGTCCAGAGTGTGGATGGCAATGCCCAGTGC
TGCGACTGCCGGGAGCCAGCCCCGGAGTGGGCCAGCATCAACCTTGGTGTCACCCTCTGC
ATTCAGTGTTCCGGCATCCACAGGAGCCTTGGTGTTCACTTCTCCAAAGTCCGGTCTCTG
ACCCTTGACTCATGGGAGCCAGAACTAGTGAAGCTCATGTGTGAGCTGGGAAATGTCATC
ATCAACCAGATCTATGAGGCCCGCGTGGAGGCCATGGCAGTGAAGAAACCAGGGCCCAGC
TGCTCCCGGCAGGAGAAGGAGGCCTGGATTCACGCTAAATACGTGGAGAAGAAGTTCCTG
ACCAAGCTGCCTGAGATTCGAGGGCGAAGAGGTGGCCGGGGGCGCCCAAGGGGGCAGCCT
CCTGTGCCCCCAAAGCCTTCCATCAGGCCCCGGCCAGGGAGCTTGAGATCCAAGCCAGAG
CCCCCCTCTGAGGACCTGGGAAGCCTGCACCCTGGGGCCCTACTGTTTCGAGCGTCTGGG
CATCCTCCATCTCTTCCCACCATGGCTGATGCCCTTGCCCATGGAGCTGATGTCAACTGG
GTCAATGGGGGCCAAGATAATGCCACACCGCTGATCCAGGCCACAGCTGCTAATTCTCTT
CTGGCCTGTGAGTTTCTCCTCCAGAACGGGGCGAACGTGAACCAAGCGGACAGTGCGGGC
CGGGGCCCGCTGCACCACGCAACCATTCTTGGCCACACGGGGCTCGCCTGCCTGTTCCTG
AAACGGGGAGCTGATCTGGGGGCTCGAGACTCTGAAGGCAGGGACCCTCTGACCATCGCC
ATGGAAACAGCCAACGCTGACATCGTCACCCTGCTACGACTGGCAAAGATGAGGGAGGCT
GAAGCGGCCCAGGGGCAGGCAGGAGATGAGACGTATCTTGACATCTTCCGCGACTTCTCC
CTCATGGCGTCAGACGACCCGGAGAAGCTGAGCCGTCGCAGTCATGACCTCCACACGCTG
TGA
Enzyme 79 GenBank Gene ID BC018543 Link Image
Enzyme 79 GeneCard ID ACAP1 Link Image
Enzyme 79 GenAtlas ID ACAP1 Link Image
Enzyme 79 HGNC ID HGNC:16467 Link Image
Enzyme 79 Chromosome Location 1
Enzyme 79 Locus 17p13.1
Enzyme 79 SNPs SNPJam Report Link Image
Enzyme 79 General References
  1. Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1994;1(5):223-9. [PubMed Link Image]
  2. 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]
  3. Jackson TR, Brown FD, Nie Z, Miura K, Foroni L, Sun J, Hsu VW, Donaldson JG, Randazzo PA: ACAPs are arf6 GTPase-activating proteins that function in the cell periphery. J Cell Biol. 2000 Oct 30;151(3):627-38. [PubMed Link Image]
  4. Li J, Ballif BA, Powelka AM, Dai J, Gygi SP, Hsu VW: Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent recycling of integrin beta1 to control cell migration. Dev Cell. 2005 Nov;9(5):663-73. [PubMed Link Image]
  5. Shinozaki-Narikawa N, Kodama T, Shibasaki Y: Cooperation of phosphoinositides and BAR domain proteins in endosomal tubulation. Traffic. 2006 Nov;7(11):1539-50. Epub 2006 Sep 30. [PubMed Link Image]
  6. Ma Z, Nie Z, Luo R, Casanova JE, Ravichandran KS: Regulation of Arf6 and ACAP1 signaling by the PTB-domain-containing adaptor protein GULP. Curr Biol. 2007 Apr 17;17(8):722-7. Epub 2007 Mar 29. [PubMed Link Image]
  7. Li J, Peters PJ, Bai M, Dai J, Bos E, Kirchhausen T, Kandror KV, Hsu VW: An ACAP1-containing clathrin coat complex for endocytic recycling. J Cell Biol. 2007 Jul 30;178(3):453-64. [PubMed Link Image]
  8. Zhan X, Desiderio DM: Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry. Anal Biochem. 2006 Jul 15;354(2):279-89. Epub 2006 Jun 5. [PubMed Link Image]
  9. 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]
  10. 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 79 Metabolite References Not Available
Enzyme 80 [top]
Enzyme 80 ID 16985
Enzyme 80 Name Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1
Enzyme 80 Synonyms
  1. 130 kDa phosphatidylinositol 4,5-biphosphate-dependent ARF1 GTPase-activating protein
  2. ADP-ribosylation factor-directed GTPase-activating protein 1
  3. ARF GTPase-activating protein 1
  4. Development and differentiation-enhancing factor 1
  5. DEF-1
  6. Differentiation-enhancing factor 1
  7. PIP2-dependent ARF1 GAP
Enzyme 80 Gene Name ASAP1
Enzyme 80 Protein Sequence >Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1
MRSSASRLSSFSSRDSLWNRMPDQISVSEFIAETTEDYNSPTTSSFTTRLHNCRNTVTLL
EEALDQDRTALQKVKKSVKAIYNSGQDHVQNEENYAQVLDKFGSNFLSRDNPDLGTAFVK
FSTLTKELSTLLKNLLQGLSHNVIFTLDSLLKGDLKGVKGDLKKPFDKAWKDYETKFTKI
EKEKREHAKQHGMIRTEITGAEIAEEMEKERRLFQLQMCEYLIKVNEIKTKKGVDLLQNL
IKYYHAQCNFFQDGLKTADKLKQYIEKLAADLYNIKQTQDEEKKQLTALRDLIKSSLQLD
QKEDSQSRQGGYSMHQLQGNKEYGSEKKGYLLKKSDGIRKVWQRRKCSVKNGILTISHAT
SNRQPAKLNLLTCQVKPNAEDKKSFDLISHNRTYHFQAEDEQDYVAWISVLTNSKEEALT
MAFRGEQSAGENSLEDLTKAIIEDVQRLPGNDICCDCGSSEPTWLSTNLGILTCIECSGI
HREMGVHISRIQSLELDKLGTSELLLAKNVGNNSFNDIMEANLPSPSPKPTPSSDMTVRK
EYITAKYVDHRFSRKTCSTSSAKLNELLEAIKSRDLLALIQVYAEGVELMEPLLEPGQEL
GETALHLAVRTADQTSLHLVDFLVQNCGNLDKQTALGNTVLHYCSMYSKPECLKLLLRSK
PTVDIVNQAGETALDIAKRLKATQCEDLLSQAKSGKFNPHVHVEYEWNLRQEEIDESDDD
LDDKPSPIKKERSPRPQSFCHSSSISPQDKLALPGFSTPRDKQRLSYGAFTNQIFVSTST
DSPTSPTTEAPPLPPRNAGKGPTGPPSTLPLSTQTSSGSSTLSKKRPPPPPPGHKRTLSD
PPSPLPHGPPNKGAVPWGNDGGPSSSSKTTNKFEGLSQQSSTSSAKTALGPRVLPKLPQK
VALRKTDHLSLDKATIPPEIFQKSSQLAELPQKPPPGDLPPKPTELAPKPQIGDLPPKPG
ELPPKPQLGDLPPKPQLSDLPPKPQMKDLPPKPQLGDLLAKSQTGDVSPKAQQPSEVTLK
SHPLDLSPNVQSRDAIQKQASEDSNDLTPTLPETPVPLPRKINTGKNKVRRVKTIYDCQA
DNDDELTFIEGEVIIVTGEEDQEWWIGHIEGQPERKGVFPVSFVHILSD
Enzyme 80 Number of Residues 1129
Enzyme 80 Molecular Weight 125496.9
Enzyme 80 Theoretical pI 7.34
Enzyme 80 GO Classification
Function
  • ARF GTPase activator activity
  • GTPase regulator activity
  • binding
  • cation binding
  • enzyme regulator activity
  • ion binding
  • metal ion binding
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • regulation of ARF GTPase activity
  • regulation of GTP catabolic process
  • regulation of GTPase activity
  • regulation of Ras GTPase activity
  • regulation of biological process
  • regulation of cellular metabolic process
  • regulation of metabolic process
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • regulation of nucleotide catabolic process
  • regulation of nucleotide metabolic process
  • regulation of purine nucleotide catabolic process
Component
Enzyme 80 General Function Involved in ARF GTPase activator activity
Enzyme 80 Specific Function Possesses phosphatidylinositol 4,5-biphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types
Enzyme 80 Pathways Not Available
Enzyme 80 Reactions Not Available
Enzyme 80 Pfam Domain Function
Enzyme 80 Signals
  • None
Enzyme 80 Transmembrane Regions
  • None
Enzyme 80 Essentiality Not Available
Enzyme 80 GenBank ID Protein 46094081 Link Image
Enzyme 80 UniProtKB/Swiss-Prot ID Q9ULH1 Link Image
Enzyme 80 UniProtKB/Swiss-Prot Entry Name ASAP1_HUMAN Link Image
Enzyme 80 PDB ID Not Available
Enzyme 80 Cellular Location Not Available
Enzyme 80 Gene Sequence >3390 bp
ATGAGATCTTCAGCCTCCAGGCTCTCCAGTTTTTCGTCGAGAGATTCACTATGGAATCGG
ATGCCGGACCAGATCTCTGTCTCGGAGTTCATCGCCGAGACCACCGAGGACTACAACTCG
CCCACCACGTCCAGCTTCACCACGCGGCTGCACAACTGCAGGAACACCGTCACGCTGCTG
GAGGAGGCTCTAGACCAAGATAGAACAGCCCTTCAGAAAGTGAAGAAGTCTGTAAAAGCA
ATATATAATTCTGGTCAAGATCATGTACAAAATGAAGAAAACTATGCACAAGTTCTTGAT
AAGTTTGGGAGTAATTTTTTAAGTCGAGACAACCCCGACCTTGGCACCGCGTTTGTCAAG
TTTTCTACTCTTACAAAGGAACTGTCCACACTGCTGAAAAATCTGCTCCAGGGTTTGAGC
CACAATGTGATCTTCACCTTGGATTCTTTGTTAAAAGGAGACCTAAAGGGAGTCAAAGGA
GATCTCAAGAAGCCATTTGACAAAGCCTGGAAAGATTATGAGACAAAGTTTACAAAAATT
GAGAAAGAGAAAAGAGAGCACGCAAAACAACATGGGATGATCCGCACAGAGATAACAGGA
GCTGAGATTGCGGAAGAAATGGAGAAGGAAAGGCGCCTCTTTCAGCTCCAAATGTGTGAA
TATCTCATTAAAGTTAATGAAATCAAGACCAAAAAGGGTGTGGATCTGCTGCAGAATCTT
ATAAAGTATTACCATGCACAGTGCAATTTCTTTCAAGATGGCTTGAAAACAGCTGATAAG
TTGAAACAGTACATTGAAAAACTGGCTGCTGATTTATATAATATAAAACAGACCCAGGAT
GAAGAAAAGAAACAGCTAACTGCACTCCGAGACTTAATAAAATCCTCTCTTCAACTGGAT
CAGAAAGAAGATTCTCAGAGCCGGCAAGGAGGATACAGCATGCATCAGCTCCAGGGCAAT
AAGGAATATGGCAGTGAAAAGAAGGGGTACCTGCTAAAGAAAAGTGACGGGATCCGGAAA
GTATGGCAGAGGAGGAAGTGTTCAGTCAAGAATGGGATTCTGACCATCTCACATGCCACA
TCTAACAGGCAACCAGCCAAGTTGAACCTTCTCACCTGCCAAGTAAAACCTAATGCCGAA
GACAAAAAATCTTTTGACCTGATATCACATAATAGAACATATCACTTTCAGGCAGAAGAT
GAGCAGGATTATGTAGCATGGATATCAGTATTGACAAATAGCAAAGAAGAGGCCCTAACC
ATGGCCTTCCGTGGAGAGCAGAGTGCGGGAGAGAACAGCCTGGAAGACCTGACAAAAGCC
ATTATTGAGGATGTCCAGCGGCTCCCAGGGAATGACATTTGCTGCGATTGTGGCTCATCA
GAACCCACCTGGCTTTCAACCAACTTGGGTATTTTGACCTGTATAGAATGTTCTGGCATC
CATAGGGAAATGGGGGTTCATATTTCTCGCATTCAGTCTTTGGAACTAGACAAATTAGGA
ACTTCTGAACTCTTGCTGGCCAAGAATGTAGGAAACAATAGTTTTAATGATATTATGGAA
GCAAATTTACCCAGCCCCTCACCAAAACCCACCCCTTCAAGTGATATGACTGTACGAAAA
GAATATATCACTGCAAAGTATGTAGATCATAGGTTTTCAAGGAAGACCTGTTCAACTTCA
TCAGCTAAACTAAATGAATTGCTTGAGGCCATCAAATCCAGGGATTTACTTGCACTAATT
CAAGTCTATGCAGAAGGGGTAGAGCTAATGGAACCACTGCTGGAACCTGGGCAGGAGCTT
GGGGAGACAGCCCTTCACCTTGCCGTCCGAACTGCAGATCAGACATCTCTCCATTTGGTT
GACTTCCTTGTACAAAACTGTGGGAACCTGGATAAGCAGACGGCCCTGGGAAACACAGTT
CTACACTACTGTAGTATGTACAGTAAACCTGAGTGTTTGAAGCTTTTGCTCAGGAGCAAG
CCCACTGTGGATATAGTTAACCAGGCTGGAGAAACTGCCCTAGACATAGCAAAGAGACTA
AAAGCTACCCAGTGTGAAGATCTGCTTTCCCAGGCTAAATCTGGAAAGTTCAATCCACAC
GTCCACGTAGAATATGAGTGGAATCTTCGACAGGAGGAGATAGATGAGAGCGATGATGAT
CTGGATGACAAACCAAGCCCTATCAAGAAAGAGCGCTCACCCAGACCTCAGAGCTTCTGC
CACTCCTCCAGCATCTCCCCCCAGGACAAGCTGGCACTGCCAGGATTCAGCACTCCAAGG
GACAAACAGCGGCTCTCCTATGGAGCCTTCACCAACCAGATCTTCGTTTCCACAAGCACA
GACTCGCCCACATCACCAACCACGGAGGCTCCCCCTCTGCCTCCTAGGAACGCCGGGAAA
GGTCCAACTGGCCCACCTTCAACACTCCCTCTAAGCACCCAGACCTCTAGTGGCAGCTCC
ACCCTATCCAAGAAGAGGCCTCCTCCCCCACCACCCGGACACAAGAGAACCCTATCCGAC
CCTCCCAGCCCACTACCTCATGGGCCCCCAAACAAAGGCGCAGTTCCTTGGGGTAACGAT
GGGGGTCCATCCTCTTCAAGTAAGACTACAAACAAGTTTGAGGGACTATCCCAGCAGTCG
AGCACCAGTTCTGCAAAGACTGCCCTTGGCCCAAGAGTTCTTCCTAAACTACCTCAGAAA
GTGGCACTAAGGAAAACAGATCATCTCTCCCTAGACAAAGCCACCATCCCGCCCGAAATC
TTTCAGAAATCATCACAGTTGGCAGAGTTGCCACAAAAGCCACCACCTGGAGACCTGCCC
CCAAAGCCCACAGAACTGGCCCCCAAGCCCCAAATTGGAGATTTGCCGCCTAAGCCAGGA
GAACTGCCCCCCAAACCACAGCTGGGGGACCTGCCACCCAAACCCCAACTCTCAGACTTA
CCTCCCAAACCACAGATGAAGGACCTGCCCCCCAAACCACAGCTGGGAGACCTGCTAGCA
AAATCCCAGACTGGAGATGTCTCACCCAAGGCTCAGCAACCCTCTGAGGTCACACTGAAG
TCACACCCATTGGATCTATCCCCAAATGTGCAGTCCAGAGACGCCATCCAAAAGCAAGCA
TCTGAAGACTCCAACGACCTCACGCCTACTCTGCCAGAGACGCCCGTACCACTGCCCAGA
AAAATCAATACGGGGAAAAATAAAGTGAGGCGAGTGAAGACCATTTATGACTGCCAGGCA
GACAACGATGACGAGCTCACATTCATCGAGGGAGAAGTGATTATCGTCACAGGGGAAGAG
GACCAGGAGTGGTGGATTGGCCACATCGAAGGACAGCCTGAAAGGAAGGGGGTCTTTCCA
GTGTCCTTTGTTCATATCCTGTCTGACTAG
Enzyme 80 GenBank Gene ID NM_018482.2 Link Image
Enzyme 80 GeneCard ID ASAP1 Link Image
Enzyme 80 GenAtlas ID ASAP1 Link Image
Enzyme 80 HGNC ID HGNC:2720 Link Image
Enzyme 80 Chromosome Location 8
Enzyme 80 Locus 8q24.1-q24.2
Enzyme 80 SNPs SNPJam Report Link Image
Enzyme 80 General References
  1. 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]
  2. 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]
  3. Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [PubMed Link Image]
  4. Brown MT, Andrade J, Radhakrishna H, Donaldson JG, Cooper JA, Randazzo PA: ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src. Mol Cell Biol. 1998 Dec;18(12):7038-51. [PubMed Link Image]
  5. 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]
  6. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  7. 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]
  8. 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 80 Metabolite References Not Available