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Human Metabolome Database Version 2.5

 

Showing metabocard for DG(14:0/14:1(9Z)/0:0) (HMDB07009)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2008-09-12 02:12:59
Update Date 2009-05-05 21:01:33
Accession Number HMDB07009
Secondary Accession Numbers Not Available
Common Name DG(14:0/14:1(9Z)/0:0)
Description DG(14:0/14:1(9Z)/0:0) is a diglyceride, or a diacylglycerol (DAG). It is a glyceride consisting of two fatty acid chains covalently bonded to a glycerol molecule through ester linkages. Diacylglycerols can have many different combinations of fatty acids attached at both the C-1 and C-2 positions. DG(14:0/14:1(9Z)/0:0), in particular, consists of one chain of myristic acid at the C-1 position and one chain of myristoleic acid at the C-2 position. The myristic acid moiety is derived from nutmeg and butter, while the myristoleic acid moiety is derived from milk fats. Mono- and diacylglycerols are common food additives used to blend together certain ingredients, such as oil and water, which would not otherwise blend well. Dacylglycerols are often found in bakery products, beverages, ice cream, chewing gum, shortening, whipped toppings, margarine, and confections. Synthesis of diacylglycerol begins with glycerol-3-phosphate, which is derived primarily from dihydroxyacetone phosphate, a product of glycolysis (usually in the cytoplasm of liver or adipose tissue cells). Glycerol-3-phosphate is first acylated with acyl-coenzyme A (acyl-CoA) to form lysophosphatidic acid, which is then acylated with another molecule of acyl-CoA to yield phosphatidic acid. Phosphatidic acid is then de-phosphorylated to form diacylglycerol. Diacylglycerols are precursors to triacylglycerols (triglyceride), which are formed by the addition of a third fatty acid to the diacylglycerol under the catalysis of diglyceride acyltransferase.Since diacylglycerols are synthesized via phosphatidic acid, they will usually contain a saturated fatty acid at the C-1 position on the glycerol moiety and an unsaturated fatty acid at the C-2 position.
Synonyms
  1. DAG(14:0/14:1)
  2. Diacylglycerol(14:0/14:1)
  3. DG(14:0/14:1n5)
  4. Diacylglycerol(14:0/14:1w5)
  5. Diacylglycerol(28:1)
  6. 1-myristoyl-2-myristoleoyl-sn-glycerol
  7. DG(14:0/14:1w5)
  8. DG(14:0/14:1)
  9. Diglyceride
  10. Diacylglycerol
  11. DAG(14:0/14:1n5)
  12. DG(28:1)
  13. DAG(28:1)
  14. DAG(14:0/14:1w5)
  15. Diacylglycerol(14:0/14:1n5)
Chemical IUPAC Name 1-tetradecanoyl-2-(9Z-tetradecenoyl)-sn-glycerol
Chemical Formula C31H58O5
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Lipids
Class
  • Glycerolipids
Sub Class
  • Diacylglycerols
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • carboxylic acid ester
  • alkene
Biofunction
  • Membrane component
  • Energy source
  • Cell signaling
Application
Source
  • Endogenous
Average Molecular Weight 510.789
Monoisotopic Molecular Weight 510.428436
Isomeric SMILES CCCCCCCCCCCCCC(=O)OC[C@H](CO)OC(=O)CCCCCCCC=C/CCCC
Canonical SMILES CCCCCCCCCCCCCC(=O)OCC(CO)OC(=O)CCCCCCCC=CCCCC
KEGG Compound ID Not Available
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB07009 Link Image
Metagene Link HMDB07009 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/C31H58O5/c1-3-5-7-9-11-13-15-17-19-21-23-25-30(33)35-28-29(27-32)36-31(34)26-24-22-20-18-16-14-12-10-8-6-4-2/h10,12,29,32H,3-9,11,13-28H2,1-2H3/b12-10-/t29-/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 3.23e-05 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 9.02 [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
  • Blood
Tissue Location
Tissue References
All Tissues
Concentrations (Normal)
Biofluid Blood
Value 1.036 +/- 0.271 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal (Upper Limit)
Comments Not Available
References
  • Psychogios N, Hau DD, Peng J, Guo AC, Mandal R, Bouatra S, Sinelnikov I, Krishnamurthy R, Eisner R, Gautam B, Young N, Xia J, Knox C, Dong E, Huang P, Hollander Z, Pedersen TL, Smith SR, Bamforth F, Greiner R, McManus B, Newman JW, Goodfriend T, Wishart DS: The human serum metabolome. PLoS One. 2011 Feb 16;6(2):e16957. [PubMed Link Image]
  • Wishart DS, Knox C, Guo AC, Eisner R, Young N, Gautam B, Hau DD, Psychogios N, Dong E, Bouatra S, Mandal R, Sinelnikov I, Xia J, Jia L, Cruz JA, Lim E, Sobsey CA, Shrivastava S, Huang P, Liu P, Fang L, Peng J, Fradette R, Cheng D, Tzur D, Clements M, Lewis A, De Souza A, Zuniga A, Dawe M, Xiong Y, Clive D, Greiner R, Nazyrova A, Shaykhutdinov R, Li L, Vogel HJ, Forsythe I: HMDB: a knowledgebase for the human metabolome. Nucleic Acids Res. 2008 Oct 25. [PubMed Link Image]
Biofluid Blood
Value 0.032734 +/- 0.017119 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal (Most Probable)
Comments Not Available
References
  • Psychogios N, Hau DD, Peng J, Guo AC, Mandal R, Bouatra S, Sinelnikov I, Krishnamurthy R, Eisner R, Gautam B, Young N, Xia J, Knox C, Dong E, Huang P, Hollander Z, Pedersen TL, Smith SR, Bamforth F, Greiner R, McManus B, Newman JW, Goodfriend T, Wishart DS: The human serum metabolome. PLoS One. 2011 Feb 16;6(2):e16957. [PubMed Link Image]
  • Wishart DS, Knox C, Guo AC, Eisner R, Young N, Gautam B, Hau DD, Psychogios N, Dong E, Bouatra S, Mandal R, Sinelnikov I, Xia J, Jia L, Cruz JA, Lim E, Sobsey CA, Shrivastava S, Huang P, Liu P, Fang L, Peng J, Fradette R, Cheng D, Tzur D, Clements M, Lewis A, De Souza A, Zuniga A, Dawe M, Xiong Y, Clive D, Greiner R, Nazyrova A, Shaykhutdinov R, Li L, Vogel HJ, Forsythe I: HMDB: a knowledgebase for the human metabolome. Nucleic Acids Res. 2008 Oct 25. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways Not Available
General References Not Available
Metabolic Enzymes
  1. Diacylglycerol kinase theta
  2. Pancreatic triacylglycerol lipase
  3. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1
  4. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4
  5. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2
  6. Diacylglycerol kinase gamma
  7. Hepatic triacylglycerol lipase
  8. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3
  9. Pancreatic lipase-related protein 1
  10. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2
  11. Lipid phosphate phosphohydrolase 2
  12. Patatin-like phospholipase domain-containing protein 3
  13. Diacylglycerol kinase alpha
  14. Diacylglycerol kinase delta
  15. Diacylglycerol kinase epsilon
  16. Gastric triacylglycerol lipase
  17. Lipid phosphate phosphohydrolase 1
  18. Diacylglycerol kinase beta
  19. Endothelial lipase
  20. Diacylglycerol kinase iota
  21. Bile salt-activated lipase
  22. Lipid phosphate phosphohydrolase 3
  23. Diacylglycerol O-acyltransferase 1
  24. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1
  25. Pancreatic lipase-related protein 2
  26. Diacylglycerol kinase zeta
  27. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1
  28. Lipoprotein lipase
  29. Galactosylceramide sulfotransferase
  30. Hormone-sensitive lipase
  31. Phosphatidate cytidylyltransferase 2
  32. Choline-phosphate cytidylyltransferase A
  33. Phosphatidate cytidylyltransferase 1
  34. Phosphatidylcholine:ceramide cholinephosphotransferase 2
  35. CDP-diacylglycerol--inositol 3-phosphatidyltransferase
  36. Phosphatidylcholine:ceramide cholinephosphotransferase 1
  37. Rap guanine nucleotide exchange factor 2
  38. RAF proto-oncogene serine/threonine-protein kinase
  39. Protein kinase C alpha type
  40. Serine/threonine-protein kinase A-Raf
  41. Citron Rho-interacting kinase
  42. Protein kinase C beta type
  43. Protein kinase C zeta type
  44. Protein kinase C iota type
  45. Rho-associated protein kinase 1
  46. Serine/threonine-protein kinase D1
  47. Protein kinase C gamma type
  48. Rho-associated protein kinase 2
  49. Protein kinase C delta type
  50. Serine/threonine-protein kinase D3
  51. Protein kinase C theta type
  52. Protein kinase C eta type
  53. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-2
  54. Protein kinase C epsilon type
  55. Ras association domain-containing protein 1
  56. Serine/threonine-protein kinase B-raf
  57. Short transient receptor potential channel 3
  58. Cholinephosphotransferase 1
  59. Inactive phospholipase C-like protein 1
  60. 2-acylglycerol O-acyltransferase 2
  61. Patatin-like phospholipase domain-containing protein 4
  62. CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
  63. Diacylglycerol kinase eta
  64. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
  65. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-1
  66. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1
  67. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
  68. Diacylglycerol O-acyltransferase 2
  69. 2-acylglycerol O-acyltransferase 1
  70. Acyl-CoA wax alcohol acyltransferase 1
  71. Acyl-CoA wax alcohol acyltransferase 2
  72. Diacylglycerol O-acyltransferase 2-like protein 6
  73. Putative diacylglycerol O-acyltransferase 2-like protein 7
  74. Sn1-specific diacylglycerol lipase alpha
  75. Sn1-specific diacylglycerol lipase beta
  76. 2-acylglycerol O-acyltransferase 3
  77. Diacylglycerol kinase kappa
  78. Serine/threonine-protein kinase D2
  79. Inactive phospholipase C-like protein 2
  80. Membrane-associated phosphatidylinositol transfer protein 1
  81. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase zeta-1
  82. Patatin-like phospholipase domain-containing protein 2
  83. A-kinase anchor protein 13
  84. RAS guanyl-releasing protein 1
  85. RAS guanyl-releasing protein 2
  86. Myosin-IXb
  87. Short transient receptor potential channel 6
  88. Short transient receptor potential channel 7
  89. Protein unc-13 homolog A
  90. Protein unc-13 homolog B
  91. Protein unc-13 homolog C
  92. Rho guanine nucleotide exchange factor 2
  93. RAS guanyl-releasing protein 4
  94. Serine/threonine-protein kinase MRCK alpha
  95. Serine/threonine-protein kinase MRCK beta
  96. Serine/threonine-protein kinase MRCK gamma
  97. Guanine nucleotide exchange factor VAV3
  98. Acylglycerol kinase, mitochondrial
  99. Protein kinase C, epsilon (Protein kinase C, epsilon, isoform CRA_b)
  100. Pancreatic lipase-related protein 3
  101. CDC42 binding protein kinase beta (DMPK-like)
  102. cDNA, FLJ92607, highly similar to Homo sapiens protein kinase C, gamma (PRKCG), mRNA
  103. Kinase suppressor of Ras 2
  104. cDNA FLJ76797, highly similar to Homo sapiens protein kinase C, zeta (PRKCZ), mRNA
  105. cDNA FLJ60459, highly similar to Protein kinase C theta type (EC 2.7.11.13)
  106. Tensin-like C1 domain-containing phosphatase
  107. Protein kinase C, alpha variant
  108. Kinase suppressor of Ras 1
  109. cDNA, FLJ94469, highly similar to Homo sapiens protein kinase C, epsilon (PRKCE), mRNA
  110. Protein kinase C, eta, isoform CRA_a
  111. cDNA, FLJ96384, highly similar to Homo sapiens protein kinase C, iota (PRKCI), mRNA
  112. cDNA FLJ57052, highly similar to Protein kinase C delta type (EC 2.7.11.13)
  113. Protein kinase C, gamma variant
  114. CDC42-binding protein kinase beta
  115. PRKCA protein
  116. SH3 and cysteine-rich domain-containing protein 3
  117. GEM-interacting protein
  118. Differentially expressed in FDCP 8 homolog
  119. Rho GTPase-activating protein 29
  120. Pleckstrin homology domain-containing family M member 3
  121. Minor histocompatibility protein HA-1
  122. Guanine nucleotide exchange factor VAV2
  123. UNC13B variant protein
  124. Rho-guanine nucleotide exchange factor
  125. Pleckstrin homology domain-containing family M member 1
  126. Putative uncharacterized protein ROCK2
  127. SH3 and cysteine-rich domain-containing protein 2
  128. Beta-chimaerin
  129. Gamma-1-syntrophin
  130. N-chimaerin
  131. Citron
  132. Unc-13 homolog B (C. elegans)
  133. Myosin-IXa
  134. Ras association domain-containing protein 5
  135. UNC13B protein
  136. Aging-associated gene 6 protein
  137. PDZ domain-containing protein 8
  138. Proto-oncogene vav
  139. Putative pleckstrin homology domain-containing family M member 1P
  140. SH3 and cysteine-rich domain-containing protein
  141. Rac GTPase-activating protein 1
  142. Ras guanyl-releasing protein 3
Enzyme 1 [top]
Enzyme 1 ID 5452
Enzyme 1 Name Diacylglycerol kinase theta
Enzyme 1 Synonyms
  1. DAG kinase theta
  2. Diglyceride kinase theta
  3. DGK-theta
Enzyme 1 Gene Name DGKQ
Enzyme 1 Protein Sequence >Diacylglycerol kinase theta
MAAAAEPGARAWLGGGSPRPGSPACSPVLGSGGRARPGPGPGPGPERAGVRAPGPAAAPG
HSFRKVTLTKPTFCHLCSDFIWGLAGFLCDVCNFMSHEKCLKHVRIPCTSVAPSLVRVPV
AHCFGPRGLHKRKFCAVCRKVLEAPALHCEVCELHLHPDCVPFACSDCRQCHQDGHQDHD
THHHHWREGNLPSGARCEVCRKTCGSSDVLAGVRCEWCGVQAHSLCSAALAPECGFGRLR
SLVLPPACVRLLPGGFSKTQSFRIVEAAEPGEGGDGADGSAAVGPGRETQATPESGKQTL
KIFDGDDAVRRSQFRLVTVSRLAGAEEVLEAALRAHHIPEDPGHLELCRLPPSSQACDAW
AGGKAGSAVISEEGRSPGSGEATPEAWVIRALPRAQEVLKIYPGWLKVGVAYVSVRVTPK
STARSVVLEVLPLLGRQAESPESFQLVEVAMGCRHVQRTMLMDEQPLLDRLQDIRQMSVR
QVSQTRFYVAESRDVAPHVSLFVGGLPPGLSPEEYSSLLHEAGATKATVVSVSHIYSSQG
AVVLDVACFAEAERLYMLLKDMAVRGRLLTALVLPDLLHAKLPPDSCPLLVFVNPKSGGL
KGRDLLCSFRKLLNPHQVFDLTNGGPLPGLHLFSQVPCFRVLVCGGDGTVGWVLGALEET
RYRLACPEPSVAILPLGTGNDLGRVLRWGAGYSGEDPFSVLLSVDEADAVLMDRWTILLD
AHEAGSAENDTADAEPPKIVQMSNYCGIGIDAELSLDFHQAREEEPGKFTSRLHNKGVYV
RVGLQKISHSRSLHKQIRLQVERQEVELPSIEGLIFINIPSWGSGADLWGSDSDTRFEKP
RMDDGLLEVVGVTGVVHMGQVQGGLRSGIRIAQGSYFRVTLLKATPVQVDGEPWVQAPGH
MIISAAGPKVHMLRKAKQKPRRAGTTRDARADAAPAPESDPR
Enzyme 1 Number of Residues 942
Enzyme 1 Molecular Weight 101154.0
Enzyme 1 Theoretical pI 7.50
Enzyme 1 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • biological regulation
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 1 General Function Involved in diacylglycerol kinase activity
Enzyme 1 Specific Function Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA). May regulate the activity of protein kinase C by controlling the balance between these two signaling lipids. Activated in the nucleus in response to alpha-thrombin and nerve growth factor. May be involved in cAMP- induced activation of NR5A1 and subsequent steroidogenic gene transcription by delivering PA as ligand for NR5A1. Acts synergistically with NR5A1 on CYP17 transcriptional activity
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 40806175 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P52824 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name DGKQ_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2829 bp
ATGGCGGCGGCGGCCGAGCCCGGGGCCCGCGCCTGGCTGGGCGGCGGCTCCCCGCGCCCC
GGCAGCCCGGCCTGCAGCCCCGTGCTGGGCTCAGGAGGCCGCGCGCGCCCGGGGCCGGGG
CCGGGGCCGGGACCCGAGCGGGCGGGCGTCAGAGCCCCGGGCCCCGCTGCCGCGCCGGGA
CACAGCTTCCGGAAGGTGACGCTCACCAAGCCCACCTTCTGCCACCTCTGCTCCGACTTC
ATCTGGGGGCTGGCCGGCTTCCTGTGCGACGTCTGCAATTTCATGTCTCATGAGAAGTGC
CTGAAGCACGTGAGGATCCCGTGCACGAGTGTGGCACCCAGCCTGGTCCGGGTTCCTGTA
GCCCACTGCTTCGGCCCCCGGGGGCTCCACAAGCGCAAGTTCTGTGCTGTCTGCCGCAAG
GTCCTGGAGGCACCGGCGCTCCACTGCGAAGTGTGTGAGCTGCACCTCCACCCAGACTGT
GTGCCCTTCGCCTGCAGTGACTGCCGCCAGTGCCACCAGGATGGGCACCAGGATCACGAC
ACCCATCACCACCACTGGCGGGAGGGGAACCTGCCCTCGGGAGCGCGCTGCGAGGTCTGC
AGGAAGACGTGCGGCTCCTCTGACGTGCTGGCCGGCGTGCGCTGCGAGTGGTGCGGGGTC
CAGGCGCACTCCCTCTGCTCCGCGGCGCTGGCTCCCGAGTGTGGCTTCGGGCGTCTGCGC
TCCCTGGTCCTGCCTCCCGCGTGCGTGCGCCTTCTGCCCGGCGGCTTCAGCAAGACGCAG
AGCTTCCGCATCGTGGAGGCCGCGGAGCCGGGCGAGGGGGGCGACGGCGCCGACGGGAGC
GCTGCCGTGGGTCCAGGCAGAGAGACACAGGCAACTCCGGAGTCCGGGAAGCAAACGCTG
AAGATCTTTGATGGCGACGACGCGGTGAGAAGAAGCCAGTTCCGCCTCGTCACGGTGTCC
CGCCTGGCCGGTGCCGAGGAGGTGCTGGAGGCCGCACTGCGGGCCCACCACATCCCCGAG
GACCCTGGCCACCTGGAGCTGTGCCGGCTGCCCCCTTCCTCTCAGGCCTGTGACGCCTGG
GCTGGGGGCAAGGCTGGGAGTGCTGTGATCTCGGAGGAGGGCAGAAGCCCCGGGTCCGGC
GAGGCCACGCCAGAGGCCTGGGTCATCCGGGCTCTGCCGCGGGCCCAGGAGGTCCTGAAG
ATCTACCCTGGCTGGCTCAAGGTGGGCGTGGCCTACGTGTCCGTGCGAGTGACCCCGAAG
AGCACGGCCCGCTCTGTGGTGCTGGAGGTCCTGCCGCTGCTCGGCCGCCAGGCCGAGAGT
CCCGAGAGCTTCCAGCTGGTGGAGGTGGCGATGGGCTGCAGGCACGTCCAGCGGACGATG
CTGATGGACGAACAGCCCCTGCTGGACCGGCTACAGGACATCCGGCAGATGTCTGTGCGG
CAGGTGAGCCAGACGCGGTTCTACGTGGCAGAGAGCAGGGATGTAGCCCCGCACGTCTCC
CTGTTTGTTGGCGGCCTGCCTCCCGGCCTGTCTCCCGAGGAGTACAGCAGCCTGCTGCAT
GAGGCCGGGGCTACCAAAGCCACCGTGGTGTCCGTGAGTCACATCTACTCCTCCCAAGGC
GCGGTAGTGTTGGACGTTGCCTGCTTTGCGGAGGCCGAGCGGCTGTACATGCTGCTGAAG
GACATGGCTGTGCGGGGCCGGCTGCTCACTGCCCTGGTGCTCCCCGACCTGCTGCACGCG
AAGCTGCCCCCAGACAGCTGTCCCCTCCTTGTGTTCGTGAACCCCAAGAGTGGAGGCCTC
AAGGGCCGAGACCTGCTCTGCAGCTTCCGGAAGCTACTGAACCCTCATCAGGTCTTCGAC
CTGACCAACGGAGGTCCTCTTCCCGGGCTCCACCTGTTCTCCCAGGTGCCCTGCTTCCGG
GTGCTGGTGTGTGGTGGCGATGGCACTGTGGGCTGGGTGCTTGGCGCCCTGGAGGAGACA
CGGTACCGACTGGCCTGCCCGGAGCCTTCTGTGGCCATCCTGCCCCTGGGCACAGGGAAT
GACCTTGGTCGAGTCCTCCGCTGGGGGGCGGGCTACAGCGGCGAGGACCCGTTCTCCGTA
CTGCTGTCTGTGGACGAGGCCGACGCCGTGCTCATGGACCGCTGGACCATCCTGCTGGAT
GCCCACGAGGCTGGCAGTGCAGAGAACGACACGGCAGACGCAGAGCCCCCCAAGATCGTG
CAGATGAGTAACTACTGTGGCATTGGCATCGACGCGGAGCTGAGCCTGGACTTCCACCAG
GCACGGGAAGAGGAGCCTGGCAAGTTCACAAGCAGGCTGCACAACAAGGGTGTGTACGTG
CGGGTGGGGCTGCAGAAGATCAGTCACTCTCGGAGCCTGCACAAGCAGATCCGGCTGCAG
GTGGAGCGGCAGGAGGTGGAGCTGCCCAGTATTGAAGGCCTCATCTTCATCAACATCCCC
AGCTGGGGCTCGGGGGCCGACCTGTGGGGCTCCGACAGCGACACCAGGTTTGAGAAGCCA
CGCATGGACGACGGGCTGCTGGAGGTTGTGGGCGTGACGGGCGTCGTGCACATGGGCCAG
GTCCAGGGTGGGCTGCGCTCCGGAATCCGGATTGCCCAGGGTTCCTACTTCCGAGTCACG
CTCCTCAAGGCCACCCCGGTGCAGGTGGACGGGGAGCCCTGGGTCCAGGCCCCGGGGCAC
ATGATCATCTCAGCTGCTGGCCCTAAGGTGCACATGCTGAGGAAGGCCAAGCAGAAGCCG
AGGAGGGCCGGGACCACCAGGGATGCCCGGGCGGATGCTGCGCCTGCCCCTGAGAGCGAT
CCTAGGTAG
Enzyme 1 GenBank Gene ID NM_001347.2 Link Image
Enzyme 1 GeneCard ID DGKQ Link Image
Enzyme 1 GenAtlas ID DGKQ Link Image
Enzyme 1 HGNC ID HGNC:2856 Link Image
Enzyme 1 Chromosome Location 4
Enzyme 1 Locus 4p16.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Pilz A, Schaap D, Hunt D, Fitzgibbon J: Chromosomal localization of three mouse diacylglycerol kinase (DAGK) genes: genes sharing sequence homology to the Drosophila retinal degeneration A (rdgA) gene. Genomics. 1995 Apr 10;26(3):599-601. [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. Houssa B, de Widt J, Kranenburg O, Moolenaar WH, van Blitterswijk WJ: Diacylglycerol kinase theta binds to and is negatively regulated by active RhoA. J Biol Chem. 1999 Mar 12;274(11):6820-2. [PubMed Link Image]
  5. 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]
  6. Los AP, van Baal J, de Widt J, Divecha N, van Blitterswijk WJ: Structure-activity relationship of diacylglycerol kinase theta. Biochim Biophys Acta. 2004 Mar 22;1636(2-3):169-74. [PubMed Link Image]
  7. van Baal J, de Widt J, Divecha N, van Blitterswijk WJ: Translocation of diacylglycerol kinase theta from cytosol to plasma membrane in response to activation of G protein-coupled receptors and protein kinase C. J Biol Chem. 2005 Mar 18;280(11):9870-8. Epub 2005 Jan 4. [PubMed Link Image]
  8. Li D, Urs AN, Allegood J, Leon A, Merrill AH Jr, Sewer MB: Cyclic AMP-stimulated interaction between steroidogenic factor 1 and diacylglycerol kinase theta facilitates induction of CYP17. Mol Cell Biol. 2007 Oct;27(19):6669-85. Epub 2007 Jul 30. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5453
Enzyme 2 Name Pancreatic triacylglycerol lipase
Enzyme 2 Synonyms
  1. PL
  2. Pancreatic lipase
Enzyme 2 Gene Name PNLIP
Enzyme 2 Protein Sequence >Pancreatic triacylglycerol lipase
MLPLWTLSLLLGAVAGKEVCYERLGCFSDDSPWSGITERPLHILPWSPKDVNTRFLLYTN
ENPNNFQEVAADSSSISGSNFKTNRKTRFIIHGFIDKGEENWLANVCKNLFKVESVNCIC
VDWKGGSRTGYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVIGHSLGAHAAGEAGR
RTNGTIGRITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDGAPIVPNLGFGMSQVVGH
LDFFPNGGVEMPGCKKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYTDSIVNPDGFAGF
PCASYNVFTANKCFPCPSGGCPQMGHYADRYPGKTNDVGQKFYLDTGDASNFARWRYKVS
VTLSGKKVTGHILVSLFGNKGNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWY
NNVINPTLPRVGASKIIVETNVGKQFNFCSPETVREEVLLTLTPC
Enzyme 2 Number of Residues 465
Enzyme 2 Molecular Weight 51156.5
Enzyme 2 Theoretical pI 6.72
Enzyme 2 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • triglyceride lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 2 General Function Involved in catalytic activity
Enzyme 2 Specific Function Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-16
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID P16233 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name LIPP_HUMAN Link Image
Enzyme 2 PDB ID 1N8S Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1398 bp
ATGCTGCCACTTTGGACTCTTTCACTGCTGCTGGGAGCAGTAGCAGGAAAAGAAGTTTGC
TACGAAAGACTCGGCTGCTTCAGTGATGACTCCCCATGGTCAGGAATTACGGAAAGACCC
CTCCATATATTGCCTTGGTCTCCAAAAGATGTCAACACCCGCTTCCTCCTATATACTAAT
GAGAACCCAAACAACTTTCAAGAAGTTGCCGCAGATTCATCAAGCATCAGTGGCTCCAAT
TTCAAAACAAATAGAAAAACTCGCTTTATTATTCATGGATTCATAGACAAGGGAGAAGAA
AACTGGCTGGCCAATGTGTGCAAGAATCTGTTCAAGGTGGAAAGTGTGAACTGTATCTGT
GTGGACTGGAAAGGTGGCTCCCGAACTGGATACACACAAGCCTCGCAGAACATCAGGATC
GTGGGAGCAGAAGTGGCATATTTTGTTGAATTTCTTCAGTCGGCGTTCGGTTACTCACCT
TCCAACGTGCATGTCATTGGCCACAGCCTGGGTGCCCACGCTGCTGGGGAGGCTGGAAGG
AGAACCAATGGGACCATTGGACGCATCACAGGGTTGGACCCAGCAGAACCTTGCTTTCAG
GGCACACCTGAATTAGTCCGATTGGACCCCAGCGATGCCAAATTTGTGGATGTAATTCAC
ACGGATGGTGCCCCCATAGTCCCCAATTTGGGGTTTGGAATGAGCCAAGTCGTGGGCCAC
CTAGATTTCTTTCCAAATGGAGGAGTGGAAATGCCTGGATGTAAAAAGAACATTCTCTCT
CAGATTGTGGACATAGACGGAATCTGGGAAGGGACTCGAGACTTTGCGGCCTGTAATCAC
TTAAGAAGCTACAAATATTACACTGATAGCATCGTCAACCCTGATGGCTTTGCTGGATTC
CCCTGTGCCTCTTACAACGTCTTCACTGCAAACAAGTGTTTCCCTTGTCCAAGTGGAGGC
TGCCCACAGATGGGTCACTATGCTGATAGATATCCTGGGAAAACAAATGATGTGGGCCAG
AAATTTTATCTAGACACTGGTGATGCCAGTAATTTTGCACGTTGGAGGTATAAGGTATCT
GTCACACTGTCTGGAAAAAAGGTTACAGGACACATACTAGTTTCTTTGTTCGGAAATAAA
GGAAACTCTAAGCAGTATGAAATTTTCAAGGGCACTCTCAAACCAGATAGTACTCATTCC
AATGAATTTGACTCAGATGTGGATGTTGGGGACTTGCAGATGGTTAAATTTATTTGGTAT
AACAATGTGATCAACCCAACTTTACCTAGAGTGGGAGCATCCAAGATTATAGTGGAGACA
AATGTTGGAAAACAGTTCAACTTCTGTAGTCCAGAAACCGTCAGGGAGGAAGTTCTGCTC
ACCCTCACACCGTGTTAG
Enzyme 2 GenBank Gene ID J05125 Link Image
Enzyme 2 GeneCard ID PNLIP Link Image
Enzyme 2 GenAtlas ID PNLIP Link Image
Enzyme 2 HGNC ID HGNC:9155 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 10q26.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Lowe ME, Rosenblum JL, Strauss AW: Cloning and characterization of human pancreatic lipase cDNA. J Biol Chem. 1989 Nov 25;264(33):20042-8. [PubMed Link Image]
  2. Giller T, Buchwald P, Blum-Kaelin D, Hunziker W: Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J Biol Chem. 1992 Aug 15;267(23):16509-16. [PubMed Link Image]
  3. Sims HF, Jennens ML, Lowe ME: The human pancreatic lipase-encoding gene: structure and conservation of an Alu sequence in the lipase gene family. Gene. 1993 Sep 15;131(2):281-5. [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. Winkler FK, D'Arcy A, Hunziker W: Structure of human pancreatic lipase. Nature. 1990 Feb 22;343(6260):771-4. [PubMed Link Image]
  6. van Tilbeurgh H, Sarda L, Verger R, Cambillau C: Structure of the pancreatic lipase-procolipase complex. Nature. 1992 Sep 10;359(6391):159-62. [PubMed Link Image]
  7. van Tilbeurgh H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C: Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature. 1993 Apr 29;362(6423):814-20. [PubMed Link Image]
  8. Carriere F, Thirstrup K, Boel E, Verger R, Thim L: Structure-function relationships in naturally occurring mutants of pancreatic lipase. Protein Eng. 1994 Apr;7(4):563-9. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5454
Enzyme 3 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1
Enzyme 3 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 3 Gene Name PLCB1
Enzyme 3 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 3 Number of Residues 1216
Enzyme 3 Molecular Weight 138565.8
Enzyme 3 Theoretical pI 6.12
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 12083581 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9NQ66 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PLCB1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 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 3 GenBank Gene ID NM_015192.2 Link Image
Enzyme 3 GeneCard ID PLCB1 Link Image
Enzyme 3 GenAtlas ID PLCB1 Link Image
Enzyme 3 HGNC ID HGNC:15917 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 20p12
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5455
Enzyme 4 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4
Enzyme 4 Synonyms
  1. Phosphoinositide phospholipase C-beta-4
  2. Phospholipase C-beta-4
  3. PLC-beta-4
Enzyme 4 Gene Name PLCB4
Enzyme 4 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 4 Number of Residues 1175
Enzyme 4 Molecular Weight 134462.6
Enzyme 4 Theoretical pI 6.90
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 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. This form has a role in retina signal transduction
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 57284038 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q15147 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PLCB4_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 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 4 GenBank Gene ID AL023805 Link Image
Enzyme 4 GeneCard ID PLCB4 Link Image
Enzyme 4 GenAtlas ID PLCB4 Link Image
Enzyme 4 HGNC ID HGNC:9059 Link Image
Enzyme 4 Chromosome Location 2
Enzyme 4 Locus 20p12
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5456
Enzyme 5 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2
Enzyme 5 Synonyms
  1. Phosphoinositide phospholipase C-beta-2
  2. Phospholipase C-beta-2
  3. PLC-beta-2
Enzyme 5 Gene Name PLCB2
Enzyme 5 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 5 Number of Residues 1185
Enzyme 5 Molecular Weight 134023.2
Enzyme 5 Theoretical pI 6.21
Enzyme 5 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 5 General Function Involved in calcium ion binding
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
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 95147333 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q00722 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PLCB2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 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 5 GenBank Gene ID NM_004573.2 Link Image
Enzyme 5 GeneCard ID PLCB2 Link Image
Enzyme 5 GenAtlas ID PLCB2 Link Image
Enzyme 5 HGNC ID HGNC:9055 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 15q15
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5457
Enzyme 6 Name Diacylglycerol kinase gamma
Enzyme 6 Synonyms
  1. DAG kinase gamma
  2. Diglyceride kinase gamma
  3. DGK-gamma
Enzyme 6 Gene Name DGKG
Enzyme 6 Protein Sequence >Diacylglycerol kinase gamma
MGEERWVSLTPEEFDQLQKYSEYSSKKIKDALTEFNEGGSLKQYDPHEPISYDVFKLFMR
AYLEVDLPQPLSTHLFLAFSQKPRHETSDHPTEGASNSEANSADTNIQNADNATKADEAC
APDTESNMAEKQAPAEDQVAATPLEPPVPRSSSSESPVVYLKDVVCYLSLLETGRPQDKL
EFMFRLYDSDENGLLDQAEMDCIVNQMLHIAQYLEWDPTELRPILKEMLQGMDYDRDGFV
SLQEWVHGGMTTIPLLVLLGMDDSGSKGDGRHAWTMKHFKKPTYCNFCHIMLMGVRKQGL
CCTYCKYTVHERCVSKNIPGCVKTYSKAKRSGEVMQHAWVEGNSSVKCDRCHKSIKCYQS
VTARHCVWCRMTFHRKCELSTLCDGGELRDHILLPTSICPITRDRPGEKSDGCVSAKGEL
VMQYKIIPTPGTHPLLVLVNPKSGGRQGERILRKFHYLLNPKQVFNLDNGGPTPGLNFFR
DTPDFRVLACGGDGTVGWILDCIDKANFAKHPPVAVLPLGTGNDLARCLRWGGGYEGGSL
TKILKDIEQSPLVMLDRWHLEVIPREEVENGDQVPYSIMNNYFSIGVDASIAHRFHVMRE
KHPEKFNSRMKNKLWYFEFGTSETFAATCKKLHDHIELECDGVGVDLSNIFLEGIAILNI
PSMYGGTNLWGENKKNRAVIRESRKGVTDPKELKFCVQDLSDQLLEVVGLEGAMEMGQIY
TGLKSAGRRLAQCASVTIRTNKLLPMQVDGEPWMQPCCTIKITHKNQAPMMMGPPQKSSF
FSLRRKSRSKD
Enzyme 6 Number of Residues 791
Enzyme 6 Molecular Weight 89095.3
Enzyme 6 Theoretical pI 6.80
Enzyme 6 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • diacylglycerol kinase activity
  • ion binding
  • kinase activity
  • metal ion binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 6 General Function Involved in diacylglycerol kinase activity
Enzyme 6 Specific Function Reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 124256476 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P49619 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name DGKG_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >2376 bp
ATGGGTGAAGAACGGTGGGTCTCCCTCACTCCAGAAGAATTTGACCAACTCCAGAAATAT
TCAGAATATTCCTCCAAGAAGATAAAAGATGCCTTGACTGAATTTAATGAGGGTGGGAGC
CTCAAACAATATGACCCACATGAGCCGATTAGCTATGATGTCTTCAAGCTGTTCATGAGG
GCGTACCTGGAGGTGGACCTTCCCCAGCCACTGAGCACTCACCTCTTCCTGGCCTTCAGC
CAGAAGCCCAGACACGAGACCTCTGACCACCCGACGGAGGGAGCCAGCAACAGTGAGGCC
AACAGCGCAGATACTAATATACAGAATGCAGATAATGCCACCAAAGCAGACGAGGCCTGT
GCCCCTGATACTGAATCAAATATGGCTGAGAAGCAAGCACCAGCTGAAGACCAAGTGGCT
GCGACCCCCCTGGAACCCCCCGTCCCTCGGTCTTCAAGCTCGGAATCCCCAGTGGTATAC
CTGAAGGATGTTGTGTGCTACCTGTCCCTGCTGGAGACGGGGAGGCCTCAGGATAAGCTG
GAGTTCATGTTTCGCCTCTATGATTCAGATGAGAACGGTCTCCTGGACCAAGCGGAGATG
GATTGCATTGTCAACCAAATGCTGCATATTGCCCAGTACCTGGAGTGGGATCCCACAGAG
CTGAGGCCTATATTGAAGGAGATGCTGCAAGGGATGGACTACGACCGGGACGGCTTTGTG
TCTCTACAGGAATGGGTCCATGGAGGGATGACCACCATCCCATTGCTGGTCCTCCTGGGG
ATGGATGACTCTGGCTCCAAGGGGGATGGGCGGCACGCCTGGACCATGAAGCACTTCAAG
AAACCAACCTACTGCAACTTCTGCCATATCATGCTCATGGGCGTCCGCAAGCAAGGCCTG
TGCTGCACTTACTGTAAATACACTGTCCACGAACGCTGTGTGTCCAGAAACATTCCTGGT
TGTGTCAAAACGTACTCAAAAGCCAAAAGGAGTGGTGAGGTGATGCAGCACGCATGGGTG
GAAGGGAACTCCTCCGTCAAGTGTGACCGGTGCCACAAAAGTATCAAGTGCTACCAGAGT
GTCACCGCGCGGCACTGCGTGTGGTGCCGGATGACGTTTCACCGCAAATGTGAATTATCA
ACGTTGTGTGACGGTGGGGAACTCAGAGACCACATCTTACTGCCCACCTCCATATGCCCC
ATCACCCGGGACAGGCCAGGTGAGAAGTCTGATGGCTGCGTGTCCGCCAAGGGCGAACTT
GTCATGCAGTATAAGATCATCCCCACCCCGGGTACCCACCCCCTGCTGGTCTTGGTGAAC
CCCAAGAGTGGAGGGAGACAAGGAGAAAGAATTCTTCGGAAATTCCACTATCTGCTCAAC
CCCAAACAAGTTTTCAACCTGGACAATGGGGGGCCTACTCCAGGGTTGAACTTTTTCCGT
GATACTCCAGACTTCCGTGTTTTGGCCTGTGGTGGAGATGGGACAGTTGGCTGGATTTTG
GATTGCATTGATAAGGCCAACTTTGCAAAGCATCCACCAGTGGCTGTCCTGCCTCTTGGA
ACAGGAAATGACCTTGCCCGTTGTCTCCGCTGGGGAGGAGGTTATGAAGGGGGCAGCTTG
ACAAAAATCCTGAAAGACATTGAGCAGAGCCCCTTGGTGATGCTGGACCGCTGGCATCTG
GAAGTCATCCCCAGAGAGGAAGTGGAAAACGGGGACCAGGTCCCATACAGCATCATGAAC
AACTATTTCTCCATTGGTGTGGACGCTTCCATTGCACACAGATTCCATGTGATGAGAGAG
AAACATCCTGAAAAATTCAACAGCAGGATGAAGAACAAGCTGTGGTACTTTGAATTTGGC
ACCTCGGAGACTTTTGCAGCGACCTGCAAGAAACTCCACGACCACATTGAGTTGGAGTGT
GATGGGGTTGGGGTGGACCTGAGCAACATCTTCCTGGAAGGCATTGCCATTCTCAACATT
CCCAGCATGTACGGAGGCACCAATCTCTGGGGAGAAAACAAGAAGAACCGGGCTGTGATC
CGGGAAAGCAGGAAGGGTGTCACTGACCCCAAAGAACTGAAATTCTGCGTTCAAGACCTC
AGTGACCAGCTCCTTGAAGTGGTGGGGCTAGAAGGAGCCATGGAGATGGGGCAGATCTAC
ACCGGCCTGAAGAGTGCAGGCAGGAGGCTGGCCCAGTGCGCCTCTGTCACCATCAGGACA
AACAAGCTGCTGCCAATGCAAGTGGATGGAGAACCCTGGATGCAGCCATGTTGCACGATT
AAAATTACTCACAAGAACCAAGCGCCCATGATGATGGGGCCTCCCCAGAAGAGCAGCTTC
TTCTCGTTGAGAAGGAAGAGCCGTTCAAAAGACTAA
Enzyme 6 GenBank Gene ID NM_001346.2 Link Image
Enzyme 6 GeneCard ID DGKG Link Image
Enzyme 6 GenAtlas ID DGKG Link Image
Enzyme 6 HGNC ID HGNC:2853 Link Image
Enzyme 6 Chromosome Location 3
Enzyme 6 Locus 3q27.2-q27.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Kai M, Sakane F, Imai S, Wada I, Kanoh H: Molecular cloning of a diacylglycerol kinase isozyme predominantly expressed in human retina with a truncated and inactive enzyme expression in most other human cells. J Biol Chem. 1994 Jul 15;269(28):18492-8. [PubMed Link Image]
  2. Stohr H, Klein J, Gehrig A, Koehler MR, Jurklies B, Kellner U, Leo-Kottler B, Schmid M, Weber BH: Mapping and genomic characterization of the gene encoding diacylglycerol kinase gamma (DAGK3): assessment of its role in dominant optic atrophy (OPA1). Hum Genet. 1999 Jan;104(1):99-105. [PubMed Link Image]
  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. 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]
  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. 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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5458
Enzyme 7 Name Hepatic triacylglycerol lipase
Enzyme 7 Synonyms
  1. HL
  2. Hepatic lipase
  3. Lipase member C
Enzyme 7 Gene Name LIPC
Enzyme 7 Protein Sequence >Hepatic triacylglycerol lipase
MDTSPLCFSILLVLCIFIQSSALGQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQ
GCQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQMVAALKSQPAQPVNVGLV
DWITLAHDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSS
IGGTHKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGH
YDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQTIKCSHERSVHLFIDSLLHAGTQSMAY
PCGDMNSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSKRLFLVTRAQSPFKVYHYQLKIQF
INQTETPIQTTFTMSLLGTKEKMQKIPITLGKGIASNKTYSFLITLDVDIGELIMIKFKW
ENSAVWANVWDTVQTIIPWSTGPRHSGLVLKTIRVKAGETQQRMTFCSENTDDLLLRPTQ
EKIFVKCEIKSKTSKRKIR
Enzyme 7 Number of Residues 499
Enzyme 7 Molecular Weight 55880.1
Enzyme 7 Theoretical pI 9.37
Enzyme 7 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • triglyceride lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 7 General Function Involved in catalytic activity
Enzyme 7 Specific Function Hepatic lipase has the capacity to catalyze hydrolysis of phospholipids, mono-, di-, and triglycerides, and acyl-CoA thioesters. It is an important enzyme in HDL metabolism. Hepatic lipase binds heparin
Enzyme 7 Pathways
Enzyme 7 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-22
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 194097335 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P11150 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name LIPC_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1500 bp
ATGGACACAAGTCCCCTGTGTTTCTCCATTCTGTTGGTTTTATGCATCTTTATCCAATCA
AGTGCCCTTGGACAAAGCCTGAAACCAGAGCCATTTGGAAGAAGAGCTCAAGCTGTTGAA
ACAAACAAAACGCTGCATGAGATGAAGACCAGATTCCTGCTCTTTGGAGAAACCAATCAG
GGCTGTCAGATTCGAATCAATCATCCGGACACGTTACAGGAGTGCGGCTTCAACTCCTCC
CTGCCTCTGGTGATGATAATCCACGGGTGGTCGGTGGACGGCGTGCTAGAAAACTGGATC
TGGCAGATGGTGGCCGCGCTGAAGTCTCAGCCGGCCCAGCCAGTGAACGTGGGGCTGGTG
GACTGGATCACCCTGGCCCACGACCACTACACCATCGCCGTCCGCAACACCCGCCTTGTG
GGCAAGGAGGTCGCGGCTCTTCTCCGGTGGCTGGAGGAATCTGTGCAACTCTCTCGAAGC
CATGTTCACCTAATTGGGTACAGCCTGGGTGCACACGTGTCAGGATTTGCCGGCAGTTCC
ATCGGTGGAACGCACAAGATTGGGAGAATCACAGGGCTGGATGCCGCGGGACCTTTGTTT
GAGGGAAGTGCCCCCAGCAATCGTCTTTCTCCAGATGATGCCAATTTTGTGGATGCCATT
CATACCTTTACCCGGGAGCACATGGGCCTGAGCGTGGGCATCAAACAGCCCATAGGACAC
TATGACTTCTATCCCAACGGGGGCTCCTTCCAGCCTGGCTGCCACTTCCTAGAGCTCTAC
AGACATATTGCCCAGCACGGCTTCAATGCCATCACCCAGACCATAAAATGCTCCCACGAG
CGATCGGTGCACCTTTTCATCGACTCCTTGCTGCACGCCGGCACGCAGAGCATGGCCTAC
CCGTGTGGTGACATGAACAGCTTCAGCCAGGGCCTGTGCCTGAGCTGCAAGAAGGGCCGC
TGCAACACGCTGGGCTACCACGTCCGCCAGGAGCCGCGGAGCAAGAGCAAGAGGCTCTTC
CTCGTAACGCGAGCCCAGTCCCCCTTCAAAGTTTATCATTACCAGTTCAAGATCCAGTTC
ATCAACCAAACTGAGACACCAATACAAACAACTTTTACCATGTCACTACTCGGAACAAAA
GAGAAAATGCAGAAAATTCCCATCACTCTGGGCAAAGGAATTGCTAGTAATAAAACGTAT
TCCTTTCTTATCACGCTGGATGTGGATATCGGCGAGCTGATCATGATCAAGTTCAAGTGG
GAAAACAGTGCAGTGTGGGCCAATGTCTGGGACACGGTCCAGACCATCATCCCATGGAGC
ACAGGGCCGCGCCACTCAGGCCTCGTTCTGAAGACGATCAGAGTCAAAGCAGGAGAAACC
CAGCAAAGAATGACATTTTGTTCAGAAAACACAGATGACCTACTACTTCGCCCAACCCAG
GAAAAAATCTTCGTGAAATGTGAAATAAAGTCTAAAACATCAAAGCGAAAGATCAGATGA
Enzyme 7 GenBank Gene ID NM_000236.2 Link Image
Enzyme 7 GeneCard ID LIPC Link Image
Enzyme 7 GenAtlas ID LIPC Link Image
Enzyme 7 HGNC ID HGNC:6619 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 15q21-q23
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Martin GA, Busch SJ, Meredith GD, Cardin AD, Blankenship DT, Mao SJ, Rechtin AE, Woods CW, Racke MM, Schafer MP, et al.: Isolation and cDNA sequence of human postheparin plasma hepatic triglyceride lipase. J Biol Chem. 1988 Aug 5;263(22):10907-14. [PubMed Link Image]
  2. Stahnke G, Sprengel R, Augustin J, Will H: Human hepatic triglyceride lipase: cDNA cloning, amino acid sequence and expression in a cultured cell line. Differentiation. 1987;35(1):45-52. [PubMed Link Image]
  3. Datta S, Luo CC, Li WH, VanTuinen P, Ledbetter DH, Brown MA, Chen SH, Liu SW, Chan L: Human hepatic lipase. Cloned cDNA sequence, restriction fragment length polymorphisms, chromosomal localization, and evolutionary relationships with lipoprotein lipase and pancreatic lipase. J Biol Chem. 1988 Jan 25;263(3):1107-10. [PubMed Link Image]
  4. Cai SJ, Wong DM, Chen SH, Chan L: Structure of the human hepatic triglyceride lipase gene. Biochemistry. 1989 Nov 14;28(23):8966-71. [PubMed Link Image]
  5. Ameis D, Stahnke G, Kobayashi J, McLean J, Lee G, Buscher M, Schotz MC, Will H: Isolation and characterization of the human hepatic lipase gene. J Biol Chem. 1990 Apr 25;265(12):6552-5. [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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Tiebel O, Gehrisch S, Pietzsch J, Gromeier S, Jaross W: 18 bp insertion/duplication with internal missense mutation in human hepatic lipase gene exon 3. Mutations in brief no. 181. Online. Hum Mutat. 1998;12(3):216. [PubMed Link Image]
  9. Takagi A, Ikeda Y, Mori A, Ashida Y, Yamamoto A: Identification of a BstNI polymorphism in exon 9 of the human hepatic triglyceride lipase gene. Mol Cell Probes. 1996 Aug;10(4):313-4. [PubMed Link Image]
  10. Todorova B, Kubaszek A, Pihlajamaki J, Lindstrom J, Eriksson J, Valle TT, Hamalainen H, Ilanne-Parikka P, Keinanen-Kiukaanniemi S, Tuomilehto J, Uusitupa M, Laakso M: The G-250A promoter polymorphism of the hepatic lipase gene predicts the conversion from impaired glucose tolerance to type 2 diabetes mellitus: the Finnish Diabetes Prevention Study. J Clin Endocrinol Metab. 2004 May;89(5):2019-23. [PubMed Link Image]
  11. Grarup N, Andreasen CH, Andersen MK, Albrechtsen A, Sandbaek A, Lauritzen T, Borch-Johnsen K, Jorgensen T, Schmitz O, Hansen T, Pedersen O: The -250G>A promoter variant in hepatic lipase associates with elevated fasting serum high-density lipoprotein cholesterol modulated by interaction with physical activity in a study of 16,156 Danish subjects. J Clin Endocrinol Metab. 2008 Jun;93(6):2294-9. Epub 2008 Mar 25. [PubMed Link Image]
  12. Hegele RA, Tu L, Connelly PW: Human hepatic lipase mutations and polymorphisms. Hum Mutat. 1992;1(4):320-4. [PubMed Link Image]
  13. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  14. 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5460
Enzyme 8 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3
Enzyme 8 Synonyms
  1. Phosphoinositide phospholipase C-beta-3
  2. Phospholipase C-beta-3
  3. PLC-beta-3
Enzyme 8 Gene Name PLCB3
Enzyme 8 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 8 Number of Residues 1234
Enzyme 8 Molecular Weight 138797.7
Enzyme 8 Theoretical pI 5.66
Enzyme 8 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 8 General Function Involved in calcium ion binding
Enzyme 8 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 8 Pathways
Enzyme 8 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 148745659 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q01970 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PLCB3_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 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 8 GenBank Gene ID BC142681 Link Image
Enzyme 8 GeneCard ID PLCB3 Link Image
Enzyme 8 GenAtlas ID PLCB3 Link Image
Enzyme 8 HGNC ID HGNC:9056 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 11q13
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5461
Enzyme 9 Name Pancreatic lipase-related protein 1
Enzyme 9 Synonyms
  1. PL-RP1
Enzyme 9 Gene Name PNLIPRP1
Enzyme 9 Protein Sequence >Pancreatic lipase-related protein 1
MLIFWTITLFLLGAAKGKEVCYEDLGCFSDTEPWGGTAIRPLKILPWSPEKIGTRFLLYT
NENPNNFQILLLSDPSTIEASNFQMDRKTRFIIHGFIDKGDESWVTDMCKKLFEVEEVNC
ICVDWKKGSQATYTQAANNVRVVGAQVAQMLDILLTEYSYPPSKVHLIGHSLGAHVAGEA
GSKTPGLSRITGLDPVEASFESTPEEVRLDPSDADFVDVIHTDAAPLIPFLGFGTNQQMG
HLDFFPNGGESMPGCKKNALSQIVDLDGIWAGTRDFVACNHLRSYKYYLESILNPDGFAA
YPCTSYKSFESDKCFPCPDQGCPQMGHYADKFAGRTSEEQQKFFLNTGEASNFARWRYGV
SITLSGRTATGQIKVALFGNKGNTHQYSIFRGILKPGSTHSYEFDAKLDVGTIEKVKFLW
NNNVINPTLPKVGATKITVQKGEEKTVYNFCSEDTVREDTLLTLTPC
Enzyme 9 Number of Residues 467
Enzyme 9 Molecular Weight 51847.4
Enzyme 9 Theoretical pI 5.47
Enzyme 9 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • triglyceride lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 9 General Function Involved in catalytic activity
Enzyme 9 Specific Function Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Enzyme 9 Pathways
Enzyme 9 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-17
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 5453920 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P54315 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name LIPR1_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1404 bp
ATGCTGATCTTCTGGACAATCACACTTTTCCTGCTGGGAGCAGCCAAAGGAAAAGAAGTT
TGCTATGAGGACCTCGGGTGCTTTTCTGACACTGAGCCCTGGGGCGGGACAGCAATCAGG
CCCCTGAAAATTCTCCCCTGGAGCCCTGAGAAGATCGGCACCCGCTTCCTGCTGTACACC
AATGAAAACCCAAACAACTTTCAAATTCTCCTCCTCTCTGATCCATCAACAATTGAGGCA
TCAAATTTTCAAATGGACAGAAAGACCCGGTTCATCATCCATGGCTTCATAGACAAAGGA
GATGAGAGCTGGGTGACAGACATGTGCAAGAAACTGTTCGAGGTGGAGGAGGTGAACTGC
ATCTGCGTGGACTGGAAGAAGGGCTCCCAAGCCACCTACACACAGGCTGCCAACAACGTG
CGAGTGGTGGGCGCCCAGGTGGCCCAGATGCTCGACATCCTCTTGACAGAGTATAGCTAC
CCCCCTTCCAAAGTTCACCTCATTGGCCACAGCCTGGGAGCCCACGTGGCTGGAGAGGCA
GGAAGCAAGACTCCAGGCCTGAGCAGGATTACAGGGTTGGATCCTGTAGAAGCAAGTTTC
GAGAGTACTCCTGAAGAGGTGCGACTTGATCCCTCTGATGCTGACTTTGTTGATGTGATT
CACACGGATGCAGCTCCCCTGATCCCATTCTTGGGTTTTGGAACGAACCAACAGATGGGT
CATCTTGACTTCTTCCCCAATGGAGGAGAGAGCATGCCGGGATGCAAGAAGAATGCCCTG
TCTCAGATCGTGGATCTAGATGGCATCTGGGCGGGAACCCGGGACTTTGTGGCTTGCAAT
CACCTAAGAAGCTACAAGTATTACTTGGAAAGCATCCTCAATCCCGATGGGTTTGCTGCA
TATCCCTGCACTTCCTACAAGTCCTTTGAGTCTGACAAGTGCTTCCCGTGTCCAGATCAA
GGATGCCCACAGATGGGTCACTATGCTGATAAATTTGCTGGCAGGACAAGTGAAGAGCAG
CAGAAATTCTTCTTGAACACAGGAGAGGCTAGCAATTTCGCTCGCTGGAGATATGGGGTT
TCCATCACACTGTCTGGAAGAACAGCCACTGGTCAGATCAAAGTTGCTTTGTTTGGAAAT
AAGGGAAACACTCACCAGTACAGCATCTTCAGGGGGATTCTCAAACCAGGCTCAACCCAT
TCCTATGAGTTTGATGCAAAGCTGGATGTTGGAACAATTGAGAAAGTCAAGTTTCTTTGG
AATAACAATGTGATAAATCCAACCCTCCCCAAAGTGGGTGCCACCAAGATCACTGTGCAA
AAGGGAGAAGAGAAGACAGTGTACAACTTCTGTAGCGAAGACACAGTGCGGGAAGACACG
CTGCTCACCCTCACGCCCTGCTAA
Enzyme 9 GenBank Gene ID NM_006229.2 Link Image
Enzyme 9 GeneCard ID PNLIPRP1 Link Image
Enzyme 9 GenAtlas ID PNLIPRP1 Link Image
Enzyme 9 HGNC ID HGNC:9156 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 10q25.3
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Giller T, Buchwald P, Blum-Kaelin D, Hunziker W: Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J Biol Chem. 1992 Aug 15;267(23):16509-16. [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. 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 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5462
Enzyme 10 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2
Enzyme 10 Synonyms
  1. Phosphoinositide phospholipase C-gamma-2
  2. Phospholipase C-IV
  3. PLC-IV
  4. Phospholipase C-gamma-2
  5. PLC-gamma-2
Enzyme 10 Gene Name PLCG2
Enzyme 10 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 10 Number of Residues 1265
Enzyme 10 Molecular Weight 147868.7
Enzyme 10 Theoretical pI 6.60
Enzyme 10 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 10 General Function Involved in phosphoinositide phospholipase C activity
Enzyme 10 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 10 Pathways
Enzyme 10 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 117320537 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P16885 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PLCG2_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 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 10 GenBank Gene ID NM_002661.2 Link Image
Enzyme 10 GeneCard ID PLCG2 Link Image
Enzyme 10 GenAtlas ID PLCG2 Link Image
Enzyme 10 HGNC ID HGNC:9066 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 16q24.1
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5463
Enzyme 11 Name Lipid phosphate phosphohydrolase 2
Enzyme 11 Synonyms
  1. PAP2-gamma
  2. PAP2-G
  3. Phosphatidate phosphohydrolase type 2c
  4. Phosphatidic acid phosphatase 2c
  5. PAP-2c
  6. PAP2c
Enzyme 11 Gene Name PPAP2C
Enzyme 11 Protein Sequence >Lipid phosphate phosphohydrolase 2
MQRRWVFVLLDVLCLLVASLPFAILTLVNAPYKRGFYCGDDSIRYPYRPDTITHGLMAGV
TITATVILVSAGEAYLVYTDRLYSRSDFNNYVAAVYKVLGTFLFGAAVSQSLTDLAKYMI
GRLRPNFLAVCDPDWSRVNCSVYVQLEKVCRGNPADVTEARLSFYSGHSSFGMYCMVFLA
LYVQARLCWKWARLLRPTVQFFLVAFALYVGYTRVSDYKHHWSDVLVGLLQGALVAALTV
CYISDFFKARPPQHCLKEEELERKPSLSLTLTLGEADHNHYGYPHSSS
Enzyme 11 Number of Residues 288
Enzyme 11 Molecular Weight 32573.4
Enzyme 11 Theoretical pI 8.44
Enzyme 11 GO Classification
Function
  • catalytic activity
Process
Component
  • cell part
  • membrane
Enzyme 11 General Function Involved in catalytic activity
Enzyme 11 Specific Function Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1- phosphate (S-1-P). The relative catalytic efficiency is PA > C-1-P > LPA > S-1-P
Enzyme 11 Pathways
Enzyme 11 Reactions
  • a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate [RN:R02239]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • 5-25 52-72 88-108 163-183 197-217 227-247
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 4505977 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID O43688 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name LPP2_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >867 bp
ATGCAGCGGAGGTGGGTCTTCGTGCTGCTCGACGTGCTGTGCTTACTGGTCGCCTCCCTG
CCCTTCGCTATCCTGACGCTGGTGAACGCCCCGTACAAGCGAGGATTTTACTGCGGGGAT
GACTCCATCCGGTACCCCTACCGTCCAGATACCATCACCCACGGGCTCATGGCTGGGGTC
ACCATCACGGCCACCGTCATCCTTGTCTCGGCCGGGGAAGCCTACCTGGTGTACACAGAC
CGGCTCTATTCTCGCTCGGACTTCAACAACTACGTGGCTGCTGTATACAAGGTGCTGGGG
ACCTTCCTGTTTGGGGCTGCCGTGAGCCAGTCTCTGACAGACCTGGCCAAGTACATGATT
GGGCGTCTGAGGCCCAACTTCCTAGCCGTCTGCGACCCCGACTGGAGCCGGGTCAACTGC
TCGGTCTATGTGCAGCTGGAGAAGGTGTGCAGGGGAAACCCTGCTGATGTCACCGAGGCC
AGGTTGTCTTTCTACTCGGGACACTCTTCCTTTGGGATGTACTGCATGGTGTTCTTGGCG
CTGTATGTGCAGGCACGACTCTGTTGGAAGTGGGCACGGCTGCTGCGACCCACAGTCCAG
TTCTTCCTGGTGGCCTTTGCCCTCTACGTGGGCTACACCCGCGTGTCTGATTACAAACAC
CACTGGAGCGATGTCCTTGTTGGCCTCCTGCAGGGGGCACTGGTGGCTGCCCTCACTGTC
TGCTACATCTCAGACTTCTTCAAAGCCCGACCCCCACAGCACTGTCTGAAGGAGGAGGAG
CTGGAACGGAAGCCCAGCCTGTCACTGACGTTGACCCTGGGCGAGGCTGACCACAACCAC
TATGGATACCCGCACTCCTCCTCCTGA
Enzyme 11 GenBank Gene ID NM_003712.2 Link Image
Enzyme 11 GeneCard ID PPAP2C Link Image
Enzyme 11 GenAtlas ID PPAP2C Link Image
Enzyme 11 HGNC ID HGNC:9230 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 19p13
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Leung DW, Tompkins CK, White T: Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. DNA Cell Biol. 1998 Apr;17(4):377-85. [PubMed Link Image]
  2. Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed Link Image]
  3. Hooks SB, Ragan SP, Lynch KR: Identification of a novel human phosphatidic acid phosphatase type 2 isoform. FEBS Lett. 1998 May 8;427(2):188-92. [PubMed Link Image]
  4. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5464
Enzyme 12 Name Patatin-like phospholipase domain-containing protein 3
Enzyme 12 Synonyms
  1. Acylglycerol O-acyltransferase
  2. Adiponutrin
  3. Calcium-independent phospholipase A2-epsilon
  4. iPLA2-epsilon
Enzyme 12 Gene Name PNPLA3
Enzyme 12 Protein Sequence >Patatin-like phospholipase domain-containing protein 3
MYDAERGWSLSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALHCVGVLSGI
PLEQTLQVLSDLVRKARSRNIGIFHPSFNLSKFLRQGLCKCLPANVHQLISGKIGISLTR
VSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDGGVSDNVPFIDAKT
TITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLR
GYLDAFRFLEEKGICNRPQPGLKSSSEGMDPEVAMPSWANMSLDSSPESAALAVRLEGDE
LLDHLRLSILPWDESILDTLSPRLATALSEEMKDKGGYMSKICNLLPIRIMSYVMLPCTL
PVESAIAIVQRLVTWLPDMPDDVLWLQWVTSQVFTRVLMCLLPASRSQMPVSSQQASPCT
PEQDWPCWTPCSPKGCPAETKAEATPRSILRSSLNFFLGNKVPAGAEGLSTFPSFSLEKS
L
Enzyme 12 Number of Residues 481
Enzyme 12 Molecular Weight 52864.6
Enzyme 12 Theoretical pI 6.68
Enzyme 12 GO Classification
Function
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 12 General Function Involved in metabolic process
Enzyme 12 Specific Function Multifunctional enzyme which has both triacylglycerol lipase and acylglycerol O-acyltransferase activities
Enzyme 12 Pathways
Enzyme 12 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 42-62
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 17059636 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9NST1 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name PLPL3_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1446 bp
ATGTACGACGCAGAGCGCGGCTGGAGCTTGTCCTTCGCGGGCTGCGGCTTCCTGGGCTTC
TACCACGTCGGGGCGACCCGCTGCCTGAGCGAGCACGCCCCGCACCTCCTCCGCGACGCG
CGCATGTTGTTCGGCGCTTCGGCCGGGGCGTTGCACTGCGTCGGCGTCCTCTCCGGTATC
CCGCTGGAGCAGACTCTGCAGGTCCTCTCAGATCTTGTGCGGAAGGCCAGGAGTCGGAAC
ATTGGCATCTTCCATCCATCCTTCAACTTAAGCAAGTTCCTCCGACAGGGTCTCTGCAAA
TGCCTCCCGGCCAATGTCCACCAGCTCATCTCCGGCAAAATAGGCATCTCTCTTACCAGA
GTGTCTGATGGGGAAAACGTTCTGGTGTCTGACTTTCGGTCCAAAGACGAAGTCGTGGAT
GCCTTGGTATGTTCCTGCTTCATCCCCTTCTACAGTGGCCTTATCCCTCCTTCCTTCAGA
GGCGTGCGATATGTGGATGGAGGAGTGAGTGACAACGTACCCTTCATTGATGCCAAAACA
ACCATCACCGTGTCCCCCTTCTATGGGGAGTACGACATCTGCCCTAAAGTCAAGTCCACG
AACTTTCTTCATGTGGACATCACCAAGCTCAGTCTACGCCTCTGCACAGGGAACCTCTAC
CTTCTCTCGAGAGCTTTTGTCCCCCCGGATCTCAAGGTGCTGGGAGAGATATGCCTTCGA
GGATATTTGGATGCATTCAGGTTCTTGGAAGAGAAGGGCATCTGCAACAGGCCCCAGCCA
GGCCTGAAGTCATCCTCAGAAGGGATGGATCCTGAGGTCGCCATGCCCAGCTGGGCAAAC
ATGAGTCTGGATTCTTCCCCGGAGTCGGCTGCCTTGGCTGTGAGGCTGGAGGGAGATGAG
CTGCTAGACCACCTGCGTCTCAGCATCCTGCCCTGGGATGAGAGCATCCTGGACACCCTC
TCGCCCAGGCTCGCTACAGCACTGAGTGAAGAAATGAAAGACAAAGGTGGATACATGAGC
AAGATTTGCAACTTGCTACCCATTAGGATAATGTCTTATGTAATGCTGCCCTGTACCCTG
CCTGTGGAATCTGCCATTGCGATTGTCCAGAGACTGGTGACATGGCTTCCAGATATGCCC
GACGATGTCCTGTGGTTGCAGTGGGTGACCTCACAGGTGTTCACTCGAGTGCTGATGTGT
CTGCTCCCCGCCTCCAGGTCCCAAATGCCAGTGAGCAGCCAACAGGCCTCCCCATGCACA
CCTGAGCAGGACTGGCCCTGCTGGACTCCCTGCTCCCCCAAGGGCTGTCCAGCAGAGACC
AAAGCAGAGGCCACCCCGCGGTCCATCCTCAGGTCCAGCCTGAACTTCTTCTTGGGCAAT
AAAGTACCTGCTGGTGCTGAGGGGCTCTCCACCTTTCCCAGTTTTTCACTAGAGAAGAGT
CTGTGA
Enzyme 12 GenBank Gene ID AL138578 Link Image
Enzyme 12 GeneCard ID PNPLA3 Link Image
Enzyme 12 GenAtlas ID PNPLA3 Link Image
Enzyme 12 HGNC ID HGNC:18590 Link Image
Enzyme 12 Chromosome Location 2
Enzyme 12 Locus 22q13.31
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Collins JE, Goward ME, Cole CG, Smink LJ, Huckle EJ, Knowles S, Bye JM, Beare DM, Dunham I: Reevaluating human gene annotation: a second-generation analysis of chromosome 22. Genome Res. 2003 Jan;13(1):27-36. [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. 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. 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]
  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. Jenkins CM, Mancuso DJ, Yan W, Sims HF, Gibson B, Gross RW: Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J Biol Chem. 2004 Nov 19;279(47):48968-75. Epub 2004 Sep 10. [PubMed Link Image]
  7. Liu YM, Moldes M, Bastard JP, Bruckert E, Viguerie N, Hainque B, Basdevant A, Langin D, Pairault J, Clement K: Adiponutrin: A new gene regulated by energy balance in human adipose tissue. J Clin Endocrinol Metab. 2004 Jun;89(6):2684-9. [PubMed Link Image]
  8. Johansson LE, Lindblad U, Larsson CA, Rastam L, Ridderstrale M: Polymorphisms in the adiponutrin gene are associated with increased insulin secretion and obesity. Eur J Endocrinol. 2008 Nov;159(5):577-83. Epub 2008 Aug 26. [PubMed Link Image]
  9. Romeo S, Kozlitina J, Xing C, Pertsemlidis A, Cox D, Pennacchio LA, Boerwinkle E, Cohen JC, Hobbs HH: Genetic variation in PNPLA3 confers susceptibility to nonalcoholic fatty liver disease. Nat Genet. 2008 Dec;40(12):1461-5. Epub 2008 Sep 25. [PubMed Link Image]
  10. Kotronen A, Johansson LE, Johansson LM, Roos C, Westerbacka J, Hamsten A, Bergholm R, Arkkila P, Arola J, Kiviluoto T, Fisher RM, Ehrenborg E, Orho-Melander M, Ridderstrale M, Groop L, Yki-Jarvinen H: A common variant in PNPLA3, which encodes adiponutrin, is associated with liver fat content in humans. Diabetologia. 2009 Jun;52(6):1056-60. Epub 2009 Feb 18. [PubMed Link Image]
  11. He S, McPhaul C, Li JZ, Garuti R, Kinch L, Grishin NV, Cohen JC, Hobbs HH: A sequence variation (I148M) in PNPLA3 associated with nonalcoholic fatty liver disease disrupts triglyceride hydrolysis. J Biol Chem. 2010 Feb 26;285(9):6706-15. Epub 2009 Dec 23. [PubMed Link Image]
  12. Sookoian S, Castano GO, Burgueno AL, Gianotti TF, Rosselli MS, Pirola CJ: A nonsynonymous gene variant in the adiponutrin gene is associated with nonalcoholic fatty liver disease severity. J Lipid Res. 2009 Oct;50(10):2111-6. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5465
Enzyme 13 Name Diacylglycerol kinase alpha
Enzyme 13 Synonyms
  1. DAG kinase alpha
  2. 80 kDa diacylglycerol kinase
  3. Diglyceride kinase alpha
  4. DGK-alpha
Enzyme 13 Gene Name DGKA
Enzyme 13 Protein Sequence >Diacylglycerol kinase alpha
MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIY
LEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFK
LYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEW
VRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKY
TVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHC
VWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNL
STSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRL
FKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQ
NLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIM
REKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVL
NIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLE
GAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDGEPWMQTPCTIKITHKNQMPML
MGPPPRSTNFFGFLS
Enzyme 13 Number of Residues 735
Enzyme 13 Molecular Weight 82629.5
Enzyme 13 Theoretical pI 6.71
Enzyme 13 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • diacylglycerol kinase activity
  • ion binding
  • kinase activity
  • metal ion binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 13 General Function Involved in diacylglycerol kinase activity
Enzyme 13 Specific Function Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity
Enzyme 13 Pathways
Enzyme 13 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 30823 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P23743 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name DGKA_HUMAN Link Image
Enzyme 13 PDB ID 1TUZ Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >2208 bp
ATGGCCAAGGAGAGGGGCCTAATAAGCCCCAGTGATTTTGCCCAGCTGCAAAAATACATG
GAATACTCCACCAAAAAGGTCAGTGATGTCCTAAAGCTCTTCGAGGATGGCGAGATGGCT
AAATATGTCCAAGGAGATGCCATTGGGTACGAGGGATTCCAGCAATTCCTGAAAATCTAT
CTCGAAGTGGATAATGTTCCCAGACACCTAAGCCTGGCACTGTTTCAATCCTTTGAGACT
GGTCACTGCTTAAATGAGACAAATGTGACAAAAGATGTGGTGTGTCTCAATGATGTTTCC
TGCTACTTTTCCCTTCTGGAGGGTGGTCGGCCAGAAGACAAGTTAGAATTCACCTTCAAG
CTGTACGACACGGACAGAAATGGGATCCTGGACAGCTCAGAAGTGGACAAAATTATCCTA
CAGATGATGCGAGTGGCTGAATACCTGGATTGGGATGTGTCTGAGCTGAGGCCGATTCTT
CAGGAGATGATGAAAGAGATTGACTATGATGGCAGTGGCTCTGTCTCTCAAGCTGAGTGG
GTCCGGGCTGGGGCCACCACCGTGCCACTGCTAGTGCTGCTGGGTCTGGAGATGACTCTG
AAGGACGACGGACAGCACATGTGGAGGCCCAAGAGGTTCCCCAGACCAGTCTACTGCAAT
CTGTGCGAGTCAAGCATTGGTCTTGGCAAACAGGGACTGAGCTGTAACCTCTGTAAGTAC
ACTGTTCACGACCAGTGTGCCATGAAAGCCCTGCCTTGTGAAGTCAGCACCTATGCCAAG
TCTCGGAAGGACATTGGTGTCCAATCACATGTGTGGGTGCGAGGAGGCTGTGAGTCCGGG
CGCTGCGACCGCTGTCAGAAAAAGATCCGGATCTACCACAGTCTGACCGGGCTGCATTGT
GTATGGTGCCACCTAGAGATCCACGATGACTGCCTGCAAGCGGTGGGCCATGAGTGTGAC
TGTGGGCTGCTCCGGGATCACATCCTGCCTCCATCTTCCATCTATCCCAGTGTCCTGGCC
TCTGGACCGGATCGTAAAAATAGCAAAACAAGCCAGAAGACCATGGATGATTTAAATTTG
AGCACCTCTGAGGCTCTGCGGATTGACCCTGTTCCTAACACCCACCCACTTCTCGTCTTT
GTCAATCCTAAGAGTGGCGGGAAGCAGGGGCAGAGGGTGCTCTGGAAGTTCCAGTATATA
TTAAACCCTCGACAGGTGTTCAACCTCCTAAAGGATGGTCCTGAGATAGGGCTCCGATTA
TTCAAGGATGTTCCTGATAGCCGGATTTTGGTGTGTGGTGGAGACGGCACAGTAGGCTGG
ATTCTAGAGACCATTGACAAAGCTAACTTGCCAGTTTTGCCTCCTGTTGCTGTGTTGCCC
CTGGGTACTGGAAATGATCTGGCTCGATGCCTAAGATGGGGAGGAGGTTATGAAGGACAG
AATCTGGCAAAGATCCTCAAGGATTTAGAGATGAGTAAAGTGGTACATATGGATCGATGG
TCTGTGGAGGTGATACCTCAACAAACTGAAGAAAAAAGTGACCCAGTCCCCTTTCAAATC
ATCAATAACTACTTCTCTATTGGCGTGGATGCCTCTATTGCTCATCGATTCCACATCATG
CGAGAGAAATATCCGGAGAAGTTCAACAGCAGAATGAAGAACAAGCTATGGTACTTCGAA
TTTGCCACATCTGAATCCATCTTCTCAACATGCAAAAAGCTGGAGGAGTCTTTGACAGTT
GAGATCTGTGGGAAACCGCTGGATCTGAGCAACCTGTCCCTAGAAGGCATCGCAGTGCTA
AACATCCCTAGCATGCATGGTGGCTCCAACCTCTGGGGTGATACCAGGAGACCCCATGGG
GATATCTATGGGATCAACCAGGCCTTAGGTGCTACAGCTAAAGTCATCACCGACCCTGAT
ATCCTGAAAACCTGTGTACCAGACCTAAGTGACAAGAGACTGGAAGTGGTTGGGCTGGAG
GGTGCAATTGAGATGGGCCAAATCTATACCAAGCTCAAGAATGCTGGACGTCGGCTGGCC
AAGTGCTCTGAGATCACCTTCCACACCACAAAAACCCTTCCCATGCAAATTGACGTAGAA
CCCTGGATGCAGACGCCCTGTACAATCAAGATCACCCACAAGAACCAGATGCCCATGCTC
ATGGGCCCACCCCCCCGCTCCACCAATTTCTTTGGCTTCTTGAGCTAA
Enzyme 13 GenBank Gene ID X62535 Link Image
Enzyme 13 GeneCard ID DGKA Link Image
Enzyme 13 GenAtlas ID DGKA Link Image
Enzyme 13 HGNC ID HGNC:2849 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 12q13.3
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Schaap D, de Widt J, van der Wal J, Vandekerckhove J, van Damme J, Gussow D, Ploegh HL, van Blitterswijk WJ, van der Bend RL: Purification, cDNA-cloning and expression of human diacylglycerol kinase. FEBS Lett. 1990 Nov 26;275(1-2):151-8. [PubMed Link Image]
  2. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Hart TC, Champagne C, Zhou J, Van Dyke TE: Assignment of the gene for diacylglycerol kinase (DAGK) to human chromosome 12. Mamm Genome. 1994 Feb;5(2):123-4. [PubMed Link Image]
  5. Hart TC, Zhou J, Champagne C, Van Dyke TE, Rao PN, Pettenati MJ: Assignment of the human diacylglycerol kinase gene (DAGK) to 12q13.3 using fluorescence in situ hybridization analysis. Genomics. 1994 Jul 1;22(1):246-7. [PubMed Link Image]
  6. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  7. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5466
Enzyme 14 Name Diacylglycerol kinase delta
Enzyme 14 Synonyms
  1. DAG kinase delta
  2. 130 kDa diacylglycerol kinase
  3. Diglyceride kinase delta
  4. DGK-delta
Enzyme 14 Gene Name DGKD
Enzyme 14 Protein Sequence >Diacylglycerol kinase delta
MAAAAGAPPPGPPQPPPPPPPEESSDSEPEAEPGSPQKLIRKVSTSGQIRQKTIIKEGML
TKQNNSFQRSKRRYFKLRGRTLYYAKTAKSIIFDEVDLTDASVAESSTKNVNNSFTVITP
CRKLILCADNRKEMEDWIAALKTVQNREHFEPTQYSMDHFSGMHNWYACSHARPTYCNVC
REALSGVTSHGLSCEVCKFKAHKRCAVRATNNCKWTTLASIGKDIIEDADGIAMPHQWLE
GNLPVSAKCTVCDKTCGSVLRLQDWRCLWCKAMVHTSCKESLLTKCPLGLCKVSVIPPTA
LNSIDSDGFWKASCPPSCTSPLLVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPH
LGLRLFQKFDTFRILVCGGDGSVGWVLSEIDSLNLHKQCQLGVLPLGTGNDLARVLGWGS
ACDDDTQLPQILEKLERASTKMLDRWSVMAYEAKLPRQASSSTVTEDFSEDSEVQQILFY
EDSVAAHLSKILTSDQHSVVISSAKVLCETVKDFVARVGKAYEKTTESSEESEVMAKKCS
VLKEKLDSLLKTLDDESQASSSLPNPPPTIAEEAEDGDGSGSICGSTGDRLVASACPARP
QIFRPREQLMLRANSLKKAIRQIIEHTEKAVDEQNAQTQEQEGFVLGLSESEEKMDHRVC
PPLSHSESFGVPKGRSQRKVSKSPCEKLISKGSLSLGSSASLPPQPGSRDGLPALNTKIL
YPNVRAGMSGSLPGGSVISRLLINADPFNSEPETLEYYTEKCVMNNYFGIGLDAKISLDF
NNKRDEHPEKCRSRTKNMMWYGVLGTKELLHRTYKNLEQKVLLECDGRPIPLPSLQGIAV
LNIPSYAGGTNFWGGTKEDDTFAAPSFDDKILEVVAVFGSMQMAVSRVIRLQHHRIAQCR
TVKISILGDEGVPVQVDGEAWVQPPGYIRIVHKNRAQTLTRDRAFESTLKSWEDKQKCEL
PRPPSCSLHPEMLSEEEATQMDQFGQAAGVLIHSIREIAQSHRDMEQELAHAVNASSKSM
DRVYGKPRTTEGLNCSFVLEMVNNFRALRSETELLLSGKMALQLDPPQKEQLGSALAEMD
RQLRRLADTPWLCQSAEPGDEESVMLDLAKRSRSGKFRLVTKFKKEKNNKNKEAHSSLGA
PVHLWGTEEVAAWLEHLSLCEYKDIFTRHDIRGSELLHLERRDLKDLGVTKVGHMKRILC
GIKELSRSAPAVEA
Enzyme 14 Number of Residues 1214
Enzyme 14 Molecular Weight 134524.2
Enzyme 14 Theoretical pI 7.58
Enzyme 14 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 14 General Function Involved in diacylglycerol kinase activity
Enzyme 14 Specific Function Isoform 2 may be involved in cell growth and tumorigenesis. Involved in clathrin-dependent endocytosis
Enzyme 14 Pathways
Enzyme 14 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 22773821 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q16760 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name DGKD_HUMAN Link Image
Enzyme 14 PDB ID 1R79 Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >3645 bp
ATGGCGGCGGCGGCGGGCGCCCCTCCGCCGGGTCCCCCGCAACCGCCTCCGCCGCCGCCG
CCCGAGGAGTCGTCCGACAGCGAGCCCGAGGCGGAGCCCGGCTCCCCACAGAAGCTCATC
CGCAAGGTGTCCACGTCGGGTCAGATCCGACAGAAGACCATCATCAAAGAGGGGATGCTG
ACCAAACAGAACAATTCATTCCAGCGATCAAAAAGGAGATACTTTAAGCTTCGAGGGCGA
ACGCTTTACTATGCCAAAACGGCAAAGTCAATCATATTTGATGAGGTGGATCTGACAGAT
GCCAGCGTAGCTGAATCCAGTACCAAAAACGTCAACAACAGTTTTACGGTCATAACTCCA
TGCAGGAAGCTCATCTTGTGTGCTGATAACAGAAAAGAAATGGAAGATTGGATTGCAGCA
TTAAAGACTGTGCAGAACAGGGAGCACTTTGAGCCCACCCAGTACAGCATGGACCACTTC
TCAGGGATGCACAATTGGTACGCCTGTTCCCACGCGAGGCCGACCTACTGCAATGTGTGC
CGTGAGGCTCTGTCTGGGGTCACGTCGCACGGGCTGTCCTGCGAGGTGTGCAAATTTAAG
GCCCACAAGCGCTGTGCTGTGCGTGCAACCAATAACTGCAAGTGGACCACACTGGCCTCG
ATCGGGAAGGACATCATTGAAGATGCAGATGGGATTGCAATGCCCCACCAGTGGTTGGAA
GGAAACCTACCTGTGAGCGCCAAGTGCACTGTGTGCGACAAGACCTGTGGCAGTGTGCTG
CGCCTGCAGGACTGGCGCTGCCTCTGGTGCAAGGCCATGGTTCACACATCGTGTAAAGAA
TCCTTGCTGACCAAGTGCCCACTTGGCCTGTGCAAAGTGTCAGTCATCCCACCCACGGCT
CTCAACAGCATCGACTCCGATGGGTTCTGGAAGGCCAGCTGTCCTCCTTCTTGCACAAGC
CCACTGTTGGTCTTCGTCAATTCAAAAAGTGGGGACAACCAGGGTGTGAAGTTCCTCAGA
AGATTCAAACAGCTACTAAACCCCGCCCAGGTCTTCGACCTCATGAACGGAGGCCCACAC
CTCGGCTTACGGTTATTCCAGAAGTTTGACACATTCCGGATTCTGGTTTGTGGCGGGGAT
GGAAGTGTTGGCTGGGTCCTCTCCGAAATCGACAGCCTCAACCTTCATAAACAGTGTCAG
CTGGGAGTGCTGCCGCTCGGCACAGGGAACGACTTGGCCCGAGTACTGGGCTGGGGCTCA
GCCTGCGATGACGACACCCAGCTCCCCCAGATCTTGGAGAAGTTGGAGAGAGCCAGCACC
AAGATGCTGGACAGGTGGAGCGTCATGGCATACGAGGCCAAGCTCCCCCGGCAGGCCTCC
TCCTCTACCGTCACCGAAGACTTCAGCGAGGATTCCGAGGTACAGCAGATTCTCTTCTAT
GAAGACTCGGTTGCAGCCCACCTTTCTAAAATCCTCACCTCGGACCAGCACTCGGTGGTC
ATCTCCTCGGCCAAAGTGCTCTGTGAGACGGTGAAGGACTTCGTGGCACGGGTGGGGAAG
GCCTATGAGAAGACGACCGAGAGCTCGGAGGAGTCAGAGGTCATGGCCAAGAAGTGCTCT
GTCCTGAAAGAGAAGCTGGATTCCCTTCTCAAGACCTTGGACGATGAGTCCCAGGCCTCG
TCCTCTCTGCCCAACCCGCCCCCCACCATTGCCGAGGAGGCTGAAGATGGAGATGGGTCG
GGCAGCATCTGCGGTTCCACCGGAGACCGCTTGGTGGCATCAGCTTGCCCGGCCCGGCCG
CAGATATTCCGGCCTCGAGAACAGCTCATGCTGAGAGCCAACAGCCTGAAGAAAGCAATT
CGTCAGATCATAGAACACACAGAAAAAGCTGTCGATGAGCAGAATGCCCAGACCCAGGAG
CAGGAGGGCTTCGTCCTGGGCCTCTCTGAGTCAGAGGAGAAGATGGACCACAGAGTGTGC
CCACCACTGTCCCACAGCGAGAGCTTCGGGGTCCCCAAGGGGAGGAGCCAGCGCAAAGTG
TCGAAATCTCCGTGTGAAAAGCTGATCAGCAAAGGGAGTCTGTCCCTAGGCAGTTCTGCT
TCCCTTCCGCCCCAGCCGGGAAGCCGGGACGGCCTGCCTGCGCTCAACACCAAGATCCTG
TACCCAAATGTCCGGGCTGGAATGTCTGGTTCCTTACCCGGTGGCTCAGTCATCAGTCGC
CTGTTAATTAATGCTGATCCCTTCAACTCTGAACCAGAAACCCTAGAGTATTACACGGAG
AAATGTGTCATGAACAACTATTTTGGCATTGGCCTGGATGCGAAGATATCCCTGGACTTT
AACAACAAGCGCGATGAGCACCCAGAGAAGTGCAGGAGCCGAACCAAGAACATGATGTGG
TATGGAGTTCTTGGAACCAAAGAGTTGCTGCACAGAACCTACAAGAACCTGGAGCAAAAG
GTCTTGCTGGAGTGTGACGGGCGACCCATCCCACTCCCCAGTCTTCAGGGAATTGCTGTC
CTTAACATTCCCAGCTATGCCGGAGGAACCAACTTCTGGGGGGGTACCAAGGAAGATGAT
ACTTTCGCAGCTCCATCATTCGATGACAAGATTCTGGAGGTGGTCGCCGTGTTCGGCAGC
ATGCAGATGGCCGTCTCTCGAGTCATCAGGCTACAGCATCATCGGATCGCCCAGTGTCGC
ACGGTGAAGATCTCCATCCTTGGGGATGAGGGCGTGCCTGTGCAGGTGGACGGAGAGGCC
TGGGTCCAGCCGCCAGGGTACATTCGGATTGTCCACAAGAACCGGGCACAGACACTGACC
AGAGACAGGGCATTTGAGAGCACCCTGAAGTCCTGGGAAGACAAGCAGAAGTGCGAGGTG
CCCCGCCCTCCATCCTGTTCCCTGCACCCGGAGATGCTGTCCGAGGAGGAGGCCACCCAG
ATGGACCAGTTTGGGCAGGCAGCAGGGGTCCTCATTCACAGTATCCGAGAAATAGCTCAG
TCTCACCGGGACATGGAGCAGGAACTGGCCCACGCCGTCAATGCCAGCTCCAAGTCCATG
GACCGTGTGTATGGCAAGCCCAGAACCACAGAGGGGCTCAACTGCAGCTTCGTCCTGGAA
ATGGTGAATAACTTCAGAGCTCTGCGCAGTGAGACGGAGCTGCTGCTGTCTGGGAAGATG
GCCCTGCAGCTGGATCCGCCTCAGAAGGAGCAGCTGGGGAGTGCTCTTGCCGAGATGGAC
CGACAGCTCAGGAGGCTGGCAGACACCCCGTGGCTCTGCCAGTCCGCAGAGCCCGGCGAC
GAAGAGAGTGTGATGCTGGATCTTGCCAAGCGCAGTCGCAGTGGTAAATTCCGCCTCGTG
ACCAAGTTTAAAAAGGAGAAAAACAACAAGAACAAAGAAGCTCACAGTAGCCTGGGAGCC
CCGGTTCACCTCTGGGGGACAGAGGAGGTTGCTGCCTGGCTGGAGCACCTCAGTCTCTGT
GAGTATAAGGACATCTTCACACGGCACGACATCCGGGGCTCTGAGCTCCTGCACCTGGAG
CGGAGGGACCTCAAGGACCTGGGCGTGACCAAGGTGGGCCACATGAAGAGGATCCTGTGT
GGCATCAAGGAGCTGAGCCGCAGCGCCCCCGCCGTCGAGGCCTAG
Enzyme 14 GenBank Gene ID AB078966 Link Image
Enzyme 14 GeneCard ID DGKD Link Image
Enzyme 14 GenAtlas ID DGKD Link Image
Enzyme 14 HGNC ID HGNC:2851 Link Image
Enzyme 14 Chromosome Location 2
Enzyme 14 Locus 2q37.1
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Sakane F, Imai S, Yamada K, Murakami T, Tsushima S, Kanoh H: Alternative splicing of the human diacylglycerol kinase delta gene generates two isoforms differing in their expression patterns and in regulatory functions. J Biol Chem. 2002 Nov 8;277(45):43519-26. Epub 2002 Aug 27. [PubMed Link Image]
  2. Nagase T, Seki N, Tanaka A, Ishikawa K, Nomura N: Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995 Aug 31;2(4):167-74, 199-210. [PubMed Link Image]
  3. Sakane F, Imai S, Kai M, Wada I, Kanoh H: Molecular cloning of a novel diacylglycerol kinase isozyme with a pleckstrin homology domain and a C-terminal tail similar to those of the EPH family of protein-tyrosine kinases. J Biol Chem. 1996 Apr 5;271(14):8394-401. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Imai S, Sakane F, Kanoh H: Phorbol ester-regulated oligomerization of diacylglycerol kinase delta linked to its phosphorylation and translocation. J Biol Chem. 2002 Sep 20;277(38):35323-32. Epub 2002 Jun 25. [PubMed Link Image]
  6. Kawasaki T, Kobayashi T, Ueyama T, Shirai Y, Saito N: Regulation of clathrin-dependent endocytosis by diacylglycerol kinase delta: importance of kinase activity and binding to AP2alpha. Biochem J. 2008 Jan 15;409(2):471-9. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5467
Enzyme 15 Name Diacylglycerol kinase epsilon
Enzyme 15 Synonyms
  1. DAG kinase epsilon
  2. Diglyceride kinase epsilon
  3. DGK-epsilon
Enzyme 15 Gene Name DGKE
Enzyme 15 Protein Sequence >Diacylglycerol kinase epsilon
MEAERRPAPGSPSEGLFADGHLILWTLCSVLLPVFITFWCSLQRSRRQLHRRDIFRKSKH
GWRDTDLFSQPTYCCVCAQHILQGAFCDCCGLRVDEGCLRKADKRFQCKEIMLKNDTKVL
DAMPHHWIRGNVPLCSYCMVCKQQCGCQPKLCDYRCIWCQKTVHDECMKNSLKNEKCDFG
EFKNLIIPPSYLTSINQMRKDKKTDYEVLASKLGKQWTPLIILANSRSGTNMGEGLLGEF
RILLNPVQVFDVTKTPPIKALQLCTLLPYYSARVLVCGGDGTVGWVLDAVDDMKIKGQEK
YIPQVAVLPLGTGNDLSNTLGWGTGYAGEIPVAQVLRNVMEADGIKLDRWKVQVTNKGYY
NLRKPKEFTMNNYFSVGPDALMALNFHAHREKAPSLFSSRILNKAVYLFYGTKDCLVQEC
KDLNKKVELELDGERVALPSLEGIIVLNIGYWGGGCRLWEGMGDETYPLARHDDGLLEVV
GVYGSFHCAQIQVKLANPFRIGQAHTVRLILKCSMMPMQVDGEPWAQGPCTVTITHKTHA
MMLYFSGEQTDDDISSTSDQEDIKATE
Enzyme 15 Number of Residues 567
Enzyme 15 Molecular Weight 63926.6
Enzyme 15 Theoretical pI 7.78
Enzyme 15 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 15 General Function Involved in diacylglycerol kinase activity
Enzyme 15 Specific Function Highly selective for arachidonate-containing species of diacylglycerol (DAG). May terminate signals transmitted through arachidonoyl-DAG or may contribute to the synthesis of phospholipids with defined fatty acid composition
Enzyme 15 Pathways
Enzyme 15 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • 22-42 436-456
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 4503313 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P52429 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name DGKE_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1704 bp
ATGGAAGCGGAGAGGCGGCCGGCGCCGGGCTCGCCCTCCGAGGGCCTGTTTGCGGACGGG
CACCTGATCTTGTGGACGCTGTGCTCGGTCCTGCTGCCGGTGTTCATCACCTTCTGGTGT
AGCCTCCAGCGGTCGCGCCGGCAGCTGCACCGCAGGGACATCTTCCGCAAGAGCAAGCAC
GGGTGGCGCGACACGGACCTGTTCAGCCAGCCCACCTACTGCTGCGTGTGCGCGCAGCAC
ATTCTGCAGGGCGCCTTCTGCGACTGCTGCGGGCTCCGCGTGGACGAGGGCTGCCTCAGG
AAGGCCGACAAGCGCTTCCAGTGCAAGGAGATTATGCTCAAGAATGACACCAAGGTCCTG
GACGCCATGCCCCACCACTGGATCCGGGGCAACGTGCCCCTGTGCAGTTACTGTATGGTT
TGCAAGCAGCAGTGTGGCTGTCAACCCAAGCTTTGCGATTACAGGTGCATTTGGTGCCAG
AAAACAGTACATGATGAGTGCATGAAAAATAGTTTAAAGAATGAAAAATGTGATTTTGGA
GAATTCAAAAACCTAATCATTCCACCAAGTTATTTAACATCCATTAATCAGATGCGTAAA
GACAAAAAAACAGATTATGAAGTGCTAGCCTCTAAGCTTGGAAAGCAGTGGACCCCATTA
ATAATCCTGGCCAACTCTCGTAGTGGAACTAATATGGGAGAAGGACTGTTGGGAGAATTT
AGGATCTTGTTGAATCCAGTCCAGGTTTTTGATGTAACTAAAACTCCTCCTATCAAAGCC
CTACAACTCTGTACTCTTCTCCCATATTATTCAGCTCGAGTACTTGTTTGTGGAGGGGAT
GGGACTGTAGGGTGGGTCCTGGATGCAGTTGATGACATGAAGATTAAGGGACAAGAAAAG
TACATTCCACAAGTTGCAGTTTTGCCTCTGGGAACAGGCAACGATCTATCCAATACATTG
GGTTGGGGTACAGGTTATGCTGGAGAAATTCCAGTTGCGCAGGTTTTGCGAAATGTAATG
GAAGCAGATGGAATTAAACTAGATCGATGGAAAGTTCAAGTAACAAATAAAGGATACTAC
AACTTAAGAAAACCCAAGGAATTCACAATGAACAACTATTTTTCTGTTGGACCTGATGCT
CTCATGGCTCTCAATTTTCATGCTCATCGTGAGAAGGCACCATCTCTGTTTTCTAGCAGA
ATTCTTAATAAGGCGGTTTACTTATTCTATGGAACCAAAGATTGTTTAGTGCAAGAATGT
AAAGATTTGAATAAAAAAGTTGAGCTAGAACTGGATGGTGAGCGAGTAGCACTGCCCAGC
TTGGAAGGTATTATAGTTCTGAACATCGGATACTGGGGCGGTGGCTGCAGACTATGGGAA
GGGATGGGGGACGAGACTTACCCTCTAGCCAGGCATGACGATGGTCTGCTGGAAGTCGTT
GGAGTATATGGGTCTTTCCACTGTGCTCAGATTCAAGTAAAACTGGCTAATCCTTTTCGA
ATAGGACAGGCACATACAGTGAGGCTGATTTTGAAGTGCTCCATGATGCCAATGCAGGTG
GATGGGGAGCCTTGGGCCCAAGGGCCCTGCACTGTCACCATAACTCACAAGACACATGCA
ATGATGTTATATTTCTCTGGAGAACAAACAGATGATGACATCTCTAGTACTTCGGATCAA
GAAGATATAAAGGCGACTGAATAG
Enzyme 15 GenBank Gene ID NM_003647.2 Link Image
Enzyme 15 GeneCard ID DGKE Link Image
Enzyme 15 GenAtlas ID DGKE Link Image
Enzyme 15 HGNC ID HGNC:2852 Link Image
Enzyme 15 Chromosome Location 1
Enzyme 15 Locus 17q22
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Tang W, Bunting M, Zimmerman GA, McIntyre TM, Prescott SM: Molecular cloning of a novel human diacylglycerol kinase highly selective for arachidonate-containing substrates. J Biol Chem. 1996 Apr 26;271(17):10237-41. [PubMed Link Image]
  2. Tang W, Bardien S, Bhattacharya SS, Prescott SM: Characterization of the human diacylglycerol kinase epsilon gene and its assessment as a candidate for inherited retinitis pigmentosa. Gene. 1999 Oct 18;239(1):185-92. [PubMed Link Image]
  3. 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 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5468
Enzyme 16 Name Gastric triacylglycerol lipase
Enzyme 16 Synonyms
  1. GL
  2. Gastric lipase
Enzyme 16 Gene Name LIPF
Enzyme 16 Protein Sequence >Gastric triacylglycerol lipase
MWLLLTMASLISVLGTTHGLFGKLHPGSPEVTMNISQMITYWGYPNEEYEVVTEDGYILE
VNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRG
NTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGTTIGFI
AFSTNPSLAKRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQF
LATEVCSREMLNLLCSNALFIICGFDSKNFNTSRLDVYLSHNPAGTSVQNMFHWTQAVKS
GKFQAYDWGSPVQNRMHYDQSQPPYYNVTAMNVPIAVWNGGKDLLADPQDVGLLLPKLPN
LIYHKEIPFYNHLDFIWAMDAPQEVYNDIVSMISEDKK
Enzyme 16 Number of Residues 398
Enzyme 16 Molecular Weight 45237.4
Enzyme 16 Theoretical pI 7.37
Enzyme 16 GO Classification
Function
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 16 General Function Involved in lipid metabolic process
Enzyme 16 Specific Function Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Enzyme 16 Pathways
Enzyme 16 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-19
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 758063 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P07098 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name LIPG_HUMAN Link Image
Enzyme 16 PDB ID 1HLG Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1197 bp
ATGTGGCTGCTTTTAACAATGGCAAGTTTGATATCTGTACTGGGGACTACACATGGTTTG
TTTGGAAAATTACATCCTGGAAGCCCTGAAGTGACTATGAACATTAGTCAGATGATTACT
TATTGGGGATACCCAAATGAAGAATATGAAGTTGTGACTGAAGATGGTTATATTCTTGAA
GTCAATAGAATTCCTTATGGGAAGAAAAATTCAGGGAATACAGGCCAGAGACCTGTTGTG
TTTTTGCAGCATGGTTTGCTTGCATCAGCCACAAACTGGATTTCCAACCTGCCGAACAAC
AGCCTTGCCTTCATTCTGGCAGATGCTGGTTATGATGTGTGGCTGGGCAACAGCAGAGGA
AACACCTGGGCCAGAAGAAACTTGTACTATTCACCAGATTCAGTTGAATTCTGGGCTTTC
AGCTTTGATGAAATGGCTAAATATGACCTTCCAGCCACAATCGACTTCATTGTAAAGAAA
ACTGGACAGAAGCAGCTACACTATGTTGGCCATTCCCAGGGCACCACCATTGGTTTTATT
GCCTTTTCCACCAATCCCAGCCTGGCTAAAAGAATCAAAACCTTCTATGCTCTAGCTCCT
GTTGCCACTGTGAAGTATACAAAAAGCCTTATAAACAAACTTAGATTTGTTCCTCAATCC
CTCTTCAAGTTTATATTTGGTGACAAAATATTCTACCCACACAACTTCTTTGATCAATTT
CTTGCTACTGAAGTGTGCTCCCGTGAGATGCTGAATCTCCTTTGCAGCAATGCCTTATTT
ATAATTTGTGGATTTGACAGTAAGAACTTTAACACGAGTCGCTTGGATGTGTATCTATCA
CATAATCCAGCAGGAACTTCTGTTCAAAACATGTTCCATTGGACCCAGGCTGTTAAGTCT
GGGAAATTCCAAGCTTATGACTGGGGAAGCCCAGTTCAGAATAGGATGCACTATGATCAG
TCCCAACCTCCCTACTACAATGTGACAGCCATGAATGTACCAATTGCAGTGTGGAACGGT
GGCAAGGACCTGTTGGCTGACCCCCAAGATGTTGGCCTTTTGCTTCCAAAACTCCCCAAT
CTTATTTACCACAAGGAGATTCCTTTTTACAATCACTTGGACTTTATCTGGGCAATGGAT
GCCCCTCAAGAAGTTTACAATGACATTGTTTCTATGATATCAGAAGATAAAAAGTAG
Enzyme 16 GenBank Gene ID X05997 Link Image
Enzyme 16 GeneCard ID LIPF Link Image
Enzyme 16 GenAtlas ID LIPF Link Image
Enzyme 16 HGNC ID HGNC:6622 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 10q23.31
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Bodmer MW, Angal S, Yarranton GT, Harris TJ, Lyons A, King DJ, Pieroni G, Riviere C, Verger R, Lowe PA: Molecular cloning of a human gastric lipase and expression of the enzyme in yeast. Biochim Biophys Acta. 1987 Aug 25;909(3):237-44. [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. Bernback S, Blackberg L: Human gastric lipase. The N-terminal tetrapeptide is essential for lipid binding and lipase activity. Eur J Biochem. 1989 Jul 1;182(3):495-9. [PubMed Link Image]
  4. Roussel A, Canaan S, Egloff MP, Riviere M, Dupuis L, Verger R, Cambillau C: Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest. J Biol Chem. 1999 Jun 11;274(24):16995-7002. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5469
Enzyme 17 Name Lipid phosphate phosphohydrolase 1
Enzyme 17 Synonyms
  1. PAP2-alpha
  2. Phosphatidate phosphohydrolase type 2a
  3. Phosphatidic acid phosphatase 2a
  4. PAP-2a
  5. PAP2a
Enzyme 17 Gene Name PPAP2A
Enzyme 17 Protein Sequence >Lipid phosphate phosphohydrolase 1
MFDKTRLPYVALDVLCVLLAGLPFAILTSRHTPFQRGVFCNDESIKYPYKEDTIPYALLG
GIIIPFSIIVIILGETLSVYCNLLHSNSFIRNNYIATIYKAIGTFLFGAAASQSLTDIAK
YSIGRLRPHFLDVCDPDWSKINCSDGYIEYYICRGNAERVKEGRLSFYSGHSSFSMYCML
FVALYLQARMKGDWARLLRPTLQFGLVAVSIYVGLSRVSDYKHHWSDVLTGLIQGALVAI
LVAVYVSDFFKERTSFKERKEEDSHTTLHETPTTGNHYPSNHQP
Enzyme 17 Number of Residues 284
Enzyme 17 Molecular Weight 32155.7
Enzyme 17 Theoretical pI 8.06
Enzyme 17 GO Classification
Function
  • catalytic activity
Process
Component
  • cell part
  • membrane
Enzyme 17 General Function Involved in catalytic activity
Enzyme 17 Specific Function Broad-specificity phosphohydrolase that dephosphorylates exogenous bioactive glycerolipids and sphingolipids. Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). Pivotal regulator of lysophosphatidic acid (LPA) signaling in the cardiovascular system. Major enzyme responsible of dephosphorylating LPA in platelets, which terminates signaling actions of LPA. May control circulating, and possibly also regulate localized, LPA levels resulting from platelet activation. It has little activity towards ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA > PA > S-1-P > C-1-P. It's down-regulation may contribute to the development of colon adenocarcinoma
Enzyme 17 Pathways
Enzyme 17 Reactions
  • a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate [RN:R02239]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • 7-27 54-74 95-115 165-185 200-220 230-250
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 2467298 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID O14494 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name LPP1_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >855 bp
ATGTTCGACAAGACGCGGCTGCCGTACGTGGCCCTCGATGTGCTCTGCGTGTTGCTGGCT
GGATTGCCTTTTGCAATTCTTACTTCAAGGCATACCCCCTTCCAACGAGGAGTATTCTGT
AATGATGAGTCCATCAAGTACCCTTACAAAGAAGACACCATACCTTATGCGTTATTAGGT
GGAATAATCATTCCATTCAGTATTATCGTTATTATTCTTGGAGAAACCCTGTCTGTTTAC
TGTAACCTTTTGCACTCAAATTCCTTTATCAGGAATAACTACATAGCCACTATTTACAAA
GCCATTGGAACCTTTTTATTTGGTGCAGCTGCTAGTCAGTCCCTGACTGACATTGCCAAG
TATTCAATAGGCAGACTGCGGCCTCACTTCTTGGATGTTTGTGATCCAGATTGGTCAAAA
ATCAACTGCAGCGATGGTTACATTGAATACTACATATGTCGAGGGAATGCAGAAAGAGTT
AAGGAAGGCAGGTTGTCCTTCTATTCAGGCCACTCTTCGTTTTCCATGTACTGCATGCTG
TTTGTGGCACTTTATCTTCAAGCCAGGATGAAGGGAGACTGGGCAAGACTCTTACGCCCC
ACACTGCAATTTGGTCTTGTTGCCGTATCCATTTATGTGGGCCTTTCTCGAGTTTCTGAT
TATAAACACCACTGGAGCGATGTGTTGACTGGACTCATTCAGGGAGCTCTGGTTGCAATA
TTAGTTGCTGTATATGTATCGGATTTCTTCAAAGAAAGAACTTCTTTTAAAGAAAGAAAA
GAGGAGGACTCTCATACAACTCTGCATGAAACACCAACAACTGGGAATCACTATCCGAGC
AATCACCAGCCTTGA
Enzyme 17 GenBank Gene ID AB000888 Link Image
Enzyme 17 GeneCard ID PPAP2A Link Image
Enzyme 17 GenAtlas ID PPAP2A Link Image
Enzyme 17 HGNC ID HGNC:9228 Link Image
Enzyme 17 Chromosome Location 5
Enzyme 17 Locus 5q11
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Kai M, Wada I, Imai S, Sakane F, Kanoh H: Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. J Biol Chem. 1997 Sep 26;272(39):24572-8. [PubMed Link Image]
  2. Leung DW, Tompkins CK, White T: Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. DNA Cell Biol. 1998 Apr;17(4):377-85. [PubMed Link Image]
  3. Ulrix W, Swinnen JV, Heyns W, Verhoeven G: Identification of the phosphatidic acid phosphatase type 2a isozyme as an androgen-regulated gene in the human prostatic adenocarcinoma cell line LNCaP. J Biol Chem. 1998 Feb 20;273(8):4660-5. [PubMed Link Image]
  4. Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Smyth SS, Sciorra VA, Sigal YJ, Pamuklar Z, Wang Z, Xu Y, Prestwich GD, Morris AJ: Lipid phosphate phosphatases regulate lysophosphatidic acid production and signaling in platelets: studies using chemical inhibitors of lipid phosphate phosphatase activity. J Biol Chem. 2003 Oct 31;278(44):43214-23. Epub 2003 Aug 8. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5470
Enzyme 18 Name Diacylglycerol kinase beta
Enzyme 18 Synonyms
  1. DAG kinase beta
  2. 90 kDa diacylglycerol kinase
  3. Diglyceride kinase beta
  4. DGK-beta
Enzyme 18 Gene Name DGKB
Enzyme 18 Protein Sequence >Diacylglycerol kinase beta
MTNQEKWAHLSPSEFSQLQKYAEYSTKKLKDVLEEFHGNGVLAKYNPEGKQDILNQTIDF
EGFKLFMKTFLEAELPDDFTAHLFMSFSNKFPHSSPMVKSKPALLSGGLRMNKGAITPPR
TTSPANTCSPEVIHLKDIVCYLSLLERGRPEDKLEFMFRLYDTDGNGFLDSSELENIISQ
MMHVAEYLEWDVTELNPILHEMMEEIDYDHDGTVSLEEWIQGGMTTIPLLVLLGLENNVK
DDGQHVWRLKHFNKPAYCNLCLNMLIGVGKQGLCCSFCKYTVHERCVARAPPSCIKTYVK
SKRNTDVMHHYWVEGNCPTKCDKCHKTVKCYQGLTGLHCVWCQITLHNKCASHLKPECDC
GPLKDHILPPTTICPVVLQTLPTSGVSVPEERQSTVKKEKSGSQQPNKVIDKNKMQRANS
VTVDGQGLQVTPVPGTHPLLVFVNPKSGGKQGERIYRKFQYLLNPRQVYSLSGNGPMPGL
NFFRDVPDFRVLACGGDGTVGWVLDCIEKANVGKHPPVAILPLGTGNDLARCLRWGGGYE
GENLMKILKDIENSTEIMLDRWKFEVIPNDKDEKGDPVPYSIINNYFSIGVDASIAHRFH
IMREKHPEKFNSRMKNKFWYFEFGTSETFSATCKKLHESVEIECDGVQIDLINISLEGIA
ILNIPSMHGGSNLWGESKKRRSHRRIEKKGSDKRTTVTDAKELKFASQDLSDQLLEVVGL
EGAMEMGQIYTGLKSAGRRLAQCSCVVIRTSKSLPMQIDGEPWMQTPCTIKITHKNQAPM
LMGPPPKTGLFCSLVKRTRNRSKE
Enzyme 18 Number of Residues 804
Enzyme 18 Molecular Weight 90594.7
Enzyme 18 Theoretical pI 7.90
Enzyme 18 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • diacylglycerol kinase activity
  • ion binding
  • kinase activity
  • metal ion binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 18 General Function Involved in diacylglycerol kinase activity
Enzyme 18 Specific Function Exhibits high phosphorylation activity for long-chain diacylglycerols
Enzyme 18 Pathways
Enzyme 18 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 22027632 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9Y6T7 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name DGKB_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >2415 bp
ATGACAAACCAGGAAAAATGGGCCCACCTCAGCCCTTCGGAATTTTCCCAACTTCAGAAA
TATGCTGAGTATTCTACAAAGAAATTAAAGGATGTTCTTGAAGAATTCCATGGTAATGGT
GTGCTTGCAAAGTATAATCCTGAAGGGAAACAAGACATTCTTAACCAAACAATAGATTTT
GAAGGTTTCAAACTATTCATGAAGACATTCCTGGAAGCCGAGCTTCCTGATGATTTCACT
GCACACCTTTTCATGTCATTTAGCAACAAGTTTCCTCATTCTAGTCCAATGGTAAAAAGT
AAGCCTGCTCTCCTATCAGGCGGTCTGAGAATGAATAAAGGTGCCATCACCCCTCCCCGG
ACTACTTCTCCTGCAAATACGTGTTCCCCAGAAGTAATCCATCTGAAGGACATTGTCTGT
TACCTGTCTCTGCTTGAAAGAGGAAGACCTGAGGATAAGCTTGAGTTTATGTTTCGCCTT
TATGACACGGATGGGAATGGCTTCCTGGACAGCTCGGAGCTAGAAAATATCATCAGTCAG
ATGATGCATGTTGCAGAATACCTTGAGTGGGATGTCACTGAACTTAATCCAATCCTCCAT
GAAATGATGGAAGAAATTGACTATGATCATGATGGAACCGTGTCTCTGGAGGAATGGATT
CAAGGAGGAATGACAACGATTCCACTTCTTGTGCTCCTGGGCTTAGAAAATAACGTGAAG
GATGATGGACAGCACGTGTGGCGACTGAAGCACTTTAACAAACCTGCCTATTGCAACCTT
TGCCTGAACATGCTGATTGGCGTGGGGAAGCAGGGCCTCTGCTGTTCCTTCTGCAAGTAC
ACAGTCCATGAGCGCTGTGTGGCTCGAGCACCTCCCTCTTGCATCAAGACCTATGTGAAG
TCCAAAAGGAACACTGATGTCATGCACCATTACTGGGTTGAAGGTAACTGCCCAACCAAG
TGTGATAAGTGCCACAAAACTGTTAAATGTTACCAGGGCCTGACAGGACTGCATTGTGTT
TGGTGTCAGATCACACTGCATAATAAATGTGCTTCTCATCTAAAACCTGAATGTGACTGT
GGACCTTTGAAGGACCATATTTTACCACCCACAACAATCTGTCCAGTGGTACTGCAGACT
CTGCCCACTTCAGGAGTTTCAGTTCCTGAGGAAAGACAATCAACAGTGAAAAAGGAAAAG
AGTGGTTCCCAGCAGCCAAACAAAGTGATTGACAAGAATAAAATGCAAAGAGCCAACTCT
GTTACTGTAGATGGACAAGGCCTGCAGGTCACTCCTGTGCCTGGTACTCACCCACTTTTA
GTTTTTGTGAACCCCAAAAGTGGTGGAAAACAAGGAGAACGAATTTACAGAAAATTCCAG
TATCTATTAAATCCTCGTCAGGTTTACAGTCTTTCTGGAAATGGACCAATGCCAGGGTTA
AACTTTTTCCGTGATGTTCCTGACTTCAGAGTGTTAGCCTGTGGTGGAGATGGAACCGTG
GGCTGGGTTTTGGATTGCATAGAAAAGGCCAATGTAGGCAAGCATCCTCCAGTTGCGATT
CTGCCTCTTGGGACTGGCAATGATCTAGCAAGATGCCTGCGATGGGGAGGAGGTTACGAA
GGTGAGAATCTGATGAAAATTCTAAAAGACATTGAAAACAGCACAGAAATCATGTTGGAC
AGGTGGAAGTTTGAAGTCATACCTAATGACAAAGATGAGAAAGGAGACCCAGTGCCTTAC
AGTATCATCAATAATTACTTTTCCATTGGCGTGGATGCCTCCATTGCACACAGATTCCAC
ATCATGAGAGAAAAACACCCAGAGAAATTCAACAGTAGAATGAAGAACAAATTTTGGTAT
TTTGAGTTTGGCACATCTGAAACTTTCTCAGCCACCTGCAAGAAGCTACATGAATCTGTA
GAAATAGAATGTGATGGAGTACAGATAGATTTAATAAACATCTCTCTGGAAGGAATTGCT
ATTTTGAATATACCAAGCATGCATGGAGGATCCAATCTTTGGGGAGAGTCTAAGAAAAGA
CGAAGCCATCGACGAATAGAGAAAAAAGGGTCTGACAAAAGGACCACCGTCACAGATGCC
AAAGAGTTGAAGTTTGCAAGTCAAGATCTCAGTGACCAGCTGCTGGAGGTGGTCGGCTTG
GAAGGAGCCATGGAGATGGGGCAAATATACACAGGCCTGAAAAGTGCTGGCCGGCGGCTG
GCTCAGTGCTCCTGCGTGGTCATCAGGACGAGCAAGTCTCTGCCAATGCAAATTGATGGG
GAGCCATGGATGCAGACCCCATGCACAATAAAAATTACACACAAGAACCAAGCCCCAATG
CTGATGGGCCCGCCTCCAAAAACCGGTTTATTCTGCTCCCTCGTCAAAAGGACAAGAAAC
CGAAGCAAGGAATAA
Enzyme 18 GenBank Gene ID NM_004080.2 Link Image
Enzyme 18 GeneCard ID DGKB Link Image
Enzyme 18 GenAtlas ID DGKB Link Image
Enzyme 18 HGNC ID HGNC:2850 Link Image
Enzyme 18 Chromosome Location 7
Enzyme 18 Locus 7p21.2
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  2. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Oct 30;5(5):277-86. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5471
Enzyme 19 Name Endothelial lipase
Enzyme 19 Synonyms
  1. Endothelial cell-derived lipase
  2. EDL
  3. EL
Enzyme 19 Gene Name LIPG
Enzyme 19 Protein Sequence >Endothelial lipase
MSNSVPLLCFWSLCYCFAAGSPVPFGPEGRLEDKLHKPKATQTEVKPSVRFNLRTSKDPE
HEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVV
VDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGN
FVKGTVGRITGLDPAGPMFEGADIHKRLSPDDADFVDVLHTYTRSFGLSIGIQMPVGHID
IYPNGGDFQPGCGLNDVLGSIAYGTITEVVKCEHERAVHLFVDSLVNQDKPSFAFQCTDS
NRFKKGICLSCRKNRCNSIGYNAKKMRNKRNSKMYLKTRAGMPFRVYHYQMKIHVFSYKN
MGEIEPTFYVTLYGTNADSQTLPLEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGAS
QSWYNLWKEFRSYLSQPRNPGRELNIRRIRVKSGETQRKLTFCTEDPENTSISPGRELWF
RKCRDGWRMKNETSPTVELP
Enzyme 19 Number of Residues 500
Enzyme 19 Molecular Weight 56794.3
Enzyme 19 Theoretical pI 8.00
Enzyme 19 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipoprotein lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 19 General Function Involved in catalytic activity
Enzyme 19 Specific Function Has phospholipase and triglyceride lipase activities. Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins. Binds heparin
Enzyme 19 Pathways
Enzyme 19 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-20
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 4836419 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9Y5X9 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name LIPE_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1503 bp
ATGAGCAACTCCGTTCCTCTGCTCTGTTTCTGGAGCCTCTGCTATTGCTTTGCTGCGGGG
AGCCCCGTACCTTTTGGTCCAGAGGGACGGCTGGAAGATAAGCTCCACAAACCCAAAGCT
ACACAGACTGAGGTCAAACCATCTGTGAGGTTTAACCTCCGCACCTCCAAGGACCCAGAG
CATGAAGGATGCTACCTCTCCGTCGGCCACAGCCAGCCCTTAGAAGACTGCAGTTTCAAC
ATGACAGCTAAAACCTTTTTCATCATTCACGGATGGACGATGAGCGGTATCTTTGAAAAC
TGGCTGCACAAACTCGTGTCAGCCCTGCACACAAGAGAGAAAGACGCCAATGTAGTTGTG
GTTGACTGGCTCCCCCTGGCCCACCAGCTTTACACGGATGCGGTCAATAATACCAGGGTG
GTGGGACACAGCATTGCCAGGATGCTCGACTGGCTGCAGGAGAAGGACGATTTTTCTCTC
GGGAATGTCCACTTGATCGGCTACAGCCTCGGAGCGCACGTGGCCGGGTATGCAGGCAAC
TTCGTGAAAGGAACGGTGGGCCGAATCACAGGTTTGGATCCTGCCGGGCCCATGTTTGAA
GGGGCCGACATCCACAAGAGGCTCTCTCCGGACGATGCAGATTTTGTGGATGTCCTCCAC
ACCTACACGCGTTCCTTCGGCTTGAGCATTGGTATTCAGATGCCTGTGGGCCACATTGAC
ATCTACCCCAATGGGGGTGACTTCCAGCCAGGCTGTGGACTCAACGATGTCTTGGGATCA
ATTGCATATGGAACAATCACAGAGGTGGTAAAATGTGAGCATGAGCGAGCCGTCCACCTC
TTTGTTGACTCTCTGGTGAATCAGGACAAGCCGAGTTTTGCCTTCCAGTGCACTGACTCC
AATCGCTTCAAAAAGGGGATCTGTCTGAGCTGCCGCAAGAACCGTTGTAATAGCATTGGC
TACAATGCCAAGAAAATGAGGAACAAGAGGAACAGCAAAATGTACCTAAAAACCCGGGCA
GGCATGCCTTTCAGAGTTTACCATTATCAGATGAAAATCCATGTCTTCAGTTACAAGAAC
ATGGGAGAAATTGAGCCCACCTTTTACGTCACCCTTTATGGCACTAATGCAGATTCCCAG
ACTCTGCCACTGGAAATAGTGGAGCGGATCGAGCAGAATGCCACCAACACCTTCCTGGTC
TACACCGAGGAGGACTTGGGAGACCTCTTGAAGATCCAGCTCACCTGGGAGGGGGCCTCT
CAGTCTTGGTACAACCTGTGGAAGGAGTTTCGCAGCTACCTGTCTCAACCCCGCAACCCC
GGACGGGAGCTGAATATCAGGCGCATCCGGGTGAAGTCTGGGGAAACCCAGCGGAAACTG
ACATTTTGTACAGAAGACCCTGAGAACACCAGCATATCCCCAGGCCGGGAGCTCTGGTTT
CGCAAGTGTCGGGATGGCTGGAGGATGAAAAACGAAACCAGTCCCACTGTGGAGCTTCCC
TGA
Enzyme 19 GenBank Gene ID AF118767 Link Image
Enzyme 19 GeneCard ID LIPG Link Image
Enzyme 19 GenAtlas ID LIPG Link Image
Enzyme 19 HGNC ID HGNC:6623 Link Image
Enzyme 19 Chromosome Location 1
Enzyme 19 Locus 18q21.1
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Hirata K, Dichek HL, Cioffi JA, Choi SY, Leeper NJ, Quintana L, Kronmal GS, Cooper AD, Quertermous T: Cloning of a unique lipase from endothelial cells extends the lipase gene family. J Biol Chem. 1999 May 14;274(20):14170-5. [PubMed Link Image]
  2. Jaye M, Lynch KJ, Krawiec J, Marchadier D, Maugeais C, Doan K, South V, Amin D, Perrone M, Rader DJ: A novel endothelial-derived lipase that modulates HDL metabolism. Nat Genet. 1999 Apr;21(4):424-8. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. 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. McCoy MG, Sun GS, Marchadier D, Maugeais C, Glick JM, Rader DJ: Characterization of the lipolytic activity of endothelial lipase. J Lipid Res. 2002 Jun;43(6):921-9. [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. 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 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5472
Enzyme 20 Name Diacylglycerol kinase iota
Enzyme 20 Synonyms
  1. DAG kinase iota
  2. Diglyceride kinase iota
  3. DGK-iota
Enzyme 20 Gene Name DGKI
Enzyme 20 Protein Sequence >Diacylglycerol kinase iota
MDAAGRGCHLLPLPAARGPARAPAAAAAAAASPPGPCSGAACAPSAAAGAGAMNPSSSAG
EEKGATGGSSSSGSGAGSCCLGAEGGADPRGAGSAAAAGAAALDEPAAAGQKEKDEALEE
KLRNLTFRKQVSYRKAISRAGLQHLAPAHPLSLPVANGPAKEPRATLDWSENAVNGEHLW
LETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG
SRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCF
MLHHIEEPCSLGAHAAVIVPPTWIIKVKKPQNSLKASNRKKKRTSFKRKASKRGMEQENK
GRPFVIKPISSPLMKPLLVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEL
YRKVPNLRILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLARTLNWGGGYTDE
PVSKILCQVEDGTVVQLDRWNLHVERNPDLPPEELEDGVCKLPLNVFNNYFSLGFDAHVT
LEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIQEL
KFQCIVFLNIPRYCAGTMPWGNPGDHHDFEPQRHDDGYIEVIGFTMASLAALQVGGHGER
LHQCREVMLLTYKSIPMQVDGEPCRLAPAMIRISLRNQANMVQKSKRRTSMPLLNDPQSV
PDRLRIRVNKISLQDYEGFHYDKEKLREASISDWLRTIAGELVQSFGAIPLGILVVRGDC
DLETCRMYIDRLQEDLQSVSSGSQRVHYQDHETSFPRALSAQRLSPRWCFLDDRSQEHLH
FVMEISQDEIFILDPDMVVSQPAGTPPGMPDLVVEQASGISDWWNPALRKRMLSDSGLGM
IAPYYEDSDLKDLSHSRVLQSPVSSEDHAILQAVIAGDLMKLIESYKNGGSLLIQGPDHC
SLLHYAAKTGNGEIVKYILDHGPSELLDMADSETGETALHKAACQRNRAVCQLLVDAGAS
LRKTDSKGKTPQERAQQAGDPDLAAYLESRQNYKVIGHEDLETAV
Enzyme 20 Number of Residues 1065
Enzyme 20 Molecular Weight 116996.2
Enzyme 20 Theoretical pI 7.81
Enzyme 20 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 20 General Function Involved in diacylglycerol kinase activity
Enzyme 20 Specific Function ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl- sn-glycerol 3-phosphate
Enzyme 20 Pathways
Enzyme 20 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 3676530 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID O75912 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name DGKI_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >3198 bp
ATGGATGCTGCGGGAAGGGGCTGCCATTTGCTGCCCCTGCCAGCGGCGCGCGGACCTGCC
CGCGCTCCTGCAGCCGCCGCCGCCGCCGCCGCCAGCCCGCCCGGCCCCTGCAGCGGCGCC
GCCTGCGCTCCCTCCGCGGCCGCCGGAGCGGGCGCCATGAACCCCAGCTCCTCGGCGGGA
GAGGAGAAAGGGGCGACGGGCGGCAGCAGCAGCAGCGGAAGCGGCGCCGGGAGCTGCTGC
CTGGGCGCCGAGGGCGGCGCGGACCCGCGGGGCGCAGGGTCAGCCGCGGCGGCGGGGGCC
GCTGCCCTGGACGAGCCCGCGGCCGCCGGCCAGAAGGAGAAGGACGAAGCGCTGGAGGAG
AAGCTGAGGAACTTAACTTTCCGGAAGCAGGTCTCGTACAGGAAAGCAATCTCCCGGGCA
GGCCTCCAGCATCTGGCTCCTGCACATCCCCTCAGCCTTCCTGTGGCAAATGGTCCAGCC
AAGGAGCCCAGAGCGACTTTGGACTGGAGTGAGAATGCCGTGAATGGAGAACACCTGTGG
CTGGAGACCAACGTCTCGGGAGACCTCTGCTACCTTGGAGAGGAGAACTGCCAAGTCAGA
TTTGCAAAATCAGCTCTCAGGAGGAAGTGTGCAGTCTGTAAAATCGTCGTCCACACCGCC
TGCATTGAGCAGCTAGAAAAGATTAATTTCAGATGTAAACCAACATTTCGAGAAGGAGGC
TCAAGGTCACCAAGAGAAAATTTTGTACGTCATCACTGGGTGCACAGGCGTCGGCAGGAG
GGGAAATGTAAGCAGTGTGGTAAGGGCTTCCAGCAAAAGTTCTCCTTCCACAGTAAAGAG
ATTGTGGCTATCAGCTGTTCCTGGTGCAAGCAGGCGTTTCACAATAAGGTGACCTGCTTC
ATGCTGCATCACATTGAAGAACCCTGCTCCCTGGGGGCTCATGCTGCTGTTATTGTCCCG
CCCACTTGGATCATTAAGGTGAAGAAACCTCAGAACTCCCTGAAGGCTTCAAATCGGAAG
AAGAAGAGAACAAGCTTTAAAAGAAAAGCCAGTAAAAGAGGGATGGAACAGGAAAACAAA
GGTCGTCCTTTTGTGATAAAACCCATCTCTTCTCCTCTCATGAAACCCTTGCTTGTATTT
GTGAATCCCAAGAGTGGAGGCAACCAGGGAACCAAAGTCCTGCAGATGTTCATGTGGTAC
CTGAATCCACGGCAAGTCTTTGATCTTTCTCAGGAAGGGCCAAAAGATGCGCTTGAATTG
TATAGGAAAGTACCAAATCTGCGAATTCTGGCCTGTGGTGGGGATGGAACGGTGGGCTGG
ATCCTTTCCATCCTGGATGAACTGCAGCTGAGCCCTCAGCCTCCTGTGGGGGTCCTTCCT
CTGGGGACTGGGAATGACCTGGCTCGAACTCTCAACTGGGGAGGGGGCTACACTGATGAA
CCTGTTTCTAAGATCCTGTGTCAAGTGGAAGATGGGACAGTTGTACAGCTAGATCGCTGG
AACCTCCATGTGGAAAGAAACCCCGACTTGCCTCCAGAAGAACTTGAAGATGGCGTATGT
AAGCTCCCTCTGAATGTTTTCAATAACTACTTCAGCCTTGGATTTGATGCCCATGTCACA
CTGGAGTTCCATGAATCCAGAGAAGCAAATCCAGAGAAATTCAACAGTCGTTTTCGAAAT
AAAATGTTCTATGCAGGGGCAGCTTTTTCTGACTTCCTACAGAGAAGTTCTAGAGATCTA
TCCAAACATGTTAAAGTTGTTTGTGATGGAACAGATCTCACCCCAAAGATTCAGGAACTG
AAGTTCCAGTGTATAGTATTTTTAAATATACCCAGATATTGTGCTGGCACAATGCCCTGG
GGAAACCCAGGTGATCACCATGATTTCGAACCTCAGCGTCATGATGATGGTTATATTGAA
GTCATTGGATTTACCATGGCCTCTTTGGCAGCCCTGCAAGTTGGGGGCCATGGAGAGAGG
CTACACCAGTGTCGAGAAGTCATGCTTCTAACTTACAAATCCATCCCCATGCAAGTGGAT
GGGGAGCCCTGTAGGTTGGCCCCAGCTATGATTCGGATCTCCCTGAGGAATCAGGCCAAC
ATGGTACAGAAGAGCAAGAGGAGAACATCCATGCCTTTACTCAATGATCCCCAGTCTGTC
CCAGATCGTCTGAGGATCCGGGTGAACAAAATCAGTTTACAAGACTATGAAGGATTCCAC
TATGACAAGGAGAAACTCCGAGAAGCTTCTATTTCAGACTGGTTAAGAACCATTGCTGGG
GAACTAGTGCAGTCATTTGGAGCGATACCTCTGGGTATTCTAGTTGTGCGTGGAGACTGT
GATTTGGAGACTTGCCGTATGTACATAGACCGCCTACAGGAGGACCTACAGTCAGTTTCT
TCTGGCTCCCAGAGAGTTCATTACCAGGACCATGAAACCTCCTTCCCCAGGGCTCTCTCA
GCACAGAGGCTCTCTCCTCGGTGGTGCTTCCTAGATGACAGATCTCAGGAACATTTGCAC
TTTGTGATGGAGATTTCCCAAGATGAGATTTTTATTCTGGACCCAGATATGGTGGTGTCA
CAGCCGGCGGGGACACCTCCGGGCATGCCTGACCTGGTGGTGGAACAAGCCTCGGGGATC
TCAGACTGGTGGAATCCTGCCCTGCGGAAACGCATGCTGAGTGACAGTGGGCTGGGGATG
ATAGCTCCCTATTATGAGGACTCAGATCTGAAAGATCTCAGCCACTCCCGCGTGCTACAG
TCACCAGTCTCTTCAGAAGATCATGCAATTTTGCAGGCAGTAATAGCTGGTGATCTTATG
AAGCTAATAGAAAGCTATAAAAATGGAGGCAGTCTGCTAATTCAGGGACCAGACCACTGT
TCACTCCTTCACTACGCAGCTAAAACCGGCAACGGGGAGATTGTGAAATATATCCTTGAC
CACGGACCTTCCGAGTTATTGGATATGGCAGACAGTGAAACGGGTGAGACTGCACTGCAC
AAGGCTGCCTGCCAGCGGAACCGGGCTGTGTGCCAGCTTCTGGTGGATGCAGGAGCATCT
CTGAGAAAGACGGACTCCAAGGGTAAGACACCTCAAGAAAGAGCACAGCAGGCTGGGGAC
CCAGACTTGGCTGCTTACCTAGAAAGCCGTCAGAACTATAAGGTCATTGGCCATGAGGAC
CTGGAAACTGCTGTTTGA
Enzyme 20 GenBank Gene ID AF061936 Link Image
Enzyme 20 GeneCard ID DGKI Link Image
Enzyme 20 GenAtlas ID DGKI Link Image
Enzyme 20 HGNC ID HGNC:2855 Link Image
Enzyme 20 Chromosome Location 7
Enzyme 20 Locus 7q32.3-q33
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Ding L, Traer E, McIntyre TM, Zimmerman GA, Prescott SM: The cloning and characterization of a novel human diacylglycerol kinase, DGKiota. J Biol Chem. 1998 Dec 4;273(49):32746-52. [PubMed Link Image]
  2. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  3. Bowne SJ, Sullivan LS, Ding L, Traer E, Prescott SM, Birch DG, Kennan A, Humphries P, Daiger SP: Evaluation of human diacylglycerol kinase(iota), DGKI, a homolog of Drosophila rdgA, in inherited retinopathy mapping to 7q. Mol Vis. 2000 Feb 22;6:6-9. [PubMed Link Image]
  4. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5473
Enzyme 21 Name Bile salt-activated lipase
Enzyme 21 Synonyms
  1. BAL
  2. Bile salt-stimulated lipase
  3. BSSL
  4. Bucelipase
  5. Carboxyl ester lipase
  6. Cholesterol esterase
  7. Pancreatic lysophospholipase
  8. Sterol esterase
Enzyme 21 Gene Name CEL
Enzyme 21 Protein Sequence >Bile salt-activated lipase
MGRLQLVVLGLTCCWAVASAAKLGAVYTEGGFVEGVNKKLGLLGDSVDIFKGIPFAAPTK
ALENPQPHPGWQGTLKAKNFKKRCLQATITQDSTYGDEDCLYLNIWVPQGRKQVSRDLPV
MIWIYGGAFLMGSGHGANFLNNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDANLPG
NYGLRDQHMAIAWVKRNIAAFGGDPNNITLFGESAGGASVSLQTLSPYNKGLIRRAISQS
GVALSPWVIQKNPLFWAKKVAEKVGCPVGDAARMAQCLKVTDPRALTLAYKVPLAGLEYP
MLHYVGFVPVIDGDFIPADPINLYANAADIDYIAGTNNMDGHIFASIDMPAINKGNKKVT
EEDFYKLVSEFTITKGLRGAKTTFDVYTESWAQDPSQENKKKTVVDFETDVLFLVPTEIA
LAQHRANAKSAKTYAYLFSHPSRMPVYPKWVGADHADDIQYVFGKPFATPTGYRPQDRTV
SKAMIAYWTNFAKTGDPNMGDSAVPTHWEPYTTENSGYLEITKKMGSSSMKRSLRTNFLR
YWTLTYLALPTVTDQEATPVPPTGDSEATPVPPTGDSETAPVPPTGDSGAPPVPPTGDSG
APPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVP
PTGDSGAPPVPPTGDAGPPPVPPTGDSGAPPVPPTGDSGAPPVTPTGDSETAPVPPTGDS
GAPPVPPTGDSEAAPVPPTDDSKEAQMPAVIRF
Enzyme 21 Number of Residues 753
Enzyme 21 Molecular Weight 79320.9
Enzyme 21 Theoretical pI 4.94
Enzyme 21 GO Classification Not Available
Enzyme 21 General Function Lipid transport and metabolism
Enzyme 21 Specific Function Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides
Enzyme 21 Pathways
Enzyme 21 Reactions
  • a steryl ester + H2O = a sterol + a fatty acid [RN:R02115]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • 1-20
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 148536848 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID P19835 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name CEL_HUMAN Link Image
Enzyme 21 PDB ID 1F6W Link Image
Enzyme 21 PDB File Show
Enzyme 21 3D Structure
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >2271 bp
ATGCTCACCATGGGGCGCCTGCAACTGGTTGTGTTGGGCCTCACCTGCTGCTGGGCAGTG
GCGAGTGCCGCGAAGCTGGGCGCCGTGTACACAGAAGGTGGGTTCGTGGAAGGCGTCAAT
AAGAAGCTCGGCCTCCTGGGTGACTCTGTGGACATCTTCAAGGGCATCCCCTTCGCAGCT
CCCACCAAGGCCCTGGAAAATCCTCAGCCACATCCTGGCTGGCAAGGGACCCTGAAGGCC
AAGAACTTCAAGAAGAGATGCCTGCAGGCCACCATCACCCAGGACAGCACCTACGGGGAT
GAAGACTGCCTGTACCTCAACATTTGGGTGCCCCAGGGCAGGAAGCAAGTCTCCCGGGAC
CTGCCCGTTATGATCTGGATCTATGGAGGCGCCTTCCTCATGGGGTCCGGCCATGGGGCC
AACTTCCTCAACAACTACCTGTATGACGGCGAGGAGATCGCCACACGCGGAAACGTCATC
GTGGTCACCTTCAACTACCGTGTCGGCCCCCTTGGGTTCCTCAGCACTGGGGACGCCAAT
CTGCCAGGTAACTATGGCCTTCGGGATCAGCACATGGCCATTGCTTGGGTGAAGAGGAAT
ATCGCGGCCTTCGGGGGGGACCCCAACAACATCACGCTCTTCGGGGAGTCTGCTGGAGGT
GCCAGCGTCTCTCTGCAGACCCTCTCCCCCTACAACAAGGGCCTCATCCGGCGAGCCATC
AGCCAGAGCGGCGTGGCCCTGAGTCCCTGGGTCATCCAGAAAAACCCACTCTTCTGGGCC
AAAAAGGTGGCTGAGAAGGTGGGTTGCCCTGTGGGTGATGCCGCCAGGATGGCCCAGTGT
CTGAAGGTTACTGATCCCCGAGCCCTGACGCTGGCCTATAAGGTGCCGCTGGCAGGCCTG
GAGTACCCCATGCTGCACTATGTGGGCTTCGTCCCTGTCATTGATGGAGACTTCATCCCC
GCTGACCCGATCAACCTGTACGCCAACGCCGCCGACATCGACTATATAGCAGGCACCAAC
AACATGGACGGCCACATCTTCGCCAGCATCGACATGCCTGCCATCAACAAGGGCAACAAG
AAAGTCACGGAGGAGGACTTCTACAAGCTGGTCAGTGAGTTCACAATCACCAAGGGGCTC
AGAGGCGCCAAGACGACCTTTGATGTCTACACCGAGTCCTGGGCCCAGGACCCATCCCAG
GAGAATAAGAAGAAGACTGTGGTGGACTTTGAGACCGATGTCCTCTTCCTGGTGCCCACC
GAGATTGCCCTAGCCCAGCACAGAGCCAATGCCAAGAGTGCCAAGACCTACGCCTACCTG
TTTTCCCATCCCTCTCGGATGCCCGTCTACCCCAAATGGGTGGGGGCCGACCATGCAGAT
GACATTCAGTACGTTTTCGGGAAGCCCTTCGCCACCCCCACGGGCTACCGGCCCCAAGAC
AGGACAGTCTCTAAGGCCATGATCGCCTACTGGACCAACTTTGCCAAAACAGGGGACCCC
AACATGGGCGACTCGGCTGTGCCCACACACTGGGAACCCTACACTACGGAAAACAGCGGC
TACCTGGAGATCACCAAGAAGATGGGCAGCAGCTCCATGAAGCGGAGCCTGAGAACCAAC
TTCCTGCGCTACTGGACCCTCACCTATCTGGCGCTGCCCACAGTGACCGACCAGGAGGCC
ACCCCTGTGCCCCCCACAGGGGACTCCGAGGCCACTCCCGTGCCCCCCACGGGTGACTCC
GAGACCGCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGT
GACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCC
ACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTG
CCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCC
CCCGTGCCGCCCACGGGTGACTCCGGCGCCCCCCCCGTGCCGCCCACGGGTGACGCCGGG
CCCCCCCCCGTGCCGCCCACGGGTGACTCCGGCGCCCCCCCCGTGCCGCCCACGGGTGAC
TCCGGGGCCCCCCCCGTGACCCCCACGGGTGACTCCGAGACCGCCCCCGTGCCGCCCACG
GGTGACTCCGGGGCCCCCCCTGTGCCCCCCACGGGTGACTCTGAGGCTGCCCCTGTGCCC
CCCACAGATGACTCCAAGGAAGCTCAGATGCCTGCAGTCATTAGGTTTTAG
Enzyme 21 GenBank Gene ID Not Available
Enzyme 21 GeneCard ID CEL Link Image
Enzyme 21 GenAtlas ID CEL Link Image
Enzyme 21 HGNC ID HGNC:1848 Link Image
Enzyme 21 Chromosome Location 9
Enzyme 21 Locus 9q34.3
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Nilsson J, Blackberg L, Carlsson P, Enerback S, Hernell O, Bjursell G: cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase. Eur J Biochem. 1990 Sep 11;192(2):543-50. [PubMed Link Image]
  2. Hui DY, Kissel JA: Sequence identity between human pancreatic cholesterol esterase and bile salt-stimulated milk lipase. FEBS Lett. 1990 Dec 10;276(1-2):131-4. [PubMed Link Image]
  3. Baba T, Downs D, Jackson KW, Tang J, Wang CS: Structure of human milk bile salt activated lipase. Biochemistry. 1991 Jan 15;30(2):500-10. [PubMed Link Image]
  4. Lidberg U, Nilsson J, Stromberg K, Stenman G, Sahlin P, Enerback S, Bjursell G: Genomic organization, sequence analysis, and chromosomal localization of the human carboxyl ester lipase (CEL) gene and a CEL-like (CELL) gene. Genomics. 1992 Jul;13(3):630-40. [PubMed Link Image]
  5. Roudani S, Miralles F, Margotat A, Escribano MJ, Lombardo D: Bile salt-dependent lipase transcripts in human fetal tissues. Biochim Biophys Acta. 1995 Oct 17;1264(1):141-50. [PubMed Link Image]
  6. Madeyski K, Lidberg U, Bjursell G, Nilsson J: Structure and organization of the human carboxyl ester lipase locus. Mamm Genome. 1998 Apr;9(4):334-8. [PubMed Link Image]
  7. 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]
  8. Hui DY, Hayakawa K, Oizumi J: Lipoamidase activity in normal and mutagenized pancreatic cholesterol esterase (bile salt-stimulated lipase). Biochem J. 1993 Apr 1;291 ( Pt 1):65-9. [PubMed Link Image]
  9. Christie DL, Cleverly DR, O'Connor CJ: Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases. FEBS Lett. 1991 Jan 28;278(2):190-4. [PubMed Link Image]
  10. Wang CS, Dashti A, Jackson KW, Yeh JC, Cummings RD, Tang J: Isolation and characterization of human milk bile salt-activated lipase C-tail fragment. Biochemistry. 1995 Aug 22;34(33):10639-44. [PubMed Link Image]
  11. Mechref Y, Chen P, Novotny MV: Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk. Glycobiology. 1999 Mar;9(3):227-34. [PubMed Link Image]
  12. Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC: Crystal structure of the catalytic domain of human bile salt activated lipase. Protein Sci. 2000 Sep;9(9):1783-90. [PubMed Link Image]
  13. Raeder H, Johansson S, Holm PI, Haldorsen IS, Mas E, Sbarra V, Nermoen I, Eide SA, Grevle L, Bjorkhaug L, Sagen JV, Aksnes L, Sovik O, Lombardo D, Molven A, Njolstad PR: Mutations in the CEL VNTR cause a syndrome of diabetes and pancreatic exocrine dysfunction. Nat Genet. 2006 Jan;38(1):54-62. Epub 2005 Dec 20. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5474
Enzyme 22 Name Lipid phosphate phosphohydrolase 3
Enzyme 22 Synonyms
  1. PAP2-beta
  2. Phosphatidate phosphohydrolase type 2b
  3. Phosphatidic acid phosphatase 2b
  4. PAP-2b
  5. PAP2b
  6. Vascular endothelial growth factor and type I collagen-inducible protein
  7. VCIP
Enzyme 22 Gene Name PPAP2B
Enzyme 22 Protein Sequence >Lipid phosphate phosphohydrolase 3
MQNYKYDKAIVPESKNGGSPALNNNPRRSGSKRVLLICLDLFCLFMAGLPFLIIETSTIK
PYHRGFYCNDESIKYPLKTGETINDAVLCAVGIVIAILAIITGEFYRIYYLKKSRSTIQN
PYVAALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLSVCNPDFSQINCSEGYIQNYR
CRGDDSKVQEARKSFFSGHASFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFY
TGLSRVSDHKHHPSDVLAGFAQGALVACCIVFFVSDLFKTKTTLSLPAPAIRKEILSPVD
IIDRNNHHNMM
Enzyme 22 Number of Residues 311
Enzyme 22 Molecular Weight 35115.6
Enzyme 22 Theoretical pI 9.40
Enzyme 22 GO Classification
Function
  • catalytic activity
Process
Component
  • cell part
  • membrane
Enzyme 22 General Function Involved in catalytic activity
Enzyme 22 Specific Function Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1- phosphate (S-1-P). The relative catalytic efficiency is LPA = PA > C-1-P > S-1-P. May be involved in cell adhesion and in cell-cell interactions
Enzyme 22 Pathways
Enzyme 22 Reactions
  • a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate [RN:R02239]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 34-54 86-106 123-143 194-214 228-248 258-278
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein Not Available
Enzyme 22 UniProtKB/Swiss-Prot ID O14495 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name LPP3_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >936 bp
ATGCAAAACTACAAGTACGACAAAGCGATCGTCCCGGAGAGCAAGAACGGCGGCAGCCCG
GCGCTCAACAACAACCCGAGGAGGAGCGGCAGCAAGCGGGTGCTGCTCATCTGCCTCGAC
CTCTTCTGCCTCTTCATGGCGGGCCTCCCCTTCCTCATCATCGAGACAAGCACCATCAAG
CCTTACCACCGAGGGTTTTACTGCAATGATGAGAGCATCAAGTACCCACTGAAAACTGGT
GAGACAATAAATGACGCTGTGCTCTGTGCCGTGGGGATCGTCATTGCCATCCTCGCGATC
ATCACGGGGGAATTCTACCGGATCTATTACCTGAAGAAGTCGCGGTCGACGATTCAGAAC
CCCTACGTGGCAGCACTCTATAAGCAAGTGGGCTGCTTCCTCTTTGGCTGTGCCATCAGC
CAGTCTTTCACAGACATTGCCAAAGTGTCCATAGGGCGCCTGCGTCCTCACTTCTTGAGT
GTCTGCAACCCTGATTTCAGCCAGATCAACTGCTCTGAAGGCTACATTCAGAACTACAGA
TGCAGAGGTGATGACAGCAAAGTCCAGGAAGCCAGGAAGTCCTTCTTCTCTGGCCATGCC
TCCTTCTCCATGTACACTATGCTGTATTTGGTGCTATACCTGCAGGCCCGCTTCACTTGG
CGAGGAGCCCGCCTGCTCCGGCCCCTCCTGCAGTTCACCTTGATCATGATGGCCTTCTAC
ACGGGACTGTCTCGCGTATCAGACCACAAGCACCATCCCAGTGATGTTCTGGCAGGATTT
GCTCAAGGAGCCCTGGTGGCCTGCTGCATAGTTTTCTTCGTGTCTGACCTCTTCAAGACT
AAGACGACGCTCTCCCTGCCTGCCCCTGCTATCCGGAAGGAAATCCTTTCACCTGTGGAC
ATTATTGACAGGAACAATCACCACAACATGATGTAG
Enzyme 22 GenBank Gene ID AB000889 Link Image
Enzyme 22 GeneCard ID PPAP2B Link Image
Enzyme 22 GenAtlas ID PPAP2B Link Image
Enzyme 22 HGNC ID HGNC:9229 Link Image
Enzyme 22 Chromosome Location 1
Enzyme 22 Locus 1pter-p22.1
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Kai M, Wada I, Imai S, Sakane F, Kanoh H: Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. J Biol Chem. 1997 Sep 26;272(39):24572-8. [PubMed Link Image]
  2. Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed Link Image]
  3. Humtsoe JO, Feng S, Thakker GD, Yang J, Hong J, Wary KK: Regulation of cell-cell interactions by phosphatidic acid phosphatase 2b/VCIP. EMBO J. 2003 Apr 1;22(7):1539-54. [PubMed Link Image]
  4. Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Burnett C, Makridou P, Hewlett L, Howard K: Lipid phosphate phosphatases dimerise, but this interaction is not required for in vivo activity. BMC Biochem. 2004 Jan 16;5:2. [PubMed Link Image]
  8. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  9. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5475
Enzyme 23 Name Diacylglycerol O-acyltransferase 1
Enzyme 23 Synonyms
  1. ACAT-related gene product 1
  2. Diglyceride acyltransferase
Enzyme 23 Gene Name DGAT1
Enzyme 23 Protein Sequence >Diacylglycerol O-acyltransferase 1
MGDRGSSRRRRTGSRPSSHGGGGPAAAEEEVRDAAAGPDVGAAGDAPAPAPNKDGDAGVG
SGHWELRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQV
VSLFLKDPYSWPAPCLVIAANVFAVAAFQVEKRLAVGALTEQAGLLLHVANLATILCFPA
AVVLLVESITPVGSLLALMAHTILFLKLFSYRDVNSWCRRARAKAASAGKKASSAAAPHT
VSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRILEMLFFTQLQVGLIQQWM
VPTIQNSMKPFKDMDYSRIIERLLKLAVPNHLIWLIFFYWLFHSCLNAVAELMQFGDREF
YRDWWNSESVTYFWQNWNIPVHKWCIRHFYKPMLRRGSSKWMARTGVFLASAFFHEYLVS
VPLRMFRLWAFTGMMAQIPLAWFVGRFFQGNYGNAAVWLSLIIGQPIAVLMYVHDYYVLN
YEAPAAEA
Enzyme 23 Number of Residues 488
Enzyme 23 Molecular Weight 55277.7
Enzyme 23 Theoretical pI 9.60
Enzyme 23 GO Classification Not Available
Enzyme 23 General Function Involved in diacylglycerol O-acyltransferase activity
Enzyme 23 Specific Function Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly
Enzyme 23 Pathways
Enzyme 23 Reactions
  • acyl-CoA + 1,2-diacyl-sn-glycerol = CoA + triacylglycerol [RN:R02251]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 104-124 130-150 166-186 189-209 282-302 332-352 406-426 428-448 453-473
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 29170487 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID O75907 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name DGAT1_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1467 bp
ATGGGCGACCGCGGCAGCTCCCGGCGCCGGAGGACAGGGTCGCGGCCCTCGAGCCACGGC
GGCGGCGGGCCTGCGGCGGCGGAAGAGGAGGTGCGGGACGCCGCTGCGGGCCCCGACGTG
GGAGCCGCGGGGGACGCGCCAGCCCCGGCCCCCAACAAGGACGGAGACGCCGGCGTGGGC
AGCGGCCACTGGGAGCTGAGGTGCCATCGCCTGCAGGATTCTTTATTCAGCTCTGACAGT
GGCTTCAGCAACTACCGTGGCATCCTGAACTGGTGTGTGGTGATGCTGATCTTGAGCAAT
GCCCGGTTATTTCTGGAGAACCTCATCAAGTATGGCATCCTGGTGGACCCCATCCAGGTG
GTTTCTCTGTTCCTGAAGGATCCCTATAGCTGGCCCGCCCCATGCCTGGTTATTGCGGCC
AATGTCTTTGCTGTGGCTGCATTCCAGGTTGAGAAGCGCCTGGCGGTGGGTGCCCTGACG
GAGCAGGCGGGACTGCTGCTGCACGTGGCCAACCTGGCCACCATTCTGTGTTTCCCAGCG
GCTGTGGTCTTACTGGTTGAGTCTATCACTCCAGTGGGCTCCCTGCTGGCGCTGATGGCG
CACACCATCCTCTTCCTCAAGCTCTTCTCCTACCGCGACGTCAACTCATGGTGCCGCAGG
GCCAGGGCCAAGGCTGCCTCTGCAGGGAAGAAGGCCAGCAGTGCTGCTGCCCCGCACACC
GTGAGCTACCCGGACAATCTGACCTACCGCGATCTCTACTACTTCCTCTTCGCCCCCACC
TTGTGCTACGAGCTCAACTTTCCCCGCTCTCCCCGCATCCGGAAGCGCTTTCTGCTGCGA
CGGATCCTTGAGATGCTGTTCTTCACCCAGCTCCAGGTGGGGCTGATCCAGCAGTGGATG
GTCCCCACCATCCAGAACTCCATGAAGCCCTTCAAGGACATGGACTACTCACGCATCATC
GAGCGCCTCCTGAAGCTGGCGGTCCCCAATCACCTCATCTGGCTCATCTTCTTCTACTGG
CTCTTCCACTCCTGCCTGAATGCCGTGGCTGAGCTCATGCAGTTTGGAGACCGGGAGTTC
TACCGGGACTGGTGGAACTCCGAGTCTGTCACCTACTTCTGGCAGAACTGGAACATCCCT
GTGCACAAGTGGTGCATCAGACACTTCTACAAGCCCATGCTTCGACGGGGCAGCAGCAAG
TGGATGGCCAGGACAGGGGTGTTCCTGGCCTCGGCCTTCTTCCACGAGTACCTGGTGAGC
GTCCCTCTGCGAATGTTCCGCCTCTGGGCGTTCACGGGCATGATGGCTCAGATCCCACTG
GCCTGGTTCGTGGGCCGCTTTTTCCAGGGCAACTATGGCAACGCAGCTGTGTGGCTGTCG
CTCATCATCGGACAGCCAATAGCCGTCCTCATGTACGTCCACGACTACTACGTGCTCAAC
TATGAGGCCCCAGCGGCAGAGGCCTGA
Enzyme 23 GenBank Gene ID AB057815 Link Image
Enzyme 23 GeneCard ID DGAT1 Link Image
Enzyme 23 GenAtlas ID DGAT1 Link Image
Enzyme 23 HGNC ID HGNC:2843 Link Image
Enzyme 23 Chromosome Location 8
Enzyme 23 Locus 8q24.3
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Oelkers P, Behari A, Cromley D, Billheimer JT, Sturley SL: Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes. J Biol Chem. 1998 Oct 9;273(41):26765-71. [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 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5476
Enzyme 24 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1
Enzyme 24 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 24 Gene Name PLCG1
Enzyme 24 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 24 Number of Residues 1290
Enzyme 24 Molecular Weight 148530.8
Enzyme 24 Theoretical pI 5.91
Enzyme 24 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 24 General Function Involved in calcium ion binding
Enzyme 24 Specific Function PLC-gamma is a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase
Enzyme 24 Pathways
Enzyme 24 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 3336979 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P19174 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PLCG1_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 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 24 GenBank Gene ID AL022394 Link Image
Enzyme 24 GeneCard ID PLCG1 Link Image
Enzyme 24 GenAtlas ID PLCG1 Link Image
Enzyme 24 HGNC ID HGNC:9065 Link Image
Enzyme 24 Chromosome Location 2
Enzyme 24 Locus 20q12-q13.1
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 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 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5477
Enzyme 25 Name Pancreatic lipase-related protein 2
Enzyme 25 Synonyms
  1. PL-RP2
Enzyme 25 Gene Name PNLIPRP2
Enzyme 25 Protein Sequence >Pancreatic lipase-related protein 2
MLPPWTLGLLLLATVRGKEVCYGQLGCFSDEKPWAGTLQRPVKLLPWSPEDIDTRFLLYT
NENPNNFQLITGTEPDTIEASNFQLDRKTRFIIHGFLDKAEDSWPSDMCKKMFEVEKVNC
ICVDWRHGSRAMYTQAVQNIRVVGAETAFLIQALSTQLGYSLEDVHVIGHSLGAHTAAEA
GRRLGGRVGRITGLDPAGPCFQDEPEEVRLDPSDAVFVDVIHTDSSPIVPSLGFGMSQKV
GHLDFFPNGGKEMPGCKKNVLSTITDIDGIWEGIGGFVSCNHLRSFEYYSSSVLNPDGFL
GYPCASYDEFQESKCFPCPAEGCPKMGHYADQFKGKTSAVEQTFFLNTGESGNFTSWRYK
VSVTLSGKEKVNGYIRIALYGSNENSKQYEIFKGSLKPDASHTCAIDVDFNVGKIQKVKF
LWNKRGINLSEPKLGASQITVQSGEDGTEYNFCSSDTVEENVLQSLYPC
Enzyme 25 Number of Residues 469
Enzyme 25 Molecular Weight 51946.3
Enzyme 25 Theoretical pI 5.11
Enzyme 25 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • triglyceride lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 25 General Function Involved in catalytic activity
Enzyme 25 Specific Function Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Enzyme 25 Pathways
Enzyme 25 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • 1-17
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein Not Available
Enzyme 25 UniProtKB/Swiss-Prot ID P54317 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name LIPR2_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >1410 bp
ATGCTGCCCCCTTGGACCCTCGGCCTTCTCCTGCTGGCCACAGTCAGAGGAAAAGAGGTC
TGCTACGGACAACTTGGCTGCTTTTCTGATGAAAAACCATGGGCAGGAACCCTTCAGCGA
CCTGTAAAATTACTTCCCTGGTCCCCCGAGGACATTGACACCCGCTTTCTTCTGTACACA
AATGAAAATCCAAACAACTTCCAACTAATCACTGGCACGGAACCAGACACCATTGAGGCT
TCAAACTTCCAACTGGACCGCAAGACACGCTTCATCATCCATGGCTTCTTAGACAAGGCG
GAGGACAGCTGGCCATCGGACATGTGCAAGAAAATGTTTGAAGTGGAGAAGGTGAACTGC
ATCTGTGTGGACTGGAGGCACGGGTCCCGGGCAATGTACACCCAAGCCGTGCAAAACATT
CGGGTTGTTGGGGCGGAGACAGCTTTCTTAATACAAGCACTGTCGACGCAGCTAGGGTAC
AGCCTTGAGGACGTGCATGTCATCGGCCACAGCCTGGGCGCGCACACGGCCGCGGAGGCG
GGCAGGAGGCTGGGGGGCCGCGTGGGCAGGATCACAGGGCTGGATCCAGCAGGGCCGTGC
TTCCAGGATGAACCTGAGGAGGTTCGGTTGGATCCATCTGACGCCGTGTTTGTGGATGTG
ATTCACACAGATTCTTCTCCCATAGTTCCTTCCCTAGGTTTCGGAATGAGCCAAAAGGTG
GGCCATCTGGATTTCTTTCCAAATGGAGGAAAGGAAATGCCCGGATGTAAGAAAAATGTC
CTTTCAACCATTACTGATATTGATGGAATATGGGAAGGAATTGGTGGCTTTGTGTCTTGC
AATCACCTAAGAAGCTTCGAGTATTACTCAAGCAGCGTCCTCAACCCTGATGGCTTCCTG
GGCTATCCCTGTGCCTCCTACGATGAGTTTCAGGAGAGTAAGTGTTTCCCTTGTCCAGCT
GAAGGATGCCCCAAAATGGGGCACTATGCTGACCAATTTAAGGGGAAAACAAGTGCTGTG
GAACAAACCTTTTTCCTGAACACAGGAGAGAGTGGTAACTTTACTAGTTGGAGATATAAG
GTATCAGTCACACTTTCTGGAAAAGAGAAAGTGAATGGGTACATCAGGATTGCTTTGTAT
GGAAGTAATGAAAACTCGAAACAATATGAGATTTTCAAAGGATCCCTCAAACCAGATGCA
AGTCACACGTGTGCTATTGATGTGGATTTTAATGTTGGAAAAATACAGAAAGTTAAATTC
CTCTGGAACAAACGTGGGATAAATCTATCTGAGCCCAAACTGGGGGCTTCCCAAATCACA
GTGCAAAGTGGTGAAGATGGGACTGAGTATAATTTTTGTAGCAGCGACACTGTGGAAGAA
AACGTCTTGCAATCTCTTTACCCTTGTTAA
Enzyme 25 GenBank Gene ID M93284 Link Image
Enzyme 25 GeneCard ID PNLIPRP2 Link Image
Enzyme 25 GenAtlas ID PNLIPRP2 Link Image
Enzyme 25 HGNC ID HGNC:9157 Link Image
Enzyme 25 Chromosome Location 1
Enzyme 25 Locus 10q25.3
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Giller T, Buchwald P, Blum-Kaelin D, Hunziker W: Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J Biol Chem. 1992 Aug 15;267(23):16509-16. [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. Eydoux C, Spinelli S, Davis TL, Walker JR, Seitova A, Dhe-Paganon S, De Caro A, Cambillau C, Carriere F: Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation. Biochemistry. 2008 Sep 9;47(36):9553-64. Epub 2008 Aug 15. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5478
Enzyme 26 Name Diacylglycerol kinase zeta
Enzyme 26 Synonyms
  1. DAG kinase zeta
  2. Diglyceride kinase zeta
  3. DGK-zeta
Enzyme 26 Gene Name DGKZ
Enzyme 26 Protein Sequence >Diacylglycerol kinase zeta
METFFRRHFRGKVPGPGEGQQRPSSVGLPTGKARRRSPAGQASSSLAQRRRSSAQLQGCL
LSCGVRAQGSSRRRSSTVPPSCNPRFIVDKVLTPQPTTVGAQLLGAPLLLTGLVGMNEEE
GVQEDVVAEASSAIQPGTKTPGPPPPRGAQPLLPLPRYLRRASSHLLPADAVYDHALWGL
HGYYRRLSQRRPSGQHPGPGGRRASGTTAGTMLPTRVRPLSRRRQVALRRKAAGPQAWSA
LLAKAITKSGLQHLAPPPPTPGAPCSESERQIRSTVDWSESATYGEHIWFETNVSGDFCY
VGEQYCVARMLKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESGSRNVREPTFVR
HHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCS
LGVHAAVVIPPTWILRARRPQNTLKASKKKKRASFKRKSSKKGPEEGRWRPFIIRPTPSP
LMKPLLVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHNLRILAC
GGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEG
NVVQLDRWDLHAEPNPEAGPEDRDEGATDRLPLDVFNNYFSLGFDAHVTLEFHESREANP
EKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIQDLKPQCVVFLNIP
RYCAGTMPWGHPGEHHDFEPQRHDDGYLEVIGFTMTSLAALQVGGHGERLTQCREVVLTT
SKAIPVQVDGEPCKLAASRIRIALRNQATMVQKAKRRSAAPLHSDQQPVPEQLRIQVSRV
SMHDYEALHYDKEQLKEASVPLGTVVVPGDSDLELCRAHIERLQQEPDGAGAKSPTCQKL
SPKWCFLDATTASRFYRIDRAQEHLNYVTEIAQDEIYILDPELLGASARPDLPTPTSPLP
TSPCSPTPRSLQGDAAPPQGEELIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAV
STGSKDVVRYLLDHAPPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQG
DTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETAV
Enzyme 26 Number of Residues 1117
Enzyme 26 Molecular Weight 124127.3
Enzyme 26 Theoretical pI 9.31
Enzyme 26 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 26 General Function Involved in diacylglycerol kinase activity
Enzyme 26 Specific Function Displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. Isoform 2 but not isoform 1 regulates RASGRP1 activity
Enzyme 26 Pathways
Enzyme 26 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 157688564 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q13574 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name DGKZ_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >3354 bp
ATGGAGACTTTCTTTAGGAGACATTTCCGGGGGAAGGTGCCAGGCCCTGGAGAGGGGCAG
CAGCGGCCCAGCAGCGTGGGGCTGCCCACAGGCAAGGCCCGGCGTCGCTCCCCCGCTGGG
CAGGCCTCCTCCTCACTGGCACAGCGGCGCCGCTCCAGCGCCCAGCTCCAGGGCTGCCTC
CTGAGTTGCGGGGTGAGGGCCCAGGGTTCCAGCCGCCGGCGCTCCAGCACTGTGCCCCCT
TCCTGCAACCCCCGCTTCATCGTGGATAAGGTGCTCACTCCACAGCCTACCACCGTGGGG
GCCCAGCTTCTGGGTGCACCCCTGCTGTTGACCGGGCTTGTGGGCATGAATGAGGAGGAG
GGTGTCCAGGAGGATGTGGTAGCCGAGGCATCGAGCGCCATCCAGCCAGGCACCAAGACA
CCAGGGCCACCCCCACCTCGGGGCGCCCAGCCGCTGTTGCCCCTACCCCGCTACCTGCGC
CGAGCCTCCTCCCACCTGCTCCCCGCGGATGCCGTATATGACCACGCTCTCTGGGGCCTG
CACGGCTACTATCGGCGCCTCAGCCAGCGGCGGCCCTCAGGCCAGCACCCTGGCCCTGGG
GGCCGAAGAGCCTCAGGCACCACCGCCGGCACCATGCTGCCCACCCGTGTGCGCCCACTG
TCCCGCAGGCGCCAGGTAGCCCTACGGCGCAAGGCGGCCGGACCCCAGGCCTGGAGCGCC
CTGCTCGCGAAAGCCATCACCAAGTCGGGCCTCCAGCACCTGGCCCCCCCTCCGCCCACC
CCTGGGGCCCCGTGCAGCGAGTCAGAGCGGCAGATCCGGAGTACAGTGGACTGGAGCGAG
TCAGCGACATATGGGGAGCACATCTGGTTCGAGACCAACGTGTCCGGGGACTTCTGCTAC
GTTGGGGAGCAGTACTGTGTAGCCAGGATGCTGAAGTCAGTGTCTCGAAGAAAGTGCGCA
GCCTGCAAGATTGTGGTGCACACGCCCTGCATCGAGCAGCTGGAGAAGATAAATTTCCGC
TGTAAGCCGTCCTTCCGTGAATCAGGCTCCAGGAATGTCCGCGAGCCAACCTTTGTACGG
CACCACTGGGTACACAGACGACGCCAGGACGGCAAGTGTCGGCACTGTGGGAAGGGATTC
CAGCAGAAGTTCACCTTCCACAGCAAGGAGATTGTGGCCATCAGCTGCTCGTGGTGCAAG
CAGGCATACCACAGCAAGGTGTCCTGCTTCATGCTGCAGCAGATCGAGGAGCCGTGCTCG
CTGGGGGTCCACGCAGCCGTGGTCATCCCGCCCACCTGGATCCTCCGCGCCCGGAGGCCC
CAGAATACTCTGAAAGCAAGCAAGAAGAAGAAGAGGGCATCCTTCAAGAGGAAGTCCAGC
AAGAAAGGGCCTGAGGAGGGCCGCTGGAGACCCTTCATCATCAGGCCCACCCCCTCCCCG
CTCATGAAGCCCCTGCTGGTGTTTGTGAACCCCAAGAGTGGGGGCAACCAGGGTGCAAAG
ATCATCCAGTCTTTCCTCTGGTATCTCAATCCCCGACAAGTCTTCGACCTGAGCCAGGGA
GGGCCCAAGGAGGCGCTGGAGATGTACCGCAAAGTGCACAACCTGCGGATCCTGGCGTGC
GGGGGCGACGGCACGGTGGGCTGGATCCTCTCCACCCTGGACCAGCTACGCCTGAAGCCG
CCACCCCCTGTTGCCATCCTGCCCCTGGGTACTGGCAACGACTTGGCCCGAACCCTCAAC
TGGGGTGGGGGCTACACAGATGAGCCTGTGTCCAAGATCCTCTCCCACGTGGAGGAGGGG
AACGTGGTACAGCTGGACCGCTGGGACCTCCACGCTGAGCCCAACCCCGAGGCAGGGCCT
GAGGACCGAGATGAAGGCGCCACCGACCGGTTGCCCCTGGATGTCTTCAACAACTACTTC
AGCCTGGGCTTTGACGCCCACGTCACCCTGGAGTTCCACGAGTCTCGAGAGGCCAACCCA
GAGAAATTCAACAGCCGCTTTCGGAATAAGATGTTCTACGCCGGGACAGCTTTCTCTGAC
TTCCTGATGGGCAGCTCCAAGGACCTGGCCAAGCACATCCGAGTGGTGTGTGATGGAATG
GACTTGACTCCCAAGATCCAGGACCTGAAACCCCAGTGTGTTGTTTTCCTGAACATCCCC
AGGTACTGTGCGGGCACCATGCCCTGGGGCCACCCTGGGGAGCACCACGACTTTGAGCCC
CAGCGGCATGACGACGGCTACCTCGAGGTCATTGGCTTCACCATGACGTCGTTGGCCGCG
CTGCAGGTGGGCGGACACGGCGAGCGGCTGACGCAGTGTCGCGAGGTGGTGCTCACCACA
TCCAAGGCCATCCCGGTGCAGGTGGATGGCGAGCCCTGCAAGCTTGCAGCCTCACGCATC
CGCATCGCCCTGCGCAACCAGGCCACCATGGTGCAGAAGGCCAAGCGGCGGAGCGCCGCC
CCCCTGCACAGCGACCAGCAGCCGGTGCCAGAGCAGTTGCGCATCCAGGTGAGTCGCGTC
AGCATGCACGACTATGAGGCCCTGCACTACGACAAGGAGCAGCTCAAGGAGGCCTCTGTG
CCGCTGGGCACTGTGGTGGTCCCAGGAGACAGTGACCTAGAGCTCTGCCGTGCCCACATT
GAGAGACTCCAGCAGGAGCCCGATGGTGCTGGAGCCAAGTCCCCGACATGCCAGAAACTG
TCCCCCAAGTGGTGCTTCCTGGACGCCACCACTGCCAGCCGCTTCTACAGGATCGACCGA
GCCCAGGAGCACCTCAACTATGTGACTGAGATCGCACAGGATGAGATTTATATCCTGGAC
CCTGAGCTGCTGGGGGCATCGGCCCGGCCTGACCTCCCAACCCCCACTTCCCCTCTCCCC
ACCTCACCCTGCTCACCCACGCCCCGGTCACTGCAAGGGGATGCTGCACCCCCTCAAGGT
GAAGAGCTGATTGAGGCTGCCAAGAGGAACGACTTCTGTAAGCTCCAGGAGCTGCACCGA
GCTGGGGGCGACCTCATGCACCGAGACGAGCAGAGTCGCACGCTCCTGCACCACGCAGTC
AGCACTGGCAGCAAGGATGTGGTCCGCTACCTGCTGGACCACGCCCCCCCAGAGATCCTT
GATGCGGTGGAGGAAAACGGGGAGACCTGTTTGCACCAAGCAGCGGCCCTGGGCCAGCGC
ACCATCTGCCACTACATCGTGGAGGCCGGGGCCTCGCTCATGAAGACAGACCAGCAGGGC
GACACTCCCCGGCAGCGGGCTGAGAAGGCTCAGGACACCGAGCTGGCCGCCTACCTGGAG
AACCGGCAGCACTACCAGATGATCCAGCGGGAGGACCAGGAGACGGCTGTGTAG
Enzyme 26 GenBank Gene ID NM_001105540.1 Link Image
Enzyme 26 GeneCard ID DGKZ Link Image
Enzyme 26 GenAtlas ID DGKZ Link Image
Enzyme 26 HGNC ID HGNC:2857 Link Image
Enzyme 26 Chromosome Location 1
Enzyme 26 Locus 11p11.2
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Bunting M, Tang W, Zimmerman GA, McIntyre TM, Prescott SM: Molecular cloning and characterization of a novel human diacylglycerol kinase zeta. J Biol Chem. 1996 Apr 26;271(17):10230-6. [PubMed Link Image]
  2. Ding L, Bunting M, Topham MK, McIntyre TM, Zimmerman GA, Prescott SM: Alternative splicing of the human diacylglycerol kinase zeta gene in muscle. Proc Natl Acad Sci U S A. 1997 May 27;94(11):5519-24. [PubMed Link Image]
  3. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed Link Image]
  4. Topham MK, Bunting M, Zimmerman GA, McIntyre TM, Blackshear PJ, Prescott SM: Protein kinase C regulates the nuclear localization of diacylglycerol kinase-zeta. Nature. 1998 Aug 13;394(6694):697-700. [PubMed Link Image]
  5. Hogan A, Shepherd L, Chabot J, Quenneville S, Prescott SM, Topham MK, Gee SH: Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta. Regulation of nuclear localization by PDZ interactions. J Biol Chem. 2001 Jul 13;276(28):26526-33. Epub 2001 May 14. [PubMed Link Image]
  6. Topham MK, Prescott SM: Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism. J Cell Biol. 2001 Mar 19;152(6):1135-43. [PubMed Link Image]
  7. Rincon E, Santos T, Avila-Flores A, Albar JP, Lalioti V, Lei C, Hong W, Merida I: Proteomics identification of sorting nexin 27 as a diacylglycerol kinase zeta-associated protein: new diacylglycerol kinase roles in endocytic recycling. Mol Cell Proteomics. 2007 Jun;6(6):1073-87. Epub 2007 Mar 9. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 5479
Enzyme 27 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1
Enzyme 27 Synonyms
  1. Phosphoinositide phospholipase C-delta-1
  2. Phospholipase C-III
  3. PLC-III
  4. Phospholipase C-delta-1
  5. PLC-delta-1
Enzyme 27 Gene Name PLCD1
Enzyme 27 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1
MDSGRDFLTLHGLQDDEDLQALLKGSQLLKVKSSSWRRERFYKLQEDCKTIWQESRKVMR
TPESQLFSIEDIQEVRMGHRTEGLEKFARDVPEDRCFSIVFKDQRNTLDLIAPSPADAQH
WVLGLHKIIHHSGSMDQRQKLQHWIHSCLRKADKNKDNKMSFKELQNFLKELNIQVDDSY
ARKIFRECDHSQTDSLEDEEIEAFYKMLTQRVEIDRTFAEAAGSGETLSVDQLVTFLQHQ
QREEAAGPALALSLIERYEPSETAKAQRQMTKDGFLMYLLSADGSAFSLAHRRVYQDMGQ
PLSHYLVSSSHNTYLLEDQLAGPSSTEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTF
TSKILFCDVLRAIRDYAFKASPYPVILSLENHCTLEQQRVMARHLHAILGPMLLNRPLDG
VTNSLPSPEQLKGKILLKGKKLGGLLPPGGEGGPEATVVSDEDEAAEMEDEAVRSRVQHK
PKEDKLRLAQELSDMVIYCKSVHFGGFSSPGTPGQAFYEMASFSENRALRLLQESGNGFV
RHNVGHLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYQGRFQDNGACG
YVLKPAFLRDPNGTFNPRALAQGPWWARKRLNIRVISGQQLPKVNKNKNSIVDPKVTVEI
HGVSRDVASRQTAVITNNGFNPWWDTEFAFEVVVPDLALIRFLVEDYDASSKNDFIGQST
IPLNSLKQGYRHVHLMSKNGDQHPSATLFVKISLQD
Enzyme 27 Number of Residues 756
Enzyme 27 Molecular Weight 85664.3
Enzyme 27 Theoretical pI 6.68
Enzyme 27 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 27 General Function Involved in calcium ion binding
Enzyme 27 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 27 Pathways
Enzyme 27 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 37572274 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID P51178 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name PLCD1_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 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 27 GenBank Gene ID BC050382 Link Image
Enzyme 27 GeneCard ID PLCD1 Link Image
Enzyme 27 GenAtlas ID PLCD1 Link Image
Enzyme 27 HGNC ID HGNC:9060 Link Image
Enzyme 27 Chromosome Location 3
Enzyme 27 Locus 3p22-p21.3
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 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 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 5545
Enzyme 28 Name Lipoprotein lipase
Enzyme 28 Synonyms
  1. LPL
Enzyme 28 Gene Name LPL
Enzyme 28 Protein Sequence >Lipoprotein lipase
MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGV
AESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEH
YPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRIT
GLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQ
PGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKG
LCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQ
AFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDW
WSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG
Enzyme 28 Number of Residues 475
Enzyme 28 Molecular Weight 53162.1
Enzyme 28 Theoretical pI 8.26
Enzyme 28 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipoprotein lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 28 General Function Involved in catalytic activity
Enzyme 28 Specific Function The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium
Enzyme 28 Pathways
Enzyme 28 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • 1-27
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 189065397 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID P06858 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name LIPL_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1428 bp
ATGGAGAGCAAAGCCCTGCTCGTGCTGACTCTGGCCGTGTGGCTCCAGAGTCTGACCGCC
TCCCGCGGAGGGGTGGCCGCCGCCGACCAAAGAAGAGATTTTATCGACATCGAAAGTAAA
TTTGCCCTAAGGACCCCTGAAGACACAGCTGAGGACACTTGCCACCTCATTCCCGGAGTA
GCAGAGTCCGTGGCTACCTGTCATTTCAATCACAGCAGCAAAACCTTCATGGTGATCCAT
GGCTGGACGGTAACAGGAATGTATGAGAGTTGGGTGCCAAAACTTGTGGCCGCCCTGTAC
AAGAGAGAACCAGACTCCAATGTCATTGTGGTGGACTGGCTGTCACGGGCTCAGGAGCAT
TACCCAGTGTCCGCGGGCTACACCAAACTGGTGGGACAGGATGTGGCCCGGTTTATCAAC
TGGATGGAGGAGGAGTTTAACTACCCTCTGGACAATGTCCATCTCTTGGGATACAGCCTT
GGAGCCCATGCTGCTGGCATTGCAGGAAGTCTGACCAATAAGAAAGTCAACAGAATTACT
GGCCTCGATCCAGCTGGACCTAACTTTGAGTATGCAGAAGCCCCGAGTCGTCTTTCTCCT
GATGATGCAGATTTTGTAGACGTCTTACACACATTCACCAGAGGGTCCCCTGGTCGAAGC
ATTGGAATCCAGAAACCAGTTGGGCATGTTGACATTTACCCGAATGGAGGTACTTTTCAG
CCAGGATGTAACATTGGAGAAGCTATCCGCGTGATTGCAGAGAGAGGACTTGGAGATGTG
GACCAGCTAGTGAAGTGCTCCCACGAGCGCTCCATTCATCTCTTCATCGACTCTCTGTTG
AATGAAGAAAATCCAAGTAAGGCCTACAGGTGCAGTTCCAAGGAAGCCTTTGAGAAAGGG
CTCTGCTTGAGTTGTAGAAAGAACCGCTGCAACAATCTGGGCTATGAGATCAATAAAGTC
AGAGCCAAAAGAAGCAGCAAAATGTACCTGAAGACTCGTTCTCAGATGCCCTACAAAGTC
TTCCATTACCAAGTAAAGATTCATTTTTCTGGGACTGAGAGTGAAACCCATACCAATCAG
GCCTTTGAGATTTCTCTGTATGGCACCGTGGCCGAGAGTGAGAACATCCCATTCACTCTG
CCTGAAGTTTCCACAAATAAGACCTACTCCTTCCTAATTTACACAGAGGTAGATATTGGA
GAACTACTCATGTTGAAGCTCAAATGGAAGAGTGATTCATACTTTAGCTGGTCAGACTGG
TGGAGCAGTCCCGGCTTCGCCATTCAGAAGATCAGAGTAAAAGCAGGAGAGACTCAGAAA
AAGGTGATCTTCTGTTCTAGGGAGAAAGTGTCTCATTTGCAGAAAGGAAAGGCACCTGCG
GTATTTGTGAAATGCCATGACAAGTCTCTGAATAAGAAGTCAGGCTGA
Enzyme 28 GenBank Gene ID AK312311 Link Image
Enzyme 28 GeneCard ID LPL Link Image
Enzyme 28 GenAtlas ID LPL Link Image
Enzyme 28 HGNC ID HGNC:6677 Link Image
Enzyme 28 Chromosome Location 8
Enzyme 28 Locus 8p22
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Wion KL, Kirchgessner TG, Lusis AJ, Schotz MC, Lawn RM: Human lipoprotein lipase complementary DNA sequence. Science. 1987 Mar 27;235(4796):1638-41. [PubMed Link Image]
  2. Gotoda T, Senda M, Gamou T, Furuichi Y, Oka K: Nucleotide sequence of human cDNA coding for a lipoprotein lipase (LPL) cloned from placental cDNA library. Nucleic Acids Res. 1989 Mar 25;17(6):2351. [PubMed Link Image]
  3. Takagi A, Ikeda Y, Yamamoto A: DNA sequence of lipoprotein lipase cDNA cloned from human monocytic leukemia THP-1 cells. Nucleic Acids Res. 1990 Nov 11;18(21):6436. [PubMed Link Image]
  4. Chuat JC, Raisonnier A, Etienne J, Galibert F: The lipoprotein lipase-encoding human gene: sequence from intron-6 to intron-9 and presence in intron-7 of a 40-million-year-old Alu sequence. Gene. 1992 Jan 15;110(2):257-61. [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. Enerback S, Ohlsson BG, Samuelsson L, Bjursell G: Characterization of the human lipoprotein lipase (LPL) promoter: evidence of two cis-regulatory regions, LP-alpha and LP-beta, of importance for the differentiation-linked induction of the LPL gene during adipogenesis. Mol Cell Biol. 1992 Oct;12(10):4622-33. [PubMed Link Image]
  8. Zechner R: Rapid and simple isolation procedure for lipoprotein lipase from human milk. Biochim Biophys Acta. 1990 May 1;1044(1):20-5. [PubMed Link Image]
  9. Lutz EP, Merkel M, Kako Y, Melford K, Radner H, Breslow JL, Bensadoun A, Goldberg IJ: Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues. J Clin Invest. 2001 May;107(9):1183-92. [PubMed Link Image]
  10. Gin P, Beigneux AP, Davies B, Young MF, Ryan RO, Bensadoun A, Fong LG, Young SG: Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 containing a G56R amino acid substitution. Biochim Biophys Acta. 2007 Dec;1771(12):1464-8. Epub 2007 Oct 22. [PubMed Link Image]
  11. Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. [PubMed Link Image]
  12. van Tilbeurgh H, Roussel A, Lalouel JM, Cambillau C: Lipoprotein lipase. Molecular model based on the pancreatic lipase x-ray structure: consequences for heparin binding and catalysis. J Biol Chem. 1994 Feb 11;269(6):4626-33. [PubMed Link Image]
  13. Hata A, Emi M, Luc G, Basdevant A, Gambert P, Iverius PH, Lalouel JM: Compound heterozygote for lipoprotein lipase deficiency: Ser----Thr244 and transition in 3' splice site of intron 2 (AG----AA) in the lipoprotein lipase gene. Am J Hum Genet. 1990 Oct;47(4):721-6. [PubMed Link Image]
  14. Emi M, Wilson DE, Iverius PH, Wu L, Hata A, Hegele R, Williams RR, Lalouel JM: Missense mutation (Gly----Glu188) of human lipoprotein lipase imparting functional deficiency. J Biol Chem. 1990 Apr 5;265(10):5910-6. [PubMed Link Image]
  15. Monsalve MV, Henderson H, Roederer G, Julien P, Deeb S, Kastelein JJ, Peritz L, Devlin R, Bruin T, Murthy MR, et al.: A missense mutation at codon 188 of the human lipoprotein lipase gene is a frequent cause of lipoprotein lipase deficiency in persons of different ancestries. J Clin Invest. 1990 Sep;86(3):728-34. [PubMed Link Image]
  16. Beg OU, Meng MS, Skarlatos SI, Previato L, Brunzell JD, Brewer HB Jr, Fojo SS: Lipoprotein lipaseBethesda: a single amino acid substitution (Ala-176----Thr) leads to abnormal heparin binding and loss of enzymic activity. Proc Natl Acad Sci U S A. 1990 May;87(9):3474-8. [PubMed Link Image]
  17. Dichek HL, Fojo SS, Beg OU, Skarlatos SI, Brunzell JD, Cutler GB Jr, Brewer HB Jr: Identification of two separate allelic mutations in the lipoprotein lipase gene of a patient with the familial hyperchylomicronemia syndrome. J Biol Chem. 1991 Jan 5;266(1):473-7. [PubMed Link Image]
  18. Faustinella F, Chang A, Van Biervliet JP, Rosseneu M, Vinaimont N, Smith LC, Chen SH, Chan L: Catalytic triad residue mutation (Asp156----Gly) causing familial lipoprotein lipase deficiency. Co-inheritance with a nonsense mutation (Ser447----Ter) in a Turkish family. J Biol Chem. 1991 Aug 5;266(22):14418-24. [PubMed Link Image]
  19. Ameis D, Kobayashi J, Davis RC, Ben-Zeev O, Malloy MJ, Kane JP, Lee G, Wong H, Havel RJ, Schotz MC: Familial chylomicronemia (type I hyperlipoproteinemia) due to a single missense mutation in the lipoprotein lipase gene. J Clin Invest. 1991 Apr;87(4):1165-70. [PubMed Link Image]
  20. Henderson HE, Ma Y, Hassan MF, Monsalve MV, Marais AD, Winkler F, Gubernator K, Peterson J, Brunzell JD, Hayden MR: Amino acid substitution (Ile194----Thr) in exon 5 of the lipoprotein lipase gene causes lipoprotein lipase deficiency in three unrelated probands. Support for a multicentric origin. J Clin Invest. 1991 Jun;87(6):2005-11. [PubMed Link Image]
  21. Gotoda T, Yamada N, Kawamura M, Kozaki K, Mori N, Ishibashi S, Shimano H, Takaku F, Yazaki Y, Furuichi Y, et al.: Heterogeneous mutations in the human lipoprotein lipase gene in patients with familial lipoprotein lipase deficiency. J Clin Invest. 1991 Dec;88(6):1856-64. [PubMed Link Image]
  22. Ma Y, Henderson HE, Murthy V, Roederer G, Monsalve MV, Clarke LA, Normand T, Julien P, Gagne C, Lambert M, et al.: A mutation in the human lipoprotein lipase gene as the most common cause of familial chylomicronemia in French Canadians. N Engl J Med. 1991 Jun 20;324(25):1761-6. [PubMed Link Image]
  23. Ishimura-Oka K, Faustinella F, Kihara S, Smith LC, Oka K, Chan L: A missense mutation (Trp86----Arg) in exon 3 of the lipoprotein lipase gene: a cause of familial chylomicronemia. Am J Hum Genet. 1992 Jun;50(6):1275-80. [PubMed Link Image]
  24. Bruin T, Kastelein JJ, Van Diermen DE, Ma Y, Henderson HE, Stuyt PM, Stalenhoef AF, Sturk A, Brunzell JD, Hayden MR: A missense mutation Pro157 Arg in lipoprotein lipase (LPLNijmegen) resulting in loss of catalytic activity. Eur J Biochem. 1992 Sep 1;208(2):267-72. [PubMed Link Image]
  25. Ma Y, Wilson BI, Bijvoet S, Henderson HE, Cramb E, Roederer G, Ven Murthy MR, Julien P, Bakker HD, Kastelein JJ, et al.: A missense mutation (Asp250----Asn) in exon 6 of the human lipoprotein lipase gene causes chylomicronemia in patients of different ancestries. Genomics. 1992 Jul;13(3):649-53. [PubMed Link Image]
  26. Ma YH, Bruin T, Tuzgol S, Wilson BI, Roederer G, Liu MS, Davignon J, Kastelein JJ, Brunzell JD, Hayden MR: Two naturally occurring mutations at the first and second bases of codon aspartic acid 156 in the proposed catalytic triad of human lipoprotein lipase. In vivo evidence that aspartic acid 156 is essential for catalysis. J Biol Chem. 1992 Jan 25;267(3):1918-23. [PubMed Link Image]
  27. Emmerich J, Beg OU, Peterson J, Previato L, Brunzell JD, Brewer HB Jr, Santamarina-Fojo S: Human lipoprotein lipase. Analysis of the catalytic triad by site-directed mutagenesis of Ser-132, Asp-156, and His-241. J Biol Chem. 1992 Feb 25;267(6):4161-5. [PubMed Link Image]
  28. Hata A, Ridinger DN, Sutherland SD, Emi M, Kwong LK, Shuhua J, Lubbers A, Guy-Grand B, Basdevant A, Iverius PH, et al.: Missense mutations in exon 5 of the human lipoprotein lipase gene. Inactivation correlates with loss of dimerization. J Biol Chem. 1992 Oct 5;267(28):20132-9. [PubMed Link Image]
  29. Ishimura-Oka K, Semenkovich CF, Faustinella F, Goldberg IJ, Shachter N, Smith LC, Coleman T, Hide WA, Brown WV, Oka K, et al.: A missense (Asp250----Asn) mutation in the lipoprotein lipase gene in two unrelated families with familial lipoprotein lipase deficiency. J Lipid Res. 1992 May;33(5):745-54. [PubMed Link Image]
  30. Reina M, Brunzell JD, Deeb SS: Molecular basis of familial chylomicronemia: mutations in the lipoprotein lipase and apolipoprotein C-II genes. J Lipid Res. 1992 Dec;33(12):1823-32. [PubMed Link Image]
  31. Kobayashi J, Sasaki N, Tashiro J, Inadera H, Saito Y, Yoshida S: A missense mutation (Ala334-->Thr) in exon 7 of the lipoprotein lipase gene in a case with type I hyperlipidemia. Biochem Biophys Res Commun. 1993 Mar 31;191(3):1046-54. [PubMed Link Image]
  32. Haubenwallner S, Horl G, Shachter NS, Presta E, Fried SK, Hofler G, Kostner GM, Breslow JL, Zechner R: A novel missense mutation in the gene for lipoprotein lipase resulting in a highly conservative amino acid substitution (Asp180-->Glu) causes familial chylomicronemia (type I hyperlipoproteinemia). Genomics. 1993 Nov;18(2):392-6. [PubMed Link Image]
  33. Ma Y, Liu MS, Ginzinger D, Frohlich J, Brunzell JD, Hayden MR: Gene-environment interaction in the conversion of a mild-to-severe phenotype in a patient homozygous for a Ser172-->Cys mutation in the lipoprotein lipase gene. J Clin Invest. 1993 May;91(5):1953-8. [PubMed Link Image]
  34. Wilson DE, Hata A, Kwong LK, Lingam A, Shuhua J, Ridinger DN, Yeager C, Kaltenborn KC, Iverius PH, Lalouel JM: Mutations in exon 3 of the lipoprotein lipase gene segregating in a family with hypertriglyceridemia, pancreatitis, and non-insulin-dependent diabetes. J Clin Invest. 1993 Jul;92(1):203-11. [PubMed Link Image]
  35. Bruin T, Tuzgol S, van Diermen DE, Hoogerbrugge-van der Linden N, Brunzell JD, Hayden MR, Kastelein JJ: Recurrent pancreatitis and chylomicronemia in an extended Dutch kindred is caused by a Gly154-->Ser substitution in lipoprotein lipase. J Lipid Res. 1993 Dec;34(12):2109-19. [PubMed Link Image]
  36. Pepe G, Chimienti G, Resta F, Di Perna V, Tarricone C, Lovecchio M, Colacicco AM, Capurso A: A new Italian case of lipoprotein lipase deficiency: a Leu365- > Val change resulting in loss of enzyme activity. Biochem Biophys Res Commun. 1994 Mar 15;199(2):570-6. [PubMed Link Image]
  37. Kobayashi J, Inadera H, Fujita Y, Talley G, Morisaki N, Yoshida S, Saito Y, Fojo SS, Brewer HB Jr: A naturally occurring mutation at the second base of codon asparagine 43 in the proposed N-linked glycosylation site of human lipoprotein lipase: in vivo evidence that asparagine 43 is essential for catalysis and secretion. Biochem Biophys Res Commun. 1994 Nov 30;205(1):506-15. [PubMed Link Image]
  38. Ma Y, Liu MS, Chitayat D, Bruin T, Beisiegel U, Benlian P, Foubert L, De Gennes JL, Funke H, Forsythe I, et al.: Recurrent missense mutations at the first and second base of codon Arg243 in human lipoprotein lipase in patients of different ancestries. Hum Mutat. 1994;3(1):52-8. [PubMed Link Image]
  39. Bruin T, Tuzgol S, Mulder WJ, van den Ende AE, Jansen H, Hayden MR, Kastelein JJ: A compound heterozygote for lipoprotein lipase deficiency, Val69-->Leu and Gly188-->Glu: correlation between in vitro LPL activity and clinical expression. J Lipid Res. 1994 Mar;35(3):438-45. [PubMed Link Image]
  40. Ma Y, Ooi TC, Liu MS, Zhang H, McPherson R, Edwards AL, Forsythe IJ, Frohlich J, Brunzell JD, Hayden MR: High frequency of mutations in the human lipoprotein lipase gene in pregnancy-induced chylomicronemia: possible association with apolipoprotein E2 isoform. J Lipid Res. 1994 Jun;35(6):1066-75. [PubMed Link Image]
  41. Previato L, Guardamagna O, Dugi KA, Ronan R, Talley GD, Santamarina-Fojo S, Brewer HB Jr: A novel missense mutation in the C-terminal domain of lipoprotein lipase (Glu410-->Val) leads to enzyme inactivation and familial chylomicronemia. J Lipid Res. 1994 Sep;35(9):1552-60. [PubMed Link Image]
  42. Reymer PW, Gagne E, Groenemeyer BE, Zhang H, Forsyth I, Jansen H, Seidell JC, Kromhout D, Lie KE, Kastelein J, et al.: A lipoprotein lipase mutation (Asn291Ser) is associated with reduced HDL cholesterol levels in premature atherosclerosis. Nat Genet. 1995 May;10(1):28-34. [PubMed Link Image]
  43. Henderson HE, Hassan F, Marais D, Hayden MR: A new mutation destroying disulphide bridging in the C-terminal domain of lipoprotein lipase. Biochem Biophys Res Commun. 1996 Oct 3;227(1):189-94. [PubMed Link Image]
  44. de Bruin TW, Mailly F, van Barlingen HH, Fisher R, Castro Cabezas M, Talmud P, Dallinga-Thie GM, Humphries SE: Lipoprotein lipase gene mutations D9N and N291S in four pedigrees with familial combined hyperlipidaemia. Eur J Clin Invest. 1996 Aug;26(8):631-9. [PubMed Link Image]
  45. Wiebusch H, Funke H, Bruin T, Bucher H, von Eckardstein A, Kastelein JJ, Assmann G: Compound heterozygosity for a known (D250N) and a novel (E410K) missense mutation in the C-terminal domain of lipoprotein lipase causes familial chylomicronemia. Hum Mutat. 1996;8(4):381-3. [PubMed Link Image]
  46. Wiebusch H, Funke H, Santer R, Richter W, Assmann G: A novel missense (E163G) mutation in the catalytic subunit of lipoprotein lipase causes familial chylomicronemia. Hum Mutat. 1996;8(4):392. [PubMed Link Image]
  47. Rouis M, Lohse P, Dugi KA, Lohse P, Beg OU, Ronan R, Talley GD, Brunzell JD, Santamarina-Fojo S: Homozygosity for two point mutations in the lipoprotein lipase (LPL) gene in a patient with familial LPL deficiency: LPL(Asp9-->Asn, Tyr262-->His). J Lipid Res. 1996 Mar;37(3):651-61. [PubMed Link Image]
  48. Benlian P, De Gennes JL, Foubert L, Zhang H, Gagne SE, Hayden M: Premature atherosclerosis in patients with familial chylomicronemia caused by mutations in the lipoprotein lipase gene. N Engl J Med. 1996 Sep 19;335(12):848-54. [PubMed Link Image]
  49. Foubert L, Bruin T, De Gennes JL, Ehrenborg E, Furioli J, Kastelein J, Benlian P, Hayden M: A single Ser259Arg mutation in the gene for lipoprotein lipase causes chylomicronemia in Moroccans of Berber ancestry. Hum Mutat. 1997;10(3):179-85. [PubMed Link Image]
  50. Mailly F, Palmen J, Muller DP, Gibbs T, Lloyd J, Brunzell J, Durrington P, Mitropoulos K, Betteridge J, Watts G, Lithell H, Angelico F, Humphries SE, Talmud PJ: Familial lipoprotein lipase (LPL) deficiency: a catalogue of LPL gene mutations identified in 20 patients from the UK, Sweden, and Italy. Hum Mutat. 1997;10(6):465-73. [PubMed Link Image]
  51. Foubert L, De Gennes JL, Lagarde JP, Ehrenborg E, Raisonnier A, Girardet JP, Hayden MR, Benlian P: Assessment of French patients with LPL deficiency for French Canadian mutations. J Med Genet. 1997 Aug;34(8):672-5. [PubMed Link Image]
  52. Henderson HE, Bijvoet SM, Mannens MA, Bruin T, Erkelens DW, Hayden MR, Kastelein JJ: Ile225Thr loop mutation in the lipoprotein lipase (LPL) gene is a de novo event. Am J Med Genet. 1998 Jul 24;78(4):313-6. [PubMed Link Image]
  53. Henderson H, Leisegang F, Hassan F, Hayden M, Marais D: A novel Glu421Lys substitution in the lipoprotein lipase gene in pregnancy-induced hypertriglyceridemic pancreatitis. Clin Chim Acta. 1998 Jan 12;269(1):1-12. [PubMed Link Image]
  54. Evans D, Wendt D, Ahle S, Guerra A, Beisiegel U: Compound heterozygosity for a new (S259G) and a previously described (G188E) mutation in lipoprotein lipase (LpL) as a cause of chylomicronemia. Mutations in brief no. 183. Online. Hum Mutat. 1998;12(3):217. [PubMed Link Image]
  55. Zhang Q, Liu Y, Liu BW, Fan P, Cavanna J, Galton DJ: Common genetic variants of lipoprotein lipase and apolipoproteins AI-CIII that relate to coronary artery disease: a study in Chinese and European subjects. Mol Genet Metab. 1998 Jul;64(3):177-83. [PubMed Link Image]
  56. Nickerson DA, Taylor SL, Weiss KM, Clark AG, Hutchinson RG, Stengard J, Salomaa V, Vartiainen E, Boerwinkle E, Sing CF: DNA sequence diversity in a 9.7-kb region of the human lipoprotein lipase gene. Nat Genet. 1998 Jul;19(3):233-40. [PubMed Link Image]
  57. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  58. Takagi A, Ikeda Y, Takeda E, Yamamoto A: A newly identified lipoprotein lipase (LPL) gene mutation (F270L) in a Japanese patient with familial LPL deficiency. Biochim Biophys Acta. 2000 Nov 15;1502(3):433-46. [PubMed Link Image]
  59. Ikeda Y, Goji K, Takagi A: A compound heterozygote for a novel missense mutation (G105R) in exon 3 and a missense mutation (D204E) in exon 5 of the lipoprotein lipase gene in a Japanese infant with hyperchylomicronaemia. Clin Sci (Lond). 2000 Dec;99(6):569-78. [PubMed Link Image]
  60. Hoffmann MM, Jacob S, Luft D, Schmulling RM, Rett K, Marz W, Haring HU, Matthaei S: Type I hyperlipoproteinemia due to a novel loss of function mutation of lipoprotein lipase, Cys(239)-->Trp, associated with recurrent severe pancreatitis. J Clin Endocrinol Metab. 2000 Dec;85(12):4795-8. [PubMed Link Image]
  61. Holzl B, Kraft HG, Wiebusch H, Sandhofer A, Patsch J, Sandhofer F, Paulweber B: Two novel mutations in the lipoprotein lipase gene in a family with marked hypertriglyceridemia in heterozygous carriers. Potential interaction with the polymorphic marker D1S104 on chromosome 1q21-q23. J Lipid Res. 2000 May;41(5):734-41. [PubMed Link Image]
  62. Ikeda Y, Takagi A, Nakata Y, Sera Y, Hyoudou S, Hamamoto K, Nishi Y, Yamamoto A: Novel compound heterozygous mutations for lipoprotein lipase deficiency. A G-to-T transversion at the first position of exon 5 causing G154V missense mutation and a 5' splice site mutation of intron 8. J Lipid Res. 2001 Jul;42(7):1072-81. [PubMed Link Image]
  63. Chan LY, Lam CW, Mak YT, Tomlinson B, Tsang MW, Baum L, Masarei JR, Pang CP: Genotype-phenotype studies of six novel LPL mutations in Chinese patients with hypertriglyceridemia. Hum Mutat. 2002 Sep;20(3):232-3. [PubMed Link Image]
  64. Saika Y, Sakai N, Takahashi M, Maruyama T, Kihara S, Ouchi N, Ishigami M, Hiraoka H, Nakamura T, Yamashita S, Matsuzawa Y: Novel LPL mutation (L303F) found in a patient associated with coronary artery disease and severe systemic atherosclerosis. Eur J Clin Invest. 2003 Mar;33(3):216-22. [PubMed Link Image]
  65. 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]
  66. Abifadel M, Jambart S, Allard D, Rabes JP, Varret M, Derre A, Chouery E, Salem N, Junien C, Aydenian H, Boileau C: Identification of the first Lebanese mutation in the LPL gene and description of a rapid detection method. Clin Genet. 2004 Feb;65(2):158-61. [PubMed Link Image]
  67. Kavazarakis E, Stabouli S, Gourgiotis D, Roumeliotou K, Traeger-Synodinos J, Bossios A, Fretzayas A, Kanavakis E: Severe hypertriglyceridaemia in a Greek infant: a clinical, biochemical and genetic study. Eur J Pediatr. 2004 Aug;163(8):462-6. Epub 2004 Jun 5. [PubMed Link Image]
  68. Maruyama T, Yamashita S, Matsuzawa Y, Bujo H, Takahashi K, Saito Y, Ishibashi S, Ohashi K, Shionoiri F, Gotoda T, Yamada N, Kita T: Mutations in Japanese subjects with primary hyperlipidemia--results from the Research Committee of the Ministry of Health and Welfare of Japan since 1996--. J Atheroscler Thromb. 2004;11(3):131-45. [PubMed Link Image]
  69. Santer R, Gokcay G, Demirkol M, Gal A, Lukacs Z: Hyperchylomicronaemia due to lipoprotein lipase deficiency as a cause of false-positive newborn screening for biotinidase deficiency. J Inherit Metab Dis. 2005;28(2):137-40. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 5554
Enzyme 29 Name Galactosylceramide sulfotransferase
Enzyme 29 Synonyms
  1. GalCer sulfotransferase
  2. 3'-phosphoadenosine-5'-phosphosulfate:GalCer sulfotransferase
  3. 3'-phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase
  4. Cerebroside sulfotransferase
Enzyme 29 Gene Name GAL3ST1
Enzyme 29 Protein Sequence >Galactosylceramide sulfotransferase
MLPPQKKPWESMAKGLVLGALFTSFLLLVYSYAVPPLHAGLASTTPEAAASCSPPALEPE
AVIRANGSAGECQPRRNIVFLKTHKTASSTLLNILFRFGQKHRLKFAFPNGRNDFDYPTF
FARSLVQDYRPGACFNIICNHMRFHYDEVRGLVPTNAIFITVLRDPARLFESSFHYFGPV
VPLTWKLSAGDKLTEFLQDPDRYYDPNGFNAHYLRNLLFFDLGYDNSLDPSSPQVQEHIL
EVERRFHLVLLQEYFDESLVLLKDLLCWELEDVLYFKLNARRDSPVPRLSGELYGRATAW
NMLDSHLYRHFNASFWRKVEAFGRERMAREVAALRHANERMRTICIDGGHAVDAAAIQDE
AMQPWQPLGTKSILGYNLKKSIGQRHAQLCRRMLTPEIQYLMDLGANLWVTKLWKFIRDF
LRW
Enzyme 29 Number of Residues 423
Enzyme 29 Molecular Weight 48763.6
Enzyme 29 Theoretical pI 8.78
Enzyme 29 GO Classification
Function
  • catalytic activity
  • galactose 3-O-sulfotransferase activity
  • galactosylceramide sulfotransferase activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • biosynthetic process
  • metabolic process
Component
  • Golgi apparatus
  • cell part
  • integral to membrane
  • intracellular membrane-bounded organelle
  • intrinsic to membrane
  • membrane part
  • membrane-bounded organelle
  • organelle
Enzyme 29 General Function Involved in galactosylceramide sulfotransferase activity
Enzyme 29 Specific Function Catalyzes the sulfation of membrane glycolipids. Seems to prefer beta-glycosides at the non-reducing termini of sugar chains attached to a lipid moiety. Catalyzes the synthesis of galactosylceramide sulfate (sulfatide), a major lipid component of the myelin sheath and of monogalactosylalkylacylglycerol sulfate (seminolipid), present in spermatocytes. Also acts on lactosylceramide, galactosyl 1-alkyl-2-sn-glycerol and galactosyl diacylglycerol (in vitro)
Enzyme 29 Pathways
Enzyme 29 Reactions
  • 3'-phosphoadenylyl sulfate + a galactosylceramide = adenosine 3',5'-bisphosphate + a galactosylceramidesulfate [RN:R04017 R06279]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • 15-35
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 6714628 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q99999 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name G3ST1_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >1272 bp
ATGCTGCCACCGCAGAAGAAGCCCTGGGAGTCCATGGCTAAGGGGCTGGTGCTGGGCGCG
CTCTTCACTAGTTTCCTGCTGCTGGTGTACTCCTATGCCGTGCCCCCGCTGCATGCCGGC
CTGGCCTCCACGACCCCGGAGGCCGCAGCGTCCTGCTCTCCACCTGCACTCGAGCCAGAG
GCAGTGATCCGGGCCAACGGCTCGGCGGGGGAGTGCCAGCCGCGGCGCAACATCGTGTTC
TTGAAGACGCACAAGACGGCCAGCAGCACCCTGCTCAACATCCTGTTCCGCTTCGGCCAG
AAGCACCGGCTCAAGTTCGCCTTCCCTAACGGCCGCAATGACTTCGACTACCCGACCTTC
TTCGCCCGCAGCCTGGTGCAGGACTATCGGCCCGGGGCCTGCTTCAACATCATCTGCAAC
CACATGCGCTTCCACTACGACGAGGTGCGCGGCCTGGTGCCGACCAACGCCATCTTCATC
ACGGTGCTCCGCGACCCCGCCCGCTTGTTCGAGTCCTCCTTCCACTACTTCGGGCCGGTG
GTGCCCCTCACGTGGAAGCTCTCGGCCGGCGACAAGCTGACCGAGTTCCTGCAAGACCCG
GATCGCTACTACGACCCCAACGGCTTCAATGCCCACTACCTCCGAAACCTGCTCTTCTTC
GACCTGGGCTATGACAACAGCCTGGACCCCAGCAGCCCGCAGGTGCAGGAGCACATCCTG
GAGGTGGAGCGTCGCTTCCACCTGGTGCTCCTTCAAGAGTACTTCGACGAGTCGCTGGTG
CTGCTGAAGGACCTGCTGTGCTGGGAGCTGGAGGACGTGCTCTACTTCAAGCTCAACGCC
CGCCGCGACTCGCCCGTGCCGCGGCTCTCGGGGGAGCTGTATGGGCGCGCCACCGCCTGG
AACATGCTGGACTCCCACCTCTACCGCCACTTCAACGCCAGCTTCTGGCGCAAGGTGGAG
GCCTTCGGGCGGGAGCGCATGGCCCGCGAGGTGGCCGCCCTGCGCCATGCCAACGAGCGC
ATGCGGACCATCTGCATCGACGGGGGCCACGCCGTGGACGCCGCCGCCATCCAGGACGAG
GCCATGCAGCCCTGGCAGCCGCTGGGCACCAAGTCCATCCTGGGCTACAACCTCAAGAAG
AGCATCGGGCAGCGGCACGCGCAGCTCTGCCGGCGCATGCTCACGCCCGAGATCCAGTAC
CTGATGGACCTCGGCGCCAACCTGTGGGTCACCAAGCTCTGGAAGTTCATTCGCGATTTC
CTGCGGTGGTGA
Enzyme 29 GenBank Gene ID AB029901 Link Image
Enzyme 29 GeneCard ID GAL3ST1 Link Image
Enzyme 29 GenAtlas ID GAL3ST1 Link Image
Enzyme 29 HGNC ID HGNC:24240 Link Image
Enzyme 29 Chromosome Location 2
Enzyme 29 Locus 22q12.2
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Honke K, Tsuda M, Hirahara Y, Ishii A, Makita A, Wada Y: Molecular cloning and expression of cDNA encoding human 3'-phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase. J Biol Chem. 1997 Feb 21;272(8):4864-8. [PubMed Link Image]
  2. Tsuda M, Egashira M, Niikawa N, Wada Y, Honke K: Cancer-associated alternative usage of multiple promoters of human GalCer sulfotransferase gene. Eur J Biochem. 2000 May;267(9):2672-9. [PubMed Link Image]
  3. 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]
  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. Honke K, Yamane M, Ishii A, Kobayashi T, Makita A: Purification and characterization of 3'-phosphoadenosine-5'-phosphosulfate:GalCer sulfotransferase from human renal cancer cells. J Biochem (Tokyo). 1996 Mar;119(3):421-7. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 5781
Enzyme 30 Name Hormone-sensitive lipase
Enzyme 30 Synonyms
  1. HSL
Enzyme 30 Gene Name LIPE
Enzyme 30 Protein Sequence >Hormone-sensitive lipase
MEPGSKSVSRSDWQPEPHQRPITPLEPGPEKTPIAQPESKTLQGSNTQQKPASNQRPLTQ
QETPAQHDAESQKEPRAQQKSASQEEFLAPQKPAPQQSPYIQRVLLTQQEAASQQGPGLG
KESITQQEPALRQRHVAQPGPGPGEPPPAQQEAESTPAAQAKPGAKREPSAPTESTSQET
PEQSDKQTTPVQGAKSKQGSLTELGFLTKLQELSIQRSALEWKALSEWVTDSESESDVGS
SSDTDSPATMGGMVAQGVKLGFKGKSGYKVMSGYSGTSPHEKTSARNHRHYQDTASRLIH
NMDLRTMTQSLVTLAEDNIAFFSSQGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAH
LFDLDPETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRTSHNLAELEAYLAALT
QLRALVYYAQRLLVTNRPGVLFFEGDEGLTADFLREYVTLHKGCFYGRCLGFQFTPAIRP
FLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWK
AFWNITEMEVLSSLANMASATVRVSRLLSLPPEAFEMPLTADPTLTVTISPPLAHTGPGP
VLVRLISYDLREGQDSEELSSLIKSNGQRSLELWPRPQQAPRSRSLIVHFHGGGFVAQTS
RSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGSTGERIC
LAGDSAGGNLCFTVALRAAAYGVRVPDGIMAAYPATMLQPAASPSRLLSLMDPLLPLSVL
SKCVSAYAGAKTEDHSNSDQKALGMMGLVRRDTALLLRDFRLGASSWLNSFLELSGRKSQ
KMSEPIAEPMRRSVSEAALAQPQGPLGTDSLKNLTLRDLSLRGNSETSSDTPEMSLSAET
LSPSTPSDVNFLLPPEDAGEEAEAKNELSPMDRGLGVRAAFPEGFHPRRSSQGATQMPLY
SSPIVKNPFMSPLLAPDSMLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVE
DLPHGFLTLAALCRETRQAAELCVERIRLVLTPPAGAGPSGETGAAGVDGGCGGRH
Enzyme 30 Number of Residues 1076
Enzyme 30 Molecular Weight 116596.7
Enzyme 30 Theoretical pI 6.68
Enzyme 30 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
Process
  • alcohol metabolic process
  • cholesterol metabolic process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • small molecule metabolic process
  • sterol metabolic process
Component
Enzyme 30 General Function Involved in hydrolase activity
Enzyme 30 Specific Function In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions
  • (1) diacylglycerol + H2O = monoacylglycerol + a carboxylate [RN:R05209]
  • (2) triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
  • (3) monoacylglycerol + H2O = glycerol + a carboxylate [RN:R07293]
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 47124456 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q05469 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name LIPS_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >3231 bp
ATGGAGCCAGGTTCTAAGTCAGTGTCTAGGTCAGACTGGCAACCTGAACCACACCAGAGG
CCTATAACCCCGCTAGAGCCTGGGCCAGAAAAGACACCCATAGCCCAGCCAGAATCGAAG
ACTCTGCAGGGATCCAATACCCAACAGAAGCCTGCTTCAAACCAAAGACCCCTCACCCAG
CAGGAGACCCCTGCACAACATGATGCTGAATCCCAGAAGGAACCTAGAGCCCAACAAAAA
TCTGCTTCACAAGAGGAATTTCTTGCCCCACAGAAGCCCGCACCACAGCAATCACCTTAC
ATCCAAAGGGTGCTGCTCACTCAACAGGAAGCTGCCTCCCAGCAGGGACCTGGGCTAGGA
AAAGAATCTATAACTCAACAGGAGCCAGCATTGAGACAAAGACATGTAGCCCAGCCAGGG
CCTGGGCCAGGAGAGCCACCTCCAGCTCAACAAGAAGCTGAATCAACACCTGCGGCCCAG
GCTAAACCTGGAGCCAAAAGGGAGCCATCTGCCCCGACTGAATCTACGTCCCAAGAGACA
CCTGAACAGTCAGACAAGCAAACAACGCCAGTCCAGGGAGCCAAATCCAAGCAGGGATCT
TTGACAGAGCTGGGATTTCTAACAAAACTTCAGGAACTATCCATACAGCGATCAGCCCTA
GAGTGGAAGGCACTTTCTGAGTGGGTCACAGATTCTGAGTCAGAATCAGATGTGGGATCA
TCTTCAGACACAGATTCTCCAGCCACGATGGGTGGAATGGTGGCCCAGGGAGTGAAGCTA
GGCTTCAAAGGAAAATCTGGTTATAAAGTGATGTCAGGATACAGTGGGACGTCGCCACAT
GAGAAAACCAGTGCTCGGAATCACAGACACTACCAGGATACAGCCTCAAGGCTCATCCAC
AACATGGACCTGCGCACAATGACACAGTCGCTGGTGACTCTGGCGGAGGACAACATAGCC
TTCTTCTCGAGCCAGGGTCCTGGGGAAACGGCCCAGCGGCTGTCAGGCGTTTTTGCCGGT
GTACGGGAGCAGGCGCTGGGGCTGGAGCCGGCCCTGGGCCGCCTGCTGGGTGTGGCGCAC
CTCTTTGACCTGGACCCAGAGACACCGGCCAACGGGTACCGCAGCCTAGTGCACACAGCC
CGCTGCTGCCTGGCGCACCTCCTGCACAAATCCCGCTATGTGGCCTCCAACCGCCGCAGC
ATCTTCTTCCGCACCAGCCACAACCTGGCCGAGCTGGAGGCCTACCTGGCTGCCCTCACC
CAGCTCCGCGCTCTGGTCTACTACGCCCAGCGCCTGCTGGTTACCAATCGGCCGGGGGTA
CTCTTCTTTGAGGGCGACGAGGGGCTCACCGCCGACTTCCTCCGGGAGTATGTCACGCTG
CATAAGGGATGCTTCTATGGCCGCTGCCTGGGCTTCCAGTTCACGCCTGCCATCCGGCCA
TTCCTGCAGACCATCTACATTGGGCTGGTGTCCTTCGGGGAGCACTACAAACGCAACGAG
ACAGGCCTCAGTGTGGCCGCCAGCTCTCTCTTCACCAGCGGCCGCTTTGCCATCGACCCC
GAGCTGCGTGGGGCTGAGTTTGAGCGGATCACACAGAACCTGGACGTGCACTTCTGGAAA
GCCTTCTGGAACATCACCGAGATGGAAGTGCTATCGTCTCTGGCCAACATGGCATCGGCC
ACCGTGAGGGTAAGCCGCCTGCTCAGCCTGCCACCCGAAGCCTTTGAGATGCCACTGACT
GCCGACCCCACGCTCACGGTCACCATCTCACCCCCACTGGCCCACACAGGCCCTGGGCCC
GTCCTCGTCAGGCTCATCTCCTGTGACCTGCGTGAAGGACAGGACAGTGAGGAGCTCAGC
AGCCTGATAAAGTCCAACGGCCAACGGAGCCTGGAGCTGTGGCCGCGCCCCCAGCAGGCA
CCCCGCTCGCGGTCCCTGATAGTGCACTTCCACGGCGGTGGCTTTGTGGCCCAGACCTCC
AGATCCCACGAGCCCTACCTCAAGAGCTGGGCCCAGGAGCTGGGCGCCCCCATCATCTCC
ATCGACTACTCCCTGGCCCCTGAGGCCCCCTTCCCCCGTGCGCTGGAGGAGTGCTTCTTC
GCCTACTGCTGGGCCATCAAGCACTGCGCCCTCCTTGGCTCAACAGGGGAACGAATCTGC
CTTGCGGGGGACAGTGCAGGCGGGAACCTCTGCTTCACCGTGGCTCTTCGGGCAGCAGCC
TACGGGGTGCGGGTGCCAGATGGCATCATGGCAGCCTACCCGGCCACAATGCTGCAGCCT
GCCGCCTCTCCCTCCCGCCTGCTGAGCCTCATGGACCCCTTGCTGCCCCTCAGTGTGCTC
TCCAAGTGTGTCAGCGCCTATGCTGGTGCAAAGACGGAGGACCACTCCAACTCAGACCAG
AAAGCCCTCGGCATGATGGGGCTGGTGCGGCGGGACACAGCCCTGCTCCTCCGAGACTTC
CGCCTGGGTGCCTCCTCATGGCTCAACTCCTTCCTGGAGTTAAGTGGGCGCAAGTCCCAG
AAGATGTCGGAGCCCATAGCAGAGCCGATGCGCCGCAGTGTGTCTGAAGCAGCACTGGCC
CAGCCCCAGGGCCCACTGGGCACGGATTCCCTCAAGAACCTGACCCTGAGGGACTTGAGC
CTGAGGGGAAACTCCGAGACGTCGTCGGACACCCCCGAGATGTCGCTGTCAGCTGAGACA
CTTAGCCCCTCCACACCCTCCGATGTCAACTTCTTATTACCACCTGAGGATGCAGGGGAA
GAGGCTGAGGCCAAAAATGAGCTGAGCCCCATGGACAGAGGCCTGGGCGTCCGTGCCGCC
TTCCCCGAGGGTTTCCACCCCCGACGCTCCAGCCAGGGTGCCACACAGATGCCCCTCTAC
TCCTCACCCATAGTCAAGAACCCCTTCATGTCGCCGCTGCTGGCACCCGACAGCATGCTC
AAGAGCCTGCCACCTGTGCACATCGTGGCGTGCGCGCTGGACCCCATGCTGGACGACTCG
GTCATGCTCGCGCGGCGACTGCGCAACCTGGGCCAGCCGGTGACGCTGCGCGTGGTGGAG
GACCTGCCGCACGGCTTCCTGACCCTAGCGGCGCTGTGCCGCGAGACGCGCCAGGCCGCA
GAGCTGTGCGTGGAGCGCATCCGCCTCGTCCTCACTCCTCCCGCCGGAGCCGGGCCGAGC
GGGGAGACGGGGGCTGCGGGGGTAGACGGGGGCTGCGGGGGGCGACACTAA
Enzyme 30 GenBank Gene ID BC070041 Link Image
Enzyme 30 GeneCard ID LIPE Link Image
Enzyme 30 GenAtlas ID LIPE Link Image
Enzyme 30 HGNC ID HGNC:6621 Link Image
Enzyme 30 Chromosome Location 1
Enzyme 30 Locus 19q13.2
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Langin D, Laurell H, Holst LS, Belfrage P, Holm C: Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):4897-901. [PubMed Link Image]
  2. Holst LS, Langin D, Mulder H, Laurell H, Grober J, Bergh A, Mohrenweiser HW, Edgren G, Holm C: Molecular cloning, genomic organization, and expression of a testicular isoform of hormone-sensitive lipase. Genomics. 1996 Aug 1;35(3):441-7. [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. Aboulaich N, Ortegren U, Vener AV, Stralfors P: Association and insulin regulated translocation of hormone-sensitive lipase with PTRF. Biochem Biophys Res Commun. 2006 Nov 24;350(3):657-61. Epub 2006 Sep 28. [PubMed Link Image]
  5. Ortegren U, Yin L, Ost A, Karlsson H, Nystrom FH, Stralfors P: Separation and characterization of caveolae subclasses in the plasma membrane of primary adipocytes; segregation of specific proteins and functions. FEBS J. 2006 Jul;273(14):3381-92. Epub 2006 Jun 26. [PubMed Link Image]
  6. 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]
  7. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 6021
Enzyme 31 Name Phosphatidate cytidylyltransferase 2
Enzyme 31 Synonyms
  1. CDP-DAG synthase 2
  2. CDP-DG synthase 2
  3. CDP-diacylglycerol synthase 2
  4. CDS 2
  5. CDP-diglyceride pyrophosphorylase 2
  6. CDP-diglyceride synthase 2
  7. CTP:phosphatidate cytidylyltransferase 2
Enzyme 31 Gene Name CDS2
Enzyme 31 Protein Sequence >Phosphatidate cytidylyltransferase 2
MTELRQRVAHEPVAPPEDKESESEAKVDGETASDSESRAESAPLPVSADDTPEVLNRALS
NLSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMIIVMCVQIKCFHEIITIGYNVYHSY
DLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFTLYLIGFCM
FVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAY
MFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSF
TVDCEPSDLFRLQEYNIPGVIQSVIGWKTVRMYPFQIHSIALSTFASLIGPFGGFFASGF
KRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLIQQFLTLRPDQ
QLHIFNTLRSHLIDKGMLTSTTEDE
Enzyme 31 Number of Residues 445
Enzyme 31 Molecular Weight 51417.5
Enzyme 31 Theoretical pI 7.10
Enzyme 31 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
Component
  • cell part
  • membrane
Enzyme 31 General Function Involved in transferase activity, transferring phosphorus-containing groups
Enzyme 31 Specific Function Provides CDP-diacylglycerol an important precursor for the synthesis of phosphatidylinositol, phosphatidylglycerol, and cardiolipin
Enzyme 31 Pathways
Enzyme 31 Reactions
  • CTP + phosphatidate = diphosphate + CDP-diacylglycerol [RN:R01799]
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • 79-99 132-152 166-186 213-233 262-282 340-360
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 4186023 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID O95674 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name CDS2_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1338 bp
ATGACAGAGCTGAGGCAGAGGGTGGCCCATGAGCCGGTTGCGCCACCCGAGGACAAGGAG
TCAGAGTCAGAAGCAAAGGTAGATGGAGAGACTGCATCGGACAGTGAGAGCCGGGCAGAA
TCCGCACCCCTGCCAGTCTCTGCAGATGATACCCCGGAGGTCCTCAATAGGGCCCTTTCC
AACTTGTCTTCAAGATGGAAGAACTGGTGGGTGAGAGGCATCCTGACTTTGGCCATGATT
GCATTTTTCTTCATCATCATTTACCTGGGACCAATGGTTTTGATGATAATCGTGATGTGC
GTTCAGATTAAGTGTTTCCATGAGATAATCACTATTGGCTACAACGTCTACCACTCATAT
GATCTGCCCTGGTTCAGGACGCTCAGCTGGTACTTTCTCCTGTGTGTAAACTATTTCTTC
TATGGTGAGACAGTGACGGATTACTTCTTCACCCTGGTCCAGAGAGAAGAGCCTTTGCGG
ATTCTCAGTAAATACCACCGGTTCATTTCCTTTACTCTCTATCTAATAGGATTCTGCATG
TTTGTACTGAGTCTGGTCAAGAAGCATTATCGACTGCAGTTCTACATGTTTGGCTGGACC
CATGTGACATTGCTGATTGTTGTAACACAGTCACATCTTGTTATCCACAACCTATTTGAA
GGAATGATCTGGTTCATTGTCCCCATATCTTGTGTGATCTGTAATGACATCATGGCCTAT
ATGTTTGGCTTTTTCTTTGGTCGGACCCCACTCATCAAGCTGTCCCCGAAGAAGACCTGG
GAAGGCTTCATTGGGGGCTTCTTTGCTACTGTGGTGTTTGGCCTTCTGCTGTCCTATGTG
ATGTCCGGGTACAGATGCTTTGTCTGCCCTGTGGAGTACAACAATGACACCAACAGCTTC
ACTGTGGACTGTGAGCCCTCGGACCTGTTTCGCCTGCAGGAGTACAACATTCCTGGGGTG
ATCCAGTCAGTCATTGGCTGGAAAACGGTCCGGATGTACCCCTTCCAGATTCACAGCATC
GCTCTCTCCACCTTTGCCTCGCTCATTGGCCCCTTTGGAGGATTCTTCGCAAGTGGATTC
AAACGAGCCTTTAAAATCAAAGACTTTGCCAATACCATTCCTGGCCATGGAGGCATCATG
GATCGCTTTGACTGCCAGTATCTGATGGCCACCTTTGTCAATGTATACATCGCCAGTTTT
ATCAGAGGCCCTAACCCAAGCAAACTGATTCAGCAGTTCCTGACTTTACGGCCAGATCAG
CAGCTCCACATCTTCAACACGCTGCGGTCTCATCTGATCGACAAAGGGATGCTGACATCC
ACCACAGAGGACGAGTAG
Enzyme 31 GenBank Gene ID Y16521 Link Image
Enzyme 31 GeneCard ID CDS2 Link Image
Enzyme 31 GenAtlas ID CDS2 Link Image
Enzyme 31 HGNC ID HGNC:1801 Link Image
Enzyme 31 Chromosome Location 2
Enzyme 31 Locus 20p13
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Volta M, Bulfone A, Gattuso C, Rossi E, Mariani M, Consalez GG, Zuffardi O, Ballabio A, Banfi S, Franco B: Identification and characterization of CDS2, a mammalian homolog of the Drosophila CDP-diacylglycerol synthase gene. Genomics. 1999 Jan 1;55(1):68-77. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Halford S, Dulai KS, Daw SC, Fitzgibbon J, Hunt DM: Isolation and chromosomal localization of two human CDP-diacylglycerol synthase (CDS) genes. Genomics. 1998 Nov 15;54(1):140-4. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed Link Image]
  10. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 6030
Enzyme 32 Name Choline-phosphate cytidylyltransferase A
Enzyme 32 Synonyms
  1. CCT-alpha
  2. CTP:phosphocholine cytidylyltransferase A
  3. CCT A
  4. CT A
  5. Phosphorylcholine transferase A
Enzyme 32 Gene Name PCYT1A
Enzyme 32 Protein Sequence >Choline-phosphate cytidylyltransferase A
MDAQCSAKVNARKRRKEAPGPNGATEEDGVPSKVQRCAVGLRQPAPFSDEIEVDFSKPYV
RVTMEEASRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHN
FKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDD
VYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKY
HLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGPEGALK
HMLKEGKGRMLQAISPKQSPSSSPTRERSPSPSFRWPFSGKTSPPCSPANLSRHKAAAYD
ISEDEED
Enzyme 32 Number of Residues 367
Enzyme 32 Molecular Weight 41730.7
Enzyme 32 Theoretical pI 7.29
Enzyme 32 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • metabolic process
Component
Enzyme 32 General Function Involved in catalytic activity
Enzyme 32 Specific Function Controls phosphatidylcholine synthesis
Enzyme 32 Pathways
Enzyme 32 Reactions
  • CTP + choline phosphate = diphosphate + CDP-choline [RN:R01890]
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 28204946 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID P49585 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name PCY1A_HUMAN Link Image
Enzyme 32 PDB ID 1PEH Link Image
Enzyme 32 PDB File Show
Enzyme 32 3D Structure
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >1104 bp
ATGGATGCACAGTGTTCAGCCAAGGTCAATGCAAGGAAGAGGAGAAAAGAGGCGCCCGGA
CCCAACGGGGCAACAGAAGAAGATGGGGTTCCTTCCAAAGTGCAGCGCTGTGCAGTGGGC
TTACGGCAACCAGCTCCTTTTTCTGATGAAATTGAAGTTGACTTTAGTAAGCCCTATGTC
AGGGTAACTATGGAAGAAGCCAGCAGAGGAACTCCTTGTGAGCGACCTGTGAGAGTTTAT
GCCGATGGAATATTTGACTTATTTCACTCTGGTCACGCCCGAGCTCTGATGCAAGCGAAG
AACCTTTTCCCTAATACGTACCTCATTGTGGGAGTTTGCAGTGATGAGCTCACACACAAC
TTCAAAGGCTTCACGGTGATGAACGAGAATGAGCGCTATGACGCAGTCCAGCACTGCCGC
TACGTGGATGAGGTGGTGAGGAATGCGCCCTGGACGCTGACACCCGAGTTCCTGGCCGAA
CACCGGATTGATTTTGTAGCCCATGATGATATTCCTTATTCATCTGCTGGCAGTGATGAT
GTTTATAAGCACATCAAGGAGGCAGGCATGTTTGCTCCAACACAGAGGACAGAAGGTATC
TCCACATCAGACATCATCACCCGAATTGTGCGGGATTATGATGTGTATGCGAGGCGGAAC
CTGCAGAGGGGCTACACAGCAAAGGAGCTCAATGTCAGCTTTATCAACGAGAAGAAATAC
CACTTGCAGGAGAGGGTTGACAAAGTAAAGAAGAAAGTGAAAGATGTGGAGGAAAAGTCA
AAAGAATTTGTTCAGAAGGTGGAGGAAAAAAGCATTGACCTCATTCAGAAGTGGGAGGAG
AAGTCCCGAGAATTCATTGGAAGTTTTCTGGAAATGTTTGGTCCGGAAGGAGCACTGAAA
CATATGCTGAAAGAGGGGAAGGGCCGGATGCTGCAGGCCATCAGCCCGAAGCAGAGCCCC
AGCAGCAGCCCTACTCGCGAGCGCTCCCCCTCCCCCTCTTTCCGATGGCCCTTCTCCGGC
AAGACTTCCCCACCTTGCTCCCCAGCAAATCTCTCCAGGCACAAGGCTGCAGCCTATGAT
ATCAGTGAGGATGAAGAAGACTAA
Enzyme 32 GenBank Gene ID BC046355 Link Image
Enzyme 32 GeneCard ID PCYT1A Link Image
Enzyme 32 GenAtlas ID PCYT1A Link Image
Enzyme 32 HGNC ID HGNC:8754 Link Image
Enzyme 32 Chromosome Location 3
Enzyme 32 Locus 3q29
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Kalmar GB, Kay RJ, LaChance AC, Cornell RB: Primary structure and expression of a human CTP:phosphocholine cytidylyltransferase. Biochim Biophys Acta. 1994 Oct 18;1219(2):328-34. [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. Johnson JE, Cornell RB: Membrane-binding amphipathic alpha-helical peptide derived from CTP:phosphocholine cytidylyltransferase. Biochemistry. 1994 Apr 12;33(14):4327-35. [PubMed Link Image]
  4. Dunne SJ, Cornell RB, Johnson JE, Glover NR, Tracey AS: Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase. Biochemistry. 1996 Sep 17;35(37):11975-84. [PubMed Link Image]
  5. Xie M, Smith JL, Ding Z, Zhang D, Cornell RB: Membrane binding modulates the quaternary structure of CTP:phosphocholine cytidylyltransferase. J Biol Chem. 2004 Jul 2;279(27):28817-25. Epub 2004 Apr 6. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  8. Giorgianni F, Zhao Y, Desiderio DM, Beranova-Giorgianni S: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line. Electrophoresis. 2007 Jun;28(12):2027-34. [PubMed Link Image]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 6040
Enzyme 33 Name Phosphatidate cytidylyltransferase 1
Enzyme 33 Synonyms
  1. CDP-DAG synthase 1
  2. CDP-DG synthase 1
  3. CDP-diacylglycerol synthase 1
  4. CDS 1
  5. CDP-diglyceride pyrophosphorylase 1
  6. CDP-diglyceride synthase 1
  7. CTP:phosphatidate cytidylyltransferase 1
Enzyme 33 Gene Name CDS1
Enzyme 33 Protein Sequence >Phosphatidate cytidylyltransferase 1
MLELRHRGSCPGPREAVSPPHREGEAAGGDHETESTSDKETDIDDRYGDLDSRTDSDIPE
IPPSSDRTPEILKKALSGLSSRWKNWWIRGILTLTMISLFFLIIYMGSFMLMLLVLGIQV
KCFHEIITIGYRVYHSYDLPWFRTLSWYFLLCVNYFFYGETVADYFATFVQREEQLQFLI
RYHRFISFALYLAGFCMFVLSLVKKHYRLQFYMFAWTHVTLLITVTQSHLVIQNLFEGMI
WFLVPISSVICNDITAYLFGFFFGRTPLIKLSPKKTWEGFIGGFFSTVVFGFIAAYVLSK
YQYFVCPVEYRSDVNSFVTECEPSELFQLQTYSLPPFLKAVLRQERVSLYPFQIHSIALS
TFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVHVYITSFIRG
PNPSKVLQQLLVLQPEQQLNIYKTLKTHLIEKGILQPTLKV
Enzyme 33 Number of Residues 461
Enzyme 33 Molecular Weight 53303.6
Enzyme 33 Theoretical pI 8.19
Enzyme 33 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
Component
  • cell part
  • membrane
Enzyme 33 General Function Involved in transferase activity, transferring phosphorus-containing groups
Enzyme 33 Specific Function Provides CDP-diacylglycerol an important precursor for the synthesis of phosphatidylinositol (PtdIns), phosphatidylglycerol, and cardiolipin. Overexpression may amplify cellular signaling responses from cytokines. May also play an important role in the signal transduction mechanism of retina and neural cells
Enzyme 33 Pathways
Enzyme 33 Reactions
  • CTP + phosphatidate = diphosphate + CDP-diacylglycerol [RN:R01799]
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • 96-116 149-169 183-203 230-250 279-299 357-377
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 189054385 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q92903 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name CDS1_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >1386 bp
ATGTTGGAGCTGAGGCACCGGGGAAGCTGCCCCGGCCCCAGGGAAGCGGTGTCGCCGCCA
CACCGCGAGGGAGAGGCGGCCGGCGGCGACCACGAAACCGAGAGCACCAGCGACAAAGAA
ACAGATATTGATGACAGATATGGAGATTTGGATTCCAGAACAGATTCTGATATTCCGGAA
ATTCCACCATCCTCAGATAGAACCCCTGAGATTCTCAAAAAAGCTCTATCTGGTTTATCT
TCAAGGTGGAAAAACTGGTGGATACGTGGAATTCTCACTCTAACTATGATCTCGTTGTTT
TTCCTGATCATCTATATGGGATCCTTCATGCTGATGCTTCTTGTTCTGGGCATCCAAGTG
AAATGCTTCCATGAAATTATCACTATAGGTTATAGAGTCTATCATTCTTATGATCTACCA
TGGTTTAGAACACTAAGTTGGTACTTTCTATTGTGTGTAAACTACTTTTTCTATGGAGAG
ACTGTAGCTGATTATTTTGCTACATTTGTTCAAAGAGAAGAACAACTTCAGTTCCTCATT
CGCTACCATAGATTTATATCATTTGCCCTCTATCTGGCAGGTTTCTGCATGTTTGTACTG
AGTTTGGTGAAGAAACATTATCGTCTGCAGTTTTATATGTTCGCATGGACTCATGTCACT
TTACTGATAACTGTCACTCAGTCACACCTTGTCATCCAAAATCTGTTTGAAGGCATGATA
TGGTTCCTTGTTCCAATATCAAGTGTTATCTGCAATGACATAACTGCTTACCTTTTTGGA
TTTTTTTTTGGGAGAACTCCATTAATTAAGTTGTCTCCTAAAAAGACTTGGGAAGGATTC
ATTGGTGGTTTCTTTTCCACAGTTGTGTTTGGATTCATTGCTGCCTATGTGTTATCCAAA
TACCAGTACTTTGTCTGCCCAGTGGAATACCGAAGTGATGTAAACTCCTTCGTGACAGAA
TGTGAGCCCTCAGAACTTTTCCAGCTTCAGACTTACTCACTTCCACCCTTTCTAAAGGCA
GTCTTGAGACAGGAAAGAGTGAGCTTGTACCCTTTCCAGATCCACAGCATTGCACTGTCA
ACCTTTGCATCTTTAATTGGCCCATTTGGAGGCTTCTTTGCTAGTGGATTCAAAAGAGCC
TTCAAAATCAAGGATTTTGCAAATACCATTCCTGGACATGGTGGGATAATGGACAGATTT
GATTGTCAGTATTTGATGGCAACTTTTGTACATGTGTACATCACAAGTTTTATAAGGGGC
CCAAATCCCAGCAAAGTGCTACAGCAGTTGTTGGTGCTTCAACCTGAACAGCAGTTAAAT
ATATATAAAACCCTGAAGACTCATCTCATTGAGAAAGGAATCCTACAACCCACCTTGAAG
GTATAA
Enzyme 33 GenBank Gene ID AK314245 Link Image
Enzyme 33 GeneCard ID CDS1 Link Image
Enzyme 33 GenAtlas ID CDS1 Link Image
Enzyme 33 HGNC ID HGNC:1800 Link Image
Enzyme 33 Chromosome Location 4
Enzyme 33 Locus 4q21.23
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Heacock AM, Uhler MD, Agranoff BW: Cloning of CDP-diacylglycerol synthase from a human neuronal cell line. J Neurochem. 1996 Nov;67(5):2200-3. [PubMed Link Image]
  2. Weeks R, Dowhan W, Shen H, Balantac N, Meengs B, Nudelman E, Leung DW: Isolation and expression of an isoform of human CDP-diacylglycerol synthase cDNA. DNA Cell Biol. 1997 Mar;16(3):281-9. [PubMed Link Image]
  3. Lykidis A, Jackson PD, Rock CO, Jackowski S: The role of CDP-diacylglycerol synthetase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content. J Biol Chem. 1997 Dec 26;272(52):33402-9. [PubMed Link Image]
  4. Halford S, Dulai KS, Daw SC, Fitzgibbon J, Hunt DM: Isolation and chromosomal localization of two human CDP-diacylglycerol synthase (CDS) genes. Genomics. 1998 Nov 15;54(1):140-4. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 6049
Enzyme 34 Name Phosphatidylcholine:ceramide cholinephosphotransferase 2
Enzyme 34 Synonyms
  1. Sphingomyelin synthase 2
Enzyme 34 Gene Name SGMS2
Enzyme 34 Protein Sequence >Phosphatidylcholine:ceramide cholinephosphotransferase 2
MDIIETAKLEEHLENQPSDPTNTYARPAEPVEEENKNGNGKPKSLSSGLRKGTKKYPDYI
QIAMPTESRNKFPLEWWKTGIAFIYAVFNLVLTTVMITVVHERVPPKELSPPLPDKFFDY
IDRVKWAFSVSEINGIILVGLWITQWLFLRYKSIVGRRFCFIIGTLYLYRCITMYVTTLP
VPGMHFQCAPKLNGDSQAKVQRILRLISGGGLSITGSHILCGDFLFSGHTVTLTLTYLFI
KEYSPRHFWWYHLICWLLSAAGIICILVAHEHYTIDVIIAYYITTRLFWWYHSMANEKNL
KVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCKKYSRVQKIGED
NEKST
Enzyme 34 Number of Residues 365
Enzyme 34 Molecular Weight 42279.8
Enzyme 34 Theoretical pI 9.00
Enzyme 34 GO Classification
Function
  • catalytic activity
Process
Component
  • cell part
  • membrane
Enzyme 34 General Function Involved in catalytic activity
Enzyme 34 Specific Function Bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase. Required for cell growth
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions
  • a ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol [RN:R08969]
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • 80-100 128-148 159-179 206-226 248-268 275-295
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein Not Available
Enzyme 34 UniProtKB/Swiss-Prot ID Q8NHU3 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name SMS2_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1098 bp
ATGGATATCATAGAGACAGCAAAACTTGAAGAACATTTGGAAAATCAACCCAGTGATCCT
ACGAACACTTATGCAAGACCCGCTGAACCTGTTGAAGAAGAAAACAAAAATGGCAATGGT
AAACCCAAGAGCTTATCCAGTGGGCTGCGAAAAGGCACCAAAAAGTACCCGGACTATATC
CAAATTGCTATGCCCACTGAATCAAGGAACAAATTTCCACTAGAGTGGTGGAAAACGGGC
ATTGCCTTCATATATGCAGTTTTCAACCTCGTCTTGACAACCGTCATGATCACAGTTGTA
CATGAGAGGGTCCCTCCCAAGGAGCTTAGCCCTCCACTCCCAGACAAGTTTTTTGATTAC
ATTGATAGGGTGAAATGGGCATTTTCTGTATCAGAAATAAATGGGATTATATTAGTTGGA
TTATGGATCACCCAGTGGCTGTTTCTGAGATACAAGTCAATAGTGGGACGCAGATTCTGT
TTTATTATTGGAACTTTATACCTGTATCGCTGCATTACAATGTATGTTACTACTCTACCT
GTGCCTGGAATGCATTTCCAGTGTGCTCCAAAGCTCAATGGAGACTCTCAGGCAAAAGTT
CAACGGATTCTACGATTGATTTCTGGTGGTGGATTGTCCATAACTGGATCACATATCTTA
TGTGGAGACTTCCTCTTCAGCGGTCACACGGTTACGCTGACACTGACTTATTTGTTCATC
AAAGAATATTCGCCTCGTCACTTCTGGTGGTATCATTTAATCTGCTGGCTGCTGAGTGCT
GCCGGGATCATCTGCATTCTTGTAGCACACGAACACTACACTATCGATGTGATCATTGCT
TATTATATCACAACACGACTGTTTTGGTGGTACCATTCAATGGCCAATGAAAAGAACTTG
AAGGTCTCTTCACAGACTAATTTCTTATCTCGAGCATGGTGGTTCCCCATCTTTTATTTT
TTTGAGAAAAATGTACAAGGCTCAATTCCTTGCTGCTTCTCCTGGCCGCTGTCTTGGCCT
CCTGGCTGCTTCAAATCATCATGCAAAAAGTATTCACGGGTTCAGAAGATTGGTGAAGAC
AATGAGAAATCGACCTGA
Enzyme 34 GenBank Gene ID AF452717 Link Image
Enzyme 34 GeneCard ID SGMS2 Link Image
Enzyme 34 GenAtlas ID SGMS2 Link Image
Enzyme 34 HGNC ID HGNC:28395 Link Image
Enzyme 34 Chromosome Location 4
Enzyme 34 Locus 4q25
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 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. Huitema K, van den Dikkenberg J, Brouwers JF, Holthuis JC: Identification of a family of animal sphingomyelin synthases. EMBO J. 2004 Jan 14;23(1):33-44. Epub 2003 Dec 18. [PubMed Link Image]
  4. Dong J, Liu J, Lou B, Li Z, Ye X, Wu M, Jiang XC: Adenovirus-mediated overexpression of sphingomyelin synthases 1 and 2 increases the atherogenic potential in mice. J Lipid Res. 2006 Jun;47(6):1307-14. Epub 2006 Feb 28. [PubMed Link Image]
  5. Tafesse FG, Huitema K, Hermansson M, van der Poel S, van den Dikkenberg J, Uphoff A, Somerharju P, Holthuis JC: Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells. J Biol Chem. 2007 Jun 15;282(24):17537-47. Epub 2007 Apr 22. [PubMed Link Image]
  6. Tani M, Kuge O: Sphingomyelin synthase 2 is palmitoylated at the COOH-terminal tail, which is involved in its localization in plasma membranes. Biochem Biophys Res Commun. 2009 Apr 10;381(3):328-32. Epub 2009 Feb 20. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 6050
Enzyme 35 Name CDP-diacylglycerol--inositol 3-phosphatidyltransferase
Enzyme 35 Synonyms
  1. Phosphatidylinositol synthase
  2. PI synthase
  3. PtdIns synthase
Enzyme 35 Gene Name CDIPT
Enzyme 35 Protein Sequence >CDP-diacylglycerol--inositol 3-phosphatidyltransferase
MPDENIFLFVPNLIGYARIVFAIISFYFMPCCPLTASSFYLLSGLLDAFDGHAARALNQG
TRFGAMLDMLTDRCSTMCLLVNLALLYPGATLFFQISMSLDVASHWLHLHSSVVRGSESH
KMIDLSGNPVLRIYYTSRPALFTLCAGNELFYCLLYLFHFSEGPLVGSVGLFRMGLWVTA
PIALLKSLISVIHLITAARNMAALDAADRAKKK
Enzyme 35 Number of Residues 213
Enzyme 35 Molecular Weight 23538.5
Enzyme 35 Theoretical pI 8.13
Enzyme 35 GO Classification
Function
  • catalytic activity
  • phosphotransferase activity, for other substituted phosphate groups
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid biosynthetic process
  • phospholipid metabolic process
Component
  • cell part
  • membrane
Enzyme 35 General Function Involved in phosphotransferase activity, for other substituted phosphate groups
Enzyme 35 Specific Function Catalyzes the biosynthesis of phosphatidylinositol (PtdIns) as well as PtdIns:inositol exchange reaction. May thus act to reduce an excessive cellular PtdIns content. The exchange activity is due to the reverse reaction of PtdIns synthase and is dependent on CMP, which is tightly bound to the enzyme
Enzyme 35 Pathways
Enzyme 35 Reactions
  • CDP-diacylglycerol + myo-inositol = CMP + phosphatidyl-1D-myo-inositol [RN:R01802]
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • 6-26 29-49 76-96 140-160 175-195
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein Not Available
Enzyme 35 UniProtKB/Swiss-Prot ID O14735 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name CDIPT_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >642 bp
ATGCCAGACGAAAATATCTTCCTGTTCGTGCCCAACCTCATCGGTTATGCCCGGATTGTC
TTCGCCATCATTTCTTTCTACTTCATGCCCTGCTGCCCCCTCACGGCCTCCTCCTTCTAC
CTGCTCAGCGGCCTGCTGGACGCTTTCGATGGACACGCTGCTCGCGCTCTTAATCAAGGA
ACCCGGTTTGGGGCCATGCTGGACATGCTGACGGACCGCTGCTCCACCATGTGCCTGTTG
GTCAACCTGGCCCTGCTGTACCCTGGAGCCACGCTGTTCTTCCAAATCAGCATGAGTTTG
GATGTGGCCAGTCACTGGCTGCACCTCCACAGTTCTGTGGTCCGAGGCAGTGAGAGTCAC
AAGATGATCGACTTGTCCGGGAATCCGGTGCTTCGGATCTACTACACCTCGAGGCCTGCT
CTGTTCACCTTGTGTGCTGGGAATGAGCTCTTCTACTGCCTCCTCTACCTGTTCCATTTC
TCTGAGGGACCTTTAGTTGGCTCTGTGGGACTGTTCCGGATGGGCCTCTGGGTCACTGCC
CCCATCGCCTTGCTGAAGTCGCTCATCAGCGTCATCCACCTGATCACGGCCGCCCGCAAC
ATGGCTGCCCTGGACGCAGCAGACCGCGCCAAGAAGAAGTGA
Enzyme 35 GenBank Gene ID AF014807 Link Image
Enzyme 35 GeneCard ID CDIPT Link Image
Enzyme 35 GenAtlas ID CDIPT Link Image
Enzyme 35 HGNC ID HGNC:1769 Link Image
Enzyme 35 Chromosome Location 1
Enzyme 35 Locus 16p11.2
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Lykidis A, Jackson PD, Rock CO, Jackowski S: The role of CDP-diacylglycerol synthetase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content. J Biol Chem. 1997 Dec 26;272(52):33402-9. [PubMed Link Image]
  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. Antonsson BE: Purification and characterization of phosphatidylinositol synthase from human placenta. Biochem J. 1994 Feb 1;297 ( Pt 3):517-22. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 6054
Enzyme 36 Name Phosphatidylcholine:ceramide cholinephosphotransferase 1
Enzyme 36 Synonyms
  1. Medulla oblongata-derived protein
  2. Protein Mob
  3. Sphingomyelin synthase 1
  4. Transmembrane protein 23
Enzyme 36 Gene Name SGMS1
Enzyme 36 Protein Sequence >Phosphatidylcholine:ceramide cholinephosphotransferase 1
MLSASTMKEVVYWSPKKVADWLLENAMPEYCEPLEHFTGQDLINLTQEDFKKPPLCRVSS
DNGQRLLDMIETLKMEHHLEAHKNGHANGHLNIGVDIPTPDGSFSIKIKPNGMPNGYRKE
MIKIPMPELERSQYPMEWGKTFLAFLYALSCFVLTTVMISVVHERVPPKEVQPPLPDTFF
DHFNRVQWAFSICEINGMILVGLWLIQWLLLKYKSIISRRFFCIVGTLYLYRCITMYVTT
LPVPGMHFNCSPKLFGDWEAQLRRIMKLIAGGGLSITGSHNMCGDYLYSGHTVMLTLTYL
FIKEYSPRRLWWYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYHTMANQQ
VLKEASQMNLLARVWWYRPFQYFEKNVQGIVPRSYHWPFPWPVVHLSRQVKYSRLVNDT
Enzyme 36 Number of Residues 419
Enzyme 36 Molecular Weight 49207.3
Enzyme 36 Theoretical pI 8.51
Enzyme 36 GO Classification
Function
  • catalytic activity
Process
Component
  • cell part
  • membrane
Enzyme 36 General Function Involved in catalytic activity
Enzyme 36 Specific Function Bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase. Suppresses BAX-mediated apoptosis and also prevents cell death in response to stimuli such as hydrogen peroxide, osmotic stress, elevated temperature and exogenously supplied sphingolipids. May protect against cell death by reversing the stress-inducible increase in levels of proapoptotic ceramide. Required for cell growth
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions
  • a ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol [RN:R08969]
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • 142-162 190-210 221-241 282-302 310-330
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 29789379 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q86VZ5 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name SMS1_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >1242 bp
ATGAAGGAAGTGGTTTATTGGTCACCCAAGAAGGTGGCAGACTGGCTGCTGGAGAATGCT
ATGCCAGAATACTGTGAGCCTCTGGAGCATTTCACAGGCCAGGACTTGATCAACCTAACC
CAAGAGGATTTCAAAAAACCCCCCTTGTGCCGAGTCTCCTCTGACAATGGGCAGCGGCTC
CTGGACATGATAGAAACCCTGAAAATGGAGCACCATTTGGAAGCACACAAGAACGGCCAT
GCCAATGGGCACCTCAACATTGGCGTAGACATCCCCACCCCCGACGGCAGCTTCAGCATC
AAGATTAAACCCAACGGGATGCCAAATGGGTATAGGAAAGAGATGATAAAGATCCCCATG
CCAGAACTGGAGCGCTCTCAGTACCCCATGGAGTGGGGCAAGACTTTTCTGGCCTTTCTT
TATGCACTTTCCTGTTTCGTTCTCACCACAGTGATGATCTCGGTCGTCCACGAACGAGTA
CCTCCTAAGGAGGTGCAGCCTCCACTACCGGACACATTTTTTGACCATTTTAACCGGGTG
CAGTGGGCCTTTTCTATTTGTGAAATTAATGGCATGATCCTTGTAGGACTCTGGTTAATT
CAGTGGCTGCTCTTAAAATACAAGTCTATTATTAGCAGAAGATTTTTCTGCATAGTTGGC
ACGCTGTACCTGTATCGGTGTATTACAATGTATGTAACTACACTCCCAGTACCTGGTATG
CATTTCAACTGTTCTCCGAAGCTTTTCGGAGACTGGGAAGCCCAACTGCGAAGAATAATG
AAGCTCATTGCTGGAGGTGGCTTGTCTATCACTGGCTCTCACAACATGTGTGGGGACTAT
CTGTACAGCGGCCACACGGTCATGCTAACACTTACCTACTTATTTATCAAAGAGTATTCC
CCTCGGCGACTCTGGTGGTATCACTGGATTTGCTGGCTTCTCAGCGTAGTTGGAATCTTC
TGTATTCTCTTAGCGCATGACCACTACACTGTGGACGTGGTGGTGGCATATTACATCACC
ACGAGACTCTTCTGGTGGTATCACACTATGGCCAATCAGCAAGTGCTAAAGGAAGCTTCC
CAGATGAACCTCCTGGCCAGGGTGTGGTGGTACAGGCCATTTCAGTACTTTGAAAAGAAT
GTCCAAGGAATTGTACCTCGATCTTACCATTGGCCTTTCCCCTGGCCAGTAGTCCACCTC
AGTAGGCAAGTTAAATACAGCCGGCTGGTGAATGACACATAA
Enzyme 36 GenBank Gene ID Not Available
Enzyme 36 GeneCard ID SGMS1 Link Image
Enzyme 36 GenAtlas ID SGMS1 Link Image
Enzyme 36 HGNC ID HGNC:29799 Link Image
Enzyme 36 Chromosome Location 1
Enzyme 36 Locus 10q11.2
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Yamaoka S, Miyaji M, Kitano T, Umehara H, Okazaki T: Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells. J Biol Chem. 2004 Apr 30;279(18):18688-93. Epub 2004 Feb 19. [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. Vladychenskaya IP, Dergunova LV, Dmitrieva VG, Limborska SA: Human gene MOB: structure specification and aspects of transcriptional activity. Gene. 2004 Sep 1;338(2):257-65. [PubMed Link Image]
  5. Vladychenskaya IP, Dergunova LV, Limborska SA: In vitro and in silico analysis of the predicted human MOB gene encoding a phylogenetically conserved transmembrane protein. Biomol Eng. 2002 Feb;18(6):263-8. [PubMed Link Image]
  6. Huitema K, van den Dikkenberg J, Brouwers JF, Holthuis JC: Identification of a family of animal sphingomyelin synthases. EMBO J. 2004 Jan 14;23(1):33-44. Epub 2003 Dec 18. [PubMed Link Image]
  7. Dong J, Liu J, Lou B, Li Z, Ye X, Wu M, Jiang XC: Adenovirus-mediated overexpression of sphingomyelin synthases 1 and 2 increases the atherogenic potential in mice. J Lipid Res. 2006 Jun;47(6):1307-14. Epub 2006 Feb 28. [PubMed Link Image]
  8. Tafesse FG, Huitema K, Hermansson M, van der Poel S, van den Dikkenberg J, Uphoff A, Somerharju P, Holthuis JC: Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells. J Biol Chem. 2007 Jun 15;282(24):17537-47. Epub 2007 Apr 22. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 6417
Enzyme 37 Name Rap guanine nucleotide exchange factor 2
Enzyme 37 Synonyms
  1. Neural RAP guanine nucleotide exchange protein
  2. nRap GEP
  3. PDZ domain-containing guanine nucleotide exchange factor 1
  4. PDZ-GEF1
  5. RA-GEF
Enzyme 37 Gene Name RAPGEF2
Enzyme 37 Protein Sequence >Rap guanine nucleotide exchange factor 2
MKPLAIPANHGVMGQQEKHSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLS
DIYQATESEAGDMDLSGLPETAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTD
DDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAGTIVLNDGEELDSWSVILNGS
VEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEK
NMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLL
TYRTFLSSPMEVGKKLLEWFNDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENN
LEREKMGGHLRLLNIACAAKAKRRLMTLTKPSREAPLPFILLGGSEKGFGIFVDSVDSGS
KATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEE
KRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKT
RISILPQKPYNDIGIGQSQDDSIVGLRQTKHIPTALPVSGTLSSSNPDLLQSHHRILDFS
ATPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIREFAVTATPDQYSLCEVSVTPE
GVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVE
VATQLSMRNFELFRNIEPTEYIDDLFKLRSKTSCANLKRFEEVINQETFWVASEILRETN
QLKRMKIIKHFIKIALHCRECKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDL
QDLFDPSRNMAKYRNVLNSQNLQPPIIPLFPVIKKDLTFLHEGNDSKVDGLVNFEKLRMI
AKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSTNATVLDVAQTGGHKKRVRRSS
FLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATNTLPKNPGDKKPVKSE
TSPVAPRAGSQQKAQSLPQPQQQPPPAHKINQGLQVPAVSLYPSRKKVPVKDLPPFGINS
PQALKKILSLSEEGSLERHKKQAEDTISNASSQLSSPPTSPQSSPRKGYTLAPSGTVDNF
SDSGHSEISSRSSIVSNSSFDSVPVSLHDERRQRHSVSIVETNLGMGRMERRTMIEPDQY
SLGSYAPMSEGRGLYATATVISSPSTEELSQDQGDRASLDAADSGRGSWTSCSSGSHDNI
QTIQHQRSWETLPFGHTHFDYSGDPAGLWASSSHMDQIMFSDHSTKYNRQNQSRESLEQA
QSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSIEAESSSLTSVTTEETKPVPMPAHIAV
ASSTTKGLIARKEGRYREPPPTPPGYIGIPITDFPEGHSHPARKPPDYNVALQRSRMVAR
SSDTAGPSSVQQPHGHPTSSRPVNKPQWHKPNESDPRLAPYQSQGFSTEEDEDEQVSAV
Enzyme 37 Number of Residues 1499
Enzyme 37 Molecular Weight 167415.5
Enzyme 37 Theoretical pI 6.64
Enzyme 37 GO Classification
Function
  • GTPase regulator activity
  • binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • protein binding
Process
  • biological regulation
  • intracellular 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
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 37 General Function Involved in protein binding
Enzyme 37 Specific Function Guanine nucleotide exchange factor (GEF) for Rap1A, Rap1B and Rap2B GTPases. Does not interact with cAMP or cGMP
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions Not Available
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 7657261 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q9Y4G8 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name RPGF2_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >4500 bp
ATGAAACCACTAGCAATCCCAGCTAACCATGGAGTTATGGGCCAGCAGGAGAAACACTCA
CTTCCTGCAGATTTCACAAAACTGCATCTTACTGACAGTCTCCACCCACAGGTGACCCAC
GTTTCTTCTAGCCATTCAGGATGTAGTATCACTAGTGATTCTGGGAGCAGCAGTCTTTCT
GATATCTACCAGGCCACAGAAAGCGAGGCTGGTGATATGGACCTGAGTGGGTTGCCAGAA
ACAGCAGTGGATTCCGAAGACGACGACGATGAAGAAGACATTGAGAGAGCATCAGATCCT
CTGATGAGCAGGGACATTGTGAGAGACTGCCTAGAGAAGGACCCAATTGACCGGACAGAT
GATGACATTGAACAACTCTTGGAATTTATGCACCAGTTGCCTGCTTTTGCCAATATGACA
ATGTCAGTGAGGCGAGAACTCTGTGCTGTGATGGTGTTCGCAGTGGTGGAAAGAGCAGGG
ACCATAGTGTTAAATGATGGTGAAGAGCTGGACTCCTGGTCAGTGATTCTCAATGGATCT
GTGGAAGTGACTTATCCAGATGGAAAAGCAGAAATACTGTGCATGGGAAATAGTTTTGGT
GTCTCTCCTACCATGGACAAAGAATACATGAAAGGAGTGATGAGAACAAAGGTGGATGAC
TGCCAGTTTGTCTGCATAGCCCAGCAAGATTACTGCCGTATTCTCAATCAAGTAGAAAAG
AACATGCAAAAAGTTGAAGAGGAAGGAGAGATTGTTATGGTGAAAGAACACCGAGAACTT
GATCGAACTGGAACAAGAAAGGGACACATTGTCATCAAGGGTACCTCAGAAAGGTTAACA
ATGCATTTGGTGGAAGAGCATTCAGTAGTAGATCCAACATTCATAGAAGACTTTCTGTTG
ACCTATAGGACTTTTCTTTCTAGCCCAATGGAAGTGGGCAAAAAGTTATTGGAGTGGTTT
AATGACCCGAGCCTCAGGGATAAGGTTACACGGGTAGTATTATTGTGGGTAAATAATCAC
TTCAATGACTTTGAAGGAGATCCTGCAATGACTCGATTTTTAGAAGAATTTGAAAACAAT
CTGGAAAGAGAGAAAATGGGTGGACACCTAAGGCTGTTGAATATCGCGTGTGCTGCTAAA
GCAAAAAGAAGATTGATGACGTTAACAAAACCATCCCGAGAAGCTCCTTTGCCTTTTATC
TTACTTGGAGGCTCTGAGAAGGGATTTGGAATCTTTGTTGACAGTGTAGATTCAGGTAGC
AAAGCAACTGAAGCAGGCTTGAAACGGGGGGATCAGATATTAGAAGTAAATGGCCAAAAC
TTTGAAAACATTCAGCTGTCAAAAGCTATGGAAATTCTTAGAAATAACACACATTTATCT
ATCACTGTGAAAACCAATTTATTTGTATTTAAAGAACTTCTAACAAGATTGTCAGAAGAG
AAAAGAAATGGTGCCCCCCACCTTCCTAAAATTGGTGACATTAAAAAGGCCAGTCGCTAC
TCCATTCCAGATCTTGCTGTAGATGTAGAACAGGTGATAGGACTTGAAAAAGTGAACAAA
AAAAGTAAAGCCAACACTGTGGGAGGAAGGAACAAGCTGAAAAAGATACTCGACAAGACT
CGGATCAGTATCTTGCCACAGAAACCATACAATGATATTGGGATTGGTCAGTCTCAAGAT
GACAGCATAGTAGGATTAAGGCAGACAAAGCACATCCCAACTGCATTGCCTGTCAGTGGA
ACCTTATCATCCAGTAATCCTGATTTATTGCAGTCACATCATCGCATTTTAGACTTCAGT
GCTACTCCTGACTTGCCAGATCAAGTGCTAAGGGTTTTTAAGGCTGATCAGCAAAGCCGC
TACATCATGATCAGTAAGGACACTACAGCAAAGGAAGTGGTCATTCAGGCTATCAGGGAG
TTTGCTGTTACTGCCACCCCGGATCAATATTCACTATGTGAGGTCTCTGTCACACCTGAG
GGAGTAATCAAACAAAGAAGACTTCCAGATCAGCTTTCCAAACTTGCAGACAGAATACAA
CTGAGTGGAAGGTATTATCTGAAAAACAACATGGAAACAGAAACTCTTTGTTCAGATGAA
GATGCTCAGGAGTTGTTGAGAGAGAGTCAAATTTCCCTCCTTCAGCTCAGCACTGTGGAA
GTTGCAACACAGCTCTCTATGCGAAATTTTGAACTCTTTCGCAACATTGAACCTACTGAA
TATATAGATGATTTATTTAAACTCAGATCAAAAACCAGCTGTGCCAACCTGAAGAGATTT
GAAGAAGTCATTAACCAGGAAACATTTTGGGTAGCATCTGAAATTCTCAGAGAAACAAAC
CAGCTGAAGAGGATGAAGATCATTAAGCATTTCATCAAGATAGCACTGCACTGTAGGGAA
TGCAAGAATTTTAACTCAATGTTTGCAATCATCAGTGGCCTAAACCTGGCACCAGTGGCA
AGACTGCGAACGACCTGGGAGAAACTTCCCAATAAATACGAAAAACTATTTCAAGATCTC
CAAGACCTGTTTGATCCTTCCAGAAACATGGCAAAATATCGTAATGTTCTCAATAGTCAA
AATCTACAACCTCCCATAATCCCTCTATTCCCAGTTATCAAAAAGGATCTCACCTTCCTT
CACGAAGGAAATGACTCAAAAGTAGACGGGCTGGTCAATTTTGAGAAGCTAAGGATGATT
GCAAAAGAAATTCGTCACGTTGGCCGAATGGCTTCAGTGAACATGGACCCTGCCCTCATG
TTCAGGACTCGGAAGAAGAAATGGCGGAGTTTGGGGTCTCTCAGCCAGGGTAGTACAAAT
GCAACAGTGCTAGATGTTGCTCAGACAGGTGGTCATAAAAAGCGGGTACGTCGTAGTTCC
TTTCTCAATGCCAAAAAGCTTTATGAAGATGCCCAAATGGCTCGAAAAGTGAAGCAGTAC
CTTTCCAATTTGGAGCTAGAAATGGACGAGGAGAGTCTTCAGACATTATCTCTGCAGTGT
GAGCCAGCAACCAACACATTGCCTAAGAATCCTGGTGACAAAAAGCCTGTCAAATCCGAG
ACCTCTCCAGTAGCTCCAAGGGCAGGGTCACAACAGAAAGCTCAGTCCCTGCCACAGCCC
CAGCAGCAGCCACCACCAGCACATAAAATCAACCAGGGACTACAGGTTCCCGCCGTGTCC
CTTTATCCTTCACGGAAGAAAGTGCCCGTAAAGGATCTCCCACCTTTTGGCATAAACTCT
CCACAAGCTTTAAAAAAAATTCTTTCTTTGTCTGAAGAAGGAAGTTTGGAACGTCACAAG
AAACAGGCTGAAGATACAATATCAAATGCATCTTCGCAGCTTTCTTCTCCTCCTACTTCT
CCACAGAGTTCTCCAAGGAAAGGCTATACTTTGGCTCCCAGTGGTACTGTGGATAATTTT
TCAGATTCTGGTCACAGTGAAATTTCTTCACGATCCAGTATTGTTAGCAATTCGTCTTTT
GACTCAGTGCCAGTCTCACTGCACGATGAGAGGCGCCAGAGGCATTCTGTCAGCATCGTG
GAAACAAACCTAGGGATGGGCAGGATGGAGAGGCGGACCATGATTGAACCTGATCAGTAT
AGCTTGGGGTCCTATGCACCAATGTCCGAGGGCCGAGGCTTATATGCTACAGCTACAGTA
ATTTCTTCTCCAAGCACAGAGGAACTTTCCCAGGATCAGGGGGATCGCGCGTCACTTGAT
GCTGCTGACAGTGGCCGTGGGAGCTGGACGTCATGCTCAAGTGGCTCCCATGATAATATA
CAGACGATCCAGCACCAGAGAAGCTGGGAGACTCTTCCATTCGGGCATACTCACTTTGAT
TATTCAGGGGATCCTGCAGGTTTATGGGCATCAAGCAGCCATATGGACCAAATTATGTTT
TCTGATCATAGCACAAAGTATAACAGGCAAAATCAAAGTAGAGAGAGCCTTGAACAAGCC
CAGTCCCGAGCAAGCTGGGCGTCTTCCACAGGTTACTGGGGAGAAGACTCAGAAGGTGAC
ACAGGCACAATAAAGCGGAGGGGTGGAAAGGATGTTTCCATTGAAGCCGAAAGCAGTAGC
CTAACGTCTGTGACTACGGAAGAAACCAAGCCTGTCCCCATGCCTGCCCACATAGCTGTG
GCATCAAGTACTACAAAGGGGCTCATTGCACGAAAGGAGGGCAGGTATCGAGAGCCCCCG
CCCACCCCTCCCGGCTACATTGGAATTCCCATTACTGACTTTCCAGAAGGGCACTCCCAT
CCAGCCAGGAAACCGCCGGACTACAACGTGGCCCTTCAGAGATCGCGGATGGTCGCACGA
TCCTCCGACACAGCTGGGCCTTCATCCGTACAGCAGCCACATGGGCATCCCACCAGCAGC
AGGCCTGTGAACAAACCTCAGTGGCATAAACCGAACGAGTCTGACCCGCGCCTCGCCCCC
TATCAGTCCCAAGGGTTTTCCACCGAGGAGGATGAAGATGAACAAGTTTCTGCTGTTTGA
Enzyme 37 GenBank Gene ID NM_014247.2 Link Image
Enzyme 37 GeneCard ID RAPGEF2 Link Image
Enzyme 37 GenAtlas ID RAPGEF2 Link Image
Enzyme 37 HGNC ID HGNC:16854 Link Image
Enzyme 37 Chromosome Location 4
Enzyme 37 Locus 4q32.1
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  2. Ohtsuka T, Hata Y, Ide N, Yasuda T, Inoue E, Inoue T, Mizoguchi A, Takai Y: nRap GEP: a novel neural GDP/GTP exchange protein for rap1 small G protein that interacts with synaptic scaffolding molecule (S-SCAM). Biochem Biophys Res Commun. 1999 Nov;265(1):38-44. [PubMed Link Image]
  3. de Rooij J, Boenink NM, van Triest M, Cool RH, Wittinghofer A, Bos JL: PDZ-GEF1, a guanine nucleotide exchange factor specific for Rap1 and Rap2. J Biol Chem. 1999 Dec 31;274(53):38125-30. [PubMed Link Image]
  4. Rebhun JF, Castro AF, Quilliam LA: Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction. J Biol Chem. 2000 Nov 10;275(45):34901-8. [PubMed Link Image]
  5. 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]
  6. 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]
  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. 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 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 6449
Enzyme 38 Name RAF proto-oncogene serine/threonine-protein kinase
Enzyme 38 Synonyms
  1. Proto-oncogene c-RAF
  2. cRaf
  3. Raf-1
Enzyme 38 Gene Name RAF1
Enzyme 38 Protein Sequence >RAF proto-oncogene serine/threonine-protein kinase
MEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRV
FLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAAS
LIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKV
PTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFTF
NTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIEDAIRSHSESASPSALSSSPNNL
SPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSF
GTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIV
TQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL
TVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYE
LMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFP
QILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVF
Enzyme 38 Number of Residues 648
Enzyme 38 Molecular Weight 73051.0
Enzyme 38 Theoretical pI 9.62
Enzyme 38 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • molecular transducer activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • receptor signaling protein activity
  • signal transducer activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biological regulation
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 38 General Function Involved in intracellular signaling pathway
Enzyme 38 Specific Function Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. Part of the Ras-dependent signaling pathway from receptors to the nucleus. Protects cells from apoptosis mediated by STK3
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 35842 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID P04049 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name RAF1_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >1947 bp
ATGGAGCACATACAGGGAGCTTGGAAGACGATCAGCAATGGTTTTGGATTCAAAGATGCC
GTGTTTGATGGCTCCAGCTGCATCTCTCCTACAATAGTTCAGCAGTTTGGCTATCAGCGC
CGGGCATCAGATGATGGCAAACTCACAGATCCTTCTAAGACAAGCAACACTATCCGTGTT
TTCTTGCCGAACAAGCAAAGAACAGTGGTCAATGTGCGAAATGGAATGAGCTTGCATGAC
TGCCTTATGAAAGCACTCAAGGTGAGGGGCCTGCAACCAGAGTGCTGTGCAGTGTTCAGA
CTTCTCCACGAACACAAAGGTAAAAAAGCACGCTTAGATTGGAATACTGATGCTGCGTCT
TTGATTGGAGAAGAACTTCAAGTAGATTTCCTGGATCATGTTCCCCTCACAACACACAAC
TTTGCTCGGAAGACGTTCCTGAAGCTTGCCTTCTGTGACATCTGTCAGAAATTCCTGCTC
AATGGATTTCGATGTCAGACTTGTGGCTACAAATTTCATGAGCACTGTAGCACCAAAGTA
CCTACTATGTGTGTGGACTGGAGTAACATCAGACAACTCTTATTGTTTCCAAATTCCACT
ATTGGTGATAGTGGAGTCCCAGCACTACCTTCTTTGACTATGCGTCGTATGCGAGAGTCT
GTTTCCAGGATGCCTGTTAGTTCTCAGCACAGATATTCTACACCTCACGCCTTCACCTTT
AACACCTCCAGTCCCTCATCTGAAGGTTCCCTCTCCCAGAGGCAGAGGTCGACATCCACA
CCTAATGTCCACATGGTCAGCACCACGCTGCCTGTGGACAGCAGGATGATTGAGGATGCA
ATTCGAAGTCACAGCGAATCAGCCTCACCTTCAGCCCTGTCCAGTAGCCCCAACAATCTG
AGCCCAACAGGCTGGTCACAGCCGAAAACCCCCGTGCCAGCACAAAGAGAGCGGGCACCA
GTATCTGGGACCCAGGAGAAAAACAAAATTAGGCCTCGTGGACAGAGAGATTCAAGCTAT
TATTGGGAAATAGAAGCCAGTGAAGTGATGCTGTCCACTCGGATTGGGTCAGGCTCTTTT
GGAACTGTTTATAAGGGTAAATGGCACGGAGATGTTGCAGTAAAGATCCTAAAGGTTGTC
GACCCAACCCCAGAGCAATTCCAGGCCTTCAGGAATGAGGTGGCTGTTCTGCGCAAAACA
CGGCATGTGAACATTCTGCTTTTCATGGGGTACATGACAAAGGACAACCTGGCAATTGTG
ACCCAGTGGTGCGAGGGCAGCAGCCTCTACAAACACCTGCATGTCCAGGAGACCAAGTTT
CAGATGTTCCAGCTAATTGACATTGCCCGGCAGACGGCTCAGGGAATGGACTATTTGCAT
GCAAAGAACATCATCCATAGAGACATGAAATCCAACAATATATTTCTCCATGAAGGCTTA
ACAGTGAAAATTGGAGATTTTGGTTTGGCAACAGTAAAGTCACGCTGGAGTGGTTCTCAG
CAGGTTGAACAACCTACTGGCTCTGTCCTCTGGATGGCCCCAGAGGTGATCCGAATGCAG
GATAACAACCCATTCAGTTTCCAGTCGGATGTCTACTCCTATGGCATCGTATTGTATGAA
CTGATGACGGGGGAGCTTCCTTATTCTCACATCAACAACCGAGATCAGATCATCTTCATG
GTGGGCCGAGGATATGCCTCCCCAGATCTTAGTAAGCTATATAAGAACTGCCCCAAAGCA
ATGAAGAGGCTGGTAGCTGACTGTGTGAAGAAAGTAAAGGAAGAGAGGCCTCTTTTTCCC
CAGATCCTGTCTTCCATTGAGCTGCTCCAACACTCTCTACCGAAGATCAACCGGAGCGCT
TCCGAGCCATCCTTGCATCGGGCAGCCCACACTGAGGATATCAATGCTTGCACGCTGACC
ACGTCCCCGAGGCTGCCTGTCTTCTAG
Enzyme 38 GenBank Gene ID X03484 Link Image
Enzyme 38 GeneCard ID RAF1 Link Image
Enzyme 38 GenAtlas ID RAF1 Link Image
Enzyme 38 HGNC ID HGNC:9829 Link Image
Enzyme 38 Chromosome Location 3
Enzyme 38 Locus 3p25
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Bonner TI, Oppermann H, Seeburg P, Kerby SB, Gunnell MA, Young AC, Rapp UR: The complete coding sequence of the human raf oncogene and the corresponding structure of the c-raf-1 gene. Nucleic Acids Res. 1986 Jan 24;14(2):1009-15. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. 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. Bonner TI, Kerby SB, Sutrave P, Gunnell MA, Mark G, Rapp UR: Structure and biological activity of human homologs of the raf/mil oncogene. Mol Cell Biol. 1985 Jun;5(6):1400-7. [PubMed Link Image]
  5. Yao B, Zhang Y, Delikat S, Mathias S, Basu S, Kolesnick R: Phosphorylation of Raf by ceramide-activated protein kinase. Nature. 1995 Nov 16;378(6554):307-10. [PubMed Link Image]
  6. Dozier C, Ansieau S, Ferreira E, Coll J, Stehelin D: An alternatively spliced c-mil/raf mRNA is predominantly expressed in chicken muscular tissues and conserved among vertebrate species. Oncogene. 1991 Aug;6(8):1307-11. [PubMed Link Image]
  7. Morrison DK, Heidecker G, Rapp UR, Copeland TD: Identification of the major phosphorylation sites of the Raf-1 kinase. J Biol Chem. 1993 Aug 15;268(23):17309-16. [PubMed Link Image]
  8. Dubois T, Rommel C, Howell S, Steinhussen U, Soneji Y, Morrice N, Moelling K, Aitken A: 14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction. J Biol Chem. 1997 Nov 14;272(46):28882-8. [PubMed Link Image]
  9. King AJ, Sun H, Diaz B, Barnard D, Miao W, Bagrodia S, Marshall MS: The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338. Nature. 1998 Nov 12;396(6707):180-3. [PubMed Link Image]
  10. Wang Y, Waldron RT, Dhaka A, Patel A, Riley MM, Rozengurt E, Colicelli J: The RAS effector RIN1 directly competes with RAF and is regulated by 14-3-3 proteins. Mol Cell Biol. 2002 Feb;22(3):916-26. [PubMed Link Image]
  11. Kunapuli P, Kasyapa CS, Hawthorn L, Cowell JK: LGI1, a putative tumor metastasis suppressor gene, controls in vitro invasiveness and expression of matrix metalloproteinases in glioma cells through the ERK1/2 pathway. J Biol Chem. 2004 May 28;279(22):23151-7. Epub 2004 Mar 26. [PubMed Link Image]
  12. O'Neill E, Rushworth L, Baccarini M, Kolch W: Role of the kinase MST2 in suppression of apoptosis by the proto-oncogene product Raf-1. Science. 2004 Dec 24;306(5705):2267-70. [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. Rodriguez-Viciana P, Oses-Prieto J, Burlingame A, Fried M, McCormick F: A phosphatase holoenzyme comprised of Shoc2/Sur8 and the catalytic subunit of PP1 functions as an M-Ras effector to modulate Raf activity. Mol Cell. 2006 Apr 21;22(2):217-30. [PubMed Link Image]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
  19. 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]
  20. 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]
  21. 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]
  22. Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A: The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature. 1995 Jun 15;375(6532):554-60. [PubMed Link Image]
  23. Nassar N, Horn G, Herrmann C, Block C, Janknecht R, Wittinghofer A: Ras/Rap effector specificity determined by charge reversal. Nat Struct Biol. 1996 Aug;3(8):723-9. [PubMed Link Image]
  24. Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC: Solution structure of the Ras-binding domain of c-Raf-1 and identification of its Ras interaction surface. Biochemistry. 1995 May 30;34(21):6911-8. [PubMed Link Image]
  25. Mott HR, Carpenter JW, Zhong S, Ghosh S, Bell RM, Campbell SL: The solution structure of the Raf-1 cysteine-rich domain: a novel ras and phospholipid binding site. Proc Natl Acad Sci U S A. 1996 Aug 6;93(16):8312-7. [PubMed Link Image]
  26. Pandit B, Sarkozy A, Pennacchio LA, Carta C, Oishi K, Martinelli S, Pogna EA, Schackwitz W, Ustaszewska A, Landstrom A, Bos JM, Ommen SR, Esposito G, Lepri F, Faul C, Mundel P, Lopez Siguero JP, Tenconi R, Selicorni A, Rossi C, Mazzanti L, Torrente I, Marino B, Digilio MC, Zampino G, Ackerman MJ, Dallapiccola B, Tartaglia M, Gelb BD: Gain-of-function RAF1 mutations cause Noonan and LEOPARD syndromes with hypertrophic cardiomyopathy. Nat Genet. 2007 Aug;39(8):1007-12. Epub 2007 Jul 1. [PubMed Link Image]
  27. Razzaque MA, Nishizawa T, Komoike Y, Yagi H, Furutani M, Amo R, Kamisago M, Momma K, Katayama H, Nakagawa M, Fujiwara Y, Matsushima M, Mizuno K, Tokuyama M, Hirota H, Muneuchi J, Higashinakagawa T, Matsuoka R: Germline gain-of-function mutations in RAF1 cause Noonan syndrome. Nat Genet. 2007 Aug;39(8):1013-7. Epub 2007 Jul 1. [PubMed Link Image]
  28. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 6476
Enzyme 39 Name Protein kinase C alpha type
Enzyme 39 Synonyms
  1. PKC-A
  2. PKC-alpha
Enzyme 39 Gene Name PRKCA
Enzyme 39 Protein Sequence >Protein kinase C alpha type
MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGF
GKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGS
LLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDA
KNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRL
SVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNME
LRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKG
TEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYV
NGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIA
DFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDG
EDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTKHPAKRLGCGPEGERDVREHAFFRRI
DWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVN
PQFVHPILQSAV
Enzyme 39 Number of Residues 672
Enzyme 39 Molecular Weight 76763.5
Enzyme 39 Theoretical pI 7.05
Enzyme 39 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • metal ion binding
  • nucleoside binding
  • protein kinase C activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • zinc ion binding
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 39 General Function Involved in protein serine/threonine kinase activity
Enzyme 39 Specific Function PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 35483 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID P17252 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name KPCA_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >2019 bp
ATGGCTGACGTTTTCCCGGGCAACGACTCCACGGCGTCTCAGGACGTGGCCAACCGCTTC
GCCCGCAAAGGGGCGCTGAGGCAGAAGAACGTGCACGAGGTGAAGGACCACAAATTCATC
GCGCGCTTCTTCAAGCAGCCCACCTTCTGCAGCCACTGCACCGACTTCATCTGGGGGTTT
GGGAAACAAGGCTTCCAGTGCCAAGTTTGCTGTTTTGTGGTCCACAAGAGGTGCCATGAA
TTTGTTACTTTTTCTTGTCCGGGTGCGGATAAGGGACCCGACACTGATGACCCCAGGAGC
AAGCACAAGTTCAAAATCCACACTTACGGAAGCCCCACCTTCTGCGATCACTGTGGGTCA
CTGCTCTATGGACTTATCCATCAAGGGATGAAATGTGACACCTGCGATATGAACGTTCAC
AAGCAATGCGTCATCAATGTCCCCAGCCTCTGCGGAATGGATCACACTGAGAAGAGGGGG
CGGATTTACCTAAAGGCTGAGGTTGCTGATGAAAAGCTCCATGTCACAGTACGAGATGCA
AAAAATCTAATCCCTATGGATCCAAACGGGCTTTCAGATCCTTATGTGAAGCTGAAACTT
ATTCCTGATCCCAAGAATGAAAGCAAGCAAAAAACCAAAACCATCCGCTCCACACTAAAT
CCGCAGTGGAATGAGTCCTTTACATTCAAATTGAAACCTTCAGACAAAGACCGACGACTG
TCTGTAGAAATCTGGGACTGGGATCGAACAACAAGGAATGACTTCATGGGATCCCTTTCC
TTTGGAGTTTCGGAGCTGATGAAGATGCCGGCCAGTGGATGGTACAAGTTGCTTAACCAA
GAAGAAGGTGAGTACTACAACGTACCCATTCCGGAAGGGGACGAGGAAGGAAACATGGAA
CTCAGGCAGAAATTCGAGAAAGCCAAACTTGGCCCTGCTGGCAACAAAGTCATCAGTCCC
TCTGAAGACAGGAAACAACCTTCCAACAACCTTGACCGAGTGAAACTCACGGACTTCAAT
TTCCTCATGGTGTTGGGAAAGGGGAGTTTTGGAAAGGTGATGCTTGCCGACAGGAAGGGC
ACAGAAGAACTGTATGCAATCAAAATCCTGAAGAAGGATGTGGTGATTCAGGATGATGAC
GTGGAGTGCACCATGGTAGAAAAGCGAGTCTTGGCCCTGCTTGACAAACCCCCGTTCTTG
ACGCAGCTGCACTCCTGCTTCCAGACAGTGGATCGGCTGTACTTCGTCATGGAATATGTC
AACGGTGGGGACCTCATGTACCACATTCAGCAAGTAGGAAAATTTAAGGAACCACAAGCA
GTATTCTATGCGGCAGAGATTTCCATCGGATTGTTCTTTCTTCATAAAAGAGGAATCATT
TATAGGGATCTGAAGTTAGATAACGTCATGTTGGATTCAGAAGGACATATCAAAATTGCT
GACTTTGGGATGTGCAAGGAACACATGATGGATGGAGTCACGACCAGGACCTTCTGTGGG
ACTCCAGATTATATCGCCCCAGAGATAATCGCTTATCAGCCGTATGGAAAATCTGTGGAC
TGGTGGGCCTATGGCGTCCTGTTGTATGAAATGCTTGCCGGGCAGCCTCCATTTGATGGT
GAAGATGAAGACGAGCTATTTCAGTCTATCATGGAGCACAACGTTTCCTATCCAAAATCC
TTGTCCAAGGAGGCTGTTTCTATCTGCAAAGGACTGATGACCAAACACCCAGCCAAGCGG
CTGGGCTGTGGGCCTGAGGGGGAGAGGGACGTGAGAGAGCATGCCTTCTTCCGGAGGATC
GACTGGGAAAAACTGGAGAACAGGGAGATCCAGCCACCATTCAAGCCCAAAGTGTGTGGC
AAAGGAGCAGAGAACTTTGACAAGTTCTTCACACGAGGACAGCCCGTCTTAACACCACCT
GATCAGCTGGTTATTGCTAACATAGACCAGTCTGATTTTGAAGGGTTCTCGTATGTCAAC
CCCCAGTTTGTGCACCCCATCTTACAGAGTGCAGTATGA
Enzyme 39 GenBank Gene ID X52479 Link Image
Enzyme 39 GeneCard ID PRKCA Link Image
Enzyme 39 GenAtlas ID PRKCA Link Image
Enzyme 39 HGNC ID HGNC:9393 Link Image
Enzyme 39 Chromosome Location 1
Enzyme 39 Locus 17q22-q23.2
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Finkenzeller G, Marme D, Hug H: Sequence of human protein kinase C alpha. Nucleic Acids Res. 1990 Apr 25;18(8):2183. [PubMed Link Image]
  2. 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]
  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. McSwine-Kennick RL, McKeegan EM, Johnson MD, Morin MJ: Phorbol diester-induced alterations in the expression of protein kinase C isozymes and their mRNAs. Analysis in wild-type and phorbol diester-resistant HL-60 cell clones. J Biol Chem. 1991 Aug 15;266(23):15135-43. [PubMed Link Image]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  6. Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A: Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C. Biochem Biophys Res Commun. 2003 Aug 1;307(3):459-65. [PubMed Link Image]
  7. Dev KK, Nakanishi S, Henley JM: The PDZ domain of PICK1 differentially accepts protein kinase C-alpha and GluR2 as interacting ligands. J Biol Chem. 2004 Oct 1;279(40):41393-7. Epub 2004 Jul 9. [PubMed Link Image]
  8. Makagiansar IT, Williams S, Dahlin-Huppe K, Fukushi J, Mustelin T, Stallcup WB: Phosphorylation of NG2 proteoglycan by protein kinase C-alpha regulates polarized membrane distribution and cell motility. J Biol Chem. 2004 Dec 31;279(53):55262-70. Epub 2004 Oct 25. [PubMed Link Image]
  9. 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]
  10. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  11. 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]
  12. Chen D, Gould C, Garza R, Gao T, Hampton RY, Newton AC: Amplitude control of protein kinase C by RINCK, a novel E3 ubiquitin ligase. J Biol Chem. 2007 Nov 16;282(46):33776-87. Epub 2007 Sep 24. [PubMed Link Image]
  13. Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed Link Image]
  14. 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]
  15. 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]
  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. 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]
  19. 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]
  20. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 6515
Enzyme 40 Name Serine/threonine-protein kinase A-Raf
Enzyme 40 Synonyms
  1. Proto-oncogene A-Raf
  2. Proto-oncogene A-Raf-1
  3. Proto-oncogene Pks
Enzyme 40 Gene Name ARAF
Enzyme 40 Protein Sequence >Serine/threonine-protein kinase A-Raf
MEPPRGPPANGAEPSRAVGTVKVYLPNKQRTVVTVRDGMSVYDSLDKALKVRGLNQDCCV
VYRLIKGRKTVTAWDTAIAPLDGEELIVEVLEDVPLTMHNFVRKTFFSLAFCDFCLKFLF
HGFRCQTCGYKFHQHCSSKVPTVCVDMSTNRQQFYHSVQDLSGGSRQHEAPSNRPLNELL
TPQGPSPRTQHCDPEHFPFPAPANAPLQRIRSTSTPNVHMVSTTAPMDSNLIQLTGQSFS
TDAAGSRGGSDGTPRGSPSPASVSSGRKSPHSKSPAEQRERKSLADDKKKVKNLGYRDSG
YYWEVPPSEVQLLKRIGTGSFGTVFRGRWHGDVAVKVLKVSQPTAEQAQAFKNEMQVLRK
TRHVNILLFMGFMTRPGFAIITQWCEGSSLYHHLHVADTRFDMVQLIDVARQTAQGMDYL
HAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGAQPLEQPSGSVLWMAAEVIRM
QDPNPYSFQSDVYAYGVVLYELMTGSLPYSHIGCRDQIIFMVGRGYLSPDLSKISSNCPK
AMRRLLSDCLKFQREERPLFPQILATIELLQRSLPKIERSASEPSLHRTQADELPACLLS
AARLVP
Enzyme 40 Number of Residues 606
Enzyme 40 Molecular Weight 67584.8
Enzyme 40 Theoretical pI 9.30
Enzyme 40 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • molecular transducer activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • receptor signaling protein activity
  • signal transducer activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biological regulation
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 40 General Function Involved in intracellular signaling pathway
Enzyme 40 Specific Function Involved in the transduction of mitogenic signals from the cell membrane to the nucleus
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 1340152 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID P10398 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name ARAF_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >1821 bp
ATGGAGCCACCACGGGGCCCCCCTGCCAATGGGGCCGAGCCATCCCGGGCAGTGGGCACC
GTCAAAGTATACCTGCCCAACAAGCAACGCACGGTGGTGACTGTCCGGGATGGCATGAGT
GTCTACGACTCTCTAGACAAGGCCCTGAAGGTGCGGGGTCTAAATCAGGACTGCTGTGTG
GTCTACCGACTCATCAAGGGACGAAAGACGGTCACTGCCTGGGACACAGCCATTGCTCCC
CTGGATGGCGAGGAGCTCATTGTCGAGGTCCTTGAAGATGTCCCGCTGACCATGCACAAT
TTTGTACGGAAGACCTTCTTCAGCCTGGCGTTCTGTGACTTCTGCCTTAAGTTTCTGTTC
CATGGCTTCCGTTGCCAAACCTGTGGCTACAAGTTCCACCAGCATTGTTCCTCCAAGGTC
CCCACAGTCTGTGTTGACATGAGTACCAACCGCCAACAGTTCTACCACAGTGTCCAGGAT
TTGTCCGGAGGCTCCAGACAGCATGAGGCTCCCTCGAACCGCCCCCTGAATGAGTTGCTA
ACCCCCCAGGGTCCCAGCCCCCGCACCCAGCACTGTGACCCGGAGCACTTCCCCTTCCCT
GCCCCAGCCAATGCCCCCCTACAGCGCATCCGCTCCACGTCCACTCCCAACGTCCATATG
GTCAGCACCACGGCCCCCATGGACTCCAACCTCATCCAGCTCACTGGCCAGAGTTTCAGC
ACTGATGCTGCCGGTAGTAGAGGAGGTAGTGATGGAACCCCCCGGGGGAGCCCCAGCCCA
GCCAGCGTGTCCTCGGGGAGGAAGTCCCCACATTCCAAGTCACCAGCAGAGCAGCGCGAG
CGGAAGTCCTTGGCCGATGACAAGAAGAAAGTGAAGAACCTGGGGTACCGGGANTCAGGC
TATTACTGGGAGGTACCACCCAGTGAGGTGCAGCTGCTGAAGAGGATCGGGACGGGCTCG
TTTGGCACCGTGTTTCGAGGGCGGTGGCATGGCGATGTGGCCGTGAAGGTGCTCAAGGTG
TCCCAGCCCACAGCTGAGCAGGCCCAGGCTTTCAAGAATGAGATGCAGGTGCTCAGGAAG
ACGCGACATGTCAACATCTTGCTGTTTATGGGCTTCATGACCCGGCCGGGATTTGCCATC
ATCACACAGTGGTGTGAGGGCTCCAGCCTCTACCATCACCTGCATGTGGCCGACACACGC
TTCGACATGGTCCAGCTCATCGACGTGGCCCGGCAGACTGCCCAGGGCATGGACTACCTC
CATGCCAAGAACATCATCCACCGAGATCTCAAGTCTAACAACATCTTCCTACATGAGGGG
CTCACGGTGAAGATCGGTGACTTTGGCTTGGCCACAGTGAAGACTCGATGGAGCGGGGCC
CAGCCCTTGGAGCAGCCCTCAGGATCTGTGCTGTGGATGGCAGCTGAGGTGATCCGTATG
CAGGACCCGAACCCCTACAGCTTCCAGTCAGACGTCTATGCCTACGGGGTTGTGCTCTAC
GAGCTTATGACTGGCTCACTGCCTTACAGCCACATTGGCTGCCGTGACCAGATTATCTTT
ATGGTGGGCCGTGGCTATCTGTCCCCGGACCTCAGCAAAATCTCCAGCAACTGCCCCAAG
GCCATGCGGCGCCTGCTGTCTGACTGCCTCAAGTTCCAGCGGGAGGAGCGGCCCCTCTTC
CCCCAGATCCTGGCCACAATTGAGCTGCTGCAACGGTCACTCCCCAAGATTGAGCGGAGT
GCCTCGGAACCCTCCTTGCACCGCACCCAGGCCGATGAGTTGCCTGCCTGCCTACTCAGC
GCAGCCCGCCTTGTGCCTTAG
Enzyme 40 GenBank Gene ID X04790 Link Image
Enzyme 40 GeneCard ID ARAF Link Image
Enzyme 40 GenAtlas ID ARAF Link Image
Enzyme 40 HGNC ID HGNC:646 Link Image
Enzyme 40 Chromosome Location Not Available
Enzyme 40 Locus Not Available
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Beck TW, Huleihel M, Gunnell M, Bonner TI, Rapp UR: The complete coding sequence of the human A-raf-1 oncogene and transforming activity of a human A-raf carrying retrovirus. Nucleic Acids Res. 1987 Jan 26;15(2):595-609. [PubMed Link Image]
  2. Lee JE, Beck TW, Brennscheidt U, DeGennaro LJ, Rapp UR: The complete sequence and promoter activity of the human A-raf-1 gene (ARAF1). Genomics. 1994 Mar 1;20(1):43-55. [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]
  5. Mark GE, Seeley TW, Shows TB, Mountz JD: Pks, a raf-related sequence in humans. Proc Natl Acad Sci U S A. 1986 Sep;83(17):6312-6. [PubMed Link Image]
  6. Yin XL, Chen S, Gu JX: Identification of TH1 as an interaction partner of A-Raf kinase. Mol Cell Biochem. 2002 Feb;231(1-2):69-74. [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. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  9. 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]
  10. 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]
  11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  12. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 6633
Enzyme 41 Name Citron Rho-interacting kinase
Enzyme 41 Synonyms
  1. CRIK
  2. Serine/threonine-protein kinase 21
Enzyme 41 Gene Name CIT
Enzyme 41 Protein Sequence >Citron Rho-interacting kinase
MLKFKYGARNPLDAGAAEPIASRASRLNLFFQGKPPFMTQQQMSPLSREGILDALFVLFE
ECSQPALMKIKHVSNFVRKYSDTIAELQELQPSAKDFEVRSLVGCGHFAEVQVVREKATG
DIYAMKVMKKKALLAQEQVSFFEEERNILSRSTSPWIPQLQYAFQDKNHLYLVMEYQPGG
DLLSLLNRYEDQLDENLIQFYLAELILAVHSVHLMGYVHRDIKPENILVDRTGHIKLVDF
GSAAKMNSNKMVNAKLPIGTPDYMAPEVLTVMNGDGKGTYGLDCDWWSVGVIAYEMIYGR
SPFAEGTSARTFNNIMNFQRFLKFPDDPKVSSDFLDLIQSLLCGQKERLKFEGLCCHPFF
SKIDWNNIRNSPPPFVPTLKSDDDTSNFDEPEKNSWVSSSPCQLSPSGFSGEELPFVGFS
YSKALGILGRSESVVSGLDSPAKTSSMEKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVS
EVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLH
DIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFK
RKATECQHKLLKAKDQGKPEVGEYAKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQ
NIRQAKERAERELEKLQNREDSSEGIRKKLVEAEELEEKHREAQVSAQHLEVHLKQKEQH
YEEKIKVLDNQIKKDLADKETLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQR
IVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKI
SHQDHSDKNRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAAL
ESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDN
AELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCT
MLEEQVMDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQ
RITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQ
KLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLEN
IQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNE
LKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHPHPSTPATARQQIAMSAIV
RSPEHQPSAMSLLAPPSSRRKESSTPEEFSRRLKERMHHNIPHRFNVGLNMRATKCAVCL
DTVHFGRQASKCLECQVMCHPKCSTCLPATCGLPAEYATHFTEAFCRDKMNSPGLQTKEP
SSSLHLEGWMKVPRNNKRGQQGWDRKYIVLEGSKVLIYDNEAREAGQRPVEEFELCLPDG
DVSIHGAVGASELANTAKADVPYILKMESHPHTTCWPGRTLYLLAPSFPDKQRWVTALES
VVAGGRVSREKAEADAKLLGNSLLKLEGDDRLDMNCTLPFSDQVVLVGTEEGLYALNVLK
NSLTHVPGIGAVFQIYIIKDLEKLLMIAGEERALCLVDVKKVKQSLAQSHLPAQPDISPN
IFEAVKGCHLFGAGKIENGLCICAAMPSKVVILRYNENLSKYCIRKEIETSEPCSCIHFT
NYSILIGTNKFYEIDMKQYTLEEFLDKNDHSLAPAVFAASSNSFPVSIVQVNSAGQREEY
LLCFHEFGVFVDSYGRRSRTDDLKWSRLPLAFAYREPYLFVTHFNSLEVIEIQARSSAGT
PARAYLDIPNPRYLGPAISSGAIYLASSYQDKLRVICCKGNLVKESGTEHHRGPSTSRSS
PNKRGPPTYNEHITKRVASSPAPPEGPSHPREPSTPHRYREGRTELRRDKSPGRPLEREK
SPGRMLSTRRERSPGRLFEDSSRGRLPAGAVRTPLSQVNKVWDQSSV
Enzyme 41 Number of Residues 2027
Enzyme 41 Molecular Weight 231428.9
Enzyme 41 Theoretical pI 6.54
Enzyme 41 GO Classification
Function
  • ATP binding
  • GTPase regulator activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • enzyme regulator activity
  • kinase activity
  • nucleoside binding
  • nucleoside-triphosphatase regulator activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • small GTPase regulator activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 41 General Function Involved in protein serine/threonine kinase activity
Enzyme 41 Specific Function Required for KIF14 localization to the central spindle and midbody. May play a role in cytokinesis. Putative RHO/RAC effector that binds to the GTP-bound forms of RHO and RAC1. It probably binds p21 with a tighter specificity in vivo. Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Plays an important role in the regulation of cytokinesis and the development of the central nervous system
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 32698688 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID O14578 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name CTRO_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >6084 bp
ATGTTGAAGTTCAAATATGGAGCGCGGAATCCTTTGGATGCTGGTGCTGCTGAACCCATT
GCCAGCCGGGCCTCCAGGCTGAATCTGTTCTTCCAGGGGAAACCACCCTTTATGACTCAA
CAGCAGATGTCTCCTCTTTCCCGAGAAGGGATATTAGATGCCCTCTTTGTTCTCTTTGAA
GAATGCAGTCAGCCTGCTCTGATGAAGATTAAGCACGTGAGCAACTTTGTCCGGAAGTAT
TCCGACACCATAGCTGAGTTACAGGAGCTCCAGCCTTCGGCAAAGGACTTCGAAGTCAGA
AGTCTTGTAGGTTGTGGTCACTTTGCTGAAGTGCAGGTGGTAAGAGAGAAAGCAACCGGG
GACATCTATGCTATGAAAGTGATGAAGAAGAAGGCTTTATTGGCCCAGGAGCAGGTTTCA
TTTTTTGAGGAAGAGCGGAACATATTATCTCGAAGCACAAGCCCGTGGATCCCCCAATTA
CAGTATGCCTTTCAGGACAAAAATCACCTTTATCTGGTCATGGAATATCAGCCTGGAGGG
GACTTGCTGTCACTTTTGAATAGATATGAGGACCAGTTAGATGAAAACCTGATACAGTTT
TACCTAGCTGAGCTGATTTTGGCTGTTCACAGCGTTCATCTGATGGGATACGTGCATCGA
GACATCAAGCCTGAGAACATTCTCGTTGACCGCACAGGACACATCAAGCTGGTGGATTTT
GGATCTGCCGCGAAAATGAATTCAAACAAGATGGTGAATGCCAAACTCCCGATTGGGACC
CCAGATTACATGGCTCCTGAAGTGCTGACTGTGATGAACGGGGATGGAAAAGGCACCTAC
GGCCTGGACTGTGACTGGTGGTCAGTGGGCGTGATTGCCTATGAGATGATTTATGGGAGA
TCCCCCTTCGCAGAGGGAACCTCTGCCAGAACCTTCAATAACATTATGAATTTCCAGCGG
TTTTTGAAATTTCCAGATGACCCCAAAGTGAGCAGTGACTTTCTTGATCTGATTCAAAGC
TTGTTGTGCGGCCAGAAAGAGAGACTGAAGTTTGAAGGTCTTTGCTGCCATCCTTTCTTC
TCTAAAATTGACTGGAACAACATTCGTAACTCTCCTCCCCCCTTCGTTCCCACCCTCAAG
TCTGACGATGACACCTCCAATTTTGATGAACCAGAGAAGAATTCGTGGGTTTCATCCTCT
CCGTGCCAGCTGAGCCCCTCAGGCTTCTCGGGTGAAGAACTGCCGTTTGTGGGGTTTTCG
TACAGCAAGGCACTGGGGATTCTTGGTAGATCTGAGTCTGTTGTGTCGGGTCTGGACTCC
CCTGCCAAGACTAGCTCCATGGAAAAGAAACTTCTCATCAAAAGCAAAGAGCTACAAGAC
TCTCAGGACAAGTGTCACAAGATGGAGCAGGAAATGACCCGGTTACATCGGAGAGTGTCA
GAGGTGGAGGCTGTGCTTAGTCAGAAGGAGGTGGAGCTGAAGGCCTCTGAGACTCAGAGA
TCCCTCCTGGAGCAGGACCTTGCTACCTACATCACAGAATGCAGTAGCTTAAAGCGAAGT
TTGGAGCAAGCACGGATGGAGGTGTCCCAGGAGGATGACAAAGCACTGCAGCTTCTCCAT
GATATCAGAGAGCAGAGCCGGAAGCTCCAAGAAATCAAAGAGCAGGAGTACCAGGCTCAA
GTGGAAGAAATGAGGTTGATGATGAATCAGTTGGAAGAGGATCTTGTCTCAGCAAGAAGA
CGGAGTGATCTCTACGAATCTGAGCTGAGAGAGTCTCGGCTTGCTGCTGAAGAATTCAAG
CGGAAAGCGACAGAATGTCAGCATAAACTGTTGAAGGCTAAGGATCAAGGGAAGCCTGAA
GTGGGAGAATATGCGAAACTGGAGAAGATCAATGCTGAGCAGCAGCTCAAAATTCAGGAG
CTCCAAGAGAAACTGGAGAAGGCTGTAAAAGCCAGCACGGAGGCCACCGAGCTGCTGCAG
AATATCCGCCAGGCAAAGGAGCGAGCCGAGAGGGAGCTGGAGAAGCTGCAGAACCGAGAG
GATTCTTCTGAAGGCATCAGAAAGAAGCTGGTGGAAGCTGAGGAGCTCGAAGAGAAACAT
CGGGAGGCCCAAGTCTCAGCCCAGCACCTAGAAGTGCACCTGAAACAGAAAGAGCAGCAC
TATGAGGAAAAGATTAAAGTGTTGGACAATCAGATAAAGAAAGACCTGGCTGACAAGGAG
ACACTGGAGAACATGATGCAGAGACACGAGGAGGAGGCCCATGAGAAGGGCAAAATTCTC
AGCGAACAGAAGGCGATGATCAATGCTATGGATTCCAAGATCAGATCCCTGGAACAGAGG
ATTGTGGAACTGTCTGAAGCCAATAAACTTGCAGCAAATAGCAGTCTTTTTACCCAAAGG
AACATGAAGGCCCAAGAAGAGATGATTTCTGAACTCAGGCAACAGAAATTTTACCTGGAG
ACACAGGCTGGGAAGTTGGAGGCCCAGAACCGAAAACTGGAGGAGCAGCTGGAGAAGATC
AGCCACCAAGACCACAGTGACAAGAATCGGCTGCTGGAACTGGAGACAAGATTGCGGGAG
GTCAGTCTAGAGCACGAGGAGCAGAAACTGGAGCTCAAGCGCCAGCTCACAGAGCTACAG
CTCTCCCTGCAGGAGCGCGAGTCACAGTTGACAGCCCTGCAGGCTGCACGGGCGGCCCTG
GAGAGCCAGCTTCGCCAGGCGAAGACAGAGCTGGAAGAGACCACAGCAGAAGCTGAAGAG
GAGATCCAGGCACTCACGGCACATAGAGATGAAATCCAGCGCAAATTTGATGCTCTTCGT
AACAGCTGTACTGTAATCACAGACCTGGAGGAGCAGCTAAACCAGCTGACCGAGGACAAC
GCTGAACTCAACAACCAAAACTTCTACTTGTCCAAACAACTCGATGAGGCTTCTGGCGCC
AACGACGAGATTGTACAACTGCGAAGTGAAGTGGACCATCTCCGCCGGGAGATCACGGAA
CGAGAGATGCAGCTTACCAGCCAGAAGCAAACGATGGAGGCTCTGAAGACCACGTGCACC
ATGCTGGAGGAACAGGTCATGGATTTGGAGGCCCTAAACGATGAGCTGCTAGAAAAAGAG
CGGCAGTGGGAGGCCTGGAGGAGCGTCCTGGGTGATGAGAAATCCCAGTTTGAGTGTCGG
GTTCGAGAGCTGCAGAGAATGCTGGACACCGAGAAACAGAGCAGGGCGAGAGCCGATCAG
CGGATCACCGAGTCTCGCCAGGTGGTGGAGCTGGCAGTGAAGGAGCACAAGGCTGAGATT
CTCGCTCTGCAGCAGGCTCTCAAAGAGCAGAAGCTGAAGGCCGAGAGCCTCTCTGACAAG
CTCAATGACCTGGAGAAGAAGCATGCTATGCTTGAAATGAATGCCCGAAGCTTACAGCAG
AAGCTGGAGACTGAACGAGAGCTCAAACAGAGGCTTCTGGAAGAGCAAGCCAAATTACAG
CAGCAGATGGACCTGCAGAAAAATCACATTTTCCGTCTGACTCAAGGACTGCAAGAAGCT
CTAGATCGGGCTGATCTACTGAAGACAGAAAGAAGTGACTTGGAGTATCAGCTGGAAAAC
ATTCAGGTTCTCTATTCTCATGAAAAGGTGAAAATGGAAGGCACTATTTCTCAACAAACC
AAACTCATTGATTTTCTGCAAGCCAAAATGGACCAACCTGCTAAAAAGAAAAAGGGTTTA
TTTAGTCGACGGAAAGAGGACCCTGCTTTACCCACACAGGTTCCTCTGCAGTACAATGAG
CTGAAGCTGGCCCTGGAGAAGGAGAAAGCTCGCTGTGCAGAGCTAGAGGAAGCCCTTCAG
AAGACCCGCATCGAGCTCCGGTCCGCCCGGGAGGAAGCTGCCCACCGCAAAGCAACGGAC
CACCCACACCCATCCACGCCAGCCACCGCGAGGCAGCAGATCGCCATGTCCGCCATCGTG
CGGTCGCCAGAGCACCAGCCCAGTGCCATGAGCCTGCTGGCCCCGCCATCCAGCCGCAGA
AAGGAGTCTTCAACTCCAGAGGAATTTAGTCGGCGTCTTAAGGAACGCATGCACCACAAT
ATTCCTCACCGATTCAACGTAGGACTGAACATGCGAGCCACAAAGTGTGCTGTGTGTCTG
GATACCGTGCACTTTGGACGCCAGGCATCCAAATGTCTCGAATGTCAGGTGATGTGTCAC
CCCAAGTGCTCCACGTGCTTGCCAGCCACCTGCGGCTTGCCTGCTGAATATGCCACACAC
TTCACCGAGGCCTTCTGCCGTGACAAAATGAACTCCCCAGGTCTCCAGACCAAGGAGCCC
AGCAGCAGCTTGCACCTGGAAGGGTGGATGAAGGTGCCCAGGAATAACAAACGAGGACAG
CAAGGCTGGGACAGGAAGTACATTGTCCTGGAGGGATCAAAAGTCCTCATTTATGACAAT
GAAGCCAGAGAAGCTGGACAGAGGCCGGTGGAAGAATTTGAGCTGTGCCTTCCCGACGGG
GATGTATCTATTCATGGTGCCGTTGGTGCTTCCGAACTCGCAAATACAGCCAAAGCAGAT
GTCCCATACATACTGAAGATGGAATCTCACCCGCACACCACCTGCTGGCCCGGGAGAACC
CTCTACTTGCTAGCTCCCAGCTTCCCTGACAAACAGCGCTGGGTCACCGCCTTAGAATCA
GTTGTCGCAGGTGGGAGAGTTTCTAGGGAAAAAGCAGAAGCTGATGCTAAACTGCTTGGA
AACTCCCTGCTGAAACTGGAAGGTGATGACCGTCTAGACATGAACTGCACGCTGCCCTTC
AGTGACCAGGTGGTGTTGGTGGGCACCGAGGAAGGGCTCTACGCCCTGAATGTCTTGAAA
AACTCCCTAACCCATGTCCCAGGAATTGGAGCAGTCTTCCAAATTTATATTATCAAGGAC
CTGGAGAAGCTACTCATGATAGCAGGAGAAGAGCGGGCACTGTGTCTTGTGGACGTGAAG
AAAGTGAAACAGTCCCTGGCCCAGTCCCACCTGCCTGCCCAGCCCGACATCTCACCCAAC
ATTTTTGAAGCTGTCAAGGGCTGCCACTTGTTTGGGGCAGGCAAGATTGAGAACGGGCTC
TGCATCTGTGCAGCCATGCCCAGCAAAGTCGTCATTCTCCGCTACAACGAAAACCTCAGC
AAATACTGCATCCGGAAAGAGATAGAGACCTCAGAGCCCTGCAGCTGTATCCACTTCACC
AATTACAGTATCCTCATTGGAACCAATAAATTCTACGAAATCGACATGAAGCAGTACACG
CTCGAGGAATTCCTGGATAAGAATGACCATTCCTTGGCACCTGCTGTGTTTGCCGCCTCT
TCCAACAGCTTCCCTGTCTCAATCGTGCAGGTGAACAGCGCAGGGCAGCGAGAGGAGTAC
TTGCTGTGTTTCCACGAATTTGGAGTGTTCGTGGATTCTTACGGAAGACGTAGCCGCACA
GACGATCTCAAGTGGAGTCGCTTACCTTTGGCCTTTGCCTACAGAGAACCCTATCTGTTT
GTGACCCACTTCAACTCACTCGAAGTAATTGAGATCCAGGCACGCTCCTCAGCAGGGACC
CCTGCCCGAGCGTACCTGGACATCCCGAACCCGCGCTACCTGGGCCCTGCCATTTCCTCA
GGAGCGATTTACTTGGCGTCCTCATACCAGGATAAATTAAGGGTCATTTGCTGCAAGGGA
AACCTCGTGAAGGAGTCCGGCACTGAACACCACCGGGGCCCGTCCACCTCCCGCAGCAGC
CCCAACAAGCGAGGCCCACCCACGTACAACGAGCACATCACCAAGCGCGTGGCCTCCAGC
CCAGCGCCGCCCGAAGGCCCCAGCCACCCGCGAGAGCCAAGCACACCCCACCGCTACCGC
GAGGGGCGGACCGAGCTGCGCAGGGACAAGTCTCCTGGCCGCCCCCTGGAGCGAGAGAAG
TCCCCCGGCCGGATGCTCAGCACGCGGAGAGAGCGGTCCCCCGGGAGGCTGTTTGAAGAC
AGCAGCAGGGGCCGGCTGCCTGCGGGAGCCGTGAGGACCCCGCTGTCCCAGGTGAACAAG
GTCTGGGACCAGTCTTCAGTATAA
Enzyme 41 GenBank Gene ID NM_007174.1 Link Image
Enzyme 41 GeneCard ID CIT Link Image
Enzyme 41 GenAtlas ID CIT Link Image
Enzyme 41 HGNC ID HGNC:1985 Link Image
Enzyme 41 Chromosome Location 1
Enzyme 41 Locus 12q24
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Feb 26;6(1):63-70. [PubMed Link Image]
  2. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  3. Gruneberg U, Neef R, Li X, Chan EH, Chalamalasetty RB, Nigg EA, Barr FA: KIF14 and citron kinase act together to promote efficient cytokinesis. J Cell Biol. 2006 Jan 30;172(3):363-72. Epub 2006 Jan 23. [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. Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R: Phosphoproteome analysis of the human mitotic spindle. Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5391-6. Epub 2006 Mar 24. [PubMed Link Image]
  6. Berto G, Camera P, Fusco C, Imarisio S, Ambrogio C, Chiarle R, Silengo L, Di Cunto F: The Down syndrome critical region protein TTC3 inhibits neuronal differentiation via RhoA and Citron kinase. J Cell Sci. 2007 Jun 1;120(Pt 11):1859-67. Epub 2007 May 8. [PubMed Link Image]
  7. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  8. 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. 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]
  10. 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]
  11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  12. 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]
  13. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 6668
Enzyme 42 Name Protein kinase C beta type
Enzyme 42 Synonyms
  1. PKC-B
  2. PKC-beta
Enzyme 42 Gene Name PRKCB
Enzyme 42 Protein Sequence >Protein kinase C beta type
MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGF
GKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGS
LLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDA
KNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRL
SVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEE
LRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSE
RKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVM
EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHI
KIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAP
FEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFF
RYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGF
SYTNPEFVINV
Enzyme 42 Number of Residues 671
Enzyme 42 Molecular Weight 76868.4
Enzyme 42 Theoretical pI 7.00
Enzyme 42 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • metal ion binding
  • nucleoside binding
  • protein kinase C activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • zinc ion binding
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 42 General Function Involved in protein serine/threonine kinase activity
Enzyme 42 Specific Function Calcium-activated and phospholipid-dependent serine/threonine-protein kinase involved in various processes such as regulation of the B-cell receptor (BCR) signalosome, apoptosis and transcription regulation. Plays a key role in B-cell activation and function by regulating BCR-induced NF-kappa-B activation and B-cell suvival. Required for recruitment and activation of the IKK kinase to lipid rafts and mediates phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser- 652', leading to activate the NF-kappa-B signaling. Involved in apoptosis following oxidative damage:in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. Also involved in triglyceride homeostasis. Serves as the receptor for phorbol esters, a class of tumor promoters
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 47157322 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID P05771 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name KPCB_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >2016 bp
ATGGCTGACCCGGCTGCGGGGCCGCCGCCGAGCGAGGGCGAGGAGAGCACCGTGCGCTTC
GCCCGCAAAGGCGCCCTCCGGCAGAAGAACGTGCATGAGGTCAAGAACCACAAATTCACC
GCCCGCTTCTTCAAGCAGCCCACCTTCTGCAGCCACTGCACCGACTTCATCTGGGGCTTC
GGGAAGCAGGGATTCCAGTGCCAAGTTTGCTGCTTTGTGGTGCACAAGCGGTGCCATGAA
TTTGTCACATTCTCCTGCCCTGGCGCTGACAAGGGTCCAGCCTCCGATGACCCCCGCAGC
AAACACAAGTTTAAGATCCACACGTACTCCAGCCCCACGTTTTGTGACCACTGTGGGTCA
CTGCTGTATGGACTCATCCACCAGGGGATGAAATGTGACACCTGCATGATGAATGTGCAC
AAGCGCTGCGTGATGAATGTTCCCAGCCTGTGTGGCACGGACCACACGGAGCGCCGCGGC
CGCATCTACATCCAGGCCCACATCGACAGGGACGTCCTCATTGTCCTCGTAAGAGATGCT
AAAAACCTTGTACCTATGGACCCCAATGGCCTGTCAGATCCCTACGTAAAACTGAAACTG
ATTCCCGATCCCAAAAGTGAGAGCAAACAGAAGACCAAAACCATCAAATGCTCCCTCAAC
CCTGAGTGGAATGAGACATTTAGATTTCAGCTGAAAGAATCGGACAAAGACAGAAGACTG
TCAGTAGAGATTTGGGATTGGGATTTGACCAGCAGGAATGACTTCATGGGATCTTTGTCC
TTTGGGATTTCTGAACTTCAGAAAGCCAGTGTTGATGGCTGGTTTAAGTTACTGAGCCAG
GAGGAAGGCGAGTACTTCAATGTGCCTGTGCCACCAGAAGGAAGTGAGGCCAATGAAGAA
CTGCGGCAGAAATTTGAGAGGGCCAAGATCAGTCAGGGAACCAAGGTCCCGGAAGAAAAG
ACGACCAACACTGTCTCCAAATTTGACAACAATGGCAACAGAGACCGGATGAAACTGACC
GATTTTAACTTCCTAATGGTGCTGGGGAAAGGCAGCTTTGGCAAGGTCATGCTTTCAGAA
CGAAAAGGCACAGATGAGCTCTATGCTGTGAAGATCCTGAAGAAGGACGTTGTGATCCAA
GATGATGACGTGGAGTGCACTATGGTGGAGAAGCGGGTGTTGGCCCTGCCTGGGAAGCCG
CCCTTCCTGACCCAGCTCCACTCCTGCTTCCAGACCATGGACCGCCTGTACTTTGTGATG
GAGTACGTGAATGGGGGCGACCTCATGTATCACATCCAGCAAGTCGGCCGGTTCAAGGAG
CCCCATGCTGTATTTTACGCTGCAGAAATTGCCATCGGTCTGTTCTTCTTACAGAGTAAG
GGCATCATTTACCGTGACCTAAAACTTGACAACGTGATGCTCGATTCTGAGGGACACATC
AAGATTGCCGATTTTGGCATGTGTAAGGAAAACATCTGGGATGGGGTGACAACCAAGACA
TTCTGTGGCACTCCAGACTACATCGCCCCCGAGATAATTGCTTATCAGCCCTATGGGAAG
TCCGTGGATTGGTGGGCATTTGGAGTCCTGCTGTATGAAATGTTGGCTGGGCAGGCACCC
TTTGAAGGGGAGGATGAAGATGAACTCTTCCAATCCATCATGGAACACAACGTAGCCTAT
CCCAAGTCTATGTCCAAGGAAGCTGTGGCCATCTGCAAAGGGCTGATGACCAAACACCCA
GGCAAACGTCTGGGTTGTGGACCTGAAGGCGAACGTGATATCAAAGAGCATGCATTTTTC
CGGTATATTGATTGGGAGAAACTTGAACGCAAAGAGATCCAGCCCCCTTATAAGCCAAAA
GCTAGAGACAAGAGAGACACCTCCAACTTCGACAAAGAGTTCACCAGACAGCCTGTGGAA
CTGACCCCCACTGATAAACTCTTCATCATGAACTTGGACCAAAATGAATTTGCTGGCTTC
TCTTATACTAACCCAGAGTTTGTCATTAATGTGTAG
Enzyme 42 GenBank Gene ID NM_212535.2 Link Image
Enzyme 42 GeneCard ID PRKCB Link Image
Enzyme 42 GenAtlas ID PRKCB Link Image
Enzyme 42 HGNC ID HGNC:9395 Link Image
Enzyme 42 Chromosome Location 1
Enzyme 42 Locus 16p11.2
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Coussens L, Parker PJ, Rhee L, Yang-Feng TL, Chen E, Waterfield MD, Francke U, Ullrich A: Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways. Science. 1986 Aug 22;233(4766):859-66. [PubMed Link Image]
  2. Kubo K, Ohno S, Suzuki K: Primary structures of human protein kinase C beta I and beta II differ only in their C-terminal sequences. FEBS Lett. 1987 Oct 19;223(1):138-42. [PubMed Link Image]
  3. Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J, Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y, Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC, Adams MD: Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. Genomics. 1999 Sep 15;60(3):295-308. [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. Mahajna J, King P, Parker P, Haley J: Autoregulation of cloned human protein kinase C beta and gamma gene promoters in U937 cells. DNA Cell Biol. 1995 Mar;14(3):213-22. [PubMed Link Image]
  6. Niino YS, Ohno S, Suzuki K: Positive and negative regulation of the transcription of the human protein kinase C beta gene. J Biol Chem. 1992 Mar 25;267(9):6158-63. [PubMed Link Image]
  7. Obeid LM, Blobe GC, Karolak LA, Hannun YA: Cloning and characterization of the major promoter of the human protein kinase C beta gene. Regulation by phorbol esters. J Biol Chem. 1992 Oct 15;267(29):20804-10. [PubMed Link Image]
  8. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  9. Coussens L, Rhee L, Parker PJ, Ullrich A: Alternative splicing increases the diversity of the human protein kinase C family. DNA. 1987 Oct;6(5):389-94. [PubMed Link Image]
  10. Kubo K, Ohno S, Suzuki K: Nucleotide sequence of the 3' portion of a human gene for protein kinase C beta I/beta II. Nucleic Acids Res. 1987 Sep 11;15(17):7179-80. [PubMed Link Image]
  11. Graff JR, McNulty AM, Hanna KR, Konicek BW, Lynch RL, Bailey SN, Banks C, Capen A, Goode R, Lewis JE, Sams L, Huss KL, Campbell RM, Iversen PW, Neubauer BL, Brown TJ, Musib L, Geeganage S, Thornton D: The protein kinase Cbeta-selective inhibitor, Enzastaurin (LY317615.HCl), suppresses signaling through the AKT pathway, induces apoptosis, and suppresses growth of human colon cancer and glioblastoma xenografts. Cancer Res. 2005 Aug 15;65(16):7462-9. [PubMed Link Image]
  12. Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed Link Image]
  13. Gao T, Brognard J, Newton AC: The phosphatase PHLPP controls the cellular levels of protein kinase C. J Biol Chem. 2008 Mar 7;283(10):6300-11. Epub 2007 Dec 27. [PubMed Link Image]
  14. 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]
  15. 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]
  16. Metzger E, Imhof A, Patel D, Kahl P, Hoffmeyer K, Friedrichs N, Muller JM, Greschik H, Kirfel J, Ji S, Kunowska N, Beisenherz-Huss C, Gunther T, Buettner R, Schule R: Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Nature. 2010 Apr 1;464(7289):792-6. Epub 2010 Mar 14. [PubMed Link Image]
  17. Grodsky N, Li Y, Bouzida D, Love R, Jensen J, Nodes B, Nonomiya J, Grant S: Structure of the catalytic domain of human protein kinase C beta II complexed with a bisindolylmaleimide inhibitor. Biochemistry. 2006 Nov 28;45(47):13970-81. [PubMed Link Image]
  18. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 6670
Enzyme 43 Name Protein kinase C zeta type
Enzyme 43 Synonyms
  1. nPKC-zeta
Enzyme 43 Gene Name PRKCZ
Enzyme 43 Protein Sequence >Protein kinase C zeta type
MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKW
VDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGAR
RWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTC
RKHMDSVMPSQEPPVDDKNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDG
IKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTE
KHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEI
CIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAP
EILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRF
LSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQIT
DDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV
Enzyme 43 Number of Residues 592
Enzyme 43 Molecular Weight 67659.3
Enzyme 43 Theoretical pI 5.52
Enzyme 43 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • metal ion binding
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • zinc ion binding
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 43 General Function Involved in protein serine/threonine kinase activity
Enzyme 43 Specific Function PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. Subunit of a quaternary complex that plays a central role in epithelial cell polarization
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 158255426 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID Q05513 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name KPCZ_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >1779 bp
ATGCCCAGCAGGACCGGCCCCAAGATGGAAGGGAGCGGCGGCCGCGTCCGCCTCAAGGCG
CATTACGGGGGGGACATCTTCATCACCAGCGTGGACGCCGCCACGACCTTCGAGGAGCTC
TGTGAGGAAGTGAGAGACATGTGTCGTCTGCACCAGCAGCACCCGCTCACCCTCAAGTGG
GTGGACAGCGAAGGTGACCCTTGCACGGTGTCCTCCCAGATGGAGCTGGAAGAGGCTTTC
CGCCTGGCCCGTCAGTGCAGGGACGAAGGCCTCATCATTCATGTTTTCCCGAGCACCCCT
GAGCAGCCTGGCCTGCCATGTCCGGGAGAAGACAAATCTATCTACCGCCGGGGAGCCAGA
AGATGGAGGAAGCTGTACCGTGCCAACGGCCACCTCTTCCAAGCCAAGCGCTTTAACAGG
AGAGCGTACTGCGGTCAGTGCAGCGAGAGGATATGGGGCCTCGCGAGGCAAGGCTACAGG
TGCATCAACTGCAAACTGCTGGTCCATAAGCGCTGCCACGGCCTCGTCCCGCTGACCTGC
AGGAAGCATATGGATTCTGTCATGCCTTCCCAAGAGCCTCCAGTAGACGACAGGAACGAG
GACGCCGACCTTCCTTCCGAGGAGACAGATGGAATTGCTTACATTTCCTCATCCCGGAAG
CATGACAGCATTAAAGACGACTCGGAGGACCTTAAGCCAGTTATCGATGGGATGGATGGA
ATCAAAATCTCTCAGGGGCTTGGGCTGCAGGACTTTGACCTAATCAGAGTCATCGGGCGC
GGGAGCTACGCCAAGGTTCTCCTGGTGCGGTTGAAGAAGAATGACCAAATTTACGCCATG
AAAGTGGTGAAGAAAGAGCTGGTGCATGATGACGAGGATATTGACTGGGTACAGACAGAG
AAGCACGTGTTTGAGCAGGCATCCAGCAACCCCTTCCTGGTCGGATTACACTCCTGCTTC
CAGACGACAAGTCGGTTGTTCCTGGTCATTGAGTACGTCAACGGCGGGGACCTGATGTTC
CACATGCAGAGGCAGAGGAAGCTCCCTGAGGAGCACGCCAGGTTCTACGCGGCCGAGATC
TGCATCGCCCTCAACCTCCTGCACGAGAGGGGGATCATCTACAGGGACCTGAAGCTGGAC
AACGTCCTCCTGGATGCGGACGGGCACATCAAGCTCACAGACTACGGCATGTGCAAGGAA
GGCCTGGGCCCTGGTGACACAACGAGCACTTTCTGCGGAACCCCGAATTACATCGCCCCC
GAAATCCTGCGGGGAGAGGAGTACGGGTTCAGCGTGGACTGGTGGGCGCTGGGAGTCCTC
ATGTTTGAGATGATGGCCGGGCGCTCCCCGTTCGACATCATCACCGACAACCCGGACATG
AACACAGAGGACTACCTTTTCCAAGTGATCCTGGAGAAGCCCATCCGGATCCCCCGGTTC
CTGTCCGTCAAAGCCTCCCATGTTTTAAAAGGATTTTTAAATAAGGACCCCAAAGAGGGG
CTCGGCTGCCGGCCACAGACTGGATTTTCTGACATCAAGTCCCACGCGTTCTTCCGCAGC
ATAGGCTGGGACTTGCTGGAGAAGAAGCAGGCGCTCCCTCCATTCCAGCCACAGATCACA
GACGACTACGGTCTGGACAACTTTGACACACAGTTCACCAGCGAGCCCGTGCAGCTGACC
CCAGACGATGAGGATGCCATAAAGAGGATCGACCAGTCAGAGTTCGAAGGCTTTGAGTAT
ATCAACCCATTATTGCTGTCCACCGAGGAGTCGGTGTGA
Enzyme 43 GenBank Gene ID AK290995 Link Image
Enzyme 43 GeneCard ID PRKCZ Link Image
Enzyme 43 GenAtlas ID PRKCZ Link Image
Enzyme 43 HGNC ID HGNC:9412 Link Image
Enzyme 43 Chromosome Location 1
Enzyme 43 Locus 1p36.33-p36.2
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Barbee JL, Deutscher SL, Loomis CR, Burns DJ: The cDNA sequence encoding human protein kinase C-zeta. Gene. 1993 Oct 15;132(2):305-6. [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. 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. Kochs G, Hummel R, Meyer D, Hug H, Marme D, Sarre TF: Activation and substrate specificity of the human protein kinase C alpha and zeta isoenzymes. Eur J Biochem. 1993 Sep 1;216(2):597-606. [PubMed Link Image]
  6. Sanchez P, De Carcer G, Sandoval IV, Moscat J, Diaz-Meco MT: Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62. Mol Cell Biol. 1998 May;18(5):3069-80. [PubMed Link Image]
  7. Chou MM, Hou W, Johnson J, Graham LK, Lee MH, Chen CS, Newton AC, Schaffhausen BS, Toker A: Regulation of protein kinase C zeta by PI 3-kinase and PDK-1. Curr Biol. 1998 Sep 24;8(19):1069-77. [PubMed Link Image]
  8. Sanz L, Sanchez P, Lallena MJ, Diaz-Meco MT, Moscat J: The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation. EMBO J. 1999 Jun 1;18(11):3044-53. [PubMed Link Image]
  9. Noda Y, Takeya R, Ohno S, Naito S, Ito T, Sumimoto H: Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C. Genes Cells. 2001 Feb;6(2):107-19. [PubMed Link Image]
  10. Chang S, Kim JH, Shin J: p62 forms a ternary complex with PKCzeta and PAR-4 and antagonizes PAR-4-induced PKCzeta inhibition. FEBS Lett. 2002 Jan 2;510(1-2):57-61. [PubMed Link Image]
  11. Gao L, Macara IG, Joberty G: Multiple splice variants of Par3 and of a novel related gene, Par3L, produce proteins with different binding properties. Gene. 2002 Jul 10;294(1-2):99-107. [PubMed Link Image]
  12. Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A: Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C. Biochem Biophys Res Commun. 2003 Aug 1;307(3):459-65. [PubMed Link Image]
  13. Wilson MI, Gill DJ, Perisic O, Quinn MT, Williams RL: PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62. Mol Cell. 2003 Jul;12(1):39-50. [PubMed Link Image]
  14. 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]
  15. Hilton HN, Stanford PM, Harris J, Oakes SR, Kaplan W, Daly RJ, Ormandy CJ: KIBRA interacts with discoidin domain receptor 1 to modulate collagen-induced signalling. Biochim Biophys Acta. 2008 Mar;1783(3):383-93. Epub 2008 Jan 9. [PubMed Link Image]
  16. 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]
  17. 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]
  18. 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]
  19. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 6732
Enzyme 44 Name Protein kinase C iota type
Enzyme 44 Synonyms
  1. Atypical protein kinase C-lambda/iota
  2. PRKC-lambda/iota
  3. aPKC-lambda/iota
  4. nPKC-iota
Enzyme 44 Gene Name PRKCI
Enzyme 44 Protein Sequence >Protein kinase C iota type
MPTQRDSSTMSHTVAGGGSGDHSHQVRVKAYYRGDIMITHFEPSISFEGLCNEVRDMCSF
DNEQLFTMKWIDEEGDPCTVSSQLELEEAFRLYELNKDSELLIHVFPCVPERPGMPCPGE
DKSIYRRGARRWRKLYCANGHTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHK
KCHKLVTIECGRHSLPQEPVMPMDQSSMHSDHAQTVIPYNPSSHESLDQVGEEKEAMNTR
ESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQ
TEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSA
EISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYI
APEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIR
IPRSLSVKAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFK
PNISGEFGLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV
Enzyme 44 Number of Residues 596
Enzyme 44 Molecular Weight 68261.9
Enzyme 44 Theoretical pI 5.68
Enzyme 44 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • metal ion binding
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • zinc ion binding
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 44 General Function Involved in protein serine/threonine kinase activity
Enzyme 44 Specific Function Calcium-independent, phospholipid-dependent, serine- and threonine-specific kinase. May play a role in the secretory response to nutrients. Involved in cell polarization processes and the formation of epithelial tight junctions. Implicated in the activation of several signaling pathways including Ras, c-Src and NF-kappa-B pathways. Functions in both pro- and anti-apoptotic pathways. Functions in the RAC1/ERK signaling required for transformed growth. Plays a role in microtubule dynamics through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs)
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 133908623 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID P41743 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name KPCI_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >1791 bp
ATGCCGACCCAGAGGGACAGCAGCACCATGTCCCACACGGTCGCAGGCGGCGGCAGCGGG
GACCATTCCCACCAGGTCCGGGTGAAAGCCTACTACCGCGGGGATATCATGATAACACAT
TTTGAACCTTCCATCTCCTTTGAGGGCCTTTGCAATGAGGTTCGAGACATGTGTTCTTTT
GACAACGAACAGCTCTTCACCATGAAATGGATAGATGAGGAAGGAGACCCGTGTACAGTA
TCATCTCAGTTGGAGTTAGAAGAAGCCTTTAGACTTTATGAGCTAAACAAGGATTCTGAA
CTCTTGATTCATGTGTTCCCTTGTGTACCAGAACGTCCTGGGATGCCTTGTCCAGGAGAA
GATAAATCCATCTACCGTAGAGGTGCACGCCGCTGGAGAAAGCTTTATTGTGCCAATGGC
CACACTTTCCAAGCCAAGCGTTTCAACAGGCGTGCTCACTGTGCCATCTGCACAGACCGA
ATATGGGGACTTGGACGCCAAGGATATAAGTGCATCAACTGCAAACTCTTGGTTCATAAG
AAGTGCCATAAACTCGTCACAATTGAATGTGGGCGGCATTCTTTGCCACAGGAACCAGTG
ATGCCCATGGATCAGTCATCCATGCATTCTGACCATGCACAGACAGTAATTCCATATAAT
CCTTCAAGTCATGAGAGTTTGGATCAAGTTGGTGAAGAAAAAGAGGCAATGAACACCAGG
GAAAGTGGCAAAGCTTCATCCAGTCTAGGTCTTCAGGATTTTGATTTGCTCCGGGTAATA
GGAAGAGGAAGTTATGCCAAAGTACTGTTGGTTCGATTAAAAAAAACAGATCGTATTTAT
GCAATGAAAGTTGTGAAAAAAGAGCTTGTTAATGATGATGAGGATATTGATTGGGTACAG
ACAGAGAAGCATGTGTTTGAGCAGGCATCCAATCATCCTTTCCTTGTTGGGCTGCATTCT
TGCTTTCAGACAGAAAGCAGATTGTTCTTTGTTATAGAGTATGTAAATGGAGGAGACCTA
ATGTTTCATATGCAGCGACAAAGAAAACTTCCTGAAGAACATGCCAGATTTTACTCTGCA
GAAATCAGTCTAGCATTAAATTATCTTCATGAGCGAGGGATAATTTATAGAGATTTGAAA
CTGGACAATGTATTACTGGACTCTGAAGGCCACATTAAACTCACTGACTACGGCATGTGT
AAGGAAGGATTACGGCCAGGAGATACAACCAGCACTTTCTGTGGTACTCCTAATTACATT
GCTCCTGAAATTTTAAGAGGAGAAGATTATGGTTTCAGTGTTGACTGGTGGGCTCTTGGA
GTGCTCATGTTTGAGATGATGGCAGGAAGGTCTCCATTTGATATTGTTGGGAGCTCCGAT
AACCCTGACCAGAACACAGAGGATTATCTCTTCCAAGTTATTTTGGAAAAACAAATTCGC
ATACCACGTTCTCTGTCTGTAAAAGCTGCAAGTGTTCTGAAGAGTTTTCTTAATAAGGAC
CCTAAGGAACGATTGGGTTGTCATCCTCAAACAGGATTTGCTGATATTCAGGGACACCCG
TTCTTCCGAAATGTTGATTGGGATATGATGGAGCAAAAACAGGTGGTACCTCCCTTTAAA
CCAAATATTTCTGGGGAATTTGGTTTGGACAACTTTGATTCTCAGTTTACTAATGAACCT
GTCCAGCTCACTCCAGATGACGATGACATTGTGAGGAAGATTGATCAGTCTGAATTTGAA
GGTTTTGAGTATATCAATCCTCTTTTGATGTCTGCAGAAGAATGTGTCTGA
Enzyme 44 GenBank Gene ID NM_002740.5 Link Image
Enzyme 44 GeneCard ID PRKCI Link Image
Enzyme 44 GenAtlas ID PRKCI Link Image
Enzyme 44 HGNC ID HGNC:9404 Link Image
Enzyme 44 Chromosome Location 3
Enzyme 44 Locus 3q26.3
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References
  1. Selbie LA, Schmitz-Peiffer C, Sheng Y, Biden TJ: Molecular cloning and characterization of PKC iota, an atypical isoform of protein kinase C derived from insulin-secreting cells. J Biol Chem. 1993 Nov 15;268(32):24296-302. [PubMed Link Image]
  2. Mazzarella R, Ciccodicola A, Esposito T, Arcucci A, Migliaccio C, Jones C, Schlessinger D, D'Urso M, D'Esposito M: Human protein kinase C Iota gene (PRKCI) is closely linked to the BTK gene in Xq21.3. Genomics. 1995 Apr 10;26(3):629-31. [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. Diaz-Meco MT, Municio MM, Sanchez P, Lozano J, Moscat J: Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo. Mol Cell Biol. 1996 Jan;16(1):105-14. [PubMed Link Image]
  5. Sanchez P, De Carcer G, Sandoval IV, Moscat J, Diaz-Meco MT: Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62. Mol Cell Biol. 1998 May;18(5):3069-80. [PubMed Link Image]
  6. Sanz L, Sanchez P, Lallena MJ, Diaz-Meco MT, Moscat J: The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation. EMBO J. 1999 Jun 1;18(11):3044-53. [PubMed Link Image]
  7. Noda Y, Takeya R, Ohno S, Naito S, Ito T, Sumimoto H: Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C. Genes Cells. 2001 Feb;6(2):107-19. [PubMed Link Image]
  8. Suzuki A, Yamanaka T, Hirose T, Manabe N, Mizuno K, Shimizu M, Akimoto K, Izumi Y, Ohnishi T, Ohno S: Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures. J Cell Biol. 2001 Mar 19;152(6):1183-96. [PubMed Link Image]
  9. Tisdale EJ: Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway. J Biol Chem. 2002 Feb 1;277(5):3334-41. Epub 2001 Nov 27. [PubMed Link Image]
  10. Wooten MW, Vandenplas ML, Seibenhener ML, Geetha T, Diaz-Meco MT: Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase C's via a src kinase pathway. Mol Cell Biol. 2001 Dec;21(24):8414-27. [PubMed Link Image]
  11. White WO, Seibenhener ML, Wooten MW: Phosphorylation of tyrosine 256 facilitates nuclear import of atypical protein kinase C. J Cell Biochem. 2002;85(1):42-53. [PubMed Link Image]
  12. Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A: Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C. Biochem Biophys Res Commun. 2003 Aug 1;307(3):459-65. [PubMed Link Image]
  13. Yamanaka T, Horikoshi Y, Sugiyama Y, Ishiyama C, Suzuki A, Hirose T, Iwamatsu A, Shinohara A, Ohno S: Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of PAR-3 to regulate epithelial cell polarity. Curr Biol. 2003 Apr 29;13(9):734-43. [PubMed Link Image]
  14. Tisdale EJ: Rab2 interacts directly with atypical protein kinase C (aPKC) iota/lambda and inhibits aPKCiota/lambda-dependent glyceraldehyde-3-phosphate dehydrogenase phosphorylation. J Biol Chem. 2003 Dec 26;278(52):52524-30. Epub 2003 Oct 21. [PubMed Link Image]
  15. Regala RP, Weems C, Jamieson L, Copland JA, Thompson EA, Fields AP: Atypical protein kinase Ciota plays a critical role in human lung cancer cell growth and tumorigenicity. J Biol Chem. 2005 Sep 2;280(35):31109-15. Epub 2005 Jul 1. [PubMed Link Image]
  16. Bicaku E, Patel R, Acevedo-Duncan M: Cyclin-dependent kinase activating kinase/Cdk7 co-localizes with PKC-iota in human glioma cells. Tissue Cell. 2005 Feb;37(1):53-8. Epub 2005 Jan 25. [PubMed Link Image]
  17. Tisdale EJ, Artalejo CR: Src-dependent aprotein kinase C iota/lambda (aPKCiota/lambda) tyrosine phosphorylation is required for aPKCiota/lambda association with Rab2 and glyceraldehyde-3-phosphate dehydrogenase on pre-golgi intermediates. J Biol Chem. 2006 Mar 31;281(13):8436-42. Epub 2006 Feb 1. [PubMed Link Image]
  18. 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]
  19. Hirano Y, Yoshinaga S, Ogura K, Yokochi M, Noda Y, Sumimoto H, Inagaki F: Solution structure of atypical protein kinase C PB1 domain and its mode of interaction with ZIP/p62 and MEK5. J Biol Chem. 2004 Jul 23;279(30):31883-90. Epub 2004 May 13. [PubMed Link Image]
  20. Hirano Y, Yoshinaga S, Takeya R, Suzuki NN, Horiuchi M, Kohjima M, Sumimoto H, Inagaki F: Structure of a cell polarity regulator, a complex between atypical PKC and Par6 PB1 domains. J Biol Chem. 2005 Mar 11;280(10):9653-61. Epub 2004 Dec 7. [PubMed Link Image]
  21. Messerschmidt A, Macieira S, Velarde M, Badeker M, Benda C, Jestel A, Brandstetter H, Neuefeind T, Blaesse M: Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif. J Mol Biol. 2005 Sep 30;352(4):918-31. [PubMed Link Image]
  22. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 6751
Enzyme 45 Name Rho-associated protein kinase 1
Enzyme 45 Synonyms
  1. Renal carcinoma antigen NY-REN-35
  2. Rho-associated, coiled-coil-containing protein kinase 1
  3. p160 ROCK-1
  4. p160ROCK
Enzyme 45 Gene Name ROCK1
Enzyme 45 Protein Sequence >Rho-associated protein kinase 1
MSTGDSFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYK
DTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAF
FWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTA
EVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDY
ISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFP
DDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLS
SDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYSNRRYLSSANPNDNRTSSNA
DKSLQESLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLEST
VSQIEKEKMLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKL
SQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQTD
KDYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLN
HSEKEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKL
KEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEQES
NKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMR
ELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKKIQELQNEKETLATQLDLAETKAE
SEQLARGLLEEQYFELTQESKKAASRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENE
ELTEKMKKAEEEYKLEKEEEISNLKAAFEKNINTERTLKTQAVNKLAEIMNRKDFKIDRK
KANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQL
ASKESDIEQLRAKLLDLSDSTSVASFPSADETDGNLPESRIEGWLSVPNRGNIKRYGWKK
QYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQILY
ANEGECRKDVEMEPVQQAEKTNFQNHKGHEFIPTLYHFPANCDACAKPLWHVFKPPPALE
CRRCHVKCHRDHLDKKEDLICPCKVSYDVTSARDMLLLACSQDEQKKWVTHLVKKIPKNP
PSGFVRASPRTLSTRSTANQSFRKVVKNTSGKTS
Enzyme 45 Number of Residues 1354
Enzyme 45 Molecular Weight 158173.5
Enzyme 45 Theoretical pI 5.67
Enzyme 45 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biological regulation
  • cell division
  • cellular metabolic process
  • cellular process
  • cytokinesis
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
Enzyme 45 General Function Involved in protein serine/threonine kinase activity
Enzyme 45 Specific Function Phosphorylates and activates DAPK3, which then regulates myosin light chain phosphatase through phosphorylation of MYPT1 thereby regulating the assembly of the actin cytoskeleton, cell migration, invasiveness of tumor cells, smooth muscle contraction and neurite outgrowth. Required for centromere positioning and centromere-dependent exit from mitosis. Necessary for apoptotic membrane blebbing
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein Not Available
Enzyme 45 UniProtKB/Swiss-Prot ID Q13464 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name ROCK1_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >4065 bp
ATGTCGACTGGGGACAGTTTTGAGACTCGATTTGAAAAAATGGACAACCTGCTGCGGGAT
CCCAAATCGGAAGTGAATTCGGATTGTTTGCTGGATGGATTGGATGCTTTGGTATATGAT
TTGGATTTTCCTGCCTTAAGAAAAAACAAAAATATTGACAACTTTTTAAGCAGATATAAA
GACACAATAAATAAAATCAGAGATTTACGAATGAAAGCTGAAGATTATGAAGTAGTGAAG
GTGATTGGTAGAGGTGCATTTGGAGAAGTTCAATTGGTAAGGCATAAATCCACCAGGAAG
GTATATGCTATGAAGCTTCTCAGCAAATTTGAAATGATAAAGAGATCTGATTCTGCTTTT
TTCTGGGAAGAAAGGGACATCATGGCTTTTGCCAACAGTCCTTGGGTTGTTCAGCTTTTT
TATGCATTCCAAGATGATCGTTATCTCTACATGGTGATGGAATACATGCCTGGTGGAGAT
CTTGTAAACTTAATGAGCAACTATGATGTGCCTGAAAAATGGGCACGATTCTATACTGCA
GAAGTAGTTCTTGCATTGGATGCAATCCATTCCATGGGTTTTATTCACAGAGATGTGAAG
CCTGATAACATGCTGCTGGATAAATCTGGACATTTGAAGTTAGCAGATTTTGGTACTTGT
ATGAAGATGAATAAGGAAGGCATGGTACGATGTGATACAGCGGTTGGAACACCTGATTAT
ATTTCCCCTGAAGTATTAAAATCCCAAGGTGGTGATGGTTATTATGGAAGAGAATGTGAC
TGGTGGTCGGTTGGGGTATTTTTATACGAAATGCTTGTAGGTGATACACCTTTTTATGCA
GATTCTTTGGTTGGAACTTACAGTAAAATTATGAACCATAAAAATTCACTTACCTTTCCT
GATGATAATGACATATCAAAAGAAGCAAAAAACCTTATTTGTGCCTTCCTTACTGACAGG
GAAGTGAGGTTAGGGCGAAATGGTGTAGAAGAAATCAAACGACATCTCTTCTTCAAAAAT
GACCAGTGGGCTTGGGAAACGCTCCGAGACACTGTAGCACCAGTTGTACCCGATTTAAGT
AGTGACATTGATACTAGTAATTTTGATGACTTGGAAGAAGATAAAGGAGAGGAAGAAACA
TTCCCTATTCCTAAAGCTTTCGTTGGCAATCAACTACCTTTTGTAGGATTTACATATTAT
AGCAATCGTAGATACTTATCTTCAGCAAATCCTAATGATAACAGAACTAGCTCCAATGCA
GATAAAAGCTTGCAGGAAAGTTTGCAAAAAACAATCTATAAGCTGGAAGAACAGCTGCAT
AATGAAATGCAGTTAAAAGATGAAATGGAGCAGAAGTGCAGAACCTCAAACATAAAACTA
GACAAGATAATGAAAGAATTGGATGAAGAGGGAAATCAAAGAAGAAATCTAGAATCTACA
GTGTCTCAGATTGAGAAGGAGAAAATGTTGCTACAGCATAGAATTAATGAGTACCAAAGA
AAAGCTGAACAGGAAAATGAGAAGAGAAGAAATGTAGAAAATGAAGTTTCTACATTAAAG
GATCAGTTGGAAGACTTAAAGAAAGTCAGTCAGAATTCACAGCTTGCTAATGAGAAGCTG
TCCCAGTTACAAAAGCAGCTAGAAGAAGCCAATGACTTACTTAGGACAGAATCGGACACA
GCTGTAAGATTGAGGAAGAGTCACACAGAGATGAGCAAGTCAATTAGTCAGTTAGAGTCC
CTGAACAGAGAGTTGCAAGAGAGAAATCGAATTTTAGAGAATTCTAAGTCACAAACAGAC
AAAGATTATTACCAGCTGCAAGCTATATTAGAAGCTGAACGAAGAGACAGAGGTCATGAT
TCTGAGATGATTGGAGACCTTCAAGCTCGAATTACATCTTTACAAGAGGAGGTGAAGCAT
CTCAAACATAATCTCGAAAAAGTGGAAGGAGAAAGAAAAGAGGCTCAAGACATGCTTAAT
CACTCAGAAAAGGAAAAGAATAATTTAGAGATAGATTTAAACTACAAACTTAAATCATTA
CAACAACGGTTAGAACAAGAGGTAAATGAACACAAAGTAACCAAAGCTCGTTTAACTGAC
AAACATCAATCTATTGAAGAGGCAAAGTCTGTGGCAATGTGTGAGATGGAAAAAAAGCTG
AAAGAAGAAAGAGAAGCTCGAGAGAAGGCTGAAAATCGGGTTGTTCAGATTGAGAAACAG
TGTTCCATGCTAGACGTTGATCTGAAGCAATCTCAGCAGAAACTAGAACATTTGACTGGA
AATAAAGAAAGGATGGAGGATGAAGTTAAGAATCTAACCCTGCAACTGGAGCAGGAATCA
AATAAGCGGCTGTTGTTACAAAATGAATTGAAGACTCAAGCATTTGAGGCAGACAATTTA
AAAGGTTTAGAAAAGCAGATGAAACAGGAAATAAATACTTTATTGGAAGCAAAGAGATTA
TTAGAATTTGAGTTAGCTCAGCTTACGAAACAGTATAGAGGAAATGAAGGACAGATGCGG
GAGCTACAAGATCAGCTTGAAGCTGAGCAATATTTCTCGACACTTTATAAAACCCAGGTA
AAGGAACTTAAAGAAGAAATTGAAGAAAAAAACAGAGAAAATTTAAAGAAAATACAGGAA
CTACAAAATGAAAAAGAAACTCTTGCTACTCAGTTGGATCTAGCAGAAACAAAAGCTGAG
TCTGAGCAGTTGGCGCGAGGCCTTCTGGAAGAACAGTATTTTGAATTGACGCAAGAAAGC
AAGAAAGCTGCTTCAAGAAATAGACAAGAGATTACAGATAAAGATCACACTGTTAGTCGG
CTTGAAGAAGCAAACAGCATGCTAACCAAAGATATTGAAATATTAAGAAGAGAGAATGAA
GAGCTAACAGAGAAAATGAAGAAGGCAGAGGAAGAATATAAACTGGAGAAGGAGGAGGAG
ATCAGTAATCTTAAGGCTGCCTTTGAAAAGAATATCAACACTGAACGAACCCTTAAAACA
CAGGCTGTTAACAAATTGGCAGAAATAATGAATCGAAAAGATTTTAAAATTGATAGAAAG
AAAGCTAATACACAAGATTTGAGAAAGAAAGAAAAGGAAAATCGAAAGCTGCAACTGGAA
CTCAACCAAGAAAGAGAGAAATTCAACCAGATGGTAGTGAAACATCAGAAGGAACTGAAT
GACATGCAAGCGCAATTGGTAGAAGAATGTGCACATAGGAATGAGCTTCAGATGCAGTTG
GCCAGCAAAGAGAGTGATATTGAGCAATTGCGTGCTAAACTTTTGGACCTCTCGGATTCT
ACAAGTGTTGCTAGTTTTCCTAGTGCTGATGAAACTGATGGTAACCTCCCAGAGTCAAGA
ATTGAAGGTTGGCTTTCAGTACCAAATAGAGGAAATATCAAACGATATGGCTGGAAGAAA
CAGTATGTTGTGGTAAGCAGCAAAAAAATTTTGTTCTATAATGACGAACAAGATAAGGAG
CAATCCAATCCATCTATGGTATTGGACATAGATAAACTGTTTCACGTTAGACCTGTAACC
CAAGGAGATGTGTATAGAGCTGAAACTGAAGAAATTCCTAAAATATTCCAGATACTATAT
GCAAATGAAGGTGAATGTAGAAAAGATGTAGAGATGGAACCAGTACAACAAGCTGAAAAA
ACTAATTTCCAAAATCACAAAGGCCATGAGTTTATTCCTACACTCTACCACTTTCCTGCC
AATTGTGATGCCTGTGCCAAACCTCTCTGGCATGTTTTTAAGCCACCCCCTGCCCTAGAG
TGTCGAAGATGCCATGTTAAGTGCCACAGAGATCACTTAGATAAGAAAGAGGACTTAATT
TGTCCATGTAAAGTAAGTTATGATGTAACATCAGCAAGAGATATGCTGCTGTTAGCATGT
TCTCAGGATGAACAAAAAAAATGGGTAACTCATTTAGTAAAGAAAATCCCTAAGAATCCA
CCATCTGGTTTTGTTCGTGCTTCCCCTCGAACGCTTTCTACAAGATCCACTGCAAATCAG
TCTTTCCGGAAAGTGGTCAAAAATACATCTGGAAAAACTAGTTAA
Enzyme 45 GenBank Gene ID U43195 Link Image
Enzyme 45 GeneCard ID ROCK1 Link Image
Enzyme 45 GenAtlas ID ROCK1 Link Image
Enzyme 45 HGNC ID HGNC:10251 Link Image
Enzyme 45 Chromosome Location 1
Enzyme 45 Locus 18q11.1
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Ishizaki T, Maekawa M, Fujisawa K, Okawa K, Iwamatsu A, Fujita A, Watanabe N, Saito Y, Kakizuka A, Morii N, Narumiya S: The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase. EMBO J. 1996 Apr 15;15(8):1885-93. [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. Van Eyk JE, Arrell DK, Foster DB, Strauss JD, Heinonen TY, Furmaniak-Kazmierczak E, Cote GP, Mak AS: Different molecular mechanisms for Rho family GTPase-dependent, Ca2+-independent contraction of smooth muscle. J Biol Chem. 1998 Sep 4;273(36):23433-9. [PubMed Link Image]
  4. Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed Link Image]
  5. Kawano Y, Fukata Y, Oshiro N, Amano M, Nakamura T, Ito M, Matsumura F, Inagaki M, Kaibuchi K: Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo. J Cell Biol. 1999 Nov 29;147(5):1023-38. [PubMed Link Image]
  6. Maekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A, Iwamatsu A, Obinata T, Ohashi K, Mizuno K, Narumiya S: Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science. 1999 Aug 6;285(5429):895-8. [PubMed Link Image]
  7. Sumi T, Matsumoto K, Nakamura T: Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase. J Biol Chem. 2001 Jan 5;276(1):670-6. [PubMed Link Image]
  8. Sebbagh M, Renvoize C, Hamelin J, Riche N, Bertoglio J, Breard J: Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing. Nat Cell Biol. 2001 Apr;3(4):346-52. [PubMed Link Image]
  9. Riento K, Guasch RM, Garg R, Jin B, Ridley AJ: RhoE binds to ROCK I and inhibits downstream signaling. Mol Cell Biol. 2003 Jun;23(12):4219-29. [PubMed Link Image]
  10. Riento K, Ridley AJ: Rocks: multifunctional kinases in cell behaviour. Nat Rev Mol Cell Biol. 2003 Jun;4(6):446-56. [PubMed Link Image]
  11. Morita E, Sandrin V, Chung HY, Morham SG, Gygi SP, Rodesch CK, Sundquist WI: Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis. EMBO J. 2007 Oct 3;26(19):4215-27. Epub 2007 Sep 13. [PubMed Link Image]
  12. Hagerty L, Weitzel DH, Chambers J, Fortner CN, Brush MH, Loiselle D, Hosoya H, Haystead TA: ROCK1 phosphorylates and activates zipper-interacting protein kinase. J Biol Chem. 2007 Feb 16;282(7):4884-93. Epub 2006 Dec 8. [PubMed Link Image]
  13. 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]
  14. 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]
  15. 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]
  16. 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]
  17. 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]
  18. Dvorsky R, Blumenstein L, Vetter IR, Ahmadian MR: Structural insights into the interaction of ROCKI with the switch regions of RhoA. J Biol Chem. 2004 Feb 20;279(8):7098-104. Epub 2003 Dec 2. [PubMed Link Image]
  19. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 6767
Enzyme 46 Name Serine/threonine-protein kinase D1
Enzyme 46 Synonyms
  1. Protein kinase C mu type
  2. Protein kinase D
  3. nPKC-D1
  4. nPKC-mu
Enzyme 46 Gene Name PRKD1
Enzyme 46 Protein Sequence >Serine/threonine-protein kinase D1
MSAPPVLRPPSPLLPVAAAAAAAAAALVPGSGPGPAPFLAPVAAPVGGISFHLQIGLSRE
PVLLLQDSSGDYSLAHVREMACSIVDQKFPECGFYGMYDKILLFRHDPTSENILQLVKAA
SDIQEGDLIEVVLSASATFEDFQIRPHALFVHSYRAPAFCDHCGEMLWGLVRQGLKCEGC
GLNYHKRCAFKIPNNCSGVRRRRLSNVSLTGVSTIRTSSAELSTSAPDEPLLQKSPSESF
IGREKRSNSQSYIGRPIHLDKILMSKVKVPHTFVIHSYTRPTVCQYCKKLLKGLFRQGLQ
CKDCRFNCHKRCAPKVPNNCLGEVTINGDLLSPGAESDVVMEEGSDDNDSERNSGLMDDM
EEAMVQDAEMAMAECQNDSGEMQDPDPDHEDANRTISPSTSNNIPLMRVVQSVKHTKRKS
STVMKEGWMVHYTSKDTLRKRHYWRLDSKCITLFQNDTGSRYYKEIPLSEILSLEPVKTS
ALIPNGANPHCFEITTANVVYYVGENVVNPSSPSPNNSVLTSGVGADVARMWEIAIQHAL
MPVIPKGSSVGTGTNLHRDISVSISVSNCQIQENVDISTVYQIFPDEVLGSGQFGIVYGG
KHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVME
KLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPF
PQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGT
FPFNEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQ
DYQTWLDLRELECKIGERYITHESDDLRWEKYAGEQGLQYPTHLINPSASHSDTPETEET
EMKALGERVSIL
Enzyme 46 Number of Residues 912
Enzyme 46 Molecular Weight 101703.3
Enzyme 46 Theoretical pI 6.61
Enzyme 46 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase C activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 46 General Function Involved in intracellular signaling pathway
Enzyme 46 Specific Function Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress through activation of NF-kappa-B
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 189054333 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID Q15139 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name KPCD1_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >2739 bp
ATGAGCGCCCCTCCGGTCCTGCGGCCGCCCAGTCCGCTGCTGCCCGTGGCGGCGGCAGCT
GCCGCAGCGGCCGCCGCACTGGTCCCAGGGTCCGGGCCCGGGCCCGCGCCGTTCTTGGCT
CCTGTCGCGGCCCCGGTCGGGGGCATCTCGTTCCATCTGCAGATCGGCCTGAGCCGTGAG
CCGGTGCTGCTGCTGCAGGACTCGTCCGGGGACTACAGCCTGGCGCACGTCCGCGAGATG
GCTTGCTCCATTGTCGACCAGAAGTTCCCTGAATGTGGTTTCTACGGAATGTATGATAAG
ATCCTGCTTTTTCGCCATGACCCTACCTCTGAAAACATCCTTCAGCTGGTGAAAGCGGCC
AGTGATATCCAGGAAGGCGATCTTATTGAAGTGGTCTTGTCAGCTTCCGCCACCTTTGAA
GACTTTCAGATTCGTCCCCACGCTCTCTTTGTTCATTCATACAGAGCTCCAGCTTTCTGT
GATCACTGTGGAGAAATGCTGTGGGGGCTGGTACGTCAAGGTCTTAAATGTGAAGGGTGT
GGTCTGAATTACCATAAGAGATGTGCATTTAAAATACCCAACAATTGCAGCGGTGTGAGG
CGGAGAAGGCTCTCAAACGTTTCCCTCACTGGGGTCAGCACCATCCGCACATCATCTGCT
GAACTCTCTACAAGTGCCCCTGATGAGCCCCTTCTGCAAAAATCACCATCAGAGTCGTTT
ATTGGTCGAGAGAAGAGGTCAAATTCTCAATCATACATTGGACGACCAATTCACCTTGAC
AAGATTTTGATGTCTAAAGTTAAAGTGCCGCACACATTTGTCATCCACTCCTACACCCGG
CCCACAGTGTGCCAGTACTGCAAGAAGCTTCTGAAGGGGCTTTTCAGGCAGGGCTTGCAG
TGCAAAGATTGCAGATTCAACTGCCATAAACGTTGTGCACCGAAAGTACCAAACAACTGC
CTTGGCGAAGTGACCATTAATGGAGATTTGCTTAGCCCTGGGGCAGAGTCTGATGTGGTC
ATGGAAGAAGGGAGTGATGACAATGATAGTGAAAGGAACAGTGGGCTCATGGATGATATG
GAAGAAGCAATGGTCCAAGATGCAGAGATGGCAATGGCAGAGTGCCAGAACGACAGTGGC
GAGATGCAAGATCCAGACCCAGACCACGAGGACGCCAACAGAACCATCAGTCCATCAACA
AGCAACAATATCCCACTCATGAGGGTAGTGCAGTCTGTCAAACACACGAAGAGGAAAAGC
AGCACAGTCATGAAAGAAGGATGGATGGTCCACTACACCAGCAAGGACACGCTGCGGAAA
CGGCACTATTGGAGATTGGATAGCAAATGTATTACCCTCTTTCAGAATGACACAGGAAGC
AGGTACTACAAGGAAATTCCTTTATCTGAAATTTTGTCTCTGGAACCAGTAAAAACTTCA
GCTTTAATTCCTAATGGGGCCAATCCTCATTGTTTCGAAATCACTACGGCAAATGTAGTG
TATTATGTGGGAGAAAATGTGGTCAATCCTTCCAGCCCATCACCAAATAACAGTGTTCTC
ACCAGTGGCGTTGGTGCAGATGTGGCCAGGATGTGGGAGATAGCCATCCAGCATGCCCTT
ATGCCCGTCATTCCCAAGGGCTCCTCCGTGGGTACAGGAACCAACTTGCACAGAGATATC
TCTGTGAGTATTTCAGTATCAAATTGCCAGATTCAAGAAAATGTGGACATCAGCACAGTA
TATCAGATTTTTCCTGATGAAGTACTGGGTTCTGGACAGTTTGGAATTGTTTATGGAGGA
AAACATCGTAAAACAGGAAGAGATGTAGCTATTAAAATCATTGACAAATTACGATTTCCA
ACAAAACAAGAAAGCCAGCTTCGTAATGAGGTTGCAATTCTACAGAACCTTCATCACCCT
GGTGTTGTAAATTTGGAGTGTATGTTTGAGACGCCTGAAAGAGTGTTTGTTGTTATGGAA
AAACTCCATGGAGACATGCTGGAAATGATCTTGTCAAGTGAAAAGGGCAGGTTGCCAGAG
CACATAACGAAGTTTTTAATTACTCAGATACTCGTGGCTTTGCGGCACCTTCATTTTAAA
AATATCGTTCACTGTGACCTCAAACCAGAAAATGTGTTGCTAGCCTCAGCTGATCCTTTT
CCTCAGGTGAAACTTTGTGATTTTGGTTTTGCCCGGATCATTGGAGAGAAGTCTTTCCGG
AGGTCAGTGGTGGGTACCCCCGCTTACCTGGCTCCTGAGGTCCTAAGGAACAAGGGCTAC
AATCGCTCTCTAGACATGTGGTCTGTTGGGGTCATCATCTATGTAAGCCTAAGCGGCACA
TTCCCATTTAATGAAGATGAAGACATACACGACCAAATTCAGAATGCAGCTTTCATGTAT
CCACCAAATCCCTGGAAGGAAATATCTCATGAAGCCATTGATCTTATCAACAATTTGCTG
CAAGTAAAAATGAGAAAGCGCTACAGTGTGGATAAGACCTTGAGCCACCCTTGGCTACAG
GACTATCAGACCTGGTTAGATTTGCGAGAGCTGGAATGCAAAATCGGGGAGCGCTACATC
ACCCATGAAAGTGATGACCTGAGGTGGGAGAAGTATGCAGGCGAGCAGGGGCTGCAGTAC
CCCACACACCTGATCAATCCAAGTGCTAGCCACAGTGACACTCCTGAGACTGAAGAAACA
GAAATGAAAGCCCTCGGTGAGCGTGTCAGCATCCTCTGA
Enzyme 46 GenBank Gene ID AK314170 Link Image
Enzyme 46 GeneCard ID PRKD1 Link Image
Enzyme 46 GenAtlas ID PRKD1 Link Image
Enzyme 46 HGNC ID HGNC:9407 Link Image
Enzyme 46 Chromosome Location 1
Enzyme 46 Locus 14q11
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Johannes FJ, Prestle J, Eis S, Oberhagemann P, Pfizenmaier K: PKCu is a novel, atypical member of the protein kinase C family. J Biol Chem. 1994 Feb 25;269(8):6140-8. [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. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  4. Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A: Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C. Biochem Biophys Res Commun. 2003 Aug 1;307(3):459-65. [PubMed Link Image]
  5. Storz P, Doppler H, Johannes FJ, Toker A: Tyrosine phosphorylation of protein kinase D in the pleckstrin homology domain leads to activation. J Biol Chem. 2003 May 16;278(20):17969-76. Epub 2003 Mar 11. [PubMed Link Image]
  6. Giorgianni F, Zhao Y, Desiderio DM, Beranova-Giorgianni S: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line. Electrophoresis. 2007 Jun;28(12):2027-34. [PubMed Link Image]
  7. Doppler H, Storz P: A novel tyrosine phosphorylation site in protein kinase D contributes to oxidative stress-mediated activation. J Biol Chem. 2007 Nov 2;282(44):31873-81. Epub 2007 Sep 5. [PubMed Link Image]
  8. Chen J, Deng F, Li J, Wang QJ: Selective binding of phorbol esters and diacylglycerol by individual C1 domains of the PKD family. Biochem J. 2008 Apr 15;411(2):333-42. [PubMed Link Image]
  9. 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]
  10. 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]
  11. 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]
  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]
  13. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 6775
Enzyme 47 Name Protein kinase C gamma type
Enzyme 47 Synonyms
  1. PKC-gamma
Enzyme 47 Gene Name PRKCG
Enzyme 47 Protein Sequence >Protein kinase C gamma type
MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIG
KQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSL
LYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEA
RNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRL
SVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQ
KFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKG
SFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQL
HSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRD
LKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWS
FGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGS
GPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRL
VLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM
Enzyme 47 Number of Residues 697
Enzyme 47 Molecular Weight 78447.2
Enzyme 47 Theoretical pI 7.49
Enzyme 47 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • metal ion binding
  • nucleoside binding
  • protein kinase C activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • zinc ion binding
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 47 General Function Involved in protein serine/threonine kinase activity
Enzyme 47 Specific Function PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein Not Available
Enzyme 47 UniProtKB/Swiss-Prot ID P05129 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name KPCG_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >2094 bp
ATGGCTGGTCTGGGCCCCGGCGTAGGCGATTCAGAGGGGGGACCCCGGCCCCTGTTCTGC
AGAAAGGGGGCTCTGAGGCAGAAGGTGGTCCACGAAGTCAAGAGCCACAAGTTCACCGCT
CGCTTCTTCAAGCAGCCCACCTTCTGCAGCCACTGCACCGACTTCATCTGGGGTATCGGA
AAGCAGGGCCTGCAATGTCAAGTCTGCAGCTTTGTGGTTCATCGACGATGCCACGAATTT
GTGACCTTCGAGTGTCCAGGCGCTGGGAAGGGCCCCCAGACGGACGACCCCCGGAACAAA
CACAAGTTCCGCCTGCATAGCTACAGCAGCCCCACCTTCTGCGACCACTGTGGCTCCCTC
CTCTACGGGCTTGTGCACCAGGGCATGAAATGTTCTTGCTGCGAGATGAACGTGCACCGG
CGCTGTGTGCGTAGCGTGCCCTCTCTGTGCGGTGTGGACCACACCGAGCGCCGCGGGCGC
CTGCAGCTGGAGATCCGGGCTCCCACAGCAGATGAGATCCACGTAACTGTTGGCGAGGCC
CGTAACCTAATTCCTATGGACCCCAATGGTCTCTCTGATCCCTATGTGAAACTGAAGCTC
ATCCCAGACCCTCGGAACCTGACGAAACAGAAGACCCGAACGGTGAAAGCCACGCTAAAC
CCTGTGTGGAATGAGACCTTTGTGTTCAACCTGAAGCCAGGGGATGTGGAGCGCCGGCTC
AGCGTGGAGGTGTGGGACTGGGACCGGACCTCCCGCAACGACTTCATGGGGGCCATGTCC
TTTGGCGTCTCGGAGCTGCTCAAGGCGCCCGTGGATGGCTGGTACAAGTTACTGAACCAG
GAGGAGGGCGAGTATTACAATGTGCCGGTGGCCGATGCTGACAACTGCAGCCTCCTCCAG
AAGTTTGAGGCTTGTAACTACCCCCTGGAATTGTATGAGCGGGTGCGGATGGGCCCCTCT
TCCTCTCCCATCCCCTCCCCTTCCCCTAGTCCCACCGACCCCAAGCGCTGCTTCTTCGGG
GCGAGTCCAGGACGCCTGCACATCTCCGACTTCAGCTTCCTCATGGTTCTAGGAAAAGGC
AGTTTTGGGAAGGTGATGCTGGCCGAGCGCAGGGGCTCTGATGAGCTCTACGCCATCAAG
ATCTTGAAAAAGGACGTGATCGTCCAGGACGACGATGTGGACTGCACGCTGGTGGAGAAA
CGTGTGCTGGCGCTGGGGGGCCGGGGTCCTGGCGGCCGGCCCCACTTCCTCACCCAGCTC
CACTCCACCTTCCAGACCCCGGACCGCCTGTATTTCGTGATGGAGTACGTCACCGGGGGA
GACTTGATGTACCACATTCAACAGCTGGGCAAGTTTAAGGAGCCCCATGCAGCGTTCTAC
GCGGCAGAAATCGCTATCGGCCTCTTCTTCCTTCACAATCAGGGCATCATCTACAGGGAC
CTGAAGCTGGACAATGTGATGCTGGATGCTGAGGGACACATCAAGATCACTGACTTTGGC
ATGTGTAAGGAGAACGTCTTCCCCGGGACGACAACCCGCACCTTCTGCGGGACCCCGGAC
TACATAGCCCCGGAGATCATTGCCTACCAGCCCTATGGGAAGTCTGTCGATTGGTGGTCC
TTTGGAGTTCTGCTGTATGAGATGTTGGCAGGACAGCCTCCCTTCGATGGGGAGGACGAG
GAGGAGCTGTTTCAGGCCATCATGGAACAAACTGTCACCTACCCCAAGTCGCTTTCCCGG
GAAGCCGTGGCCATCTGCAAGGGGTTCCTGACCAAGCACCCAGGGAAGCGCCTGGGCTCA
GGGCCTGATGGGGAACCTACCATCCGTGCACATGGCTTTTTCCGCTGGATTGACTGGGAG
CGGCTGGAACGATTGGAGATCCCGCCTCCTTTCAGACCCCGCCCGTGTGGCCGCAGCGGC
GAGAACTTTGACAAGTTCTTCACGCGGGCGGCGCCAGCGCTGACCCCTCCAGACCGCCTA
GTCCTGGCCAGCATCGACCAGGCCGATTTCCAGGGCTTCACCTACGTGAACCCCGACTTC
GTGCACCCGGATGCCCGCAGCCCCACCAGCCCAGTGCCTGTGCCCGTCATGTAA
Enzyme 47 GenBank Gene ID AF345987 Link Image
Enzyme 47 GeneCard ID PRKCG Link Image
Enzyme 47 GenAtlas ID PRKCG Link Image
Enzyme 47 HGNC ID HGNC:9402 Link Image
Enzyme 47 Chromosome Location 1
Enzyme 47 Locus 19q13.4
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Coussens L, Parker PJ, Rhee L, Yang-Feng TL, Chen E, Waterfield MD, Francke U, Ullrich A: Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways. Science. 1986 Aug 22;233(4766):859-66. [PubMed Link Image]
  3. Kochs G, Hummel R, Meyer D, Hug H, Marme D, Sarre TF: Activation and substrate specificity of the human protein kinase C alpha and zeta isoenzymes. Eur J Biochem. 1993 Sep 1;216(2):597-606. [PubMed Link Image]
  4. Benes CH, Wu N, Elia AE, Dharia T, Cantley LC, Soltoff SP: The C2 domain of PKCdelta is a phosphotyrosine binding domain. Cell. 2005 Apr 22;121(2):271-80. [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. 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. 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]
  9. Al-Maghtheh M, Vithana EN, Inglehearn CF, Moore T, Bird AC, Bhattacharya SS: Segregation of a PRKCG mutation in two RP11 families. Am J Hum Genet. 1998 May;62(5):1248-52. [PubMed Link Image]
  10. Dryja TP, McEvoy J, McGee TL, Berson EL: No mutations in the coding region of the PRKCG gene in three families with retinitis pigmentosa linked to the RP11 locus on chromosome 19q. Am J Hum Genet. 1999 Sep;65(3):926-8. [PubMed Link Image]
  11. Chen DH, Brkanac Z, Verlinde CL, Tan XJ, Bylenok L, Nochlin D, Matsushita M, Lipe H, Wolff J, Fernandez M, Cimino PJ, Bird TD, Raskind WH: Missense mutations in the regulatory domain of PKC gamma: a new mechanism for dominant nonepisodic cerebellar ataxia. Am J Hum Genet. 2003 Apr;72(4):839-49. Epub 2003 Mar 17. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 6814
Enzyme 48 Name Rho-associated protein kinase 2
Enzyme 48 Synonyms
  1. Rho kinase 2
  2. Rho-associated, coiled-coil-containing protein kinase 2
  3. p164 ROCK-2
Enzyme 48 Gene Name ROCK2
Enzyme 48 Protein Sequence >Rho-associated protein kinase 2
MSRPPPTGKMPGAPETAPGDGAGASRQRKLEALIRDPRSPINVESLLDGLNSLVLDLDFP
ALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAM
KLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNL
MSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMD
ETGMVHCDTAVGTPDYISPEVLKSQGGDGFYGRECDWWSVGVFLYEMLVGDTPFYADSLV
GTYSKIMDHKNSLCFPEDAEISKHAKNLICAFLTDREVRLGRNGVEEIRQHPFFKNDQWH
WDNIRETAAPVVPELSSDIDSSNFDDIEDDKGDVETFPIPKAFVGNQLPFIGFTYYRENL
LLSDSPSCRETDSIQSRKNEESQEIQKKLYTLEEHLSNEMQAKEELEQKCKSVNTRLEKT
AKELEEEITLRKSVESALRQLEREKALLQHKNAEYQRKADHEADKKRNLENDVNSLKDQL
EDLKKRNQNSQISTEKVNQLQRQLDETNALLRTESDTAARLRKTQAESSKQIQQLESNNR
DLQDKNCLLETAKLKLEKEFINLQSALESERRDRTHGSEIINDLQGRICGLEEDLKNGKI
LLAKVELEKRQLQERFTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNK
IYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLK
QKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMN
LEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQK
KQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQE
LTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQF
EKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQ
MIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLDSSSIGSGPG
DAEADDGFPESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVL
DIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEQEFPVEPVGEKSNYICHKG
HEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYD
ISTAKNLLLLANSTEEQQKWVSRLVKKIPKKPPAPDPFARSSPRTSMKIQQNQSIRRPSR
QLAPNKPS
Enzyme 48 Number of Residues 1388
Enzyme 48 Molecular Weight 160898.6
Enzyme 48 Theoretical pI 5.84
Enzyme 48 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cell division
  • cellular metabolic process
  • cellular process
  • cytokinesis
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 48 General Function Involved in protein serine/threonine kinase activity
Enzyme 48 Specific Function Regulates the assembly of the actin cytoskeleton. Promotes formation of stress fibers and of focal adhesion complexes. Plays a role in smooth muscle contraction
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 41872583 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID O75116 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name ROCK2_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >4167 bp
ATGAGCCGGCCCCCGCCGACGGGGAAAATGCCCGGCGCCCCCGAGACCGCGCCGGGGGAC
GGGGCAGGCGCGAGCCGCCAGAGGAAGCTGGAGGCGCTGATCCGAGACCCTCGCTCCCCC
ATCAACGTGGAGAGCTTGCTGGATGGCTTAAATTCCTTGGTCCTTGATTTAGATTTTCCT
GCTTTGAGGAAAAACAAGAACATAGATAATTTCTTAAATAGATATGAGAAAATTGTGAAA
AAAATCAGAGGTCTACAGATGAAGGCAGAAGACTATGATGTTGTAAAAGTTATTGGAAGA
GGTGCTTTTGGTGAAGTGCAGTTGGTTCGTCACAAGGCATCGCAGAAGGTTTATGCTATG
AAGCTTCTTAGTAAGTTTGAAATGATAAAAAGATCAGATTCTGCCTTTTTTTGGGAAGAA
AGAGATATTATGGCCTTTGCCAATAGCCCCTGGGTGGTTCAGCTTTTTTATGCCTTTCAA
GATGATAGGTATCTGTACATGGTAATGGAGTACATGCCTGGTGGAGACCTTGTAAACCTT
ATGAGTAATTATGATGTGCCTGAAAAATGGGCCAAATTTTACACTGCTGAAGTTGTTCTT
GCTCTGGATGCAATACACTCCATGGGTTTAATACACAGAGATGTGAAGCCTGACAACATG
CTCTTGGATAAACATGGACATCTAAAATTAGCAGATTTTGGCACGTGTATGAAGATGGAT
GAAACAGGCATGGTACATTGTGATACAGCAGTTGGAACACCGGATTATATATCACCTGAG
GTTCTGAAATCACAAGGGGGTGATGGTTTCTATGGGCGAGAATGTGATTGGTGGTCTGTA
GGTGTTTTCCTTTATGAGATGCTAGTGGGGGATACTCCATTTTATGCGGATTCACTTGTA
GGAACATATAGCAAAATTATGGATCATAAGAATTCACTGTGTTTCCCTGAAGATGCAGAA
ATTTCCAAACATGCAAAGAATCTCATCTGTGCTTTCTTAACAGATAGGGAGGTACGACTT
GGGAGAAATGGGGTGGAAGAAATCAGACAGCATCCTTTCTTTAAGAATGATCAGTGGCAT
TGGGATAACATAAGAGAAACGGCAGCTCCTGTAGTACCTGAACTCAGCAGTGACATAGAC
AGCAGCAATTTCGATGACATTGAAGATGACAAAGGAGATGTAGAAACCTTCCCAATTCCT
AAAGCTTTTGTTGGAAATCAGCTGCCTTTCATCGGATTTACCTACTATAGAGAAAATTTA
TTATTAAGTGACTCTCCATCTTGTAGAGAAACTGATTCCATACAATCAAGGAAAAATGAA
GAAAGTCAAGAGATTCAGAAAAAACTGTATACATTAGAAGAACATCTTAGCAATGAGATG
CAAGCCAAAGAGGAACTGGAACAGAAGTGCAAATCTGTTAATACTCGCCTAGAAAAAACA
GCAAAGGAGCTAGAAGAGGAGATTACCTTACGGAAAAGTGTGGAATCAGCATTAAGACAG
TTAGAAAGAGAAAAGGCGCTTCTTCAGCACAAAAATGCAGAATATCAGAGGAAAGCTGAT
CATGAAGCAGACAAAAAACGAAATTTGGAAAATGATGTTAACAGCTTAAAAGATCAACTT
GAAGATTTGAAAAAAAGAAATCAAAACTCTCAAATATCCACTGAGAAAGTGAATCAACTC
CAGAGACAACTGGATGAAACCAATGCTTTACTGCGAACAGAGTCTGATACTGCAGCCCGG
TTAAGGAAAACCCAGGCAGAAAGTTCAAAACAGATTCAGCAGCTGGAATCTAACAATAGA
GATCTACAAGATAAAAACTGCCTGCTGGAGACTGCCAAGTTAAAACTTGAAAAGGAATTT
ATCAATCTTCAGTCAGCTCTAGAATCTGAAAGGAGGGATCGAACCCATGGATCAGAGATA
ATTAATGATTTACAAGGTAGAATATGTGGCCTAGAAGAAGATTTAAAGAACGGCAAAATC
TTACTAGCGAAAGTAGAACTGGAGAAGAGACAACTTCAGGAGAGATTTACTGATTTGGAA
AAGGAAAAAAGCAACATGGAAATAGATATGACATACCAACTAAAAGTTATACAGCAGAGC
CTAGAACAAGAAGAAGCTGAACATAAGGCCACAAAGGCACGACTAGCAGATAAAAATAAG
ATCTATGAGTCCATCGAAGAAGCCAAATCAGAAGCCATGAAAGAAATGGAGAAGAAGCTC
TTGGAGGAAAGAACTTTAAAACAGAAAGTGGAGAACCTATTGCTAGAAGCTGAGAAAAGA
TGTTCTCTATTAGACTGTGACCTCAAACAGTCACAGCAGAAAATAAATGAGCTCCTTAAA
CAGAAAGATGTGCTAAATGAGGATGTTAGAAACCTGACATTAAAAATAGAGCAAGAAACT
CAGAAGCGCTGCCTTACACAAAATGACCTGAAGATGCAAACACAACAGGTTAACACACTA
AAAATGTCAGAAAAGCAGTTAAAGCAAGAAAATAACCATCTCATGGAAATGAAAATGAAC
TTGGAAAAACAAAATGCTGAACTTCGAAAAGAACGTCAGGATGCAGATGGGCAAATGAAA
GAGCTCCAGGATCAGCTCGAAGCAGAACAGTATTTCTCAACCCTTTATAAAACACAAGTT
AGGGAGCTTAAAGAAGAATGTGAAGAAAAGACCAAACTTGGTAAAGAATTGCAGCAGAAG
AAACAGGAATTACAGGATGAACGGGACTCTTTGGCTGCCCAACTGGAGATCACCTTGACC
AAAGCAGATTCTGAGCAACTGGCTCGTTCAATTGCTGAAGAACAATATTCTGATTTGGAA
AAAGAGAAGATCATGAAAGAGCTGGAGATCAAAGAGATGATGGCTAGACACAAACAGGAA
CTTACGGAAAAAGATGCTACAATTGCTTCTCTTGAGGAAACTAATAGGACACTAACTAGT
GATGTTGCCAATCTTGCAAATGAGAAAGAAGAATTAAATAACAAATTGAAAGATGTTCAA
GAGCAACTGTCAAGATTGAAAGATGAAGAAATAAGCGCAGCAGCTATTAAAGCACAGTTT
GAGAAGCAGCTATTAACAGAAAGAACACTCAAAACTCAAGCTGTGAATAAGTTGGCTGAG
ATCATGAATCGAAAAGAACCTGTCAAGCGTGGTAATGACACAGATGTGCGGAGAAAAGAG
AAGGAGAATAGAAAGCTACATATGGAGCTTAAATCTGAACGTGAGAAATTGACCCAGCAG
ATGATCAAGTATCAGAAAGAACTGAATGAAATGCAGGCACAAATAGCTGAAGAGAGCCAG
ATTCGAATTGAACTGCAGATGACATTGGACAGTAAAGACAGTGACATTGAGCAGCTGCGG
TCACAACTCCAAGCCTTGCATATTGGTCTGGATAGTTCCAGTATAGGCAGTGGACCAGGG
GATGCTGAGGCAGATGATGGGTTTCCAGAATCAAGATTAGAAGGATGGCTTTCATTGCCT
GTACGAAACAACACTAAGAAATTTGGATGGGTTAAAAAGTATGTGATTGTAAGCAGTAAG
AAGATTCTTTTCTATGACAGTGAACAAGATAAAGAACAATCCAATCCTTACATGGTTTTA
GATATAGACAAGTTATTTCATGTCCGACCAGTTACACAGACAGATGTGTATAGAGCAGAT
GCTAAAGAAATTCCAAGGATATTCCAGATTCTGTATGCCAATGAAGGAGAAAGTAAGAAG
GAACAAGAATTTCCAGTGGAGCCAGTTGGAGAAAAATCTAATTATATTTGCCACAAGGGA
CATGAGTTTATTCCTACTCTTTATCATTTCCCAACCAACTGTGAGGCTTGTATGAAGCCC
CTGTGGCACATGTTTAAGCCTCCTCCTGCTTTGGAGTGCCGCCGTTGCCATATTAAGTGT
CATAAAGATCATATGGACAAAAAGGAGGAGATTATAGCACCTTGCAAAGTATATTATGAT
ATTTCAACGGCAAAGAATCTGTTATTACTAGCAAATTCTACAGAAGAGCAGCAGAAGTGG
GTTAGTCGGTTGGTGAAAAAGATACCTAAAAAGCCCCCAGCTCCAGACCCTTTTGCCCGA
TCATCTCCTAGAACTTCAATGAAGATACAGCAAAACCAGTCTATTAGACGGCCAAGTCGA
CAGCTTGCCCCAAACAAACCTAGCTAA
Enzyme 48 GenBank Gene ID NM_004850.3 Link Image
Enzyme 48 GeneCard ID ROCK2 Link Image
Enzyme 48 GenAtlas ID ROCK2 Link Image
Enzyme 48 HGNC ID HGNC:10252 Link Image
Enzyme 48 Chromosome Location 2
Enzyme 48 Locus 2p24
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Takahashi N, Tuiki H, Saya H, Kaibuchi K: Localization of the gene coding for ROCK II/Rho kinase on human chromosome 2p24. Genomics. 1999 Jan 15;55(2):235-7. [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. 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]
  4. 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]
  5. 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]
  6. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  7. 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]
  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. 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]
  10. 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]
  11. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 7218
Enzyme 49 Name Protein kinase C delta type
Enzyme 49 Synonyms
  1. nPKC-delta
Enzyme 49 Gene Name PRKCD
Enzyme 49 Protein Sequence >Protein kinase C delta type
MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFD
AHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQY
FLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVW
GLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMS
PTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASR
RSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSF
GKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTK
DHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVL
LDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYE
MLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIH
PFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAF
AGFSFVNPKFEHLLED
Enzyme 49 Number of Residues 676
Enzyme 49 Molecular Weight 77504.4
Enzyme 49 Theoretical pI 7.81
Enzyme 49 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase C activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 49 General Function Involved in protein serine/threonine kinase activity
Enzyme 49 Specific Function This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May play a role in antigen-dependent control of B-cell function. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • None
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 189053779 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q05655 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name KPCD_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >2031 bp
ATGGCGCCGTTCCTGCGCATCGCCTTCAACTCCTATGAGCTGGGCTCCCTGCAGGCCGAG
GACGAGGCGAACCAGCCCTTCTGTGCCGTGAAGATGAAGGAGGCGCTCAGCACAGAGCGT
GGGAAAACACTGGTGCAGAAGAAGCCGACCATGTATCCTGAGTGGAAGTCGACGTTCGAT
GCCCACATCTATGAGGGGCGCGTCATCCAGATTGTGCTAATGCGGGCAGCAGAGGAGCCA
GTGTCTGAGGTGACCGTGGGTGTGTCGGTGCTGGCCGAGCGCTGCAAGAAGAACAATGGC
AAGGCTGAGTTCTGGCTGGACCTGCAGCCTCAGGCCAAGGTGTTGATGTCTGTTCAGTAT
TTCCTGGAGGACGTGGATTGCAAACAGTCTATGCGCAGTGAGGACGAGGCCAAGTTCCCA
ACGATGAACCGCCGCGGAGCCATCAAACAGGCCAAAATCCACTACATCAAGAACCATGAG
TTTATCGCCACCTTCTTTGGGCAACCCACCTTCTGTTCTGTGTGCAAAGACTTTGTCTGG
GGCCTCAACAAGCAAGGCTACAAATGCAGGCAATGTAACGCTGCCATCCACAAGAAATGC
ATCGACAAGATCATCGGCAGATGCACTGGCACCGCGGCCAACAGCCGGGACACTATATTC
CAGAAAGAACGCTTCAACATCGACATGCCGCACCGCTTCAAGGTTCACAACTACATGAGC
CCCACCTTTTGTGACCACTGCGGCAGCCTGCTCTGGGGACTGGTGAAGCAGGGATTAAAG
TGTGAAGACTGCGGCATGAATGTGCACCATAAATGCCGGGAGAAGGTGGCCAACCTCTGC
GGCATCAACCAGAAGCTTTTGGCTGAGGCCTTGAACCAAGTCACCCAGAGAGCCTCCCGG
AGATCAGACTCAGCCTCCTCAGAGCCTGTTGGGATATATCAGGGTTTCGAGAAGAAGACC
GGAGTTGCTGGGGAGGACATGCAAGACAACAGTGGGACCTACGGCAAGATCTGGGAGGGC
AGCAGCAAGTGCAACATCAACAACTTCATCTTCCACAAGGTCCTGGGCAAAGGCAGCTTC
GGGAAGGTGCTGCTTGGAGAGCTGAAGGGCAGAGGAGAGTACTTTGCCATCAAGGCCCTC
AAGAAGGATGTGGTCCTGATCGACGACGACGTGGAGTGCACCATGGTTGAGAAGCGGGTG
CTGACACTTGCCGCAGAGAATCCCTTTCTCACCCACCTCATCTGCACCTTCCAGACCAAG
GACCACCTGTTCTTTGTGATGGAGTTCCTCAACGGGGGGGACCTGATGTACCACATCCAG
GACAAAGGCCGCTTTGAACTCTACCGTGCCACGTTTTATGCCGCTGAGATAATGTGTGGA
CTGCAGTTTCTACACAGCAAGGGCATCATTTACAGGGACCTCAAACTGGACAATGTGCTG
TTGGACCGGGATGGCCACATCAAGATTGCCGACTTTGGGATGTGCAAAGAGAACATATTC
GGGGAGAGCCGGGCCAGCACCTTCTGCGGCACCCCTGACTATATCGCCCCTGAGATCCTA
CAGGGCCTGAGGTACACATTCTCTGTGGACTGGTGGTCTTTCGGGGTCCTTCTGTACGAG
ATGCTCATTGGCCAGTCCCCCTTCCATGGTGATGATGAGGATGAACTCTTCGAGTCCATC
CGTGTGGACACGCCACATTATCCCCGCTGGATCACCAAGGAGTCCAAGGACATCCTGGAG
AAGCTCTTTGAAAGGGAACCAACCAAGAGGCTGGGAGTGACGGGAAACATCAAAATCCAC
CCCTTCTTCAAGACCATAAACTGGACTCTGCTGGAAAAGCGGAGGTTGGAGCCACCCTTC
AGGCCCAAAGTGAAGTCACCCAGAGACTACAGTAACTTTGACCAGGAGTTCCTGAACGAG
AAGGCGCGCCTCTCCTACAGCGACAAGAACCTCATCGACTCCATGGACCAGTCTGCATTC
GCTGGCTTCTCCTTTGTGAACCCCAAATTCGAGCACCTCCTGGAAGATTGA
Enzyme 49 GenBank Gene ID AK313216 Link Image
Enzyme 49 GeneCard ID PRKCD Link Image
Enzyme 49 GenAtlas ID PRKCD Link Image
Enzyme 49 HGNC ID HGNC:9399 Link Image
Enzyme 49 Chromosome Location 3
Enzyme 49 Locus 3p21.31
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Aris JP, Basta PV, Holmes WD, Ballas LM, Moomaw C, Rankl NB, Blobel G, Loomis CR, Burns DJ: Molecular and biochemical characterization of a recombinant human PKC-delta family member. Biochim Biophys Acta. 1993 Aug 19;1174(2):171-81. [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. Nomoto S, Watanabe Y, Ninomiya-Tsuji J, Yang LX, Nagai Y, Kiuchi K, Hagiwara M, Hidaka H, Matsumoto K, Irie K: Functional analyses of mammalian protein kinase C isozymes in budding yeast and mammalian fibroblasts. Genes Cells. 1997 Oct;2(10):601-14. [PubMed Link Image]
  5. Palmer RH, Ridden J, Parker PJ: Identification of multiple, novel, protein kinase C-related gene products. FEBS Lett. 1994 Dec 12;356(1):5-8. [PubMed Link Image]
  6. Ren J, Li Y, Kufe D: Protein kinase C delta regulates function of the DF3/MUC1 carcinoma antigen in beta-catenin signaling. J Biol Chem. 2002 May 17;277(20):17616-22. Epub 2002 Mar 4. [PubMed Link Image]
  7. Yoshida K, Wang HG, Miki Y, Kufe D: Protein kinase Cdelta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9. EMBO J. 2003 Mar 17;22(6):1431-41. [PubMed Link Image]
  8. 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]
  9. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  10. 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]
  11. 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]
  12. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  13. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  14. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  15. 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]
  16. 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]
  17. 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]
  18. Benes CH, Wu N, Elia AE, Dharia T, Cantley LC, Soltoff SP: The C2 domain of PKCdelta is a phosphotyrosine binding domain. Cell. 2005 Apr 22;121(2):271-80. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 7219
Enzyme 50 Name Serine/threonine-protein kinase D3
Enzyme 50 Synonyms
  1. Protein kinase C nu type
  2. Protein kinase EPK2
  3. nPKC-nu
Enzyme 50 Gene Name PRKD3
Enzyme 50 Protein Sequence >Serine/threonine-protein kinase D3
MSANNSPPSAQKSVLPTAIPAVLPAASPCSSPKTGLSARLSNGSFSAPSLTNSRGSVHTV
SFLLQIGLTRESVTIEAQELSLSAVKDLVCSIVYQKFPECGFFGMYDKILLFRHDMNSEN
ILQLITSADEIHEGDLVEVVLSALATVEDFQIRPHTLYVHSYKAPTFCDYCGEMLWGLVR
QGLKCEGCGLNYHKRCAFKIPNNCSGVRKRRLSNVSLPGPGLSVPRPLQPEYVALPSEES
HVHQEPSKRIPSWSGRPIWMEKMVMCRVKVPHTFAVHSYTRPTICQYCKRLLKGLFRQGM
QCKDCKFNCHKRCASKVPRDCLGEVTFNGEPSSLGTDTDIPMDIDNNDINSDSSRGLDDT
EEPSPPEDKMFFLDPSDLDVERDEEAVKTISPSTSNNIPLMRVVQSIKHTKRKSSTMVKE
GWMVHYTSRDNLRKRHYWRLDSKCLTLFQNESGSKYYKEIPLSEILRISSPRDFTNISQG
SNPHCFEIITDTMVYFVGENNGDSSHNPVLAATGVGLDVAQSWEKAIRQALMPVTPQASV
CTSPGQGKDHKDLSTSISVSNCQIQENVDISTVYQIFADEVLGSGQFGIVYGGKHRKTGR
DVAIKVIDKMRFPTKQESQLRNEVAILQNLHHPGIVNLECMFETPERVFVVMEKLHGDML
EMILSSEKSRLPERITKFMVTQILVALRNLHFKNIVHCDLKPENVLLASAEPFPQVKLCD
FGFARIIGEKSFRRSVVGTPAYLAPEVLRSKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE
DINDQIQNAAFMYPPNPWREISGEAIDLINNLLQVKMRKRYSVDKSLSHPWLQDYQTWLD
LREFETRIGERYITHESDDARWEIHAYTHNLVYPKHFIMAPNPDDMEEDP
Enzyme 50 Number of Residues 890
Enzyme 50 Molecular Weight 100469.8
Enzyme 50 Theoretical pI 6.87
Enzyme 50 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase C activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 50 General Function Involved in intracellular signaling pathway
Enzyme 50 Specific Function Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 4115769 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID O94806 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name KPCD3_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >2673 bp
ATGTCTGCAAATAATTCCCCTCCATCAGCCCAGAAGTCTGTATTACCCACAGCTATTCCT
GCTGTGCTTCCAGCTGCTTCTCCGTGTTCAAGTCCTAAGACGGGACTCTCTGCCCGACTC
TCTAATGGAAGCTTCAGTGCACCATCACTCACCAACTCCAGAGGCTCAGTGCATACAGTT
TCATTTCTACTGCAAATTGGCCTCACACGGGAGAGTGTTACCATTGAAGCCCAGGAACTG
TCTTTATCTGCTGTCAAGGATCTTGTGTGCTCCATAGTTTATCAAAAGTTTCCAGAGTGT
GGATTCTTTGGCATGTATGACAAAATTCTTCTCTTTCGCCATGACATGAACTCAGAAAAC
ATTTTGCAGCTGATTACCTCAGCAGATGAAATACATGAAGGAGACCTAGTGGAAGTGGTT
CTTTCAGCTTTAGCCACAGTAGAAGACTTCCAGATTCGTCCACATACTCTCTATGTACAT
TCTTACAAAGCTCCTACTTTCTGTGATTACTGTGGTGAGATGCTGTGGGGATTGGTACGT
CAAGGACTGAAATGTGAAGGCTGTGGATTAAATTACCATAAACGATGTGCCTTCAAGATT
CCAAATAACTGTAGTGGAGTAAGAAAGAGACGTCTGTCAAATGTATCTTTACCAGGACCC
GGCCTCTCAGTTCCAAGACCCCTACAGCCTGAATATGTAGCCCTTCCCAGTGAAGAGTCA
CATGTCCACCAGGAACCAAGTAAGAGAATTCCTTCTTGGAGTGGTCGCCCAATCTGGATG
GAAAAGATGGTAATGTGCAGAGTGAAAGTTCCACACACATTTGCTGTTCACTCTTACACC
CGTCCCACGATATGTCAGTACTGCAAGCGGTTACTGAAAGGCCTCTTTCGCCAAGGAATG
CAGTGTAAAGATTGCAAATTCAACTGCCATAAACGCTGTGCATCAAAAGTACCAAGAGAC
TGCCTTGGAGAGGTTACTTTCAATGGAGAACCTTCCAGTCTGGGAACAGATACAGATATA
CCAATGGATATTGACAATAATGACATAAATAGTGATAGTAGTCGGGGTTTGGATGACACA
GAAGAGCCATCACCCCCAGAAGATAAGATGTTCTTCTTGGATCCATCTGATCTCGATGTG
GAAAGAGATGAAGAAGCCGTTAAAACAATCAGTCCATCAACAAGCAATAATATTCCGCTA
ATGAGGGTTGTACAATCCATCAAGCACACAAAGAGGAAGAGCAGCACAATGGTGAAGGAA
GGGTGGATGGTCCATTACACCAGCAGGGATAACCTGAGAAAGAGGCATTATTGGAGACTT
GACAGCAAATGTCTAACATTATTTCAGAATGAATCTGGATCAAAGTATTATAAGGAAATT
CCACTTTCAGAAATTCTCCGCATATCTTCACCACGAGATTTCACAAACATTTCACAAGGC
AGCAATCCACACTGTTTTGAAATCATTACTGATACTATGGTATACTTCGTTGGTGAGAAC
AATGGGGACAGCTCTCATAATCCTGTTCTTGCTGCCACTGGAGTTGGACTTGATGTAGCA
CAGAGCTGGGAAAAAGCAATTCGCCAAGCCCTCATGCCTGTTACTCCTCAAGCAAGTGTT
TGCACTTCTCCAGGGCAAGGGAAAGATCACAAAGATTTGTCTACAAGTATCTCTGTATCT
AATTGTCAGATTCAGGAGAATGTGGATATCAGTACTGTTTACCAGATCTTTGCAGATGAG
GTGCTTGGTTCAGGCCAGTTTGGCATCGTTTATGGAGGAAAACATAGAAAGACTGGGAGG
GATGTGGCTATTAAAGTAATTGATAAGATGAGATTCCCCACAAAACAAGAAAGTCAACTC
CGTAATGAAGTGGCTATTTTACAGAATTTGCACCATCCTGGGATTGTAAACCTGGAATGT
ATGTTTGAAACCCCAGAACGAGTCTTTGTAGTAATGGAAAAGCTGCATGGAGATATGTTG
GAAATGATTCTATCCAGTGAGAAAAGTCGGCTTCCAGAACGAATTACTAAATTCATGGTC
ACACAGATACTTGTTGCTTTGAGGAATCTGCATTTTAAGAATATTGTGCACTGTGATTTA
AAGCCAGAAAATGTGCTGCTTGCATCAGCAGAGCCATTTCCTCAGGTGAAGCTGTGTGAC
TTTGGATTTGCACGCATCATTGGTGAAAAGTCATTCAGGAGATCTGTGGTAGGAACTCCA
GCATACTTAGCCCCTGAAGTTCTCCGGAGCAAAGGTTACAACCGTTCCCTAGATATGTGG
TCAGTGGGAGTTATCATCTATGTGAGCCTCAGTGGCACATTTCCTTTTAATGAGGATGAA
GATATAAATGACCAAATCCAAAATGCTGCATTTATGTACCCACCAAATCCATGGAGAGAA
ATTTCTGGTGAAGCAATTGATCTGATAAACAATCTGCTTCAAGTGAAGATGAGAAAACGT
TACAGTGTTGACAAATCTCTTAGTCATCCCTGGCTACAGGACTATCAGACTTGGCTTGAC
CTTAGAGAATTTGAAACTCGCATTGGAGAACGTTACATTACACATGAAAGTGATGATGCT
CGCTGGGAAATACATGCATACACACATAACCTTGTATACCCAAAGCACTTCATTATGGCT
CCTAATCCAGATGATATGGAAGAAGATCCTTAA
Enzyme 50 GenBank Gene ID AB015982 Link Image
Enzyme 50 GeneCard ID PRKD3 Link Image
Enzyme 50 GenAtlas ID PRKD3 Link Image
Enzyme 50 HGNC ID HGNC:9408 Link Image
Enzyme 50 Chromosome Location 2
Enzyme 50 Locus 2p21
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References
  1. Hayashi A, Seki N, Hattori A, Kozuma S, Saito T: PKCnu, a new member of the protein kinase C family, composes a fourth subfamily with PKCmu. Biochim Biophys Acta. 1999 May 6;1450(1):99-106. [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. 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. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  6. Chen J, Deng F, Li J, Wang QJ: Selective binding of phorbol esters and diacylglycerol by individual C1 domains of the PKD family. Biochem J. 2008 Apr 15;411(2):333-42. [PubMed Link Image]
  7. 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]
  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. 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]
  10. 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]
  11. 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]
  12. 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]
  13. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 7220
Enzyme 51 Name Protein kinase C theta type
Enzyme 51 Synonyms
  1. nPKC-theta
Enzyme 51 Gene Name PRKCQ
Enzyme 51 Protein Sequence >Protein kinase C theta type
MSPFLRIGLSNFDCGSCQSCQGEAVNPYCAVLVKEYVESENGQMYIQKKPTMYPPWDSTF
DAHINKGRVMQIIVKGKNVDLISETTVELYSLAERCRKNNGKTEIWLELKPQGRMLMNAR
YFLEMSDTKDMNEFETEGFFALHQRRGAIKQAKVHHVKCHEFTATFFPQPTFCSVCHEFV
WGLNKQGYQCRQCNAAIHKKCIDKVIAKCTGSAINSRETMFHKERFKIDMPHRFKVYNYK
SPTFCEHCGTLLWGLARQGLKCDACGMNVHHRCQTKVANLCGINQKLMAEALAMIESTQQ
ARCLRDTEQIFREGPVEIGLPCSIKNEARPPCLPTPGKREPQGISWESPLDEVDKMCHLP
EPELNKERPSLQIKLKIEDFILHKMLGKGSFGKVFLAEFKKTNQFFAIKALKKDVVLMDD
DVECTMVEKRVLSLAWEHPFLTHMFCTFQTKENLFFVMEYLNGGDLMYHIQSCHKFDLSR
ATFYAAEIILGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKTNTFC
GTPDYIAPEILLGQKYNHSVDWWSFGVLLYEMLIGQSPFHGQDEEELFHSIRMDNPFYPR
WLEKEAKDLLVKLFVREPEKRLGVRGDIRQHPLFREINWEELERKEIDPPFRPKVKSPFD
CSNFDKEFLNEKPRLSFADRALINSMDQNMFRNFSFMNPGMERLIS
Enzyme 51 Number of Residues 706
Enzyme 51 Molecular Weight 81864.1
Enzyme 51 Theoretical pI 7.64
Enzyme 51 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase C activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 51 General Function Involved in protein serine/threonine kinase activity
Enzyme 51 Specific Function PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • None
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 55957459 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID Q04759 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name KPCT_HUMAN Link Image
Enzyme 51 PDB ID 1XJD Link Image
Enzyme 51 PDB File Show
Enzyme 51 3D Structure
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >2121 bp
ATGTCGCCATTTCTTCGGATTGGCTTGTCCAACTTTGACTGCGGGTCCTGCCAGTCTTGT
CAGGGCGAGGCTGTTAACCCTTACTGTGCTGTGCTCGTCAAAGAGTATGTCGAATCAGAG
AACGGGCAGATGTATATCCAGAAAAAGCCTACCATGTACCCACCCTGGGACAGCACTTTT
GATGCCCATATCAACAAGGGAAGAGTCATGCAGATCATTGTGAAAGGCAAAAACGTGGAC
CTCATCTCTGAAACCACCGTGGAGCTCTACTCGCTGGCTGAGAGGTGCAGGAAGAACAAC
GGGAAGACAGAAATATGGTTAGAGCTGAAACCTCAAGGCCGAATGCTAATGAATGCAAGA
TACTTTCTGGAAATGAGTGACACAAAGGACATGAATGAATTTGAGACGGAAGGCTTCTTT
GCTTTGCATCAGCGCCGGGGTGCCATCAAGCAGGCAAAGGTCCACCACGTCAAGTGCCAC
GAGTTCACTGCCACCTTCTTCCCACAGCCCACATTTTGCTCTGTCTGCCACGAGTTTGTC
TGGGGCCTGAACAAACAGGGCTACCAGTGCCGACAATGCAATGCAGCAATTCACAAGAAG
TGTATTGATAAAGTTATAGCAAAGTGCACAGGATCAGCTATCAATAGCCGAGAAACCATG
TTCCACAAGGAGAGATTCAAAATTGACATGCCACACAGATTTAAAGTCTACAATTACAAG
AGCCCGACCTTCTGTGAACACTGTGGGACCCTGCTGTGGGGACTGGCACGGCAAGGACTC
AAGTGTGATGCATGTGGCATGAATGTGCATCATAGATGCCAGACAAAGGTGGCCAACCTT
TGTGGCATAAACCAGAAGCTAATGGCTGAAGCGCTGGCCATGATTGAGAGCACTCAACAG
GCTCGCTGCTTAAGAGATACTGAACAGATCTTCAGAGAAGGTCCGGTTGAAATTGGTCTC
CCATGCTCCATCAAAAATGAAGCAAGGCCGCCATGTTTACCGACACCGGGAAAAAGAGAG
CCTCAGGGCATTTCCTGGGAGTCTCCGTTGGATGAGGTGGATAAAATGTGCCATCTTCCA
GAACCTGAACTGAACAAAGAAAGACCATCTCTGCAGATTAAACTAAAAATTGAGGATTTT
ATCTTGCACAAAATGTTGGGGAAAGGAAGTTTTGGCAAGGTCTTCCTGGCAGAATTCAAG
AAAACCAATCAATTTTTCGCAATAAAGGCCTTAAAGAAAGATGTGGTCTTGATGGACGAT
GATGTTGAGTGCACGATGGTAGAGAAGAGAGTTCTTTCCTTGGCCTGGGAGCATCCGTTT
CTGACGCACATGTTTTGTACATTCCAGACCAAGGAAAACCTCTTTTTTGTGATGGAGTAC
CTCAACGGAGGGGACTTAATGTACCACATCCAAAGCTGCCACAAGTTCGACCTTTCCAGA
GCGACGTTTTATGCTGCTGAAATCATTCTTGGTCTGCAGTTCCTTCATTCCAAAGGAATA
GTCTACAGGGACCTGAAGCTAGATAACATCCTGTTAGACAAAGATGGACATATCAAGATC
GCGGATTTTGGAATGTGCAAGGAGAACATGTTAGGAGATGCCAAGACGAATACCTTCTGT
GGGACACCTGACTACATCGCCCCAGAGATCTTGCTGGGTCAGAAATACAACCACTCTGTG
GACTGGTGGTCCTTCGGGGTTCTCCTTTATGAAATGCTGATTGGTCAGTCGCCTTTCCAC
GGGCAGGATGAGGAGGAGCTCTTCCACTCCATCCGCATGGACAATCCCTTTTACCCACGG
TGGCTGGAGAAGGAAGCAAAGGACCTTCTGGTGAAGCTCTTCGTGCGAGAACCTGAGAAG
AGGCTGGGCGTGAGGGGAGACATCCGCCAGCACCCTTTGTTTCGGGAGATCAACTGGGAG
GAACTTGAACGGAAGGAGATTGACCCACCGTTCCGGCCGAAAGTGAAATCACCATTTGAC
TGCAGCAATTTCGACAAAGAATTCTTAAACGAGAAGCCCCGGCTGTCATTTGCCGACAGA
GCACTGATCAACAGCATGGACCAGAATATGTTCAGGAACTTTTCCTTCATGAACCCCGGG
ATGGAGCGGCTGATATCCTGA
Enzyme 51 GenBank Gene ID AL137145 Link Image
Enzyme 51 GeneCard ID PRKCQ Link Image
Enzyme 51 GenAtlas ID PRKCQ Link Image
Enzyme 51 HGNC ID HGNC:9410 Link Image
Enzyme 51 Chromosome Location 1
Enzyme 51 Locus 10p15
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 General References
  1. Chang JD, Xu Y, Raychowdhury MK, Ware JA: Molecular cloning and expression of a cDNA encoding a novel isoenzyme of protein kinase C (nPKC). A new member of the nPKC family expressed in skeletal muscle, megakaryoblastic cells, and platelets. J Biol Chem. 1993 Jul 5;268(19):14208-14. [PubMed Link Image]
  2. Zhang K, Max EE, Cheah HK, Saxon A: Complex alternative RNA splicing of epsilon-immunoglobulin transcripts produces mRNAs encoding four potential secreted protein isoforms. J Biol Chem. 1994 Dec 9;269(49):31322. [PubMed Link Image]
  3. Baier G, Telford D, Giampa L, Coggeshall KM, Baier-Bitterlich G, Isakov N, Altman A: Molecular cloning and characterization of PKC theta, a novel member of the protein kinase C (PKC) gene family expressed predominantly in hematopoietic cells. J Biol Chem. 1993 Mar 5;268(7):4997-5004. [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. Witte S, Villalba M, Bi K, Liu Y, Isakov N, Altman A: Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain. J Biol Chem. 2000 Jan 21;275(3):1902-9. [PubMed Link Image]
  7. Thuille N, Heit I, Fresser F, Krumbock N, Bauer B, Leuthaeusser S, Dammeier S, Graham C, Copeland TD, Shaw S, Baier G: Critical role of novel Thr-219 autophosphorylation for the cellular function of PKCtheta in T lymphocytes. EMBO J. 2005 Nov 16;24(22):3869-80. Epub 2005 Oct 27. [PubMed Link Image]
  8. Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed Link Image]
  9. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  10. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  11. 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]
  12. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 7221
Enzyme 52 Name Protein kinase C eta type
Enzyme 52 Synonyms
  1. PKC-L
  2. nPKC-eta
Enzyme 52 Gene Name PRKCH
Enzyme 52 Protein Sequence >Protein kinase C eta type
MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTK
QKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTTGASDTFEG
WVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLR
QPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDSKIAEQRF
GINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAV
ELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNGIGVNSSNRLGIDNFEFIRV
LGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLF
CCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHDKGIIYRDL
KLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAM
GVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSL
TQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDE
GHLPMINQDEFRNFSYVSPELQP
Enzyme 52 Number of Residues 683
Enzyme 52 Molecular Weight 77828.0
Enzyme 52 Theoretical pI 7.80
Enzyme 52 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase C activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 52 General Function Involved in protein serine/threonine kinase activity
Enzyme 52 Specific Function PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 158261389 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID P24723 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name KPCL_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >2052 bp
ATGTCGTCTGGCACCATGAAGTTCAATGGCTATTTGAGGGTCCGCATCGGTGAGGCAGTG
GGGCTGCAGCCCACCCGCTGGTCCCTGCGCCACTCGCTCTTCAAGAAGGGCCACCAGCTG
CTGGACCCCTATCTGACGGTGAGCGTGGACCAGGTGCGCGTGGGCCAGACCAGCACCAAG
CAGAAGACCAACAAACCCACGTACAACGAGGAGTTTTGCGCTAACGTCACCGACGGCGGC
CACCTCGAGTTGGCCGTCTTCCACGAGACGCCCCTGGGCTACGACCACTTCGTGGCCAAC
TGCACCCTGCAGTTCCAGGAGCTGCTGCGCACGACCGGCGCCTCGGACACCTTCGAGGGT
TGGGTGGATCTCGAGCCAGAGGGGAAAGTATTTGTGGTAATAACCCTTACCGGGAGTTTC
ACTGAAGCTACTCTCCAGAGAGACCGGATCTTCAAACATTTTACCAGGAAGCGCCAAAGG
GCTATGCGAAGGCGAGTCCACCAGATCAATGGACACAAGTTCATGGCCACGTATCTGAGG
CAGCCCACCTACTGCTCTCACTGCAGGGAGTTTATCTGGGGAGTGTTTGGGAAACAGGGT
TATCAGTGCCAAGTGTGCACCTGTGTCGTCCATAAACGCTGCCATCATCTAATTGTTACA
GCCTGTACTTGCCAAAACAATATTAACAAAGTGGATTCAAAGATTGCAGAACAGAGGTTC
GGGATCAACATCCCACACAAGTTCAGCATCCACAACTACAAAGTGCCAACATTCTGCGAT
CACTGTGGCTCACTGCTCTGGGGAATAATGCGACAAGGACTTCAGTGTAAAATATGTAAA
ATGAATGTGCATATTCGATGTCAAGCGAACGTGGCCCCTAACTGTGGGGTAAATGCGGTG
GAACTTGCCAAGACCCTGGCAGGGATGGGTCTCCAACCCGGAAATATTTCTCCAACCTCG
AAACTCGTTTCCAGATCGACCCTAAGACGACAGGGAAAGGAGAGCAGCAAAGAAGGAAAT
GGGATTGGGGTTAATTCTTCCAACCGACTTGGTATCGACAACTTTGAGTTCATCCGAGTG
TTGGGGAAGGGGAGTTTTGGGAAGGTGATGCTTGCAAGAGTAAAAGAAACAGGAGACCTC
TATGCTGTGAAGGTGCTGAAGAAGGACGTGATTCTGCAGGATGATGATGTGGAATGCACC
ATGACCGAGAAAAGGATCCTGTCTCTGGCCCGCAATCACCCCTTCCTCACTCAGTTGTTC
TGCTGCTTTCAGACCCCCGATCGTCTGTTTTTTGTGATGGAGTTTGTGAATGGGGGTGAC
TTGATGTTCCACATTCAGAAGTCTCGTCGTTTTGATGAAGCACGAGCTCGCTTCTATGCT
GCAGAAATCATTTCGGCTCTCATGTTCCTCCATGATAAAGGAATCATCTATAGAGATCTG
AAACTGGACAATGTCCTGTTGGACCACGAGGGTCACTGTAAACTGGCAGACTTCGGAATG
TGCAAGGAGGGGATTTGCAATGGTGTCACCACGGCCACATTCTGTGGCACGCCAGACTAT
ATCGCTCCAGAGATCCTCCAGGAAATGCTGTACGGGCCTGCAGTAGACTGGTGGGCAATG
GGCGTGTTGCTCTATGAGATGCTCTGTGGTCACGCGCCTTTTGAGGCAGAGAATGAAGAT
GACCTCTTTGAGGCCATACTGAATGATGAGGTGGTCTACCCTACCTGGCTCCATGAAGAT
GCCACAGGGATCCTAAAATCTTTCATGACCAAGAACCCCACCATGCGCTTGGGCAGCCTG
ACTCAGGGAGGCGAGCACGCCATCTTGAGACATCCTTTTTTTAAGGAAATCGACTGGGCC
CAGCTGAACCATCGCCAAATAGAACCGCCTTTCAGACCCAGAATCAAATCCCGAGAAGAT
GTCAGTAATTTTGACCCTGACTTCATAAAGGAAGAGCCAGTTTTAACTCCAATTGATGAG
GGACATCTTCCAATGATTAACCAGGATGAGTTTAGAAACTTTTCCTATGTGTCTCCAGAA
TTGCAACCATAG
Enzyme 52 GenBank Gene ID AK290183 Link Image
Enzyme 52 GeneCard ID PRKCH Link Image
Enzyme 52 GenAtlas ID PRKCH Link Image
Enzyme 52 HGNC ID HGNC:9403 Link Image
Enzyme 52 Chromosome Location 1
Enzyme 52 Locus 14q23.1
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References
  1. Bacher N, Zisman Y, Berent E, Livneh E: Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart. Mol Cell Biol. 1991 Jan;11(1):126-33. [PubMed Link Image]
  2. Bacher N, Zisman Y, Berent E, Livneh E: Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart. Mol Cell Biol. 1992 Mar;12(3):1404. [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. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [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. Palmer RH, Ridden J, Parker PJ: Identification of multiple, novel, protein kinase C-related gene products. FEBS Lett. 1994 Dec 12;356(1):5-8. [PubMed Link Image]
  7. van Baal J, de Widt J, Divecha N, van Blitterswijk WJ: Translocation of diacylglycerol kinase theta from cytosol to plasma membrane in response to activation of G protein-coupled receptors and protein kinase C. J Biol Chem. 2005 Mar 18;280(11):9870-8. Epub 2005 Jan 4. [PubMed Link Image]
  8. 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]
  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]
  10. 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]
  11. Littler DR, Walker JR, She YM, Finerty PJ Jr, Newman EM, Dhe-Paganon S: Structure of human protein kinase C eta (PKCeta) C2 domain and identification of phosphorylation sites. Biochem Biophys Res Commun. 2006 Nov 3;349(4):1182-9. Epub 2006 Sep 5. [PubMed Link Image]
  12. Kubo M, Hata J, Ninomiya T, Matsuda K, Yonemoto K, Nakano T, Matsushita T, Yamazaki K, Ohnishi Y, Saito S, Kitazono T, Ibayashi S, Sueishi K, Iida M, Nakamura Y, Kiyohara Y: A nonsynonymous SNP in PRKCH (protein kinase C eta) increases the risk of cerebral infarction. Nat Genet. 2007 Feb;39(2):212-7. Epub 2007 Jan 7. [PubMed Link Image]
  13. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 7222
Enzyme 53 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-2
Enzyme 53 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 53 Gene Name PLCH2
Enzyme 53 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 53 Number of Residues 1416
Enzyme 53 Molecular Weight 154667.0
Enzyme 53 Theoretical pI 7.89
Enzyme 53 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 53 General Function Involved in calcium ion binding
Enzyme 53 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 53 Pathways
Enzyme 53 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein Not Available
Enzyme 53 UniProtKB/Swiss-Prot ID O75038 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name PLCH2_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 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 53 GenBank Gene ID DQ176850 Link Image
Enzyme 53 GeneCard ID PLCH2 Link Image
Enzyme 53 GenAtlas ID PLCH2 Link Image
Enzyme 53 HGNC ID HGNC:29037 Link Image
Enzyme 53 Chromosome Location 1
Enzyme 53 Locus 1p36.32
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 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 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 7223
Enzyme 54 Name Protein kinase C epsilon type
Enzyme 54 Synonyms
  1. nPKC-epsilon
Enzyme 54 Gene Name PRKCE
Enzyme 54 Protein Sequence >Protein kinase C epsilon type
MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKT
NSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLE
PEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQP
TYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVN
MPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIA
KVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELE
NNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFG
KVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKD
RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL
DAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEM
MAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGED
AIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQI
NQEEFKGFSYFGEDLMP
Enzyme 54 Number of Residues 737
Enzyme 54 Molecular Weight 83673.2
Enzyme 54 Theoretical pI 7.13
Enzyme 54 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase C activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 54 General Function Involved in protein serine/threonine kinase activity
Enzyme 54 Specific Function PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters
Enzyme 54 Pathways Not Available
Enzyme 54 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • None
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein 4885563 Link Image
Enzyme 54 UniProtKB/Swiss-Prot ID Q02156 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name KPCE_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence >2214 bp
ATGGTAGTGTTCAATGGCCTTCTTAAGATCAAAATCTGCGAGGCCGTGAGCTTGAAGCCC
ACAGCCTGGTCGCTGCGCCATGCGGTGGGACCCCGGCCGCAGACTTTCCTTCTCGACCCC
TACATTGCCCTCAATGTGGACGACTCGCGCATCGGCCAAACGGCCACCAAGCAGAAGACC
AACAGCCCGGCCTGGCACGACGAGTTCGTCACCGATGTGTGCAACGGACGCAAGATCGAG
CTGGCTGTCTTTCACGATGCCCCCATAGGCTACGACGACTTCGTGGCCAACTGCACCATC
CAGTTTGAGGAGCTGCTGCAGAACGGGAGCCGCCACTTCGAGGACTGGATTGATCTGGAG
CCAGAAGGAAGAGTGTATGTGATCATCGATCTCTCAGGGTCGTCGGGTGAAGCCCCTAAA
GACAATGAAGAGCGTGTGTTCAGGGAACGCATGCGGCCGAGGAAGCGGCAGGGGGCCGTC
AGGCGCAGGGTCCATCAGGTCAACGGCCACAAGTTCATGGCCACCTATCTTCGGCAGCCC
ACCTACTGCTCCCATTGCAGAGACTTCATCTGGGGTGTCATAGGAAAGCAGGGATACCAG
TGTCAAGTCTGCACCTGCGTGGTCCACAAGCGGTGCCACGAGCTCATAATCACAAAGTGT
GCTGGGTTAAAGAAGCAGGAGACCCCCGACCAGGTGGGCTCCCAGCGGTTCAGCGTCAAC
ATGCCCCACAAGTTCGGTATCCACAACTACAAGGTCCCTACCTTCTGCGATCACTGTGGG
TCCCTGCTCTGGGGACTCTTGCGGCAGGGTTTGCAGTGTAAAGTCTGCAAAATGAATGTT
CACCGTCGATGTGAGACCAACGTGGCTCCCAACTGTGGAGTGGATGCCAGAGGAATCGCC
AAAGTACTGGCCGACCTGGGCGTTACCCCAGACAAAATCACCAACAGCGGCCAGAGAAGG
AAAAAGCTCATTGCTGGTGCCGAGTCCCCGCAGCCTGCTTCTGGAAGCTCACCATCTGAG
GAAGATCGATCCAAGTCAGCACCCACCTCCCCTTGTGACCAGGAAATAAAAGAACTTGAG
AACAACATTCGGAAAGCCTTGTCATTTGACAACCGAGGAGAGGAGCACCGGGCAGCATCG
TCTCCTGATGGCCAGCTGATGAGCCCCGGTGAGAATGGCGAAGTCCGGCAAGGCCAGGCC
AAGCGCCTGGGCCTGGATGAGTTCAACTTCATCAAGGTGTTGGGCAAAGGCAGCTTTGGC
AAGGTCATGTTGGCAGAACTCAAGGGCAAAGATGAAGTATATGCTGTGAAGGTCTTAAAG
AAGGACGTCATCCTTCAGGATGATGACGTGGACTGCACAATGACAGAGAAGAGGATTTTG
GCTCTGGCACGGAAACACCCGTACCTTACCCAACTCTACTGCTGCTTCCAGACCAAGGAC
CGCCTCTTTTTCGTCATGGAATATGTAAATGGTGGAGACCTCATGTTTCAGATTCAGCGC
TCCCGAAAATTCGACGAGCCTCGTTCACGGTTCTATGCTGCAGAGGTCACATCGGCCCTC
ATGTTCCTCCACCAGCATGGAGTCATCTACAGGGATTTGAAACTGGACAACATCCTTCTG
GATGCAGAAGGTCACTGCAAGCTGGCTGACTTCGGGATGTGCAAGGAAGGGATTCTGAAT
GGTGTGACGACCACCACGTTCTGTGGGACTCCTGACTACATAGCTCCTGAGATCCTGCAG
GAGTTGGAGTATGGCCCCTCCGTGGACTGGTGGGCCCTGGGGGTGCTGATGTACGAGATG
ATGGCTGGACAGCCTCCCTTTGAGGCCGACAATGAGGACGACCTATTTGAGTCCATCCTC
CATGACGACGTGCTGTACCCAGTCTGGCTCAGCAAGGAGGCTGTCAGCATCTTGAAAGCT
TTCATGACGAAGAATCCCCACAAGCGCCTGGGCTGTGTGGCATCGCAGAATGGCGAGGAC
GCCATCAAGCAGCACCCATTCTTCAAAGAGATTGACTGGGTGCTCCTGGAGCAGAAGAAG
ATCAAGCCACCCTTCAAACCACGCATTAAAACCAAAAGAGACGTCAATAATTTTGACCAA
GACTTTACCCGGGAAGAGCCGGTACTCACCCTTGTGGACGAAGCAATTGTAAAGCAGATC
AACCAGGAGGAATTCAAAGGTTTCTCCTACTTTGGTGAAGACCTGATGCCCTGA
Enzyme 54 GenBank Gene ID NM_005400.2 Link Image
Enzyme 54 GeneCard ID PRKCE Link Image
Enzyme 54 GenAtlas ID PRKCE Link Image
Enzyme 54 HGNC ID HGNC:9401 Link Image
Enzyme 54 Chromosome Location 2
Enzyme 54 Locus 2p21
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References
  1. Basta P, Strickland MB, Holmes W, Loomis CR, Ballas LM, Burns DJ: Sequence and expression of human protein kinase C-epsilon. Biochim Biophys Acta. 1992 Sep 24;1132(2):154-60. [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. Cenni V, Doppler H, Sonnenburg ED, Maraldi N, Newton AC, Toker A: Regulation of novel protein kinase C epsilon by phosphorylation. Biochem J. 2002 May 1;363(Pt 3):537-45. [PubMed Link Image]
  5. van Baal J, de Widt J, Divecha N, van Blitterswijk WJ: Translocation of diacylglycerol kinase theta from cytosol to plasma membrane in response to activation of G protein-coupled receptors and protein kinase C. J Biol Chem. 2005 Mar 18;280(11):9870-8. Epub 2005 Jan 4. [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. 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]
  9. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 7733
Enzyme 55 Name Ras association domain-containing protein 1
Enzyme 55 Synonyms Not Available
Enzyme 55 Gene Name RASSF1
Enzyme 55 Protein Sequence >Ras association domain-containing protein 1
MSGEPELIELRELAPAGRAGKGRTRLERANALRIARGTACNPTRQLVPGRGHRFQPAGPA
THTWCDLCGDFIWGVVRKGLQCARLSADCKFTCHYRCRALVCLDCCGPRDLGWEPAVERD
TNVDEPVEWETPDLSQAEIEQKIKEYNAQINSNLFMSLNKDGSYTGFIKVQLKLVRPVSV
PSSKKPPSLQDARRGPGRGTSVRRRTSFYLPKDAVKHLHVLSRTRAREVIEALLRKFLVV
DDPRKFALFERAERHGQVYLRKLLDDEQPLRLRLLAGPSDKALSFVLKENDSGEVNWDAF
SMPELHNFLRILQREEEEHLRQILQKYSYCRQKIQEALHACPLG
Enzyme 55 Number of Residues 344
Enzyme 55 Molecular Weight 39218.6
Enzyme 55 Theoretical pI 9.19
Enzyme 55 GO Classification
Function
  • binding
  • protein binding
Process
  • biological regulation
  • intracellular signaling pathway
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 55 General Function Involved in intracellular signaling pathway
Enzyme 55 Specific Function Potential tumor suppressor. Required for death receptor- dependent apoptosis. Mediates activation of STK4 during Fas- induced apoptosis. When associated with MOAP1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF10 stimulation. Isoform A interacts with CDC20, an activator of the anaphase-promoting complex, APC, resulting in the inhibition of APC activity and mitotic progression. Inhibits proliferation by negatively regulating cell cycle progression at the level of G1/S-phase transition by regulating accumulation of cyclin D1 protein. Isoform C has been shown not to perform these roles, no function has been identified for this isoform. Isoform A disrupts interactions among MDM2, DAXX and USP7, thus contributing to the efficient activation of TP53 by promoting MDM2 self-ubiquitination in cell-cycle checkpoint control in response to DNA damage
Enzyme 55 Pathways Not Available
Enzyme 55 Reactions Not Available
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • None
Enzyme 55 Transmembrane Regions
  • None
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 25777684 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID Q9NS23 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name RASF1_HUMAN Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >1035 bp
ATGTCGGGGGAGCCTGAGCTCATTGAGCTGCGGGAGCTGGCACCCGCTGGGCGCGCTGGG
AAGGGCCGCACCCGGCTGGAGCGTGCCAACGCGCTGCGCATCGCGCGGGGCACCGCGTGC
AACCCCACACGGCAGCTGGTCCCTGGCCGTGGCCACCGCTTCCAGCCCGCGGGGCCCGCC
ACGCACACGTGGTGCGACCTCTGTGGCGACTTCATCTGGGGCGTCGTGCGCAAAGGCCTG
CAGTGCGCGCGCCTCTCTGCAGATTGCAAGTTCACCTGCCACTACCGCTGCCGCGCGCTC
GTCTGCCTGGACTGTTGCGGGCCCCGGGACCTGGGCTGGGAACCCGCGGTGGAGCGGGAC
ACGAACGTGGACGAGCCTGTGGAGTGGGAGACACCTGACCTTTCTCAAGCTGAGATTGAG
CAGAAGATCAAGGAGTACAATGCCCAGATCAACAGCAACCTCTTCATGAGCTTGAACAAG
GACGGTTCTTACACAGGCTTCATCAAGGTTCAGCTGAAGCTGGTGCGCCCTGTCTCTGTG
CCCTCCAGCAAGAAGCCACCCTCCTTGCAGGATGCCCGGCGGGGCCCAGGACGGGGCACA
AGTGTCAGGCGCCGCACTTCCTTTTACCTGCCCAAGGATGCTGTCAAGCACCTGCATGTG
CTGTCACGCACAAGGGCACGTGAAGTCATTGAGGCCCTGCTGCGAAAGTTCTTGGTGGTG
GATGACCCCCGCAAGTTTGCACTCTTTGAGCGCGCTGAGCGTCACGGCCAAGTGTACTTG
CGGAAGCTGTTGGATGATGAGCAGCCCCTGCGGCTGCGGCTCCTGGCAGGGCCCAGTGAC
AAGGCCCTGAGCTTTGTCCTGAAGGAAAATGACTCTGGGGAGGTGAACTGGGACGCCTTC
AGCATGCCTGAACTACATAACTTCCTACGTATCCTGCAGCGGGAGGAGGAGGAGCACCTC
CGCCAGATCCTGCAGAAGTACTCCTATTGCCGCCAGAAGATCCAAGAGGCCCTGCACGCC
TGCCCCCTTGGGTGA
Enzyme 55 GenBank Gene ID NM_170714.1 Link Image
Enzyme 55 GeneCard ID RASSF1 Link Image
Enzyme 55 GenAtlas ID RASSF1 Link Image
Enzyme 55 HGNC ID HGNC:9882 Link Image
Enzyme 55 Chromosome Location 3
Enzyme 55 Locus 3p21.3
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References
  1. Dammann R, Li C, Yoon JH, Chin PL, Bates S, Pfeifer GP: Epigenetic inactivation of a RAS association domain family protein from the lung tumour suppressor locus 3p21.3. Nat Genet. 2000 Jul;25(3):315-9. [PubMed Link Image]
  2. Burbee DG, Forgacs E, Zochbauer-Muller S, Shivakumar L, Fong K, Gao B, Randle D, Kondo M, Virmani A, Bader S, Sekido Y, Latif F, Milchgrub S, Toyooka S, Gazdar AF, Lerman MI, Zabarovsky E, White M, Minna JD: Epigenetic inactivation of RASSF1A in lung and breast cancers and malignant phenotype suppression. J Natl Cancer Inst. 2001 May 2;93(9):691-9. [PubMed Link Image]
  3. 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]
  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. Shivakumar L, Minna J, Sakamaki T, Pestell R, White MA: The RASSF1A tumor suppressor blocks cell cycle progression and inhibits cyclin D1 accumulation. Mol Cell Biol. 2002 Jun;22(12):4309-18. [PubMed Link Image]
  6. Ortiz-Vega S, Khokhlatchev A, Nedwidek M, Zhang XF, Dammann R, Pfeifer GP, Avruch J: The putative tumor suppressor RASSF1A homodimerizes and heterodimerizes with the Ras-GTP binding protein Nore1. Oncogene. 2002 Feb 21;21(9):1381-90. [PubMed Link Image]
  7. Fenton SL, Dallol A, Agathanggelou A, Hesson L, Ahmed-Choudhury J, Baksh S, Sardet C, Dammann R, Minna JD, Downward J, Maher ER, Latif F: Identification of the E1A-regulated transcription factor p120 E4F as an interacting partner of the RASSF1A candidate tumor suppressor gene. Cancer Res. 2004 Jan 1;64(1):102-7. [PubMed Link Image]
  8. Dallol A, Agathanggelou A, Fenton SL, Ahmed-Choudhury J, Hesson L, Vos MD, Clark GJ, Downward J, Maher ER, Latif F: RASSF1A interacts with microtubule-associated proteins and modulates microtubule dynamics. Cancer Res. 2004 Jun 15;64(12):4112-6. [PubMed Link Image]
  9. Song MS, Song SJ, Ayad NG, Chang JS, Lee JH, Hong HK, Lee H, Choi N, Kim J, Kim H, Kim JW, Choi EJ, Kirschner MW, Lim DS: The tumour suppressor RASSF1A regulates mitosis by inhibiting the APC-Cdc20 complex. Nat Cell Biol. 2004 Feb;6(2):129-37. Epub 2004 Jan 25. [PubMed Link Image]
  10. Praskova M, Khoklatchev A, Ortiz-Vega S, Avruch J: Regulation of the MST1 kinase by autophosphorylation, by the growth inhibitory proteins, RASSF1 and NORE1, and by Ras. Biochem J. 2004 Jul 15;381(Pt 2):453-62. [PubMed Link Image]
  11. Liu L, Vo A, McKeehan WL: Specificity of the methylation-suppressed A isoform of candidate tumor suppressor RASSF1 for microtubule hyperstabilization is determined by cell death inducer C19ORF5. Cancer Res. 2005 Mar 1;65(5):1830-8. [PubMed Link Image]
  12. Baksh S, Tommasi S, Fenton S, Yu VC, Martins LM, Pfeifer GP, Latif F, Downward J, Neel BG: The tumor suppressor RASSF1A and MAP-1 link death receptor signaling to Bax conformational change and cell death. Mol Cell. 2005 Jun 10;18(6):637-50. [PubMed Link Image]
  13. Oh HJ, Lee KK, Song SJ, Jin MS, Song MS, Lee JH, Im CR, Lee JO, Yonehara S, Lim DS: Role of the tumor suppressor RASSF1A in Mst1-mediated apoptosis. Cancer Res. 2006 Mar 1;66(5):2562-9. [PubMed Link Image]
  14. Song MS, Song SJ, Kim SY, Oh HJ, Lim DS: The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex. EMBO J. 2008 Jul 9;27(13):1863-74. Epub 2008 Jun 19. [PubMed Link Image]
  15. 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]
  16. 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 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 8096
Enzyme 56 Name Serine/threonine-protein kinase B-raf
Enzyme 56 Synonyms
  1. Proto-oncogene B-Raf
  2. p94
  3. v-Raf murine sarcoma viral oncogene homolog B1
Enzyme 56 Gene Name BRAF
Enzyme 56 Protein Sequence >Serine/threonine-protein kinase B-raf
MAALSGGGGGGAEPGQALFNGDMEPEAGAGAGAAASSAADPAIPEEVWNIKQMIKLTQEH
IEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASMDTV
TSSSSSSLSVLPSSLSVFQNPTDVARSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDS
LKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRK
TFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPI
PQEEASLAETALTSGSSPSAPASDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQR
DRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSP
GPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDV
AVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHH
LHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATV
KSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNIN
NRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARS
LPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGAFPVH
Enzyme 56 Number of Residues 766
Enzyme 56 Molecular Weight 84436.1
Enzyme 56 Theoretical pI 7.58
Enzyme 56 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • molecular transducer activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • receptor signaling protein activity
  • signal transducer activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biological regulation
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 56 General Function Involved in intracellular signaling pathway
Enzyme 56 Specific Function Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May play a role in the postsynaptic responses of hippocampal neuron
Enzyme 56 Pathways Not Available
Enzyme 56 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 56 Pfam Domain Function
Enzyme 56 Signals
  • None
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein 33188459 Link Image
Enzyme 56 UniProtKB/Swiss-Prot ID P15056 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name BRAF_HUMAN Link Image
Enzyme 56 PDB ID 1UWJ Link Image
Enzyme 56 PDB File Show
Enzyme 56 3D Structure
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence >2301 bp
ATGGCGGCGCTGAGCGGTGGCGGTGGTGGCGGCGCGGAGCCGGGCCAGGCTCTGTTCAAC
GGGGACATGGAGCCCGAGGCCGGCGCCGGCGCCGGCGCCGCGGCCTCTTCGGCTGCGGAC
CCTGCCATTCCGGAGGAGGTGTGGAATATCAAACAAATGATTAAGTTGACACAGGAACAT
ATAGAGGCCCTATTGGACAAATTTGGTGGGGAGCATAATCCACCATCAATATATCTGGAG
GCCTATGAAGAATACACCAGCAAGCTAGATGCACTCCAACAAAGAGAACAACAGTTATTG
GAATCTCTGGGGAACGGAACTGATTTTTCTGTTTCTAGCTCTGCATCAATGGATACCGTT
ACATCTTCTTCCTCTTCTAGCCTTTCAGTGCTACCTTCATCTCTTTCAGTTTTTCAAAAT
CCCACAGATGTGGCACGGAGCAACCCCAAGTCACCACAAAAACCTATCGTTAGAGTCTTC
CTGCCCAACAAACAGAGGACAGTGGTACCTGCAAGGTGTGGAGTTACAGTCCGAGACAGT
CTAAAGAAAGCACTGATGATGAGAGGTCTAATCCCAGAGTGCTGTGCTGTTTACAGAATT
CAGGATGGAGAGAAGAAACCAATTGGTTGGGACACTGATATTTCCTGGCTTACTGGAGAA
GAATTGCATGTGGAAGTGTTGGAGAATGTTCCACTTACAACACACAACTTTGTACGAAAA
ACGTTTTTCACCTTAGCATTTTGTGACTTTTGTCGAAAGCTGCTTTTCCAGGGTTTCCGC
TGTCAAACATGTGGTTATAAATTTCACCAGCGTTGTAGTACAGAAGTTCCACTGATGTGT
GTTAATTATGACCAACTTGATTTGCTGTTTGTCTCCAAGTTCTTTGAACACCACCCAATA
CCACAGGAAGAGGCGTCCTTAGCAGAGACTGCCCTAACATCTGGATCATCCCCTTCCGCA
CCCGCCTCGGACTCTATTGGGCCCCAAATTCTCACCAGTCCGTCTCCTTCAAAATCCATT
CCAATTCCACAGCCCTTCCGACCAGCAGATGAAGATCATCGAAATCAATTTGGGCAACGA
GACCGATCCTCATCAGCTCCCAATGTGCATATAAACACAATAGAACCTGTCAATATTGAT
GACTTGATTAGAGACCAAGGATTTCGTGGTGATGGAGGATCAACCACAGGTTTGTCTGCT
ACCCCCCCTGCCTCATTACCTGGCTCACTAACTAACGTGAAAGCCTTACAGAAATCTCCA
GGACCTCAGCGAGAAAGGAAGTCATCTTCATCCTCAGAAGACAGGAATCGAATGAAAACA
CTTGGTAGACGGGACTCGAGTGATGATTGGGAGATTCCTGATGGGCAGATTACAGTGGGA
CAAAGAATTGGATCTGGATCATTTGGAACAGTCTACAAGGGAAAGTGGCATGGTGATGTG
GCAGTGAAAATGTTGAATGTGACAGCACCTACACCTCAGCAGTTACAAGCCTTCAAAAAT
GAAGTAGGAGTACTCAGGAAAACACGACATGTGAATATCCTACTCTTCATGGGCTATTCC
ACAAAGCCACAACTGGCTATTGTTACCCAGTGGTGTGAGGGCTCCAGCTTGTATCACCAT
CTCCATATCATTGAGACCAAATTTGAGATGATCAAACTTATAGATATTGCACGACAGACT
GCACAGGGCATGGATTACTTACACGCCAAGTCAATCATCCACAGAGACCTCAAGAGTAAT
AATATATTTCTTCATGAAGACCTCACAGTAAAAATAGGTGATTTTGGTCTAGCTACAGTG
AAATCTCGATGGAGTGGGTCCCATCAGTTTGAACAGTTGTCTGGATCCATTTTGTGGATG
GCACCAGAAGTCATCAGAATGCAAGATAAAAATCCATACAGCTTTCAGTCAGATGTATAT
GCATTTGGAATTGTTCTGTATGAATTGATGACTGGACAGTTACCTTATTCAAACATCAAC
AACAGGGACCAGATAATTTTTATGGTGGGACGAGGATACCTGTCTCCAGATCTCAGTAAG
GTACGGAGTAACTGTCCAAAAGCCATGAAGAGATTAATGGCAGAGTGCCTCAAAAAGAAA
AGAGATGAGAGACCACTCTTTCCCCAAATTCTCGCCTCTATTGAGCTGCTGGCCCGCTCA
TTGCCAAAAATTCACCGCAGTGCATCAGAACCCTCCTTGAATCGGGCTGGTTTCCAAACA
GAGGATTTTAGTCTATATGCTTGTGCTTCTCCAAAAACACCCATCCAGGCAGGGGGATAT
GGTGCGTTTCCTGTCCACTGA
Enzyme 56 GenBank Gene ID NM_004333.4 Link Image
Enzyme 56 GeneCard ID BRAF Link Image
Enzyme 56 GenAtlas ID BRAF Link Image
Enzyme 56 HGNC ID HGNC:1097 Link Image
Enzyme 56 Chromosome Location 7
Enzyme 56 Locus 7q34
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 General References
  1. Stephens RM, Sithanandam G, Copeland TD, Kaplan DR, Rapp UR, Morrison DK: 95-kilodalton B-Raf serine/threonine kinase: identification of the protein and its major autophosphorylation site. Mol Cell Biol. 1992 Sep;12(9):3733-42. [PubMed Link Image]
  2. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Eychene A, Barnier JV, Apiou F, Dutrillaux B, Calothy G: Chromosomal assignment of two human B-raf(Rmil) proto-oncogene loci: B-raf-1 encoding the p94Braf/Rmil and B-raf-2, a processed pseudogene. Oncogene. 1992 Aug;7(8):1657-60. [PubMed Link Image]
  6. Sithanandam G, Kolch W, Duh FM, Rapp UR: Complete coding sequence of a human B-raf cDNA and detection of B-raf protein kinase with isozyme specific antibodies. Oncogene. 1990 Dec;5(12):1775-80. [PubMed Link Image]
  7. Ikawa S, Fukui M, Ueyama Y, Tamaoki N, Yamamoto T, Toyoshima K: B-raf, a new member of the raf family, is activated by DNA rearrangement. Mol Cell Biol. 1988 Jun;8(6):2651-4. [PubMed Link Image]
  8. 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]
  9. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  10. 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]
  11. Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed Link Image]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
  19. Naoki K, Chen TH, Richards WG, Sugarbaker DJ, Meyerson M: Missense mutations of the BRAF gene in human lung adenocarcinoma. Cancer Res. 2002 Dec 1;62(23):7001-3. [PubMed Link Image]
  20. Davies H, Bignell GR, Cox C, Stephens P, Edkins S, Clegg S, Teague J, Woffendin H, Garnett MJ, Bottomley W, Davis N, Dicks E, Ewing R, Floyd Y, Gray K, Hall S, Hawes R, Hughes J, Kosmidou V, Menzies A, Mould C, Parker A, Stevens C, Watt S, Hooper S, Wilson R, Jayatilake H, Gusterson BA, Cooper C, Shipley J, Hargrave D, Pritchard-Jones K, Maitland N, Chenevix-Trench G, Riggins GJ, Bigner DD, Palmieri G, Cossu A, Flanagan A, Nicholson A, Ho JW, Leung SY, Yuen ST, Weber BL, Seigler HF, Darrow TL, Paterson H, Marais R, Marshall CJ, Wooster R, Stratton MR, Futreal PA: Mutations of the BRAF gene in human cancer. Nature. 2002 Jun 27;417(6892):949-54. Epub 2002 Jun 9. [PubMed Link Image]
  21. Rajagopalan H, Bardelli A, Lengauer C, Kinzler KW, Vogelstein B, Velculescu VE: Tumorigenesis: RAF/RAS oncogenes and mismatch-repair status. Nature. 2002 Aug 29;418(6901):934. [PubMed Link Image]
  22. Lee JW, Yoo NJ, Soung YH, Kim HS, Park WS, Kim SY, Lee JH, Park JY, Cho YG, Kim CJ, Ko YH, Kim SH, Nam SW, Lee JY, Lee SH: BRAF mutations in non-Hodgkin's lymphoma. Br J Cancer. 2003 Nov 17;89(10):1958-60. [PubMed Link Image]
  23. Hingorani SR, Jacobetz MA, Robertson GP, Herlyn M, Tuveson DA: Suppression of BRAF(V599E) in human melanoma abrogates transformation. Cancer Res. 2003 Sep 1;63(17):5198-202. [PubMed Link Image]
  24. Niihori T, Aoki Y, Narumi Y, Neri G, Cave H, Verloes A, Okamoto N, Hennekam RC, Gillessen-Kaesbach G, Wieczorek D, Kavamura MI, Kurosawa K, Ohashi H, Wilson L, Heron D, Bonneau D, Corona G, Kaname T, Naritomi K, Baumann C, Matsumoto N, Kato K, Kure S, Matsubara Y: Germline KRAS and BRAF mutations in cardio-facio-cutaneous syndrome. Nat Genet. 2006 Mar;38(3):294-6. Epub 2006 Feb 12. [PubMed Link Image]
  25. 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]
  26. Rodriguez-Viciana P, Tetsu O, Tidyman WE, Estep AL, Conger BA, Cruz MS, McCormick F, Rauen KA: Germline mutations in genes within the MAPK pathway cause cardio-facio-cutaneous syndrome. Science. 2006 Mar 3;311(5765):1287-90. Epub 2006 Jan 26. [PubMed Link Image]
  27. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
  28. Sarkozy A, Carta C, Moretti S, Zampino G, Digilio MC, Pantaleoni F, Scioletti AP, Esposito G, Cordeddu V, Lepri F, Petrangeli V, Dentici ML, Mancini GM, Selicorni A, Rossi C, Mazzanti L, Marino B, Ferrero GB, Silengo MC, Memo L, Stanzial F, Faravelli F, Stuppia L, Puxeddu E, Gelb BD, Dallapiccola B, Tartaglia M: Germline BRAF mutations in Noonan, LEOPARD, and cardiofaciocutaneous syndromes: molecular diversity and associated phenotypic spectrum. Hum Mutat. 2009 Apr;30(4):695-702. [PubMed Link Image]
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 8121
Enzyme 57 Name Short transient receptor potential channel 3
Enzyme 57 Synonyms
  1. TrpC3
  2. Transient receptor protein 3
  3. TRP-3
  4. hTrp-3
  5. hTrp3
Enzyme 57 Gene Name TRPC3
Enzyme 57 Protein Sequence >Short transient receptor potential channel 3
MEGSPSLRRMTVMREKGRRQAVRGPAFMFNDRGTSLTAEEERFLDAAEYGNIPVVRKMLE
ESKTLNVNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARIGDALLLAISKGYVRIVEA
ILNHPGFAASKRLTLSPCEQELQDDDFYAYDEDGTRFSPDITPIILAAHCQKYEVVHMLL
MKGARIERPHDYFCKCGDCMEKQRHDSFSHSRSRINAYKGLASPAYLSLSSEDPVLTALE
LSNELAKLANIEKEFKNDYRKLSMQCKDFVVGVLDLCRDSEEVEAILNGDLESAEPLEVH
RHKASLSRVKLAIKYEVKKFVAHPNCQQQLLTIWYENLSGLREQTIAIKCLVVLVVALGL
PFLAIGYWIAPCSRLGKILRSPFMKFVAHAASFIIFLGLLVFNASDRFEGITTLPNITVT
DYPKQIFRVKTTQFTWTEMLIMVWVLGMMWSECKELWLEGPREYILQLWNVLDFGMLSIF
IAAFTARFLAFLQATKAQQYVDSYVQESDLSEVTLPPEIQYFTYARDKWLPSDPQIISEG
LYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVLFIMVFFAFMIGMFILYS
YYLGAKVNAAFTTVEESFKTLFWSIFGLSEVTSVVLKYDHKFIENIGYVLYGIYNVTMVV
VLLNMLIAMINSSYQEIEDDSDVEWKFARSKLWLSYFDDGKTLPPPFSLVPSPKSFVYFI
MRIVNFPKCRRRRLQKDIEMGMGNSKSRLNLFTQSNSRVFESHSFNSILNQPTRYQQIMK
RLIKRYVLKAQVDKENDEVNEGELKEIKQDISSLRYELLEDKSQATEELAILIHKLSEKL
NPSMLRCE
Enzyme 57 Number of Residues 848
Enzyme 57 Molecular Weight 97354.1
Enzyme 57 Theoretical pI 6.74
Enzyme 57 GO Classification
Function
  • calcium channel activity
  • cation channel activity
  • ion channel activity
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • calcium ion transport
  • cation transport
  • di-, tri-valent inorganic cation transport
  • divalent metal ion transport
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 57 General Function Involved in ion channel activity
Enzyme 57 Specific Function Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C, and by inositol-1,4,5- triphosphate receptors (ITPR) with bound IP3. May also be activated by internal calcium store depletion
Enzyme 57 Pathways Not Available
Enzyme 57 Reactions Not Available
Enzyme 57 Pfam Domain Function
Enzyme 57 Signals
  • None
Enzyme 57 Transmembrane Regions
  • 350-370 382-402 431-451 464-484 536-556 580-600 616-636 650-670 707-726
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein Not Available
Enzyme 57 UniProtKB/Swiss-Prot ID Q13507 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name TRPC3_HUMAN Link Image
Enzyme 57 PDB ID Not Available
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence >2547 bp
ATGGAGGGAAGCCCATCCCTGAGACGCATGACAGTGATGCGGGAGAAGGGCCGGCGCCAG
GCTGTCAGGGGCCCGGCCTTCATGTTCAATGACCGCGGCACCAGCCTCACCGCCGAGGAG
GAGCGCTTCCTCGACGCCGCCGAGTACGGCAACATCCCAGTGGTGCGCAAGATGCTGGAG
GAGTCCAAGACGCTGAACGTCAACTGCGTGGACTACATGGGCCAGAACGCGCTGCAGCTG
GCTGTGGGCAACGAGCACCTGGAGGTGACCGAGCTGCTGCTCAAGAAGGAGAACCTGGCG
CGCATTGGCGACGCCCTGCTGCTCGCCATCAGCAAGGGCTACGTGCGCATTGTAGAGGCC
ATCCTCAACCACCCTGGCTTCGCGGCCAGCAAGCGTCTCACTCTGAGCCCCTGTGAGCAG
GAGCTGCAGGACGACGACTTCTACGCTTACGATGAGGACGGCACGCGCTTCTCGCCGGAC
ATCACCCCCATCATCCTGGCGGCGCACTGCCAGAAATACGAAGTGGTGCACATGCTGCTG
ATGAAGGGTGCCAGGATCGAGCGGCCGCACGACTATTTCTGCAAGTGCGGGGACTGCATG
GAGAAGCAGAGGCACGACTCCTTCAGCCACTCACGCTCGAGGATCAATGCCTACAAGGGG
CTGGCCAGCCCGGCTTACCTCTCATTGTCCAGCGAGGACCCGGTGCTTACGGCCCTAGAG
CTCAGCAACGAGCTGGCCAAGCTGGCCAACATAGAGAAGGAGTTCAAGAATGACTATCGG
AAGCTCTCCATGCAATGCAAAGACTTTGTAGTGGGTGTGCTGGATCTCTGCCGAGACTCA
GAAGAGGTAGAAGCCATTCTGAATGGAGATCTGGAATCAGCAGAGCCTCTGGAGGTACAC
AGGCACAAAGCTTCATTAAGTCGTGTCAAACTTGCCATTAAGTATGAAGTCAAAAAGTTT
GTGGCTCATCCCAACTGCCAGCAGCAGCTCTTGACGATCTGGTATGAGAACCTCTCAGGC
CTAAGGGAGCAGACCATAGCTATCAAGTGTCTCGTTGTGCTGGTCGTGGCCCTGGGCCTT
CCATTCCTGGCCATTGGCTACTGGATCGCACCTTGCAGCAGGCTGGGGAAAATTCTGCGA
AGCCCTTTTATGAAGTTTGTAGCACATGCAGCTTCTTTCATCATCTTCCTGGGTCTGCTT
GTGTTCAATGCCTCAGACAGGTTCGAAGGCATCACCACGCTGCCCAATATCACAGTTACT
GACTATCCCAAACAGATCTTCAGGGTGAAAACCACCCAGTTTACATGGACTGAAATGCTA
ATTATGGTCTGGGTTCTTGGAATGATGTGGTCTGAATGTAAAGAGCTCTGGCTGGAAGGA
CCTAGGGAATACATTTTGCAGTTGTGGAATGTGCTTGACTTTGGGATGCTGTCCATCTTC
ATTGCTGCTTTCACAGCCAGATTCCTAGCTTTCCTTCAGGCAACGAAGGCACAACAGTAT
GTGGACAGTTACGTCCAAGAGAGTGACCTCAGTGAAGTGACACTCCCACCAGAGATACAG
TATTTCACTTATGCTAGAGATAAATGGCTCCCTTCTGACCCTCAGATTATATCTGAAGGC
CTTTATGCCATAGCTGTTGTGCTCAGCTTCTCTCGGATTGCGTACATCCTCCCTGCAAAT
GAGAGCTTTGGCCCCCTGCAGATCTCTCTTGGAAGGACTGTAAAGGACATATTCAAGTTC
ATGGTCCTCTTTATTATGGTGTTTTTTGCCTTTATGATTGGCATGTTCATACTTTATTCT
TACTACCTTGGGGCTAAAGTTAATGCTGCTTTTACCACTGTAGAAGAAAGTTTCAAGACT
TTATTTTGGTCAATATTTGGGTTGTCTGAAGTGACTTCCGTTGTGCTCAAATATGATCAC
AAATTCATAGAAAATATTGGATACGTTCTTTATGGAATATACAATGTAACTATGGTGGTC
GTTTTACTCAACATGCTAATTGCTATGATTAATAGCTCATATCAAGAAATTGAGGATGAC
AGTGATGTAGAATGGAAGTTTGCTCGTTCAAAACTTTGGTTATCCTATTTTGATGATGGA
AAAACATTACCTCCACCTTTCAGTCTAGTTCCTAGTCCAAAATCATTTGTTTATTTCATC
ATGCGAATTGTTAACTTTCCCAAATGCAGAAGGAGAAGACTTCAGAAGGATATAGAAATG
GGAATGGGTAACTCAAAGTCCAGGTTAAACCTCTTCACTCAGTCTAACTCAAGAGTTTTT
GAATCACACAGTTTTAACAGCATTCTCAATCAGCCAACACGTTATCAGCAGATAATGAAA
AGACTTATAAAGCGGTATGTCTTGAAAGCACAAGTAGACAAAGAAAATGATGAAGTTAAT
GAAGGTGAATTAAAAGAAATCAAGCAAGATATCTCCAGCCTTCGTTATGAACTTTTGGAA
GACAAGAGCCAAGCAACTGAGGAATTAGCCATTCTAATTCATAAACTTAGTGAGAAACTG
AATCCCAGCATGCTGAGATGTGAATGA
Enzyme 57 GenBank Gene ID U47050 Link Image
Enzyme 57 GeneCard ID TRPC3 Link Image
Enzyme 57 GenAtlas ID TRPC3 Link Image
Enzyme 57 HGNC ID HGNC:12335 Link Image
Enzyme 57 Chromosome Location 4
Enzyme 57 Locus 4q27
Enzyme 57 SNPs SNPJam Report Link Image
Enzyme 57 General References
  1. Zhu X, Jiang M, Peyton M, Boulay G, Hurst R, Stefani E, Birnbaumer L: trp, a novel mammalian gene family essential for agonist-activated capacitative Ca2+ entry. Cell. 1996 May 31;85(5):661-71. [PubMed Link Image]
  2. Xu XZ, Li HS, Guggino WB, Montell C: Coassembly of TRP and TRPL produces a distinct store-operated conductance. Cell. 1997 Jun 27;89(7):1155-64. [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. Wes PD, Chevesich J, Jeromin A, Rosenberg C, Stetten G, Montell C: TRPC1, a human homolog of a Drosophila store-operated channel. Proc Natl Acad Sci U S A. 1995 Oct 10;92(21):9652-6. [PubMed Link Image]
  5. Vannier B, Zhu X, Brown D, Birnbaumer L: The membrane topology of human transient receptor potential 3 as inferred from glycosylation-scanning mutagenesis and epitope immunocytochemistry. J Biol Chem. 1998 Apr 10;273(15):8675-9. [PubMed Link Image]
  6. Zhu X, Jiang M, Birnbaumer L: Receptor-activated Ca2+ influx via human Trp3 stably expressed in human embryonic kidney (HEK)293 cells. Evidence for a non-capacitative Ca2+ entry. J Biol Chem. 1998 Jan 2;273(1):133-42. [PubMed Link Image]
  7. Kiselyov K, Xu X, Mozhayeva G, Kuo T, Pessah I, Mignery G, Zhu X, Birnbaumer L, Muallem S: Functional interaction between InsP3 receptors and store-operated Htrp3 channels. Nature. 1998 Dec 3;396(6710):478-82. [PubMed Link Image]
  8. Hofmann T, Obukhov AG, Schaefer M, Harteneck C, Gudermann T, Schultz G: Direct activation of human TRPC6 and TRPC3 channels by diacylglycerol. Nature. 1999 Jan 21;397(6716):259-63. [PubMed Link Image]
  9. Boulay G, Brown DM, Qin N, Jiang M, Dietrich A, Zhu MX, Chen Z, Birnbaumer M, Mikoshiba K, Birnbaumer L: Modulation of Ca(2+) entry by polypeptides of the inositol 1,4, 5-trisphosphate receptor (IP3R) that bind transient receptor potential (TRP): evidence for roles of TRP and IP3R in store depletion-activated Ca(2+) entry. Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14955-60. [PubMed Link Image]
  10. Lussier MP, Cayouette S, Lepage PK, Bernier CL, Francoeur N, St-Hilaire M, Pinard M, Boulay G: MxA, a member of the dynamin superfamily, interacts with the ankyrin-like repeat domain of TRPC. J Biol Chem. 2005 May 13;280(19):19393-400. Epub 2005 Mar 9. [PubMed Link Image]
  11. Lussier MP, Lepage PK, Bousquet SM, Boulay G: RNF24, a new TRPC interacting protein, causes the intracellular retention of TRPC. Cell Calcium. 2008 May;43(5):432-43. Epub 2007 Sep 11. [PubMed Link Image]
Enzyme 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 8362
Enzyme 58 Name Cholinephosphotransferase 1
Enzyme 58 Synonyms
  1. hCPT1
  2. AAPT1-like protein
  3. Diacylglycerol cholinephosphotransferase 1
Enzyme 58 Gene Name CHPT1
Enzyme 58 Protein Sequence >Cholinephosphotransferase 1
MAAGAGAGSAPRWLRALSEPLSAAQLRRLEEHRYSAAGVSLLEPPLQLYWTWLLQWIPLW
MAPNSITLLGLAVNVVTTLVLISYCPTATEEAPYWTYLLCALGLFIYQSLDAIDGKQARR
TNSCSPLGELFDHGCDSLSTVFMAVGASIAARLGTYPDWFFFCSFIGMFVFYCAHWQTYV
SGMLRFGKVDVTEIQIALVIVFVLSAFGGATMWDYTIPILEIKLKILPVLGFLGGVIFSC
SNYFHVILHGGVGKNGSTIAGTSVLSPGLHIGLIIILAIMIYKKSATDVFEKHPCLYILM
FGCVFAKVSQKLVVAHMTKSELYLQDTVFLGPGLLFLDQYFNNFIDEYVVLWMAMVISSF
DMVIYFSALCLQISRHLHLNIFKTACHQAPEQVQVLSSKSHQNNMD
Enzyme 58 Number of Residues 406
Enzyme 58 Molecular Weight 45096.5
Enzyme 58 Theoretical pI 6.92
Enzyme 58 GO Classification
Function
  • catalytic activity
  • phosphotransferase activity, for other substituted phosphate groups
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid biosynthetic process
  • phospholipid metabolic process
Component
  • cell part
  • membrane
Enzyme 58 General Function Involved in phosphotransferase activity, for other substituted phosphate groups
Enzyme 58 Specific Function Catalyzes phosphatidylcholine biosynthesis from CDP- choline. It thereby plays a central role in the formation and maintenance of vesicular membranes
Enzyme 58 Pathways Not Available
Enzyme 58 Reactions
  • CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine [RN:R01321]
Enzyme 58 Pfam Domain Function
Enzyme 58 Signals
  • None
Enzyme 58 Transmembrane Regions
  • 66-86 93-113 153-173 193-213 226-248 261-281 295-315 349-369
Enzyme 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein 50726996 Link Image
Enzyme 58 UniProtKB/Swiss-Prot ID Q8WUD6 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name CHPT1_HUMAN Link Image
Enzyme 58 PDB ID Not Available
Enzyme 58 Cellular Location Not Available
Enzyme 58 Gene Sequence >1221 bp
ATGGCGGCAGGCGCCGGGGCCGGGTCCGCGCCGCGCTGGCTGAGGGCGCTGAGCGAGCCG
CTGAGCGCGGCGCAGCTGCGGCGACTGGAGGAGCACCGCTACAGCGCGGCGGGCGTCTCG
CTGCTCGAGCCGCCGCTGCAGCTCTACTGGACCTGGCTGCTCCAGTGGATCCCGCTCTGG
ATGGCCCCCAACTCCATCACCCTGCTGGGGCTCGCCGTCAACGTGGTCACCACGCTCGTG
CTCATCTCCTACTGTCCCACGGCCACCGAAGAGGCACCATACTGGACATACCTTTTATGT
GCACTGGGACTTTTTATTTACCAGTCACTGGATGCTATTGATGGGAAACAAGCCAGAAGA
ACAAACTCTTGTTCCCCTTTAGGGGAGCTCTTTGACCATGGCTGTGACTCTCTTTCCACA
GTATTTATGGCAGTGGGAGCTTCAATTGCCGCTCGCTTAGGAACTTATCCTGACTGGTTT
TTTTTCTGCTCTTTTATTGGGATGTTTGTGTTTTATTGCGCTCATTGGCAGACTTATGTT
TCAGGCATGTTGAGATTTGGAAAAGTGGATGTAACTGAAATTCAGATAGCTTTAGTGATT
GTCTTTGTGTTGTCTGCATTTGGAGGAGCAACAATGTGGGACTATACGATTCCTATTCTA
GAAATAAAATTGAAGATCCTTCCAGTTCTTGGATTTCTAGGTGGAGTAATATTTTCCTGT
TCAAATTATTTCCATGTTATCCTCCATGGTGGTGTTGGCAAGAATGGATCCACTATAGCA
GGCACCAGTGTCTTGTCACCTGGACTCCACATAGGACTAATTATTATACTGGCAATAATG
ATCTATAAAAAGTCAGCAACTGATGTGTTTGAAAAGCATCCTTGTCTTTATATCCTAATG
TTTGGATGTGTCTTTGCTAAAGTCTCACAAAAATTAGTGGTAGCTCACATGACCAAAAGT
GAACTATATCTTCAAGACACTGTCTTTTTGGGGCCAGGTCTTTTGTTTTTAGACCAGTAC
TTTAATAACTTTATAGACGAATATGTTGTTCTATGGATGGCAATGGTGATTTCTTCATTT
GATATGGTGATATACTTTAGTGCTTTGTGCCTGCAAATTTCAAGACACCTTCATCTAAAT
ATATTCAAGACTGCATGTCATCAAGCACCTGAACAGGTTCAAGTTCTTTCTTCAAAGAGT
CATCAGAATAACATGGATTGA
Enzyme 58 GenBank Gene ID NM_020244.2 Link Image
Enzyme 58 GeneCard ID CHPT1 Link Image
Enzyme 58 GenAtlas ID CHPT1 Link Image
Enzyme 58 HGNC ID HGNC:17852 Link Image
Enzyme 58 Chromosome Location 1
Enzyme 58 Locus 12q
Enzyme 58 SNPs SNPJam Report Link Image
Enzyme 58 General References
  1. Henneberry AL, Wistow G, McMaster CR: Cloning, genomic organization, and characterization of a human cholinephosphotransferase. J Biol Chem. 2000 Sep 22;275(38):29808-15. [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. 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. Sinha Roy S, Mukherjee S, Kabir S, Rajaratnam V, Smith M, Das SK: Inhibition of cholinephosphotransferase activity in lung injury induced by 2-chloroethyl ethyl sulfide, a mustard analog. J Biochem Mol Toxicol. 2005;19(5):289-97. [PubMed Link Image]
  5. Ghosh A, Akech J, Mukherjee S, Das SK: Differential expression of cholinephosphotransferase in normal and cancerous human mammary epithelial cells. Biochem Biophys Res Commun. 2002 Oct 4;297(4):1043-8. [PubMed Link Image]
  6. Henneberry AL, Wright MM, McMaster CR: The major sites of cellular phospholipid synthesis and molecular determinants of Fatty Acid and lipid head group specificity. Mol Biol Cell. 2002 Sep;13(9):3148-61. [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]
Enzyme 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 8433
Enzyme 59 Name Inactive phospholipase C-like protein 1
Enzyme 59 Synonyms
  1. PLC-L1
  2. Phospholipase C-deleted in lung carcinoma
  3. Phospholipase C-related but catalytically inactive protein
  4. PRIP
Enzyme 59 Gene Name PLCL1
Enzyme 59 Protein Sequence >Inactive phospholipase C-like protein 1
MAEGAAGREDPAPPDAAGGEDDPRVGPDAAGDCVTAASGGRMRDRRSGVALPGAAGTPAD
SEAGLLEAARATPRRSSIIKDPSNQKCGGRKKTVSFSSMPSEKKISSANDCISFMQAGCE
LKKVRPNSRIYNRFFTLDTDLQALRWEPSKKDLEKAKLDISAIKEIRLGKNTETFRNNGL
ADQICEDCAFSILHGENYESLDLVANSADVANIWVSGLRYLVSRSKQPLDFMEGNQNTPR
FMWLKTVFEAADVDGNGIMLEDTSVELIKQLNPTLKEAKIRLKFKEIQKSKEKLTTRVTE
EEFCEAFCELCTRPEVYFLLVQISKNKEYLDANDLMLFLEAEQGVTHITEDICLDIIRRY
ELSEEGRQKGFLAIDGFTQYLLSSECDIFDPEQKKVAQDMTQPLSHYYINASHNTYLIED
QFRGPADINGYIRALKMGCRSVELDVSDGSDNEPILCNRNNMTTHVSFRSVIEVINKFAF
VASEYPLILCLGNHCSLPQQKVMAQQMKKVFGNKLYTEAPLPSESYLPSPEKLKRMIIVK
GKKLPSDPDVLEGEVTDEDEEAEMSRRMSVDYNGEQKQIRLCRELSDLVSICKSVQYRDF
ELSMKSQNYWEMCSFSETEASRIANEYPEDFVNYNKKFLSRIYPSAMRIDSSNLNPQDFW
NCGCQIVAMNFQTPGPMMDLHTGWFLQNGGCGYVLRPSIMRDEVSYFSANTKGILPGVSP
LALHIKIISGQNFPKPKGACAKGDVIDPYVCIEIHGIPADCSEQRTKTVQQNSDNPIFDE
TFEFQVNLPELAMIRFVVLDDDYIGDEFIGQYTIPFECLQPGYRHVPLRSFVGDIMEHVT
LFVHIAITNRSGGGKAQKRSLSVRMGKKVREYTMLRNIGLKTIDDIFKIAVHPLREAIDM
RENMQNAIVSIKELCGLPPIASLKQCLLTLSSRLITSDNTPSVSLVMKDSFPYLEPLGAI
PDVQKKMLTAYDLMIQESRFLIEMADTVQEKIVQCQKAGMEFHEELHNLGAKEGLKGRKL
NKATESFAWNITVLKGQGDLLKNAKNEAIENMKQIQLACLSCGLSKAPSSSAEAKSKRSL
EAIEEKESSEENGKL
Enzyme 59 Number of Residues 1095
Enzyme 59 Molecular Weight 122727.0
Enzyme 59 Theoretical pI 5.30
Enzyme 59 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 59 General Function Involved in calcium ion binding
Enzyme 59 Specific Function Involved in an inositol phospholipid-based intracellular signaling cascade. Shows no PLC activity to phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol. Component in the phospho-dependent endocytosis process of GABA A receptor. Regulates the turnover of receptors and thus contributes to the maintenance of GABA-mediated synaptic inhibition. Its aberrant expression could contribute to the genesis and progression of lung carcinoma. Acts as a inhibitor of PPP1C
Enzyme 59 Pathways Not Available
Enzyme 59 Reactions Not Available
Enzyme 59 Pfam Domain Function
Enzyme 59 Signals
  • None
Enzyme 59 Transmembrane Regions
  • None
Enzyme 59 Essentiality Not Available
Enzyme 59 GenBank ID Protein 254939661 Link Image
Enzyme 59 UniProtKB/Swiss-Prot ID Q15111 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name PLCL1_HUMAN Link Image
Enzyme 59 PDB ID Not Available
Enzyme 59 Cellular Location Not Available
Enzyme 59 Gene Sequence >3288 bp
ATGGCCGAGGGCGCGGCCGGCAGGGAGGATCCGGCGCCGCCCGACGCGGCGGGGGGCGAA
GACGACCCCCGAGTGGGCCCGGATGCCGCCGGGGACTGCGTGACGGCGGCCTCTGGGGGC
CGGATGAGGGACCGTCGCAGCGGGGTCGCACTGCCAGGCGCCGCGGGGACCCCAGCGGAC
AGCGAGGCGGGCCTCCTGGAGGCAGCACGGGCGACCCCCCGGCGCAGCAGCATCATCAAG
GATCCTTCAAACCAAAAATGTGGTGGAAGAAAGAAAACCGTGTCTTTCAGCAGCATGCCA
TCGGAAAAGAAAATTAGCAGTGCAAATGACTGCATCAGCTTCATGCAAGCTGGCTGTGAG
TTGAAGAAAGTCCGGCCAAATTCTCGCATTTACAACCGTTTTTTCACTCTGGACACAGAC
CTTCAAGCTCTTCGCTGGGAACCTTCAAAGAAAGACCTCGAGAAAGCCAAGCTTGATATT
TCTGCCATAAAAGAGATCAGACTGGGGAAAAACACGGAAACATTTAGAAACAATGGCCTT
GCTGACCAGATCTGTGAGGACTGTGCCTTTTCCATACTCCACGGGGAAAACTATGAGTCT
CTGGACCTAGTTGCCAATTCAGCAGATGTGGCAAACATCTGGGTGTCTGGGTTACGGTAC
CTGGTTTCTCGAAGTAAGCAGCCTCTTGATTTTATGGAGGGCAACCAGAACACACCACGG
TTCATGTGGTTGAAAACAGTGTTTGAAGCAGCAGATGTTGATGGGAATGGGATTATGTTG
GAAGACACCTCTGTAGAGTTAATAAAACAACTCAACCCTACTCTGAAGGAAGCCAAGATC
AGGTTAAAGTTTAAAGAAATCCAGAAGAGCAAGGAAAAACTAACCACCCGCGTGACCGAA
GAGGAATTTTGTGAAGCTTTTTGTGAACTTTGCACCAGGCCAGAAGTGTATTTCTTACTT
GTACAGATATCTAAAAACAAAGAATATTTGGATGCCAATGATCTCATGCTCTTTTTAGAA
GCTGAGCAAGGAGTCACCCATATCACCGAGGATATATGCTTAGACATCATAAGGAGATAC
GAACTTTCTGAAGAGGGACGTCAAAAAGGGTTTCTTGCAATTGATGGCTTTACCCAGTAT
TTATTGTCATCAGAATGTGACATTTTTGATCCTGAGCAAAAGAAGGTTGCCCAAGATATG
ACCCAGCCATTATCTCACTACTATATCAATGCCTCTCATAACACCTATCTAATAGAAGAC
CAGTTCAGGGGGCCAGCTGACATCAATGGGTACATTAGAGCTTTGAAAATGGGCTGTCGA
AGCGTTGAACTCGATGTAAGTGATGGTTCAGATAATGAACCAATCCTTTGTAATCGAAAT
AACATGACAACCCATGTTTCCTTTCGAAGTGTCATAGAGGTAATAAATAAATTTGCCTTT
GTTGCTTCTGAATACCCACTCATTCTTTGCTTGGGAAATCACTGCTCCTTGCCGCAGCAG
AAGGTAATGGCTCAACAGATGAAAAAGGTCTTTGGCAATAAACTCTATACTGAAGCACCT
TTGCCCTCAGAATCCTACCTCCCATCACCAGAAAAATTAAAAAGAATGATCATTGTGAAA
GGAAAGAAGTTGCCTTCTGATCCAGATGTGTTAGAAGGAGAAGTAACAGATGAAGATGAA
GAAGCTGAAATGTCTCGAAGGATGTCGGTAGATTACAATGGTGAGCAGAAGCAAATCCGA
CTCTGTAGGGAGCTCTCTGATTTGGTGTCTATTTGTAAATCTGTTCAATACAGGGATTTT
GAACTATCTATGAAAAGCCAAAACTATTGGGAAATGTGTTCATTTAGTGAAACAGAGGCC
AGCCGCATTGCAAATGAGTACCCAGAGGATTTTGTTAATTATAATAAGAAGTTCTTATCA
AGAATCTATCCAAGTGCCATGAGGATCGATTCCAGTAACTTGAATCCACAGGACTTTTGG
AATTGTGGCTGTCAGATTGTAGCAATGAATTTTCAGACTCCGGGTCCAATGATGGACCTT
CACACGGGCTGGTTTCTTCAAAACGGGGGATGTGGTTATGTTCTAAGGCCGTCTATAATG
CGAGATGAAGTTTCTTACTTCAGCGCAAATACAAAGGGCATTCTACCTGGGGTGTCTCCT
CTAGCTCTTCATATCAAGATCATCAGTGGTCAGAATTTCCCAAAGCCCAAGGGAGCTTGT
GCCAAAGGGGATGTCATAGATCCCTATGTTTGTATAGAGATACACGGAATTCCAGCGGAT
TGTTCGGAACAAAGAACTAAAACTGTACAGCAAAACAGTGATAATCCTATTTTTGATGAA
ACTTTTGAGTTCCAAGTAAACCTACCTGAGCTGGCCATGATCCGTTTTGTTGTTCTGGAT
GATGACTACATTGGGGATGAGTTTATAGGGCAATATACGATACCATTTGAATGTTTGCAG
CCTGGATATCGGCATGTTCCCCTGCGTTCTTTTGTGGGTGACATCATGGAGCACGTAACC
CTTTTTGTCCACATAGCAATAACTAATCGAAGTGGAGGAGGAAAGGCACAGAAGCGCAGT
CTTTCAGTGAGAATGGGGAAGAAAGTTCGGGAATATACCATGCTCAGGAATATCGGTCTT
AAAACCATTGATGACATCTTTAAAATAGCGGTTCATCCATTACGAGAAGCCATAGATATG
AGAGAAAATATGCAGAATGCAATCGTGTCTATTAAGGAACTATGTGGACTCCCTCCAATT
GCCAGTCTGAAGCAGTGCCTGTTAACTCTGTCATCTCGGCTCATCACCAGTGACAATACT
CCTTCAGTCTCACTTGTGATGAAAGACAGCTTTCCTTACCTGGAGCCTCTGGGTGCAATT
CCAGATGTGCAGAAAAAGATGCTGACTGCTTATGATCTGATGATTCAAGAGAGCCGGTTT
CTCATAGAAATGGCGGACACAGTCCAGGAAAAGATTGTACAGTGTCAGAAAGCAGGGATG
GAGTTCCATGAAGAACTTCATAATTTGGGGGCAAAAGAAGGCTTGAAGGGAAGAAAACTC
AACAAAGCAACTGAGAGCTTTGCTTGGAACATTACAGTATTGAAGGGCCAAGGAGATCTG
TTGAAGAATGCCAAGAATGAAGCTATAGAAAACATGAAGCAGATCCAGCTGGCATGCCTG
TCCTGTGGACTGAGTAAAGCCCCCAGCAGCAGTGCTGAGGCCAAGAGCAAGCGCAGCCTG
GAAGCCATAGAGGAGAAGGAAAGTAGTGAGGAGAATGGGAAGCTGTGA
Enzyme 59 GenBank Gene ID NM_006226.3 Link Image
Enzyme 59 GeneCard ID PLCL1 Link Image
Enzyme 59 GenAtlas ID PLCL1 Link Image
Enzyme 59 HGNC ID HGNC:9063 Link Image
Enzyme 59 Chromosome Location 2
Enzyme 59 Locus 2q33
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 General References
  1. Kohno T, Otsuka T, Takano H, Yamamoto T, Hamaguchi M, Terada M, Yokota J: Identification of a novel phospholipase C family gene at chromosome 2q33 that is homozygously deleted in human small cell lung carcinoma. Hum Mol Genet. 1995 Apr;4(4):667-74. [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. 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. Yoshimura K, Takeuchi H, Sato O, Hidaka K, Doira N, Terunuma M, Harada K, Ogawa Y, Ito Y, Kanematsu T, Hirata M: Interaction of p130 with, and consequent inhibition of, the catalytic subunit of protein phosphatase 1alpha. J Biol Chem. 2001 May 25;276(21):17908-13. Epub 2001 Mar 2. [PubMed Link Image]
  6. Kanematsu T, Jang IS, Yamaguchi T, Nagahama H, Yoshimura K, Hidaka K, Matsuda M, Takeuchi H, Misumi Y, Nakayama K, Yamamoto T, Akaike N, Hirata M, Nakayama K: Role of the PLC-related, catalytically inactive protein p130 in GABA(A) receptor function. EMBO J. 2002 Mar 1;21(5):1004-11. [PubMed Link Image]
  7. Kanematsu T, Takeuchi H, Terunuma M, Hirata M: PRIP, a novel Ins(1,4,5)P3 binding protein, functional significance in Ca2+ signaling and extension to neuroscience and beyond. Mol Cells. 2005 Dec 31;20(3):305-14. [PubMed Link Image]
  8. Yanagihori S, Terunuma M, Koyano K, Kanematsu T, Ho Ryu S, Hirata M: Protein phosphatase regulation by PRIP, a PLC-related catalytically inactive protein--implications in the phospho-modulation of the GABAA receptor. Adv Enzyme Regul. 2006;46:203-22. Epub 2006 Jul 18. [PubMed Link Image]
  9. Murakami A, Matsuda M, Nakasima A, Hirata M: Characterization of the human PRIP-1 gene structure and transcriptional regulation. Gene. 2006 Nov 1;382:129-39. Epub 2006 Jul 20. [PubMed Link Image]
  10. Kanematsu T, Yasunaga A, Mizoguchi Y, Kuratani A, Kittler JT, Jovanovic JN, Takenaka K, Nakayama KI, Fukami K, Takenawa T, Moss SJ, Nabekura J, Hirata M: Modulation of GABA(A) receptor phosphorylation and membrane trafficking by phospholipase C-related inactive protein/protein phosphatase 1 and 2A signaling complex underlying brain-derived neurotrophic factor-dependent regulation of GABAergic inhibition. J Biol Chem. 2006 Aug 4;281(31):22180-9. Epub 2006 Jun 5. [PubMed Link Image]
  11. Kanematsu T, Fujii M, Mizokami A, Kittler JT, Nabekura J, Moss SJ, Hirata M: Phospholipase C-related inactive protein is implicated in the constitutive internalization of GABAA receptors mediated by clathrin and AP2 adaptor complex. J Neurochem. 2007 May;101(4):898-905. Epub 2007 Jan 24. [PubMed Link Image]
Enzyme 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 8626
Enzyme 60 Name 2-acylglycerol O-acyltransferase 2
Enzyme 60 Synonyms
  1. Acyl-CoA:monoacylglycerol acyltransferase 2
  2. MGAT2
  3. hMGAT2
  4. Diacylglycerol O-acyltransferase candidate 5
  5. hDC5
  6. Diacylglycerol acyltransferase 2-like protein 5
  7. Monoacylglycerol O-acyltransferase 2
Enzyme 60 Gene Name MOGAT2
Enzyme 60 Protein Sequence >2-acylglycerol O-acyltransferase 2
MVEFAPLFMPWERRLQTLAVLQFVFSFLALAEICTVGFIALLFTRFWLLTVLYAAWWYLD
RDKPRQGGRHIQAIRCWTIWKYMKDYFPISLVKTAELDPSRNYIAGFHPHGVLAVGAFAN
LCTESTGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKESAAHILNRKGGGNL
LGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSG
SWLRYIQNRLQKIMGISLPLFHGRGVFQYSFGLIPYRRPITTVVGKPIEVQKTLHPSEEE
VNQLHQRYIKELCNLFEAHKLKFNIPADQHLEFC
Enzyme 60 Number of Residues 334
Enzyme 60 Molecular Weight 38195.3
Enzyme 60 Theoretical pI 9.77
Enzyme 60 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 60 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 60 Specific Function Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity
Enzyme 60 Pathways
Enzyme 60 Reactions
  • acyl-CoA + 2-acylglycerol = CoA + diacylglycerol [RN:R01368]
Enzyme 60 Pfam Domain Function
Enzyme 60 Signals
  • None
Enzyme 60 Transmembrane Regions
  • 23-37 38-59 103-123
Enzyme 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein 37537527 Link Image
Enzyme 60 UniProtKB/Swiss-Prot ID Q3SYC2 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name MOGT2_HUMAN Link Image
Enzyme 60 PDB ID Not Available
Enzyme 60 Cellular Location Not Available
Enzyme 60 Gene Sequence >1005 bp
ATGGTAGAGTTCGCGCCCTTGTTTATGCCGTGGGAGCGCAGGCTGCAGACACTTGCTGTC
CTACAGTTTGTCTTCTCCTTCTTGGCACTGGCCGAGATCTGCACTGTGGGCTTCATAGCC
CTCCTGTTTACAAGATTCTGGCTCCTCACTGTCCTGTATGCGGCCTGGTGGTATCTGGAC
CGAGACAAGCCACGGCAGGGGGGCCGGCACATCCAGGCCATCAGGTGCTGGACTATATGG
AAGTACATGAAGGACTATTTCCCCATCTCGCTGGTCAAGACTGCTGAGCTGGACCCCTCT
CGGAACTACATTGCGGGCTTCCACCCCCATGGAGTCCTGGCAGTCGGAGCCTTTGCCAAC
CTGTGCACTGAGAGCACAGGCTTCTCTTCGATCTTCCCCGGTATCCGCCCCCATCTGATG
ATGCTGACCTTGTGGTTCCGGGCCCCCTTCTTCAGAGATTACATCATGTCTGCAGGGTTG
GTCACATCAGAAAAGGAGAGTGCTGCTCACATTCTGAACAGGAAGGGTGGCGGAAACTTG
CTGGGCATCATTGTAGGGGGTGCCCAGGAGGCCCTGGATGCCAGGCCTGGATCCTTCACG
CTGTTACTGCGGAACCGAAAGGGCTTCGTCAGGCTCGCCCTGACACACGGGGCACCCCTG
GTGCCAATCTTCTCCTTCGGGGAGAATGACCTATTTGACCAGATTCCCAACTCTTCTGGC
TCCTGGTTACGCTATATCCAGAATCGGTTGCAGAAGATCATGGGCATCTCCCTCCCACTC
TTTCATGGCCGTGGTGTCTTCCAGTACAGCTTTGGTTTAATACCCTACCGCCGGCCCATC
ACCACTGTGGTGGGGAAGCCCATCGAGGTACAGAAGACGCTGCATCCCTCGGAGGAGGAG
GTGAACCAGCTGCACCAGCGTTATATCAAAGAGCTGTGCAACCTCTTCGAGGCCCACAAA
CTTAAGTTCAACATCCCTGCTGACCAGCACTTGGAGTTCTGCTGA
Enzyme 60 GenBank Gene ID NM_025098.2 Link Image
Enzyme 60 GeneCard ID MOGAT2 Link Image
Enzyme 60 GenAtlas ID MOGAT2 Link Image
Enzyme 60 HGNC ID HGNC:23248 Link Image
Enzyme 60 Chromosome Location 1
Enzyme 60 Locus 11q13.5
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 General References
  1. Yen CL, Farese RV Jr: MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine. J Biol Chem. 2003 May 16;278(20):18532-7. Epub 2003 Mar 5. [PubMed Link Image]
  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. Lockwood JF, Cao J, Burn P, Shi Y: Human intestinal monoacylglycerol acyltransferase: differential features in tissue expression and activity. Am J Physiol Endocrinol Metab. 2003 Nov;285(5):E927-37. Epub 2003 Jun 24. [PubMed Link Image]
Enzyme 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 8715
Enzyme 61 Name Patatin-like phospholipase domain-containing protein 4
Enzyme 61 Synonyms
  1. Protein GS2
Enzyme 61 Gene Name PNPLA4
Enzyme 61 Protein Sequence >Patatin-like phospholipase domain-containing protein 4
MKHINLSFAACGFLGIYHLGAASALCRHGKKLVKDVKAFAGASAGSLVASVLLTAPEKIE
ECNQFTYKFAEEIRRQSFGAVTPGYDFMARLRSGMESILPPSAHELAQNRLHVSITNAKT
RENHLVSTFSSREDLIKVLLASSFVPIYAGLKLVEYKGQKWVDGGLTNALPILPVGRTVT
ISPFSGRLDISPQDKGQLDLYVNIAKQDIMLSLANLVRLNQALFPPSKRKMESLYQCGFD
DTVKFLLKENWFE
Enzyme 61 Number of Residues 253
Enzyme 61 Molecular Weight 27980.2
Enzyme 61 Theoretical pI 9.54
Enzyme 61 GO Classification
Function
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 61 General Function Involved in metabolic process
Enzyme 61 Specific Function Lipid hydrolase
Enzyme 61 Pathways Not Available
Enzyme 61 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • None
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein 158260799 Link Image
Enzyme 61 UniProtKB/Swiss-Prot ID P41247 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name PLPL4_HUMAN Link Image
Enzyme 61 PDB ID Not Available
Enzyme 61 Cellular Location Not Available
Enzyme 61 Gene Sequence >762 bp
ATGAAGCACATCAACCTATCATTTGCAGCGTGTGGATTTCTGGGCATTTACCACTTGGGG
GCAGCATCTGCACTTTGCAGACATGGCAAAAAACTTGTGAAGGATGTCAAAGCCTTCGCT
GGGGCGTCTGCGGGATCGTTGGTTGCTTCTGTTCTGCTAACAGCACCAGAAAAAATAGAG
GAATGTAACCAATTTACCTACAAGTTTGCCGAAGAAATCAGAAGGCAGTCTTTCGGGGCA
GTAACGCCCGGTTATGACTTCATGGCCCGACTAAGAAGTGGGATGGAGTCGATTCTTCCT
CCCAGCGCTCACGAGCTGGCCCAGAACCGACTGCACGTATCCATCACCAACGCCAAAACC
AGAGAAAATCACTTAGTCTCCACTTTTTCCTCCAGGGAGGACCTCATTAAGGTCCTCCTA
GCCAGCAGTTTTGTGCCCATTTATGCAGGACTGAAGCTAGTGGAATACAAAGGGCAGAAG
TGGGTGGACGGAGGCCTCACCAACGCTCTTCCCATCCTGCCCGTCGGCCGGACAGTAACC
ATCTCCCCCTTCAGTGGACGACTGGACATCTCCCCGCAGGACAAAGGGCAGCTAGATCTG
TATGTTAATATCGCCAAGCAGGATATCATGTTGTCCCTGGCAAACCTGGTGAGACTCAAC
CAAGCCCTTTTTCCCCCAAGCAAGAGGAAAATGGAATCTTTGTATCAGTGTGGTTTTGAT
GACACTGTTAAGTTTTTACTTAAAGAAAATTGGTTTGAATAA
Enzyme 61 GenBank Gene ID AK289888 Link Image
Enzyme 61 GeneCard ID PNPLA4 Link Image
Enzyme 61 GenAtlas ID PNPLA4 Link Image
Enzyme 61 HGNC ID HGNC:24887 Link Image
Enzyme 61 Chromosome Location Not Available
Enzyme 61 Locus Not Available
Enzyme 61 SNPs SNPJam Report Link Image
Enzyme 61 General References
  1. Lee WC, Salido E, Yen PH: Isolation of a new gene GS2 (DXS1283E) from a CpG island between STS and KAL1 on Xp22.3. Genomics. 1994 Jul 15;22(2):372-6. [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. Jenkins CM, Mancuso DJ, Yan W, Sims HF, Gibson B, Gross RW: Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J Biol Chem. 2004 Nov 19;279(47):48968-75. Epub 2004 Sep 10. [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 61 Metabolite References Not Available
Enzyme 62 [top]
Enzyme 62 ID 8976
Enzyme 62 Name CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
Enzyme 62 Synonyms
  1. Phosphatidylglycerophosphate synthase 1
  2. PGP synthase 1
Enzyme 62 Gene Name PGS1
Enzyme 62 Protein Sequence >CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
MAVAAAAAAGPVFWRRLLGLLPGRPGLAALLGRLSDRLGRNRDRQRRRSPWLLLAPLLSP
AVPQVTSPPCCLCPEGVHRFQWIRNLVPEFGVSSSHVRVLSSPAEFFELMKGQIRVAKRR
VVMASLYLGTGPLEQELVDCLESTLEKSLQAKFPSNLKVSILLDFTRGSRGRKNSRTMLL
PLLRRFPEQVRVSLFHTPHLRGLLRLLIPERFNETIGLQHIKVYLFDNSVILSGANLSDS
YFTNRQDRYVFLQDCAEIADFFTELVDAVGDVSLQLQGDDTVQVVDGMVHPYKGDRAEYC
KAANKRVMDVINSARTRQQMLHAQTFHSNSLLTQEDAAAAGDRRPAPDTWIYPLIQMKPF
EIQIDEIVTETLLTEAERGAKVYLTTGYFNLTQAYMDLVLGTRAEYQILLASPEVNGFFG
AKGVAGAIPAAYVHIERQFFSEVCSLGQQERVQLQEYWRRGWTFHAKGLWLYLAGSSLPC
LTLIGSPNFGYRSVHRDLEAQIAIVTENQALQQQLHQEQEQLYLRSGVVSSATFEQPSRQ
VKLWVKMVTPLIKNFF
Enzyme 62 Number of Residues 556
Enzyme 62 Molecular Weight 62729.7
Enzyme 62 Theoretical pI 9.11
Enzyme 62 GO Classification
Function
  • catalytic activity
  • phosphotransferase activity, for other substituted phosphate groups
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid biosynthetic process
  • phospholipid metabolic process
Component
Enzyme 62 General Function Involved in phosphotransferase activity, for other substituted phosphate groups
Enzyme 62 Specific Function Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin
Enzyme 62 Pathways Not Available
Enzyme 62 Reactions
  • CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate [RN:R01801]
Enzyme 62 Pfam Domain Function Not Available
Enzyme 62 Signals
  • None
Enzyme 62 Transmembrane Regions
  • None
Enzyme 62 Essentiality Not Available
Enzyme 62 GenBank ID Protein Not Available
Enzyme 62 UniProtKB/Swiss-Prot ID Q32NB8 Link Image
Enzyme 62 UniProtKB/Swiss-Prot Entry Name PGPS1_HUMAN Link Image
Enzyme 62 PDB ID Not Available
Enzyme 62 Cellular Location Not Available
Enzyme 62 Gene Sequence >1671 bp
ATGGCGGTGGCGGCGGCAGCTGCGGCGGGACCCGTGTTCTGGAGGCGACTGCTGGGCCTC
CTGCCTGGCCGCCCAGGGCTGGCCGCGCTCCTGGGACGCCTGTCCGACCGCCTCGGCAGG
AACCGGGACCGCCAGCGCAGGAGGTCACCATGGCTGTTATTGGCTCCCTTGCTGTCCCCA
GCTGTTCCCCAGGTCACCTCCCCACCTTGCTGCCTGTGTCCAGAAGGCGTGCACCGGTTC
CAGTGGATCAGAAACCTGGTTCCAGAATTTGGAGTCTCCAGTTCTCACGTTAGGGTGCTT
TCTTCCCCGGCAGAGTTTTTCGAGCTCATGAAGGGGCAGATAAGAGTAGCCAAGAGGCGG
GTCGTGATGGCATCCCTCTACCTGGGGACAGGTCCTTTGGAACAGGAGCTGGTGGACTGC
CTGGAAAGTACTCTAGAAAAGTCACTCCAAGCAAAGTTTCCTTCAAATCTCAAGGTCTCC
ATTCTCTTAGACTTCACGCGGGGCTCACGAGGTCGGAAGAACTCCCGCACAATGCTGCTC
CCACTCCTGCGGAGGTTCCCAGAGCAGGTCCGAGTCTCCCTCTTTCACACGCCGCACCTC
CGTGGGCTGCTTCGGCTCCTCATCCCTGAGCGCTTCAACGAGACCATCGGCCTCCAGCAC
ATTAAGGTGTACCTCTTCGACAACAGCGTCATCTTGAGCGGTGCAAACCTGAGTGACTCC
TACTTCACCAACCGCCAGGACCGCTACGTGTTCCTGCAGGACTGTGCGGAGATTGCCGAC
TTCTTCACGGAGCTGGTGGACGCGGTGGGGGATGTGTCCCTGCAGCTGCAGGGGGACGAC
ACGGTGCAGGTGGTGGATGGGATGGTGCATCCTTACAAAGGGGACCGGGCCGAGTACTGC
AAGGCAGCCAATAAGAGGGTCATGGATGTGATCAACTCAGCCAGGACCCGCCAGCAGATG
CTGCATGCCCAGACCTTCCACAGCAACTCTCTTTTGACCCAGGAAGATGCAGCAGCTGCT
GGGGATCGCAGACCAGCCCCTGACACCTGGATTTATCCGCTGATTCAGATGAAGCCCTTC
GAGATTCAAATCGATGAGATTGTCACTGAGACCCTGTTGACTGAGGCGGAGCGCGGGGCA
AAGGTCTACCTCACCACTGGCTATTTCAACCTGACCCAGGCCTACATGGACCTGGTCTTG
GGCACTCGGGCTGAGTACCAGATCCTGCTGGCCTCACCAGAGGTGAATGGCTTCTTTGGG
GCCAAGGGGGTGGCCGGCGCCATCCCAGCGGCCTATGTGCACATCGAGCGACAGTTCTTC
AGTGAGGTGTGCAGCCTGGGACAGCAGGAGCGGGTCCAGCTTCAGGAGTACTGGCGGAGG
GGCTGGACGTTCCACGCCAAAGGCCTCTGGCTGTACCTGGCAGGGAGCAGCCTGCCCTGT
CTCACGCTGATTGGCTCTCCTAATTTTGGGTACAGGTCAGTTCACCGGGACCTGGAGGCC
CAGATTGCGATCGTGACGGAGAACCAGGCCCTGCAGCAGCAGCTTCACCAGGAGCAAGAG
CAGCTCTACCTGAGGTCAGGTGTGGTGTCCTCTGCCACCTTCGAGCAGCCGAGTCGCCAG
GTGAAGCTGTGGGTGAAGATGGTGACTCCACTGATCAAGAACTTCTTCTGA
Enzyme 62 GenBank Gene ID AK316147 Link Image
Enzyme 62 GeneCard ID PGS1 Link Image
Enzyme 62 GenAtlas ID PGS1 Link Image
Enzyme 62 HGNC ID HGNC:30029 Link Image
Enzyme 62 Chromosome Location 1
Enzyme 62 Locus 17q25.3
Enzyme 62 SNPs SNPJam Report Link Image
Enzyme 62 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]
Enzyme 62 Metabolite References Not Available
Enzyme 63 [top]
Enzyme 63 ID 9821
Enzyme 63 Name Diacylglycerol kinase eta
Enzyme 63 Synonyms
  1. DAG kinase eta
  2. Diglyceride kinase eta
  3. DGK-eta
Enzyme 63 Gene Name DGKH
Enzyme 63 Protein Sequence >Diacylglycerol kinase eta
MAGAGGQHHPPGAAGGAAAGAGAAVTSAAASAGPGEDSSDSEAEQEGPQKLIRKVSTSGQ
IRTKTSIKEGQLLKQTSSFQRWKKRYFKLRGRTLYYAKDSKSLIFDEVDLSDASVAEAST
KNANNSFTIITPFRRLMLCAENRKEMEDWISSLKSVQTREPYEVAQFNVEHFSGMHNWYA
CSHARPTFCNVCRESLSGVTSHGLSCEVCKFKAHKRCAVRATNNCKWTTLASIGKDIIED
EDGVAMPHQWLEGNLPVSAKCAVCDKTCGSVLRLQDWKCLWCKTMVHTACKDLYHPICPL
GQCKVSIIPPIALNSTDSDGFCRATFSFCVSPLLVFVNSKSGDNQGVKFLRRFKQLLNPA
QVFDLMNGGPHLGLRLFQKFDNFRILVCGGDGSVGWVLSEIDKLNLNKQCQLGVLPLGTG
NDLARVLGWGGSYDDDTQLPQILEKLERASTKMLDRWSIMTYELKLPPKASLLPGPPEAS
EEFYMTIYEDSVATHLTKILNSDEHAVVISSAKTLCETVKDFVAKVEKTYDKTLENAVVA
DAVASKCSVLNEKLEQLLQALHTDSQAAPVLPGLSPLIVEEDAVESSSEESLGESKEQLG
DDVTKPSSQKAVKPREIMLRANSLKKAVRQVIEEAGKVMDDPTVHPCEPANQSSDYDSTE
TDESKEEAKDDGAKESITVKTAPRSPDARASYGHSQTDSVPGPAVAASKENLPVLNTRII
CPGLRAGLAASIAGSSIINKMLLANIDPFGATPFIDPDLDSVDGYSEKCVMNNYFGIGLD
AKISLEFNNKREEHPEKCRSRTKNLMWYGVLGTRELLQRSYKNLEQRVQLECDGQYIPLP
SLQGIAVLNIPSYAGGTNFWGGTKEDDIFAAPSFDDKILEVVAIFDSMQMAVSRVIKLQH
HRIAQCRTVKITIFGDEGVPVQVDGEAWVQPPGIIKIVHKNRAQMLTRDRAFESTLKSWE
DKQKCDSGKPVLRTHLYIHHAIDLATEEVSQMQLCSQAAEELITRICDAATIHCLLEQEL
AHAVNACSHALNKANPRCPESLTRDTATEIAINVKALYNETESLLVGRVPLQLESPHEER
VSNALHSVEVELQKLTEIPWLYYILHPNEDEEPPMDCTKRNNRSTVFRIVPKFKKEKVQK
QKTSSQPVQKWGTEEVAAWLDLLNLGEYKDIFIRHDIRGAELLHLERRDLKDLGIPKVGH
VKRILQGIKELGRSTPQSEV
Enzyme 63 Number of Residues 1220
Enzyme 63 Molecular Weight 134864.3
Enzyme 63 Theoretical pI 6.51
Enzyme 63 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 63 General Function Involved in diacylglycerol kinase activity
Enzyme 63 Specific Function Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA)
Enzyme 63 Pathways
Enzyme 63 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 63 Pfam Domain Function
Enzyme 63 Signals
  • None
Enzyme 63 Transmembrane Regions
  • None
Enzyme 63 Essentiality Not Available
Enzyme 63 GenBank ID Protein 29788751 Link Image
Enzyme 63 UniProtKB/Swiss-Prot ID Q86XP1 Link Image
Enzyme 63 UniProtKB/Swiss-Prot Entry Name DGKH_HUMAN Link Image
Enzyme 63 PDB ID 1R79 Link Image
Enzyme 63 PDB File Show
Enzyme 63 3D Structure
Enzyme 63 Cellular Location Not Available
Enzyme 63 Gene Sequence >3663 bp
ATGGCAGGGGCCGGAGGCCAGCACCACCCTCCGGGCGCCGCTGGAGGAGCGGCCGCCGGA
GCCGGCGCCGCGGTCACCTCCGCCGCTGCCTCGGCGGGGCCGGGAGAGGATTCGTCTGAC
AGCGAAGCGGAGCAAGAGGGACCCCAGAAACTGATCCGCAAAGTGTCTACCTCGGGGCAG
ATCCGGACCAAGACCAGTATTAAAGAGGGACAGCTATTGAAGCAAACCAGTTCTTTCCAA
AGGTGGAAAAAGCGATACTTCAAACTTCGAGGCCGCACCCTTTACTATGCAAAGGACTCA
AAGTCTCTGATATTTGATGAAGTTGACCTCTCAGATGCTAGTGTAGCTGAAGCAAGCACG
AAAAATGCTAACAACAGCTTCACGATCATCACTCCATTCAGAAGGCTAATGCTGTGTGCT
GAGAACAGAAAGGAGATGGAGGATTGGATCAGCTCACTGAAGTCTGTACAGACCAGAGAA
CCCTACGAGGTGGCCCAGTTTAATGTGGAACATTTCTCAGGGATGCACAACTGGTACGCC
TGCTCCCACGCCCGACCCACCTTCTGTAACGTGTGCAGAGAGAGTCTTTCTGGAGTCACC
TCCCATGGCCTGTCCTGCGAAGTGTGTAAATTCAAGGCTCACAAAAGATGTGCAGTGAGA
GCAACAAATAACTGTAAATGGACTACCCTGGCCTCCATCGGGAAGGACATTATAGAAGAT
GAAGATGGCGTCGCGATGCCTCACCAGTGGCTTGAGGGCAACCTGCCTGTAAGTGCCAAG
TGTGCTGTCTGCGACAAAACATGTGGCAGTGTTCTCCGTCTACAGGATTGGAAATGCCTT
TGGTGTAAGACAATGGTACACACTGCCTGCAAAGATTTATACCATCCAATATGTCCACTT
GGTCAATGTAAAGTATCTATCATACCTCCAATTGCACTAAACAGCACCGATTCCGATGGT
TTCTGTAGAGCAACATTTTCGTTCTGTGTTAGTCCTCTATTGGTTTTTGTCAATTCTAAG
AGTGGAGATAATCAGGGAGTAAAGTTCCTCCGTCGCTTTAAACAGTTGCTAAATCCGGCT
CAGGTGTTTGATTTAATGAATGGAGGTCCTCATTTAGGTTTAAGATTATTTCAGAAGTTT
GACAATTTCCGGATTCTTGTTTGTGGAGGCGATGGAAGTGTAGGTTGGGTTTTGTCAGAA
ATCGATAAGCTCAACTTGAATAAACAGTGTCAGCTGGGAGTGTTGCCTTTGGGTACAGGA
AATGACCTTGCCCGAGTTCTTGGCTGGGGAGGTTCATATGACGATGACACCCAACTTCCT
CAGATCCTAGAGAAACTGGAACGAGCCAGTACCAAAATGTTGGACAGGTGGAGTATAATG
ACATATGAACTCAAATTGCCACCAAAAGCTTCCCTACTTCCAGGACCTCCAGAAGCATCT
GAAGAATTTTATATGACGATTTATGAAGACTCAGTTGCAACGCATCTTACAAAAATCCTC
AATTCTGATGAACATGCAGTGGTCATATCTTCTGCCAAGACGCTATGTGAAACTGTAAAG
GACTTCGTTGCCAAAGTAGAAAAGACGTATGACAAAACCTTGGAAAATGCCGTTGTAGCT
GATGCCGTGGCCAGTAAATGTTCAGTCCTAAACGAGAAGCTCGAACAACTGCTGCAGGCT
TTGCACACAGATTCCCAGGCTGCGCCTGTTCTCCCTGGCCTCAGCCCTCTCATTGTGGAA
GAAGATGCTGTGGAATCGTCCAGTGAAGAGTCCCTGGGTGAAAGCAAAGAGCAGCTTGGG
GATGACGTTACAAAACCTTCCTCCCAGAAAGCCGTCAAACCAAGGGAAATCATGTTGCGG
GCAAATAGTTTAAAGAAAGCAGTGAGGCAAGTCATTGAGGAAGCCGGAAAAGTTATGGAT
GACCCGACAGTTCACCCCTGTGAACCAGCTAATCAGTCCTCTGATTATGACAGCACAGAA
ACAGATGAATCTAAGGAGGAAGCTAAAGATGATGGTGCCAAAGAATCAATAACTGTTAAA
ACTGCACCTCGGTCTCCAGATGCCCGGGCAAGTTATGGCCATTCCCAAACTGATTCTGTC
CCTGGTCCAGCTGTGGCAGCCAGCAAAGAAAACCTCCCTGTGCTCAATACCAGAATAATC
TGCCCAGGTTTAAGAGCAGGACTGGCTGCCTCAATTGCTGGGAGTTCGATTATCAACAAA
ATGTTACTGGCAAACATTGATCCTTTTGGTGCCACGCCGTTTATTGACCCGGATCTAGAT
TCCGTAGATGGATATTCAGAAAAATGTGTCATGAACAATTACTTTGGGATTGGATTAGAT
GCAAAAATTTCATTAGAATTTAATAATAAAAGAGAGGAGCACCCTGAAAAATGCAGGAGC
CGAACTAAAAACTTGATGTGGTATGGAGTCCTTGGAACCCGGGAGTTATTACAGAGATCG
TACAAGAATTTAGAACAAAGGGTTCAACTTGAGTGTGATGGGCAGTATATTCCTCTTCCC
AGCTTGCAAGGCATAGCCGTGTTGAACATTCCCAGCTATGCTGGAGGCACTAACTTTTGG
GGTGGAACTAAAGAGGATGATATATTTGCTGCACCATCCTTTGATGACAAGATCCTGGAA
GTTGTAGCAATATTTGATAGCATGCAAATGGCAGTTTCAAGGGTCATTAAACTGCAGCAT
CATCGAATAGCCCAGTGCCGTACAGTGAAAATCACTATATTTGGTGACGAAGGAGTCCCA
GTGCAAGTGGATGGTGAAGCGTGGGTTCAGCCTCCAGGGATTATCAAAATTGTGCACAAA
AACAGAGCACAAATGCTAACAAGGGACAGAGCCTTTGAGAGCACTCTGAAATCTTGGGAA
GATAAGCAGAAGTGTGATTCTGGTAAACCAGTTCTCCGAACCCATTTGTACATCCATCAC
GCCATTGACTTGGCAACAGAAGAGGTGTCGCAGATGCAGCTATGCTCCCAGGCTGCAGAG
GAGCTCATTACTAGGATATGTGACGCAGCCACAATTCACTGTCTTTTGGAGCAAGAACTG
GCCCATGCTGTGAATGCCTGCTCCCATGCCCTGAATAAAGCCAACCCAAGGTGCCCGGAG
AGTCTTACAAGAGACACTGCCACTGAAATAGCCATCAATGTGAAGGCGCTGTATAATGAA
ACAGAATCTTTGCTAGTTGGCAGGGTTCCTTTGCAGCTGGAATCGCCACATGAAGAGCGA
GTATCCAATGCCTTACACTCTGTGGAGGTGGAATTACAGAAACTGACAGAGATTCCTTGG
CTTTATTATATCTTACACCCAAATGAGGATGAGGAACCTCCTATGGATTGCACCAAAAGG
AACAACAGAAGCACCGTATTTCGAATAGTGCCAAAGTTTAAAAAGGAAAAGGTTCAGAAG
CAGAAGACAAGTTCACAGCCTGTTCAGAAATGGGGCACAGAGGAAGTTGCTGCTTGGCTG
GATCTGCTCAATTTGGGAGAGTACAAAGATATCTTCATCCGTCATGACATCAGAGGGGCT
GAACTTTTGCATCTGGAAAGGCGAGATCTTAAGGATCTGGGGATACCGAAAGTGGGTCAT
GTGAAGCGAATTCTCCAGGGAATTAAAGAGCTTGGAAGGAGCACTCCACAGTCGGAGGTG
TAA
Enzyme 63 GenBank Gene ID NM_178009.2 Link Image
Enzyme 63 GeneCard ID DGKH Link Image
Enzyme 63 GenAtlas ID DGKH Link Image
Enzyme 63 HGNC ID HGNC:2854 Link Image
Enzyme 63 Chromosome Location 1
Enzyme 63 Locus 13q14.11
Enzyme 63 SNPs SNPJam Report Link Image
Enzyme 63 General References
  1. Murakami T, Sakane F, Imai S, Houkin K, Kanoh H: Identification and characterization of two splice variants of human diacylglycerol kinase eta. J Biol Chem. 2003 Sep 5;278(36):34364-72. Epub 2003 Jun 16. [PubMed Link Image]
  2. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 63 Metabolite References Not Available
Enzyme 64 [top]
Enzyme 64 ID 10047
Enzyme 64 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
Enzyme 64 Synonyms
  1. hPLCD4
  2. Phosphoinositide phospholipase C-delta-4
  3. Phospholipase C-delta-4
  4. PLC-delta-4
Enzyme 64 Gene Name PLCD4
Enzyme 64 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
MASLLQDQLTTDQDLLLMQEGMPMRKVRSKSWKKLRYFRLQNDGMTVWHARQARGSAKPS
FSISDVETIRNGHDSELLRSLAEELPLEQGFTIVFHGRRSNLDLMANSVEEAQIWMRGLQ
LLVDLVTSMDHQERLDQWLSDWFQRGDKNQDGKMSFQEVQRLLHLMNVEMDQEYAFSLFQ
AADTSQSGTLEGEEFVQFYKALTKRAEVQELFESFSADGQKLTLLEFLDFLQEEQKERDC
TSELALELIDRYEPSDSGKLRHVLSMDGFLSYLCSKDGDIFNPACLPIYQDMTQPLNHYF
ICSSHNTYLVGDQLCGQSSVEGYIRALKRGCRCVEVDVWDGPSGEPVVYHGHTLTSRILF
KDVVATVAQYAFQTSDYPVILSLETHCSWEQQQTMARHLTEILGEQLLSTTLDGVLPTQL
PSPEELRRKILVKGKKLTLEEDLEYEEEEAEPELEESELALESQFETEPEPQEQNLQNKD
KKKKSKPILCPALSSLVIYLKSVSFRSFTHSKEHYHFYEISSFSETKAKRLIKEAGNEFV
QHNTWQLSRVYPSGLRTDSSNYNPQELWNAGCQMVAMNMQTAGLEMDICDGHFRQNGGCG
YVLKPDFLRDIQSSFHPEKPISPFKAQTLLIQVISGQQLPKVDKTKEGSIVDPLVKVQIF
GVRLDTARQETNYVENNGFNPYWGQTLCFRVLVPELAMLRFVVMDYDWKSRNDFIGQYTL
PWTCMQQGYRHIHLLSKDGISLRPASIFVYICIQEGLEGDES
Enzyme 64 Number of Residues 762
Enzyme 64 Molecular Weight 87584.5
Enzyme 64 Theoretical pI 4.85
Enzyme 64 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 64 General Function Involved in calcium ion binding
Enzyme 64 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 64 Pathways
Enzyme 64 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 64 Pfam Domain Function
Enzyme 64 Signals
  • None
Enzyme 64 Transmembrane Regions
  • None
Enzyme 64 Essentiality Not Available
Enzyme 64 GenBank ID Protein 62897967 Link Image
Enzyme 64 UniProtKB/Swiss-Prot ID Q9BRC7 Link Image
Enzyme 64 UniProtKB/Swiss-Prot Entry Name PLCD4_HUMAN Link Image
Enzyme 64 PDB ID Not Available
Enzyme 64 Cellular Location Not Available
Enzyme 64 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 64 GenBank Gene ID AK223203 Link Image
Enzyme 64 GeneCard ID PLCD4 Link Image
Enzyme 64 GenAtlas ID PLCD4 Link Image
Enzyme 64 HGNC ID HGNC:9062 Link Image
Enzyme 64 Chromosome Location 2
Enzyme 64 Locus 2q35
Enzyme 64 SNPs SNPJam Report Link Image
Enzyme 64 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 64 Metabolite References Not Available
Enzyme 65 [top]
Enzyme 65 ID 10048
Enzyme 65 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-1
Enzyme 65 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 65 Gene Name PLCH1
Enzyme 65 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 65 Number of Residues 1693
Enzyme 65 Molecular Weight 189221.5
Enzyme 65 Theoretical pI 7.79
Enzyme 65 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 65 General Function Involved in calcium ion binding
Enzyme 65 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 65 Pathways Not Available
Enzyme 65 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 65 Pfam Domain Function
Enzyme 65 Signals
  • None
Enzyme 65 Transmembrane Regions
  • None
Enzyme 65 Essentiality Not Available
Enzyme 65 GenBank ID Protein 195972871 Link Image
Enzyme 65 UniProtKB/Swiss-Prot ID Q4KWH8 Link Image
Enzyme 65 UniProtKB/Swiss-Prot Entry Name PLCH1_HUMAN Link Image
Enzyme 65 PDB ID Not Available
Enzyme 65 Cellular Location Not Available
Enzyme 65 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 65 GenBank Gene ID NM_001130960.1 Link Image
Enzyme 65 GeneCard ID PLCH1 Link Image
Enzyme 65 GenAtlas ID PLCH1 Link Image
Enzyme 65 HGNC ID HGNC:29185 Link Image
Enzyme 65 Chromosome Location 3
Enzyme 65 Locus 3q25.31
Enzyme 65 SNPs SNPJam Report Link Image
Enzyme 65 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 65 Metabolite References Not Available
Enzyme 66 [top]
Enzyme 66 ID 10049
Enzyme 66 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1
Enzyme 66 Synonyms
  1. Pancreas-enriched phospholipase C
  2. Phosphoinositide phospholipase C-epsilon-1
  3. Phospholipase C-epsilon-1
  4. PLC-epsilon-1
Enzyme 66 Gene Name PLCE1
Enzyme 66 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 66 Number of Residues 2302
Enzyme 66 Molecular Weight 258712.3
Enzyme 66 Theoretical pI 6.44
Enzyme 66 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 66 General Function Involved in calcium ion binding
Enzyme 66 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 66 Pathways
Enzyme 66 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 66 Pfam Domain Function
Enzyme 66 Signals
  • None
Enzyme 66 Transmembrane Regions
  • None
Enzyme 66 Essentiality Not Available
Enzyme 66 GenBank ID Protein 117168250 Link Image
Enzyme 66 UniProtKB/Swiss-Prot ID Q9P212 Link Image
Enzyme 66 UniProtKB/Swiss-Prot Entry Name PLCE1_HUMAN Link Image
Enzyme 66 PDB ID Not Available
Enzyme 66 Cellular Location Not Available
Enzyme 66 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 66 GenBank Gene ID NM_016341.3 Link Image
Enzyme 66 GeneCard ID PLCE1 Link Image
Enzyme 66 GenAtlas ID PLCE1 Link Image
Enzyme 66 HGNC ID HGNC:17175 Link Image
Enzyme 66 Chromosome Location 1
Enzyme 66 Locus 10q23
Enzyme 66 SNPs SNPJam Report Link Image
Enzyme 66 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 66 Metabolite References Not Available
Enzyme 67 [top]
Enzyme 67 ID 10050
Enzyme 67 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
Enzyme 67 Synonyms
  1. Phosphoinositide phospholipase C-delta-3
  2. Phospholipase C-delta-3
  3. PLC-delta-3
Enzyme 67 Gene Name PLCD3
Enzyme 67 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 67 Number of Residues 789
Enzyme 67 Molecular Weight 89257.5
Enzyme 67 Theoretical pI 6.97
Enzyme 67 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 67 General Function Involved in calcium ion binding
Enzyme 67 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 67 Pathways
Enzyme 67 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 67 Pfam Domain Function
Enzyme 67 Signals
  • None
Enzyme 67 Transmembrane Regions
  • None
Enzyme 67 Essentiality Not Available
Enzyme 67 GenBank ID Protein Not Available
Enzyme 67 UniProtKB/Swiss-Prot ID Q8N3E9 Link Image
Enzyme 67 UniProtKB/Swiss-Prot Entry Name PLCD3_HUMAN Link Image
Enzyme 67 PDB ID Not Available
Enzyme 67 Cellular Location Not Available
Enzyme 67 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 67 GenBank Gene ID AK074240 Link Image
Enzyme 67 GeneCard ID PLCD3 Link Image
Enzyme 67 GenAtlas ID PLCD3 Link Image
Enzyme 67 HGNC ID HGNC:9061 Link Image
Enzyme 67 Chromosome Location 1
Enzyme 67 Locus 17q21.31
Enzyme 67 SNPs SNPJam Report Link Image
Enzyme 67 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 67 Metabolite References Not Available
Enzyme 68 [top]
Enzyme 68 ID 10076
Enzyme 68 Name Diacylglycerol O-acyltransferase 2
Enzyme 68 Synonyms
  1. Diglyceride acyltransferase 2
Enzyme 68 Gene Name DGAT2
Enzyme 68 Protein Sequence >Diacylglycerol O-acyltransferase 2
MKTLIAAYSGVLRGERQAEADRSQRSHGGPALSREGSGRWGTGSSILSALQDLFSVTWLN
RSKVEKQLQVISVLQWVLSFLVLGVACSAILMYIFCTDCWLIAVLYFTWLVFDWNTPKKG
GRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATE
VSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVSRDTIDYLLSKNGSGNAIIIVVGG
AAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPIYSFGENEVYKQVIFEEGSWGRWVQ
KKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITIPKLEHPTQQDIDLYHT
MYMEALVKLFDKHKTKFGLPETEVLEVN
Enzyme 68 Number of Residues 388
Enzyme 68 Molecular Weight 43830.5
Enzyme 68 Theoretical pI 9.80
Enzyme 68 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 68 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 68 Specific Function Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation
Enzyme 68 Pathways
Enzyme 68 Reactions
  • acyl-CoA + 1,2-diacyl-sn-glycerol = CoA + triacylglycerol [RN:R02251]
Enzyme 68 Pfam Domain Function
Enzyme 68 Signals
  • None
Enzyme 68 Transmembrane Regions
  • 76-96 98-117
Enzyme 68 Essentiality Not Available
Enzyme 68 GenBank ID Protein 22506631 Link Image
Enzyme 68 UniProtKB/Swiss-Prot ID Q96PD7 Link Image
Enzyme 68 UniProtKB/Swiss-Prot Entry Name DGAT2_HUMAN Link Image
Enzyme 68 PDB ID Not Available
Enzyme 68 Cellular Location Not Available
Enzyme 68 Gene Sequence >1167 bp
ATGAAGACCCTCATAGCCGCCTACTCCGGGGTCCTGCGCGGCGAGCGTCAGGCCGAGGCT
GACCGGAGCCAGCGCTCTCACGGAGGACCTGCGCTGTCGCGCGAGGGGTCTGGGAGATGG
GGCACTGGATCCAGCATCCTCTCCGCCCTCCAGGACCTCTTCTCTGTCACCTGGCTCAAT
AGGTCCAAGGTGGAAAAGCAGCTACAGGTCATCTCAGTGCTCCAGTGGGTCCTGTCCTTC
CTTGTACTGGGAGTGGCCTGCAGTGCCATCCTCATGTACATATTCTGCACTGATTGCTGG
CTCATCGCTGTGCTCTACTTCACTTGGCTGGTGTTTGACTGGAACACACCCAAGAAAGGT
GGCAGGAGGTCACAGTGGGTCCGAAACTGGGCTGTGTGGCGCTACTTTCGAGACTACTTT
CCCATCCAGCTGGTGAAGACACACAACCTGCTGACCACCAGGAACTATATCTTTGGATAC
CACCCCCATGGTATCATGGGCCTGGGTGCCTTCTGCAACTTCAGCACAGAGGCCACAGAA
GTGAGCAAGAAGTTCCCAGGCATACGGCCTTACCTGGCTACACTGGCAGGCAACTTCCGA
ATGCCTGTGTTGAGGGAGTACCTGATGTCTGGAGGTATCTGCCCTGTCAGCCGGGACACC
ATAGACTATTTGCTTTCAAAGAATGGGAGTGGCAATGCTATCATCATCGTGGTCGGGGGT
GCGGCTGAGTCTCTGAGCTCCATGCCTGGCAAGAATGCAGTCACCCTGCGGAACCGCAAG
GGCTTTGTGAAACTGGCCCTGCGTCATGGAGCTGACCTGGTTCCCATCTACTCCTTTGGA
GAGAATGAAGTGTACAAGCAGGTGATCTTCGAGGAGGGCTCCTGGGGCCGATGGGTCCAG
AAGAAGTTCCAGAAATACATTGGTTTCGCCCCATGCATCTTCCATGGTCGAGGCCTCTTC
TCCTCCGACACCTGGGGGCTGGTGCCCTACTCCAAGCCCATCACCACTGTTGTGGGAGAG
CCCATCACCATCCCCAAGCTGGAGCACCCAACCCAGCAAGACATCGACCTGTACCACACC
ATGTACATGGAGGCCCTGGTGAAGCTCTTCGACAAGCACAAGACCAAGTTCGGCCTCCCG
GAGACTGAGGTCCTGGAGGTGAACTGA
Enzyme 68 GenBank Gene ID AB048286 Link Image
Enzyme 68 GeneCard ID DGAT2 Link Image
Enzyme 68 GenAtlas ID DGAT2 Link Image
Enzyme 68 HGNC ID HGNC:16940 Link Image
Enzyme 68 Chromosome Location 1
Enzyme 68 Locus 11q13.5
Enzyme 68 SNPs SNPJam Report Link Image
Enzyme 68 General References
  1. Cases S, Stone SJ, Zhou P, Yen E, Tow B, Lardizabal KD, Voelker T, Farese RV Jr: Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members. J Biol Chem. 2001 Oct 19;276(42):38870-6. Epub 2001 Jul 31. [PubMed Link Image]
  2. Wakimoto K, Chiba H, Michibata H, Seishima M, Kawasaki S, Okubo K, Mitsui H, Torii H, Imai Y: A novel diacylglycerol acyltransferase (DGAT2) is decreased in human psoriatic skin and increased in diabetic mice. Biochem Biophys Res Commun. 2003 Oct 17;310(2):296-302. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. 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. 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]
  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. Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A: Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene. 2004 Aug 5;23(35):5901-11. [PubMed Link Image]
Enzyme 68 Metabolite References Not Available
Enzyme 69 [top]
Enzyme 69 ID 10239
Enzyme 69 Name 2-acylglycerol O-acyltransferase 1
Enzyme 69 Synonyms
  1. Acyl-CoA:monoacylglycerol acyltransferase 1
  2. MGAT1
  3. Diacylglycerol O-acyltransferase candidate 2
  4. hDC2
  5. Diacylglycerol acyltransferase 2-like protein 1
  6. Monoacylglycerol O-acyltransferase 1
Enzyme 69 Gene Name MOGAT1
Enzyme 69 Protein Sequence >2-acylglycerol O-acyltransferase 1
MKVEFAPLNIQLARRLQTVAVLQWVLKYLLLGPMSIGITVMLIIHNYLFLYIPYLMWLYF
DWHTPERGGRRSSWIKNWTLWKHFKDYFPIHLIKTQDLDPSHNYIFGFHPHGIMAVGAFG
NFSVNYSDFKDLFPGFTSYLHVLPLWFWCPVFREYVMSVGLVSVSKKSVSYMVSKEGGGN
ISVIVLGGAKESLDAHPGKFTLFIRQRKGFVKIALTHGASLVPVVSFGENELFKQTDNPE
GSWIRTVQNKLQKIMGFALPLFHARGVFQYNFGLMTYRKAIHTVVGRPIPVRQTLNPTQE
QIEELHQTYMEELRKLFEEHKGKYGIPEHETLVLK
Enzyme 69 Number of Residues 335
Enzyme 69 Molecular Weight 38812.2
Enzyme 69 Theoretical pI 9.96
Enzyme 69 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 69 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 69 Specific Function Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Probably not involved in absorption of dietary fat in the small intestine
Enzyme 69 Pathways
Enzyme 69 Reactions
  • acyl-CoA + 2-acylglycerol = CoA + diacylglycerol [RN:R01368]
Enzyme 69 Pfam Domain Function
Enzyme 69 Signals
  • None
Enzyme 69 Transmembrane Regions
  • 18-38 40-60 132-152
Enzyme 69 Essentiality Not Available
Enzyme 69 GenBank ID Protein 148746191 Link Image
Enzyme 69 UniProtKB/Swiss-Prot ID Q96PD6 Link Image
Enzyme 69 UniProtKB/Swiss-Prot Entry Name MOGT1_HUMAN Link Image
Enzyme 69 PDB ID Not Available
Enzyme 69 Cellular Location Not Available
Enzyme 69 Gene Sequence >1008 bp
ATGAAGGTAGAGTTTGCACCGCTCAACATCCAGCTGGCGCGGCGGCTGCAGACGGTGGCC
GTGCTGCAGTGGGTCCTGAAATACCTGCTGCTCGGGCCGATGTCCATTGGAATCACTGTG
ATGCTGATCATACACAACTATTTGTTCCTTTACATCCCTTATTTGATGTGGCTTTACTTT
GACTGGCATACCCCAGAGCGAGGAGGCAGGAGATCCAGCTGGATCAAAAATTGGACTCTT
TGGAAACACTTTAAGGACTATTTTCCAATTCATCTTATCAAAACTCAAGATTTGGATCCA
AGTCACAACTATATATTTGGGTTTCACCCCCATGGAATAATGGCAGTTGGAGCCTTTGGG
AATTTTTCTGTAAATTATTCTGACTTCAAGGACCTGTTTCCTGGCTTTACTTCATATCTT
CACGTGCTGCCACTTTGGTTCTGGTGTCCTGTCTTTCGAGAATATGTGATGAGTGTTGGG
CTGGTTTCAGTTTCCAAGAAAAGTGTGTCCTACATGGTAAGCAAGGAGGGAGGTGGAAAC
ATCTCTGTCATTGTCCTTGGGGGTGCAAAAGAATCACTGGATGCTCATCCTGGAAAGTTC
ACTCTGTTCATCCGCCAGCGGAAAGGATTTGTTAAAATTGCTTTGACCCATGGCGCCTCT
CTGGTCCCAGTGGTTTCTTTTGGTGAAAATGAACTGTTTAAACAAACTGACAACCCTGAA
GGATCATGGATTAGAACTGTTCAGAATAAACTGCAGAAGATCATGGGGTTTGCTTTGCCC
CTGTTTCATGCCAGGGGAGTTTTTCAGTACAATTTTGGCCTAATGACCTATAGGAAAGCC
ATCCACACTGTTGTTGGCCGCCCGATCCCTGTTCGTCAGACTCTGAACCCGACCCAGGAG
CAGATTGAGGAGTTACATCAGACCTATATGGAGGAACTTAGGAAATTGTTTGAGGAACAC
AAAGGAAAGTATGGCATTCCAGAGCACGAGACTCTTGTTTTAAAATGA
Enzyme 69 GenBank Gene ID NM_058165.2 Link Image
Enzyme 69 GeneCard ID MOGAT1 Link Image
Enzyme 69 GenAtlas ID MOGAT1 Link Image
Enzyme 69 HGNC ID HGNC:18210 Link Image
Enzyme 69 Chromosome Location 2
Enzyme 69 Locus 2q36.1
Enzyme 69 SNPs SNPJam Report Link Image
Enzyme 69 General References
  1. Cases S, Stone SJ, Zhou P, Yen E, Tow B, Lardizabal KD, Voelker T, Farese RV Jr: Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members. J Biol Chem. 2001 Oct 19;276(42):38870-6. Epub 2001 Jul 31. [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. Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed Link Image]
Enzyme 69 Metabolite References Not Available
Enzyme 70 [top]
Enzyme 70 ID 12897
Enzyme 70 Name Acyl-CoA wax alcohol acyltransferase 1
Enzyme 70 Synonyms
  1. Diacylglycerol O-acyltransferase 2-like protein 3
  2. Diacylglycerol acyltransferase 2
  3. Long-chain-alcohol O-fatty-acyltransferase 1
Enzyme 70 Gene Name AWAT1
Enzyme 70 Protein Sequence >Acyl-CoA wax alcohol acyltransferase 1
MAHSKQPSHFQSLMLLQWPLSYLAIFWILQPLFVYLLFTSLWPLPVLYFAWLFLDWKTPE
RGGRRSAWVRNWCVWTHIRDYFPITILKTKDLSPEHNYLMGVHPHGLLTFGAFCNFCTEA
TGFSKTFPGITPHLATLSWFFKIPFVREYLMAKGVCSVSQPAINYLLSHGTGNLVGIVVG
GVGEALQSVPNTTTLILQKRKGFVRTALQHGAHLVPTFTFGETEVYDQVLFHKDSRMYKF
QSCFRRIFGFYCCVFYGQSFCQGSTGLLPYSRPIVTVVGEPLPLPQIEKPSQEMVDKYHA
LYMDALHKLFDQHKTHYGCSETQKLFFL
Enzyme 70 Number of Residues 328
Enzyme 70 Molecular Weight 37758.8
Enzyme 70 Theoretical pI 9.02
Enzyme 70 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 70 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 70 Specific Function Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has a preference for arachidyl alcohol as well as decyl alcohol, demonstrating its relatively poor activity using saturated long chain alcohols (C16, C18, and C20)
Enzyme 70 Pathways Not Available
Enzyme 70 Reactions
  • acyl-CoA + a long-chain alcohol = CoA + a long-chain ester [RN:R01999]
Enzyme 70 Pfam Domain Function
Enzyme 70 Signals
  • None
Enzyme 70 Transmembrane Regions
  • 12-32 34-53
Enzyme 70 Essentiality Not Available
Enzyme 70 GenBank ID Protein 123227401 Link Image
Enzyme 70 UniProtKB/Swiss-Prot ID Q58HT5 Link Image
Enzyme 70 UniProtKB/Swiss-Prot Entry Name AWAT1_HUMAN Link Image
Enzyme 70 PDB ID Not Available
Enzyme 70 Cellular Location Not Available
Enzyme 70 Gene Sequence >987 bp
ATGGCTCATTCCAAGCAGCCTAGTCACTTCCAGAGTCTGATGCTTCTGCAGTGGCCTTTG
AGCTACCTTGCCATCTTTTGGATCTTGCAGCCATTGTTCGTCTACCTGCTGTTTACATCC
TTGTGGCCGCTACCAGTGCTTTACTTTGCCTGGTTGTTCCTGGACTGGAAGACCCCAGAG
CGAGGTGGCAGGCGTTCGGCCTGGGTAAGGAACTGGTGTGTCTGGACCCACATCAGGGAC
TATTTCCCCATTACGATCCTGAAGACAAAGGACCTATCACCTGAGCACAACTACCTCATG
GGGGTTCACCCCCATGGCCTCCTGACCTTTGGCGCCTTCTGCAACTTCTGCACTGAGGCC
ACAGGCTTCTCGAAGACCTTCCCAGGCATCACTCCTCACTTGGCCACGCTGTCCTGGTTC
TTCAAGATCCCCTTTGTTAGGGAGTACCTCATGGCCAAAGGTGTGTGCTCTGTGAGCCAG
CCAGCCATCAACTATCTGCTGAGCCATGGCACTGGCAACCTCGTGGGCATTGTAGTGGGA
GGTGTGGGTGAGGCCCTGCAAAGTGTGCCCAACACCACCACCCTCATCCTCCAGAAGCGC
AAGGGGTTCGTGCGCACAGCCCTCCAGCATGGGGCTCATCTGGTCCCCACCTTCACTTTT
GGGGAAACTGAGGTGTATGATCAGGTGCTGTTCCATAAGGATAGCAGGATGTACAAGTTC
CAGAGCTGCTTCCGCCGTATCTTTGGTTTCTACTGTTGTGTCTTCTATGGACAAAGCTTC
TGTCAAGGCTCCACTGGGCTCCTGCCATACTCCAGGCCTATTGTCACTGTGGTTGGGGAG
CCTCTGCCACTGCCCCAAATTGAAAAGCCAAGCCAGGAGATGGTGGACAAATACCATGCA
CTTTATATGGATGCTCTGCACAAACTGTTCGACCAGCATAAGACCCACTATGGCTGCTCA
GAGACCCAAAAGCTGTTTTTCCTGTGA
Enzyme 70 GenBank Gene ID AL357752 Link Image
Enzyme 70 GeneCard ID AWAT1 Link Image
Enzyme 70 GenAtlas ID AWAT1 Link Image
Enzyme 70 HGNC ID HGNC:23252 Link Image
Enzyme 70 Chromosome Location Not Available
Enzyme 70 Locus Not Available
Enzyme 70 SNPs SNPJam Report Link Image
Enzyme 70 General References
  1. Turkish AR, Henneberry AL, Cromley D, Padamsee M, Oelkers P, Bazzi H, Christiano AM, Billheimer JT, Sturley SL: Identification of two novel human acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily. J Biol Chem. 2005 Apr 15;280(15):14755-64. Epub 2005 Jan 25. [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. 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. Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed Link Image]
Enzyme 70 Metabolite References Not Available
Enzyme 71 [top]
Enzyme 71 ID 12898
Enzyme 71 Name Acyl-CoA wax alcohol acyltransferase 2
Enzyme 71 Synonyms
  1. Diacylglycerol O-acyltransferase 2-like protein 4
  2. Diacylglycerol O-acyltransferase candidate 4
  3. hDC4
  4. Long-chain-alcohol O-fatty-acyltransferase 2
  5. Multifunctional O-acyltransferase
  6. Wax synthase
  7. hWS
Enzyme 71 Gene Name AWAT2
Enzyme 71 Protein Sequence >Acyl-CoA wax alcohol acyltransferase 2
MLLPSKKDLKTALDVFAVFQWSFSALLITTTVIAVNLYLVVFTPYWPVTVLILTWLAFDW
KTPQRGGRRFTCVRHWRLWKHYSDYFPLKLLKTHDICPSRNYILVCHPHGLFAHGWFGHF
ATEASGFSKIFPGITPYILTLGAFFWMPFLREYVMSTGACSVSRSSIDFLLTHKGTGNMV
IVVIGGLAECRYSLPGSSTLVLKNRSGFVRMALQHGVPLIPAYAFGETDLYDQHIFTPGG
FVNRFQKWFQSMVHIYPCAFYGRGFTKNSWGLLPYSRPVTTIVGEPLPMPKIENPSQEIV
AKYHTLYIDALRKLFDQHKTKFGISETQELEII
Enzyme 71 Number of Residues 333
Enzyme 71 Molecular Weight 38093.2
Enzyme 71 Theoretical pI 9.69
Enzyme 71 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 71 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 71 Specific Function Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has no activity using decyl alcohol and significantly prefers the C16 and C18 alcohols. May also have 2-acylglycerol O-acyltransferase (MGAT) and acyl- CoA:retinol acyltransferase (ARAT) activities, to catalyze the synthesis of diacylglycerols and retinyl esters; however this activity is unclear in vivo
Enzyme 71 Pathways Not Available
Enzyme 71 Reactions
  • acyl-CoA + a long-chain alcohol = CoA + a long-chain ester [RN:R01999]
Enzyme 71 Pfam Domain Function
Enzyme 71 Signals
  • None
Enzyme 71 Transmembrane Regions
  • 15-35 38-58 130-150
Enzyme 71 Essentiality Not Available
Enzyme 71 GenBank ID Protein 49854214 Link Image
Enzyme 71 UniProtKB/Swiss-Prot ID Q6E213 Link Image
Enzyme 71 UniProtKB/Swiss-Prot Entry Name AWAT2_HUMAN Link Image
Enzyme 71 PDB ID Not Available
Enzyme 71 Cellular Location Not Available
Enzyme 71 Gene Sequence >1002 bp
ATGCTCTTGCCCTCTAAGAAGGACCTCAAGACTGCCCTGGATGTCTTTGCTGTTTTCCAG
TGGTCCTTCAGTGCCTTGCTTATCACAACCACTGTGATTGCTGTCAACCTCTACCTGGTG
GTGTTCACACCATACTGGCCTGTCACTGTGCTTATTCTTACCTGGCTGGCTTTTGACTGG
AAGACCCCTCAGCGAGGCGGCCGCCGGTTTACCTGTGTGAGGCACTGGCGCCTGTGGAAA
CACTACAGCGATTATTTCCCTCTCAAGCTTCTGAAGACTCATGACATCTGCCCCAGCCGC
AACTACATCCTCGTCTGCCACCCTCATGGGCTCTTTGCCCATGGATGGTTTGGCCACTTT
GCCACAGAGGCCTCAGGCTTCTCCAAGATATTTCCTGGCATCACCCCTTACATACTCACA
CTGGGAGCCTTTTTCTGGATGCCTTTCCTCAGAGAATATGTAATGTCTACAGGGGCCTGC
TCTGTGAGTCGATCCTCCATTGACTTTCTGCTGACTCATAAAGGCACAGGCAACATGGTC
ATTGTGGTGATTGGTGGACTGGCTGAGTGCAGATACAGCCTGCCAGGTTCTTCTACCCTG
GTGTTGAAGAACCGGTCTGGCTTTGTGCGCATGGCCCTTCAGCATGGGGTGCCTCTAATA
CCTGCCTATGCCTTTGGGGAGACGGACCTCTATGATCAGCACATTTTCACTCCTGGTGGC
TTTGTCAACCGCTTCCAGAAGTGGTTCCAGAGCATGGTACACATCTACCCTTGTGCTTTC
TATGGACGTGGCTTCACCAAGAACTCCTGGGGCCTTCTGCCCTATAGTCGGCCTGTAACC
ACCATCGTCGGGGAGCCTCTACCAATGCCCAAGATTGAGAATCCAAGCCAGGAGATCGTG
GCTAAATATCACACACTCTATATTGATGCCCTACGTAAACTGTTTGACCAGCATAAGACC
AAGTTTGGTATCTCAGAGACCCAGGAGCTGGAGATAATTTGA
Enzyme 71 GenBank Gene ID AY605053 Link Image
Enzyme 71 GeneCard ID AWAT2 Link Image
Enzyme 71 GenAtlas ID AWAT2 Link Image
Enzyme 71 HGNC ID HGNC:23251 Link Image
Enzyme 71 Chromosome Location Not Available
Enzyme 71 Locus Not Available
Enzyme 71 SNPs SNPJam Report Link Image
Enzyme 71 General References
  1. Cheng JB, Russell DW: Mammalian wax biosynthesis. II. Expression cloning of wax synthase cDNAs encoding a member of the acyltransferase enzyme family. J Biol Chem. 2004 Sep 3;279(36):37798-807. Epub 2004 Jun 27. [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. Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed Link Image]
  4. Turkish AR, Henneberry AL, Cromley D, Padamsee M, Oelkers P, Bazzi H, Christiano AM, Billheimer JT, Sturley SL: Identification of two novel human acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily. J Biol Chem. 2005 Apr 15;280(15):14755-64. Epub 2005 Jan 25. [PubMed Link Image]
  5. Yen CL, Brown CH 4th, Monetti M, Farese RV Jr: A human skin multifunctional O-acyltransferase that catalyzes the synthesis of acylglycerols, waxes, and retinyl esters. J Lipid Res. 2005 Nov;46(11):2388-97. Epub 2005 Aug 16. [PubMed Link Image]
Enzyme 71 Metabolite References Not Available
Enzyme 72 [top]
Enzyme 72 ID 12899
Enzyme 72 Name Diacylglycerol O-acyltransferase 2-like protein 6
Enzyme 72 Synonyms
  1. Diacylglycerol O-acyltransferase candidate 3
  2. hDC3
Enzyme 72 Gene Name DGAT2L6
Enzyme 72 Protein Sequence >Diacylglycerol O-acyltransferase 2-like protein 6
MAFFSRLNLQEGLQTFFVLQWIPVYIFLGAIPILLIPYFLLFSKFWPLAVLSLAWLTYDW
NTHSQGGRRSAWVRNWTLWKYFRNYFPVKLVKTHDLSPKHNYIIANHPHGILSFGVFINF
ATEATGIARIFPSITPFVGTLERIFWIPIVREYVMSMGVCPVSSSALKYLLTQKGSGNAV
VIVVGGAAEALLCRPGASTLFLKQRKGFVKMALQTGAYLVPSYSFGENEVFNQETFPEGT
WLRLFQKTFQDTFKKILGLNFCTFHGRGFTRGSWGFLPFNRPITTVVGEPLPIPRIKRPN
QKTVDKYHALYISALRKLFDQHKVEYGLPETQELTIT
Enzyme 72 Number of Residues 337
Enzyme 72 Molecular Weight 38592.9
Enzyme 72 Theoretical pI 10.34
Enzyme 72 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 72 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 72 Specific Function Probable acyltransferase uses fatty acyl-CoA as substrate. Has no wax synthase activity to produce wax esters
Enzyme 72 Pathways Not Available
Enzyme 72 Reactions Not Available
Enzyme 72 Pfam Domain Function
Enzyme 72 Signals
  • None
Enzyme 72 Transmembrane Regions
  • 22-42 102-122
Enzyme 72 Essentiality Not Available
Enzyme 72 GenBank ID Protein 34526048 Link Image
Enzyme 72 UniProtKB/Swiss-Prot ID Q6ZPD8 Link Image
Enzyme 72 UniProtKB/Swiss-Prot Entry Name DG2L6_HUMAN Link Image
Enzyme 72 PDB ID Not Available
Enzyme 72 Cellular Location Not Available
Enzyme 72 Gene Sequence >1014 bp
ATGGCTTTCTTCTCCCGACTGAATCTCCAGGAGGGCCTCCAAACCTTCTTTGTTTTGCAA
TGGATCCCAGTCTATATATTTTTAGGAGCTATTCCCATTCTCCTTATACCCTACTTTCTG
TTATTCAGTAAGTTCTGGCCCTTGGCTGTGCTCTCCTTAGCCTGGCTCACCTATGATTGG
AACACCCACAGTCAAGGTGGCAGGCGTTCAGCTTGGGTACGAAACTGGACCCTATGGAAG
TATTTCCGAAATTACTTCCCAGTAAAGCTGGTGAAGACTCATGATCTTTCTCCCAAACAC
AACTACATCATTGCCAATCACCCCCATGGCATTCTCTCTTTTGGTGTCTTCATCAACTTT
GCCACTGAGGCCACTGGCATTGCTCGGATTTTCCCATCCATCACTCCCTTTGTAGGGACC
TTAGAAAGGATATTTTGGATCCCAATTGTGCGAGAATATGTGATGTCAATGGGTGTGTGC
CCTGTGAGTAGCTCAGCCTTGAAGTACTTGCTGACCCAGAAAGGCTCAGGCAATGCCGTG
GTTATTGTGGTGGGTGGAGCTGCTGAAGCTCTCTTGTGCCGACCAGGAGCCTCCACTCTC
TTCCTCAAGCAGCGTAAAGGTTTTGTGAAGATGGCACTGCAAACAGGGGCATACCTTGTC
CCTTCATATTCCTTTGGTGAGAACGAAGTTTTCAATCAGGAGACCTTCCCTGAGGGCACG
TGGTTAAGGTTGTTCCAAAAAACCTTCCAGGACACATTCAAAAAAATCCTGGGACTAAAT
TTCTGTACCTTCCATGGCCGGGGCTTCACTCGCGGATCCTGGGGCTTCCTGCCTTTCAAT
CGGCCCATTACCACTGTTGTTGGGGAACCCCTTCCAATTCCCAGGATTAAGAGGCCAAAC
CAGAAGACAGTAGACAAGTATCACGCACTCTACATCAGTGCCCTGCGCAAGCTCTTTGAC
CAACACAAAGTTGAATATGGCCTCCCTGAGACCCAAGAGCTGACAATTACATAA
Enzyme 72 GenBank Gene ID AK129500 Link Image
Enzyme 72 GeneCard ID DGAT2L6 Link Image
Enzyme 72 GenAtlas ID DGAT2L6 Link Image
Enzyme 72 HGNC ID HGNC:23250 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. 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. Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed Link Image]
  4. Turkish AR, Henneberry AL, Cromley D, Padamsee M, Oelkers P, Bazzi H, Christiano AM, Billheimer JT, Sturley SL: Identification of two novel human acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily. J Biol Chem. 2005 Apr 15;280(15):14755-64. Epub 2005 Jan 25. [PubMed Link Image]
Enzyme 72 Metabolite References Not Available
Enzyme 73 [top]
Enzyme 73 ID 12900
Enzyme 73 Name Putative diacylglycerol O-acyltransferase 2-like protein 7
Enzyme 73 Synonyms Not Available
Enzyme 73 Gene Name DGAT2L7
Enzyme 73 Protein Sequence >Putative diacylglycerol O-acyltransferase 2-like protein 7
MLAVLYLLVKTAKLGTSWNYLFDFHPHRVLVVGAFANFCTEPTGCSCLFPKLPPHLLMLP
CWFHLLFFQDYIMSGASALPPGLVSFVKAPLPQWWPGGCPGVGGPLQALEAKPGQLSLPI
RNQKRLVKSALELGENELFQQFPNPQSSWVQRTQEALRPLLSVALQLFLGRRGLPLPFRA
PIRTVVGSAIPVQQSPPPSPAQVDTLQARYVGRLTQLFEEHQARYGVPADRHLVLTEARP
TAWPRLSAG
Enzyme 73 Number of Residues 249
Enzyme 73 Molecular Weight 27571.0
Enzyme 73 Theoretical pI 9.99
Enzyme 73 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 73 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 73 Specific Function Probable acyltransferase uses fatty acyl-CoA as substrate
Enzyme 73 Pathways Not Available
Enzyme 73 Reactions Not Available
Enzyme 73 Pfam Domain Function
Enzyme 73 Signals
  • 1-17
Enzyme 73 Transmembrane Regions
  • None
Enzyme 73 Essentiality Not Available
Enzyme 73 GenBank ID Protein Not Available
Enzyme 73 UniProtKB/Swiss-Prot ID Q6IED9 Link Image
Enzyme 73 UniProtKB/Swiss-Prot Entry Name DG2L7_HUMAN Link Image
Enzyme 73 PDB ID Not Available
Enzyme 73 Cellular Location Not Available
Enzyme 73 Gene Sequence Not Available
Enzyme 73 GenBank Gene ID Not Available
Enzyme 73 GeneCard ID DGAT2L7 Link Image
Enzyme 73 GenAtlas ID Not Available
Enzyme 73 HGNC ID Not Available
Enzyme 73 Chromosome Location 7
Enzyme 73 Locus 7q22.1
Enzyme 73 SNPs SNPJam Report Link Image
Enzyme 73 General References
  1. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  2. Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed Link Image]
Enzyme 73 Metabolite References Not Available
Enzyme 74 [top]
Enzyme 74 ID 12901
Enzyme 74 Name Sn1-specific diacylglycerol lipase alpha
Enzyme 74 Synonyms
  1. DGL-alpha
  2. Neural stem cell-derived dendrite regulator
Enzyme 74 Gene Name DAGLA
Enzyme 74 Protein Sequence >Sn1-specific diacylglycerol lipase alpha
MPGIVVFRRRWSVGSDDLVLPAIFLFLLHTTWFVILSVVLFGLVYNPHEACSLNLVDHGR
GYLGILLSCMIAEMAIIWLSMRGGILYTEPRDSMQYVLYVRLAILVIEFIYAIVGIVWLT
QYYTSCNDLTAKNVTLGMVVCNWVVILSVCITVLCVFDPTGRTFVKLRATKRRQRNLRTY
NLRHRLEEGQATSWSRRLKVFLCCTRTKDSQSDAYSEIAYLFAEFFRDLDIVPSDIIAGL
VLLRQRQRAKRNAVLDEANNDILAFLSGMPVTRNTKYLDLKNSQEMLRYKEVCYYMLFAL
AAYGWPMYLMRKPACGLCQLARSCSCCLCPARPRFAPGVTIEEDNCCGCNAIAIRRHFLD
ENMTAVDIVYTSCHDAVYETPFYVAVDHDKKKVVISIRGTLSPKDALTDLTGDAERLPVE
GHHGTWLGHKGMVLSAEYIKKKLEQEMVLSQAFGRDLGRGTKHYGLIVVGHSLGAGTAAI
LSFLLRPQYPTLKCFAYSPPGGLLSEDAMEYSKEFVTAVVLGKDLVPRIGLSQLEGFRRQ
LLDVLQRSTKPKWRIIVGATKCIPKSELPEEVEVTTLASTRLWTHPSDLTIALSASTPLY
PPGRIIHVVHNHPAEQCCCCEQEEPTYFAIWGDNKAFNEVIISPAMLHEHLPYVVMEGLN
KVLENYNKGKTALLSAAKVMVSPTEVDLTPELIFQQQPLPTGPPMPTGLALELPTADHRN
SSVRSKSQSEMSLEGFSEGRLLSPVVAAAARQDPVELLLLSTQERLAAELQARRAPLATM
ESLSDTESLYSFDSRRSSGFRSIRGSPSLHAVLERDEGHLFYIDPAIPEENPSLSSRTEL
LAADSLSKHSQDTQPLEAALGSGGVTPERPPSAAANDEEEEVGGGGGGPASRGELALHNG
RLGDSPSPQVLEFAEFIDSLFNLDSKSSSFQDLYCMVVPESPTSDYAEGPKSPSQQEILL
RAQFEPNLVPKPPRLFAGSADPSSGISLSPSFPLSSSGELMDLTPTGLSSQECLAADKIR
TSTPTGHGASPAKQDELVISAR
Enzyme 74 Number of Residues 1042
Enzyme 74 Molecular Weight 114950.7
Enzyme 74 Theoretical pI 6.31
Enzyme 74 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • triglyceride lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 74 General Function Involved in triglyceride lipase activity
Enzyme 74 Specific Function Catalyzes the hydrolysis of diacylglycerol (DAG) to 2- arachidonoyl-glycerol (2-AG), the most abundant endocannabinoid in tissues. Required for axonal growth during development and for retrograde synaptic signaling at mature synapses
Enzyme 74 Pathways Not Available
Enzyme 74 Reactions Not Available
Enzyme 74 Pfam Domain Function
Enzyme 74 Signals
  • None
Enzyme 74 Transmembrane Regions
  • 23-43 61-81 102-122 137-157
Enzyme 74 Essentiality Not Available
Enzyme 74 GenBank ID Protein 27262632 Link Image
Enzyme 74 UniProtKB/Swiss-Prot ID Q9Y4D2 Link Image
Enzyme 74 UniProtKB/Swiss-Prot Entry Name DGLA_HUMAN Link Image
Enzyme 74 PDB ID Not Available
Enzyme 74 Cellular Location Not Available
Enzyme 74 Gene Sequence >3129 bp
ATGCCCGGGATCGTGGTGTTCCGGCGGCGCTGGTCTGTGGGCAGTGATGACCTCGTCCTA
CCGGCCATCTTCCTCTTTCTCCTGCATACCACCTGGTTTGTGATCCTGTCCGTGGTGCTC
TTCGGCCTGGTCTATAACCCGCACGAGGCCTGCTCCCTGAACCTGGTGGACCACGGCCGC
GGCTACCTGGGCATCCTGCTGAGCTGCATGATCGCTGAGATGGCCATCATCTGGCTGAGC
ATGCGCGGGGGCATCCTCTACACGGAGCCCCGTGACTCCATGCAGTACGTGCTCTACGTG
CGCCTGGCCATCCTGGTGATCGAGTTCATCTACGCCATCGTGGGCATCGTCTGGCTCACT
CAGTACTACACCTCCTGCAACGACCTCACTGCCAAGAATGTCACCCTCGGAATGGTTGTC
TGCAACTGGGTAGTCATCCTCAGTGTGTGCATCACTGTCCTCTGCGTCTTCGACCCCACG
GGCCGCACCTTTGTCAAGCTGAGAGCCACCAAGAGGAGGCAGCGTAACCTGCGGACCTAC
AACCTGCGGCACCGCTTAGAGGAGGGTCAAGCCACCAGCTGGTCGCGCCGGCTCAAAGTG
TTCCTCTGCTGCACGCGGACGAAGGACTCCCAGTCAGATGCCTACTCAGAAATCGCCTAC
CTCTTTGCGGAGTTCTTCCGGGACCTTGACATTGTGCCATCCGACATCATTGCTGGCCTG
GTGCTGCTCCGGCAGCGGCAGCGGGCCAAGCGCAACGCCGTGCTGGACGAGGCAAACAAT
GACATCTTGGCCTTCCTGTCTGGGATGCCGGTGACCAGAAACACCAAGTACCTCGACCTC
AAGAATTCACAAGAGATGCTCCGCTACAAAGAGGTCTGCTACTACATGCTCTTTGCCCTG
GCTGCCTACGGGTGGCCCATGTACCTGATGCGGAAGCCCGCCTGCGGCCTCTGCCAACTG
GCTCGGTCCTGCTCGTGTTGCCTGTGTCCTGCGAGGCCGCGGTTCGCCCCTGGAGTCACC
ATCGAGGAAGACAACTGCTGTGGCTGTAATGCCATTGCCATCCGGCGCCACTTCCTGGAC
GAGAACATGACTGCGGTGGACATCGTCTATACCTCCTGCCATGATGCGGTCTATGAAACG
CCCTTCTACGTGGCGGTGGACCATGACAAGAAGAAAGTGGTGATCAGTATCCGGGGGACC
CTGTCCCCCAAGGATGCCCTGACTGACCTGACGGGTGATGCTGAGCGCCTCCCCGTGGAG
GGGCACCACGGCACCTGGCTGGGCCACAAGGGTATGGTCCTCTCAGCTGAGTACATCAAG
AAGAAACTGGAGCAGGAGATGGTCCTGTCCCAGGCCTTTGGGCGAGACCTGGGCCGCGGA
ACCAAACACTACGGCCTGATTGTGGTGGGCCACTCCCTGGGCGCGGGCACTGCTGCCATC
CTCTCCTTCCTTCTGCGCCCACAGTATCCGACCCTCAAGTGCTTTGCCTACTCCCCGCCA
GGGGGCCTGCTGAGTGAGGATGCGATGGAGTATTCCAAGGAGTTCGTGACTGCTGTGGTT
CTGGGCAAAGACCTCGTCCCCAGGATTGGCCTCTCTCAGCTGGAAGGCTTCCGCAGACAG
CTCCTGGATGTCCTGCAGCGAAGCACCAAGCCCAAATGGCGGATCATCGTGGGGGCCACC
AAATGCATCCCCAAGTCGGAGCTGCCTGAGGAGGTAGAGGTGACCACCCTGGCCAGCACG
CGGCTCTGGACCCACCCCAGCGACCTAACTATAGCCCTCTCAGCCAGCACTCCACTCTAC
CCGCCCGGCCGCATCATCCACGTGGTCCACAACCACCCTGCAGAGCAGTGCTGCTGCTGT
GAGCAGGAGGAGCCCACATACTTTGCCATCTGGGGCGACAACAAGGCCTTCAATGAGGTG
ATCATCTCGCCAGCCATGCTGCATGAGCACCTGCCCTATGTGGTCATGGAGGGGCTCAAC
AAGGTGCTGGAGAACTACAACAAGGGGAAGACCGCTCTGCTCTCTGCAGCCAAGGTCATG
GTGAGCCCTACCGAGGTGGACCTGACTCCTGAGCTCATCTTCCAGCAGCAGCCACTCCCC
ACGGGGCCGCCCATGCCCACTGGCCTTGCCCTGGAGCTGCCGACTGCAGACCACCGCAAC
AGCAGCGTCAGGAGCAAGTCCCAGTCTGAGATGAGCCTGGAGGGCTTCTCGGAGGGGCGG
CTGCTGTCGCCAGTGGTTGCGGCGGCGGCCCGCCAGGACCCGGTGGAGCTGCTGCTGCTG
TCTACCCAGGAGCGGCTGGCGGCGGAGCTGCAGGCCCGGCGGGCACCACTGGCCACCATG
GAGAGCCTCTCGGACACTGAGTCCCTGTACAGCTTCGACTCGCGCCGCTCCTCAGGCTTC
CGCAGCATCCGGGGCTCCCCCAGCCTCCACGCTGTGCTGGAGCGTGATGAAGGCCACCTC
TTCTACATTGACCCTGCCATCCCCGAGGAAAACCCATCCCTGAGCTCGCGCACTGAGCTG
CTGGCGGCCGACAGCCTGTCCAAGCACTCACAGGACACGCAGCCCCTGGAGGCGGCCCTG
GGCAGTGGCGGCGTCACTCCTGAGCGGCCCCCCAGTGCTGCGGCCAATGACGAGGAGGAA
GAGGTTGGCGGTGGGGGTGGCGGGCCGGCCTCCCGCGGGGAGCTGGCGCTGCACAATGGG
CGCCTGGGGGACTCGCCCAGTCCTCAGGTGCTGGAATTCGCCGAGTTCATCGACAGCCTC
TTCAACCTGGACAGCAAGAGCAGCTCCTTCCAAGACCTCTACTGCATGGTGGTGCCCGAG
AGCCCCACCAGTGACTACGCTGAGGGCCCCAAGTCCCCCAGCCAGCAAGAGATCCTGCTC
CGTGCCCAGTTCGAGCCCAACCTGGTGCCCAAGCCCCCACGGCTCTTTGCCGGCTCAGCC
GACCCCTCCTCGGGCATCTCACTCTCGCCCTCCTTCCCGCTCAGCTCCTCGGGTGAGCTC
ATGGACCTGACGCCCACGGGCCTCAGTAGCCAGGAATGCCTGGCGGCTGACAAGATCCGG
ACTTCTACCCCCACTGGCCACGGAGCCAGCCCCGCCAAGCAAGATGAGCTGGTCATCTCA
GCACGCTAG
Enzyme 74 GenBank Gene ID NM_006133.1 Link Image
Enzyme 74 GeneCard ID DAGLA Link Image
Enzyme 74 GenAtlas ID DAGLA Link Image
Enzyme 74 HGNC ID HGNC:1165 Link Image
Enzyme 74 Chromosome Location 1
Enzyme 74 Locus 11q12.2
Enzyme 74 SNPs SNPJam Report Link Image
Enzyme 74 General References
  1. 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]
  2. 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]
  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. Bisogno T, Howell F, Williams G, Minassi A, Cascio MG, Ligresti A, Matias I, Schiano-Moriello A, Paul P, Williams EJ, Gangadharan U, Hobbs C, Di Marzo V, Doherty P: Cloning of the first sn1-DAG lipases points to the spatial and temporal regulation of endocannabinoid signaling in the brain. J Cell Biol. 2003 Nov 10;163(3):463-8. [PubMed Link Image]
  5. Jung KM, Mangieri R, Stapleton C, Kim J, Fegley D, Wallace M, Mackie K, Piomelli D: Stimulation of endocannabinoid formation in brain slice cultures through activation of group I metabotropic glutamate receptors. Mol Pharmacol. 2005 Nov;68(5):1196-202. Epub 2005 Jul 28. [PubMed Link Image]
Enzyme 74 Metabolite References Not Available
Enzyme 75 [top]
Enzyme 75 ID 12902
Enzyme 75 Name Sn1-specific diacylglycerol lipase beta
Enzyme 75 Synonyms
  1. DGL-beta
  2. KCCR13L
Enzyme 75 Gene Name DAGLB
Enzyme 75 Protein Sequence >Sn1-specific diacylglycerol lipase beta
MPGMVLFGRRWAIASDDLVFPGFFELVVRVLWWIGILTLYLMHRGKLDCAGGALLSSYLI
VLMILLAVVICTVSAIMCVSMRGTICNPGPRKSMSKLLYIRLALFFPEMVWASLGAAWVA
DGVQCDRTVVNGIIATVVVSWIIIAATVVSIIIVFDPLGGKMAPYSSAGPSHLDSHDSSQ
LLNGLKTAATSVWETRIKLLCCCIGKDDHTRVAFSSTAELFSTYFSDTDLVPSDIAAGLA
LLHQQQDNIRNNQEPAQVVCHAPGSSQEADLDAELENCHHYMQFAAAAYGWPLYIYRNPL
TGLCRIGGDCCRSRTTDYDLVGGDQLNCHFGSILHTTGLQYRDFIHVSFHDKVYELPFLV
ALDHRKESVVVAVRGTMSLQDVLTDLSAESEVLDVECEVQDRLAHKGISQAARYVYQRLI
NDGILSQAFSIAPEYRLVIVGHSLGGGAAALLATMLRAAYPQVRCYAFSPPRGLWSKALQ
EYSQSFIVSLVLGKDVIPRLSVTNLEDLKRRILRVVAHCNKPKYKILLHGLWYELFGGNP
NNLPTELDGGDQEVLTQPLLGEQSLLTRWSPAYSFSSDSPLDSSPKYPPLYPPGRIIHLQ
EEGASGRFGCCSAAHYSAKWSHEAEFSKILIGPKMLTDHMPDILMRALDSVVSDRAACVS
CPAQGVSSVDVA
Enzyme 75 Number of Residues 672
Enzyme 75 Molecular Weight 73731.3
Enzyme 75 Theoretical pI 6.54
Enzyme 75 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • triglyceride lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 75 General Function Involved in triglyceride lipase activity
Enzyme 75 Specific Function Catalyzes the hydrolysis of diacylglycerol (DAG) to 2- arachidonoyl-glycerol (2-AG), the most abundant endocannabinoid in tissues. Required for axonal growth during development and for retrograde synaptic signaling at mature synapses
Enzyme 75 Pathways Not Available
Enzyme 75 Reactions Not Available
Enzyme 75 Pfam Domain Function
Enzyme 75 Signals
  • None
Enzyme 75 Transmembrane Regions
  • 18-38 59-79 103-123 133-153
Enzyme 75 Essentiality Not Available
Enzyme 75 GenBank ID Protein 17864023 Link Image
Enzyme 75 UniProtKB/Swiss-Prot ID Q8NCG7 Link Image
Enzyme 75 UniProtKB/Swiss-Prot Entry Name DGLB_HUMAN Link Image
Enzyme 75 PDB ID Not Available
Enzyme 75 Cellular Location Not Available
Enzyme 75 Gene Sequence >2019 bp
ATGCCGGGGATGGTACTCTTCGGCCGGCGCTGGGCCATCGCCAGCGACGACTTGGTCTTC
CCAGGGTTCTTCGAGCTGGTCGTGCGAGTGCTGTGGTGGATTGGCATTCTGACGTTGTAT
CTCATGCACAGAGGAAAGCTGGACTGTGCTGGTGGAGCCTTGCTCAGCAGTTACTTGATC
GTCCTCATGATTCTCCTGGCAGTTGTCATATGTACTGTGTCAGCCATCATGTGTGTCAGC
ATGAGAGGAACGATTTGTAACCCTGGACCGCGGAAGTCTATGTCTAAGCTGCTTTACATC
CGCCTGGCGCTGTTTTTTCCAGAGATGGTCTGGGCCTCTCTGGGGGCTGCCTGGGTGGCA
GATGGTGTTCAGTGCGACAGGACAGTTGTAAACGGCATCATCGCAACCGTCGTGGTCAGT
TGGATCATCATCGCTGCCACAGTGGTTTCCATTATCATTGTCTTTGACCCTCTTGGGGGG
AAAATGGCTCCATATTCCTCTGCCGGCCCCAGCCACCTGGATAGTCATGATTCAAGCCAG
TTACTTAATGGCCTCAAGACAGCAGCTACAAGCGTGTGGGAAACCAGAATCAAGCTCTTG
TGCTGTTGCATTGGGAAAGACGACCATACTCGGGTTGCTTTTTCGAGTACGGCAGAGCTT
TTCTCAACCTACTTTTCAGACACAGATCTGGTGCCCAGCGACATTGCGGCGGGCCTCGCC
CTGCTTCATCAGCAACAGGACAATATCAGGAACAACCAAGAGCCTGCCCAGGTGGTCTGC
CATGCCCCAGGGAGCTCCCAGGAAGCTGATCTGGATGCAGAATTAGAAAACTGCCATCAT
TACATGCAGTTTGCAGCAGCGGCCTATGGGTGGCCCCTCTACATCTACAGAAACCCCCTC
ACGGGGCTGTGCAGGATTGGTGGTGACTGCTGCAGAAGCAGAACCACAGACTATGACTTG
GTCGGAGGCGATCAGCTCAACTGTCACTTCGGCTCCATCCTGCACACCACAGGGCTGCAG
TACAGGGACTTCATCCACGTCAGCTTCCATGACAAGGTTTACGAGCTGCCGTTTTTAGTG
GCTCTGGATCACAGGAAAGAGTCTGTTGTGGTCGCTGTGAGGGGGACCATGTCTCTGCAG
GATGTCCTTACGGACCTGTCAGCGGAGAGTGAGGTGCTGGACGTGGAGTGTGAGGTGCAG
GACCGCCTGGCACACAAGGGTATTTCTCAAGCTGCCAGATACGTTTACCAACGACTCATC
AACGACGGGATTTTGAGCCAAGCCTTCAGCATTGCTCCTGAGTACCGGCTGGTCATAGTG
GGCCACAGCCTCGGGGGCGGGGCGGCCGCCCTGCTGGCCACCATGCTCAGAGCCGCCTAC
CCGCAGGTCAGGTGCTACGCCTTCTCCCCACCCCGGGGGCTGTGGAGCAAAGCTCTGCAG
GAATATTCTCAGAGCTTCATCGTGTCACTCGTCCTGGGGAAGGATGTGATTCCCAGGCTC
AGTGTGACCAACTTGGAAGATCTGAAGAGAAGAATCTTGCGAGTGGTCGCGCACTGCAAT
AAACCCAAGTACAAGATCTTGCTGCACGGTTTGTGGTACGAACTGTTTGGAGGAAACCCC
AACAACTTGCCCACGGAGCTGGACGGGGGCGACCAGGAAGTCCTGACACAGCCTCTTCTG
GGGGAGCAGAGCCTACTGACGCGCTGGTCCCCGGCCTACAGCTTCTCCAGCGACTCTCCA
CTGGACTCTTCTCCCAAGTACCCCCCTCTCTACCCTCCCGGCAGGATCATCCACCTGCAG
GAGGAGGGCGCCTCGGGGCGGTTTGGCTGCTGCTCTGCTGCTCACTATAGCGCCAAGTGG
TCACACGAAGCGGAATTCAGCAAAATACTCATAGGTCCGAAGATGCTCACCGACCACATG
CCAGACATCCTGATGCGGGCCTTGGACAGCGTGGTCTCCGACAGAGCGGCCTGCGTCTCC
TGTCCAGCACAAGGGGTCTCCAGTGTGGACGTGGCCTGA
Enzyme 75 GenBank Gene ID AF450090 Link Image
Enzyme 75 GeneCard ID DAGLB Link Image
Enzyme 75 GenAtlas ID DAGLB Link Image
Enzyme 75 HGNC ID HGNC:28923 Link Image
Enzyme 75 Chromosome Location 7
Enzyme 75 Locus 7p22.1
Enzyme 75 SNPs SNPJam Report Link Image
Enzyme 75 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. 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. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  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. Bisogno T, Howell F, Williams G, Minassi A, Cascio MG, Ligresti A, Matias I, Schiano-Moriello A, Paul P, Williams EJ, Gangadharan U, Hobbs C, Di Marzo V, Doherty P: Cloning of the first sn1-DAG lipases points to the spatial and temporal regulation of endocannabinoid signaling in the brain. J Cell Biol. 2003 Nov 10;163(3):463-8. [PubMed Link Image]
  6. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [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]
  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. 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 75 Metabolite References Not Available
Enzyme 76 [top]
Enzyme 76 ID 12903
Enzyme 76 Name 2-acylglycerol O-acyltransferase 3
Enzyme 76 Synonyms
  1. Acyl-CoA:monoacylglycerol acyltransferase 3
  2. MGAT3
  3. Diacylglycerol O-acyltransferase candidate 7
  4. hDC7
  5. Diacylglycerol acyltransferase 2-like protein 7
  6. Monoacylglycerol O-acyltransferase 3
Enzyme 76 Gene Name MOGAT3
Enzyme 76 Protein Sequence >2-acylglycerol O-acyltransferase 3
MGVATTLQPPTTSKTLQKQHLEAVGAYQYVLTFLFMGPFFSLLVFVLLFTSLWPFSVFYL
VWLYVDWDTPNQGGRRSEWIRNRAIWRQLRDYYPVKLVKTAELPPDRNYVLGAHPHGIMC
TGFLCNFSTESNGFSQLFPGLRPWLAVLAGLFYLPVYRDYIMSFGLCPVSRQSLDFILSQ
PQLGQAVVIMVGGAHEALYSVPGEHCLTLQKRKGFVRLALRHGASLVPVYSFGENDIFRL
KAFATGSWQHWCQLTFKKLMGFSPCIFWGRGLFSATSWGLLPFAVPITTVVGRPIPVPQR
LHPTEEEVNHYHALYMTALEQLFEEHKESCGVPASTCLTFI
Enzyme 76 Number of Residues 341
Enzyme 76 Molecular Weight 38729.8
Enzyme 76 Theoretical pI 8.70
Enzyme 76 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 76 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 76 Specific Function Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Also able to catalyze the terminal step in triacylglycerol synthesis by using diacylglycerol and fatty acyl-CoA as substrates. Has a preference toward palmitoyl-CoA and oleoyl-CoA. May be involved in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes
Enzyme 76 Pathways
Enzyme 76 Reactions
  • acyl-CoA + 2-acylglycerol = CoA + diacylglycerol [RN:R01368]
Enzyme 76 Pfam Domain Function
Enzyme 76 Signals
  • None
Enzyme 76 Transmembrane Regions
  • 29-49 50-70 137-157
Enzyme 76 Essentiality Not Available
Enzyme 76 GenBank ID Protein 29124967 Link Image
Enzyme 76 UniProtKB/Swiss-Prot ID Q86VF5 Link Image
Enzyme 76 UniProtKB/Swiss-Prot Entry Name MOGT3_HUMAN Link Image
Enzyme 76 PDB ID Not Available
Enzyme 76 Cellular Location Not Available
Enzyme 76 Gene Sequence >1026 bp
ATGGGAGTTGCCACAACCCTGCAGCCCCCAACCACTTCCAAAACCTTGCAGAAGCAGCAT
CTAGAAGCAGTGGGCGCCTACCAATATGTGCTCACTTTCCTCTTCATGGGCCCTTTCTTC
TCCCTTCTTGTCTTTGTCCTCCTCTTCACGTCACTCTGGCCCTTCTCTGTTTTTTACTTG
GTGTGGCTCTATGTGGACTGGGACACACCCAACCAAGGTGGAAGGCGTTCGGAGTGGATA
AGGAACCGGGCAATTTGGAGACAACTAAGGGATTATTATCCTGTCAAGCTGGTGAAAACA
GCAGAGCTGCCCCCGGATCGGAACTACGTGCTGGGCGCCCACCCTCATGGGATCATGTGT
ACAGGCTTCCTCTGTAATTTCTCCACCGAGAGCAATGGCTTCTCCCAGCTCTTCCCGGGG
CTCCGGCCCTGGTTAGCCGTGCTGGCTGGCCTCTTCTACCTCCCGGTCTATCGCGACTAC
ATCATGTCCTTTGGACTCTGTCCGGTGAGCCGCCAGAGCCTGGACTTCATCCTGTCCCAG
CCCCAGCTCGGGCAGGCCGTGGTCATCATGGTGGGGGGTGCGCACGAGGCCCTGTATTCA
GTCCCCGGGGAGCACTGCCTTACGCTCCAGAAGCGCAAAGGCTTCGTGCGCCTGGCGCTG
AGGCACGGGGCGTCCCTGGTGCCCGTGTACTCCTTTGGGGAGAATGACATCTTTAGACTT
AAGGCTTTTGCCACAGGCTCCTGGCAGCATTGGTGCCAGCTCACCTTCAAGAAGCTCATG
GGCTTCTCTCCTTGCATCTTCTGGGGTCGCGGTCTCTTCTCAGCCACCTCCTGGGGCCTG
CTGCCCTTTGCTGTGCCCATCACCACTGTGGTGGGCCGCCCCATCCCCGTCCCCCAGCGC
CTCCACCCCACCGAGGAGGAAGTCAATCACTATCACGCCCTCTACATGACGGCCCTGGAG
CAGCTCTTCGAGGAGCACAAGGAAAGCTGTGGGGTCCCCGCTTCCACCTGCCTCACCTTC
ATCTAG
Enzyme 76 GenBank Gene ID AY229854 Link Image
Enzyme 76 GeneCard ID MOGAT3 Link Image
Enzyme 76 GenAtlas ID MOGAT3 Link Image
Enzyme 76 HGNC ID HGNC:23249 Link Image
Enzyme 76 Chromosome Location 7
Enzyme 76 Locus 7q22.1
Enzyme 76 SNPs SNPJam Report Link Image
Enzyme 76 General References
  1. Cheng D, Nelson TC, Chen J, Walker SG, Wardwell-Swanson J, Meegalla R, Taub R, Billheimer JT, Ramaker M, Feder JN: Identification of acyl coenzyme A:monoacylglycerol acyltransferase 3, an intestinal specific enzyme implicated in dietary fat absorption. J Biol Chem. 2003 Apr 18;278(16):13611-4. Epub 2003 Mar 3. [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. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 76 Metabolite References Not Available
Enzyme 77 [top]
Enzyme 77 ID 12904
Enzyme 77 Name Diacylglycerol kinase kappa
Enzyme 77 Synonyms
  1. DAG kinase kappa
  2. 142 kDa diacylglycerol kinase
  3. Diglyceride kinase kappa
  4. DGK-kappa
Enzyme 77 Gene Name DGKK
Enzyme 77 Protein Sequence >Diacylglycerol kinase kappa
MDRGAAAAQGTAPPQDGEQPAESPEPPPPWPPPPPPPAPPPAPPLLSEASPEPIPEPCPE
LAPGPCPEATSESATELYTEPTPEPATEPASEPAPEPATEPAPEPATEPAPEPAPEPATE
SAPEPTPEPALESVPEPAPELTPEVAPELAPEPTPEPVTELAPEFCPEAAPEFRPSPAPC
LLQCPVDTRERGLKTSPSPSPSPSPRTPMSWSRIKKILKEGPMLKNCNSFKRWKLRYFLV
QGQKLYFAHHPAFAHFETIDLSQATVAESSCRNLCHSFCVITPQRKITLAAPNRKDMEEW
INIIKTIQQGEIYKIPAAENNPFLVGMHCWYSSYSHRTQHCNVCRESIPALSRDAIICEV
CKVKSHRLCALRASKDCKWNTLSITDDLLLPADEVNMPHQWVEGNMPVSSQCAVCHESCG
SYQRLQDFRCLWCNSTVHDDCRRRFSKECCFRSHRSSVIPPTALSDPKGDGQLVVSSDFW
NLDWSSACSCPLLIFINSKSGDHQGIVFLRKFKQYLNPSQVFDLLKGGPEAGLSMFKNFA
RFRILVCGGDGSVSWVLSLIDAFGLHEKCQLAVIPLGTGNDLARVLGWGAFWNKSKSPLD
ILNRVEQASVRILDRWSVMIRETPRQTPLLKGQVEMDVPRFEAAAIQHLESAATELNKIL
KAKYPTEMIIATRFLCSAVEDFVVDIVKAWGQIKQNNTAIVSVILKSDLMYDRLSVLIDV
LAEEAAATSAEKSATEYADSSKADRKPFIPQIDHIAKCKLELATKAQSLQKSLKLIIFQV
EQALDEESRQTISVKNFSSTFFLEDDPEDINQTSPRRRSRRGTLSSISSLKSEDLDNLNL
DHLHFTPESIRFKEKCVMNNYFGIGLDAKISLDFNTRRDEHPGQYNSRLKNKMWYGLLGT
KELLQRSYRKLEERVHLECDGETISLPNLQGIVVLNITSYAGGINFWGSNTATTEYEAPA
IDDGKLEVVAIFGSVQMAMSRIINLHHHRIAQCHEVMITIDGEEGIPVQVDGEAWIQRPG
LIKIRYKNAAQMLTRDRDFENSMKMWEYKHTEIQAAPQPQLDFQDSQESLSDEEYAQMQH
LARLAENLISKLNDLSKIHQHVSVLMGSVNASANILNDIFYGQDSGNEMGAASCIPIETL
SRNDAVDVTFSLKGLYDDTTAFLDEKLLRSAEDETALQSALDAMNKEFKKLSEIDWMNPI
FVPEEKSSDTDSRSLRLKIKFPKLGKKKVEEERKPKSGQSVQSFIGNLWHRRHREDEAEG
DDPLTPSRSQL
Enzyme 77 Number of Residues 1271
Enzyme 77 Molecular Weight 141827.5
Enzyme 77 Theoretical pI 5.23
Enzyme 77 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 77 General Function Involved in diacylglycerol kinase activity
Enzyme 77 Specific Function Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA)
Enzyme 77 Pathways
Enzyme 77 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 77 Pfam Domain Function
Enzyme 77 Signals
  • None
Enzyme 77 Transmembrane Regions
  • None
Enzyme 77 Essentiality Not Available
Enzyme 77 GenBank ID Protein 57753888 Link Image
Enzyme 77 UniProtKB/Swiss-Prot ID Q5KSL6 Link Image
Enzyme 77 UniProtKB/Swiss-Prot Entry Name DGKK_HUMAN Link Image
Enzyme 77 PDB ID Not Available
Enzyme 77 Cellular Location Not Available
Enzyme 77 Gene Sequence >3816 bp
ATGGACCGCGGAGCTGCCGCAGCCCAGGGCACTGCCCCGCCTCAGGATGGAGAGCAGCCC
GCTGAGTCTCCAGAGCCTCCGCCGCCTTGGCCGCCGCCGCCACCACCACCGGCTCCGCCG
CCGGCTCCGCCGCTGCTCTCCGAGGCTTCGCCAGAACCCATACCAGAGCCCTGTCCAGAG
CTTGCTCCAGGTCCCTGTCCAGAGGCGACCTCAGAATCAGCCACAGAACTGTACACAGAA
CCGACCCCAGAACCAGCCACAGAGCCGGCCTCAGAACCGGCCCCAGAACCTGCCACAGAG
CCGGCCCCAGAACCTGCCACAGAGCCGGCCCCAGAACCGGCCCCAGAACCTGCCACAGAG
TCTGCCCCAGAGCCGACTCCAGAACCTGCCCTAGAGTCGGTCCCAGAGCCGGCCCCAGAG
CTGACTCCAGAAGTTGCCCCAGAGCTGGCCCCAGAGCCGACCCCAGAACCTGTGACAGAG
CTGGCCCCAGAGTTCTGCCCTGAGGCGGCTCCAGAGTTCCGTCCAAGTCCAGCACCATGT
CTATTGCAATGTCCGGTGGACACTCGAGAGAGAGGTCTAAAGACCTCGCCATCGCCATCG
CCATCGCCATCGCCCAGAACGCCAATGTCGTGGTCCAGAATAAAGAAAATATTGAAGGAA
GGACCTATGCTGAAGAACTGTAACTCTTTCAAGAGATGGAAGCTTAGATATTTTCTGGTT
CAAGGACAGAAGCTCTACTTTGCACACCATCCCGCGTTTGCACACTTTGAAACGATTGAT
CTGTCTCAAGCCACTGTGGCAGAAAGCAGCTGTAGAAACCTTTGCCACAGTTTTTGTGTT
ATTACACCACAACGAAAAATCACTCTGGCTGCACCCAACCGGAAAGACATGGAAGAATGG
ATTAACATCATAAAAACCATCCAACAGGGAGAAATTTATAAGATACCTGCAGCAGAAAAC
AACCCTTTTCTTGTTGGAATGCATTGTTGGTACTCCAGTTACAGCCACCGGACCCAGCAC
TGCAATGTTTGTCGAGAGAGCATTCCTGCCTTATCTAGAGATGCCATCATCTGTGAAGTG
TGCAAAGTGAAATCTCACAGATTGTGTGCTTTGAGAGCAAGCAAAGACTGCAAGTGGAAT
ACATTGTCTATCACTGATGACCTCCTTCTGCCTGCAGATGAAGTAAACATGCCCCATCAA
TGGGTAGAAGGAAACATGCCTGTCAGCTCTCAGTGTGCAGTGTGTCATGAGAGCTGTGGC
AGTTATCAAAGACTTCAAGACTTCCGCTGCCTGTGGTGTAATTCTACGGTGCATGATGAC
TGTAGGAGACGGTTTTCCAAGGAATGTTGCTTCAGAAGCCATCGCTCATCAGTCATTCCT
CCCACTGCTCTAAGCGACCCCAAAGGCGATGGCCAATTAGTAGTATCTTCAGACTTCTGG
AATCTTGATTGGTCATCAGCCTGTTCATGTCCCTTGCTCATCTTCATCAACTCCAAAAGT
GGCGATCATCAGGGGATCGTCTTCCTCCGAAAATTCAAGCAATACCTTAACCCATCTCAA
GTGTTCGACTTATTGAAGGGTGGACCTGAAGCAGGGCTGTCTATGTTCAAGAACTTTGCT
CGCTTTCGCATTCTGGTTTGTGGTGGAGATGGCAGCGTGAGCTGGGTCTTATCTCTGATT
GATGCCTTTGGATTACATGAAAAGTGTCAGTTGGCAGTCATCCCACTTGGAACCGGCAAT
GATCTGGCTCGTGTTCTGGGCTGGGGTGCATTCTGGAACAAAAGCAAGTCACCTCTGGAC
ATCCTCAACAGAGTGGAGCAGGCTAGTGTGAGGATCCTAGACAGATGGAGTGTGATGATT
CGTGAGACTCCCAGACAAACCCCGCTGCTAAAAGGACAGGTTGAAATGGATGTACCACGA
TTTGAGGCTGCTGCCATCCAACACTTAGAATCTGCAGCCACCGAGTTGAACAAAATCCTG
AAGGCCAAGTACCCCACAGAGATGATCATCGCAACCAGATTCTTGTGTTCAGCTGTGGAA
GATTTTGTGGTTGATATTGTAAAGGCCTGGGGTCAGATAAAACAGAACAACACTGCAATA
GTGTCTGTGATTTTGAAAAGTGACTTAATGTATGATAGGCTCAGTGTCCTGATCGATGTC
CTGGCTGAGGAGGCAGCAGCTACTTCTGCTGAAAAAAGTGCTACAGAATATGCAGACAGC
AGCAAGGCAGATAGGAAGCCCTTCATTCCTCAAATAGACCACATAGCCAAGTGCAAGTTG
GAGCTGGCTACAAAGGCCCAGAGTCTCCAGAAATCCTTGAAACTCATCATATTTCAAGTT
GAACAAGCTCTGGATGAGGAAAGCAGACAGACAATATCTGTTAAGAACTTTAGTTCAACT
TTCTTCCTGGAAGATGACCCAGAAGATATTAACCAGACAAGCCCACGACGCCGTTCTCGT
CGTGGCACTTTGTCTTCTATATCTTCTCTCAAAAGTGAGGACCTGGACAACCTTAACTTG
GATCACTTACATTTTACACCTGAATCTATACGCTTCAAAGAAAAATGTGTCATGAACAAC
TACTTCGGAATTGGACTGGATGCTAAAATTTCTCTGGACTTCAACACCAGAAGAGATGAA
CACCCAGGGCAATACAATAGCCGCCTTAAGAACAAGATGTGGTATGGCCTTCTGGGAACC
AAAGAACTTTTGCAGCGCTCTTACAGGAAACTGGAAGAACGAGTGCATTTGGAGTGTGAT
GGAGAAACCATCTCCTTGCCAAACCTGCAAGGCATTGTAGTGCTCAACATTACCAGCTAT
GCTGGAGGTATCAACTTCTGGGGAAGCAACACAGCAACCACGGAATATGAGGCTCCTGCA
ATCGATGATGGGAAACTGGAGGTGGTGGCAATCTTTGGTTCTGTGCAGATGGCAATGTCC
CGTATCATCAACCTGCATCATCATCGCATTGCCCAGTGCCATGAGGTGATGATAACCATT
GATGGTGAAGAAGGTATCCCAGTGCAGGTGGATGGGGAGGCCTGGATTCAGAGACCAGGC
CTTATCAAAATTAGATACAAGAACGCTGCCCAGATGCTGACAAGAGATCGGGACTTTGAG
AACTCAATGAAAATGTGGGAATACAAGCATACTGAAATTCAAGCTGCCCCTCAACCCCAG
CTGGACTTCCAGGACTCTCAAGAGAGCCTCTCTGACGAGGAGTATGCCCAGATGCAGCAC
TTAGCTCGGCTTGCAGAAAACCTCATCAGCAAACTTAATGACCTGAGCAAGATCCACCAG
CATGTGTCTGTCCTCATGGGTTCTGTGAATGCCAGCGCTAACATCCTGAATGATATATTT
TACGGCCAAGACAGTGGCAATGAGATGGGTGCAGCTTCCTGTATTCCCATTGAAACTCTA
AGCAGAAATGATGCCGTAGATGTTACATTTAGTCTTAAAGGTCTCTACGATGACACCACA
GCTTTCCTGGATGAAAAGCTGCTGAGAAGTGCTGAGGATGAGACTGCACTACAAAGCGCC
CTGGATGCCATGAATAAGGAGTTCAAAAAGCTATCTGAGATTGACTGGATGAATCCAATC
TTTGTTCCAGAGGAAAAATCTTCGGACACTGACAGTAGAAGCCTCAGGCTGAAAATTAAG
TTCCCCAAATTGGGAAAGAAAAAGGTAGAAGAGGAACGCAAGCCTAAATCAGGCCAGAGT
GTCCAGAGTTTTATTGGCAATTTATGGCACCGCAGACATCGTGAAGATGAAGCAGAGGGT
GATGATCCTCTAACACCATCGAGATCTCAACTGTAG
Enzyme 77 GenBank Gene ID AB183864 Link Image
Enzyme 77 GeneCard ID DGKK Link Image
Enzyme 77 GenAtlas ID DGKK Link Image
Enzyme 77 HGNC ID HGNC:32395 Link Image
Enzyme 77 Chromosome Location Not Available
Enzyme 77 Locus Not Available
Enzyme 77 SNPs SNPJam Report Link Image
Enzyme 77 General References
  1. Imai S, Kai M, Yasuda S, Kanoh H, Sakane F: Identification and characterization of a novel human type II diacylglycerol kinase, DGK kappa. J Biol Chem. 2005 Dec 2;280(48):39870-81. Epub 2005 Oct 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]
Enzyme 77 Metabolite References Not Available
Enzyme 78 [top]
Enzyme 78 ID 12905
Enzyme 78 Name Serine/threonine-protein kinase D2
Enzyme 78 Synonyms
  1. nPKC-D2
Enzyme 78 Gene Name PRKD2
Enzyme 78 Protein Sequence >Serine/threonine-protein kinase D2
MATAPSYPAGLPGSPGPGSPPPPGGLELQSPPPLLPQIPAPGSGVSFHIQIGLTREFVLL
PAASELAHVKQLACSIVDQKFPECGFYGLYDKILLFKHDPTSANLLQLVRSSGDIQEGDL
VEVVLSASATFEDFQIRPHALTVHSYRAPAFCDHCGEMLFGLVRQGLKCDGCGLNYHKRC
AFSIPNNCSGARKRRLSSTSLASGHSVRLGTSESLPCTAEELSRSTTELLPRRPPSSSSS
SSASSYTGRPIELDKMLLSKVKVPHTFLIHSYTRPTVCQACKKLLKGLFRQGLQCKDCKF
NCHKRCATRVPNDCLGEALINGDVPMEEATDFSEADKSALMDESEDSGVIPGSHSENALH
ASEEEEGEGGKAQSSLGYIPLMRVVQSVRHTTRKSSTTLREGWVVHYSNKDTLRKRHYWR
LDCKCITLFQNNTTNRYYKEIPLSEILTVESAQNFSLVPPGTNPHCFEIVTANATYFVGE
MPGGTPGGPSGQGAEAARGWETAIRQALMPVILQDAPSAPGHAPHRQASLSISVSNSQIQ
ENVDIATVYQIFPDEVLGSGQFGVVYGGKHRKTGRDVAVKVIDKLRFPTKQESQLRNEVA
ILQSLRHPGIVNLECMFETPEKVFVVMEKLHGDMLEMILSSEKGRLPERLTKFLITQILV
ALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFRRSVVGTPAYLAP
EVLLNQGYNRSLDMWSVGVIMYVSLSGTFPFNEDEDINDQIQNAAFMYPASPWSHISAGA
IDLINNLLQVKMRKRYSVDKSLSHPWLQEYQTWLDLRELEGKMGERYITHESDDVRWEQF
AAEHPLPGSGLPTDRDLGGACPPQDHDMQGLAERISVL
Enzyme 78 Number of Residues 878
Enzyme 78 Molecular Weight 96749.4
Enzyme 78 Theoretical pI 6.84
Enzyme 78 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase C activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 78 General Function Involved in intracellular signaling pathway
Enzyme 78 Specific Function Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress
Enzyme 78 Pathways
Enzyme 78 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 78 Pfam Domain Function
Enzyme 78 Signals
  • None
Enzyme 78 Transmembrane Regions
  • None
Enzyme 78 Essentiality Not Available
Enzyme 78 GenBank ID Protein 120659782 Link Image
Enzyme 78 UniProtKB/Swiss-Prot ID Q9BZL6 Link Image
Enzyme 78 UniProtKB/Swiss-Prot Entry Name KPCD2_HUMAN Link Image
Enzyme 78 PDB ID Not Available
Enzyme 78 Cellular Location Not Available
Enzyme 78 Gene Sequence >2637 bp
ATGGCCACCGCCCCCTCTTATCCCGCCGGGCTCCCTGGCTCTCCCGGGCCGGGGTCTCCT
CCGCCCCCCGGCGGCCTAGAGCTGCAGTCGCCGCCACCGCTACTGCCCCAGATCCCGGCC
CCGGGTTCCGGGGTCTCCTTTCACATCCAGATCGGGCTGACCCGCGAGTTCGTGCTGTTG
CCCGCCGCCTCCGAGCTGGCTCATGTGAAGCAGCTGGCCTGTTCCATCGTGGACCAGAAG
TTCCCTGAGTGTGGCTTCTACGGCCTTTACGACAAGATCCTGCTTTTCAAACATGACCCC
ACGTCGGCCAACCTCCTGCAGCTGGTGCGCTCGTCCGGAGACATCCAGGAGGGCGACCTG
GTGGAGGTGGTGCTGTCGGCCTCGGCCACCTTCGAGGACTTCCAGATCCGCCCGCACGCC
CTCACGGTGCACTCCTATCGGGCGCCTGCCTTCTGTGATCACTGCGGGGAGATGCTCTTC
GGCCTAGTGCGCCAGGGCCTCAAGTGCGATGGCTGCGGGCTGAACTACCACAAGCGCTGT
GCCTTCAGCATCCCCAACAACTGTAGTGGGGCCCGCAAACGGCGCCTGTCATCCACGTCT
CTGGCCAGTGGCCACTCGGTGCGCCTCGGCACCTCCGAGTCCCTGCCCTGCACGGCTGAA
GAGCTGAGCCGTAGCACCACCGAACTCCTGCCTCGCCGTCCCCCGTCATCCTCTTCCTCC
TCTTCTGCCTCATCGTATACGGGCCGCCCCATTGAGCTGGACAAGATGCTGCTCTCCAAG
GTCAAGGTGCCGCACACCTTCCTCATCCACAGCTATACACGGCCCACCGTTTGCCAGGCT
TGCAAGAAACTCCTCAAGGGCCTCTTCCGGCAGGGCCTGCAATGCAAAGACTGCAAGTTT
AACTGTCACAAACGCTGCGCCACCCGCGTCCCTAATGACTGCCTGGGGGAGGCCCTTATC
AATGGAGATGTGCCGATGGAGGAGGCCACCGATTTCAGCGAGGCTGACAAGAGCGCCCTC
ATGGATGAGTCAGAGGACTCCGGTGTCATCCCTGGCTCCCACTCAGAGAATGCGCTCCAC
GCCAGTGAGGAGGAGGAAGGCGAGGGAGGCAAGGCCCAGAGCTCCCTGGGGTACATCCCC
CTAATGAGGGTGGTGCAATCGGTGCGACACACGACGCGGAAATCCAGCACCACGCTGCGG
GAGGGTTGGGTGGTTCATTACAGCAACAAGGACACGCTGAGAAAGCGGCACTATTGGCGC
CTGGACTGCAAGTGTATCACGCTCTTCCAGAACAACACGACCAACAGATACTATAAGGAA
ATTCCGCTGTCAGAAATCCTCACGGTGGAGTCCGCCCAGAACTTCAGCCTTGTGCCGCCG
GGCACCAACCCACACTGCTTTGAGATCGTCACTGCCAATGCCACCTACTTCGTGGGCGAG
ATGCCTGGCGGGACTCCGGGTGGGCCAAGTGGGCAGGGGGCTGAGGCCGCCCGGGGCTGG
GAGACAGCCATCCGCCAGGCCCTGATGCCCGTCATCCTTCAGGACGCACCCAGCGCCCCA
GGCCACGCGCCCCACAGACAAGCTTCTCTGAGCATCTCTGTGTCCAACAGTCAGATCCAA
GAGAATGTGGACATTGCCACTGTCTACCAGATCTTCCCTGACGAAGTGCTGGGCTCAGGG
CAGTTTGGAGTGGTCTATGGAGGAAAACACCGGAAGACAGGCCGGGACGTGGCAGTTAAG
GTCATTGACAAACTGCGCTTCCCTACCAAGCAGGAGAGCCAGCTCCGGAATGAAGTGGCC
ATTCTGCAGAGCCTGCGGCATCCCGGGATCGTGAACCTGGAGTGCATGTTCGAGACGCCT
GAGAAAGTGTTTGTGGTGATGGAGAAGCTGCATGGGGACATGTTGGAGATGATCCTGTCC
AGTGAGAAGGGCCGGCTGCCTGAGCGCCTCACCAAGTTCCTCATCACCCAGATCCTGGTG
GCTTTGAGACACCTTCACTTCAAGAACATTGTCCACTGTGACTTGAAACCAGAAAACGTG
TTGCTGGCATCAGCAGACCCATTTCCTCAGGTGAAGCTGTGTGACTTTGGCTTTGCTCGC
ATCATCGGCGAGAAGTCGTTCCGCCGCTCAGTGGTGGGCACGCCGGCCTACCTGGCACCC
GAGGTGCTGCTCAACCAGGGCTACAACCGCTCGCTGGACATGTGGTCAGTGGGCGTGATC
ATGTACGTCAGCCTCAGCGGCACCTTCCCTTTCAACGAGGATGAGGACATCAATGACCAG
ATCCAGAACGCCGCCTTCATGTACCCGGCCAGCCCCTGGAGCCACATCTCAGCTGGAGCC
ATTGACCTCATCAACAACCTGCTGCAGGTGAAGATGCGCAAACGCTACAGCGTGGACAAA
TCTCTCAGCCACCCCTGGTTACAGGAGTACCAGACGTGGCTGGACCTCCGAGAGCTGGAG
GGGAAGATGGGAGAGCGATACATCACGCATGAGAGTGACGACGCGCGCTGGGAGCAGTTT
GCAGCAGAGCATCCGCTGCCTGGGTCTGGGCTGCCCACGGACAGGGATCTCGGTGGGGCC
TGTCCACCACAGGACCACGACATGCAGGGGCTGGCGGAGCGCATCAGTGTTCTCTGA
Enzyme 78 GenBank Gene ID NM_001079880.1 Link Image
Enzyme 78 GeneCard ID PRKD2 Link Image
Enzyme 78 GenAtlas ID PRKD2 Link Image
Enzyme 78 HGNC ID HGNC:17293 Link Image
Enzyme 78 Chromosome Location 1
Enzyme 78 Locus 19q13.3
Enzyme 78 SNPs SNPJam Report Link Image
Enzyme 78 General References
  1. Sturany S, Van Lint J, Muller F, Wilda M, Hameister H, Hocker M, Brey A, Gern U, Vandenheede J, Gress T, Adler G, Seufferlein T: Molecular cloning and characterization of the human protein kinase D2. A novel member of the protein kinase D family of serine threonine kinases. J Biol Chem. 2001 Feb 2;276(5):3310-8. Epub 2000 Nov 2. [PubMed Link Image]
  2. 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]
  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. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
  5. Kim JE, Tannenbaum SR, White FM: Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J Proteome Res. 2005 Jul-Aug;4(4):1339-46. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed Link Image]
  8. Chen J, Deng F, Li J, Wang QJ: Selective binding of phorbol esters and diacylglycerol by individual C1 domains of the PKD family. Biochem J. 2008 Apr 15;411(2):333-42. [PubMed Link Image]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 78 Metabolite References Not Available
Enzyme 79 [top]
Enzyme 79 ID 12906
Enzyme 79 Name Inactive phospholipase C-like protein 2
Enzyme 79 Synonyms
  1. PLC-L(2)
  2. PLC-L2
  3. Phospholipase C-L2
  4. Phospholipase C-epsilon-2
  5. PLC-epsilon-2
Enzyme 79 Gene Name PLCL2
Enzyme 79 Protein Sequence >Inactive phospholipase C-like protein 2
MAECGRGGAAGGALPTSPGPALGAKGALKAGVGEGGGGGGRLGHGRARYDSGGVSNGDCS
LGVSGDEARASPTRGPRGVALAPTPSAVVCTLPRESKPGGLPRRSSIIKDGTKQKRERKK
TVSFSSMPTEKKISSASDCINSMVEGSELKKVRSNSRIYHRYFLLDADMQSLRWEPSKKD
SEKAKIDIKSIKEVRTGKNTDIFRSNGISDQISEDCAFSVIYGENYESLDLVANSADVAN
IWVTGLRYLISYGKHTLDMLESSQDNMRTSWVSQMFSEIDVDNLGHITLCNAVQCIRNLN
PGLKTSKIELKFKELHKSKDKAGTEVTKEEFIEVFHELCTRPEIYFLLVQFSSNKEFLDT
KDLMMFLEAEQGVAHINEEISLEIIHKYEPSKEGQEKGWLSIDGFTNYLMSPDCYIFDPE
HKKVCQDMKQPLSHYFINSSHNTYLIEDQFRGPSDITGYIRALKMGCRSVELDVWDGPDN
EPVIYTGHTMTSQIVFRSVIDIINKYAFFASEYPLILCLENHCSIKQQKVMVQHMKKLLG
DKLYTTSPNVEESYLPSPDVLKGKILIKAKKLSSNCSGVEGDVTDEDEGAEMSQRMGKEN
MEQPNNVPVKRFQLCKELSELVSICKSVQFKEFQVSFQVQKYWEVCSFNEVLASKYANEN
PGDFVNYNKRFLARVFPSPMRIDSSNMNPQDFWKCGCQIVAMNFQTPGLMMDLNIGWFRQ
NGNCGYVLRPAIMREEVSFFSANTKDSVPGVSPQLLHIKIISGQNFPKPKGSGAKGDVVD
PYVYVEIHGIPADCAEQRTKTVHQNGDAPIFDESFEFQINLPELAMVRFVVLDDDYIGDE
FIGQYTIPFECLQTGYRHVPLQSLTGEVLAHASLFVHVAITNRRGGGKPHKRGLSVRKGK
KSREYASLRTLWIKTVDEVFKNAQPPIRDATDLRENMQNAVVSFKELCGLSSVANLMQCM
LAVSPRFLGPDNTPLVVLNLSEQYPTMELQGIVPEVLKKIVTTYDMMIQSLKALIENADA
VYEKIVHCQKAAMEFHEHLHSIGTKEGLKERKLQKAVESFTWNITILKGQADLLKYAKNE
TLENLKQIHFAAVSCGLNKPGTENADVQKPRRSLEVIPEKANDETGE
Enzyme 79 Number of Residues 1127
Enzyme 79 Molecular Weight 125864.8
Enzyme 79 Theoretical pI 6.89
Enzyme 79 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 79 General Function Involved in calcium ion binding
Enzyme 79 Specific Function May play an role in the regulation of Ins(1,4,5)P3 around the endoplasmic reticulum
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 221219000 Link Image
Enzyme 79 UniProtKB/Swiss-Prot ID Q9UPR0 Link Image
Enzyme 79 UniProtKB/Swiss-Prot Entry Name PLCL2_HUMAN Link Image
Enzyme 79 PDB ID Not Available
Enzyme 79 Cellular Location Not Available
Enzyme 79 Gene Sequence >3384 bp
ATGGCGGAGTGCGGCCGGGGGGGCGCCGCCGGCGGGGCCCTGCCCACCTCCCCGGGCCCG
GCCCTCGGCGCCAAGGGCGCCCTGAAAGCCGGAGTGGGGGAAGGCGGTGGCGGGGGAGGT
CGCCTCGGCCACGGGCGGGCGCGCTATGACAGCGGCGGGGTTTCCAACGGAGACTGCAGC
CTCGGCGTGTCCGGGGACGAAGCCCGGGCTAGCCCTACCAGGGGACCCCGCGGCGTTGCG
CTCGCCCCGACCCCCAGCGCGGTCGTCTGTACCCTCCCCCGGGAGAGCAAGCCGGGCGGC
CTGCCCCGCCGGAGCAGCATCATCAAGGATGGTACAAAACAGAAGAGGGAACGGAAAAAG
ACAGTCTCATTCAGCAGCATGCCAACAGAGAAGAAGATCAGCAGTGCAAGTGATTGTATT
AATTCAATGGTTGAGGGTTCAGAACTCAAAAAGGTTCGCTCCAACTCTAGAATTTATCAT
AGGTACTTTTTACTGGATGCTGACATGCAGAGCCTAAGGTGGGAGCCATCTAAGAAGGAT
TCTGAGAAAGCCAAGATTGACATTAAATCCATCAAGGAAGTGAGAACAGGAAAAAACACA
GACATATTCCGCAGCAATGGCATTTCTGACCAGATATCTGAAGATTGTGCGTTTTCCGTC
ATATATGGAGAGAATTATGAGTCACTGGATTTGGTTGCCAACTCCGCAGATGTTGCAAAC
ATCTGGGTTACAGGACTGCGGTACCTAATTTCTTATGGAAAACATACACTTGATATGTTA
GAAAGTAGCCAAGATAACATGAGGACTTCTTGGGTTTCACAAATGTTTAGTGAAATTGAT
GTAGATAACCTTGGACATATAACTCTGTGTAATGCTGTGCAATGTATCAGAAACCTCAAT
CCTGGTTTAAAAACGAGCAAAATTGAGCTTAAGTTCAAAGAATTGCATAAATCAAAGGAC
AAAGCTGGTACCGAGGTCACAAAGGAAGAATTTATTGAGGTTTTTCATGAGCTTTGTACT
AGACCTGAAATTTATTTCCTTTTAGTTCAGTTTTCAAGCAATAAAGAATTCCTTGATACC
AAGGACCTTATGATGTTTCTTGAGGCAGAACAGGGTGTGGCACATATAAATGAGGAAATA
AGCCTTGAAATTATTCACAAATATGAACCATCCAAAGAGGGTCAGGAAAAGGGCTGGCTC
TCCATAGACGGGTTCACTAATTACCTTATGTCACCTGACTGTTATATATTCGATCCAGAA
CATAAGAAGGTCTGTCAGGATATGAAGCAACCTCTGTCTCATTACTTTATAAACTCATCT
CATAATACATACTTAATAGAGGATCAGTTCCGAGGTCCCTCCGACATCACAGGATATATT
CGAGCTCTTAAAATGGGTTGCCGGAGTGTTGAATTAGATGTATGGGATGGGCCGGACAAT
GAACCTGTAATTTACACAGGCCACACCATGACCTCTCAGATAGTTTTCCGCAGTGTCATT
GATATTATTAACAAGTATGCATTCTTTGCTTCAGAGTATCCTCTTATCTTGTGTTTAGAA
AACCACTGTTCCATTAAACAACAGAAGGTAATGGTTCAGCACATGAAGAAACTTTTAGGA
GACAAGCTCTATACAACATCACCCAATGTTGAGGAATCTTATCTACCATCCCCAGATGTC
CTGAAAGGGAAAATACTAATTAAAGCAAAGAAGCTGTCCTCAAATTGCTCTGGGGTAGAA
GGAGATGTTACTGACGAAGATGAAGGAGCAGAAATGTCTCAGAGGATGGGAAAAGAGAAC
ATGGAGCAACCCAATAATGTGCCTGTGAAGCGATTTCAGCTTTGTAAAGAACTGTCTGAA
CTGGTCAGCATCTGCAAATCAGTTCAGTTCAAAGAATTTCAGGTGTCGTTTCAGGTTCAG
AAGTACTGGGAAGTCTGTTCCTTTAATGAAGTGCTTGCCAGCAAGTACGCCAATGAAAAT
CCAGGGGACTTTGTAAATTACAACAAACGTTTTCTTGCTAGGGTTTTTCCCAGTCCAATG
AGAATTGATTCCAGTAACATGAATCCTCAAGATTTTTGGAAATGTGGTTGCCAAATTGTA
GCCATGAACTTTCAGACACCAGGACTGATGATGGACCTGAATATTGGCTGGTTTAGGCAG
AACGGAAACTGTGGCTATGTCCTCCGGCCAGCCATCATGAGGGAGGAGGTCTCCTTCTTC
AGCGCCAATACAAAAGACTCTGTCCCAGGGGTCTCACCTCAACTTCTTCACATTAAAATC
ATCAGTGGGCAGAACTTTCCCAAGCCCAAAGGATCAGGTGCCAAAGGTGATGTGGTAGAT
CCTTATGTCTATGTTGAAATCCATGGAATCCCTGCTGATTGTGCAGAACAAAGGACAAAA
ACAGTGCACCAGAATGGAGACGCTCCCATTTTTGATGAAAGCTTTGAATTTCAAATCAAC
CTGCCTGAACTGGCCATGGTGCGCTTTGTAGTGCTGGATGATGACTACATTGGGGATGAA
TTCATCGGCCAGTACACAATTCCCTTTGAATGTTTACAGACGGGCTACCGCCATGTCCCC
CTGCAGTCCTTAACTGGAGAGGTCCTTGCACATGCTTCTTTATTTGTCCACGTGGCTATT
ACTAACCGAAGAGGAGGAGGAAAGCCTCATAAAAGGGGCCTTTCTGTGAGAAAAGGGAAG
AAATCCAGGGAATATGCATCTTTGAGAACACTGTGGATTAAAACCGTGGATGAGGTATTC
AAGAATGCCCAGCCCCCTATACGGGATGCCACAGATCTGAGAGAAAACATGCAGAATGCG
GTGGTGTCATTCAAGGAGCTGTGTGGCCTCTCCTCTGTGGCCAATCTCATGCAGTGCATG
TTGGCGGTGTCTCCCCGCTTTCTGGGGCCCGATAACACACCCCTAGTGGTCCTAAATCTC
AGCGAGCAGTACCCCACAATGGAGCTGCAGGGAATTGTGCCGGAGGTTCTGAAGAAGATC
GTAACAACTTATGACATGATGATTCAGTCCCTCAAGGCGTTGATTGAAAATGCAGATGCT
GTATATGAAAAGATCGTACATTGTCAGAAGGCAGCCATGGAATTCCATGAACACTTGCAC
AGCATAGGCACCAAGGAAGGTTTGAAGGAAAGAAAACTACAAAAAGCAGTGGAGAGCTTT
ACCTGGAATATTACCATCTTAAAGGGACAAGCAGATCTTTTGAAATATGCTAAGAATGAG
ACATTGGAGAACCTGAAACAAATCCATTTTGCTGCTGTTTCATGTGGACTGAATAAACCA
GGCACCGAAAATGCTGATGTCCAGAAGCCACGCCGGAGCTTGGAAGTCATACCCGAAAAA
GCAAACGATGAAACTGGAGAATGA
Enzyme 79 GenBank Gene ID NM_001144382.1 Link Image
Enzyme 79 GeneCard ID PLCL2 Link Image
Enzyme 79 GenAtlas ID PLCL2 Link Image
Enzyme 79 HGNC ID HGNC:9064 Link Image
Enzyme 79 Chromosome Location 3
Enzyme 79 Locus 3p24.3
Enzyme 79 SNPs SNPJam Report Link Image
Enzyme 79 General References
  1. Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed Link Image]
  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. 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. 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]
  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]
  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 79 Metabolite References Not Available
Enzyme 80 [top]
Enzyme 80 ID 12958
Enzyme 80 Name Membrane-associated phosphatidylinositol transfer protein 1
Enzyme 80 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 80 Gene Name PITPNM1
Enzyme 80 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 80 Number of Residues 1244
Enzyme 80 Molecular Weight 134846.3
Enzyme 80 Theoretical pI 5.81
Enzyme 80 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • metal ion binding
Process
  • establishment of localization
  • transport
Component
  • cell part
  • intracellular
Enzyme 80 General Function Involved in metal ion binding
Enzyme 80 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 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 12667436 Link Image
Enzyme 80 UniProtKB/Swiss-Prot ID O00562 Link Image
Enzyme 80 UniProtKB/Swiss-Prot Entry Name PITM1_HUMAN Link Image
Enzyme 80 PDB ID Not Available
Enzyme 80 Cellular Location Not Available
Enzyme 80 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 80 GenBank Gene ID AF334584 Link Image
Enzyme 80 GeneCard ID PITPNM1 Link Image
Enzyme 80 GenAtlas ID PITPNM1 Link Image
Enzyme 80 HGNC ID HGNC:9003 Link Image
Enzyme 80 Chromosome Location 1
Enzyme 80 Locus 11q13
Enzyme 80 SNPs SNPJam Report Link Image
Enzyme 80 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 80 Metabolite References Not Available
Enzyme 81 [top]
Enzyme 81 ID 12964
Enzyme 81 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase zeta-1
Enzyme 81 Synonyms
  1. Phosphoinositide phospholipase C-zeta-1
  2. Phospholipase C-zeta-1
  3. PLC-zeta-1
  4. Testis-development protein NYD-SP27
Enzyme 81 Gene Name PLCZ1
Enzyme 81 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase zeta-1
MEMRWFLSKIQDDFRGGKINLEKTQRLLEKLDIRCSYIHVKQIFKDNDRLKQGRITIEEF
RAIYRIITHREEIIEIFNTYSENRKILLASNLAQFLTQEQYAAEMSKAIAFEIIQKYEPI
EEVRKAHQMSLEGFTRYMDSRECLLFKNECRKVYQDMTHPLNDYFISSSHNTYLVSDQLL
GPSDLWGYVSALVKGCRCLEIDCWDGAQNEPVVYHGYTLTSKLLFKTVIQAIHKYAFMTS
DYPVVLSLENHCSTAQQEVMADNLQATFGESLLSDMLDDFPDTLPSPEALKFKILVKNKK
IGTLKETHERKGSDKRGDNQDKETGVKKLPGVMLFKKKKTRKLKIALALSDLVIYTKAEK
FKSFQHSRLYQQFNENNSIGETQARKLSKLRVHEFIFHTRKFITRIYPKATRADSSNFNP
QEFWNIGCQMVALNFQTPGLPMDLQNGKFLDNGGSGYILKPHFLRESKSYFNPSNIKEGM
PITLTIRLISGIQLPLTHSSSNKGDSLVIIEVFGVPNDQMKQQTRVIKKNAFSPRWNETF
TFIIHVPELALIRFVVEGQGLIAGNEFLGQYTLPLLCMNKGYRRIPLFSRMGESLEPASL
FVYVWYVR
Enzyme 81 Number of Residues 608
Enzyme 81 Molecular Weight 70410.7
Enzyme 81 Theoretical pI 9.43
Enzyme 81 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 81 General Function Involved in calcium ion binding
Enzyme 81 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 81 Pathways Not Available
Enzyme 81 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 81 Pfam Domain Function
Enzyme 81 Signals
  • None
Enzyme 81 Transmembrane Regions
  • None
Enzyme 81 Essentiality Not Available
Enzyme 81 GenBank ID Protein 25053795 Link Image
Enzyme 81 UniProtKB/Swiss-Prot ID Q86YW0 Link Image
Enzyme 81 UniProtKB/Swiss-Prot Entry Name PLCZ1_HUMAN Link Image
Enzyme 81 PDB ID Not Available
Enzyme 81 Cellular Location Not Available
Enzyme 81 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 81 GenBank Gene ID AF532185 Link Image
Enzyme 81 GeneCard ID PLCZ1 Link Image
Enzyme 81 GenAtlas ID PLCZ1 Link Image
Enzyme 81 HGNC ID HGNC:19218 Link Image
Enzyme 81 Chromosome Location 1
Enzyme 81 Locus 12p12.3
Enzyme 81 SNPs SNPJam Report Link Image
Enzyme 81 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 81 Metabolite References Not Available
Enzyme 82 [top]
Enzyme 82 ID 12969
Enzyme 82 Name Patatin-like phospholipase domain-containing protein 2
Enzyme 82 Synonyms
  1. Adipose triglyceride lipase
  2. Calcium-independent phospholipase A2
  3. Desnutrin
  4. IPLA2-zeta
  5. Pigment epithelium-derived factor
  6. TTS2.2
  7. Transport-secretion protein 2
  8. TTS2
Enzyme 82 Gene Name PNPLA2
Enzyme 82 Protein Sequence >Patatin-like phospholipase domain-containing protein 2
MFPREKTWNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGV
CLGEAGAKFIEVSKEARKRFLGPLHPSFNLVKIIRSFLLKVLPADSHEHASGRLGISLTR
VSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGVRYVDGGISDNLPLYELKN
TITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYRLSKALFPPEPLVLREMCKQ
GYRDGLRFLQRNGLLNRPNPLLALPPARPHGPEDKDQAVESAQAEDYSQLPGEDHILEHL
PARLNEALLEACVEPTDLLTTLSNMLPVRLATAMMVPYTLPLESALSFTIRLLEWLPDVP
EDIRWMKEQTGSICQYLVMRAKRKLGRHLPSRLPEQVELRRVQSLPSVPLSCAAYREALP
GWMRNNLSLGDALAKWEECQRQLLLGLFCTNVAFPPEALRMRAPADPAPAPADPASPQHQ
LAGPAPLLSTPAPEARPVIGALGL
Enzyme 82 Number of Residues 504
Enzyme 82 Molecular Weight 55315.2
Enzyme 82 Theoretical pI 7.09
Enzyme 82 GO Classification
Function
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 82 General Function Involved in metabolic process
Enzyme 82 Specific Function Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. Also has acylglycerol transacylase activity. May act coordinately with LIPE/HLS within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes. May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion
Enzyme 82 Pathways
Enzyme 82 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 82 Pfam Domain Function
Enzyme 82 Signals
  • None
Enzyme 82 Transmembrane Regions
  • 9-29
Enzyme 82 Essentiality Not Available
Enzyme 82 GenBank ID Protein 32698724 Link Image
Enzyme 82 UniProtKB/Swiss-Prot ID Q96AD5 Link Image
Enzyme 82 UniProtKB/Swiss-Prot Entry Name PLPL2_HUMAN Link Image
Enzyme 82 PDB ID Not Available
Enzyme 82 Cellular Location Not Available
Enzyme 82 Gene Sequence >1515 bp
ATGTTTCCCCGCGAGAAGACGTGGAACATCTCGTTCGCGGGCTGCGGCTTCCTCGGCGTC
TACTACGTCGGCGTGGCCTCCTGCCTCCGCGAGCACGCGCCCTTCCTGGTGGCCAACGCC
ACGCACATCTACGGCGCCTCGGCCGGGGCGCTCACGGCCACGGCGCTGGTCACCGGGGTC
TGCCTGGGTGAGGCTGGTGCCAAGTTCATTGAGGTATCTAAAGAGGCCCGGAAGCGGTTC
CTGGGCCCCCTGCACCCCTCCTTCAACCTGGTAAAGATCATCCGCAGTTTCCTGCTGAAG
GTCCTGCCTGCTGATAGCCATGAGCATGCCAGTGGGCGCCTGGGCATCTCCCTGACCCGC
GTGTCAGACGGCGAGAATGTCATTATATCCCACTTCAACTCCAAGGACGAGCTCATCCAG
GCCAATGTCTGCAGCGGTTTCATCCCCGTGTACTGTGGGCTCATCCCTCCCTCCCTCCAG
GGGGTGCGCTACGTGGATGGTGGCATTTCAGACAACCTGCCACTCTATGAGCTTAAGAAC
ACCATCACAGTGTCCCCCTTCTCGGGCGAGAGTGACATCTGTCCGCAGGACAGCTCCACC
AACATCCACGAGCTGCGGGTCACCAACACCAGCATCCAGTTCAACCTGCGCAACCTCTAC
CGCCTCTCCAAGGCCCTCTTCCCGCCGGAGCCCCTGGTGCTGCGAGAGATGTGCAAGCAG
GGATACCGGGATGGCCTGCGCTTTCTGCAGCGGAACGGCCTCCTGAACCGGCCCAACCCC
TTGCTGGCGTTGCCCCCCGCCCGCCCCCACGGCCCAGAGGACAAGGACCAGGCAGTGGAG
AGCGCCCAAGCGGAGGATTACTCGCAGCTGCCCGGAGAAGATCACATCCTGGAGCACCTG
CCCGCCCGGCTCAATGAGGCCCTGCTGGAGGCCTGCGTGGAGCCCACGGACCTGCTGACC
ACCCTCTCCAACATGCTGCCTGTGCGTCTGGCCACGGCCATGATGGTGCCCTACACGCTG
CCGCTGGAGAGCGCTCTGTCCTTCACCATCCGCTTGCTGGAGTGGCTGCCCGACGTTCCC
GAGGACATCCGGTGGATGAAGGAGCAGACGGGCAGCATCTGCCAGTACCTGGTGATGCGC
GCCAAGAGGAAGCTGGGCAGGCACCTGCCCTCCAGGCTGCCGGAGCAGGTGGAGCTGCGC
CGCGTCCAGTCGCTGCCGTCCGTGCCGCTGTCCTGCGCCGCCTACAGAGAGGCACTGCCC
GGCTGGATGCGCAACAACCTCTCGCTGGGGGACGCGCTGGCCAAGTGGGAGGAGTGCCAG
CGCCAGCTGCTGCTCGGCCTCTTCTGCACCAACGTGGCCTTCCCGCCCGAAGCTCTGCGC
ATGCGCGCACCCGCCGACCCGGCTCCCGCCCCCGCGGACCCAGCATCCCCGCAGCACCAG
CTGGCCGGGCCTGCCCCCTTGCTGAGCACCCCTGCTCCCGAGGCCCGGCCCGTGATCGGG
GCCCTGGGGCTGTGA
Enzyme 82 GenBank Gene ID NM_020376.3 Link Image
Enzyme 82 GeneCard ID PNPLA2 Link Image
Enzyme 82 GenAtlas ID PNPLA2 Link Image
Enzyme 82 HGNC ID HGNC:30802 Link Image
Enzyme 82 Chromosome Location 1
Enzyme 82 Locus 11p15.5
Enzyme 82 SNPs SNPJam Report Link Image
Enzyme 82 General References
  1. Zimmermann R, Strauss JG, Haemmerle G, Schoiswohl G, Birner-Gruenberger R, Riederer M, Lass A, Neuberger G, Eisenhaber F, Hermetter A, Zechner R: Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase. Science. 2004 Nov 19;306(5700):1383-6. [PubMed Link Image]
  2. Wan D, Gong Y, Qin W, Zhang P, Li J, Wei L, Zhou X, Li H, Qiu X, Zhong F, He L, Yu J, Yao G, Jiang H, Qian L, Yu Y, Shu H, Chen X, Xu H, Guo M, Pan Z, Chen Y, Ge C, Yang S, Gu J: Large-scale cDNA transfection screening for genes related to cancer development and progression. Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15724-9. Epub 2004 Oct 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. Jenkins CM, Mancuso DJ, Yan W, Sims HF, Gibson B, Gross RW: Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J Biol Chem. 2004 Nov 19;279(47):48968-75. Epub 2004 Sep 10. [PubMed Link Image]
  5. Langin D, Dicker A, Tavernier G, Hoffstedt J, Mairal A, Ryden M, Arner E, Sicard A, Jenkins CM, Viguerie N, van Harmelen V, Gross RW, Holm C, Arner P: Adipocyte lipases and defect of lipolysis in human obesity. Diabetes. 2005 Nov;54(11):3190-7. [PubMed Link Image]
  6. Lake AC, Sun Y, Li JL, Kim JE, Johnson JW, Li D, Revett T, Shih HH, Liu W, Paulsen JE, Gimeno RE: Expression, regulation, and triglyceride hydrolase activity of Adiponutrin family members. J Lipid Res. 2005 Nov;46(11):2477-87. Epub 2005 Sep 8. [PubMed Link Image]
  7. Kim JY, Tillison K, Lee JH, Rearick DA, Smas CM: The adipose tissue triglyceride lipase ATGL/PNPLA2 is downregulated by insulin and TNF-alpha in 3T3-L1 adipocytes and is a target for transactivation by PPARgamma. Am J Physiol Endocrinol Metab. 2006 Jul;291(1):E115-27. Epub 2006 May 16. [PubMed Link Image]
  8. Smirnova E, Goldberg EB, Makarova KS, Lin L, Brown WJ, Jackson CL: ATGL has a key role in lipid droplet/adiposome degradation in mammalian cells. EMBO Rep. 2006 Jan;7(1):106-13. [PubMed Link Image]
  9. Notari L, Baladron V, Aroca-Aguilar JD, Balko N, Heredia R, Meyer C, Notario PM, Saravanamuthu S, Nueda ML, Sanchez-Sanchez F, Escribano J, Laborda J, Becerra SP: Identification of a lipase-linked cell membrane receptor for pigment epithelium-derived factor. J Biol Chem. 2006 Dec 8;281(49):38022-37. Epub 2006 Oct 10. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Schoenborn V, Heid IM, Vollmert C, Lingenhel A, Adams TD, Hopkins PN, Illig T, Zimmermann R, Zechner R, Hunt SC, Kronenberg F: The ATGL gene is associated with free fatty acids, triglycerides, and type 2 diabetes. Diabetes. 2006 May;55(5):1270-5. [PubMed Link Image]
  12. Fischer J, Lefevre C, Morava E, Mussini JM, Laforet P, Negre-Salvayre A, Lathrop M, Salvayre R: The gene encoding adipose triglyceride lipase (PNPLA2) is mutated in neutral lipid storage disease with myopathy. Nat Genet. 2007 Jan;39(1):28-30. Epub 2006 Dec 24. [PubMed Link Image]
Enzyme 82 Metabolite References Not Available
Enzyme 83 [top]
Enzyme 83 ID 13145
Enzyme 83 Name A-kinase anchor protein 13
Enzyme 83 Synonyms
  1. AKAP-13
  2. AKAP-Lbc
  3. Breast cancer nuclear receptor-binding auxiliary protein
  4. Guanine nucleotide exchange factor Lbc
  5. Human thyroid-anchoring protein 31
  6. Lymphoid blast crisis oncogene
  7. LBC oncogene
  8. Non-oncogenic Rho GTPase-specific GTP exchange factor
  9. Protein kinase A-anchoring protein 13
  10. p47
Enzyme 83 Gene Name AKAP13
Enzyme 83 Protein Sequence >A-kinase anchor protein 13
MKLNPQQAPLYGDCVVTVLLAEEDKAEDDVVFYLVFLGSTLRHCTSTRKVSSDTLETIAP
GHDCCETVKVQLCASKEGLPVFVVAEEDFHFVQDEAYDAAQFLATSAGNQQALNFTRFLD
QSGPPSGDVNSLDKKLVLAFRHLKLPTEWNVLGTDQSLHDAGPRETLMHFAVRLGLLRLT
WFLLQKPGGRGALSIHNQEGATPVSLALERGYHKLHQLLTEENAGEPDSWSSLSYEIPYG
DCSVRHHRELDIYTLTSESDSHHEHPFPGDGCTGPIFKLMNIQQQLMKTNLKQMDSLMPL
MMTAQDPSSAPETDGQFLPCAPEPTDPQRLSSSEETESTQCCPGSPVAQTESPCDLSSIV
EEENTDRSCRKKNKGVERKGEEVEPAPIVDSGTVSDQDSCLQSLPDCGVKGTEGLSSCGN
RNEETGTKSSGMPTDQESLSSGDAVLQRDLVMEPGTAQYSSGGELGGISTTNVSTPDTAG
EMEHGLMNPDATVWKNVLQGGESTKERFENSNIGTAGASDVHVTSKPVDKISVPNCAPAA
SSLDGNKPAESSLAFSNEETSTEKTAETETSRSREESADAPVDQNSVVIPAAAKDKISDG
LEPYTLLAAGIGEAMSPSDLALLGLEEDVMPHQNSETNSSHAQSQKGKSSPICSTTGDDK
LCADSACQQNTVTSSGDLVAKLCDNIVSESESTTARQPSSQDPPDASHCEDPQAHTVTSD
PVRDTQERADFCPFKVVDNKGQRKDVKLDKPLTNMLEVVSHPHPVVPKMEKELVPDQAVI
SDSTFSLANSPGSESVTKDDALSFVPSQKEKGTATPELHTATDYRDGPDGNSNEPDTRPL
EDRAVGLSTSSTAAELQHGMGNTSLTGLGGEHEGPAPPAIPEALNIKGNTDSSLQSVGKA
TLALDSVLTEEGKLLVVSESSAAQEQDKDKAVTCSSIKENALSSGTLQEEQRTPPPGQDT
QQFHEKSISADCAKDKALQLSNSPGASSAFLKAETEHNKEVAPQVSLLTQGGAAQSLVPP
GASLATESRQEALGAEHNSSALLPCLLPDGSDGSDALNCSQPSPLDVGVKNTQSQGKTSA
CEVSGDVTVDVTGVNALQGMAEPRRENISHNTQDILIPNVLLSQEKNAVLGLPVALQDKA
VTDPQGVGTPEMIPLDWEKGKLEGADHSCTMGDAEEAQIDDEAHPVLLQPVAKELPTDME
LSAHDDGAPAGVREVMRAPPSGRERSTPSLPCMVSAQDAPLPKGADLIEEAASRIVDAVI
EQVKAAGALLTEGEACHMSLSSPELGPLTKGLESAFTEKVSTFPPGESLPMGSTPEEATG
SLAGCFAGREEPEKIILPVQGPEPAAEMPDVKAEDEVDFRASSISEEVAVGSIAATLKMK
QGPMTQAINRENWCTIEPCPDAASLLASKQSPECENFLDVGLGRECTSKQGVLKRESGSD
SDLFHSPSDDMDSIIFPKPEEEHLACDITGSSSSTDDTASLDRHSSHGSDVSLSQILKPN
RSRDRQSLDGFYSHGMGAEGRESESEPADPGDVEEEEMDSITEVPANCSVLRSSMRSLSP
FRRHSWGPGKNAASDAEMNHRSSMRVLGDVVRRPPIHRRSFSLEGLTGGAGVGNKPSSSL
EVSSANAEELRHPFSGEERVDSLVSLSEEDLESDQREHRMFDQQICHRSKQQGFNYCTSA
ISSPLTKSISLMTISHPGLDNSRPFHSTFHNTSANLTESITEENYNFLPHSPSKKDSEWK
SGTKVSRTFSYIKNKMSSSKKSKEKEKEKDKIKEKEKDSKDKEKDKKTVNGHTFSSIPVV
GPISCSQCMKPFTNKDAYTCANCSAFVHKGCRESLASCAKVKMKQPKGSLQAHDTSSLPT
VIMRNKPSQPKERPRSAVLLVDETATTPIFANRRSQQSVSLSKSVSIQNITGVGNDENMS
NTWKFLSHSTDSLNKISKVNESTESLTDEGVGTDMNEGQLLGDFEIESKQLEAESWSRII
DSKFLKQQKKDVVKRQEVIYELMQTEFHHVRTLKIMSGVYSQGMMADLLFEQQMVEKLFP
CLDELISIHSQFFQRILERKKESLVDKSEKNFLIKRIGDVLVNQFSGENAERLKKTYGKF
CGQHNQSVNYFKDLYAKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLFQRI
LQCTKDNEVEQEDLAQSLSLVKDVIGAVDSKVASYEKKVRLNEIYTKTDSKSIMRMKSGQ
MFAKEDLKRKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYIFASLDQKSTV
ISLKKLIVREVAHEEKGLFLISMGMTDPEMVEVHASSKEERNSWIQIIQDTINTLNRDED
EGIPSENEEEKKMLDTRARELKEQLHQKDQKILLLLEEKEMIFRDMAECSTPLPEDCSPT
HSPRVLFRSNTEEALKGGPLMKSAINEVEILQGLVSGNLGGTLGPTVSSPIEQDVVGPVS
LPRRAETFGGFDSHQMNASKGGEKEEGDDGQDLRRTESDSGLKKGGNANLVFMLKRNSEQ
VVQSVVHLYELLSALQGVVLQQDSYIEDQKLVLSERALTRSLSRPSSLIEQEKQRSLEKQ
RQDLANLQKQQAQYLEEKRRREREWEARERELREREALLAQREEEVQQGQQDLEKEREEL
QQKKGTYQYDLERLRAAQKQLEREQEQLRREAERLSQRQTERDLCQVSHPHTKLMRIPSF
FPSPEEPPSPSAPSIAKSGSLDSELSVSPKRNSISRTHKDKGPFHILSSTSQTNKGPEGQ
SQAPASTSASTRLFGLTKPKEKKEKKKKNKTSRSQPGDGPASEVSAEGEEIFC
Enzyme 83 Number of Residues 2813
Enzyme 83 Molecular Weight 307547.7
Enzyme 83 Theoretical pI 4.88
Enzyme 83 GO Classification
Function
  • GTPase regulator activity
  • Ras guanyl-nucleotide exchange factor activity
  • Rho guanyl-nucleotide exchange factor activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • 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 83 General Function Involved in Rho guanyl-nucleotide exchange factor activity
Enzyme 83 Specific Function Anchors cAMP-dependent protein kinase (PKA) and acts as an adapter protein to selectively couple G alpha-13 and Rho. Augments gene activation by the estrogen receptor in an element- specific and ligand-dependent manner. Activates estrogen receptor beta by a p38 MAPK-dependent pathway. Isoform 6 stimulates exchange activity on Rho proteins in vitro, but not on CDC42, Ras or Rac and may bind calcium ions
Enzyme 83 Pathways Not Available
Enzyme 83 Reactions Not Available
Enzyme 83 Pfam Domain Function
Enzyme 83 Signals
  • None
Enzyme 83 Transmembrane Regions
  • None
Enzyme 83 Essentiality Not Available
Enzyme 83 GenBank ID Protein 15207794 Link Image
Enzyme 83 UniProtKB/Swiss-Prot ID Q12802 Link Image
Enzyme 83 UniProtKB/Swiss-Prot Entry Name AKP13_HUMAN Link Image
Enzyme 83 PDB ID Not Available
Enzyme 83 Cellular Location Not Available
Enzyme 83 Gene Sequence >8442 bp
ATGAAACTTAATCCACAGCAAGCTCCCTTATATGGTGATTGTGTTGTTACAGTGCTGCTT
GCTGAAGAGGACAAAGCTGAAGATGATGTAGTGTTTTACTTGGTATTTTTGGGTTCCACC
CTCCGTCACTGTACAAGTACTCGGAAGGTCAGTTCTGATACATTGGAGACCATTGCTCCT
GGTCATGATTGTTGTGAAACAGTGAAGGTGCAGCTCTGTGCTTCCAAAGAGGGCCTTCCC
GTGTTTGTGGTGGCTGAAGAAGACTTTCATTTCGTCCAGGATGAAGCGTATGATGCAGCT
CAATTCCTAGCAACCAGTGCTGGAAATCAGCAGGCTTTGAACTTTACCCGTTTTCTTGAC
CAGTCAGGACCCCCATCTGGGGATGTGAATTCCCTTGATAAGAAGTTGGTGCTGGCATTC
AGGCACCTGAAGCTGCCCACGGAGTGGAATGTATTGGGGACAGATCAGAGTTTGCATGAT
GCTGGCCCGCGAGAGACATTGATGCATTTTGCTGTGCGGCTGGGACTGCTGAGGTTGACG
TGGTTCCTGTTGCAGAAGCCAGGTGGCCGCGGAGCTCTCAGTATCCACAACCAGGAAGGG
GCGACGCCTGTGAGCTTGGCCTTGGAGCGAGGCTATCACAAGCTGCACCAGCTTCTAACC
GAGGAGAATGCTGGAGAACCAGACTCCTGGAGCAGTTTATCCTATGAAATACCGTATGGA
GACTGTTCTGTGAGGCATCATCGAGAGTTGGACATCTATACATTAACCTCTGAGTCTGAT
TCACATCATGAACACCCATTTCCTGGAGACGGTTGCACTGGACCAATTTTTAAACTTATG
AACATCCAACAGCAACTAATGAAAACAAACCTCAAGCAGATGGACAGTCTTATGCCCTTA
ATGATGACAGCACAGGATCCTTCCAGTGCCCCAGAGACAGATGGCCAGTTTCTTCCCTGT
GCACCGGAGCCCACGGACCCTCAGCGACTTTCTTCTTCTGAAGAGACTGAGAGCACTCAG
TGCTGCCCAGGGAGCCCTGTTGCACAGACTGAAAGTCCCTGTGATTTGTCAAGCATAGTT
GAGGAGGAGAATACAGACCGTTCCTGTAGGAAGAAAAATAAAGGCGTGGAAAGAAAAGGG
GAAGAGGTGGAGCCAGCACCTATTGTGGACTCTGGAACTGTATCTGATCAAGACAGCTGC
CTTCAGAGCTTGCCTGATTGTGGAGTAAAGGGCACGGAAGGCCTTTCGTCCTGTGGAAAC
AGAAATGAAGAAACTGGAACAAAATCTTCTGGAATGCCCACAGACCAGGAGTCCCTGAGC
AGTGGAGATGCTGTGCTTCAGAGAGACTTGGTCACGGAGCCAGGCACAGCCCAGTATTCC
TCTGGAGGTGAACTGGGAGGCATTTCAACAACAAATGTCAGTACCCCAGACACTGCAGGG
GAAATGGAACATGGGCTCATGAACCCAGATGCCACTGTTCGGAAGAATGTGCTTCAGGGA
GGGGAAAGTACAAAGGAAAGATTTGAGAACTCTAATATTGGCACAGCTGGAGCCTCTGAC
GTGCACGTCACAAGTAAGCCTGTGGATAAAATCAGTGTTCCAAACTGTGCCCCTGCCGCC
AGTTCCCTGGATGGTAACAAACCTGCTGAGTCTTCACTTGCATTTAGTAATGAAGAAACC
TCCACTGAAAAAACAGCAGAAACGGAAACTTCACGAAGTTGTGAGGAGAGTGCTGATGCT
CCAGTAGATCAGAATTCTGTGGTGATTCCAGCTGCTGCAAAAGACAAGATTTCAGATGGA
TTAGAACCTTATACTCTCTTAGCAGCAGGCATAGGTGAGGCAATGTCACCCTCAGATTTA
GCCCTTCTTGGGCTGGAAGAAGATGTAATGCCACACCAGAACTCAGAAACAAATTCATCT
CATGCTCAAAGCCAAAAGGGCAAATCCTCACCCATTTGTTCTACAACTGGAGACGATAAA
CTTTGTGCAGACTCTGCATGTCAACAGAACACAGTGACTTCTAGTGGCGATTTGGTTGCA
AAACTGTGTGATAACATAGTTAGCAAGTCCGAAAGCACCACAGCAAGGCAACCCAGCTCA
CAAGATCCACCCGATGCCTCCCACTGTGAAGACCCACAGGCTCATACAGTCACCTCTGAC
CCTGTAAGGGATACCCAGGAACGTGCGGATTTTTGTCCTTTCAAAGTGGTGGATAACAAA
GGCCAACGAAAAGATGTGAAACTAGATAAACCTTTAACAAATATGCTTGAGGTGGTTTCA
CATCCACATCCAGTTGTCCCTAAAATGGAGAAAGAACTGGTGCCAGACCAGGCAGTAATA
TCAGACAGTACTTTCTCTCTGGCAAACAGTCCAGGCAGTGAATCAGTAACCAAGGATGAC
GCACTTTCTTTTGTCCCCTCCCAGAAAGAAAAGGGAACAGCAACTCCTGAACTACATACA
GCTACAGATTATAGAGATGGCCCAGATGGAAATTCGAATGAGCCTGATACGCGGCCACTA
GAAGACAGGGCAGCAGGCCTGTCCACATCCTCCACTGCTGCAGAGCTTCAGCACGGGATG
GGGAATACCAGTCTCACAGGACTTGGTGGAGAGCATGAGGGTCCTGCCCCTCCAGCAATC
CCAGAAGCTCTGAATATCAAGGGGAACACTGACTCTTCCCTGCAAAGTATGGGTAAGGCC
ACTTTGGCTTTAGATTCAGTTTTGACTGAAGAAGGAAAACTTCTGGTGGTTTCAGAAAGC
TCTGCAGCTCAGGAACAAGATAAGGATAAAGCGGTGACCTGTTCCTCTATTAAGGAAAAT
GCTCTCTCTTCAGGAACTTTGCAGGAAGAGCAGAGAACACCACCTCCTGGACAAGATACT
CAACAATTTCATGAAAAATCAATCTCAGCTGACTGTGCCAAGGACAAAGCACTTCAGCTA
AGTAATTCACCGGGTGCATCCTCTGCCTTTCTTAAGGCAGAAACTGAACATAACAAGGAA
GTGGCCCCACAAGTCTCACTGCTGACTCAAGGTGGGGCTGCCCAGAGCCTGGTGCCACCA
GGAGCAAGTCTGGCCACAGAGTCAAGGCAGGAAGCCTTGGGGGCAGAGCACAACAGCTCC
GCTCTGTTGCCATGTCTGTTGCCAGATGGGTCTGATGGGTCCGATGCTCTTAACTGCAGT
CAGGCTTCTCCTCTGGATGTTGGAGTGAAGAACACTCAATCCCAGGGAAAAACTAGTGCC
TGTGAGGTGAGTGGAAATGTGACGGTGGATGTTACAGGGGTTAATGCTCTACAAGGTATG
GCTGAGCCCAGAAGAGAGAATATATCACACAACACCCAAGACATCCTGATTCCAAACGTC
TTGTTGAGCCAAGAGAAGAATGCCGTTCTAGGTTTGCCAGTGGCTCTACAGGACAAAGCT
GTGACTGACCCACAGGGAGTTGGAACCCCAGAGATGATACCTCTTGATTGGGAGAAAGGG
AAGCTGGAGGGAGCAGACCACAGCTGTACCATGGGTGACGCTGAGGAAGCCCAAATAGAC
GATGAAGCACATCCTGTCCTACTGCAGCCTGTTGCCAAGGAGCTCCCCACAGACATGGAG
CTCTCAGCCCATGATGATGGGGCCCCAGCTGGTGTGAGGGAAGTCACGCGAGCCCCGCCT
TCAGGCAGAGAAAGGAGCACTCCCTCTCTACCTTGCATGGTCTCTGCCCAGGACGCACCT
CTGCCTAAGGGGGCAGACTTGATAGAGGAGGCTGCCAGCCGTATAGTGGATGCTGTCATC
GAACAAGTCAAGGCCGCTGGAGCACTGCTTACTGAGGGGGAGGCCTGTCACATGTCACTG
TCCAGCCCTGAGTTGGGTCCTCTCACTAAAGGACTAGAGAGTGCTTTTACAGAAAAAGTG
AGTACTTTCCCACCTGGGGAGAGCCTACCAATGGGCAGTACTCCTGAGGAAGCCACGGGG
AGCCTTGCAGGATGTTTTGCTGGAAGGGAGGAGCCAGAGAAGATCATTTTACCTGTCCAG
GGGCCTGAGCCAGCAGCAGAAATGCCAGACGTGAAAGCTGAAGATGAAGTGGATTTTAGA
GCAAGTTCAATTTCTGAAGAAGTGGCTGTAGGGAGCATAGCTGCTACACTGAAGATGAAG
CAAGGCCCAATGACCCAGGCGATAAACCGAGAAAACTGGTGTACAATAGAGCCATGCCCT
GATGCAGCATCTCTTCTGGCTTCCAAGCAGAGCCCAGAATGTGAGAACTTCCTGGATGTT
GGACTGGGCAGAGAGTGTACCTCAAAACAAGGTGTACTTAAAAGAGAATCTGGGAGTGAT
TCTGACCTCTTTCACTCACCCAGTGATGACATGGACAGCATCATCTTCCCAAAGCCAGAG
GAAGAGCATTTGGCCTGTGATATCACCGGATCCAGTTCATCCACCGATGACACGGCTTCA
CTGGACCGACATTCTTCTCATGGCAGTGATGTGTCTCTCTCCCAGATTTTAAAGCCAAAC
AGGTCAAGAGATCGGCAAAGCCTTGATGGATTCTACAGCCATGGGATGGGAGCTGAGGGT
CGAGAAAGTGAGAGTGAGCCTGCTGACCCAGGCGACGTGGAGGAGGAGGAGATGGACAGT
ATCACTGAAGTGCCTGCAAACTGCTCTGTCCTAAGGAGCTCCATGCGCTCTCTTTCTCCC
TTCCGGAGGCACAGCTGGGGGCCTGGGAAAAATGCAGCCAGCGATGCAGAAATGAACCAC
CGGAGTTCAATGCGAGTTCTTGGGGATGTTGTCAGGAGACCTCCCATTCATAGGAGAAGT
TTCAGTCTAGAAGGCTTGACAGGAGGAGCTGGTGTCGGAAACAAGCCATCCTCATCTCTA
GAAGTAAGCTCTGCAAATGCCGAAGAGCTCAGACACCCATTCAGTGGTGAGGAACGGGTT
GACTCTTTGGTGTCACTTTCAGAAGAGGATCTGGAGTCAGACCAGAGAGAACATAGGATG
TTTGATCAGCAGATATGTCACAGATCTAAGCAGCAGGGATTTAATTACTGTACATCAGCC
ATTTCCTCTCCATTGACAAAATCCATCTCATTAATGACAATCAGCCATCCTGGATTGGAC
AATTCACGGCCCTTCCACAGTACCTTCCACAATACCAGTGCTAATCTGACTGAGAGTATA
ACAGAAGAGAACTATAATTTCCTGCCACATAGCCCCTCCAAGAAAGATTCTGAATGGAAG
AGTGGAACAAAAGTCAGTCGTACATTCAGCTACATCAAGAATAAAATGTCTAGCAGCAAG
AAGAGCAAAGAAAAGGAAAAAGAAAAAGATAAGATTAAGGAGAAGGAGAAAGATTCTAAA
GACAAGGAGAAAGATAAGAAGACTGTCAACGGGCACACTTTCAGTTCCATTCCTGTTGTG
GGTCCCATCAGCTGTAGCCAGTGTATGAAGCCCTTCACCAACAAAGATGCCTATACTTGT
GCAAATTGCAGTGCTTTTGTCCACAAAGGCTGCCGAGAAAGTCTAGCCTCCTGTGCAAAG
GTCAAAATGAAGCAGCCCAAAGGGAGCCTTCAGGCACATGACACATCATCACTGCCCACG
GTCATTATGAGAAACAAGCCCTCACAGCCCAAGGAGCGTCCTCGGTCCGCAGTCCTCCTG
GTGGATGAAACCGCTACCACCCCAATATTTGCCAATAGACGATCCCAGCAGAGTGTCTCG
CTCTCCAAAAGTGTCTCCATACAGAACATTACTGGAGTTGGCAATGATGAGAACATGTCA
AACACCTGGAAATTCCTGTCTCATTCAACAGACTCACTAAATAAAATCAGCAAGGTCAAT
GAGTCAACAGAATCACTTACTGATGAGGGAGTAGGTACAGACATGAATGAAGGACAACTA
CTGGGAGACTTTGAGATTGAGTCCAAACAGCTGGAAGCAGAGTCTTGGAGTCGGATAATA
GACAGCAAGTTTCTAAAACAGCAAAAGAAAGATGTGGTCAAACGGCAAGAAGTAATATAT
GAGTTGATGCAGACAGAGTTTCATCATGTCCGCACTCTCAAGATCATGAGTGGTGTGTAC
AGCCAGGGGATGATGGCGGATCTGCTTTTTGAGCAGCAGATGGTAGAAAAGCTGTTCCCC
TGTTTGGATGAGCTGATCAGTATCCATAGCCAATTCTTCCAGAGGATTCTGGAGCGGAAG
AAGGAGTCTCTGGTGGATAAAAGTGAAAAGAACTTTCTCATCAAGAGGATAGGGGATGTG
CTTGTAAATCAGTTTTCAGGTGAGAATGCAGAACGTTTAAAGAAGACATATGGCAAGTTT
TGTGGGCAACATAACCAGTCTGTAAACTACTTCAAAGACCTTTATGCCAAGGATAAGCGT
TTTCAAGCCTTTGTAAAGAAGAAGATGAGCAGTTCAGTTGTTAGAAGGCTTGGAATTCCA
GAGTGCATATTGCTTGTAACTCAGCGGATTACCAAGTACCCAGTTTTATTCCAAAGAATA
TTGCAGTGTACCAAAGACAATGAAGTGGAGCAGGAAGATCTAGCACAGTCCTTGAGCCTG
GTGAAGGATGTGATTGGAGCTGTAGACAGCAAAGTGGCAAGTTATGAAAAGAAAGTGCGT
CTCAATGAGATTTATACAAAGACAGATAGCAAGTCAATCATGAGGATGAAGAGTGGTCAG
ATGTTTGCCAAGGAAGATTTGAAACGGAAGAAGCTTGTACGTGATGGGAGTGTGTTTCTG
AAGAATGCAGCAGGAAGGTTGAAAGAGGTTCAAGCAGTTCTTCTCACTGACATTTTAGTT
TTCCTTCAAGAAAAAGACCAGAAGTACATCTTTGCATCATTGGACCAGAAGTCAACAGTG
ATCTCTTTAAAGAAGCTGATTGTGAGAGAAGTGGCACATGAGGAGAAAGGTTTATTCCTG
ATCAGCATGGGGATGACAGATCCAGAGATGGTAGAAGTCCATGCCAGCTCCAAAGAGGAA
CGAAACAGCTGGATTCAGATCATTCAGGACACAATCAACACCCTGAACAGAGATGAAGAT
GAAGGAATTCCTAGTGAGAATGAGGAAGAAAAGAAAATGTTGGACACCAGAGCCCGAGAA
TTAAAAGAACAACTTCACCAGAAGGACCAAAAAATCCTACTCTTGTTGGAAGAGAAGGAG
ATGATTTTCCGGGACATGGCTGAGTGCAGCACCCCTCTCCCAGAGGATTGCTCCCCAACA
CATAGCCCTAGAGTTCTCTTCCGCTCCAACACAGAAGAGGCTCTCAAAGGAGGACCTTTA
ATGAAAAGTGCAATAAATGAGGTGGAGATCCTTCAGGGTTTGGTGAGTGGAAATCTGGGA
GGCACACTTGGGCCGACTGTCAGCAGCCCCATTGAGCAAGATGTGGTCGGTCCCGTTTCC
CTGCCCCGGAGAGCAGAGACCTTTGGAGGATTTGACAGCCATCAGATGAATGCTTCAAAA
GGAGGCGAGAAGGAAGAGGGAGATGATGGCCAAGATCTTAGGAGAACGGAATCAGATAGT
GGCCTAAAAAAGGGTGGAAATGCTAACCTGGTATTTATGCTTAAAAGAAACAGTGAGCAG
GTTGTCCAGAGCGTTGTTCATCTCTACGAGCTCCTCAGCGCTCTGCAGGGTGTGGTGCTG
CAGCAGGACAGCTACATTGAGGACCAGAAACTGGTGCTGAGCGAGAGGGCGCTCACTCGC
AGCTTGTCCCGCCCGAGCTCCCTCATTGAGCAGGAGAAGCAGCGCAGCCTGGAGAAGCAG
CGCCAGGACCTGGCCAACCTGCAGAAGCAGCAGGCCCAGTACCTCGAGGAGAAGCGCAGG
CGCGAGCGTGAGTGGGAAGCTCGTGAGAGGGAGCTGCGGGAGCGGGAGGCCCTCCTGGCC
CAGCGCGAGGAGGAGGTGCAGCAGGGGCAGCAGGACCTGGAAAAGGAGCGGGAGGAGCTC
CAGCAGAAGAAGGGCACATACCAGTATGACCTGGAGCGACTGCGTGCTGCCCAGAAACAG
CTTGAGAGGGAACAGGAGCACGTGCGCCGGGAGGCAGAGCGGCTCAGCCAGCGGCAGACA
GAACGGGACCTGTGTCAGGTTTCCCATCCACATACCAAGCTGATGAGGATCCCATCGTTC
TTCCCCAGTCCTGAGGAGCCCCCCTCGCCATCTGCACCTTCCATAGCCAAATCAGGGTCA
TTGGACTCAGAACTTTCAGTGTCCCCAAAAAGGAACAGCATCTCTCGGACACACAAAGAT
AAGGGGCCTTTTCACATACTGAGTTCAACCAGCCAGACAAACAAAGGACCAGAAGGGCAG
AGCCAGGCCCCTGCGTCCACCTCTGCCTCTACCCGCCTGTTTGGGTTAACAAAGCCAAAG
GAAAAGAAGGAGAAAAAAAAGAAGAACAAAACCAGCCGCTCTCAGCCCGGTGATGGTCCC
GCGTCAGAAGTATCAGCAGAGGGTGAAGAGATCTTCTGCTGA
Enzyme 83 GenBank Gene ID AB055890 Link Image
Enzyme 83 GeneCard ID AKAP13 Link Image
Enzyme 83 GenAtlas ID AKAP13 Link Image
Enzyme 83 HGNC ID HGNC:371 Link Image
Enzyme 83 Chromosome Location 1
Enzyme 83 Locus 15q24-q25
Enzyme 83 SNPs SNPJam Report Link Image
Enzyme 83 General References
  1. Toksoz D, Williams DA: Novel human oncogene lbc detected by transfection with distinct homology regions to signal transduction products. Oncogene. 1994 Feb;9(2):621-8. [PubMed Link Image]
  2. Rubino D, Driggers P, Arbit D, Kemp L, Miller B, Coso O, Pagliai K, Gray K, Gutkind S, Segars J: Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action. Oncogene. 1998 May 14;16(19):2513-26. [PubMed Link Image]
  3. Sterpetti P, Hack AA, Bashar MP, Park B, Cheng SD, Knoll JH, Urano T, Feig LA, Toksoz D: Activation of the Lbc Rho exchange factor proto-oncogene by truncation of an extended C terminus that regulates transformation and targeting. Mol Cell Biol. 1999 Feb;19(2):1334-45. [PubMed Link Image]
  4. Klussmann E, Edemir B, Pepperle B, Tamma G, Henn V, Klauschenz E, Hundsrucker C, Maric K, Rosenthal W: Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling. FEBS Lett. 2001 Nov 2;507(3):264-8. [PubMed Link Image]
  5. Diviani D, Soderling J, Scott JD: AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation. J Biol Chem. 2001 Nov 23;276(47):44247-57. Epub 2001 Sep 6. [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. Carr DW, Hausken ZE, Fraser ID, Stofko-Hahn RE, Scott JD: Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain. J Biol Chem. 1992 Jul 5;267(19):13376-82. [PubMed Link Image]
  8. Driggers PH, Segars JH, Rubino DM: The proto-oncoprotein Brx activates estrogen receptor beta by a p38 mitogen-activated protein kinase pathway. J Biol Chem. 2001 Dec 14;276(50):46792-7. Epub 2001 Sep 28. [PubMed Link Image]
  9. Iwashita S, Fujii M, Mukai H, Ono Y, Miyamoto M: Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2. Biochem Biophys Res Commun. 2004 Aug 6;320(4):1063-8. [PubMed Link Image]
  10. 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]
  11. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  12. 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]
  13. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  14. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  15. 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]
  16. Newlon MG, Roy M, Morikis D, Carr DW, Westphal R, Scott JD, Jennings PA: A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes. EMBO J. 2001 Apr 2;20(7):1651-62. [PubMed Link Image]
Enzyme 83 Metabolite References Not Available
Enzyme 84 [top]
Enzyme 84 ID 13428
Enzyme 84 Name RAS guanyl-releasing protein 1
Enzyme 84 Synonyms
  1. Calcium and DAG-regulated guanine nucleotide exchange factor II
  2. CalDAG-GEFII
  3. Ras guanyl-releasing protein
Enzyme 84 Gene Name RASGRP1
Enzyme 84 Protein Sequence >RAS guanyl-releasing protein 1
MGTLGKAREAPRKPSHGCRAASKARLEAKPANSPFPSHPSLAHITQFRMMVSLGHLAKGA
SLDDLIDSCIQSFDADGNLCRSNQLLQVMLTMHRIVISSAELLQKVITLYKDALAKNSPG
LCLKICYFVRYWITEFWVMFKMDASLTDTMEEFQELVKAKGEELHCRLIDTTQINARDWS
RKLTQRIKSNTSKKRKVSLLFDHLEPEELSEHLTYLEFKSFRRISFSDYQNYLVNSCVKE
NPTMERSIALCNGISQWVQLMVLSRPTPQLRAEVFIKFIQVAQKLHQLQNFNTLMAVIGG
LCHSSISRLKETSSHVPHEINKVLGEMTELLSSSRNYDNYRRAYGECTDFKIPILGVHLK
DLISLYEAMPDYLEDGKVNVHKLLALYNHISELVQLQEVAPPLEANKDLVHLLTLSLDLY
YTEDEIYELSYAREPRNHRAPPLTPSKPPVVVDWASGVSPKPDPKTISKHVQRMVDSVFK
NYDHDQDGYISQEEFEKIAASFPFSFCVMDKDREGLISRDEITAYFMRASSIYSKLGLGF
PHNFQETTYLKPTFCDNCAGFLWGVIKQGYRCKDCGMNCHKQCKDLVVFECKKRAKNPVA
PTENNTSVGPVSNLCSLGAKDLLHAPEEGPFTFPNGEAVEHGEESKDRTIMLMGVSSQKI
SLRLKRAVAHKATQTESQPWIGSEGPSGPFVLSSPRKTAQDTLYVLPSPTSPCPSPVLVR
KRAFVKWENKDSLIKSKEELRHLRLPTYQELEQEINTLKADNDALKIQLKYAQKKIESLQ
LEKSNHVLAQMEQGDCS
Enzyme 84 Number of Residues 797
Enzyme 84 Molecular Weight 90401.0
Enzyme 84 Theoretical pI 8.02
Enzyme 84 GO Classification
Function
  • GTPase regulator activity
  • binding
  • calcium ion binding
  • cation binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • ion binding
  • metal ion binding
  • nucleoside-triphosphatase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • intracellular signaling pathway
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • signaling
  • signaling pathway
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 84 General Function Involved in calcium ion binding
Enzyme 84 Specific Function Functions as a diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP. Activates the Erk/MAP kinase cascade. Couples T-lymphocytes and B-lymphocytes antigen receptors to the activation of Ras. Hence, regulates T-cells and B-cells development, homeostasis and differentiation. Functions also in FcERI-evoked degranulation and cytokine secretion by mast cells, regulating allergic responses. May also function in other cell types differentiation
Enzyme 84 Pathways Not Available
Enzyme 84 Reactions Not Available
Enzyme 84 Pfam Domain Function
Enzyme 84 Signals
  • None
Enzyme 84 Transmembrane Regions
  • None
Enzyme 84 Essentiality Not Available
Enzyme 84 GenBank ID Protein 190684644 Link Image
Enzyme 84 UniProtKB/Swiss-Prot ID O95267 Link Image
Enzyme 84 UniProtKB/Swiss-Prot Entry Name GRP1_HUMAN Link Image
Enzyme 84 PDB ID Not Available
Enzyme 84 Cellular Location Not Available
Enzyme 84 Gene Sequence >2394 bp
ATGGGCACCCTGGGCAAGGCGAGAGAGGCTCCGCGGAAACCTTCCCATGGCTGCAGAGCT
GCCTCTAAAGCAAGACTAGAGGCAAAGCCAGCCAACAGCCCCTTCCCCTCCCATCCCAGC
TTGGCCCACATCACCCAGTTCCGAATGATGGTGTCTCTGGGACATTTAGCCAAAGGAGCC
AGCCTGGACGATCTCATTGACAGCTGCATTCAATCTTTTGATGCAGATGGAAACCTGTGT
CGAAGTAACCAACTGTTGCAAGTCATGCTGACCATGCACCGAATTGTCATCTCCTCTGCA
GAACTGCTCCAAAAAGTTATCACCCTCTATAAGGATGCTTTGGCAAAGAATTCACCAGGA
CTTTGCCTGAAGATCTGTTATTTTGTAAGGTATTGGATAACAGAATTCTGGGTCATGTTT
AAAATGGACGCCAGCTTGACAGACACTATGGAGGAGTTTCAGGAACTGGTGAAAGCTAAG
GGTGAGGAGTTACATTGCCGCCTGATTGACACAACTCAAATCAATGCCCGTGACTGGTCC
AGGAAACTTACTCAAAGGATAAAATCAAATACCAGCAAGAAACGGAAAGTCTCCCTGCTC
TTTGACCATCTGGAACCAGAAGAGCTATCCGAGCACCTCACCTACCTTGAGTTCAAGTCT
TTCCGGAGGATATCGTTCTCTGATTATCAGAATTACCTTGTAAATAGCTGTGTGAAGGAA
AACCCCACCATGGAGCGATCTATTGCTCTGTGCAACGGCATCTCCCAGTGGGTACAACTG
ATGGTTCTCAGCCGCCCCACGCCGCAGCTCCGAGCAGAAGTCTTCATCAAGTTCATCCAG
GTGGCTCAGAAGCTCCACCAACTACAGAACTTCAATACACTGATGGCTGTGATAGGTGGG
CTGTGTCACAGCTCAATCTCGAGGCTCAAGGAGACAAGTTCGCATGTCCCACATGAAATC
AATAAGGTTCTCGGTGAGATGACTGAGCTGCTGTCCTCCTCCAGAAACTACGACAATTAC
CGGCGAGCCTATGGAGAGTGCACCGACTTCAAGATCCCCATTCTGGGTGTGCATCTCAAG
GACCTCATCTCCCTGTATGAAGCCATGCCTGACTATCTGGAGGACGGGAAAGTGAACGTC
CATAAGCTACTGGCCCTATACAATCATATCAGTGAATTGGTCCAGCTGCAAGAGGTGGCC
CCACCCTTGGAGGCTAACAAGGACTTGGTACACTTGCTGACGTTATCCCTGGATCTTTAC
TACACTGAGGATGAAATCTATGAGCTTTCCTATGCCCGGGAACCAAGGAACCACAGAGCT
CCACCACTAACACCTTCAAAGCCACCAGTAGTAGTGGACTGGGCTTCTGGAGTGTCTCCC
AAACCTGATCCAAAAACCATTAGCAAACACGTCCAGAGGATGGTGGATTCTGTCTTCAAG
AACTATGATCACGACCAGGATGGATACATTTCTCAGGAAGAATTTGAAAAGATTGCTGCG
AGTTTTCCATTTTCCTTCTGTGTGATGGACAAAGACAGGGAAGGCCTCATCAGCAGGGAT
GAGATCACAGCCTACTTCATGAGAGCCAGCTCAATCTATTCCAAGCTGGGCCTGGGCTTT
CCTCACAACTTCCAAGAGACCACCTACCTGAAGCCCACTTTTTGTGACAACTGTGCTGGA
TTTCTCTGGGGAGTGATCAAACAAGGATATCGATGTAAAGACTGCGGGATGAACTGTCAC
AAACAATGCAAAGATCTGGTTGTGTTTGAGTGTAAGAAGCGAGCCAAGAACCCAGTAGCT
CCCACAGAGAACAACACTTCTGTGGGGCCAGTGTCCAACCTTTGCTCATTGGGAGCCAAA
GATCTGCTCCATGCACCTGAGGAAGGACCTTTTACATTCCCTAATGGGGAGGCTGTGGAA
CATGGTGAGGAGAGTAAGGATCGGACCATCATGCTGATGGGAGTGTCCTCACAGAAGATT
TCTCTTCGGCTGAAGAGGGCTGTTGCCCACAAGGCCACCCAGACTGAATCACAGCCTTGG
ATTGGCAGTGAGGGCCCTTCAGGTCCCTTTGTGCTGTCTTCCCCAAGGAAGACAGCCCAG
GATACTCTATATGTGCTTCCCAGTCCCACCTCTCCATGTCCTAGCCCAGTCTTGGTCAGA
AAGCGGGCTTTTGTCAAGTGGGAGAATAAAGACTCCCTCATAAAATCAAAGGAGGAGCTC
CGTCACCTCAGACTGCCTACCTACCAAGAACTGGAACAGGAAATAAATACTCTGAAAGCA
GATAATGATGCCCTAAAGATCCAACTGAAATATGCACAGAAGAAAATAGAATCCCTCCAG
CTTGAAAAAAGCAATCATGTCTTAGCTCAAATGGAGCAGGGTGACTGTTCTTAG
Enzyme 84 GenBank Gene ID NM_005739.3 Link Image
Enzyme 84 GeneCard ID RASGRP1 Link Image
Enzyme 84 GenAtlas ID RASGRP1 Link Image
Enzyme 84 HGNC ID HGNC:9878 Link Image
Enzyme 84 Chromosome Location 1
Enzyme 84 Locus 15q14
Enzyme 84 SNPs SNPJam Report Link Image
Enzyme 84 General References
  1. Kawasaki H, Springett GM, Toki S, Canales JJ, Harlan P, Blumenstiel JP, Chen EJ, Bany IA, Mochizuki N, Ashbacher A, Matsuda M, Housman DE, Graybiel AM: A Rap guanine nucleotide exchange factor enriched highly in the basal ganglia. Proc Natl Acad Sci U S A. 1998 Oct 27;95(22):13278-83. [PubMed Link Image]
  2. Bottorff D, Ebinu J, Stone JC: RasGRP, a Ras activator: mouse and human cDNA sequences and chromosomal positions. Mamm Genome. 1999 Apr;10(4):358-61. [PubMed Link Image]
  3. Yasuda S, Stevens RL, Terada T, Takeda M, Hashimoto T, Fukae J, Horita T, Kataoka H, Atsumi T, Koike T: Defective expression of Ras guanyl nucleotide-releasing protein 1 in a subset of patients with systemic lupus erythematosus. J Immunol. 2007 Oct 1;179(7):4890-900. [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. Ebinu JO, Stang SL, Teixeira C, Bottorff DA, Hooton J, Blumberg PM, Barry M, Bleakley RC, Ostergaard HL, Stone JC: RasGRP links T-cell receptor signaling to Ras. Blood. 2000 May 15;95(10):3199-203. [PubMed Link Image]
  6. Topham MK, Prescott SM: Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism. J Cell Biol. 2001 Mar 19;152(6):1135-43. [PubMed Link Image]
  7. Jones DR, Sanjuan MA, Stone JC, Merida I: Expression of a catalytically inactive form of diacylglycerol kinase alpha induces sustained signaling through RasGRP. FASEB J. 2002 Apr;16(6):595-7. [PubMed Link Image]
  8. Caloca MJ, Zugaza JL, Matallanas D, Crespo P, Bustelo XR: Vav mediates Ras stimulation by direct activation of the GDP/GTP exchange factor Ras GRP1. EMBO J. 2003 Jul 1;22(13):3326-36. [PubMed Link Image]
  9. Caloca MJ, Zugaza JL, Bustelo XR: Exchange factors of the RasGRP family mediate Ras activation in the Golgi. J Biol Chem. 2003 Aug 29;278(35):33465-73. Epub 2003 Jun 2. [PubMed Link Image]
  10. Bivona TG, Perez De Castro I, Ahearn IM, Grana TM, Chiu VK, Lockyer PJ, Cullen PJ, Pellicer A, Cox AD, Philips MR: Phospholipase Cgamma activates Ras on the Golgi apparatus by means of RasGRP1. Nature. 2003 Aug 7;424(6949):694-8. Epub 2003 Jun 29. [PubMed Link Image]
  11. Perez de Castro I, Bivona TG, Philips MR, Pellicer A: Ras activation in Jurkat T cells following low-grade stimulation of the T-cell receptor is specific to N-Ras and occurs only on the Golgi apparatus. Mol Cell Biol. 2004 Apr;24(8):3485-96. [PubMed Link Image]
  12. Zugaza JL, Caloca MJ, Bustelo XR: Inverted signaling hierarchy between RAS and RAC in T-lymphocytes. Oncogene. 2004 Jul 29;23(34):5823-33. [PubMed Link Image]
  13. Zheng Y, Liu H, Coughlin J, Zheng J, Li L, Stone JC: Phosphorylation of RasGRP3 on threonine 133 provides a mechanistic link between PKC and Ras signaling systems in B cells. Blood. 2005 May 1;105(9):3648-54. Epub 2005 Jan 18. [PubMed Link Image]
  14. Roose JP, Mollenauer M, Gupta VA, Stone J, Weiss A: A diacylglycerol-protein kinase C-RasGRP1 pathway directs Ras activation upon antigen receptor stimulation of T cells. Mol Cell Biol. 2005 Jun;25(11):4426-41. [PubMed Link Image]
  15. Kosco KA, Cerignoli F, Williams S, Abraham RT, Mustelin T: SKAP55 modulates T cell antigen receptor-induced activation of the Ras-Erk-AP1 pathway by binding RasGRP1. Mol Immunol. 2008 Jan;45(2):510-22. Epub 2007 Jul 20. [PubMed Link Image]
  16. 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 84 Metabolite References Not Available
Enzyme 85 [top]
Enzyme 85 ID 13429
Enzyme 85 Name RAS guanyl-releasing protein 2
Enzyme 85 Synonyms
  1. Calcium and DAG-regulated guanine nucleotide exchange factor I
  2. CalDAG-GEFI
  3. Cdc25-like protein
  4. hCDC25L
  5. F25B3.3 kinase-like protein
Enzyme 85 Gene Name RASGRP2
Enzyme 85 Protein Sequence >RAS guanyl-releasing protein 2
MAGTLDLDKGCTVEELLRGCIEAFDDSGKVRDPQLVRMFLMMHPWYIPSSQLAAKLLHIY
QQSRKDNSNSLQVKTCHLVRYWISAFPAEFDLNPELAEQIKELKALLDQEGNRRHSSLID
IDSVPTYKWKRQVTQRNPVGQKKRKMSLLFDHLEPMELAEHLTYLEYRSFCKILFQDYHS
FVTHGCTVDNPVLERFISLFNSVSQWVQLMILSKPTAPQRALVITHFVHVAEKLLQLQNF
NTLMAVVGGLSHSSISRLKETHSHVSPETIKLWEGLTELVTATGNYGNYRRRLAACVGFR
FPILGVHLKDLVALQLALPDWLDPARTRLNGAKMKQLFSILEELAMVTSLRPPVQANPDL
LSLLTVSLDQYQTEDELYQLSLQREPRSKSSPTSPTSCTPPPRPPVLEEWTSAAKPKLDQ
ALVVEHIEKMVESVFRNFDVDGDGHISQEEFQIIRGNFPYLSAFGDLDQNQDGCISREEM
VSYFLRSSSVLGGRMGFVHNFQESNSLRPVACRHCKALILGIYKQGLKCRACGVNCHKQC
KDRLSVECRRRAQSVSLEGSAPSPSPMHSHHHRAFSFSLPRPGRRGSRPPEIREEEVQTV
EDGVFDIHL
Enzyme 85 Number of Residues 609
Enzyme 85 Molecular Weight 69247.8
Enzyme 85 Theoretical pI 7.85
Enzyme 85 GO Classification
Function
  • GTPase regulator activity
  • binding
  • calcium ion binding
  • cation binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • ion binding
  • metal ion binding
  • nucleoside-triphosphatase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • intracellular signaling pathway
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • signaling
  • signaling pathway
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 85 General Function Involved in calcium ion binding
Enzyme 85 Specific Function Functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. May also activates other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. Functions in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation. May function in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway
Enzyme 85 Pathways Not Available
Enzyme 85 Reactions Not Available
Enzyme 85 Pfam Domain Function
Enzyme 85 Signals
  • None
Enzyme 85 Transmembrane Regions
  • None
Enzyme 85 Essentiality Not Available
Enzyme 85 GenBank ID Protein 149158727 Link Image
Enzyme 85 UniProtKB/Swiss-Prot ID Q7LDG7 Link Image
Enzyme 85 UniProtKB/Swiss-Prot Entry Name GRP2_HUMAN Link Image
Enzyme 85 PDB ID Not Available
Enzyme 85 Cellular Location Not Available
Enzyme 85 Gene Sequence >1830 bp
ATGGCAGGCACCCTGGACCTGGACAAGGGCTGCACGGTGGAGGAGCTGCTCCGCGGGTGC
ATCGAAGCCTTCGATGACTCCGGGAAGGTGCGGGACCCGCAGCTGGTGCGCATGTTCCTC
ATGATGCACCCCTGGTACATCCCCTCCTCTCAGCTGGCGGCCAAGCTGCTCCACATCTAC
CAACAATCCCGGAAGGACAACTCCAATTCCCTGCAGGTGAAAACGTGCCACCTGGTCAGG
TACTGGATCTCCGCCTTCCCAGCGGAGTTTGACTTGAACCCGGAGTTGGCTGAGCAGATC
AAGGAGCTGAAGGCTCTGCTAGACCAAGAAGGGAACCGACGGCACAGCAGCCTAATCGAC
ATAGACAGCGTCCCTACCTACAAGTGGAAGCGGCAGGTGACTCAGCGGAACCCTGTGGGA
CAGAAAAAGCGCAAGATGTCCCTGTTGTTTGACCACCTGGAGCCCATGGAGCTGGCGGAG
CATCTCACCTACTTGGAGTATCGCTCCTTCTGCAAGATCCTGTTTCAGGACTATCACAGT
TTCGTGACTCATGGCTGCACTGTGGACAACCCCGTCCTGGAGCGGTTCATCTCCCTCTTC
AACAGCGTCTCACAGTGGGTGCAGCTCATGATCCTCAGCAAACCCACAGCCCCGCAGCGG
GCCCTGGTCATCACACACTTTGTCCACGTGGCGGAGAAGCTGCTACAGCTGCAGAACTTC
AACACGCTGATGGCAGTGGTCGGGGGCCTGAGCCACAGCTCCATCTCCCGCCTCAAGGAG
ACCCACAGCCACGTTAGCCCTGAGACCATCAAGCTCTGGGAGGGTCTCACGGAACTAGTG
ACGGCGACAGGCAACTATGGCAACTACCGGCGTCGGCTGGCAGCCTGTGTGGGCTTCCGC
TTCCCGATCCTGGGTGTGCACCTCAAGGACCTGGTGGCCCTGCAGCTGGCACTGCCTGAC
TGGCTGGACCCAGCCCGGACCCGGCTCAACGGGGCCAAGATGAAGCAGCTCTTTAGCATC
CTGGAGGAGCTGGCCATGGTGACCAGCCTGCGGCCACCAGTACAGGCCAACCCCGACCTG
CTGAGCCTGCTCACGGTGTCTCTGGATCAGTATCAGACGGAGGATGAGCTGTACCAGCTG
TCCCTGCAGCGGGAGCCGCGCTCCAAGTCCTCGCCAACCAGCCCCACGAGTTGCACCCCA
CCACCCCGGCCCCCGGTACTGGAGGAGTGGACCTCGGCTGCCAAACCCAAGCTGGATCAG
GCCCTCGTGGTGGAGCACATCGAGAAGATGGTGGAGTCTGTGTTCCGGAACTTTGACGTC
GATGGGGATGGCCACATCTCACAGGAAGAATTCCAGATCATCCGTGGGAACTTCCCTTAC
CTCAGCGCCTTTGGGGACCTCGACCAGAACCAGGATGGCTGCATCAGCAGGGAGGAGATG
GTTTCCTATTTCCTGCGCTCCAGCTCTGTGTTGGGGGGGCGCATGGGCTTCGTACACAAC
TTCCAGGAGAGCAACTCCTTGCGCCCCGTCGCCTGCCGCCACTGCAAAGCCCTGATCCTG
GGCATCTACAAGCAGGGCCTCAAATGCCGAGCCTGTGGAGTGAACTGCCACAAGCAGTGC
AAGGATCGCCTGTCAGTTGAGTGTCGGCGCAGGGCCCAGAGTGTGAGCCTGGAGGGGTCT
GCACCCTCACCCTCACCCATGCACAGCCACCATCACCGCGCCTTCAGCTTCTCTCTGCCC
CGCCCTGGCAGGCGAGGCTCCAGGCCTCCAGAGATCCGTGAGGAGGAGGTACAGACGGTG
GAGGATGGGGTGTTTGACATCCACTTGTAA
Enzyme 85 GenBank Gene ID NM_001098670.1 Link Image
Enzyme 85 GeneCard ID RASGRP2 Link Image
Enzyme 85 GenAtlas ID RASGRP2 Link Image
Enzyme 85 HGNC ID HGNC:9879 Link Image
Enzyme 85 Chromosome Location 1
Enzyme 85 Locus 11q13
Enzyme 85 SNPs SNPJam Report Link Image
Enzyme 85 General References
  1. Kedra D, Seroussi E, Fransson I, Trifunovic J, Clark M, Lagercrantz J, Blennow E, Mehlin H, Dumanski J: The germinal center kinase gene and a novel CDC25-like gene are located in the vicinity of the PYGM gene on 11q13. Hum Genet. 1997 Oct;100(5-6):611-9. [PubMed Link Image]
  2. Kawasaki H, Springett GM, Toki S, Canales JJ, Harlan P, Blumenstiel JP, Chen EJ, Bany IA, Mochizuki N, Ashbacher A, Matsuda M, Housman DE, Graybiel AM: A Rap guanine nucleotide exchange factor enriched highly in the basal ganglia. Proc Natl Acad Sci U S A. 1998 Oct 27;95(22):13278-83. [PubMed Link Image]
  3. Clyde-Smith J, Silins G, Gartside M, Grimmond S, Etheridge M, Apolloni A, Hayward N, Hancock JF: Characterization of RasGRP2, a plasma membrane-targeted, dual specificity Ras/Rap exchange factor. J Biol Chem. 2000 Oct 13;275(41):32260-7. [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. Dupuy AJ, Morgan K, von Lintig FC, Shen H, Acar H, Hasz DE, Jenkins NA, Copeland NG, Boss GR, Largaespada DA: Activation of the Rap1 guanine nucleotide exchange gene, CalDAG-GEF I, in BXH-2 murine myeloid leukemia. J Biol Chem. 2001 Apr 13;276(15):11804-11. Epub 2001 Jan 22. [PubMed Link Image]
  6. Katagiri K, Shimonaka M, Kinashi T: Rap1-mediated lymphocyte function-associated antigen-1 activation by the T cell antigen receptor is dependent on phospholipase C-gamma1. J Biol Chem. 2004 Mar 19;279(12):11875-81. Epub 2003 Dec 31. [PubMed Link Image]
  7. Caloca MJ, Zugaza JL, Vicente-Manzanares M, Sanchez-Madrid F, Bustelo XR: F-actin-dependent translocation of the Rap1 GDP/GTP exchange factor RasGRP2. J Biol Chem. 2004 May 7;279(19):20435-46. Epub 2004 Feb 26. [PubMed Link Image]
  8. Ghandour H, Cullere X, Alvarez A, Luscinskas FW, Mayadas TN: Essential role for Rap1 GTPase and its guanine exchange factor CalDAG-GEFI in LFA-1 but not VLA-4 integrin mediated human T-cell adhesion. Blood. 2007 Nov 15;110(10):3682-90. Epub 2007 Aug 16. [PubMed Link Image]
  9. Pasvolsky R, Feigelson SW, Kilic SS, Simon AJ, Tal-Lapidot G, Grabovsky V, Crittenden JR, Amariglio N, Safran M, Graybiel AM, Rechavi G, Ben-Dor S, Etzioni A, Alon R: A LAD-III syndrome is associated with defective expression of the Rap-1 activator CalDAG-GEFI in lymphocytes, neutrophils, and platelets. J Exp Med. 2007 Jul 9;204(7):1571-82. Epub 2007 Jun 18. [PubMed Link Image]
  10. Kuijpers TW, van de Vijver E, Weterman MA, de Boer M, Tool AT, van den Berg TK, Moser M, Jakobs ME, Seeger K, Sanal O, Unal S, Cetin M, Roos D, Verhoeven AJ, Baas F: LAD-1/variant syndrome is caused by mutations in FERMT3. Blood. 2009 May 7;113(19):4740-6. Epub 2008 Dec 8. [PubMed Link Image]
  11. Svensson L, Howarth K, McDowall A, Patzak I, Evans R, Ussar S, Moser M, Metin A, Fried M, Tomlinson I, Hogg N: Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation. Nat Med. 2009 Mar;15(3):306-12. Epub 2009 Feb 22. [PubMed Link Image]
  12. Malinin NL, Zhang L, Choi J, Ciocea A, Razorenova O, Ma YQ, Podrez EA, Tosi M, Lennon DP, Caplan AI, Shurin SB, Plow EF, Byzova TV: A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans. Nat Med. 2009 Mar;15(3):313-8. Epub 2009 Feb 22. [PubMed Link Image]
Enzyme 85 Metabolite References Not Available
Enzyme 86 [top]
Enzyme 86 ID 13538
Enzyme 86 Name Myosin-IXb
Enzyme 86 Synonyms
  1. Unconventional myosin-9b
Enzyme 86 Gene Name MYO9B
Enzyme 86 Protein Sequence >Myosin-IXb
MSVKEAGSSGRREQAAYHLHIYPQLSTTESQASCRVTATKDSTTSDVIKDAIASLRLDGT
KCYVLVEVKESGGEEWVLDANDSPVHRVLLWPRRAQDEHPQEDGYYFLLQERNADGTIKY
VHMQLVAQATATRRLVERGLLPRQQADFDDLCNLPELTEGNLLKNLKHRFLQQKIYTYAG
SILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKRVNQCIVYPGE
SGSGKTQSTNFLIHCLTALSQKGYASGVERTILGACPVLEAFGNAKTAHNNNSSRFGKFI
QVSYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPED
YFYLNQHNLKIEDGEDLKHDFERLKQAMEMVGFLPATKKQIFAVLSAILYLGNVTYKKRA
TGREEGLEVGPPEVLDTLSQLLKVKREILVEVLTKRKTVTVNDKLILPYSLSEAITARDS
MAKSLYSALFDWIVLRINHALLNKKDVEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYA
NEQLQYYFNQHIFKLEQEEYQGEGITWHNIGYTDNVGCIHLISKKPTGLFYLLDEESNFP
HATSQTLLAKFKQQHEDNKYFLGTPVMEPAFIIQHFAGKVKYQIKDFREKNMDYMRPDIV
ALLRGSDSSYVRELIGMDPVAVFRWAVLRAAIRAMAVLREAGRLRAERAEKAAGMSSPGA
QSHPEELPRGASTPSEKLYRDLHNQMIKSIKGLPWQGEDPRSLLQSLSRLQKPRAFILKS
KGIKQKQIIPKNLLDSKSLKLIISMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLE
ALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTE
QFQVLLPKDAQPCREVISTLLEKMKIDKRNYQIGKTKVFLKETERQALQETLHREVVRKI
LLLQSWFRMVLERRHFLQMKRAAVTIQACWRSYRVRRALERTQAAVYLQAAWRGYWQRKL
YRHQKQSIIRLQSLCRGHLQRKSFSQMISEKQKAEEKEREALEAARAGAEEGGQGQAAGG
QQVAEQGPEPAEDGGHLASEPEVQPSDRSPLEHSSPEKEAPSPEKTLPPQKTVAAESHEK
VPSSREKRESRRQRGLEHVKFQNKHIQSCKEESALREPSRRVTQEQGVSLLEDKKESRED
ETLLVVETEAENTSQKQPTEQPQAMAVGKVSEETEKTLPSGSPRPGQLERPTSLALDSRV
SPPAPGSAPETPEDKSKPCGSPRVQEKPDSPGGSTQIQRYLDAERLASAVELWRGKKLVA
AASPSAMLSQSLDLSDRHRATGAALTPTEERRTSFSTSDVSKLLPSLAKAQPAAETTDGE
RSAKKPAVQKKKPGDASSLPDAGLSPGSQVDSKSTFKRLFLHKTKDKKYSLEGAEELENA
VSGHVVLEATTMKKGLEAPSGQQHRHAAGEKRTKEPGGKGKKNRNVKIGKITVSEKWRES
VFRQITNANELKYLDEFLLNKINDLRSQKTPIESLFIEATEKFRSNIKTMYSVPNGKIHV
GYKDLMENYQIVVSNLATERGQKDTNLVLNLFQSLLDEFTRGYTKNDFEPVKQSKAQKKK
RKQERAVQEHNGHVFASYQVSIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSH
CSYTYGRKGEPGAEPGHFGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAA
NRTRELRQALQTDPAAVKLENFPIHAITGVLKQWLRELPEPLMTFAQYGDFLRAVELPEK
QEQLAAIYAVLEHLPEANHNSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDN
SDPLTSMKDVLKITTCVEMLIKEQMRKYKVKMEEISQLEAAESIAFRRLSLLRQNAPWPL
KLGFSSPYEGVLNKSPQVPRDIQEEELEVLLEEEAAGGDEDREKEILIERIQSIKEEKED
ITYRLPELDPRGSDEENLDSETSASTESLLEERAGRGASEGPPAPALPCPGAPTPSPLPT
VAAPPRRRPSSFVTVRVKTPRRTPIMPTANIKLPPGLPSHLPRWAPGAREAAAPVRRREP
PARRPDQIHSVYITPGADLPVQGALEPLEEDGQPPGAKRRYSDPPTYCLPPASGQTNG
Enzyme 86 Number of Residues 2158
Enzyme 86 Molecular Weight 243556.0
Enzyme 86 Theoretical pI 9.00
Enzyme 86 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • motor activity
  • nucleoside binding
  • nucleoside-triphosphatase activity
  • purine nucleoside binding
  • pyrophosphatase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
  • macromolecular complex
  • myosin complex
  • protein complex
Enzyme 86 General Function Involved in motor activity
Enzyme 86 Specific Function Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. May be involved in the remodeling of the actin cytoskeleton. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions. Also acts as a GTPase activating protein on Rho
Enzyme 86 Pathways Not Available
Enzyme 86 Reactions Not Available
Enzyme 86 Pfam Domain Function
Enzyme 86 Signals
  • None
Enzyme 86 Transmembrane Regions
  • None
Enzyme 86 Essentiality Not Available
Enzyme 86 GenBank ID Protein 33356170 Link Image
Enzyme 86 UniProtKB/Swiss-Prot ID Q13459 Link Image
Enzyme 86 UniProtKB/Swiss-Prot Entry Name MYO9B_HUMAN Link Image
Enzyme 86 PDB ID Not Available
Enzyme 86 Cellular Location Not Available
Enzyme 86 Gene Sequence >6474 bp
ATGAGTGTGAAAGAGGCAGGCAGCTCGGGCCGCCGGGAGCAGGCGGCCTACCACCTGCAC
ATCTACCCCCAGCTGTCCACCACCGAGAGCCAGGCCTCGTGCCGCGTGACTGCCACCAAG
GACAGCACCACCTCGGACGTCATCAAGGACGCCATTGCCAGCCTGCGGCTGGACGGCACC
AAATGTTATGTGCTGGTGGAGGTCAAAGAGTCGGGAGGCGAGGAATGGGTGCTGGACGCC
AACGACTCGCCTGTGCACCGGGTGCTGCTATGGCCCCGGCGGGCACAGGACGAGCACCCT
CAGGAGGATGGCTACTACTTCCTGCTGCAGGAGCGCAACGCAGATGGAACCATCAAGTAC
GTGCATATGCAGCTGGTGGCGCAGGCCACAGCCACCCGGCGCCTAGTGGAGCGTGGCCTC
CTGCCACGGCAGCAGGCGGACTTTGATGACCTGTGTAACCTCCCCGAGCTAACCGAGGGC
AACCTCCTGAAGAACCTCAAGCACCGCTTCCTGCAACAAAAGATCTACACGTACGCGGGG
AGCATCCTGGTGGCCATCAACCCCTTTAAGTTCCTGCCCATCTACAACCCCAAGTACGTG
AAGATGTATGAGAACCAGCAGCTGGGCAAGCTGGAGCCACACGTCTTCGCGCTGGCCGAC
GTGGCCTACTACACCATGCTCAGGAAGCGCGTGAACCAGTGCATCGTGATCTCGGGTGAG
AGCGGCTCCGGCAAGACCCAGAGCACCAACTTCCTCATCCACTGCCTCACCGCCCTCAGC
CAGAAGGGCTACGCCAGCGGCGTCGAGAGGACCATCCTGGGTGCTGGCCCTGTGCTGGAG
GCTTTTGGAAATGCCAAGACAGCCCACAACAACAACTCCAGCCGGTTTGGGAAATTCATC
CAAGTCAGCTACCTAGAGAGTGGCATCGTGAGAGGAGCTGTCGTCGAGAAATATCTGCTT
GAAAAGTCTCGCCTGGTGTCTCAGGAGAAGGATGAGAGGAACTACCATGTGTTTTATTAT
TTGTTACTTGGGGTCAGCGAGGAAGAGCGCCAAGAATTTCAGCTCAAGCAGCCTGAAGAT
TATTTCTACCTCAACCAGCATAACTTGAAGATTGAAGATGGGGAGGACCTGAAGCATGAC
TTTGAGAGGCTCAAGCAGGCCATGGAGATGGTGGGCTTCCTCCCCGCCACCAAGAAGCAG
ATTTTTGCCGTCCTCTCGGCCATCCTGTACCTGGGCAACGTCACTTATAAGAAGAGAGCT
ACAGGCCGAGAGGAAGGGTTGGAGGTCGGGCCACCCGAGGTGCTGGACACCCTGTCGCAG
CTTCTGAAGGTGAAGCGAGAAATCTTGGTGGAGGTTCTGACCAAAAGAAAAACGGTGACC
GTCAACGACAAGCTTATCCTTCCCTACAGCCTCAGCGAGGCCATCACTGCCCGCGACTCC
ATGGCCAAGTCTCTGTACAGCGCCCTGTTCGACTGGATTGTGCTGCGGATCAACCACGCA
CTCCTCAACAAGAAGGACGTGGAAGAGGCAGTCTCGTGCCTGTCCATTGGGGTCCTGGAC
ATCTTCGGGTTTGAAGACTTCGAGAGGAACAGCTTTGAGCAGTTCTGCATCAACTACGCC
AATGAGCAGCTGCAGTATTACTTCAACCAGCACATCTTCAAGCTGGAGCAGGAGGAATAT
CAGGGCGAGGGGATCACGTGGCACAACATCGGCTACACAGACAATGTCGGCTGCATCCAT
CTCATCAGCAAGAAACCCACGGGCCTCTTCTACCTGCTGGACGAGGAGAGCAACTTCCCC
CACGCCACGAGCCAGACCCTGCTGGCCAAGTTCAAACAGCAACATGAGGACAATAAGTAC
TTCCTGGGCACCCCGGTCATGGAGCCAGCTTTCATCATCCAGCACTTCGCAGGGAAGGTG
AAATATCAGATCAAGGACTTCCGGGAGAAGAACATGGACTACATGCGGCCAGACATCGTG
GCCCTGCTGCGGGGCAGTGACAGCTCCTACGTGCGGGAGCTCATCGGCATGGACCCCGTG
GCCGTGTTCCGCTGGGCCGTGCTCCGGGCTGCTATCCGGGCCATGGCAGTGCTTCGGGAG
GCCGGACGCCTGCGGGCCGAGAGGGCCGAAAAGGCTGCAGGTATGAGCAGCCCTGGTGCC
CAAAGTCACCCAGAAGAGCTGCCAAGAGGAGCCAGCACCCCTTCGGAAAAACTTTACCGC
GATTTGCATAACCAAATGATCAAGAGCATCAAAGGATTGCCCTGGCAGGGCGAGGACCCC
CGTAGCCTTCTCCAGTCCCTCAGTCGGCTCCAGAAACCCCGCGCCTTCATCCTGAAAAGT
AAAGGTATCAAACAAAAGCAGATCATTCCAAAGAACCTACTGGACTCCAAGTCCCTGAAA
CTCATCATCAGCATGACTCTGCACGACCGCACCACCAAGTCCCTACTGCACCTGCACAAG
AAGAAAAAGCCACCAAGCATCAGCGCCCAGTTCCAGACATCCCTTAACAAGCTCTTGGAG
GCACTGGGGAAGGCGGAGCCCTTCTTTATCCGCTGCATCCGTTCCAATGCTGAAAAGAAA
GAGCTGTGCTTTGACGACGAGCTGGTCCTGCAGCAGCTGCGCTACACCGGCATGCTGGAG
ACCGTGCGCATCCGGAGGTCAGGGTACAGCGCCAAGTACACGTTCCAGGATTTCACCGAG
CAGTTCCAGGTGCTCCTGCCCAAGGATGCCCAGCCCTGCAGGGAGGTCATCTCCACCCTC
CTGGAGAAAATGAAGATAGACAAGAGGAACTACCAGATCGGGAAGACCAAGGTCTTCCTG
AAGGAGACGGAGCGGCAAGCCCTGCAGGAGACGCTGCACCGGGAGGTGGTGCGGAAAATC
CTGCTGCTGCAGAGCTGGTTCCGGATGGTGCTGGAGCGTCGGCACTTCCTGCAGATGAAG
CGGGCCGCCGTCACCATCCAGGCCTGCTGGCGGTCCTACCGGGTCCGGAGGGCGCTGGAG
AGGACGCAGGCTGCCGTGTACCTCCAGGCCTCATGGAGGGGCTACTGGCAGCGGAAGCTC
TACCGGCACCAGAAACAGAGCATCATCCGCCTGCAGAGCCTGTGTCGGGGGCACCTGCAG
CGCAAGAGCTTCAGCCAGATGATCTCGGAGAAGCAGAAGGCAGAAGAGAAGGAGAGGGAA
GCCCTGGAAGCCGCAAGAGCAGGTGCTGAGGAGGGCGGACAGGGTCAGGCGGCTGGAGGG
CAGCAGGTAGCTGAGCAGGGGCCGGAGCCAGCGGAGGATGGCGGGCACCTGGCATCGGAG
CCTGAGGTGCAGCCAAGTGACAGGTCCCCCCTAGAGCACTCCTCACCTGAGAAGGAGGCC
CCAAGCCCAGAGAAGACTCTCCCACCCCAGAAAACCGTGGCGGCTGAAAGTCACGAGAAA
GTCCCCAGCAGCCGGGAGAAGCGTGAGTCGCGTCGGCAAAGAGGGCTGGAGCACGTCAAG
TTCCAGAACAAACACATCCAGTCCTGCAAGGAGGAGAGTGCCCTCAGAGAACCTTCCAGA
AGGGTCACCCAGGAGCAAGGGGTGAGTCTCCTGGAAGACAAAAAGGAGAGCAGAGAAGAT
GAAACCCTTCTAGTCGTAGAGACGGAGGCTGAGAACACATCTCAAAAGCAGCCCACAGAG
CAACCCCAGGCCATGGCAGTTGGCAAGGTCTCTGAAGAAACTGAGAAGACGCTGCCCAGT
GGGAGCCCCAGGCCTGGCCAGTTGGAGCGGCCGACCAGCCTGGCCCTGGACAGCAGGGTC
AGCCCACCGGCCCCTGGCAGCGCCCCCGAGACCCCCGAGGACAAGAGCAAACCATGTGGC
AGCCCAAGGGTTCAGGAAAAGCCCGACAGCCCCGGAGGCTCCACGCAGATCCAGCGGTAC
CTGGACGCCGAGCGGCTGGCCAGCGCCGTGGAACTGTGGCGGGGCAAGAAGCTGGTGGCC
GCCGCCAGCCCTAGTGCCATGCTCAGCCAGTCCCTGGACCTCAGCGACAGACACCGGGCC
ACAGGGGCCGCCCTCACGCCCACAGAGGAGAGGCGCACCTCCTTCTCCACGAGCGACGTC
TCCAAGCTCCTCCCGTCCCTGGCCAAGGCTCAGCCTGCAGCAGAAACCACGGACGGAGAG
CGAAGTGCGAAAAAGCCAGCTGTCCAGAAGAAGAAGCCAGGCGACGCATCCTCCCTCCCA
GACGCAGGGCTGTCCCCGGGCTCTCAGGTCGACTCTAAATCCACGTTTAAGAGGCTTTTT
CTGCATAAAACCAAGGATAAAAAATACAGCCTGGAGGGCGCAGAGGAGCTGGAGAATGCA
GTGTCCGGGCACGTGGTGCTGGAAGCCACCACCATGAAGAAGGGCCTGGAAGCCCCCTCC
GGACAGCAGCATCGCCACGCTGCAGGTGAGAAGCGCACCAAGGAACCAGGAGGCAAAGGG
AAGAAGAACCGAAATGTCAAGATTGGGAAGATCACAGTGTCAGAGAAGTGGCGGGAATCG
GTGTTCCGCCAGATCACCAACGCCAATGAGCTCAAGTACCTGGACGAGTTCCTGCTCAAC
AAGATAAATGACCTCCGTTCCCAGAAGACGCCCATTGAGAGCTTGTTTATCGAAGCCACC
GAGAAGTTCAGGAGCAACATCAAAACGATGTACTCTGTCCCGAACGGGAAGATCCACGTG
GGCTACAAGGATCTGATGGAGAACTACCAGATCGTCGTCAGCAACCTGGCCACTGAGCGT
GGCCAGAAGGACACCAACCTGGTCCTCAACCTCTTCCAGTCACTGCTAGATGAGTTCACC
CGTGGCTACACCAAGAACGACTTCGAGCCAGTGAAGCAGAGCAAAGCTCAGAAGAAGAAG
CGGAAGCAGGAGCGTGCTGTCCAGGAGCACAACGGGCACGTGTTCGCCAGCTACCAGGTT
AGCATCCCGCAGTCGTGCGAGCAGTGCCTCTCCTATATCTGGCTCATGGACAAGGCCCTG
CTCTGCAGCGTGTGCAAGATGACCTGCCACAAGAAGTGCGTGCACAAGATTCAGAGCCAC
TGCTCCTACACCTACGGGAGGAAGGGCGAGCCAGGCGTTGAGCCTGGCCACTTCGGCGTG
TGCGTAGACAGCCTGACCAGCGACAAGGCCTCGGTGCCCATCGTGCTGGAGAAGCTCCTG
GAACACGTGGAGATGCACGGCCTGTACACCGAGGGCCTCTACCGCAAGTCGGGTGCTGCC
AACCGCACTCGGGAGCTCCGGCAGGCGCTGCAGACAGACCCCGCAGCAGTCAAGCTGGAG
AACTTCCCCATCCACGCCATCACAGGGGTGCTGAAGCAGTGGCTGCGGGAGCTGCCCGAG
CCCCTCATGACCTTCGCACAGTACGGCGACTTCCTCCGAGCCGTCGAGCTGCCGGAGAAG
CAGGAGCAGCTGGCTGCCATCTATGCCGTCCTGGAGCACCTTCCAGAAGCCAACCACAAC
TCCCTGGAGAGACTCATCTTCCACCTTGTCAAGGTGGCCCTGCTCGAGGATGTCAACCGC
ATGTCACCTGGGGCGCTGGCCATTATCTTCGCACCCTGCCTCCTGCGCTGCCCTGACAAC
TCGGACCCGCTGACCAGCATGAAGGACGTCCTCAAGATCACCACGTGCGTGGAGATGCTG
ATCAAGGAGCAGATGAGGAAATACAAAGTGAAGATGGAGGAGATCAGCCAACTGGAGGCT
GCAGAGAGTATCGCCTTCCGCAGGCTTTCGCTCCTGCGACAAAATGCTCCATGGCCTCTC
AAACTGGGGTTTTCGTCTCCCTATGAGGGGGTCCTGAACAAGAGCCCCAAGACCCGGGAC
ATCCAGGAGGAGGAGCTGGAGGTGCTGCTGGAGGAGGAGGCAGCCGGCGGCGATGAGGAC
CGGGAAAAGGAGATTCTCATTGAACGGATCCAGTCCATCAAGGAGGAGAAGGAGGACATC
ACCTACCGGCTGCCGGAGCTGGACCCAAGGGGCTCGGACGAGGAGAACCTGGACTCGGAG
ACGTCGGCCAGCACCGAGAGCCTGCTGGAGGAGCGGGCCGGGCGGGGGGCCTCGGAAGGG
CCCCCTGCGCCTGCTCTCCCTTGCCCCGGCGCGCCCACCCCGAGCCCCCTCCCCACCGTG
GCCGCCCCTCCACGACGAAGGCCGTCGTCCTTCGTAACGGTCAGAGTGAAGACCCCCCGG
CGGACCCCCATCATGCCCACGGCCAACATCAAGCTCCCACCAGGCCTGCCCTCCCACCTG
CCTCGCTGGGCACCGGGTGCCCGGGAGGCGGCTGCCCCAGTGCGGCGCCGGGAGCCACCT
GCCCGCCGCCCGGACCAGATACATTCCGTGTACATCACGCCCGGGGCAGACCTGCCAGTG
CAGGGCGCCCTGGAGCCCCTAGAAGAGGATGGCCAGCCACCTGGGGCCAAGCGGAGGTAC
TCGGATCCCCCAACGTACTGCCTGCCCCCCGCCTCGGGCCAGACCAATGGCTGA
Enzyme 86 GenBank Gene ID NM_004145 Link Image
Enzyme 86 GeneCard ID MYO9B Link Image
Enzyme 86 GenAtlas ID MYO9B Link Image
Enzyme 86 HGNC ID HGNC:7609 Link Image
Enzyme 86 Chromosome Location 1
Enzyme 86 Locus 19p13.1
Enzyme 86 SNPs SNPJam Report Link Image
Enzyme 86 General References
  1. Wirth JA, Jensen KA, Post PL, Bement WM, Mooseker MS: Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail. J Cell Sci. 1996 Mar;109 ( Pt 3):653-61. [PubMed Link Image]
  2. Grewal PK, Jones AM, Maconochie M, Lemmers RJ, Frants RR, Hewitt JE: Cloning of the murine unconventional myosin gene Myo9b and identification of alternative splicing. Gene. 1999 Nov 29;240(2):389-98. [PubMed Link Image]
  3. Post PL, Bokoch GM, Mooseker MS: Human myosin-IXb is a mechanochemically active motor and a GAP for rho. J Cell Sci. 1998 Apr;111 ( Pt 7):941-50. [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. Monsuur AJ, de Bakker PI, Alizadeh BZ, Zhernakova A, Bevova MR, Strengman E, Franke L, van't Slot R, van Belzen MJ, Lavrijsen IC, Diosdado B, Daly MJ, Mulder CJ, Mearin ML, Meijer JW, Meijer GA, van Oort E, Wapenaar MC, Koeleman BP, Wijmenga C: Myosin IXB variant increases the risk of celiac disease and points toward a primary intestinal barrier defect. Nat Genet. 2005 Dec;37(12):1341-4. Epub 2005 Nov 13. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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 86 Metabolite References Not Available
Enzyme 87 [top]
Enzyme 87 ID 13789
Enzyme 87 Name Short transient receptor potential channel 6
Enzyme 87 Synonyms
  1. TrpC6
  2. Transient receptor protein 6
  3. TRP-6
Enzyme 87 Gene Name TRPC6
Enzyme 87 Protein Sequence >Short transient receptor potential channel 6
MSQSPAFGPRRGSSPRGAAGAAARRNESQDYLLMDSELGEDGCPQAPLPCYGYYPCFRGS
DNRLAHRRQTVLREKGRRLANRGPAYMFSDRSTSLSIEEERFLDAAEYGNIPVVRKMLEE
CHSLNVNCVDYMGQNALQLAVANEHLEITELLLKKENLSRVGDALLLAISKGYVRIVEAI
LSHPAFAEGKRLATSPSQSELQQDDFYAYDEDGTRFSHDVTPIILAAHCQEYEIVHTLLR
KGARIERPHDYFCKCNDCNQKQKHDSFSHSRSRINAYKGLASPAYLSLSSEDPVMTALEL
SNELAVLANIEKEFKNDYKKLSMQCKDFVVGLLDLCRNTEEVEAILNGDVETLQSGDHGR
PNLSRLKLAIKYEVKKFVAHPNCQQQLLSIWYENLSGLRQQTMAVKFLVVLAVAIGLPFL
ALIYWFAPCSKMGKIMRGPFMKFVAHAASFTIFLGLLVMNAADRFEGTKLLPNETSTDNA
KQLFRMKTSCFSWMEMLIISWVIGMIWAECKEIWTQGPKEYLFELWNMLDFGMLAIFAAS
FIARFMAFWHASKAQSIIDANDTLKDLTKVTLGDNVKYYNLARIKWDPSDPQIISEGLYA
IAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVIFIMVFVAFMIGMFNLYSYYI
GAKQNEAFTTVEESFKTLFWAIFGLSEVKSVVINYNHKFIENIGYVLYGVYNVTMVIVLL
NMLIAMINSSFQEIEDDADVEWKFARAKLWFSYFEEGRTLPVPFNLVPSPKSLFYLLLKL
KKWISELFQGHKKGFQEDAEMNKINEEKKLGILGSHEDLSKLSLDKKQVGHNKQPSIRSS
EDFHLNSFNNPPRQYQKIMKRLIKRYVLQAQIDKESDEVNEGELKEIKQDISSLRYELLE
EKSQNTEDLAELIRELGEKLSMEPNQEETNR
Enzyme 87 Number of Residues 931
Enzyme 87 Molecular Weight 106325.3
Enzyme 87 Theoretical pI 6.64
Enzyme 87 GO Classification
Function
  • calcium channel activity
  • cation channel activity
  • ion channel activity
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • calcium ion transport
  • cation transport
  • di-, tri-valent inorganic cation transport
  • divalent metal ion transport
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 87 General Function Involved in ion channel activity
Enzyme 87 Specific Function Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C. Seems not to be activated by intracellular calcium store depletion
Enzyme 87 Pathways Not Available
Enzyme 87 Reactions Not Available
Enzyme 87 Pfam Domain Function
Enzyme 87 Signals
  • None
Enzyme 87 Transmembrane Regions
  • 439-459 488-508 522-542 593-613 637-657 707-727
Enzyme 87 Essentiality Not Available
Enzyme 87 GenBank ID Protein Not Available
Enzyme 87 UniProtKB/Swiss-Prot ID Q9Y210 Link Image
Enzyme 87 UniProtKB/Swiss-Prot Entry Name TRPC6_HUMAN Link Image
Enzyme 87 PDB ID Not Available
Enzyme 87 Cellular Location Not Available
Enzyme 87 Gene Sequence >2796 bp
ATGAGCCAGAGCCCGGCGTTCGGGCCCCGGAGGGGCAGTTCTCCCCGGGGCGCTGCCGGA
GCCGCTGCGCGGCGCAACGAGAGCCAGGACTATCTGCTCATGGACTCGGAGCTGGGAGAA
GACGGCTGCCCGCAAGCCCCGCTGCCTTGCTACGGCTACTACCCCTGCTTCCGGGGATCT
GACAACAGACTGGCTCACCGGCGGCAGACAGTTCTCCGTGAGAAGGGGAGAAGGTTAGCT
AATCGAGGACCAGCATACATGTTTAGTGATCGCTCCACAAGCCTATCTATAGAGGAGGAA
CGCTTTTTGGATGCAGCTGAATATGGTAACATCCCAGTGGTGCGGAAGATGTTAGAAGAA
TGCCACTCACTCAACGTTAACTGTGTGGATTACATGGGCCAGAATGCCCTACAGTTGGCA
GTGGCCAATGAGCATCTGGAAATTACAGAACTTCTTCTCAAGAAAGAAAACCTCTCTCGA
GTTGGGGATGCTTTGCTTCTAGCTATTAGTAAAGGTTATGTTCGGATTGTGGAAGCAATT
CTCAGTCATCCGGCTTTTGCTGAAGGCAAGAGGTTAGCAACCAGCCCTAGCCAGTCTGAA
CTCCAGCAAGATGATTTTTATGCCTATGATGAAGATGGGACACGGTTCTCCCATGATGTG
ACTCCAATCATTCTGGCTGCCCACTGCCAGGAATATGAAATTGTGCATACCCTCCTGCGG
AAGGGTGCTAGGATTGAACGGCCTCATGATTATTTCTGCAAGTGCAATGACTGCAACCAG
AAACAGAAGCATGACTCGTTTAGCCACTCCAGATCTAGGATTAATGCCTATAAAGGCCTG
GCAAGTCCGGCTTACCTGTCATTGTCTAGTGAAGATCCAGTCATGACGGCTTTAGAACTT
AGCAATGAACTGGCAGTTCTGGCCAATATTGAGAAAGAGTTCAAGAATGACTACAAAAAA
CTGTCAATGCAGTGCAAAGACTTTGTTGTTGGACTCCTTGATCTGTGCAGAAACACTGAA
GAAGTCGAGGCCATTCTGAATGGGGATGTTGAAACGCTCCAGAGTGGTGATCACGGTCGC
CCAAATCTCAGCCGTTTAAAACTTGCCATTAAATATGAAGTAAAAAAATTTGTAGCTCAT
CCAAACTGCCAACAGCAACTTCTCTCCATTTGGTATGAGAATCTTTCTGGTTTACGACAG
CAGACAATGGCGGTCAAGTTCCTTGTGGTCCTTGCTGTTGCCATTGGACTGCCCTTCCTG
GCTCTCATTTACTGGTTTGCTCCATGCAGCAAGATGGGGAAGATAATGCGTGGACCATTC
ATGAAGTTTGTAGCACACGCAGCCTCCTTCACCATTTTTCTGGGACTGCTAGTCATGAAT
GCAGCTGACAGATTTGAAGGCACAAAACTCCTTCCTAATGAAACCAGCACAGATAATGCA
AAACAGCTGTTCAGGATGAAAACATCCTGCTTCTCATGGATGGAGATGCTCATTATATCC
TGGGTAATAGGCATGATATGGGCTGAATGTAAAGAAATCTGGACTCAGGGCCCCAAGGAA
TATTTGTTTGAGTTGTGGAACATGCTTGATTTTGGTATGTTAGCAATTTTCGCAGCATCA
TTCATTGCGAGATTCATGGCATTTTGGCATGCTTCCAAAGCCCAGAGCATCATTGACGCA
AACGATACTTTGAAGGACTTGACGAAAGTAACATTGGGAGACAATGTGAAATACTACAAT
TTGGCCAGGATAAAGTGGGACCCCTCTGATCCTCAAATAATATCTGAAGGTCTTTATGCA
ATTGCTGTAGTTTTAAGTTTCTCTAGGATAGCTTATATTTTACCAGCAAATGAAAGCTTT
GGACCTCTGCAGATATCACTTGGAAGAACAGTCAAAGACATCTTCAAGTTCATGGTCATA
TTCATTATGGTGTTTGTGGCCTTTATGATTGGAATGTTCAATCTCTACTCCTACTACATT
GGTGCAAAACAAAATGAAGCCTTCACAACAGTTGAAGAGAGTTTTAAGACACTGTTCTGG
GCTATATTTGGACTTTCTGAAGTGAAATCAGTGGTCATCAACTATAACCACAAATTCATT
GAAAACATTGGTTACGTTCTTTATGGAGTCTATAATGTTACGATGGTCATTGTTTTGCTA
AATATGTTAATTGCCATGATCAACAGTTCATTCCAGGAAATTGAGGATGACGCTGATGTG
GAGTGGAAATTTGCAAGGGCCAAACTCTGGTTTTCCTACTTTGAGGAGGGCAGAACACTT
CCTGTACCCTTCAATCTGGTGCCGAGTCCAAAGTCCCTGTTTTATCTCTTACTGAAGCTT
AAAAAATGGATTTCTGAGCTGTTCCAGGGCCATAAAAAAGGTTTCCAGGAAGATGCAGAG
ATGAACAAGATAAATGAAGAAAAGAAACTTGGAATTTTAGGAAGTCATGAAGACCTTTCA
AAATTATCACTTGACAAAAAACAGGTTGGGCACAATAAACAACCAAGTATAAGGAGCTCA
GAAGATTTCCATCTAAATAGTTTCAATAATCCTCCAAGACAATATCAGAAAATAATGAAA
AGGCTCATTAAAAGATATGTACTGCAGGCCCAGATAGATAAGGAGAGTGATGAAGTGAAC
GAAGGGGAACTGAAGGAAATTAAGCAGGACATCTCAAGTCTCCGCTATGAACTCCTTGAA
GAAAAATCTCAGAATACAGAAGACCTAGCAGAACTTATTAGAGAACTTGGAGAGAAATTA
TCCATGGAACCAAATCAAGAGGAAACCAATAGATAA
Enzyme 87 GenBank Gene ID AF080394 Link Image
Enzyme 87 GeneCard ID TRPC6 Link Image
Enzyme 87 GenAtlas ID TRPC6 Link Image
Enzyme 87 HGNC ID HGNC:12338 Link Image
Enzyme 87 Chromosome Location 1
Enzyme 87 Locus 11q22.1
Enzyme 87 SNPs SNPJam Report Link Image
Enzyme 87 General References
  1. Hofmann T, Obukhov AG, Schaefer M, Harteneck C, Gudermann T, Schultz G: Direct activation of human TRPC6 and TRPC3 channels by diacylglycerol. Nature. 1999 Jan 21;397(6716):259-63. [PubMed Link Image]
  2. D'Esposito M, Strazzullo M, Cuccurese M, Spalluto C, Rocchi M, D'Urso M, Ciccodicola A: Identification and assignment of the human transient receptor potential channel 6 gene TRPC6 to chromosome 11q21-->q22. Cytogenet Cell Genet. 1998;83(1-2):46-7. [PubMed Link Image]
  3. Philipp S, Trost C, Warnat J, Rautmann J, Himmerkus N, Schroth G, Kretz O, Nastainczyk W, Cavalie A, Hoth M, Flockerzi V: TRP4 (CCE1) protein is part of native calcium release-activated Ca2+-like channels in adrenal cells. J Biol Chem. 2000 Aug 4;275(31):23965-72. [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. Lussier MP, Cayouette S, Lepage PK, Bernier CL, Francoeur N, St-Hilaire M, Pinard M, Boulay G: MxA, a member of the dynamin superfamily, interacts with the ankyrin-like repeat domain of TRPC. J Biol Chem. 2005 May 13;280(19):19393-400. Epub 2005 Mar 9. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Lussier MP, Lepage PK, Bousquet SM, Boulay G: RNF24, a new TRPC interacting protein, causes the intracellular retention of TRPC. Cell Calcium. 2008 May;43(5):432-43. Epub 2007 Sep 11. [PubMed Link Image]
  8. 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]
  9. Reiser J, Polu KR, Moller CC, Kenlan P, Altintas MM, Wei C, Faul C, Herbert S, Villegas I, Avila-Casado C, McGee M, Sugimoto H, Brown D, Kalluri R, Mundel P, Smith PL, Clapham DE, Pollak MR: TRPC6 is a glomerular slit diaphragm-associated channel required for normal renal function. Nat Genet. 2005 Jul;37(7):739-44. Epub 2005 May 27. [PubMed Link Image]
  10. Winn MP, Conlon PJ, Lynn KL, Farrington MK, Creazzo T, Hawkins AF, Daskalakis N, Kwan SY, Ebersviller S, Burchette JL, Pericak-Vance MA, Howell DN, Vance JM, Rosenberg PB: A mutation in the TRPC6 cation channel causes familial focal segmental glomerulosclerosis. Science. 2005 Jun 17;308(5729):1801-4. Epub 2005 May 5. [PubMed Link Image]
Enzyme 87 Metabolite References Not Available
Enzyme 88 [top]
Enzyme 88 ID 13790
Enzyme 88 Name Short transient receptor potential channel 7
Enzyme 88 Synonyms
  1. TrpC7
  2. Transient receptor protein 7
  3. TRP-7
  4. hTRP7
Enzyme 88 Gene Name TRPC7
Enzyme 88 Protein Sequence >Short transient receptor potential channel 7
MLRNSTFKNMQRRHTTLREKGRRQAIRGPAYMFNEKGTSLTPEEERFLDSAEYGNIPVVR
KMLEESKTLNFNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARVGDALLLAISKGYVR
IVEAILNHPAFAQGQRLTLSPLEQELRDDDFYAYDEDGTRFSHDITPIILAAHCQEYEIV
HILLLKGARIERPHDYFCKCNECTEKQRKDSFSHSRSRMNAYKGLASAAYLSLSSEDPVL
TALELSNELARLANIETEFKNDYRKLSMQCKDFVVGVLDLCRDTEEVEAILNGDVNFQVW
SDHHRPSLSRIKLAIKYEVKKFVAHPNCQQQLLTMWYENLSGLRQQSIAVKFLAVFGVSI
GLPFLAIAYWIAPCSKLGRTLRSPFMKFVAHAVSFTIFLGLLVVNASDRFEGVKTLPNET
FTDYPKQIFRVKTTQFSWTEMLIMKWVLGMIWSECKEIWEEGPREYVLHLWNLLDFGMLS
IFVASFTARFMAFLKATEAQLYVDQHVQDDTLHNVSLPPEVAYFTYARDKWWPSDPQIIS
EGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVIFIMVFVAFMIGMFNL
YSYYRGAKYNPAFTTVEESFKTLFWSIFGLSEVISVVLKYDHKFIENIGYVLYGVYNVTM
VVVLLNMLIAMINNSYQEIEEDADVEWKFARAKLWLSYFDEGRTLPAPFNLVPSPKSFYY
LIMRIKMCLIKLCKSKAKSCENDLEMGMLNSKFKKTRYQAGMRNSENLTANNTLSKPTRY
QKIMKRLIKRYVLKAQVDRENDEVNEGELKEIKQDISSLRYELLEEKSQATGELADLIQQ
LSEKFGKNLNKDHLRVNKGKDI
Enzyme 88 Number of Residues 862
Enzyme 88 Molecular Weight 99561.3
Enzyme 88 Theoretical pI 7.98
Enzyme 88 GO Classification
Function
  • calcium channel activity
  • cation channel activity
  • ion channel activity
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • calcium ion transport
  • cation transport
  • di-, tri-valent inorganic cation transport
  • divalent metal ion transport
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 88 General Function Involved in ion channel activity
Enzyme 88 Specific Function Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG). May also be activated by intracellular calcium store depletion
Enzyme 88 Pathways Not Available
Enzyme 88 Reactions Not Available
Enzyme 88 Pfam Domain Function
Enzyme 88 Signals
  • None
Enzyme 88 Transmembrane Regions
  • 352-372 384-404 466-486 538-558 582-602 652-672
Enzyme 88 Essentiality Not Available
Enzyme 88 GenBank ID Protein 9798452 Link Image
Enzyme 88 UniProtKB/Swiss-Prot ID Q9HCX4 Link Image
Enzyme 88 UniProtKB/Swiss-Prot Entry Name TRPC7_HUMAN Link Image
Enzyme 88 PDB ID Not Available
Enzyme 88 Cellular Location Not Available
Enzyme 88 Gene Sequence >2589 bp
ATGTTGAGGAACAGCACCTTCAAAAACATGCAGCGCCGGCACACAACGCTGAGGGAGAAG
GGCCGTCGCCAGGCCATCCGGGGTCCCGCCTACATGTTCAACGAGAAGGGCACCAGTCTG
ACGCCCGAGGAGGAGCGCTTCCTGGACTCGGCTGAGTATGGCAACATCCCGGTGGTCCGG
AAAATGCTGGAGGAGTCCAAGACCCTTAACTTCAACTGTGTGGACTACATGGGGCAGAAC
GCTCTGCAGCTGGCCGTGGGCAACGAGCACCTAGAGGTCACGGAGCTGCTGCTGAAGAAG
GAGAACCTGGCACGGGTGGGGGACGCGCTGCTGCTGGCCATCAGCAAGGGCTATGTGCGC
ATCGTGGAGGCCATCCTCAACCACCCGGCCTTCGCGCAGGGCCAGCGCCTGACGCTCAGC
CCGCTGGAACAGGAGCTGCGCGACGACGACTTCTATGCCTACGACGAGGACGGCACGCGC
TTCTCCCACGACATCACGCCCATCATCCTGGCGGCGCACTGCCAGGAGTATGAGATCGTG
CACATCCTGCTGCTCAAGGGCGCCCGCATCGAGCGGCCCCACGACTACTTCTGCAAGTGC
AATGAGTGCACCGAGAAACAGCGGAAAGACTCCTTCAGCCACTCGCGCTCGCGCATGAAC
GCCTACAAAGGACTGGCGAGTGCTGCCTACTTGTCCCTGTCCAGCGAAGACCCTGTCCTC
ACCGCCCTGGAGCTCAGCAACGAGTTAGCCAGACTAGCCAACATTGAGACTGAATTTAAG
AACGATTACAGGAAGTTATCTATGCAATGCAAGGATTTTGTAGTGGGCGTGCTGGACCTG
TGCCGAGACACAGAAGAGGTGGAAGCAATTTTAAACGGTGATGTGAACTTCCAAGTCTGG
TCCGACCACCACCGTCCAAGTCTGAGCCGGATCAAACTCGCCATTAAATATGAAGTCAAG
AAGTTCGTTGCTCATCCTAACTGTCAGCAGCAATTGCTTACCATGTGGTATGAAAATCTC
TCAGGCTTACGTCAACAGTCTATCGCTGTGAAATTCCTGGCTGTCTTTGGAGTCTCCATA
GGCCTCCCTTTTCTCGCCATAGCCTATTGGATTGCTCCGTGCAGCAAGCTAGGACGAACC
CTGAGGAGCCCTTTCATGAAGTTTGTAGCTCATGCAGTTTCTTTTACAATCTTCTTGGGA
TTATTAGTTGTGAATGCATCTGACCGATTTGAAGGTGTTAAAACCCTGCCAAACGAAACC
TTCACAGACTACCCAAAACAAATCTTCAGAGTGAAAACCACACAGTTCTCCTGGACAGAA
ATGCTCATTATGAAGTGGGTCTTAGGAATGATTTGGTCCGAATGCAAGGAAATCTGGGAG
GAGGGGCCACGGGAGTACGTGCTGCACTTGTGGAACCTGCTAGATTTCGGGATGCTGTCC
ATCTTCGTGGCCTCCTTCACAGCACGCTTCATGGCCTTCCTGAAGGCCACGGAGGCACAG
CTGTACGTGGACCAGCACGTGCAGGACGACACGCTGCACAATGTCTCGCTTCCGCCGGAA
GTGGCATACTTCACCTACGCCAGGGACAAGTGGTGGCCTTCAGACCCTCAGATCATATCG
GAAGGGCTCTACGCGATAGCCGTCGTGCTGAGCTTCTCTCGCATTGCATACATTCTGCCA
GCCAACGAGAGTTTTGGGCCCCTGCAGATCTCGCTAGGGAGAACTGTGAAAGATATCTTC
AAGTTCATGGTCATTTTCATCATGGTATTTGTGGCCTTCATGATTGGGATGTTCAACCTG
TACTCTTACTACCGAGGTGCCAAATACAACCCAGCGTTTACAACGGTTGAAGAAAGTTTT
AAAACTTTGTTTTGGTCCATATTCGGCTTATCTGAAGTAATCTCAGTGGTGCTGAAATAC
GACCACAAATTCATCGAGAACATTGGCTACGTTCTCTACGGCGTTTATAACGTCACCATG
GTGGTAGTGTTGCTCAACATGCTAATAGCCATGATAAACAACTCCTATCAGGAAATTGAG
GAGGATGCAGATGTGGAATGGAAGTTCGCCCGAGCAAAACTCTGGCTGTCTTACTTTGAT
GAAGGAAGAACTCTACCTGCTCCTTTTAATCTAGTGCCAAGTCCTAAATCATTTTATTAT
CTCATAATGAGAATCAAGATGTGCCTCATAAAACTCTGCAAATCTAAGGCCAAAAGCTGT
GAAAATGACCTTGAAATGGGCATGCTGAATTCCAAATTCAAGAAGACTCGCTACCAGGCT
GGCATGAGGAATTCTGAAAATCTGACAGCAAATAACACTTTGAGCAAGCCCACCAGATAC
CAGAAAATCATGAAACGGCTCATAAAAAGATACGTCCTGAAAGCCCAGGTGGACAGAGAA
AATGACGAAGTCAATGAAGGCGAGCTGAAGGAAATCAAGCAAGATATCTCCAGCCTGCGC
TATGAGCTTCTTGAGGAAAAATCTCAAGCTACTGGTGAGCTGGCAGACCTGATTCAACAA
CTCAGCGAGAAGTTTGGAAAGAACTTAAACAAAGACCACCTGAGGGTGAACAAGGGCAAA
GACATTTAG
Enzyme 88 GenBank Gene ID AJ272034 Link Image
Enzyme 88 GeneCard ID TRPC7 Link Image
Enzyme 88 GenAtlas ID TRPC7 Link Image
Enzyme 88 HGNC ID HGNC:20754 Link Image
Enzyme 88 Chromosome Location 5
Enzyme 88 Locus 5q31.1
Enzyme 88 SNPs SNPJam Report Link Image
Enzyme 88 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Lussier MP, Cayouette S, Lepage PK, Bernier CL, Francoeur N, St-Hilaire M, Pinard M, Boulay G: MxA, a member of the dynamin superfamily, interacts with the ankyrin-like repeat domain of TRPC. J Biol Chem. 2005 May 13;280(19):19393-400. Epub 2005 Mar 9. [PubMed Link Image]
  3. Lussier MP, Lepage PK, Bousquet SM, Boulay G: RNF24, a new TRPC interacting protein, causes the intracellular retention of TRPC. Cell Calcium. 2008 May;43(5):432-43. Epub 2007 Sep 11. [PubMed Link Image]
Enzyme 88 Metabolite References Not Available
Enzyme 89 [top]
Enzyme 89 ID 13805
Enzyme 89 Name Protein unc-13 homolog A
Enzyme 89 Synonyms
  1. Munc13-1
Enzyme 89 Gene Name UNC13A
Enzyme 89 Protein Sequence >Protein unc-13 homolog A
MSLLCVGVKKAKFDGAQEKFNTYVTLKVQNVKSTTIAVRGSQPSWEQDFMFEINRLDLGL
TVEVWNKGLIWDTMVGTVWIPLRTIRQSNEEGPGEWLTLDSQVIMADSEICGTKDPTFHR
ILLDTRFELPLDIPEEEARYWAKKLEQLNAMRDQDEYSFQDEQDKPLPVPSNQCCNWNYF
GWGEQHNDDPDSAVDDRDSDYRSETSNSIPPPYYTTSQPNASVHQYSVRPPPLGSRESYS
DSMHSYEEFSEPQALSPTGSSRYASSGELSQGSSQLSEDFDPDEHSLQGSDMEDERDRDS
YHSCHSSVSYHKDSPRWDQDEEELEEDLEDFLEEEELPEDEEELEEEEEEVPDDLGSYAQ
REDVAVAEPKDFKRISLPPAAPGKEDKAPVAPTEAPDMAKVAPKPATPDKVPAAEQIPEA
EPPKDEESFRPREDEEGQEGQDSMSRAKANWLRAFNKVRMQLQEARGEGEMSKSLWFKGG
PGGGLIIIDSMPDIRKRKPIPLVSDLAMSLVQSRKAGITSALASSTLNNEELKNHVYKKT
LQALIYPISCTTPHNFEVWTATTPTYCYECEGLLWGIARQGMRCTECGVKCHEKCQDLLN
ADCLQRAAEKSSKHGAEDRTQNIIMVLKDRMKIRERNKPEIFELIQEIFAVTKTAHTQQM
KAVKQSVLDGTSKWSAKISITVVCAQGLQAKDKTGSSDPYVTVQVGKTKKRTKTIYGNLN
PVWEENFHFECHNSSDRIKVRVWDEDDDIKSRVKQRFKRESDDFLGQTIIEVRTLSGEMD
VWYNLDKRTDKSAVSGAIRLHISVEIKGEEKVAPYHVQYTCLHENLFHFVTDVQNNGVVK
IPDAKGDDAWKVYYDETAQEIVDEFAMRYGVESIYQAMTHFACLSSKYMCPGVPAVMSTL
LANINAYYAHTTASTNVSASDRFAASNFGKERFVKLLDQLHNSLRIDLSMYRNNFPASSP
ERLQDLKSTVDLLTSITFFRMKVQELQSPPRASQVVKDCVKACLNSTYEYIFNNCHELYS
REYQTDPAKKGEVPPEEQGPSIKNLDFWSKLITLIVSIIEEDKNSYTPCLNQFPQELNVG
KISAEVMWNLFAQDMKYAMEEHDKHRLCKSADYMNLHFKVKWLYNEYVTELPAFKDRVPE
YPAWFEPFVIQWLDENEEVSRDFLHGALERDKKDGFQQTSEHALFSCSVVDVFSQLNQSF
EIIKKLECPDPQIVGHYMRRFAKTISNVLLQYADIISKDFASYCSKEKEKVPCILMNNTQ
QLRVQLEKMFEAMGGKELDAEASDILKELQVKLNNVLDELSRVFATSFQPHIEECVKQMG
DILSQVKGTGNVPASACSSVAQDADNVLQPIMDLLDSNLTLFAKICEKTVLKRVLKELWK
LVMNTMEKTIVLPPLTDQTMIGNLLRKHGKGLEKGRVKLPSHSDGTQMIFNAAKELGQLS
KLKDHMVREEAKSLTPKQCAVVELALDTIKQYFHAGGVGLKKTFLEKSPDLQSLRYALSL
YTQATDLLIKTFVQTQSAQGLGVEDPVGEVSVHVELFTHPGTGEHKVTVKVVAANDLKWQ
TSGIFRPFIEVNIIGPQLSDKKRKFATKSKNNSWAPKYNESFQFTLSADAGPECYELQVC
VKDYCFAREDRTVGLAVLQLRELAQRGSAACWLPLGRRIHMDDTGLTVLRILSQRSNDEV
AKEFVKLKSDTRSAEEGGAAPAP
Enzyme 89 Number of Residues 1703
Enzyme 89 Molecular Weight 192996.4
Enzyme 89 Theoretical pI 5.00
Enzyme 89 GO Classification
Function
Process
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 89 General Function Involved in intracellular signaling pathway
Enzyme 89 Specific Function Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in most excitatory/glutamatergic but not inhibitory/GABA-mediated synapses. Also involved in secretory granule priming in insulin secretion. Interacts with FBXO45 (via SRY domain); leading to the degradation of UNC13A by the proteasome
Enzyme 89 Pathways Not Available
Enzyme 89 Reactions Not Available
Enzyme 89 Pfam Domain Function
Enzyme 89 Signals
  • None
Enzyme 89 Transmembrane Regions
  • None
Enzyme 89 Essentiality Not Available
Enzyme 89 GenBank ID Protein 283837842 Link Image
Enzyme 89 UniProtKB/Swiss-Prot ID Q9UPW8 Link Image
Enzyme 89 UniProtKB/Swiss-Prot Entry Name UN13A_HUMAN Link Image
Enzyme 89 PDB ID 1Y8F Link Image
Enzyme 89 PDB File Show
Enzyme 89 3D Structure
Enzyme 89 Cellular Location Not Available
Enzyme 89 Gene Sequence >5112 bp
ATGTCTCTGCTTTGCGTTGGAGTCAAAAAAGCCAAGTTTGATGGTGCCCAAGAGAAATTC
AACACGTACGTGACCCTGAAAGTGCAGAATGTCAAGAGCACGACCATCGCGGTGCGGGGC
AGCCAGCCCAGCTGGGAGCAGGATTTCATGTTCGAGATTAACCGTCTGGATTTGGGACTG
ACGGTGGAGGTGTGGAATAAGGGTCTCATCTGGGACACAATGGTGGGCACTGTGTGGATC
CCACTGAGGACCATCCGCCAGTCCAATGAGGAGGGCCCTGGAGAGTGGCTGACGCTGGAC
TCCCAGGTCATCATGGCAGACAGTGAGATCTGTGGCACCAAGGACCCCACCTTCCACCGC
ATCCTCCTGGACACGCGCTTTGAGCTACCCTTAGACATTCCTGAAGAGGAGGCTCGCTAC
TGGGCCAAGAAGCTGGAGCAGCTCAATGCTATGCGGGACCAGGATGAATATTCGTTCCAA
GATGAGCAAGACAAGCCTCTGCCTGTCCCCAGCAACCAGTGCTGCAACTGGAATTATTTT
GGCTGGGGTGAGCAGCACAACGATGACCCCGACAGTGCAGTGGATGATCGTGACAGTGAC
TACCGCAGTGAAACGAGCAACAGCATCCCGCCGCCCTATTATACTACGTCACAACCCAAC
GCCTCAGTCCACCAATATTCTGTTCGCCCACCACCCCTGGGCTCCCGGGAGTCCTACAGT
GACTCCATGCACAGTTACGAGGAGTTCTCTGAGCCACAAGCCCTCAGCCCCACGGGTAGC
AGCCGCTATGCCTCTTCCGGGGAGCTGAGCCAGGGAAGCTCTCAGCTGAGCGAGGACTTC
GACCCTGACGAGCACAGCCTGCAGGGCTCCGACATGGAGGATGAGCGGGACCGGGACTCC
TACCACTCCTGCCACAGCTCGGTCAGCTACCACAAAGACTCGCCTCGCTGGGACCAGGAT
GAGGAAGAGCTGGAGGAGGACCTGGAGGACTTCCTGGAGGAGGAGGAGCTGCCTGAAGAT
GAGGAGGAGCTGGAGGAGGAGGAGGAGGAGGTGCCTGACGATTTGGGCAGCTATGCCCAG
CGTGAAGACGTAGCTGTGGCTGAGCCCAAAGACTTCAAACGCATCAGCCTCCCGCCAGCT
GCCCCAGGGAAGGAGGACAAGGCCCCAGTGGCACCCACCGAGGCCCCCGACATGGCCAAG
GTGGCCCCCAAGCCAGCCACGCCCGACAAGGTGCCTGCAGCTGAGCAGATCCCTGAGGCT
GAGCCACCCAAGGACGAGGAGAGTTTCAGGCCGAGAGAGGATGAGGAAGGCCAGGAGGGG
CAGGACTCCATGTCCAGGGCCAAGGCCAACTGGCTGCGTGCCTTCAACAAGGTGCGGATG
CAGCTGCAGGAGGCCCGGGGAGAAGGAGAGATGTCTAAATCCCTATGGTTCAAAGGCGGC
CCAGGGGGCGGTCTCATCATCATCGACAGCATGCCAGACATCCGCAAGAGGAAACCTATC
CCACTCGTGAGCGACTTGGCCATGTCCCTGGTCCAGTCCAGGAAAGCGGGCATCACCTCG
GCCTTGGCCTCCAGCACGTTGAACAACGAGGAGCTGAAAAACCACGTTTACAAGAAGACC
CTGCAAGCCTTAATCTACCCCATCTCGTGCACGACGCCACACAACTTCGAAGTGTGGACG
GCCACCACGCCCACCTACTGCTACGAGTGCGAGGGGCTGCTGTGGGGCATCGCGAGGCAG
GGCATGCGCTGCACCGAGTGCGGTGTCAAGTGCCACGAGAAGTGCCAGGACCTGCTCAAC
GCCGACTGCCTGCAGCGGGCTGCGGAGAAGAGCTCCAAGCACGGGGCGGAGGACCGGACA
CAGAACATCATCATGGTGCTCAAGGACCGCATGAAGATCCGGGAGCGCAACAAGCCCGAG
ATCTTCGAGCTCATCCAGGAGATCTTCGCGGTGACCAAGACGGCGCACACGCAGCAGATG
AAGGCGGTCAAGCAGAGCGTGCTGGACGGCACGTCCAAGTGGTCCGCCAAGATCAGCATC
ACCGTGGTCTGCGCCCAGGGCTTGCAGGCAAAGGACAAGACAGGATCCAGTGACCCCTAT
GTCACCGTCCAGGTCGGGAAGACCAAGAAACGGACAAAAACCATCTATGGGAACCTCAAC
CCGGTGTGGGAGGAGAATTTCCACTTTGAATGTCACAATTCCTCCGACCGCATCAAGGTG
CGCGTCTGGGACGAGGATGACGACATCAAATCCCGCGTGAAACAGAGGTTCAAGAGGGAA
TCTGACGATTTCCTGGGGCAGACGATCATTGAGGTGCGGACGCTCAGCGGCGAGATGGAC
GTGTGGTACAACCTGGACAAGCGAACTGACAAATCTGCCGTGTCGGGTGCCATCCGGCTC
CACATCAGTGTGGAGATCAAAGGCGAGGAGAAGGTGGCCCCGTACCATGTCCAGTACACC
TGTCTGCATGAGAACCTGTTCCACTTCGTGACCGACGTGCAGAACAATGGGGTCGTGAAG
ATCCCAGATGCCAAGGGTGACGATGCCTGGAAGGTTTACTACGATGAGACAGCCCAGGAG
ATTGTGGACGAGTTTGCCATGCGCTACGGCGTCGAGTCCATCTACCAAGCCATGACCCAC
TTTGCCTGCCTCTCCTCCAAGTATATGTGCCCAGGGGTGCCTGCCGTCATGAGCACCCTG
CTCGCCAACATCAATGCCTACTACGCACACACCACCGCCTCCACCAACGTGTCTGCCTCC
GACCGCTTCGCCGCCTCCAACTTTGGGAAAGAGCGCTTCGTGAAACTCCTGGACCAGCTG
CATAACTCCCTGCGGATTGACCTCTCCATGTACCGGAATAACTTCCCAGCCAGCAGCCCG
GAGAGACTCCAGGACCTCAAATCCACTGTGGACCTTCTCACCAGCATCACCTTCTTTCGG
ATGAAGGTACAAGAACTCCAGAGCCCGCCCCGAGCCAGCCAGGTGGTAAAGGACTGTGTG
AAAGCCTGCCTTAATTCTACCTACGAGTACATCTTCAATAACTGCCATGAACTGTACAGC
CGGGAGTACCAGACAGACCCGGCCAAGAAGGGGGAAGTTCTCCCAGAGGAACAGGGGCCC
AGCATCAAGAACCTCGACTTCTGGTCCAAGCTGATTACCCTCATAGTGTCCATCATTGAG
GAAGACAAGAATTCCTACACTCCCTGCCTCAACCAGTTTCCCCAGGAGCTGAATGTGGGT
AAAATCAGCGCTGAAGTGATGTGGAATCTGTTTGCCCAAGACATGAAGTACGCCATGGAG
GAGCACGACAAGCATCGTCTATGCAAGAGTGCCGACTACATGAACCTCCACTTCAAGGTG
AAATGGCTCTACAATGAGTATGTGACGGAACTTCCCGCCTTCAAGGACCGCGTGCCTGAG
TACCCTGCATGGTTTGAACCCTTCGTCATCCAGTGGCTGGATGAGAATGAGGAGGTGTCC
CGGGATTTCCTGCACGGTGCCCTGGAGCGAGACAAGAAGGATGGGTTCCAGCAGACCTCA
GAGCATGCCCTATTCTCCTGCTCCGTGGTGGATGTTTTCTCCCAACTCAACCAGAGCTTT
GAAATCATCAAGAAACTCGAGTGTCCCGACCCTCAGATCGTGGGGCACTACATGAGGCGC
TTTGCCAAGACCATCAGTAATGTGCTCCTCCAGTATGCAGACATCATCTCCAAGGACTTT
GCCTCCTACTGCTCCAAGGAGAAGGAGAAAGTGCCCTGCATTCTCATGAATAACACTCAA
CAGCTACGAGTTCAGCTGGAGAAGATGTTCGAAGCCATGGGAGGAAAGGAGCTGGATGCT
GAAGCCAGTGACATCCTGAAGGAGCTTCAGGTGAAACTCAATAACGTCTTGGATGAGCTC
AGCCGGGTGTTTGCTACCAGCTTCCAGCCGCACATTGAAGAGTGTGTCAAACAGATGGGT
GACATCCTTAGCCAGGTTAAGGGCACAGGCAATGTGCCAGCCAGTGCCTGCAGCAGCGTG
GCCCAGGACGCGGACAATGTGTTGCAGCCCATCATGGACCTGCTGGACAGCAACCTGACC
CTCTTTGCCAAAATCTGTGAGAAGACTGTGCTGAAGCGAGTGCTGAAGGAGCTGTGGAAG
CTGGTTATGAACACCATGGAGAAAACCATCGTCCTGCCGCCCCTCACTGACCAGACGATG
ATCGGGAACCTCTTGAGAAAACATGGCAAGGGATTAGAAAAGGGCAGGGTGAAATTGCCA
AGCCACTCAGACGGAACCCAGATGATCTTCAATGCAGCCAAGGAGCTGGGTCAGCTGTCC
AAACTCAAGGATCACATGGTACGAGAAGAAGCCAAGAGCTTGACCCCAAAGCAGTGCGCG
GTTGTTGAGTTGGCCCTGGACACCATCAAGCAATATTTCCACGCGGGTGGCGTGGGCCTC
AAGAAGACCTTCCTGGAGAAGAGCCCGGACCTGCAATCCTTGCGCTATGCCCTGTCGCTC
TACACGCAGGCCACCGACCTGCTAATCAAGACCTTTGTACAGACGCAATCGGCCCAGGGC
TTGGGTGTAGAAGACCCTGTGGGTGAAGTCTCTGTCCATGTTGAGCTGTTCACTCATCCA
GGAACTGGGGAACACAAGGTCACAGTGAAAGTGGTGGCTGCCAATGACCTCAAGTGGCAG
ACTTCTGGCATCTTCCGGCCGTTCATCGAGGTCAACATCATTGGGCCCCAGCTCAGCGAC
AAGAAACGCAAGTTTGCGACCAAATCCAAGAACAATAGCTGGGCTCCCAAGTACAATGAG
AGCTTCCAGTTCACGCTGAGCGCCGACGCGGGTCCCGAGTGCTATGAGCTGCAGGTGTGC
GTCAAGGACTACTGCTTCGCGCGCGAGGACCGCACGGTGGGGCTGGCCGTGCTGCAGCTG
CGTGAGCTGGCCCAGCGCGGGAGCGCCGCCTGCTGGCTGCCGCTCGGCCGCCGCATCCAC
ATGGACGACACGGGCCTCACGGTGCTGCGAATCCTCTCGCAGCGCAGCAACGACGAGGTG
GCCAAGGAGTTCGTGAAGCTCAAGTCGGACACGCGCTCCGCCGAGGAGGGCGGTGCCGCG
CCTGCGCCTTAG
Enzyme 89 GenBank Gene ID NM_001080421.2 Link Image
Enzyme 89 GeneCard ID UNC13A Link Image
Enzyme 89 GenAtlas ID UNC13A Link Image
Enzyme 89 HGNC ID HGNC:23150 Link Image
Enzyme 89 Chromosome Location 1
Enzyme 89 Locus 19p13.11
Enzyme 89 SNPs SNPJam Report Link Image
Enzyme 89 General References
  1. Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed Link Image]
  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. Sheu L, Pasyk EA, Ji J, Huang X, Gao X, Varoqueaux F, Brose N, Gaisano HY: Regulation of insulin exocytosis by Munc13-1. J Biol Chem. 2003 Jul 25;278(30):27556-63. Epub 2003 May 13. [PubMed Link Image]
Enzyme 89 Metabolite References Not Available
Enzyme 90 [top]
Enzyme 90 ID 13806
Enzyme 90 Name Protein unc-13 homolog B
Enzyme 90 Synonyms
  1. Munc13-2
  2. munc13
Enzyme 90 Gene Name UNC13B
Enzyme 90 Protein Sequence >Protein unc-13 homolog B
MSLLCVRVKRAKFQGSPDKFNTYVTLKVQNVKSTTVAVRGDQPSWEQDFMFEISRLDLGL
SVEVWNKGLIWDTMVGTVWIALKTIRQSDEEGPGEWSTLEAETLMKDDEICGTRNPTPHK
ILLDTRFELPFDIPEEEARYWTYKWEQINALGADNEYSSQEESQRKPLPTAAAQCSFEDP
DSAVDDRDSDYRSETSNSFPPPYHTASQPNASVHQFPVPVRSPQQLLLQGSSRDSCNDSM
QSYDLDYPERRAISPTSSSRYGSSCNVSQGSSQLSELDQYHEQDDDHRETDSIHSCHSSH
SLSRDGQAGFGEQEKPLEVTGQAEKEAACEPKEMKEDATTHPPPDLVLQKDHFLGPQESF
PEENASSPFTQARAHWIRAVTKVRLQLQEIPDDGDPSLPQWLPEGPAGGLYGIDSMPDLR
RKKPLPLVSDLSLVQSRKAGITSAMATRTSLKDEELKSHVYKKTLQALIYPISCTTPHNF
EVWTATTPTYCYECEGLLWGIARQGMRCSECGVKCHEKCQDLLNADCLQRAAEKSCKHGA
EDRTQNIIMAMKDRMKIRERNKPEIFEVIRDVFTVNKAAHVQQMKTVKQSVLDGTSKWSA
KITITVVCAQGLQAKDKTGSSDPYVTVQVSKTKKRTKTIFGNLNPVWEEKFHFECHNSSD
RIKVRVWDEDDDIKSRVKQRLKRESDDFLGQTIIEVRTLSGEMDVWYNLEKRTDKSAVSG
AIRLQISVEIKGEEKVAPYHVQYTCLHENLFHYLTDIQGSGGVRIPEARGDDAWKVYFDE
TAQEIVDEFAMRYGIESIYQAMTHFACLSSKYMCPGVPAVMSTLLANINAYYAHTTASTN
VSASDRFAASNFGKERFVKLLDQLHNSLRIDLSTYRNNFPAGSPERLQDLKSTVDLLTSI
TFFRMKVQELQSPPRASQVVKDCVKACLNSTYEYIFNNCHDLYSRQYQLKQELPPEEQGP
SIRNLDFWPKLITLIVSIIEEDKNSYTPVLNQFPQELNVGKVSAEVMWHLFAQDMKYALE
EHEKDHLCKSADYMNLHFKVKWLHNEYVRDLPVLQGQVPEYPAWFEQFVLQWLDENEDVS
LEFLRGALERDKKDGFQQTSEHALFSCSVVDVFTQLNQSFEIIRKLECPDPSILAHYMRR
FAKTIGKVLMQYADILSKDFPAYCTKEKLPCILMNNVQQLRVQLEKMFEAMGGKELDLEA
ADSLKELQVKLNTVLDELSMVFGNSFQVRIDECVRQMADILGQVRGTGNASPDARASAAQ
DADSVLRPLMDFLDGNLTLFATVCEKTVLKRVLKELWRVVMNTMERMIVLPPLTDQTGTQ
LIFTAAKELSHLSKLKDHMVREETRNLTPKQCAVLDLALDTIKQYFHAGGNGLKKTFLEK
SPDLQSLRYALSLYTQTTDTLIKTFVRSQTTQGSGVDDPVGEVSIQVDLFTHPGTGEHKV
TVKVVAANDLKWQTAGMFRPFVEVTMVGPHQSDKKRKFTTKSKSNNWAPKYNETFHFLLG
NEEGPESYELQICVKDYCFAREDRVLGLAVMPLRDVTAKGSCACWCPLGRKIHMDETGLT
ILRILSQRSNDEVAREFVKLKSESRSTEEGS
Enzyme 90 Number of Residues 1591
Enzyme 90 Molecular Weight 180677.2
Enzyme 90 Theoretical pI 5.84
Enzyme 90 GO Classification
Function
Process
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 90 General Function Involved in intracellular signaling pathway
Enzyme 90 Specific Function Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity- depending refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in a subset of excitatory/glutamatergic but not inhibitory/GABA-mediated synapses
Enzyme 90 Pathways Not Available
Enzyme 90 Reactions Not Available
Enzyme 90 Pfam Domain Function
Enzyme 90 Signals
  • None
Enzyme 90 Transmembrane Regions
  • None
Enzyme 90 Essentiality Not Available
Enzyme 90 GenBank ID Protein 2432000 Link Image
Enzyme 90 UniProtKB/Swiss-Prot ID O14795 Link Image
Enzyme 90 UniProtKB/Swiss-Prot Entry Name UN13B_HUMAN Link Image
Enzyme 90 PDB ID 1Y8F Link Image
Enzyme 90 PDB File Show
Enzyme 90 3D Structure
Enzyme 90 Cellular Location Not Available
Enzyme 90 Gene Sequence >4776 bp
ATGTCACTGCTCTGCGTGCGCGTTAAAAGGGCCAAATTCCAGGGTTCACCAGATAAATTT
AACACATATGTGACCCTGAAAGTACAGAATGTGAAGAGCACAACTGTAGCAGTTCGTGGT
GATCAGCCTTCCTGGGAACAGGATTTCATGTTTGAGATTAGTCGCCTGGACCTGGGTCTA
AGTGTGGAGGTATGGAACAAAGGACTGATCTGGGACACCATGGTGGGGACTGTGTGGATT
GCGCTGAAGACTATTCGTCAGTCGGATGAGGAAGGGCCTGGGGAATGGTCCACATTAGAG
GCAGAGACGTTAATGAAAGACGATGAGATCTGTGGAACTAGAAACCCAACTCCTCATAAA
ATTTTGCTTGATACAAGATTTGAGTTGCCTTTTGATATCCCAGAGGAGGAAGCCAGATAT
TGGACCTACAAATGGGAGCAAATCAATGCCTTGGGAGCTGACAATGAGTATTCTAGTCAA
GAAGAAAGCCAGAGGAAGCCATTGCCCACTGCTGCCGCCCAGTGTTCTTTTGAAGACCCT
GATAGTGCCGTCGATGACCGAGATAGTGACTATCGCAGTGAGACCAGCAACAGCTTCCCA
CCTCCTTACCATACAGCTTCCCAGCCCAACGCTTCTGTGCACCAGTTCCCTGTGCCGGTG
CGATCGCCACAGCAGCTGCTACTTCAAGGCAGTTCCCGGGACTCTTGTAATGACTCTATG
CAAAGTTATGACCTTGATTATCCAGAGCGGCGGGCTATCAGCCCCACCAGCAGCAGTAGG
TATGGCTCCTCCTGTAATGTGAGTCAAGGAAGCTCTCAGCTAAGTGAACTAGACCAGTAT
CACGAACAAGATGACGACCATCGGGAGACGGACTCGATTCATTCTTGCCACAGCTCTCAC
AGCCTGTCCAGAGATGGCCAAGCAGGTTTTGGAGAACAAGAGAAACCCTTGGAGGTGACA
GGTCAAGCAGAGAAGGAGGCAGCATGTGAACCCAAGGAGATGAAAGAAGATGCCACAACC
CACCCTCCCCCAGATCTGGTGCTGCAAAAAGACCACTTCCTAGGTCCCCAGGAGAGTTTT
CCTGAGGAGAATGCATCTTCACCATTTACCCAAGCCAGAGCACATTGGATCCGAGCAGTT
ACCAAGGTTCGACTCCAGCTGCAGGAGATTCCAGATGATGGTGACCCCTCTCTGCCTCAG
TGGCTCCCGGAAGGGCCAGCCGGAGGGCTCTATGGCATTGACAGCATGCCAGATTTACGC
AGAAAGAAGCCACTGCCACTTGTCAGTGATCTGTCACTGGTCCAGTCTCGGAAGGCAGGA
ATCACTTCTGCAATGGCTACACGCACTTCTCTTAAGGACGAAGAGCTGAAATCCCACGTG
TATAAGAAAACCCTGCAGGCCTTAATCTACCCCATTTCGTGCACCACTCCTCATAACTTT
GAGGTCTGGACGGCCACTACCCCAACCTACTGCTATGAGTGTGAAGGCCTGCTCTGGGGC
ATTGCCCGGCAGGGCATGCGCTGCAGCGAATGTGGAGTCAAGTGCCATGAGAAGTGCCAG
GATCTGCTCAATGCTGACTGCCTGCAGCGGGCTGCAGAAAAGAGCTGTAAACATGGAGCT
GAGGACCGGACCCAGAACATTATCATGGCCATGAAGGACCGCATGAAGATCCGAGAGCGA
AATAAGCCAGAGATCTTTGAAGTTATCCGGGACGTCTTCACAGTGAACAAAGCTGCCCAT
GTGCAGCAGATGAAAACAGTGAAGCAGAGTGTACTGGATGGCACCTCCAAGTGGTCAGCC
AAGATCACCATTACTGTGGTGTGTGCCCAGGGCCTACAAGCCAAGGACAAAACAGGATCC
AGTGACCCTTACGTGACTGTGCAAGTCAGCAAAACTAAGAAGCGTACCAAGACCATTTTT
GGAAACTTGAATCCTGTTTGGGAGGAGAAGTTCCATTTTGAGTGCCACAACTCCTCTGAC
CGCATTAAGGTGCGTGTATGGGATGAGGATGATGACATCAAGTCAAGAGTAAAGCAACGC
CTAAAGCGAGAGTCTGATGATTTCCTTGGCCAAACCATCATTGAGGTTCGGACCCTAAGT
GGCGAGATGGACGTCTGGTACAACTTGGAGAAGAGGACAGACAAATCAGCCGTCTCAGGG
GCTATCCGACTACAAATCAGTGTGGAGATCAAGGGGGAGGAGAAAGTAGCCCCATACCAC
GTGCAGTATACATGTCTCCATGAGAATCTTTTCCATTACCTCACAGACATTCAGGGCAGT
GGAGGAGTCCGCATCCCTGAAGCTCGAGGAGACGATGCCTGGAAGGTGTACTTTGATGAG
ACAGCCCAAGAAATTGTGGATGAATTTGCCATGCGTTATGGCATTGAGTCCATATATCAG
GCCATGACGCACTTTGCATGTTTATCATCCAAGTACATGTGTCCTGGTGTGCCAGCAGTG
ATGAGCACCTTACTGGCCAACATCAACGCCTACTATGCCCACACAACTGCCTCTACCAAT
GTCTCTGCATCTGATCGCTTTGCAGCCTCCAACTTTGGGAAAGAGAGATTTGTAAAACTG
CTGGACCAGCTACACAACTCACTGAGGATCGACCTCTCTACATACAGGAATAATTTCCCT
GCTGGGAGTCCTGAACGGCTTCAGGACTTAAAATCCACAGTGGATTTGCTGACCAGCATT
ACTTTCTTCAGAATGAAGGTACAAGAACTGCAAAGCCCTCCAAGAGCCAGCCAGGTGGTA
AAGGATTGTGTGAAGGCCTGTTTGAACTCCACATATGAATATATCTTCAACAACTGCCAC
GACTTATACAGCCGCCAGTACCAGCTGAAGCAGGAGCTACCTCCAGAGGAACAAGGGCCC
AGCATTCGGAACCTGGATTTCTGGCCCAAGCTCATCACACTCATCGTGTCAATCATAGAG
GAAGATAAGAATTCCTACACACCTGTTCTGAACCAGTTTCCTCAGGAGTTGAATGTGGGA
AAAGTCAGCGCAGAAGTGATGTGGCATTTGTTTGCCCAAGACATGAAATATGCATTGGAG
GAGCATGAGAAAGACCACCTGTGTAAAAGTGCTGACTACATGAACCTGCACTTCAAGGTG
AAGTGGCTCCACAATGAATACGTGCGGGATCTGCCTGTCCTCCAGGGGCAGGTGCCTGAG
TACCCAGCGTGGTTTGAGCAGTTCGTGCTACAATGGCTGGATGAGAATGAGGATGTATCC
CTGGAATTCCTGCGTGGGGCCCTGGAACGAGATAAGAAGGATGGATTCCAGCAGACATCA
GAGCATGCACTCTTTTCCTGCTCTGTGGTGGATGTCTTCACACAACTCAATCAGAGCTTT
GAGATCATCCGGAAGCTGGAATGCCCAGACCCCAGCATCCTTGCCCACTACATGAGGAGG
TTTGCTAAGACCATCGGGAAGGTGCTGATGCAGTATGCAGACATCTTGTCAAAGGACTTC
CCAGCCTATTGCACAAAGGAGAAACTGCCCTGCATCCTGATGAACAACGTGCAGCAACTG
AGGGTCCAGCTGGAGAAAATGTTTGAGGCCATGGGAGGCAAGGAGCTGGACCTTGAAGCT
GCAGACAGTCTGAAGGAGCCGCAGGTGAAACTGAATACGGTTCTGGATGAGCTCAGCATG
GTGTTTGGAAACAGTTTCCAGGTACGGATTGATGAGTGTGTTCGACAAATGGCCGACATC
CTGGGCCAGGTTCGGGGCACAGGGAATGCATCTCCAGACGCCAGGGCCTCAGCGGCTCAG
GATGCAGATAGCGTACTCCGGCCTCTCATGGACTTCCTGGATGGCAACCTCACCCTCTTT
GCCACTGTGTGTGAGAAGACGGTTCTGAAGCGTGTACTGAAGGAGCTCTGGCGCGTGGTG
ATGAACACAATGGAGAGGATGATTGTTCTGCCCCCACTCACTGACCAGACGGGCACCCAG
CTGATCTTCACTGCTGCCAAGGAGCTGAGCCATCTTTCCAAACTCAAGGATCACATGGTA
CGAGAGGAAACACGGAATCTCACTCCAAAGCAGTGTGCAGTCCTTGACCTCGCCCTGGAC
ACCATCAAGCAATACTTCCATGCAGGAGGCAATGGGCTGAAGAAAACCTTCCTGGAGAAG
AGCCCAGATCTGCAGTCTCTACGCTATGCCCTGTCTCTGTACACACAGACTACTGACACT
CTCATCAAGAGGTTTGTGCGCTCGCAGACCACCCAAGGGTCTGGTGTGGACGATCCTGTG
GGAGAAGTCTCTATTCAGGTGGACTTGTTTACACACCCTGGTACTGGGGAGCACAAGGTC
ACAGTGAAAGTGGTGGCTGCCAATGACCTCAAGTGGCAGACAGCGGGTATGTTCCGGCCT
TTCGTGGAGGTGACTATGGTTGGCCCACACCAAAGTGATAAGAAGAGGAAGTTCACAACC
AAATCCAAAAGCAACAACTGGGCCCCCAAGTACAATGAGACATTCCACTTACTCCTGGGA
AATGAGGAGGGGCCCGAGTCCTATGAGTTGCAGATATGCGTGAAGGATTACTGCTTTGCC
CGGGAAGATCGCGTGCTAGGGCTGGCTGTGATGCCTCTGAGGGATGTCACAGCCAAGGGC
AGCTGTGCCTGCTGGTGCCCCTTGGGCCGGAAGATCCATATGGATGAGACAGGCCTGACC
ATTCTCCGGATTTTATCTCAGAGGAGCAATGACGAGGTGGCCCGAGAATTTGTGAAACTC
AAATCAGAGTCTCGTTCCACGGAGGAGGGGAGCTGA
Enzyme 90 GenBank Gene ID AF020202 Link Image
Enzyme 90 GeneCard ID UNC13B Link Image
Enzyme 90 GenAtlas ID UNC13B Link Image
Enzyme 90 HGNC ID HGNC:12566 Link Image
Enzyme 90 Chromosome Location 9
Enzyme 90 Locus 9p13.3
Enzyme 90 SNPs SNPJam Report Link Image
Enzyme 90 General References
  1. Song Y, Ailenberg M, Silverman M: Cloning of a novel gene in the human kidney homologous to rat munc13s: its potential role in diabetic nephropathy. Kidney Int. 1998 Jun;53(6):1689-95. [PubMed Link Image]
  2. 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]
  3. Song Y, Ailenberg M, Silverman M: Human munc13 is a diacylglycerol receptor that induces apoptosis and may contribute to renal cell injury in hyperglycemia. Mol Biol Cell. 1999 May;10(5):1609-19. [PubMed Link Image]
  4. 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]
  5. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 90 Metabolite References Not Available
Enzyme 91 [top]
Enzyme 91 ID 13807
Enzyme 91 Name Protein unc-13 homolog C
Enzyme 91 Synonyms
  1. Munc13-3
Enzyme 91 Gene Name UNC13C
Enzyme 91 Protein Sequence >Protein unc-13 homolog C
MVANFFKSLILPYIHKLCKGMFTKKLGNTNKNKEYRQQKKDQDFPTAGQTKSPKFSYTFK
STVKKIAKCSSTHNLSTEEDEASKEFSLSPTFSYRVAIANGLQKNAKVTNSDNEDLLQEL
SSIESSYSESLNELRSSTENQAQSTHTMPVRRNRKSSSSLAPSEGSSDGERTLHGLKLGA
LRKLRKWKKSQECVSSDSELSTMKKSWGIRSKSLDRTVRNPKTNALEPGFSSSGCISQTH
DVMEMIFKELQGISQIETELSELRGHVNALKHSIDEISSSVEVVQSEIEQLRTGFVQSRR
ETRDIHDYIKHLGHMGSKASLRFLNVTEERFEYVESVVYQILIDKMGFSDAPNAIKIEFA
QRIGHQRDCPNAKPRPILVYFETPQQRDSVLKKSYKLKGTGIGISTDILTHDIRERKEKG
IPSSQTYESMAIKLSTPEPKIKKNNWQSPDDSDEDLESDLNRNSYAVLSKSELLTKGSTS
KPSSKSHSARSKNKTANSSRISNKSDYDKISSQLPESDILEKQTTTHYADATPLWHSQSD
FFTAKLSRSESDFSKLCQSYSEDFSENQFFTRTNGSSLLSSSDRELWQRKQEGTATLYDS
PKDQHLNGGVQGIQGQTETENTETVDSGMSNGMVCASGDRSHYSDSQLSLHEDLSPWKEW
NQGADLGLDSSTQEGFDYETNSLFDQQLDVYNKDLEYLGKCHSDLQDDSESYDLTQDDNS
SPCPGLDNEPQGQWVGQYDSYQGANSNELYQNQNQLSMMYRSQSELQSDDSEDAPPKSWH
SRLSIDLSDKTFSFPKFGSTLQRAKSALEVVWNKSTQSLSGYEDSGSSLMGRFRTLSQST
ANESSTTLDSDVYTEPYYYKAEDEEDYTEPVADNETDYVEVMEQVLAKLENRTSITETDE
QMQAYDHLSYETPYETPQDEGYDGPADDMVSEEGLEPLNETSAEMEIREDENQNIPEQPV
EITKPKRIRPSFKEAALRAYKKQMAELEEKILAGDSSSVDEKARIVSGNDLDASKFSALQ
VCGGAGGGLYGIDSMPDLRRKKTLPIVRDVAMTLAARKSGLSLAMVIRTSLNNEELKMHV
FKKTLQALIYPMSSTIPHNFEVWTATTPTYCYECEGLLWGIARQGMKCLECGVKCHEKCQ
DLLNADCLQRAAEKSSKHGAEDKTQTIITAMKERMKIREKNRPEVFEVIQEMFQISKEDF
VQFTKAAKQSVLDGTSKWSAKITITVVSAQGLQAKDKTGSSDPYVTVQVGKNKRRTKTIF
GNLNPVWDEKFYFECHNSTDRIKVRVWDEDDDIKSRVKQHFKKESDDFLGQTIVEVRTLS
GEMDVWYNLEKRTDKSAVSGAIRLKINVEIKGEEKVAPYHIQYTCLHENLFHYLTEVKSN
GGVKIPEVKGDEAWKVFFDDASQEIVDEFAMRYGIESIYQAMTHFSCLSSKYMCPGVPAV
MSTLLANINAFYAHTTVSTNIQVSASDRFAATNFGREKFIKLLDQLHNSLRIDLSKYREN
FPASNTERLQDLKSTVDLLTSITFFRMKVLELQSPPKASMVVKDCVRACLDSTYKYIFDN
CHELYSQLTDPSKKQDIPREDQGPTTKNLDFWPQLITLMVTIIDEDKTAYTPVLNQFPQE
LNMGKISAEIMWTLFALDMKYALEEHENQRLCKSTDYMNLHFKVKWFYNEYVRELPAFKD
AVPEYSLWFEPFVMQWLDENEDVSMEFLHGALGRDKKDGFQQTSEHALFSCSVVDVFAQL
NQSFEIIKKLECPNPEALSHLMRRFAKTINKVLLQYAAIVSSDFSSHCDKENVPCILMNN
IQQLRVQLEKMFESMGGKELDSEASTILKELQVKLSGVLDELSVTYGESFQVIIEECIKQ
MSFELNQMRANGNTTSNKNSAAMDAEIVLRSLMDFLDKTLSLSAKICEKTVLKRVLKELW
KLVLNKIEKQIVLPPLTDQTGPQMIFIAAKDLGQLSKLKEHMIREDARGLTPRQCAIMEV
VLATIKQYFHAGGNGLKKNFLEKSPDLQSLRYALSLYTQTTDALIKKFIDTQTSQSRSSK
DAVGQISVHVDITATPGTGDHKVTVKVIAINDLNWQTTAMFRPFVEVCILGPNLGDKKRK
QGTKTKSNTWSPKYNETFQFILGKENRPGAYELHLSVKDYCFAREDRIIGMTVIQLQNIA
EKGSYGAWYPLLKNISMDETGLTILRILSQRTSDDVAKEFVRLKSETRSTEESA
Enzyme 91 Number of Residues 2214
Enzyme 91 Molecular Weight 250909.3
Enzyme 91 Theoretical pI 5.71
Enzyme 91 GO Classification
Function
Process
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 91 General Function Involved in intracellular signaling pathway
Enzyme 91 Specific Function Probably plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Probably is involved in neurotransmitter release
Enzyme 91 Pathways Not Available
Enzyme 91 Reactions Not Available
Enzyme 91 Pfam Domain Function
Enzyme 91 Signals
  • None
Enzyme 91 Transmembrane Regions
  • None
Enzyme 91 Essentiality Not Available
Enzyme 91 GenBank ID Protein 122937514 Link Image
Enzyme 91 UniProtKB/Swiss-Prot ID Q8NB66 Link Image
Enzyme 91 UniProtKB/Swiss-Prot Entry Name UN13C_HUMAN Link Image
Enzyme 91 PDB ID 1Y8F Link Image
Enzyme 91 PDB File Show
Enzyme 91 3D Structure
Enzyme 91 Cellular Location Not Available
Enzyme 91 Gene Sequence >6645 bp
ATGGTGGCTAATTTTTTCAAGAGCTTGATTTTACCTTACATTCATAAGCTTTGCAAAGGA
ATGTTTACAAAGAAATTGGGAAATACAAACAAAAACAAAGAGTATCGTCAGCAGAAAAAG
GATCAAGACTTCCCCACTGCTGGCCAGACCAAATCCCCCAAATTTTCTTACACTTTTAAA
AGCACTGTAAAGAAGATTGCAAAGTGTTCATCCACTCACAACTTATCCACTGAGGAAGAC
GAGGCCAGTAAAGAGTTTTCCCTCTCACCAACATTCAGTTACCGAGTAGCTATTGCCAAT
GGCCTACAAAAGAATGCTAAAGTAACCAACAGTGATAATGAGGATCTGCTTCAAGAGCTC
TCTTCAATCGAGAGTTCCTACTCAGAATCATTAAATGAACTAAGGAGTAGCACAGAAAAC
CAGGCACAATCAACACACACAATGCCAGTTAGACGCAACAGAAAGAGTTCAAGCAGCCTT
GCACCCTCTGAGGGCAGCTCTGACGGGGAGCGTACTCTACATGGCTTAAAACTGGGAGCT
TTACGAAAACTGAGAAAATGGAAAAAGAGTCAAGAATGTGTCTCCTCAGACTCAGAGTTA
AGCACCATGAAAAAATCCTGGGGAATAAGAAGTAAGTCTTTGGACAGAACTGTCCGAAAC
CCAAAGACAAATGCCCTGGAGCCAGGGTTCAGTTCCTCTGGCTGCATTAGCCAAACACAT
GATGTCATGGAAATGATCTTTAAGGAACTTCAGGGAATAAGTCAGATTGAAACAGAACTT
TCTGAACTACGAGGGCACGTCAATGCTCTCAAGCACTCCATCGATGAGATCTCCAGCAGT
GTGGAGGTTGTACAAAGTGAAATTGAGCAGTTGCGCACAGGGTTTGTCCAGTCTCGGAGG
GAAACTAGAGACATCCATGATTATATTAAGCACTTAGGTCATATGGGTAGCAAGGCAAGC
CTGAGATTTTTAAATGTGACTGAAGAAAGATTTGAATATGTTGAAAGCGTGGTGTACCAA
ATTCTAATAGATAAAATGGGTTTTTCAGATGCACCAAATGCTATTAAAATTGAATTTGCT
CAGAGGATAGGACACCAGAGAGACTGCCCAAATGCAAAGCCTCGACCCATACTTGTGTAC
TTTGAAACCCCTCAACAAAGGGATTCTGTCTTAAAAAAGTCATATAAACTCAAAGGAACA
GGCATTGGAATCTCAACAGATATTCTAACTCATGACATCAGAGAAAGAAAAGAGAAAGGG
ATACCATCCTCCCAGACATATGAGAGCATGGCTATAAAGTTGTCTACTCCAGAGCCAAAA
ATCAAGAAGAACAATTGGCAGTCACCTGATGACAGTGATGAAGATCTTGAATCTGACCTC
AATAGAAACAGTTACGCTGTGCTTTCCAAGTCAGAGCTTCTAACAAAGGGAAGTACTTCC
AAGCCAAGCTCAAAATCACACAGTGCTAGATCCAAGAATAAAACTGCTAATAGCAGCAGA
ATTTCAAATAAATCAGATTATGATAAAATCTCCTCACAGTTGCCAGAATCAGATATCTTG
GAAAAGCAAACCACAACCCATTATGCAGATGCAACACCTCTCTGGCACTCACAGAGTGAT
TTTTTCACTGCTAAACTTAGTCGTTCTGAATCAGATTTTTCCAAATTGTGTCAGTCTTAC
TCAGAAGATTTTTCAGAAAATCAGTTTTTCACTAGAACTAATGGAAGCTCTCTCCTGTCA
TCTTCGGACCGGGAGCTATGGCAGAGGAAACAGGAAGGAACAGCGACCCTGTATGACAGT
CCCAAGGACCAGCATTTGAATGGAGGTGTTCAGGGTATCCAAGGGCAGACTGAAACTGAA
AACACAGAAACTGTGGATAGTGGAATGAGTAATGGCATGGTGTGTGCATCTGGAGACCGG
AGTCATTACAGTGATTCTCAGCTCTCTTTACATGAGGATCTTTCTCCATGGAAGGAATGG
AATCAAGGAGCTGATTTAGGCTTGGATTCATCCACCCAGGAAGGTTTTGATTATGAAACA
AACAGTCTTTTTGACCAACAGCTTGATGTTTACAATAAAGACCTAGAATACTTGGGAAAG
TGCCACAGTGATCTTCAAGATGACTCAGAGAGCTACGACTTAACTCAAGATGACAATTCT
TCTCCATGCCCTGGCTTGGATAATGAACCACAAGGCCAGTGGGTTGGCCAATATGATTCT
TATCAGGGAGCTAATTCTAATGAGCTATACCAAAATCAAAACCAGTTGTCCATGATGTAT
CGAAGTCAAAGTGAATTGCAAAGTGATGATTCAGAGGATGCCCCACCCAAATCATGGCAT
AGTCGATTAAGCATTGACCTTTCTGATAAGACTTTCAGCTTCCCAAAATTTGGATCTACA
CTGCAGAGGGCTAAATCAGCCTTGGAAGTAGTATGGAACAAAAGCACACAGAGTCTGAGT
GGGTATGAGGACAGTGGCTCTTCATTAATGGGGAGATTTCGGACATTATCTCAATCAACT
GCAAATGAGTCAAGTACCACACTTGACTCTGATGTCTACACGGAGCCCTATTACTATAAA
GCAGAGGATGAGGAAGATTATACTGAACCAGTGGCTGACAATGAAACAGATTATGTTGAA
GTCATGGAACAAGTCCTTGCTAAACTAGAAAACAGGACTAGTATTACTGAAACAGATGAA
CAAATGCAAGCATATGATCACCTTTCATATGAAACACCTTATGAAACCCCACAAGATGAG
GGTTATGATGGTCCAGCAGATGATATGGTTAGTGAAGAGGGGTTAGAACCCTTAAATGAA
ACATCAGCTGAGATGGAAATAAGAGAAGATGAAAACCAAAACATTCCTGAACAGCCAGTG
GAGATCACAAAGCCAAAGAGAATTCGTCCTTCTTTCAAAGAAGCAGCTTTAAGGGCCTAT
AAAAAGCAAATGGCAGAGTTGGAAGAGAAGATCTTGGCTGGAGATAGCAGTTCTGTGGAT
GAAAAGGCTCGAATAGTAAGTGGCAATGATTTGGATGCTTCCAAATTTTCTGCACTCCAG
GTGTGTGGTGGGGCTGGAGGTGGACTTTATGGTATTGACAGCATGCCGGATCTTCGCAGA
AAAAAAACTTTGCCTATTGTCCGAGATGTGGCCATGACCCTGGCTGCCCGGAAATCTGGA
CTCTCCCTGGCTATGGTGATTAGGACATCCCTAAATAATGAGGAACTGAAAATGCACGTC
TTCAAGAAGACCTTGCAGGCACTGATCTACCCTATGTCTTCTACCATCCCACACAATTTT
GAGGTCTGGACGGCTACCACACCCACCTACTGTTATGAGTGTGAAGGGCTCCTGTGGGGC
ATTGCAAGGCAAGGCATGAAGTGTCTGGAGTGTGGAGTGAAATGCCACGAAAAGTGTCAG
GACCTGCTAAACGCTGACTGCTTGCAGAGAGCAGCAGAAAAGAGTTCTAAACATGGTGCC
GAAGACAAGACTCAGACCATTATTACAGCAATGAAAGAAAGAATGAAGATCAGGGAGAAA
AACCGGCCAGAAGTATTTGAAGTAATCCAGGAAATGTTTCAGATTTCTAAAGAAGATTTT
GTGCAGTTTACAAAGGCGGCCAAACAGAGTGTACTGGATGGGACATCTAAGTGGTCTGCA
AAAATAACCATTACAGTGGTTTCTGCACAGGGTCTACAGGCAAAAGATAAAACAGGGTCT
AGTGATCCATATGTTACAGTTCAAGTTGGAAAGAACAAAAGAAGAACAAAAACCATTTTT
GGAAATTTGAATCCAGTATGGGATGAGAAGTTTTATTTTGAGTGTCATAACTCCACAGAT
CGAATCAAAGTCAGAGTATGGGATGAAGATGATGATATTAAATCCAGAGTCAAGCAACAT
TTCAAAAAGGAGTCAGATGATTTTCTGGGACAAACAATTGTAGAAGTGAGGACCTTGAGT
GGAGAAATGGATGTCTGGTACAACTTAGAGAAAAGGACAGATAAGTCAGCTGTATCTGGG
GCCATACGATTGAAAATCAATGTGGAGATAAAAGGAGAAGAGAAGGTTGCTCCATATCAT
ATTCAATATACATGTTTACATGAGAATCTGTTCCATTACTTGACTGAAGTGAAATCTAAT
GGTGGAGTGAAAATCCCAGAAGTCAAAGGGGATGAAGCCTGGAAGGTTTTCTTTGATGAT
GCTTCCCAAGAAATAGTTGATGAATTTGCTATGCGTTATGGAATTGAATCCATTTATCAA
GCTATGACGCACTTTTCATGTCTGTCTTCTAAATACATGTGCCCCGGTGTCCCTGCCGTC
ATGAGCACCTTGCTGGCTAATATAAATGCTTTTTATGCTCACACAACAGTTTCAACAAAC
ATACAGGTTTCTGCCTCAGATCGATTTGCTGCTACCAACTTTGGTAGGGAAAAATTCATA
AAACTACTGGACCAGTTACATAACTCTTTGAGGATTGATCTGTCAAAGTATAGGGAAAAC
TTTCCTGCAAGCAATACTGAAAGACTGCAAGACCTGAAATCAACTGTTGACCTGTTAACA
AGTATCACCTTTTTTAGGATGAAGGTTCTGGAGCTGCAAAGCCCCCCAAAAGCGAGCATG
GTGGTGAAGGACTGTGTAAGGGCTTGCCTGGATTCTACATACAAGTATATTTTTGACAAC
TGCCATGAACTCTACTCCCAGCTAACAGACCCGAGTAAGAAACAGGATATTCCTCGTGAA
GATCAGGGACCAACCACCAAGAATTTGGATTTTTGGCCCCAACTTATTACACTGATGGTT
ACTATTATTGATGAGGATAAAACTGCCTACACACCTGTCCTGAATCAGTTTCCTCAAGAG
CTGAACATGGGAAAAATAAGTGCCGAAATTATGTGGACTCTTTTTGCTCTGGATATGAAA
TATGCATTAGAAGAACATGAAAATCAGCGGTTATGCAAGAGCACCGATTATATGAATTTG
CATTTCAAAGTTAAATGGTTTTATAATGAATATGTGCGTGAACTTCCTGCCTTCAAGGAT
GCTGTTCCTGAATACTCCTTGTGGTTTGAACCTTTTGTCATGCAATGGCTAGATGAAAAC
GAAGATGTGTCAATGGAATTCCTTCATGGAGCACTGGGAAGAGACAAAAAAGATGGATTC
CAGCAGACATCTGAGCATGCTCTCTTTTCTTGCTCCGTGGTTGATGTCTTTGCTCAGCTG
AATCAGAGCTTTGAAATTATTAAGAAACTGGAATGCCCTAATCCTGAAGCATTATCTCAC
TTAATGAGAAGATTTGCAAAGACTATCAATAAAGTGCTGCTCCAGTATGCTGCAATTGTA
TCAAGTGATTTCAGTTCACATTGTGATAAGGAAAATGTGCCCTGTATCTTGATGAACAAT
ATTCAACAATTGCGGGTCCAGCTGGAAAAAATGTTTGAATCCATGGGAGGGAAGGAGCTA
GATTCTGAAGCTAGTACTATTCTAAAAGAACTTCAGGTTAAGCTCAGTGGGGTCCTGGAT
GAGCTCAGCGTCACTTATGGTGAAAGTTTCCAGGTTATAATTGAAGAGTGTATAAAACAG
ATGAGTTTCGAACTAAATCAAATGAGAGCAAATGGAAACACCACATCTAATAAGAACAGT
GCAGCAATGGATGCAGAGATTGTGTTAAGATCTCTTATGGATTTTTTGGACAAAACATTA
AGTCTCTCAGCAAAAATCTGTGAGAAAACAGTCCTAAAGCGAGTTTTAAAAGAGTTATGG
AAGCTAGTTCTCAACAAAATAGAAAAACAAATTGTTCTTCCTCCTCTGACAGATCAAACA
GGACCCCAGATGATTTTCATTGCAGCTAAAGATCTTGGACAATTATCCAAACTGAAGGAG
CACATGATTCGAGAGGATGCCAGGGGTCTGACGCCAAGACAATGCGCTATAATGGAGGTA
GTCCTGGCTACCATCAAGCAATACTTTCATGCAGGAGGAAATGGCCTGAAAAAGAATTTC
TTGGAGAAAAGCCCAGATCTTCAGTCTCTGAGATATGCTCTCAGTCTTTATACCCAAACT
ACTGATGCCTTGATAAAGAAATTCATAGATACTCAAACCTCACAGAGTCGTTCCTCCAAA
GATGCCGTGGGTCAGATATCTGTTCATGTGGACATCACTGCCACCCCAGGAACGGGAGAT
CATAAAGTCACTGTAAAAGTGATTGCTATTAATGACCTAAACTGGCAGACCACAGCAATG
TTCCGCCCCTTTGTGGAAGTTTGTATACTGGGACCCAACCTTGGAGACAAGAAGAGAAAA
CAAGGCACAAAAACAAAAAGCAACACATGGTCACCAAAGTACAATGAAACATTTCAGTTC
ATTCTCGGAAAGGAAAATCGACCAGGGGCTTATGAACTTCATCTCTCAGTTAAGGATTAC
TGCTTTGCCAGAGAAGATCGAATTATCGGAATGACAGTCATTCAGCTACAGAACATAGCA
GAAAAGGGAAGCTATGGGGCATGGTATCCTCTTCTGAAAAATATCTCTATGGATGAAACT
GGTTTGACTATCCTTAGAATACTCTCTCAGAGGACCAGTGATGATGTGGCTAAAGAATTT
GTAAGACTTAAATCTGAAACAAGATCTACTGAAGAGAGTGCTTGA
Enzyme 91 GenBank Gene ID NM_001080534.1 Link Image
Enzyme 91 GeneCard ID UNC13C Link Image
Enzyme 91 GenAtlas ID UNC13C Link Image
Enzyme 91 HGNC ID HGNC:23149 Link Image
Enzyme 91 Chromosome Location 1
Enzyme 91 Locus 15q21.3
Enzyme 91 SNPs SNPJam Report Link Image
Enzyme 91 General References
  1. 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]
  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. 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 91 Metabolite References Not Available
Enzyme 92 [top]
Enzyme 92 ID 14022
Enzyme 92 Name Rho guanine nucleotide exchange factor 2
Enzyme 92 Synonyms
  1. Guanine nucleotide exchange factor H1
  2. GEF-H1
  3. Microtubule-regulated Rho-GEF
  4. Proliferating cell nucleolar antigen p40
Enzyme 92 Gene Name ARHGEF2
Enzyme 92 Protein Sequence >Rho guanine nucleotide exchange factor 2
MSRIESLTRARIDRSRELASKTREKEKMKEAKDARYTNGHLFTTISVSGMTMCYACNKSI
TAKEALICPTCNVTIHNRCKDTLANCTKVKQKQQKAALLKNNTALQSVSLRSKTTIRERP
SSAIYPSDSFRQSLLGSRRGRSSLSLAKSVSTTNIAGHFNDESPLGLRRILSQSTDSLNM
RNRTLSVESLIDEAEVIYSELMSDFEMDEKDFAADSWSLAVDSSFLQQHKKEVMKQQDVI
YELIQTELHHVRTLKIMTRLFRTGMLEELHLEPGVVQGLFPCVDELSDIHTRFLSQLLER
RRQALCPGSTRNFVIHRLGDLLISQFSGPSAEQMCKTYSEFCSRHSKALKLYKELYARDK
RFQQFIRKVTRPAVLKRHGVQECILLVTQRITKYPLLISRILQHSHGIEEERQDLTTALG
LVKELLSNVDEGIYQLEKGARLQEIYNRMDPRAQTPVPGKGPFGREELLRRKLIHDGCLL
WKTATGRFKDVLVLLMTDVLVFLQEKDQKYIFPTLDKPSVVSLQNLIVRDIANQEKGMFL
ISAAPPEMYEVHTASRDDRSTWIRVIQQSVRTCPSREDFPLIETEDEAYLRRIKMELQQK
DRALVELLREKVGLFAEMTHFQAEEDGGSGMALPTLPRGLFRSESLESPRGERLLQDAIR
EVEGLKDLLVGPGVELLLTPREPALPLEPDSGGNTSPGVTANGEARTFNGSIELCRADSD
SSQRDRNGNQLRSPQEEALQRLVNLYGLLHGLQAAVAQQDTLMEARFPEGPERREKLCRA
NSRDGEAGRAGAAPVAPEKQATELALLQRQHALLQEELRRCRRLGEERATEAGSLEARLR
ESEQARALLEREAEEARRQLAALGQTEPLPAEAPWARRPVDPRRRSLPAGDALYLSFNPP
QPSRGTDRLDLPVTTRSVHRNFEDRERQELGSPEERLQDSSDPDTGSEEEGSSRLSPPHS
PRDFTRMQDIPEETESRDGEAVASES
Enzyme 92 Number of Residues 986
Enzyme 92 Molecular Weight 111541.3
Enzyme 92 Theoretical pI 7.27
Enzyme 92 GO Classification
Function
  • GTPase regulator activity
  • Ras guanyl-nucleotide exchange factor activity
  • Rho guanyl-nucleotide exchange factor activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • 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 92 General Function Involved in Rho guanyl-nucleotide exchange factor activity
Enzyme 92 Specific Function Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases, which was uniquely reported in PubMed:9857026. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras- GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIP2 dependent NF-kappaB signaling pathways activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides through NOD1 that is independent of its GEF activity, but also in the activation of NF-kappaB by Shigella effector proteins (IpgB2 and OspB) which requires its GEF activity and the activation of RhoA
Enzyme 92 Pathways Not Available
Enzyme 92 Reactions Not Available
Enzyme 92 Pfam Domain Function
Enzyme 92 Signals
  • None
Enzyme 92 Transmembrane Regions
  • None
Enzyme 92 Essentiality Not Available
Enzyme 92 GenBank ID Protein 253735775 Link Image
Enzyme 92 UniProtKB/Swiss-Prot ID Q92974 Link Image
Enzyme 92 UniProtKB/Swiss-Prot Entry Name ARHG2_HUMAN Link Image
Enzyme 92 PDB ID Not Available
Enzyme 92 Cellular Location Not Available
Enzyme 92 Gene Sequence >2961 bp
ATGTCTCGGATCGAATCCCTCACGCGGGCGCGGATCGACCGGAGCAGAGAGCTGGCGAGC
AAGACCCGGGAAAAGGAGAAGATGAAGGAAGCCAAGGATGCCCGCTATACCAATGGGCAC
CTCTTCACCACCATTTCAGTTTCAGGCATGACCATGTGCTATGCCTGTAACAAGAGCATC
ACAGCCAAGGAAGCCCTCATCTGCCCAACCTGCAATGTGACTATCCACAACCGCTGTAAA
GACACCCTCGCCAACTGTACCAAGGTCAAGCAGAAGCAACAGAAAGCGGCCCTGCTGAAG
AACAACACCGCCTTGCAGTCCGTTTCTCTTCGAAGTAAGACAACCATCCGGGAGCGGCCA
AGCTCGGCCATCTACCCCTCCGACAGCTTCCGGCAGTCCCTCCTGGGCTCCCGCCGTGGC
CGCTCCTCCTTGTCTTTAGCCAAGAGTGTTTCTACCACCAACATTGCTGGACATTTCAAT
GATGAGTCTCCCCTGGGGCTGCGCCGGATCCTCTCACAGTCCACAGACTCCCTCAACATG
CGGAACCGAACCCTATCCGTGGAATCCCTCATTGACGAAGCAGAGGTAATCTACAGTGAG
CTGATGAGTGACTTTGAGATGGATGAGAAGGACTTTGCAGCTGACTCTTGGAGTCTTGCT
GTGGACAGCAGCTTCCTGCAGCAGCATAAAAAGGAGGTGATGAAGCAGCAAGATGTCATC
TATGAGCTAATCCAGACAGAGCTGCACCATGTGAGGACACTGAAGATCATGACCCGCCTC
TTCCGCACGGGGATGCTGGAAGAGCTACACTTGGAGCCAGGAGTGGTCCAGGGCCTGTTC
CCCTGCGTGGACGAGCTCAGTGACATCCATACACGCTTCCTCAGCCAGCTATTAGAACGC
CGACGCCAGGCCCTGTGCCCTGGCAGCACCCGGAACTTTGTCATCCATCGCTTGGGTGAT
CTGCTCATCAGCCAGTTCTCAGGTCCTAGTGCGGAGCAGATGTGTAAGACCTACTCGGAG
TTCTGCAGCCGCCACAGCAAGGCCTTAAAGCTCTATAAGGAGCTGTACGCCCGAGACAAA
CGCTTCCAGCAATTCATCCGGAAAGTGACCCGCCCCGCCGTGCTCAAGCGGCACGGGGTA
CAGGAGTGCATCCTGCTGGTGACTCAGCGCATCACCAAGTACCCGTTACTCATCAGCCGC
ATCCTGCAGCATTCCCACGGGATCGAGGAGGAGCGCCAGGACCTGACCACAGCACTGGGG
CTAGTGAAGGAGCTGCTGTCCAATGTGGACGAGGGTATTTATCAGCTGGAGAAAGGGGCC
CGTCTGCAGGAGATCTACAACCGCATGGACCCTCGGGCCCAAACCCCAGTGCCTGGCAAG
GGCCCCTTTGGCCGAGAGGAACTTCTGAGGCGCAAACTCATCCACGATGGCTGCCTGCTC
TGGAAGACAGCGACGGGGCGCTTCAAAGATGTGCTAGTGCTGCTGATGACAGATGTACTG
GTGTTTCTCCAGGAAAAGGACCAGAAGTACATCTTTCCTACCCTGGACAAGCCTTCAGTG
GTATCGCTGCAGAATCTAATCGTACGAGACATTGCCAACCAGGAGAAAGGGATGTTTCTG
ATCAGCGCAGCCCCACCTGAGATGTACGAGGTGCACACAGCATCCCGGGATGACCGGAGC
ACCTGGATCCGGGTCATTCAGCAGAGCGTGCGCACATGCCCATCCAGGGAGGACTTCCCC
CTGATTGAGACAGAGGATGAGGCTTACCTGCGGCGAATTAAGATGGAGTTGCAGCAGAAG
GACCGGGCACTGGTGGAGCTGCTGCGAGAGAAGGTCGGGCTGTTTGCTGAGATGACCCAT
TTCCAGGCCGAAGAGGATGGTGGCAGTGGGATGGCCCTGCCCACCCTGCCCAGGGGCCTT
TTCCGCTCTGAGTCCCTTGAGTCCCCTCGTGGCGAGCGGCTGCTGCAGGATGCCATCCGT
GAGGTGGAGGGTCTGAAAGACCTGCTGGTGGGGCCAGGAGTGGAACTGCTCTTGACACCC
CGAGAGCCAGCCCTGCCCTTGGAACCAGACAGCGGTGGTAACACGAGTCCTGGGGTCACT
GCCAATGGTGAGGCCAGAACCTTCAATGGCTCCATTGAACTCTGCAGAGCTGACTCAGAC
TCTAGCCAGAGGGATCGAAATGGAAATCAGCTGAGATCACCGCAAGAGGAGGCGTTACAG
CGATTGGTCAATCTCTATGGACTTCTACATGGCCTACAGGCAGCTGTGGCCCAGCAGGAC
ACTCTGATGGAAGCCCGGTTCCCTGAGGGCCCTGAGCGGCGGGAGAAGCTGTGCCGAGCC
AACTCTCGGGATGGGGAGGCTGGCAGGGCTGGGGCTGCCCCTGTGGCCCCTGAAAAGCAG
GCCACGGAACTGGCATTACTGCAGCGGCAACATGCGCTGCTGCAGGAGGAGCTACGGCGC
TGCCGGCGGCTAGGTGAAGAACGGGCAACCGAAGCTGGCAGCCTGGAGGCCCGGCTCCGG
GAGAGTGAGCAGGCCCGGGCACTGCTGGAGCGTGAGGCCGAAGAGGCTCGAAGGCAGCTG
GCCGCCCTGGGCCAGACCGAGCCACTCCCAGCTGAGGCCCCCTGGGCCCGCAGACCTGTG
GATCCTCGGCGGCGCAGCCTCCCCGCAGGCGATGCCCTGTACTTGAGTTTCAACCCCCCA
CAGCCCAGCCGAGGCACTGACCGCCTGGATCTACCTGTCACTACTCGCTCTGTCCATCGA
AACTTTGAGGACCGAGAGAGGCAGGAACTGGGGAGCCCCGAAGAGCGGCTGCAAGACAGC
AGTGACCCTGACACTGGCAGCGAGGAGGAAGGTAGCAGCCGTCTGTCTCCGCCCCACAGT
CCACGAGACTTTACCAGAATGCAGGACATCCCGGAGGAGACGGAGAGCCGCGACGGGGAG
GCTGTAGCCTCCGAGAGCTAA
Enzyme 92 GenBank Gene ID NM_001162383.1 Link Image
Enzyme 92 GeneCard ID ARHGEF2 Link Image
Enzyme 92 GenAtlas ID ARHGEF2 Link Image
Enzyme 92 HGNC ID HGNC:682 Link Image
Enzyme 92 Chromosome Location 1
Enzyme 92 Locus 1q21-q22
Enzyme 92 SNPs SNPJam Report Link Image
Enzyme 92 General References
  1. Ren Y, Li R, Zheng Y, Busch H: Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases. J Biol Chem. 1998 Dec 25;273(52):34954-60. [PubMed Link Image]
  2. Krendel M, Zenke FT, Bokoch GM: Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton. Nat Cell Biol. 2002 Apr;4(4):294-301. [PubMed Link Image]
  3. 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]
  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. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Reddy AB, Chatterjee A, Rothblum LI, Black A, Busch H: Isolation and characterization of complementary DNA to proliferating cell nucleolar antigen P40. Cancer Res. 1989 Apr 1;49(7):1763-7. [PubMed Link Image]
  8. Zenke FT, Krendel M, DerMardirossian C, King CC, Bohl BP, Bokoch GM: p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to GEF-H1, a microtubule-localized Rho exchange factor. J Biol Chem. 2004 Apr 30;279(18):18392-400. Epub 2004 Feb 17. [PubMed Link Image]
  9. Callow MG, Zozulya S, Gishizky ML, Jallal B, Smeal T: PAK4 mediates morphological changes through the regulation of GEF-H1. J Cell Sci. 2005 May 1;118(Pt 9):1861-72. Epub 2005 Apr 12. [PubMed Link Image]
  10. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  11. Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R: Phosphoproteome analysis of the human mitotic spindle. Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5391-6. Epub 2006 Mar 24. [PubMed Link Image]
  12. Birkenfeld J, Nalbant P, Bohl BP, Pertz O, Hahn KM, Bokoch GM: GEF-H1 modulates localized RhoA activation during cytokinesis under the control of mitotic kinases. Dev Cell. 2007 May;12(5):699-712. [PubMed Link Image]
  13. 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]
  14. 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]
  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. Fujishiro SH, Tanimura S, Mure S, Kashimoto Y, Watanabe K, Kohno M: ERK1/2 phosphorylate GEF-H1 to enhance its guanine nucleotide exchange activity toward RhoA. Biochem Biophys Res Commun. 2008 Mar 28;368(1):162-7. Epub 2008 Jan 22. [PubMed Link Image]
  17. Fukazawa A, Alonso C, Kurachi K, Gupta S, Lesser CF, McCormick BA, Reinecker HC: GEF-H1 mediated control of NOD1 dependent NF-kappaB activation by Shigella effectors. PLoS Pathog. 2008 Nov;4(11):e1000228. Epub 2008 Nov 28. [PubMed Link Image]
  18. 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]
  19. Birkenfeld J, Nalbant P, Yoon SH, Bokoch GM: Cellular functions of GEF-H1, a microtubule-regulated Rho-GEF: is altered GEF-H1 activity a crucial determinant of disease pathogenesis? Trends Cell Biol. 2008 May;18(5):210-9. Epub 2008 Apr 3. [PubMed Link Image]
  20. 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]
  21. 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]
  22. 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]
  23. 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 92 Metabolite References Not Available
Enzyme 93 [top]
Enzyme 93 ID 14149
Enzyme 93 Name RAS guanyl-releasing protein 4
Enzyme 93 Synonyms Not Available
Enzyme 93 Gene Name RASGRP4
Enzyme 93 Protein Sequence >RAS guanyl-releasing protein 4
MNRKDSKRKSHQECTGKIGGRGRPRQVRRHKTCPSPREISKVMASMNLGLLSEGGCSEDE
LLEKCIQSFDSAGSLCHEDHMLNMVLAMHSWVLPSADLAARLLTSYQKATGDTQELRRLQ
ICHLVRYWLMRHPEVMHQDPQLEEVIGRFWATVAREGNSAQRRLGDSSDLLSPGGPGPPL
PMSSPGLGKKRKVSLLFDHLETGELAQHLTYLEFRSFQAITPQDLRSYVLQGSVRGCPAL
EGSVGLSNSVSRWVQVMVLSRPGPLQRAQVLDKFIHVAQRLHQLQNFNTLMAVTGGLCHS
AISRLKDSHAHLSPDSTKALLELTELLASHNNYARYRRTWAGCAGFRLPVLGVHLKDLVS
LHEAQPDRLPDGRLHLPKLNNLYLRLQELVALQGQHPPCSANEDLLHLLTLSLDLFYTED
EIYELSYAREPRCPKSLPPSPFNAPLVVEWAPGVTPKPDRVTLGRHVEQLVESVFKNYDP
EGRGTISQEDFERLSGNFPFACHGLHPPPRQGRGSFSREELTGYLLRASAICSKLGLAFL
HTFHEVTFRKPTFCDSCSGFLWGVTKQGYRCRECGLCCHKHCRDQVKVECKKRPGAKGDA
GPPGAPVPSTPAPHASCGSEENHSYTLSLEPETGCQLRHAWTQTESPHPSWETDTVPCPV
MDPPSTASSKLDS
Enzyme 93 Number of Residues 673
Enzyme 93 Molecular Weight 74881.7
Enzyme 93 Theoretical pI 8.06
Enzyme 93 GO Classification
Function
  • GTPase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • intracellular signaling pathway
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • signaling
  • signaling pathway
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 93 General Function Involved in intracellular signaling pathway
Enzyme 93 Specific Function Functions as a cation- and diacylglycerol (DAG)- regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. May function in mast cells differentiation
Enzyme 93 Pathways Not Available
Enzyme 93 Reactions Not Available
Enzyme 93 Pfam Domain Function
Enzyme 93 Signals
  • None
Enzyme 93 Transmembrane Regions
  • None
Enzyme 93 Essentiality Not Available
Enzyme 93 GenBank ID Protein 26051258 Link Image
Enzyme 93 UniProtKB/Swiss-Prot ID Q8TDF6 Link Image
Enzyme 93 UniProtKB/Swiss-Prot Entry Name GRP4_HUMAN Link Image
Enzyme 93 PDB ID Not Available
Enzyme 93 Cellular Location Not Available
Enzyme 93 Gene Sequence >2022 bp
ATGAACAGAAAAGACAGTAAGAGGAAGTCCCACCAGGAATGCACCGGAAAAATAGGAGGG
CGAGGCCGGCCCCGCCAAGTGCGCCGCCACAAGACATGCCCCAGCCCTCGGGAAATCAGC
AAGGTCATGGCTTCCATGAACCTGGGCCTGCTGAGTGAGGGCGGCTGCAGCGAAGATGAG
CTGCTGGAGAAATGCATCCAGTCCTTCGATTCAGCTGGCAGCCTGTGCCACGAGGACCAC
ATGCTCAACATGGTGCTGGCCATGCACAGCTGGGTGCTGCCGTCCGCCGACCTGGCTGCC
CGCCTGCTGACCTCATACCAGAAGGCCACAGGGGACACCCAGGAGCTGAGACGGCTGCAG
ATCTGTCACCTGGTCAGGTACTGGCTGATGCGACACCCTGAGGTGATGCACCAGGATCCC
CAGCTAGAAGAAGTCATAGGTCGTTTCTGGGCCACCGTGGCCCGGGAGGGCAACTCAGCC
CAGAGAAGACTGGGAGACTCTTCTGACCTCCTGAGCCCTGGTGGCCCTGGCCCCCCACTC
CCAATGAGCAGCCCAGGCCTGGGCAAAAAGCGCAAAGTGTCCTTGCTTTTCGACCACTTG
GAGACGGGGGAGCTGGCTCAGCACCTCACCTACCTGGAGTTCCGGTCCTTCCAGGCTATC
ACGCCCCAGGACCTGCGGAGCTACGTTTTGCAGGGCTCAGTACGAGGCTGCCCGGCCCTG
GAGGGCTCCGTAGGTCTCAGCAACAGCGTGTCCCGCTGGGTGCAGGTGATGGTGCTGAGC
CGTCCCGGGCCCCTACAGCGTGCACAGGTGCTGGACAAGTTCATTCACGTGGCACAGAGG
CTCCACCAGCTGCAGAATTTCAACACGCTGATGGCAGTCACAGGGGGCCTGTGTCACAGT
GCCATCTCCAGACTCAAGGACTCCCATGCCCACCTGAGCCCTGACAGCACCAAGGCCCTC
CTGGAGCTCACTGAGCTCCTTGCCTCCCACAACAACTACGCCCGCTACCGCCGCACCTGG
GCTGGCTGCGCGGGTTTCCGGCTGCCTGTACTGGGCGTGCACCTCAAGGACCTGGTGTCC
CTGCATGAGGCACAGCCCGACAGGTTGCCTGACGGCCGCCTGCACCTACCCAAGCTGAAC
AACCTCTACCTGCGGCTGCAGGAGCTGGTGGCCCTCCAAGGGCAGCATCCACCCTGCAGC
GCCAATGAGGATCTGCTGCACCTGCTCACGCTCTCCCTGGACCTCTTCTACACGGAAGAC
GAGATCTATGAGCTTTCTTATGCCCGGGAGCCGCGTTGTCCCAAGAGCCTGCCACCCTCC
CCCTTCAATGCACCTCTGGTGGTGGAGTGGGCCCCTGGTGTGACACCCAAGCCGGACAGG
GTCACACTGGGTCGGCATGTGGAGCAGCTGGTGGAGTCTGTGTTCAAGAATTATGACCCT
GAAGGCCGAGGAACAATCTCTCAGGAGGACTTTGAGCGACTCTCGGGCAATTTTCCCTTC
GCCTGCCATGGGCTTCACCCACCCCCACGCCAGGGGAGAGGATCCTTCAGCAGAGAGGAG
CTGACAGGGTACCTGCTCCGGGCCAGCGCCATCTGCTCCAAGTTGGGCCTGGCCTTCCTG
CACACCTTCCATGAGGTCACCTTCCGAAAGCCTACCTTCTGCGACAGCTGCAGTGGCTTC
CTCTGGGGTGTCACCAAGCAAGGCTACCGCTGTCGGGAGTGCGGGCTGTGTTGCCACAAA
CACTGCAGAGACCAGGTGAAGGTAGAATGTAAGAAGAGGCCAGGGGCCAAGGGCGATGCA
GGACCCCCCGGAGCTCCTGTCCCATCCACACCAGCTCCCCATGCCAGCTGTGGCTCCGAG
GAAAATCACTCCTACACGCTATCCCTGGAGCCTGAGACTGGGTGCCAGCTTCGCCATGCC
TGGACCCAGACTGAATCCCCACACCCTTCCTGGGAAACAGATACGGTCCCCTGCCCGGTG
ATGGACCCACCATCAACTGCATCCTCCAAGCTGGATTCCTAG
Enzyme 93 GenBank Gene ID NM_170604.2 Link Image
Enzyme 93 GeneCard ID RASGRP4 Link Image
Enzyme 93 GenAtlas ID RASGRP4 Link Image
Enzyme 93 HGNC ID HGNC:18958 Link Image
Enzyme 93 Chromosome Location 1
Enzyme 93 Locus 19q13.1
Enzyme 93 SNPs SNPJam Report Link Image
Enzyme 93 General References
  1. Yang Y, Li L, Wong GW, Krilis SA, Madhusudhan MS, Sali A, Stevens RL: RasGRP4, a new mast cell-restricted Ras guanine nucleotide-releasing protein with calcium- and diacylglycerol-binding motifs. Identification of defective variants of this signaling protein in asthma, mastocytosis, and mast cell leukemia patients and demonstration of the importance of RasGRP4 in mast cell development and function. J Biol Chem. 2002 Jul 12;277(28):25756-74. Epub 2002 Apr 15. [PubMed Link Image]
  2. Reuther GW, Lambert QT, Rebhun JF, Caligiuri MA, Quilliam LA, Der CJ: RasGRP4 is a novel Ras activator isolated from acute myeloid leukemia. J Biol Chem. 2002 Aug 23;277(34):30508-14. Epub 2002 Mar 5. [PubMed Link Image]
  3. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Li L, Yang Y, Stevens RL: RasGRP4 regulates the expression of prostaglandin D2 in human and rat mast cell lines. J Biol Chem. 2003 Feb 14;278(7):4725-9. Epub 2002 Dec 18. [PubMed Link Image]
  6. Katsoulotos GP, Qi M, Qi JC, Tanaka K, Hughes WE, Molloy TJ, Adachi R, Stevens RL, Krilis SA: The Diacylglycerol-dependent translocation of ras guanine nucleotide-releasing protein 4 inside a human mast cell line results in substantial phenotypic changes, including expression of interleukin 13 receptor alpha2. J Biol Chem. 2008 Jan 18;283(3):1610-21. Epub 2007 Nov 16. [PubMed Link Image]
Enzyme 93 Metabolite References Not Available
Enzyme 94 [top]
Enzyme 94 ID 14197
Enzyme 94 Name Serine/threonine-protein kinase MRCK alpha
Enzyme 94 Synonyms
  1. CDC42-binding protein kinase alpha
  2. DMPK-like alpha
  3. Myotonic dystrophy kinase-related CDC42-binding kinase alpha
  4. MRCK alpha
  5. Myotonic dystrophy protein kinase-like alpha
Enzyme 94 Gene Name CDC42BPA
Enzyme 94 Protein Sequence >Serine/threonine-protein kinase MRCK alpha
MSGEVRLRQLEQFILDGPAQTNGQCFSVETLLDILICLYDECNNSPLRREKNILEYLEWA
KPFTSKVKQMRLHREDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETA
CFREERDVLVNGDNKWITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFEDRLPEDMARF
YLAEMVIAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAVGT
PDYISPEILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKER
FQFPAQVTDVSENAKDLIRRLICSREHRLGQNGIEDFKKHPFFSGIDWDNIRNCEAPYIP
EVSSPTDTSNFDVDDDCLKNSETMPPPTHTAFSGHHLPFVGFTYTSSCVLSDRSCLRVTA
GPTSLDLDVNVQRTLDNNLATEAYERRIKRLEQEKLELSRKLQESTQTVQALQYSTVDGP
LTASKDLEIKNLKEEIEKLRKQVTESSHLEQQLEEANAVRQELDDAFRQIKAYEKQIKTL
QQEREDLNKELVQASERLKNQSKELKDAHCQRKLAMQEFMEINERLTELHTQKQKLARHV
RDKEEEVDLVMQKVESLRQELRRTERAKKELEVHTEALAAEASKDRKLREQSEHYSKQLE
NELEGLKQKQISYSPGVCSIEHQQEITKLKTDLEKKSIFYEEELSKREGIHANEIKNLKK
ELHDSEGQQLALNKEIMILKDKLEKTRRESQSEREEFESEFKQQYEREKVLLTEENKKLT
SELDKLTTLYENLSIHNQQLEEEVKDLADKKESVAHWEAQITEIIQWVSDEKDARGYLQA
LASKMTEELEALRNSSLGTRATDMPWKMRRFAKLDMSARLELQSALDAEIRAKQAIQEEL
NKVKASNIITECKLKDSEKKNLELLSEIEQLIKDTEELRSEKGIEHQDSQHSFLAFLNTP
TDALDQFERSPSCTPASKGRRTVDSTPLSVHTPTLRKKGCPGSTGFPPKRKTHQFFVKSF
TTPTKCHQCTSLMVGLIRQGCSCEVCGFSCHITCVNKAPTTCPVPPEQTKGPLGIDPQKG
IGTAYEGHVRIPKPAGVKKGWQRALAIVCDFKLFLYDIAEGKASQPSVVISQVIDMRDEE
FSVSSVLASDVIHASRKDIPCIFRVTASQLSASNNKCSILMLADTENEKNKWVGVLSELH
KILKKNKFRDRSVYVPKEAYDSTLPLIKTTQAAAIIDHERIALGNEEGLFVVHVTKDEII
RVGDNKKIHQIELIPNDQLVAVISGRNRHVRLFPMSALDGRETDFYKLSETKGCQTVTSG
KVRHGALTCLCVAMKRQVLCYELFQSKTRHRKFKEIQVPYNVQWMAIFSEQLCVGFQSGF
LRYPLNGEGNPYSMLHSNDHTLSFIAHQPMDAICAVEISSKEYLLCFNSIGIYTDCQGRR
SRQQELMWPANPSSCCYNAPYLSVYSENAVDIFDVNSMEWIQTLPLKKVRPLNNEGSLNL
LGLETIRLIYFKNKMAEGDELVVPETSDNSRKQMVRNINNKRRYSFRVPEEERMQQRREM
LRDPEMRNKLISNPTNFNHIAHMGPGDGIQILKDLPMNPRPQESRTVFSGSVSIPSITKS
RPEPGRSMSASSGLSARSSAQNGSALKREFSGGSYSAKRQPMPSPSEGSLSSGGMDQGSD
APARDFDGEDSDSPRHSTASNSSNLSSPPSPASPRKTKSLSLESTDRGSWDP
Enzyme 94 Number of Residues 1732
Enzyme 94 Molecular Weight 197305.2
Enzyme 94 Theoretical pI 6.55
Enzyme 94 GO Classification
Function
  • ATP binding
  • GTPase regulator activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • enzyme regulator activity
  • kinase activity
  • nucleoside binding
  • nucleoside-triphosphatase regulator activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • small GTPase regulator activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 94 General Function Involved in protein serine/threonine kinase activity
Enzyme 94 Specific Function May act as a downstream effector of CDC42 in cytoskeletal reorganization. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation
Enzyme 94 Pathways
Enzyme 94 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 94 Pfam Domain Function
Enzyme 94 Signals
  • None
Enzyme 94 Transmembrane Regions
  • None
Enzyme 94 Essentiality Not Available
Enzyme 94 GenBank ID Protein 30089962 Link Image
Enzyme 94 UniProtKB/Swiss-Prot ID Q5VT25 Link Image
Enzyme 94 UniProtKB/Swiss-Prot Entry Name MRCKA_HUMAN Link Image
Enzyme 94 PDB ID Not Available
Enzyme 94 Cellular Location Not Available
Enzyme 94 Gene Sequence >5160 bp
ATGTCTGGAGAAGTGCGTTTGAGGCAGTTGGAGCAGTTTATTTTGGACGGGCCCGCTCAG
ACCAATGGGCAGTGCTTCAGTGTGGAGACATTACTGGATATACTCATCTGCCTTTATGAT
GAATGCAATAATTCTCCATTGAGAAGAGAGAAGAACATTCTCGAATACCTAGAATGGGCT
AAACCATTTACTTCTAAAGTGAAACAAATGCGATTACATAGAGAAGACTTTGAAATATTA
AAGGTGATTGGTCGAGGAGCTTTTGGGGAGGTTGCTGTAGTAAAACTAAAAAATGCAGAT
AAAGTGTTTGCCATGAAAATATTGAATAAATGGGAAATGCTGAAAAGAGCTGAGACAGCA
TGTTTTCGTGAAGAAAGGGATGTATTAGTGAATGGAGACAATAAATGGATTACAACCTTG
CACTATGCTTTCCAGGATGACAATAACTTATACCTGGTTATGGATTATTATGTTGGTGGG
GATTTGCTTACTCTACTCAGCAAATTTGAAGATAGATTGCCTGAAGATATGGCTAGATTT
TACTTGGCTGAGATGGTGATAGCAATTGACTCAGTTCATCAGCTACATTATGTACACAGA
GACATTAAACCTGACAATATACTGATGGATATGAATGGACATATTCGGTTAGCAGATTTT
GGTTCTTGTCTGAAGCTGATGGAAGATGGAACGGTTCAGTCCTCAGTGGCTGTAGGAACT
CCAGATTATATCTCTCCTGAAATCCTTCAAGCCATGGAAGATGGAAAAGGGAGATATGGA
CCTGAATGTGACTGGTGGTCTTTGGGGGTCTGTATGTATGAAATGCTTTACGGAGAAACA
CCATTTTATGCAGAATCGCTGGTGGAGACATACGGAAAAATCATGAACCACAAAGAGAGG
TTTCAGTTTCCAGCCCAAGTGACTGATGTGTCTGAAAATGCTAAGGATCTTATTCGAAGG
CTCATTTGTAGCAGAGAACATCGACTTGGTCAAAATGGAATAGAAGACTTTAAGAAACAC
CCATTTTTCAGTGGAATTGATTGGGATAATATTCGGAACTGTGAAGCACCTTATATTCCA
GAAGTTAGTAGCCCAACAGATACATCGAATTTTGATGTAGATGATGATTGTTTAAAAAAT
TCTGAAACGATGCCCCCACCAACACATACTGCATTTTCTGGCCACCATCTGCCATTTGTT
GGTTTTACATATACTAGTAGCTGTGTACTTTCTGATCGGAGCTGTTTAAGAGTTACGGCT
GGTCCCACCTCACTGGATCTTGATGTTAATGTTCAGAGGACTCTAGACAACAACTTAGCA
ACTGAAGCTTATGAAAGAAGAATTAAGCGCCTTGAGCAAGAAAAACTTGAACTCAGTAGA
AAACTTCAAGAGTCAACACAGACTGTCCAAGCTCTGCAGTATTCAACTGTTGATGGTCCA
CTAACAGCAAGCAAAGATTTAGAAATAAAAAACTTAAAAGAAGAAATTGAAAAACTAAGA
AAACAAGTAACAGAATCAAGTCATTTGGAACAGCAACTTGAAGAAGCTAATGCTGTGAGG
CAAGAACTAGATGATGCTTTTAGACAAATCAAGGCTTATGAAAAACAAATCAAAACGTTA
CAACAAGAAAGAGAAGATCTAAATAAGGAACTAGTCCAGGCTAGTGAGCGATTAAAAAAC
CAATCCAAAGAGCTGAAAGACGCACACTGTCAGAGGAAACTGGCCATGCAGGAATTCATG
GAGATCAATGAGCGGCTAACAGAATTGCACACCCAAAAACAGAAACTTGCTCGCCATGTC
CGAGATAAGGAAGAAGAGGTGGACCTGGTGATGCAAAAAGTTGAAAGCTTAAGGCAAGAA
CTGCGCAGAACAGAAAGAGCCAAAAAAGAGCTGGAAGTTCATACAGAAGCTCTAGCTGCT
GAAGCATCTAAAGACAGGAAGCTACGTGAACAGAGTGAGCACTATTCTAAGCAACTGGAA
AATGAATTGGAGGGACTGAAGCAAAAACAAATTAGTTACTCACCAGGAGTATGCAGCATA
GAACATCAGCAAGAGATAACCAAACTAAAGACTGATTTGGAAAAGAAAAGTATCTTTTAT
GAAGAAGAATTATCTAAAAGAGAAGGAATACATGCAAATGAAATAAAAAATCTTAAGAAA
GAACTGCATGATTCAGAAGGTCAGCAACTTGCTCTCAACAAAGAAATTATGATTTTAAAA
GACAAATTGGAAAAAACCAGAAGAGAAAGTCAAAGTGAAAGGGAGGAATTTGAAAGTGAG
TTCAAACAACAATATGAACGAGAAAAAGTGTTGTTAACTGAAGAAAATAAAAAGCTGACG
AGTGAACTTGATAAGCTTACTACTTTGTATGAGAACTTAAGTATACACAACCAGCAGTTA
GAAGAAGAGGTTAAAGATCTAGCAGACAAGAAAGAATCAGTTGCACATTGGGAAGCCCAA
ATCACAGAAATAATTCAGTGGGTCAGCGATGAAAAGGATGCACGAGGGTATCTTCAGGCC
TTAGCTTCTAAAATGACTGAAGAATTGGAGGCATTAAGAAATTCCAGCTTGGGTACACGA
GCAACAGATATGCCCTGGAAAATGCGTCGTTTTGCGAAACTGGATATGTCAGCTAGACTG
GAGTTGCAGTCGGCTCTGGATGCAGAAATAAGAGCCAAACAGGCCATCCAAGAAGAGTTG
AATAAAGTTAAAGCATCTAATATCATAACAGAATGTAAACTAAAAGATTCAGAGAAGAAG
AACTTGGAACTACTCTCAGAAATCGAACAGCTGATAAAGGACACTGAAGAGCTTAGATCT
GAAAAGGGTATAGAGCACCAAGACTCACAGCATTCTTTCTTGGCATTTTTGAATACGCCT
ACCGATGCTCTGGATCAATTTGAAACTGTAGACTCCACTCCACTTTCAGTTCACACACCA
ACCTTAAGGAAAAAAGGATGTCCTGGTTCAACTGGCTTTCCACCTAAGCGCAAGACTCAC
CAGTTTTTTGTAAAATCTTTTACTACTCCTACCAAGTGTCATCAGTGTACCTCCTTGATG
GTGGGTTTAATAAGACAGGGCTGTTCATGTGAAGTGTGTGGATTCTCATGCCATATAACT
TGTGTAAACAAAGCTCCAACCACTTGTCCAGTTCCTCCTGAACAGACAAAAGGTCCCCTG
GGTATAGATCCTCAGAAAGGAATAGGAACAGCATATGAAGGTCATGTCAGGATTCCTAAG
CCAGCTGGAGTGAAGAAAGGGTGGCAGAGAGCACTGGCTATAGTGTGTGACTTCAAACTC
TTTCTGTACGATATTGCTGAAGGAAAAGCATCTCAGCCCAGTGTTGTCATTAGTCAAGTG
ATTGACATGAGGGATGAAGAATTTTCTGTGAGTTCAGTCTTGGCTTCTGATGTTATCCAT
GCAAGTCGGAAAGATATACCCTGTATATTTAGGGTCACAGCTTCCCAGCTCTCAGCATCT
AATAACAAATGTTCAATCCTGATGCTAGCAGACACTGAGAATGAGAAGAATAAGTGGGTG
GGAGTGCTGAGTGAATTGCACAAGATTTTGAAGAAAAACAAATTCAGAGACCGCTCAGTC
TATGTTCCCAAAGAGGCTTATGACAGCACTCTACCCCTCATTAAAACAACCCAGGCAGCC
GCAATCATAGATCATGAAAGAATTGCTTTGGGAAACGAAGAAGGGTTATTTGTTGTACAT
GTCACCAAAGATGAAATTATTAGAGTTGGTGACAATAAGAAGATTCATCAGATTGAACTC
ATTCCAAATGATCAGCTTGTTGCTGTGATCTCAGGACGAAATCGTCATGTACGACTTTTT
CCTATGTCAGCATTGGATGGGCGAGAGACCGATTTTTACAAGCTGTCAGAAACTAAAGGG
TGTCAAACCGTAACTTCTGGAAAGGTGCGCCATGGAGCTCTCACATGCCTGTGTGTGGCT
ATGAAAAGGCAGGTCCTCTGTTATGAACTATTTCAGAGCAAGACCCGTCACAGAAAATTT
AAAGAAATTCAAGTCCCATATAATGTCCAGTGGATGGCAATCTTCAGTGAACAACTCTGT
GTGGGATTCCAGTCAGGATTTCTAAGATACCCCTTGAATGGAGAAGGAAATCCATACAGT
ATGCTCCATTCAAATGACCATACACTATCATTTATTGCACATCAACCAATGGATGCTATC
TGCGCAGTTGAGATCTCCAGTAAAGAATATCTGCTGTGTTTTAACAGCATTGGGATATAC
ACTGACTGCCAGGGCCGAAGATCTAGACAACAGGAATTGATGTGGCCAGCAAATCCTTCC
TCTTGTTGTTACAATGCACCATATCTCTCGGTGTACAGTGAAAATGCAGTTGATATCTTT
GATGTGAACTCCATGGAATGGATTCAGACTCTTCCTCTCAAAAAGGTTCGACCCTTAAAC
AATGAAGGATCATTAAATCTTTTAGGGTTGGAGACCATTAGATTAATATATTTCAAAAAT
AAGATGGCAGAAGGGGACGAACTGGTAGTACCTGAAACATCAGATAATAGTCGGAAACAA
ATGGTTAGAAACATTAACAATAAGCGGCGTTATTCCTTCAGAGTCCCAGAAGAGGAAAGG
ATGCAGCAGAGGAGGGAAATGCTACGAGATCCAGAAATGAGAAATAAATTAATTTCTAAT
CCAACTAATTTTAATCACATAGCACACATGGGTCCTGGAGATGGAATACAGATCCTGAAA
GATCTGCCCATGAACCCTCGGCCTCAGGAAAGTCGGACAGTATTCAGTGGCTCAGTCAGT
ATTCCATCTATCACCAAATCCCGCCCTGAGCCAGGCCGCTCCATGAGTGCTAGCAGTGGC
TTGTCAGCAAGGTCATCCGCACAGAATGGCAGCGCATTAAAGAGGGAATTCTCTGGAGGA
AGCTACAGTGCCAAGCGGCAGCCCATGCCCTCCCCGTCAGAGGGCTCTTTGTCCTCTGGA
GGCATGGACCAAGGAAGTGATGCCCCAGCGAGGGACTTTGACGGAGAGGACTCTGACTCT
CCGAGGCATTCCACAGCTTCCAACAGTTCCAACCTAAGCAGCCCCCCAAGCCCAGCTTCA
CCCCGAAAAACCAAGAGCCTCTCCCTGGAGAGCACTGACCGCGGGAGCTGGGACCCGTGA
Enzyme 94 GenBank Gene ID NM_003607 Link Image
Enzyme 94 GeneCard ID CDC42BPA Link Image
Enzyme 94 GenAtlas ID CDC42BPA Link Image
Enzyme 94 HGNC ID HGNC:1737 Link Image
Enzyme 94 Chromosome Location 1
Enzyme 94 Locus 1q42.11
Enzyme 94 SNPs SNPJam Report Link Image
Enzyme 94 General References
  1. Wilkinson S, Paterson HF, Marshall CJ: Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion. Nat Cell Biol. 2005 Mar;7(3):255-61. Epub 2005 Feb 20. [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. 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. Zhao Y, Loyer P, Li H, Valentine V, Kidd V, Kraft AS: Cloning and chromosomal location of a novel member of the myotonic dystrophy family of protein kinases. J Biol Chem. 1997 Apr 11;272(15):10013-20. [PubMed Link Image]
  5. 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]
  6. Leung T, Chen XQ, Tan I, Manser E, Lim L: Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization. Mol Cell Biol. 1998 Jan;18(1):130-40. [PubMed Link Image]
  7. Tan I, Seow KT, Lim L, Leung T: Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related Cdc42-binding kinase alpha. Mol Cell Biol. 2001 Apr;21(8):2767-78. [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. 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]
  10. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 94 Metabolite References Not Available
Enzyme 95 [top]
Enzyme 95 ID 14198
Enzyme 95 Name Serine/threonine-protein kinase MRCK beta
Enzyme 95 Synonyms
  1. CDC42-binding protein kinase beta
  2. DMPK-like beta
  3. Myotonic dystrophy kinase-related CDC42-binding kinase beta
  4. MRCK beta
  5. Myotonic dystrophy protein kinase-like beta
Enzyme 95 Gene Name CDC42BPB
Enzyme 95 Protein Sequence >Serine/threonine-protein kinase MRCK beta
MSAKVRLKKLEQLLLDGPWRNESALSVETLLDVLVCLYTECSHSALRRDKYVAEFLEWAK
PFTQLVKEMQLHREDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETAC
FREERDVLVNGDCQWITALHYAFQDENHLYLVMDYYVGGDLLTLLSKFEDKLPEDMARFY
IGEMVLAIDSIHQLHYVHRDIKPDNVLLDVNGHIRLADFGSCLKMNDDGTVQSSVAVGTP
DYISPEILQAMEDGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERF
QFPSHVTDVSEEAKDLIQRLICSRERRLGQNGIEDFKKHAFFEGLNWENIRNLEAPYIPD
VSSPSDTSNFDVDDDVLRNTEILPPGSHTGFSGLHLPFIGFTFTTESCFSDRGSLKSIMQ
SNTLTKDEDVQRDLEHSLQMEAYERRIRRLEQEKLELSRKLQESTQTVQSLHGSSRALSN
SNRDKEIKKLNEEIERLKNKIADSNRLERQLEDTVALRQEREDSTQRLRGLEKQHRVVRQ
EKEELHKQLVEASERLKSQAKELKDAHQQRKLALQEFSELNERMAELRAQKQKVSRQLRD
KEEEMEVATQKVDAMRQEMRRAEKLRKELEAQLDDAVAEASKERKLREHSENFCKQMESE
LEALKVKQGGRGAGATLEHQQEISKIKSELEKKVLFYEEELVRREASHVLEVKNVKKEVH
DSESHQLALQKEILMLKDKLEKSKRERHNEMEEAVGTIKDKYERERAMLFDENKKLTAEN
EKLCSFVDKLTAQNRQLEDELQDLAAKKESVAHWEAQIAEIIQWVSDEKDARGYLQALAS
KMTEELEALRSSSLGSRTLDPLWKVRRSQKLDMSARLELQSALEAEIRAKQLVQEELRKV
KDANLTLESKLKDSEAKNRELLEEMEILKKKMEEKFRADTGLKLPDFQDSIFEYFNTAPL
AHDLTFRTSSASEQETQAPKPEASPSMSVAASEQQEDMARPPQRPSAVPLPTTQALALAG
PKPKAHQFSIKSFSSPTQCSHCTSLMVGLIRQGYACEVCSFACHVSCKDGAPQVCPIPPE
QSKRPLGVDVQRGIGTAYKGHVKVPKPTGVKKGWQRAYAVVCDCKLFLYDLPEGKSTQPG
VIASQVLDLRDDEFSVSSVLASDVIHATRRDIPCIFRVTASLLGAPSKTSSLLILTENEN
EKRKWVGILEGLQSILHKNRLRNQVVHVPLEAYDSSLPLIKAILTAAIVDADRIAVGLEE
GLYVIEVTRDVIVRAADCKKVHQIELAPREKIVILLCGRNHHVHLYPWSSLDGAEGSFDI
KLPETKGCQLMATATLKRNSGTCLFVAVKRLILCYEIQRTKPFHRKFNEIVAPGSVQCLA
VLRDRLCVGYPSGFCLLSIQGDGQPLNLVNPNDPSLAFLSQQSFDALCAVELESEEYLLC
FSHMGLYVDPQGRRARAQELMWPAAPVACSCSPTHVTVYSEYGVDVFDVRTMEWVQTIGL
RRIRPLNSEGTLNLLNCEPPRLIYFKSKFSGAVLNVPDTSDNSKKQMLRTRSKRRFVFKV
PEEERLQQRREMLRDPELRSKMISNPTNFNHVAHMGPGDGMQVLMDLPLSAVPPSQEERP
GPAPTNLARQPPSRNKPYISWPSSGGSEPSVTVPLRSMSDPDQDFDKEPDSDSTKHSTPS
NSSNPSGPPSPNSPHRSQLPLEGLEQPACDT
Enzyme 95 Number of Residues 1711
Enzyme 95 Molecular Weight 194313.6
Enzyme 95 Theoretical pI 6.31
Enzyme 95 GO Classification
Function
  • ATP binding
  • GTPase regulator activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • enzyme regulator activity
  • kinase activity
  • nucleoside binding
  • nucleoside-triphosphatase regulator activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • small GTPase regulator activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 95 General Function Involved in protein serine/threonine kinase activity
Enzyme 95 Specific Function May act as a downstream effector of CDC42 in cytoskeletal reorganization. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation
Enzyme 95 Pathways
Enzyme 95 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 95 Pfam Domain Function
Enzyme 95 Signals
  • None
Enzyme 95 Transmembrane Regions
  • None
Enzyme 95 Essentiality Not Available
Enzyme 95 GenBank ID Protein 115527097 Link Image
Enzyme 95 UniProtKB/Swiss-Prot ID Q9Y5S2 Link Image
Enzyme 95 UniProtKB/Swiss-Prot Entry Name MRCKB_HUMAN Link Image
Enzyme 95 PDB ID Not Available
Enzyme 95 Cellular Location Not Available
Enzyme 95 Gene Sequence >5136 bp
ATGTCGGCCAAGGTGCGGCTCAAGAAGCTGGAGCAGCTGCTCCTGGACGGGCCCTGGCGC
AACGAGAGCGCCCTGAGCGTGGAAACGCTGCTCGACGTGCTCGTCTGCCTGTACACCGAG
TGCAGCCACTCGGCCCTGCGCCGCGACAAGTACGTGGCCGAGTTCCTCGAGTGGGCTAAA
CCATTTACACAGCTGGTGAAAGAAATGCAGCTTCATCGAGAAGACTTTGAAATAATTAAA
GTAATTGGAAGAGGTGCTTTTGGTGAGGTTGCTGTTGTCAAAATGAAGAATACTGAACGA
ATTTATGCAATGAAAATCCTCAACAAGTGGGAGATGCTGAAAAGAGCAGAGACCGCGTGC
TTCCGAGAGGAGCGCGATGTGCTGGTGAACGGCGACTGCCAGTGGATCACCGCGCTGCAC
TACGCCTTTCAGGACGAGAACCACCTGTACTTAGTCATGGATTACTATGTGGGTGGTGAT
TTACTGACCCTGCTCAGCAAATTTGAAGACAAGCTTCCGGAAGATATGGCGAGGTTCTAC
ATTGGTGAAATGGTGCTGGCCATTGACTCCATCCATCAGCTTCATTACGTGCACAGAGAC
ATTAAACCTGACAATGTCCTTTTGGACGTGAATGGTCATATCCGCCTGGCTGACTTTGGA
TCATGTTTGAAGATGAATGATGATGGCACTGTGCAGTCCTCCGTGGCCGTGGGCACACCT
GACTACATCTCGCCGGAGATCCTGCAGGCGATGGAGGACGGCATGGGCAAATACGGGCCT
GAGTGTGACTGGTGGTCTCTGGGTGTCTGCATGTATGAGATGCTCTATGGAGAAACGCCG
TTTTATGCGGAGTCACTCGTGGAGACCTATGGGAAGATCATGAACCATGAAGAGCGATTC
CAGTTCCCATCCCATGTCACGGATGTATCTGAAGAAGCGAAGGACCTCATCCAGAGACTG
ATCTGCAGTAGAGAACGCCGGCTGGGGCAGAATGGAATAGAGGATTTCAAAAAGCATGCG
TTTTTTGAAGGTCTAAATTGGGAAAATATACGAAACCTAGAAGCACCTTATATTCCTGAT
GTGAGCAGTCCCTCTGACACATCCAACTTCGACGTGGATGACGACGTGCTGAGAAACACG
GAAATATTACCTCCTGGTTCTCACACAGGCTTTTCTGGATTACATTTGCCATTCATTGGT
TTTACATTCACAACGGAAAGCTGTTTTTCTGATCGAGGCTCTCTGAAGAGCATAATGCAG
TCCAACACATTAACCAAAGATGAGGATGTGCAGCGGGACCTGGAGCACAGCCTGCAGATG
GAAGCTTACGAGAGGAGGATTCGGAGGCTGGAACAGGAGAAGCTGGAGCTGAGCAGGAAG
CTGCAAGAGTCCACCCAGACCGTGCAGTCCCTCCACGGCTCATCTCGGGCCCTCAGCAAT
TCAAACCGAGATAAAGAAATCAAAAAGCTAAATGAAGAAATCGAACGCTTGAAGAATAAA
ATAGCAGATTCAAACAGGCTCGAGCGACAGCTTGAGGACACAGTGGCGCTTCGCCAAGAG
CGTGAGGACTCCACGCAGCGGCTGCGGGGGCTGGAGAAGCAGCACCGCGTGGTCCGGCAG
GAGAAGGAGGAGCTGCACAAGCAACTGGTTGAAGCCTCAGAGCGGTTGAAATCCCAGGCC
AAGGAACTCAAAGATGCCCATCAGCAGCGAAAGCTGGCCCTGCAGGAGTTCTCGGAGCTG
AACGAGCGCATGGCAGAGCTCCGTGCCCAGAAGCAGAAGGTGTCCCGGCAGCTGCGAGAC
AAGGAGGAGGAGATGGAGGTGGCCACGCAGAAGGTGGACGCCATGCGGCAGGAAATGCGG
AGAGCTGAGAAGCTCAGGAAAGAGCTGGAAGCTCAGCTTGATGATGCTGTTGCTGAGGCC
TCCAAGGAGCGCAAGCTTCGTGAGCACAGCGAGAACTTCTGCAAGCAAATGGAAAGCGAG
CTGGAGGCCCTCAAGGTGAAGCAAGGAGGCCGGGGAGCGGGTGCCACCTTAGAGCACCAG
CAAGAGATTTCCAAAATCAAATCCGAGCTGGAGAAGAAAGTCTTATTTTATGAAGAGGAA
TTGGTCAGACGTGAGGCCTCCCATGTGCTAGAAGTGAAAAATGTGAAGAAGGAGGTGCAT
GATTCAGAAAGCCACCAGCTGGCCCTGCAGAAAGAAATCTTGATGTTAAAAGATAAGTTA
GAAAAGTCAAAGCGAGAACGGCATAACGAGATGGAGGAGGCAGTAGGTACAATAAAAGAT
AAATACGAACGAGAAAGAGCGATGCTGTTTGATGAAAACAAGAAGCTAACTGCTGAAAAT
GAAAAGCTCTGTTCCTTTGTGGATAAACTCACAGCTCAAAATAGACAGCTGGAGGATGAG
CTGCAGGATCTGGCAGCCAAGAAGGAGTCAGTGGCCCACTGGGAAGCTCAGATTGCGGAA
ATCATTCAGTGGGTCAGTGACGAGAAAGATGCCCGGGGTTACCTTCAAGCTCTTGCTTCC
AAGATGACCGAAGAGCTCGAGGCTTTGAGGAGTTCTAGTCTGGGGTCAAGAACACTGGAC
CCGCTGTGGAAGGTGCGCCGCAGCCAGAAGCTGGACATGTCCGCGCGGCTGGAGCTGCAG
TCGGCCCTGGAGGCGGAGATCCGGGCCAAGCAGCTTGTCCAGGAGGAGCTCAGGAAGGTC
AAGGACGCCAACCTCACCTTGGAAAGCAAACTAAAGGATTCCGAAGCCAAAAACAGAGAA
TTATTAGAAGAAATGGAAATTTTGAAGAAAAAGATGGAAGAAAAATTCAGAGCAGATACT
GGGCTCAAACTTCCAGATTTTCAGGATTCCATTTTTGAGTATTTCAACACTGCTCCTCTT
GCACATGACCTGACATTTAGAACCAGCTCAGCTAGTGAGCAAGAAACACAAGCTCCGAAG
CCAGAAGCGTCCCCGTCGATGTCTGTGGCTGCATCAGAGCAGCAGGAGGACATGGCTCGG
CCCCCGCAGAGGCCATCCGCTGTGCCGTTGCCCACCACGCAGGCCCTGGCTCTGGCTGGA
CCGAAGCCAAAAGCTCACCAGTTCAGCATCAAGTCCTTCTCCAGCCCTACTCAGTGCAGC
CACTGCACCTCCCTGATGGTTGGGCTGATCCGGCAGGGCTACGCCTGCGAGGTGTGTTCC
TTTGCTTGCCACGTGTCCTGCAAAGACGGTGCCCCCCAGGTGTGCCCAATACCTCCCGAG
CAGTCCAAGAGGCCTCTGGGCGTGGACGTGCAGCGAGGCATCGGAACAGCCTACAAAGGC
CATGTCAAGGTCCCAAAGCCCACGGGGGTGAAGAAGGGATGGCAGCGCGCATATGCAGTC
GTCTGTGACTGCAAGCTCTTCCTGTATGATCTGCCTGAAGGAAAATCCACCCAGCCTGGT
GTCATTGCGAGCCAAGTCTTGGATCTCAGAGATGACGAGTTTTCCGTGAGCTCAGTCCTG
GCCTCAGATGTCATTCATGCTACACGCCGAGATATTCCATGTATATTCAGGGTGACGGCC
TCTCTCTTAGGTGCACCTTCTAAGACCAGCTCGCTGCTCATTCTGACAGAAAATGAGAAT
GAAAAGAGGAAGTGGGTTGGGATTCTAGAAGGACTCCAGTCCATCCTTCATAAAAACCGG
CTGAGGAATCAGGTCGTGCATGTTCCCTTGGAAGCCTACGACAGCTCGCTGCCTCTCATC
AAGGCCATCCTGACAGCTGCCATCGTGGATGCAGACAGGATTGCAGTCGGCCTAGAAGAA
GGGCTCTATGTCATAGAGGTCACCCGAGATGTGATCGTCCGTGCCGCTGACTGTAAGAAG
GTACACCAGATCGAGCTTGCTCCCAGGGAGAAGATCGTAATCCTCCTCTGTGGCCGGAAC
CACCATGTGCACCTCTATCCGTGGTCGTCCCTTGATGGAGCGGAAGGCAGCTTTGACATC
AAGCTTCCGGAAACCAAAGGCTGCCAGCTCATGGCCACGGCCACACTCAAGAGGAACTCT
GGCACCTGCCTGTTTGTGGCCGTGAAACGGCTGATCCTTTGCTATGAGATCCAGAGAACG
AAGCCATTCCACAGAAAGTTCAATGAGATTGTGGCTCCCGGCAGCGTGCAGTGCCTGGCG
GTGCTCAGGGACAGGCTCTGTGTGGGCTACCCTTCTGGGTTCTGCCTGCTGAGCATCCAG
GGGGACGGGCAGCCTCTAAACCTGGTAAATCCCAATGACCCCTCGCTTGCGTTCCTCTCA
CAACAGTCTTTTGATGCCCTTTGTGCTGTGGAGCTCGAAAGCGAGGAGTACCTGCTTTGC
TTCAGCCACATGGGACTGTACGTGGACCCGCAAGGCCGGAGGGCACGCGCGCAGGAGCTC
ATGTGGCCTGCGGCTCCTGTCGCCTGTAGTTGCAGCCCCACCCACGTCACGGTGTACAGC
GAGTATGGCGTGGACGTCTTTGATGTGCGCACCATGGAGTGGGTGCAGACCATCGGCCTG
CGGAGGATAAGGCCCCTGAACTCTGAAGGCACCCTCAACCTCCTCAACTGCGAGCCTCCA
CGCTTGATCTACTTCAAGAGCAAGTTCTCGGGAGCGGTTCTCAACGTGCCGGACACCTCC
GACAACAGCAAGAAGCAGATGCTGCGCACCAGGAGCAAAAGGCGGTTCGTCTTCAAGGTC
CCAGAGGAAGAGAGACTGCAGCAGAGGCGAGAGATGCTTAGAGACCCAGAATTGAGATCC
AAAATGATATCCAACCCAACCAACTTCAACCACGTGGCCCACATGGGCCCAGGCGACGGC
ATGCAGGTGCTCATGGACCTGCCTCTGAGTGCTGTGCCCCCCTCCCAGGAGGAAAGGCCG
GGCCCCGCTCCCACCAACCTGGCTCGCCAGCCTCCATCCAGGAACAAGCCCTACATCTCG
TGGCCCTCATCAGGTGGATCGGAGCCTAGCGTGACTGTGCCTCTGAGAAGTATGTCTGAT
CCAGACCAGGACTTTGACAAAGAGCCTGATTCGGACTCCACCAAACACTCAACTCCATCG
AATAGCTCCAACCCCAGCGGCCCACCGAGCCCCAACTCCCCCCACAGGAGCCAGCTCCCC
CTCGAAGGCCTGGAGCAGCCGGCCTGTGACACCTGA
Enzyme 95 GenBank Gene ID NM_006035.3 Link Image
Enzyme 95 GeneCard ID CDC42BPB Link Image
Enzyme 95 GenAtlas ID CDC42BPB Link Image
Enzyme 95 HGNC ID HGNC:1738 Link Image
Enzyme 95 Chromosome Location 1
Enzyme 95 Locus 14q32.3
Enzyme 95 SNPs SNPJam Report Link Image
Enzyme 95 General References
  1. Moncrieff CL, Bailey ME, Morrison N, Johnson KJ: Cloning and chromosomal localization of human Cdc42-binding protein kinase beta. Genomics. 1999 Apr 15;57(2):297-300. [PubMed Link Image]
  2. 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]
  3. 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]
  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. 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]
  6. 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]
  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]
  8. 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]
  9. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 95 Metabolite References Not Available
Enzyme 96 [top]
Enzyme 96 ID 14199
Enzyme 96 Name Serine/threonine-protein kinase MRCK gamma
Enzyme 96 Synonyms
  1. CDC42-binding protein kinase gamma
  2. DMPK-like gamma
  3. Myotonic dystrophy kinase-related CDC42-binding kinase gamma
  4. MRCK gamma
  5. Myotonic dystrophy protein kinase-like gamma
  6. Myotonic dystrophy protein kinase-like alpha
Enzyme 96 Gene Name CDC42BPG
Enzyme 96 Protein Sequence >Serine/threonine-protein kinase MRCK gamma
MERRLRALEQLARGEAGGCPGLDGLLDLLLALHHELSSGPLRRERSVAQFLSWASPFVSK
VKELRLQRDDFEILKVIGRGAFGEVTVVRQRDTGQIFAMKMLHKWEMLKRAETACFREER
DVLVKGDSRWVTTLHYAFQDEEYLYLVMDYYAGGDLLTLLSRFEDRLPPELAQFYLAEMV
LAIHSLHQLGYVHRDVKPDNVLLDVNGHIRLADFGSCLRLNTNGMVDSSVAVGTPDYISP
EILQAMEEGKGHYGPQCDWWSLGVCAYELLFGETPFYAESLVETYGKIMNHEDHLQFPPD
VPDVPASAQDLIRQLLCRQEERLGRGGLDDFRNHPFFEGVDWERLASSTAPYIPELRGPM
DTSNFDVDDDTLNHPGTLPPPSHGAFSGHHLPFVGFTYTSGSHSPESSSEAWAALERKLQ
CLEQEKVELSRKHQEALHAPTDHRELEQLRKEVQTLRDRLPEMLRDKASLSQTDGPPAGS
PGQDSDLRQELDRLHRELAEGRAGLQAQEQELCRAQGQQEELLQRLQEAQEREAATASQT
RALSSQLEEARAAQRELEAQVSSLSRQVTQLQGQWEQRLEESSQAKTIHTASETNGMGPP
EGGPQEAQLRKEVAALREQLEQAHSHRPSGKEEALCQLQEENRRLSREQERLEAELAQEQ
ESKQRLEGERRETESNWEAQLADILSWVNDEKVSRGYLQALATKMAEELESLRNVGTQTL
PARPLDHQWKARRLQKMEASARLELQSALEAEIRAKQGLQERLTQVQEAQLQAERRLQEA
EKQSQALQQELAMLREELRARGPVDTKPSNSLIPFLSFRSSEKDSAKDPGISGEATRHGG
EPDLRPEGRRSLRMGAVFPRAPTANTASTEGLPAKPGSHTLRPRSFPSPTKCLRCTSLML
GLGRQGLGCDACGYFCHTTCAPQAPPCPVPPDLLRTALGVHPETGTGTAYEGFLSVPRPS
GVRRGWQRVFAALSDSRLLLFDAPDLRLSPPSGALLQVLDLRDPQFSATPVLASDVIHAQ
SRDLPRIFRVTTSQLAVPPTTCTVLLLAESEGERERWLQVLGELQRLLLDARPRPRPVYT
LKEAYDNGLPLLPHTLCAAILDQDRLALGTEEGLFVIHLRSNDIFQVGECRRVQQLTLSP
SAGLLVVLCGRGPSVRLFALAELENIEVAGAKIPESRGCQVLAAGSILQARTPVLCVAVK
RQVLCYQLGPGPGPWQRRIRELQAPATVQSLGLLGDRLCVGAAGGFALYPLLNEAAPLAL
GAGLVPEELPPSRGGLGEALGAVELSLSEFLLLFTTAGIYVDGAGRKSRGHELLWPAAPM
GWGYAAPYLTVFSENSIDVFDVRRAEWVQTVPLKKVRPLNPEGSLFLYGTEKVRLTYLRN
QLAEKDEFDIPDLTDNSRRQLFRTKSKRRFFFRVSEEQQKQQRREMLKDPFVRSKLISPP
TNFNHLVHVGPANGRPGARDKSPAPEEKGRVARGSGPQRPHSFSEALRRPASMGSEGLGG
DADPMKRKPWTSLSSESVSCPQGSLSPATSLMQVSERPRSLPLSPELESSP
Enzyme 96 Number of Residues 1551
Enzyme 96 Molecular Weight 172457.6
Enzyme 96 Theoretical pI 6.21
Enzyme 96 GO Classification
Function
  • ATP binding
  • GTPase regulator activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • enzyme regulator activity
  • kinase activity
  • nucleoside binding
  • nucleoside-triphosphatase regulator activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • small GTPase regulator activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 96 General Function Involved in protein serine/threonine kinase activity
Enzyme 96 Specific Function May act as a downstream effector of CDC42 in cytoskeletal reorganization. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation
Enzyme 96 Pathways
Enzyme 96 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 96 Pfam Domain Function
Enzyme 96 Signals
  • None
Enzyme 96 Transmembrane Regions
  • None
Enzyme 96 Essentiality Not Available
Enzyme 96 GenBank ID Protein 156766068 Link Image
Enzyme 96 UniProtKB/Swiss-Prot ID Q6DT37 Link Image
Enzyme 96 UniProtKB/Swiss-Prot Entry Name MRCKG_HUMAN Link Image
Enzyme 96 PDB ID Not Available
Enzyme 96 Cellular Location Not Available
Enzyme 96 Gene Sequence >4656 bp
ATGGAGCGGCGGCTGCGCGCGCTGGAGCAGCTGGCGCGGGGCGAGGCCGGCGGCTGCCCG
GGGCTCGACGGCCTCCTAGATCTGCTGCTGGCGCTGCACCACGAGCTCAGCAGCGGCCCC
CTACGGCGGGAGCGCAGCGTGGCGCAGTTCCTGAGCTGGGCCAGCCCCTTCGTATCAAAG
GTGAAAGAACTGCGTCTGCAGAGAGATGACTTTGAGATCTTGAAGGTGATCGGCCGAGGA
GCCTTTGGGGAGGTCACCGTGGTGAGGCAGAGGGACACTGGGCAGATTTTTGCCATGAAA
ATGCTGCACAAGTGGGAGATGCTGAAGAGGGCTGAGACAGCCTGTTTCCGGGAGGAGCGG
GATGTGCTCGTGAAAGGGGACAGCCGTTGGGTGACCACTCTGCACTATGCCTTCCAAGAC
GAGGAGTACCTGTACCTTGTGATGGACTACTATGCTGGTGGGGACCTCCTGACGCTGCTG
AGCCGCTTCGAGGACCGTCTCCCGCCCGAGCTGGCCCAGTTCTACCTGGCTGAGATGGTG
CTGGCCATCCACTCGCTGCACCAGCTGGGTTATGTCCACAGGGATGTCAAGCCAGACAAC
GTCCTGCTGGATGTGAACGGGCACATTCGCCTGGCTGACTTCGGCTCCTGCCTGCGTCTC
AACACCAACGGCATGGTGGATTCATCAGTGGCAGTAGGGACGCCGGACTATATCTCCCCT
GAGATCCTGCAGGCCATGGAGGAGGGCAAGGGCCACTACGGCCCACAGTGTGACTGGTGG
TCGCTTGGAGTCTGCGCCTATGAGCTGCTCTTTGGGGAGACGCCCTTCTATGCTGAGTCC
TTGGTGGAAACCTACGGCAAGATCATGAACCACGAGGACCACCTGCAGTTCCCCCCGGAC
GTGCCTGACGTGCCAGCCAGCGCCCAAGACCTGATCCGCCAGCTGCTGTGTCGCCAGGAA
GAGCGGCTAGGCCGTGGTGGGCTGGATGACTTCCGGAACCATCCTTTCTTCGAAGGCGTG
GACTGGGAGCGGCTGGCGAGCAGCACGGCCCCCTATATTCCTGAGCTGCGGGGGCCCATG
GACACCTCCAACTTTGATGTGGATGACGACACCCTCAACCATCCAGGGACCCTGCCACCG
CCCTCCCACGGGGCCTTCTCCGGCCATCACCTGCCATTCGTGGGCTTCACCTACACCTCA
GGCAGTCACAGTCCTGAGAGCAGCTCTGAGGCTTGGGCTGCCCTGGAGCGGAAGCTCCAG
TGTCTGGAGCAGGAGAAGGTGGAGCTGAGCAGGAAGCACCAAGAGGCCCTGCACGCCCCC
ACAGACCATCGGGAGCTGGAGCAGCTACGGAAGGAAGTGCAGACTCTGCGGGACAGGCTG
CCAGAGATGCTGAGGGACAAGGCCTCATTGTCCCAGACGGATGGGCCCCCAGCTGGTAGC
CCAGGTCAGGACAGTGACCTACGGCAGGAGCTTGACCGACTTCACCGGGAGCTGGCCGAG
GGTCGGGCAGGGCTGCAGGCTCAGGAGCAGGAGCTCTGCAGGGCCCAGGGGCAGCAGGAG
GAGCTGCTTCAGAGGCTACAGGAGGCCCAGGAGAGAGAGGCGGCCACAGCTAGCCAGACC
CGGGCCCTGAGCTCCCAGCTGGAGGAAGCCCGGGCTGCCCAGAGGGAGCTGGAGGCCCAG
GTGTCCTCCCTGAGCCGGCAGGTGACGCAGCTGCAGGGACAGTGGGAGCAACGCCTTGAG
GAGTCGTCCCAGGCCAAGACCATCCACACAGCCTCTGAGACCAACGGGATGGGACCCCCT
GAGGGTGGGCCTCAGGAGGCCCAACTGAGGAAGGAGGTGGCCGCCCTGCGAGAGCAGCTG
GAGCAGGCCCACAGCCACAGGCCGAGTGGTAAGGAGGAGGCTCTGTGCCAGCTGCAGGAG
GAAAACCGGAGGCTGAGCCGGGAGCAGGAGCGGCTAGAAGCAGAGCTGGCCCAGGAGCAG
GAGAGCAAGCAGCGGCTGGAGGGTGAGCGGCGGGAGACGGAGAGCAACTGGGAGGCCCAG
CTCGCCGACATCCTCAGCTGGGTGAATGATGAGAAGGTCTCAAGAGGCTACCTGCAGGCC
CTGGCCACCAAGATGGCAGAGGAGCTGGAGTCCTTGAGGAACGTAGGCACCCAGACGCTC
CCTGCCCGGCCACTGGACCACCAGTGGAAGGCGCGGCGACTGCAGAAGATGGAGGCCTCG
GCCAGGCTGGAGCTGCAGTCAGCGCTGGAGGCCGAGATCCGCGCCAAGCAGGGCCTGCAG
GAGCGGCTGACACAGGTGCAGGAGGCCCAGCTGCAGGCTGAGCGCCGTCTGCAGGAGGCC
GAGAAGCAGAGCCAGGCCCTGCAACAGGAGCTCGCCATGCTGCGGGAGGAGCTGCGGGCC
CGAGGGCCAGTGGACACCAAGCCCTCAAACTCCCTGATTCCCTTCCTGTCCTTCCGGAGC
TCAGAGAAGGATTCTGCCAAGGACCCTGGCATCTCAGGAGAGGCCACAAGGCATGGAGGA
GAGCCAGATCTGAGGCCGGAGGGCCGACGCAGCCTGCGCATGGGGGCTGTGTTCCCCAGA
GCACCCACTGCCAACACAGCCTCTACAGAAGGTCTTCCTGCTAAGCCCGGCTCACACACG
CTGCGCCCCCGGAGCTTCCCATCCCCGACCAAGTGTCTCCGCTGCACCTCGCTGATGCTG
GGCCTGGGCCGCCAGGGCCTGGGTTGTGATGCCTGCGGCTACTTTTGTCACACAACCTGT
GCCCCACAGGCCCCACCCTGCCCCGTGCCCCCTGACCTCCTCCGCACAGCCCTGGGAGTA
CACCCCGAAACAGGCACAGGCACTGCCTATGAGGGCTTTCTGTCGGTGCCGCGGCCCTCA
GGTGTCCGGCGGGGCTGGCAGCGCGTGTTTGCTGCCCTGAGTGACTCACGCCTGCTGCTG
TTTGACGCCCCTGACCTGAGGCTCAGCCCGCCCAGTGGGGCCCTCCTGCAGGTCCTAGAT
CTGAGGGACCCCCAGTTCTCGGCTACCCCTGTCCTGGCCTCTGATGTTATCCATGCCCAA
TCCAGGGACCTGCCACGCATCTTTAGGGTGACAACCTCCCAGCTGGCAGTGCCGCCCACC
ACGTGCACTGTGCTGCTGCTGGCAGAGAGCGAGGGGGAGCGGGAACGCTGGCTGCAGGTG
CTGGGTGAGCTGCAGCGGCTGCTGCTGGACGCGCGGCCAAGACCCCGGCCCGTGTACACA
CTCAAGGAGGCTTACGACAACGGGCTGCCGCTGCTGCCTCACACGCTCTGCGCTGCCATC
CTCGACCAGGATCGACTTGCGCTTGGCACCGAGGAGGGGCTCTTTGTCATCCATCTGCGC
AGCAACGACATCTTCCAGGTGGGGGAGTGCCGGCGCGTGCAGCAGCTGACCTTGAGCCCC
AGTGCAGGCCTGCTGGTCGTGCTGTGTGGCCGCGGCCCCAGCGTGCGTCTCTTTGCCCTG
GCGGAGCTGGAGAACATAGAGGTAGCAGGTGCCAAGATCCCCGAGTCTCGAGGCTGCCAG
GTGCTGGCAGCTGGAAGCATCCTGCAGGCCCGCACCCCGGTGCTCTGTGTAGCCGTCAAG
CGCCAGGTGCTCTGCTACCAGCTGGGCCCGGGCCCTGGGCCCTGGCAGCGCCGCATCCGT
GAGCTGCAGGCACCTGCCACTGTGCAGAGCCTGGGGCTGCTGGGCGACCGGCTATGTGTG
GGCGCCGCCGGTGGCTTTGCACTCTACCCGCTGCTCAACGAGGCTGCGCCGTTGGCGCTG
GGGGCCGGTTTGGTGCCTGAGGAGCTGCCACCATCCCGCGGGGGCCTGGGTGAGGCACTG
GGTGCCGTGGAGCTTAGCCTCAGCGAGTTCCTGCTACTCTTCACCACTGCTGGCATCTAC
GTGGATGGCGCAGGCCGCAAGTCTCGTGGCCACGAGCTGTTGTGGCCAGCAGCGCCCATG
GGCTGGGGGTATGCGGCCCCCTACCTGACAGTGTTCAGCGAGAACTCCATCGATGTGTTT
GACGTGAGGAGGGCAGAATGGGTGCAGACCGTGCCGCTCAAGAAGGTGCGGCCCCTCAAT
CCAGAGGGCTCCCTGTTCCTCTACGGCACCGAGAAGGTCCGCCTGACCTACCTCAGGAAC
CAGCTGGCAGAGAAGGACGAGTTCGACATCCCGGACCTCACCGACAACAGCCGGCGCCAG
CTGTTCCGCACCAAGAGCAAGCGCCGCTTCTTTTTCCGCGTGTCGGAGGAGCAGCAGAAG
CAGCAGCGCAGGGAGATGCTGAAGGACCCTTTTGTGCGCTCCAAGCTCATCTCGCCGCCT
ACCAACTTCAACCACCTAGTACACGTGGGCCCTGCCAACGGGCGGCCCGGCGCCAGGGAC
AAGTCCCCGGCTCCCGAAGAGAAGGGCCGAGTTGCCCGCGGCTCCGGCCCACAGCGGCCC
CACAGCTTCTCCGAGGCGTTGCGGCGCCCAGCCTCCATGGGCAGCGAAGGCCTCGGTGGA
GACGCAGACCCCATGAAGAGGAAACCCTGGACATCCCTGTCCAGCGAGTCTGTGTCCTGC
CCCCAGGGATCGCTGAGCCCTGCAACCTCCCTAATGCAGGTCTCAGAACGGCCCCGAAGC
CTCCCCCTATCCCCTGAATTGGAGAGCTCTCCTTGA
Enzyme 96 GenBank Gene ID NM_017525.2 Link Image
Enzyme 96 GeneCard ID CDC42BPG Link Image
Enzyme 96 GenAtlas ID CDC42BPG Link Image
Enzyme 96 HGNC ID HGNC:29829 Link Image
Enzyme 96 Chromosome Location 1
Enzyme 96 Locus 11q13.1
Enzyme 96 SNPs SNPJam Report Link Image
Enzyme 96 General References
  1. Ng Y, Tan I, Lim L, Leung T: Expression of the human myotonic dystrophy kinase-related Cdc42-binding kinase gamma is regulated by promoter DNA methylation and Sp1 binding. J Biol Chem. 2004 Aug 13;279(33):34156-64. Epub 2004 Jun 11. [PubMed Link Image]
  2. 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]
  3. Kedra D, Seroussi E, Fransson I, Trifunovic J, Clark M, Lagercrantz J, Blennow E, Mehlin H, Dumanski J: The germinal center kinase gene and a novel CDC25-like gene are located in the vicinity of the PYGM gene on 11q13. Hum Genet. 1997 Oct;100(5-6):611-9. [PubMed Link Image]
  4. 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]
  5. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 96 Metabolite References Not Available
Enzyme 97 [top]
Enzyme 97 ID 14330
Enzyme 97 Name Guanine nucleotide exchange factor VAV3
Enzyme 97 Synonyms
  1. VAV-3
Enzyme 97 Gene Name VAV3
Enzyme 97 Protein Sequence >Guanine nucleotide exchange factor VAV3
MEPWKQCAQWLIHCKVLPTNHRVTWDSAQVFDLAQTLRDGVLLCQLLNNLRAHSINLKEI
NLRPQMSQFLCLKNIRTFLTACCETFGMRKSELFEAFDLFDVRDFGKVIETLSRLSRTPI
ALATGIRPFPTEESINDEDIYKGLPDLIDETLVEDEEDLYDCVYGEDEGGEVYEDLMKAE
EAHQPKCPENDIRSCCLAEIKQTEEKYTETLESIEKYFMAPLKRFLTAAEFDSVFINIPE
LVKLHRNLMQEIHDSIVNKNDQNLYQVFINYKERLVIYGQYCSGVESAISSLDYISKTKE
DVKLKLEECSKRANNGKFTLRDLLVVPMQRVLKYHLLLQELVKHTTDPTEKANLKLALDA
MKDLAQYVNEVKRDNETLREIKQFQLSIENLNQPVLLFGRPQGDGEIRITTLDKHTKQER
HIFLFDLAVIVCKRKGDNYEMKEIIDLQQYKIANNPTTDKENKKWSYGFYLIHTQGQNGL
EFYCKTKDLKKKWLEQFEMALSNIRPDYADSNFHDFKMHTFTRVTSCKVCQMLLRGTFYQ
GYLCFKCGARAHKECLGRVDNCGRVNSGEQGTLKLPEKRTNGLRRTPKQVDPGLPKMQVI
RNYSGTPPPALHEGPPLQLQAGDTVELLKGDAHSLFWQGRNLASGEVGFFPSDAVKPCPC
VPKPVDYSCQPWYAGAMERLQAETELINRVNSTYLVRHRTKESGEYAISIKYNNEAKHIK
ILTRDGFFHIAENRKFKSLMELVEYYKHHSLKEGFRTLDTTLQFPYKEPEHSAGQRGNRA
GNSLLSPKVLGIAIARYDFCARDMRELSLLKGDVVKIYTKMSANGWWRGEVNGRVGWFPS
TYVEEDE
Enzyme 97 Number of Residues 847
Enzyme 97 Molecular Weight 97775.1
Enzyme 97 Theoretical pI 7.06
Enzyme 97 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 97 General Function Involved in Rho guanyl-nucleotide exchange factor activity
Enzyme 97 Specific Function Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those GTPases. Plays an important role in angiogenesis. Its recruitement by phosphorylated EPHA2 is critical for EFNA1- induced RAC1 GTPase activation and vascular endothelial cell migration and assembly
Enzyme 97 Pathways Not Available
Enzyme 97 Reactions Not Available
Enzyme 97 Pfam Domain Function
Enzyme 97 Signals
  • None
Enzyme 97 Transmembrane Regions
  • None
Enzyme 97 Essentiality Not Available
Enzyme 97 GenBank ID Protein 3928847 Link Image
Enzyme 97 UniProtKB/Swiss-Prot ID Q9UKW4 Link Image
Enzyme 97 UniProtKB/Swiss-Prot Entry Name VAV3_HUMAN Link Image
Enzyme 97 PDB ID Not Available
Enzyme 97 Cellular Location Not Available
Enzyme 97 Gene Sequence >2544 bp
ATGGAGCCGTGGAAGCAGTGCGCGCAGTGGCTCATCCATTGCAAGGTGCTGCCCACCAAC
CACCGGGTGACCTGGGACTCGGCTCAGGTGTTCGACCTTGCGCAGACCCTCCGCGATGGA
GTCCTGCTCTGCCAGCTGCTTAACAACCTCCGGGCGCACTCCATCAACCTGAAGGAGATC
AACCTGAGGCCGCAGATGTCCCAGTTTCTCTGTTTGAAGAACATAAGGACATTTCTCACG
GCCTGTTGTGAGACGTTTGGAATGAGGAAAAGTGAACTTTTCGAGGCATTTGACTTGTTT
GATGTTCGTGACTTTGGAGAGGTTATAGAAACATTATCACGACTTTCTCGAACACCTATA
GCATTGGCCACAGGAATCAGGCCCTTCCCAACAGAAGAAAGCATTAATGATGAAGACATC
TACAAAGGCCTTCCTGATTTAATAGATGAAACCCTTGTGGAAGATGAAGAAGATCTCTAT
GACTGTGTTTATGGGGAAGATGAAGGTGGAGAAGTCTATGAGGACTTAATGAAGGCAGAG
GAAGCACATCAGCCCAAATGTCCAGAAAATGATATACGAAGTTGTTGTCTAGCAGAAATT
AAGCAGACAGAAGAAAAATATACAGAAACTTTGGAGTCAATAGAAAAATATTTCATGGCA
CCACTAAAAAGATTTCTGACAGCAGCAGAATTTGATTCAGTATTCATCAACATTCCTGAA
CTTGTAAAACTTCATCGGAACCTAATGCAAGAGATTCATGATTCCATTGTAAATAAAAAT
GACCAGAACTTGTACCAAGTTTTTATTAACTACAAGGAAAGATTGGTTATTTACGGGCAG
TACTGCAGTGGAGTGGAGTCAGCCATCTCTAGTTTAGACTACATTTCTAAGTCAAAAGAA
GATGTCAAACTGAAATTAGAGGAATGTTCCAAAAGAGCAAATAATGGGAAATTTACTCTT
CGAGACTTGCTTGTGGTTCCTATGCAACGTGTTTTAAAGTACCACCTTCTCCTCCAGGAA
CTGGTCAAACATACCACTGATCCGACTGAGAAGGCAAATCTGAAACTGGCTCTTGATGCC
ATGAAGGACTTGGCACAATATGTGAATGAAGTGAAAAGAGATAATGAGACCCTTCGTGAA
ATTAAACAGTTTCAGCTATCTATAGAGAATTTGAACCAACCAGTTTTGCTTTTTGGACGA
CCTCAGGGAGATGGTGAAATTCGAATAACCACTCTAGACAAGCATACCAAACAAGAAAGG
CATATCTTCTTATTTGATTTGGCAGTGATCGTATGTAAGAGAAAAGGTGATAACTATGAA
ATGAAGGAAATAATAGATCTTCAGCAGTACAAGATAGCCAATAATCCTACAACCGATAAA
GAAAACAAAAAGTGGTCTTATGGCTTCTACCTCATCCATACCCAAGGACAAAATGGGTTA
GAATTTTATTGCAAAACAAAAGATTTAAAGAAGAAATGGCTAGAACAGTTTGAAATGGCT
TTGTCTAACATAAGACCAGACTATGCAGACTCCAATTTCCACGACTTCAAGATGCATACC
TTCACTCGAGTCACATCCTGCAAAGTCTGCCAGATGCTCCTGAGGGGAACATTTTATCAA
GGCTATTTATGTTTTAAGTGTGGAGCGAGAGCACACAAAGAATGTTTGGGAAGAGTAGAC
AATTGTGGCAGAGTTAATTCTGGTGAACAAGGGACACTCAAACTACCAGAGAAACGGACC
AATGGACTGCGAAGAACTCCTAAACAGGTGGATCCAGGTTTACCAAAGATGCAGGTCATT
AGGAACTATTCTGGAACACCACCCCCAGCTCTGCATGAAGGACCCCCTTTACAGCTCCAG
GCCGGGGATACCGTTGAACTTCTGAAAGGAGATGCACACAGTCTGTTTTGGCAGGGCAGA
AATTTAGCATCTGGAGAGGTTGGATTTTTTCCAAGTGATGCAGTCAAGCCTTGCCCATGT
GTGCCCAAACCAGTAGATTATTCTTGCCAACCCTGGTATGCTGGAGCAATGGAAAGATTG
CAAGCAGAGACCGAACTTATTAATAGGGTAAATAGTACTTACCTTGTGAGGCACAGGACC
AAAGAGTCAGGAGAATATGCAATTAGCATTAAGTACAATAATGAAGCAAAGCACATCAAG
ATTTTAACAAGAGATGGCTTTTTTCACATTGCAGAAAATAGAAAATTTAAAAGTTTAATG
GAACTTGTGGAGTACTACAAGCATCATTCTCTCAAGGAAGGGTTCAGAACCTTAGATACA
ACTCTGCAGTTTCCATACAAGGAGCCAGAACATTCAGCTGGACAGAGGGGTAATAGAGCA
GGCAACAGCTTGTTAAGTCCAAAAGTGCTGGGCATTGCCATCGCTCGGTATGACTTCTGT
GCAAGAGATATGAGAGAGTTGTCCTTGTTGAAAGGAGATGTGGTGAAGATTTACACAAAG
ATGAGTGCAAATGGCTGGTGGAGAGGAGAAGTAAATGGCAGGGTGGGCTGGTTTCCATCC
ACATATGTGGAAGAGGATGAATAA
Enzyme 97 GenBank Gene ID AF067817 Link Image
Enzyme 97 GeneCard ID VAV3 Link Image
Enzyme 97 GenAtlas ID VAV3 Link Image
Enzyme 97 HGNC ID HGNC:12659 Link Image
Enzyme 97 Chromosome Location 1
Enzyme 97 Locus 1p13.3
Enzyme 97 SNPs SNPJam Report Link Image
Enzyme 97 General References
  1. Movilla N, Bustelo XR: Biological and regulatory properties of Vav-3, a new member of the Vav family of oncoproteins. Mol Cell Biol. 1999 Nov;19(11):7870-85. [PubMed Link Image]
  2. Trenkle T, Welsh J, Jung B, Mathieu-Daude F, McClelland M: Non-stoichiometric reduced complexity probes for cDNA arrays. Nucleic Acids Res. 1998 Sep 1;26(17):3883-91. [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. Yabana N, Shibuya M: Adaptor protein APS binds the NH2-terminal autoinhibitory domain of guanine nucleotide exchange factor Vav3 and augments its activity. Oncogene. 2002 Oct 31;21(50):7720-9. [PubMed Link Image]
  5. Hunter SG, Zhuang G, Brantley-Sieders D, Swat W, Cowan CW, Chen J: Essential role of Vav family guanine nucleotide exchange factors in EphA receptor-mediated angiogenesis. Mol Cell Biol. 2006 Jul;26(13):4830-42. [PubMed Link Image]
  6. 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 97 Metabolite References Not Available
Enzyme 98 [top]
Enzyme 98 ID 14426
Enzyme 98 Name Acylglycerol kinase, mitochondrial
Enzyme 98 Synonyms
  1. hAGK
  2. Multiple substrate lipid kinase
  3. HsMuLK
  4. MuLK
  5. Multi-substrate lipid kinase
Enzyme 98 Gene Name AGK
Enzyme 98 Protein Sequence >Acylglycerol kinase, mitochondrial
MTVFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQV
KKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTIVKTDYEGQAKKLLELMENTDVII
VAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATL
AIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFST
LKEWPQTHQASISYTGPTERPPNEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSP
EVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHV
EGTECLQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSP
TQ
Enzyme 98 Number of Residues 422
Enzyme 98 Molecular Weight 47136.8
Enzyme 98 Theoretical pI 8.21
Enzyme 98 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 98 General Function Involved in NAD+ kinase activity
Enzyme 98 Specific Function Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively. Does not phosphorylate sphingosine. Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth
Enzyme 98 Pathways
Enzyme 98 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 98 Pfam Domain Function
Enzyme 98 Signals
  • None
Enzyme 98 Transmembrane Regions
  • None
Enzyme 98 Essentiality Not Available
Enzyme 98 GenBank ID Protein 8922701 Link Image
Enzyme 98 UniProtKB/Swiss-Prot ID Q53H12 Link Image
Enzyme 98 UniProtKB/Swiss-Prot Entry Name AGK_HUMAN Link Image
Enzyme 98 PDB ID Not Available
Enzyme 98 Cellular Location Not Available
Enzyme 98 Gene Sequence >1269 bp
ATGACGGTGTTCTTTAAAACGCTTCGAAATCACTGGAAGAAAACTACAGCTGGGCTCTGC
CTGCTGACCTGGGGAGGCCATTGGCTCTATGGAAAACACTGTGATAACCTCCTAAGGAGA
GCAGCCTGTCAAGAAGCTCAGGTGTTTGGCAATCAACTCATTCCTCCCAATGCACAAGTG
AAGAAGGCCACTGTTTTTCTCAATCCTGCAGCTTGCAAAGGAAAAGCCAGGACTCTATTT
GAAAAAAATGCTGCCCCGATTTTACATTTATCTGGCATGGATGTGACTATTGTTAAGACA
GATTATGAGGGACAAGCCAAGAAACTCCTGGAACTGATGGAAAACACGGATGTGATCATT
GTTGCAGGAGGAGATGGGACACTGCAGGAGGTTGTTACTGGTGTTCTTCGACGAACAGAT
GAGGCTACCTTCAGTAAGATTCCCATTGGATTTATCCCACTGGGAGAGACCAGTAGTTTG
AGTCATACCCTCTTTGCCGAAAGTGGAAACAAAGTCCAACATATTACTGATGCCACACTT
GCCATTGTGAAAGGAGAGACAGTTCCACTTGATGTCTTGCAGATCAAGGGTGAAAAGGAA
CAGCCTGTATTTGCAATGACCGGCCTTCGATGGGGATCTTTCAGAGATGCTGGCGTCAAA
GTTAGCAAGTACTGGTATCTTGGGCCTCTAAAAATCAAAGCAGCCCACTTTTTCAGCACT
CTTAAGGAGTGGCCTCAGACTCATCAAGCCTCTATCTCATACACGGGACCTACAGAGAGA
CCTCCCAATGAACCAGAGGAGACCCCTGTACAAAGGCCTTCTTTGTACAGGAGAATATTA
CGAAGGCTTGCGTCCTACTGGGCACAACCACAGGATGCCCTTTCCCAAGAGGTGAGCCCG
GAGGTCTGGAAAGATGTGCAGCTGTCCACCATTGAACTGTCCATCACAACACGGAATAAT
CAGCTTGACCCGACAAGCAAAGAAGATTTTCTGAATATCTGCATTGAACCTGACACCATC
AGCAAAGGAGACTTTATAACTATAGGAAGTCGAAAGGTGAGAAACCCCAAGCTGCACGTG
GAGGGCACGGAGTGTCTCCAAGCCAGCCAGTGCACTTTGCTTATCCCGGAGGGAGCAGGG
GGCTCTTTTAGCATTGACAGTGAGGAGTATGAAGCGATGCCTGTGGAGGTGAAACTGCTC
CCCAGGAAGCTGCAGTTCTTCTGTGATCCTAGGAAGAGAGAACAGATGCTCACAAGCCCC
ACCCAGTGA
Enzyme 98 GenBank Gene ID NM_018238.3 Link Image
Enzyme 98 GeneCard ID AGK Link Image
Enzyme 98 GenAtlas ID AGK Link Image
Enzyme 98 HGNC ID HGNC:21869 Link Image
Enzyme 98 Chromosome Location 7
Enzyme 98 Locus 7q34
Enzyme 98 SNPs SNPJam Report Link Image
Enzyme 98 General References
  1. Van Overloop H, Gijsbers S, Van Veldhoven PP: Further characterization of mammalian ceramide kinase: substrate delivery and (stereo)specificity, tissue distribution, and subcellular localization studies. J Lipid Res. 2006 Feb;47(2):268-83. Epub 2005 Nov 3. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Bektas M, Payne SG, Liu H, Goparaju S, Milstien S, Spiegel S: A novel acylglycerol kinase that produces lysophosphatidic acid modulates cross talk with EGFR in prostate cancer cells. J Cell Biol. 2005 Jun 6;169(5):801-11. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 98 Metabolite References Not Available
Enzyme 99 [top]
Enzyme 99 ID 16608
Enzyme 99 Name Protein kinase C, epsilon (Protein kinase C, epsilon, isoform CRA_b)
Enzyme 99 Synonyms Not Available
Enzyme 99 Gene Name PRKCE
Enzyme 99 Protein Sequence >Protein kinase C, epsilon (Protein kinase C, epsilon, isoform CRA_b)
MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKT
NSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLE
PEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQP
TYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVN
MPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIA
KVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELE
NNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFG
KVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKD
RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL
DAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEM
MAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGED
AIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQI
NQEEFKGFSYFGEDLMP
Enzyme 99 Number of Residues 737
Enzyme 99 Molecular Weight 83675
Enzyme 99 Theoretical pI 7.13
Enzyme 99 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid phosphorylation
  • protein modification
  • signal transduction
Component
Enzyme 99 General Function Not Available
Enzyme 99 Specific Function ATP + a protein = ADP + a phosphoprotein
Enzyme 99 Pathways Not Available
Enzyme 99 Reactions Not Available
Enzyme 99 Pfam Domain Function
Enzyme 99 Signals
  • None
Enzyme 99 Transmembrane Regions
  • None
Enzyme 99 Essentiality Not Available
Enzyme 99 GenBank ID Protein Not Available
Enzyme 99 UniProtKB/Swiss-Prot ID B0LPH7 Link Image
Enzyme 99 UniProtKB/Swiss-Prot Entry Name B0LPH7_HUMAN Link Image
Enzyme 99 PDB ID Not Available
Enzyme 99 Cellular Location Not Available
Enzyme 99 Gene Sequence Not Available
Enzyme 99 GenBank Gene ID EU332867 Link Image
Enzyme 99 GeneCard ID B0LPH7 Link Image
Enzyme 99 GenAtlas ID Not Available
Enzyme 99 HGNC ID Not Available
Enzyme 99 Chromosome Location Not Available
Enzyme 99 Locus Not Available
Enzyme 99 SNPs SNPJam Report Link Image
Enzyme 99 General References Not Available
Enzyme 99 Metabolite References Not Available
Enzyme 100 [top]
Enzyme 100 ID 17240
Enzyme 100 Name Pancreatic lipase-related protein 3
Enzyme 100 Synonyms
  1. PL-RP3
Enzyme 100 Gene Name PNLIPRP3
Enzyme 100 Protein Sequence >Pancreatic lipase-related protein 3
MLGIWIVAFLFFGTSRGKEVCYERLGCFKDGLPWTRTFSTELVGLPWSPEKINTRFLLYT
IHNPNAYQEISAVNSSTIQASYFGTDKITRINIAGWKTDGKWQRDMCNVLLQLEDINCIN
LDWINGSREYIHAVNNLRVVGAEVAYFIDVLMKKFEYSPSKVHLIGHSLGAHLAGEAGSR
IPGLGRITGLDPAGPFFHNTPKEVRLDPSDANFVDVIHTNAARILFELGVGTIDACGHLD
FYPNGGKHMPGCEDLITPLLKFNFNAYKKEMASFFDCNHARSYQFYAESILNPDAFIAYP
CRSYTSFKAGNCFFCSKEGCPTMGHFADRFHFKNMKTNGSHYFLNTGSLSPFARWRHKLS
VKLSGSEVTQGTVFLRVGGAVRKTGEFAIVSGKLEPGMTYTKLIDADVNVGNITSVQFIW
KKHLFEDSQNKLGAEMVINTSGKYGYKSTFCSQDIMGPNILQNLKPC
Enzyme 100 Number of Residues 467
Enzyme 100 Molecular Weight 52253.4
Enzyme 100 Theoretical pI 8.36
Enzyme 100 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • triglyceride lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 100 General Function Involved in catalytic activity
Enzyme 100 Specific Function Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Enzyme 100 Pathways Not Available
Enzyme 100 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 100 Pfam Domain Function
Enzyme 100 Signals
  • 1-17
Enzyme 100 Transmembrane Regions
  • None
Enzyme 100 Essentiality Not Available
Enzyme 100 GenBank ID Protein 190341077 Link Image
Enzyme 100 UniProtKB/Swiss-Prot ID Q17RR3 Link Image
Enzyme 100 UniProtKB/Swiss-Prot Entry Name LIPR3_HUMAN Link Image
Enzyme 100 PDB ID Not Available
Enzyme 100 Cellular Location Not Available
Enzyme 100 Gene Sequence >1404 bp
ATGCTTGGAATTTGGATTGTTGCATTCTTGTTCTTTGGCACATCAAGAGGAAAAGAAGTT
TGCTATGAAAGGTTAGGGTGTTTCAAAGATGGTTTACCATGGACCAGGACTTTCTCAACA
GAGTTGGTAGGTTTACCCTGGTCTCCAGAGAAGATAAACACTCGTTTCCTGCTCTACACT
ATACACAATCCCAATGCCTATCAGGAGATCAGTGCGGTTAATTCTTCAACTATCCAAGCC
TCATATTTTGGAACAGACAAGATCACCCGTATCAACATAGCTGGATGGAAAACAGATGGC
AAATGGCAGAGAGACATGTGCAATGTGTTGCTACAGCTGGAAGATATAAATTGCATTAAT
TTAGATTGGATCAACGGTTCACGGGAATACATCCATGCTGTAAACAATCTCCGTGTTGTT
GGTGCTGAGGTGGCTTATTTTATTGATGTTCTCATGAAAAAATTTGAATATTCCCCTTCT
AAAGTGCACTTGATTGGCCACAGCTTGGGAGCACACCTGGCTGGGGAAGCTGGGTCAAGG
ATACCAGGCCTTGGAAGAATAACTGGGTTGGACCCAGCTGGGCCATTTTTCCACAACACT
CCAAAGGAAGTCAGGCTAGACCCCTCGGATGCCAACTTTGTTGACGTTATTCATACAAAT
GCAGCTCGCATCCTCTTTGAGCTTGGTGTTGGAACCATTGATGCTTGTGGTCATCTTGAC
TTTTACCCAAATGGAGGGAAGCACATGCCAGGATGTGAAGACTTAATTACACCTTTACTG
AAATTTAACTTCAATGCTTACAAAAAAGAAATGGCTTCCTTCTTTGACTGTAACCATGCC
CGAAGTTATCAATTTTATGCTGAAAGCATTCTTAATCCTGATGCATTTATTGCTTATCCT
TGTAGATCCTACACATCTTTTAAAGCAGGAAATTGCTTCTTTTGTTCCAAAGAAGGTTGC
CCAACAATGGGTCATTTTGCTGATAGATTTCACTTCAAAAATATGAAGACTAATGGATCA
CATTATTTTTTAAACACAGGGTCCCTTTCCCCATTTGCCCGTTGGAGGCACAAATTGTCT
GTTAAACTCAGTGGAAGCGAAGTCACTCAAGGAACTGTCTTTCTTCGTGTAGGCGGGGCA
GTTAGGAAAACTGGGGAGTTTGCCATTGTCAGTGGAAAACTTGAGCCAGGCATGACTTAC
ACAAAATTAATCGATGCAGATGTTAACGTTGGAAACATTACAAGTGTTCAGTTCATCTGG
AAAAAACATTTGTTTGAAGATTCTCAGAATAAGTTGGGAGCAGAAATGGTGATAAATACA
TCTGGGAAATATGGATATAAATCTACCTTCTGTAGCCAAGACATTATGGGACCTAATATT
CTCCAGAACCTGAAACCATGCTAA
Enzyme 100 GenBank Gene ID NM_001011709.2 Link Image
Enzyme 100 GeneCard ID PNLIPRP3 Link Image
Enzyme 100 GenAtlas ID PNLIPRP3 Link Image
Enzyme 100 HGNC ID HGNC:23492 Link Image
Enzyme 100 Chromosome Location 1
Enzyme 100 Locus 10q25.3
Enzyme 100 SNPs SNPJam Report Link Image
Enzyme 100 General References
  1. 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]
  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. Saelee P, Wongkham S, Puapairoj A, Khuntikeo N, Petmitr S, Chariyalertsak S, Sumethchotimaytha W, Karalak A: Novel PNLIPRP3 and DOCK8 gene expression and prognostic implications of DNA loss on chromosome 10q25.3 in hepatocellular carcinoma. Asian Pac J Cancer Prev. 2009 Jul-Sep;10(3):501-6. [PubMed Link Image]
Enzyme 100 Metabolite References Not Available
Enzyme 101 [top]
Enzyme 101 ID 17241
Enzyme 101 Name CDC42 binding protein kinase beta (DMPK-like)
Enzyme 101 Synonyms Not Available
Enzyme 101 Gene Name CDC42BPB
Enzyme 101 Protein Sequence >CDC42 binding protein kinase beta (DMPK-like)
MSAKVRLKKLEQLLLDGPWRNESALSVETLLDVLVCLYTECSHSALRRDKYVAEFLEWAK
PFTQLVKEMQLHREDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETAC
FREERDVLVNGDCQWITALHYAFQDENHLYLVMDYYVGGDLLTLLSKFEDKLPEDMARFY
IGEMVLAIDSIHQLHYVHRDIKPDNVLLDVNGHIRLADFGSCLKMNDDGTVQSSVAVGTP
DYISPEILQAMEDGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERF
QFPSHVTDVSEEAKDLIQRLICSRERRLGQNGIEDFKKHAFFEGLNWENIRNLEAPYIPD
VSSPSDTSNFDVDDDVLRNTEILPPGSHTGFSGLHLPFIGFTFTTESCFSDRGSLKSIMQ
SNTLTKDEDVQRDLEHSLQMEAYERRIRRLEQEKLELSRKLQESTQTVQSLHGSSRALSN
SNRDKEIKKLNEEIERLKNKIADSNRLERQLEDTVALRQEREDSTQRLRGLEKQHRVVRQ
EKEELHKQLVEASERLKSQAKELKDAHQQRKLALQEFSELNERMAELRAQKQKVSRQLRD
KEEEMEVATQKVDAMRQEMRRAEKLRKELEAQLDDAVAEASKERKLREHSENFCKQMESE
LEALKVKQGGRGAGATLEHQQEISKIKSELEKKVLFYEEELVRREASHVLEVKNVKKEVH
DSESHQLALQKEILMLKDKLEKSKRERHNEMEEAVGTIKDKYERERAMLFDENKKLTAEN
EKLCSFVDKLTAQNRQLEDELQDLAAKKESVAHWEAQIAEIIQWVSDEKDARGYLQALAS
KMTEELEALRSSSLGSRTLDPLWKVRRSQKLDMSARLELQSALEAEIRAKQLVQEELRKV
KDANLTLESKLKDSEAKNRELLEEMEILKKKMEEKFRADTGLKLPDFQDSIFEYFNTAPL
AHDLTFRTSSASEQETQAPKPEASPSMSVAASEQQEDMARPPQRPSAVPLPTTQALALAG
PKPKAHQFSIKSFSSPTQCSHCTSLMVGLIRQGYACEVCSFACHVSCKDGAPQVCPIPPE
QSKRPLGVDVQRGIGTAYKGHVKVPKPTGVKKGWQRAYAVVCDCKLFLYDLPEGKSTQPG
VIASQVLDLRDDEFSVSSVLASDVIHATRRDIPCIFRVTASLLGAPSKTSSLLILTENEN
EKKKWVGILEGLQSILHKNRLRNQVVHVPLEAYDSSLPLIKAILTAAIVDADRIAVGLEE
GLYVIEVTRDVIVRAADCKKVHQIELAPREKIVILLCGRNHHVHLYPWSSLDGAEGSFDI
KLPETKGCQLMATATLKRNSGTCLFVAVKRLILCYEIQRTKPFHRKFNEIVAPGSVQCLA
VLRDRLCVGYPSGFCLLSIQGDGQPLNLVNPNDPSLAFLSQQSFDALCAVELESEEYLLC
FSHMGLYVDPQGRRARAQELMWPAAPVACSCSPTHVTVYSEYGVDVFDVRTMEWVQTIGL
RRIRPLNSEGTLNLLNCEPPRLIYFKSKFSGAVLNVPDTSDNSKKQMLRTRSKRRFVFKV
PEEERLQQRREMLRDPELRSKMISNPTNFNHVAHMGPGDGMQVLMDLPLSAVPPSQEERP
GPAPTNLARQPPSRNKPYISWPSSGGSEPSVTVPLRSMSDPDQDFDKEPDSDSTKHSTPS
NSSNPSGPPSPNSPHRSQLPLEGLEQPACDT
Enzyme 101 Number of Residues 1711
Enzyme 101 Molecular Weight 194285.5
Enzyme 101 Theoretical pI 6.31
Enzyme 101 GO Classification
Function
  • ATP binding
  • GTPase regulator activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • enzyme regulator activity
  • kinase activity
  • nucleoside binding
  • nucleoside-triphosphatase regulator activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • small GTPase regulator activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 101 General Function Involved in protein serine/threonine kinase activity
Enzyme 101 Specific Function ATP + a protein = ADP + a phosphoprotein
Enzyme 101 Pathways Not Available
Enzyme 101 Reactions Not Available
Enzyme 101 Pfam Domain Function
Enzyme 101 Signals
  • None
Enzyme 101 Transmembrane Regions
  • None
Enzyme 101 Essentiality Not Available
Enzyme 101 GenBank ID Protein 161611364 Link Image
Enzyme 101 UniProtKB/Swiss-Prot ID A9JR72 Link Image
Enzyme 101 UniProtKB/Swiss-Prot Entry Name A9JR72_HUMAN Link Image
Enzyme 101 PDB ID Not Available
Enzyme 101 Cellular Location Not Available
Enzyme 101 Gene Sequence >5136 bp
ATGTCGGCCAAGGTGCGGCTCAAGAAGCTGGAGCAGCTGCTCCTGGACGGGCCCTGGCGC
AACGAGAGCGCCCTGAGCGTGGAAACGCTGCTCGACGTGCTCGTCTGCCTGTACACCGAG
TGCAGCCACTCGGCCCTGCGCCGCGACAAGTACGTGGCCGAGTTCCTCGAGTGGGCTAAA
CCATTTACACAGCTGGTGAAAGAAATGCAGCTTCATCGAGAAGACTTTGAAATAATTAAA
GTAATTGGAAGAGGTGCTTTTGGTGAGGTTGCTGTTGTCAAAATGAAGAATACTGAACGA
ATTTATGCAATGAAAATCCTCAACAAGTGGGAGATGCTGAAAAGAGCAGAGACCGCGTGC
TTCCGAGAGGAGCGCGATGTGCTGGTGAACGGCGACTGCCAGTGGATCACCGCGCTGCAC
TACGCCTTTCAGGACGAGAACCACCTGTATTTAGTCATGGATTACTATGTGGGTGGTGAT
TTACTGACCCTGCTCAGCAAATTTGAAGACAAGCTTCCGGAAGATATGGCGAGGTTCTAC
ATTGGTGAAATGGTGCTGGCCATTGACTCCATCCATCAGCTTCATTACGTGCACAGAGAC
ATTAAACCTGACAATGTCCTTTTGGACGTGAATGGTCATATCCGCCTGGCTGACTTTGGA
TCATGTTTGAAGATGAATGATGATGGCACTGTGCAGTCCTCCGTGGCCGTGGGCACACCT
GACTACATCTCGCCGGAGATCCTGCAGGCGATGGAGGACGGCATGGGCAAATACGGGCCT
GAGTGTGACTGGTGGTCTCTGGGTGTCTGCATGTATGAGATGCTCTATGGAGAAACGCCG
TTTTATGCGGAGTCACTCGTGGAGACCTATGGGAAGATCATGAACCATGAAGAGCGATTC
CAGTTCCCATCCCATGTCACGGATGTATCTGAAGAAGCGAAGGACCTCATCCAGAGACTG
ATCTGCAGTAGAGAACGCCGGCTGGGGCAGAATGGAATAGAGGATTTCAAAAAGCATGCG
TTTTTTGAAGGTCTAAATTGGGAAAATATACGAAACCTAGAAGCACCTTATATTCCTGAT
GTGAGCAGTCCCTCTGACACATCCAACTTCGACGTGGATGACGACGTGCTGAGAAACACG
GAAATATTACCTCCTGGTTCTCACACAGGCTTTTCTGGATTACATTTGCCATTCATTGGT
TTTACATTCACAACGGAAAGCTGTTTTTCTGATCGAGGCTCTCTGAAGAGCATAATGCAG
TCCAACACATTAACCAAAGATGAGGATGTGCAGCGGGACCTGGAGCACAGCCTGCAGATG
GAAGCTTACGAGAGGAGGATTCGGAGGCTGGAACAGGAGAAGCTGGAGCTGAGCAGGAAG
CTGCAAGAGTCCACCCAGACCGTGCAGTCCCTCCACGGCTCATCTCGGGCCCTCAGCAAT
TCAAACCGAGATAAAGAAATCAAAAAGCTAAATGAAGAAATCGAACGCTTGAAGAATAAA
ATAGCAGATTCAAACAGGCTCGAGCGACAGCTTGAGGACACAGTGGCGCTTCGCCAAGAG
CGTGAGGACTCCACGCAGCGGCTGCGGGGGCTGGAGAAGCAGCACCGCGTGGTCCGGCAG
GAGAAGGAGGAGCTGCACAAGCAACTGGTTGAAGCCTCAGAGCGGTTGAAATCCCAGGCC
AAGGAACTCAAAGATGCCCATCAGCAGCGAAAGCTGGCCCTGCAGGAGTTCTCGGAGCTG
AACGAGCGCATGGCAGAGCTCCGTGCCCAGAAGCAGAAGGTGTCCCGGCAGCTGCGAGAC
AAGGAGGAGGAGATGGAGGTGGCCACGCAGAAGGTGGACGCCATGCGGCAGGAAATGCGG
AGAGCTGAGAAGCTCAGGAAAGAGCTGGAAGCTCAGCTTGATGATGCTGTTGCTGAGGCC
TCCAAGGAGCGCAAGCTTCGTGAGCACAGCGAGAACTTCTGCAAGCAAATGGAAAGCGAG
CTGGAGGCCCTCAAGGTGAAGCAAGGAGGCCGGGGAGCGGGTGCCACCTTAGAGCACCAG
CAAGAGATTTCCAAAATCAAATCCGAGCTGGAGAAGAAAGTCTTATTTTATGAAGAGGAA
TTGGTCAGACGTGAGGCCTCCCATGTGCTAGAAGTGAAAAATGTGAAGAAGGAGGTGCAT
GATTCAGAAAGCCACCAGCTGGCCCTGCAGAAAGAAATCTTGATGTTAAAAGATAAGTTA
GAAAAGTCAAAGCGAGAACGGCATAACGAGATGGAGGAGGCAGTAGGTACAATAAAAGAT
AAATACGAACGAGAAAGAGCGATGCTGTTTGATGAAAACAAGAAGCTAACTGCTGAAAAT
GAAAAGCTCTGTTCCTTTGTGGATAAACTCACAGCTCAAAATAGACAGCTGGAGGATGAG
CTGCAGGATCTGGCAGCCAAGAAGGAGTCAGTGGCCCACTGGGAAGCTCAGATTGCGGAA
ATCATTCAGTGGGTCAGTGACGAGAAAGATGCCCGGGGTTACCTTCAAGCTCTTGCTTCC
AAGATGACCGAAGAGCTCGAGGCTTTGAGGAGTTCTAGTCTGGGGTCAAGAACACTGGAC
CCGCTGTGGAAGGTGCGCCGCAGCCAGAAGCTGGACATGTCCGCGCGGCTGGAGCTGCAG
TCGGCCCTGGAGGCGGAGATCCGGGCCAAGCAGCTTGTCCAGGAGGAGCTCAGGAAGGTC
AAGGACGCCAACCTCACCTTGGAAAGCAAACTAAAGGATTCCGAAGCCAAAAACAGAGAA
TTATTAGAAGAAATGGAAATTTTGAAGAAAAAGATGGAAGAAAAATTCAGAGCAGATACT
GGGCTCAAACTTCCAGATTTTCAGGATTCCATTTTTGAGTATTTCAACACTGCTCCTCTT
GCACATGACCTGACATTTAGAACCAGCTCAGCTAGTGAGCAAGAAACACAAGCTCCGAAG
CCAGAAGCGTCCCCGTCGATGTCTGTGGCTGCATCAGAGCAGCAGGAGGACATGGCTCGG
CCCCCGCAGAGGCCATCCGCTGTGCCGTTGCCCACCACGCAGGCCCTGGCTCTGGCTGGA
CCGAAGCCAAAAGCTCACCAGTTCAGCATCAAGTCCTTCTCCAGCCCTACTCAGTGCAGC
CACTGCACCTCCCTGATGGTTGGGCTGATCCGGCAGGGCTACGCCTGCGAGGTGTGTTCC
TTTGCTTGCCACGTGTCCTGCAAAGACGGTGCCCCCCAGGTGTGCCCAATACCTCCCGAG
CAGTCCAAGAGGCCTCTGGGCGTGGACGTGCAGCGAGGCATCGGAACAGCCTACAAAGGC
CATGTCAAGGTCCCAAAGCCCACGGGGGTGAAGAAGGGATGGCAGCGCGCATATGCAGTC
GTCTGTGACTGCAAGCTCTTCCTGTATGATCTGCCTGAAGGAAAATCCACCCAGCCTGGT
GTCATTGCGAGCCAAGTCTTGGATCTCAGAGATGACGAGTTTTCCGTGAGCTCAGTCCTG
GCCTCAGATGTCATTCATGCTACACGCCGAGATATTCCATGTATATTCAGGGTGACGGCC
TCTCTCTTAGGTGCACCTTCTAAGACCAGCTCGCTGCTCATTCTGACAGAAAATGAGAAT
GAAAAGAAGAAGTGGGTTGGGATTCTAGAAGGACTCCAGTCCATCCTTCATAAAAACCGG
CTGAGGAATCAGGTCGTGCATGTTCCCTTGGAAGCCTACGACAGCTCGCTGCCTCTCATC
AAGGCCATCCTGACAGCTGCCATCGTGGATGCAGACAGGATTGCAGTCGGCCTAGAAGAA
GGGCTCTATGTCATAGAGGTCACCCGAGATGTGATCGTCCGTGCCGCTGACTGTAAGAAG
GTACACCAGATCGAGCTTGCTCCCAGGGAGAAGATCGTAATCCTCCTCTGTGGCCGGAAC
CACCATGTGCACCTCTATCCGTGGTCGTCCCTTGATGGAGCGGAAGGCAGCTTTGACATC
AAGCTTCCGGAAACCAAAGGCTGCCAGCTCATGGCCACGGCCACACTCAAGAGGAACTCT
GGCACCTGCCTGTTTGTGGCCGTGAAACGGCTGATCCTTTGCTATGAGATCCAGAGAACG
AAGCCATTCCACAGAAAGTTCAATGAGATTGTGGCTCCCGGCAGCGTGCAGTGCCTGGCG
GTGCTCAGGGACAGGCTCTGTGTGGGCTACCCTTCTGGGTTCTGCCTGCTGAGCATCCAG
GGGGACGGGCAGCCTCTAAACCTGGTAAATCCCAATGACCCCTCGCTTGCGTTCCTCTCA
CAACAGTCTTTTGATGCCCTTTGTGCTGTGGAGCTCGAAAGCGAGGAGTACCTGCTTTGC
TTCAGCCACATGGGACTGTACGTGGACCCGCAAGGCCGGAGGGCACGCGCGCAGGAGCTC
ATGTGGCCTGCGGCTCCTGTCGCCTGTAGTTGCAGCCCCACCCACGTCACGGTGTACAGC
GAGTATGGCGTGGACGTCTTTGATGTGCGCACCATGGAGTGGGTGCAGACCATCGGCCTG
CGGAGGATAAGGCCCCTGAACTCTGAAGGCACCCTCAACCTCCTCAACTGCGAGCCTCCA
CGCTTGATCTACTTCAAGAGCAAGTTCTCGGGAGCGGTTCTCAACGTGCCGGACACCTCC
GACAACAGCAAGAAGCAGATGCTGCGCACCAGGAGCAAAAGGCGGTTCGTCTTCAAGGTC
CCAGAGGAAGAGAGACTGCAGCAGAGGCGAGAGATGCTTAGAGACCCAGAATTGAGATCC
AAAATGATATCCAACCCAACCAACTTCAACCACGTGGCCCACATGGGCCCAGGCGACGGC
ATGCAGGTGCTCATGGACCTGCCTCTGAGTGCTGTGCCCCCCTCCCAGGAGGAAAGGCCG
GGCCCCGCTCCCACCAACCTGGCTCGCCAGCCTCCATCCAGGAACAAGCCCTACATCTCG
TGGCCCTCATCAGGTGGATCGGAGCCTAGCGTGACTGTGCCTCTGAGAAGTATGTCTGAT
CCAGACCAGGACTTTGACAAAGAGCCTGATTCGGACTCCACCAAACACTCAACTCCATCG
AATAGCTCCAACCCCAGCGGCCCACCGAGCCCCAACTCCCCCCACAGGAGCCAGCTCCCC
CTCGAAGGCCTGGAGCAGCCGGCCTGTGACACCTGA
Enzyme 101 GenBank Gene ID BC155541 Link Image
Enzyme 101 GeneCard ID CDC42BPB Link Image
Enzyme 101 GenAtlas ID Not Available
Enzyme 101 HGNC ID Not Available
Enzyme 101 Chromosome Location 1
Enzyme 101 Locus 14q32.3
Enzyme 101 SNPs SNPJam Report Link Image
Enzyme 101 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 101 Metabolite References Not Available
Enzyme 102 [top]
Enzyme 102 ID 17242
Enzyme 102 Name cDNA, FLJ92607, highly similar to Homo sapiens protein kinase C, gamma (PRKCG), mRNA
Enzyme 102 Synonyms Not Available
Enzyme 102 Gene Name Not Available
Enzyme 102 Protein Sequence >cDNA, FLJ92607, highly similar to Homo sapiens protein kinase C, gamma (PRKCG), mRNA
MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIG
KQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSL
LYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEA
RNLIPMDPNGLSDPYVKLKLIPDPRNLTKHKTRTVKATLNPVWNETFVFNLKPGDVERRL
SVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQ
KFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKG
SFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQL
HSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRD
LKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWS
FGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGS
GPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRL
VLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM
Enzyme 102 Number of Residues 697
Enzyme 102 Molecular Weight 78456.2
Enzyme 102 Theoretical pI 7.50
Enzyme 102 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • metal ion binding
  • nucleoside binding
  • protein kinase C activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • zinc ion binding
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 102 General Function Involved in protein serine/threonine kinase activity
Enzyme 102 Specific Function ATP + a protein = ADP + a phosphoprotein
Enzyme 102 Pathways Not Available
Enzyme 102 Reactions Not Available
Enzyme 102 Pfam Domain Function
Enzyme 102 Signals
  • None
Enzyme 102 Transmembrane Regions
  • None
Enzyme 102 Essentiality Not Available
Enzyme 102 GenBank ID Protein 189065389 Link Image
Enzyme 102 UniProtKB/Swiss-Prot ID B2R5T1 Link Image
Enzyme 102 UniProtKB/Swiss-Prot Entry Name B2R5T1_HUMAN Link Image
Enzyme 102 PDB ID Not Available
Enzyme 102 Cellular Location Not Available
Enzyme 102 Gene Sequence >2094 bp
ATGGCTGGTCTGGGCCCCGGCGTAGGCGATTCAGAGGGGGGACCCCGGCCCCTGTTTTGC
AGAAAGGGGGCTCTGAGGCAGAAGGTGGTCCACGAAGTCAAGAGCCACAAGTTCACCGCT
CGCTTCTTCAAGCAGCCCACCTTCTGCAGCCACTGCACCGACTTCATCTGGGGTATCGGA
AAGCAGGGCCTGCAATGTCAAGTCTGCAGCTTTGTGGTTCATCGACGATGCCACGAATTT
GTGACCTTCGAGTGTCCAGGCGCTGGGAAGGGCCCCCAGACGGACGACCCCCGGAACAAA
CACAAGTTCCGCCTGCATAGCTACAGCAGCCCCACCTTCTGCGACCACTGTGGCTCCCTC
CTCTACGGGCTTGTGCACCAGGGCATGAAATGCTCCTGCTGCGAGATGAACGTGCACCGG
CGCTGTGTGCGTAGCGTGCCCTCCCTGTGCGGTGTGGACCACACCGAGCGCCGCGGGCGC
CTGCAGCTGGAGATCCGGGCTCCCACAGCAGATGAGATCCACGTAACTGTTGGCGAGGCC
CGTAACCTAATTCCTATGGACCCCAATGGTCTCTCTGATCCCTATGTGAAACTGAAGCTC
ATCCCAGACCCTCGGAACCTGACGAAACATAAGACCCGAACGGTGAAAGCCACGCTAAAC
CCTGTGTGGAATGAGACCTTTGTGTTCAACCTGAAGCCAGGGGATGTGGAGCGCCGGCTC
AGCGTGGAGGTGTGGGACTGGGACCGGACCTCCCGCAACGACTTCATGGGGGCCATGTCC
TTTGGCGTCTCGGAGCTGCTCAAGGCGCCCGTGGATGGCTGGTACAAGTTACTGAACCAG
GAGGAGGGCGAGTATTACAATGTGCCGGTGGCCGATGCTGACAACTGCAGCCTCCTCCAG
AAGTTTGAGGCTTGTAACTACCCCCTGGAATTGTATGAGCGGGTGCGGATGGGCCCCTCT
TCCTCTCCCATCCCCTCCCCTTCCCCTAGTCCCACCGACCCCAAGCGCTGCTTCTTCGGG
GCGAGTCCAGGACGCCTGCACATCTCCGACTTCAGCTTCCTCATGGTTCTAGGAAAAGGC
AGTTTTGGGAAGGTGATGCTGGCCGAGCGCAGGGGCTCTGATGAGCTCTACGCCATCAAG
ATCTTGAAAAAGGACGTGATCGTCCAGGACGACGATGTGGACTGCACGCTGGTGGAGAAA
CGTGTGCTGGCGCTGGGGGGCCGGGGTCCTGGCGGCCGGCCCCACTTCCTCACCCAGCTC
CACTCCACCTTCCAGACCCCGGACCGCCTGTATTTCGTGATGGAGTACGTCACCGGGGGA
GACTTGATGTACCACATTCAACAGCTGGGCAAGTTTAAGGAGCCCCATGCAGCGTTCTAC
GCGGCAGAAATCGCTATCGGCCTCTTCTTCCTTCACAATCAGGGCATCATCTACAGGGAC
CTGAAGCTGGACAATGTGATGCTGGATGCTGAGGGACACATCAAGATCACTGACTTTGGC
ATGTGTAAGGAGAACGTCTTCCCCGGGACGACAACCCGCACCTTCTGCGGGACCCCGGAC
TACATAGCCCCGGAGATCATTGCCTACCAGCCCTATGGGAAGTCTGTCGATTGGTGGTCC
TTTGGAGTTCTGCTGTATGAGATGTTGGCAGGACAGCCTCCCTTCGATGGGGAGGACGAG
GAGGAGCTGTTTCAGGCCATCATGGAACAAACTGTCACCTACCCCAAGTCGCTTTCCCGG
GAAGCCGTGGCCATCTGCAAGGGGTTCCTGACCAAGCACCCAGGGAAGCGCCTGGGCTCA
GGGCCTGATGGGGAACCTACCATCCGTGCACATGGCTTTTTCCGCTGGATTGACTGGGAG
CGGCTGGAACGATTGGAGATCCCGCCTCCTTTCAGACCCCGCCCGTGTGGCCGCAGCGGC
GAGAACTTTGACAAGTTCTTCACGCGGGCGGCGCCAGCGCTGACCCCTCCAGACCGCCTA
GTCCTGGCCAGCATCGACCAGGCCGATTTCCAGGGCTTCACCTACGTGAACCCCGACTTC
GTGCACCCGGATGCCCGCAGCCCCACCAGCCCAGTGCCTGTGCCCGTCATGTAA
Enzyme 102 GenBank Gene ID AK312302 Link Image
Enzyme 102 GeneCard ID Not Available
Enzyme 102 GenAtlas ID Not Available
Enzyme 102 HGNC ID HGNC:9402 Link Image
Enzyme 102 Chromosome Location Not Available
Enzyme 102 Locus Not Available
Enzyme 102 SNPs Not Available
Enzyme 102 General References Not Available
Enzyme 102 Metabolite References Not Available
Enzyme 103 [top]
Enzyme 103 ID 17243
Enzyme 103 Name Kinase suppressor of Ras 2
Enzyme 103 Synonyms
  1. hKSR2
Enzyme 103 Gene Name KSR2
Enzyme 103 Protein Sequence >Kinase suppressor of Ras 2
MDEENMTKSEEQQPLSLQKALQQCELVQNMIDLSISNLEGLRTKCATSNDLTQKEIRTLE
SKLVKYFSRQLSCKKKVALQERNAELDGFPQLRHWFRIVDVRKEVLEEISPGQLSLEDLL
EMTDEQVCETVEKYGANREECARLNASLSCLRNVHMSGGNLSKQDWTIQWPTTETGKENN
PVCPPEPTPWIRTHLSQSPRVPSKCVQHYCHTSPTPGAPVYTHVDRLTVDAYPGLCPPPP
LESGHRSLPPSPRQRHAVRTPPRTPNIVTTVTPPGTPPMRKKNKLKPPGTPPPSSRKLIH
LIPGFTALHRSKSHEFQLGHRVDEAHTPKAKKKSKPLNLKIHSSVGSCENIPSQQRSPLL
SERSLRSFFVGHAPFLPSTPPVHTEANFSANTLSVPRWSPQIPRRDLGNSIKHRFSTKYW
MSQTCTVCGKGMLFGLKCKNCKLKCHNKCTKEAPPCHLLIIHRGDPARLVRTESVPCDIN
NPLRKPPRYSDLHISQTLPKTNKINKDHIPVPYQPDSSSNPSSTTSSTPSSPAPPLPPSA
TPPSPLHPSPQCTRQQKNFNLPASHYYKYKQQFIFPDVVPVPETPTRAPQVILHPVTSNP
ILEGNPLLQIEVEPTSENEEVHDEAEESEDDFEEMNLSLLSARSFPRKASQTSIFLQEWD
IPFEQLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHE
NVVLFMGACMSPPHLAIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAK
GILHKDLKSKNVFYDNGKVVITDFGLFSISGVLQAGRREDKLRIQNGWLCHLAPEIIRQL
SPDTEEDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQIGMG
KEISDILLFCWAFEQEERPTFTKLMDMLEKLPKRNRRLSHPGHFWKSAEL
Enzyme 103 Number of Residues 950
Enzyme 103 Molecular Weight 107631.4
Enzyme 103 Theoretical pI 8.87
Enzyme 103 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 103 General Function Involved in intracellular signaling pathway
Enzyme 103 Specific Function Location-regulated scaffold connecting MEK to RAF. Blocks MAP3K8 kinase activity and MAP3K8-mediated signaling. Acts as a negative regulator of MAP3K3-mediated activation of ERK, JNK and NF-kappa-B pathways, inhibiting MAP3K3-mediated interleukin-8 production
Enzyme 103 Pathways Not Available
Enzyme 103 Reactions Not Available
Enzyme 103 Pfam Domain Function
Enzyme 103 Signals
  • None
Enzyme 103 Transmembrane Regions
  • None
Enzyme 103 Essentiality Not Available
Enzyme 103 GenBank ID Protein 167621456 Link Image
Enzyme 103 UniProtKB/Swiss-Prot ID Q6VAB6 Link Image
Enzyme 103 UniProtKB/Swiss-Prot Entry Name KSR2_HUMAN Link Image
Enzyme 103 PDB ID Not Available
Enzyme 103 Cellular Location Not Available
Enzyme 103 Gene Sequence >2766 bp
ATGATAGACTTGAGCATCTCCAACCTGGAAGGGCTTAGGACCAAATGTGCTACCTCCAAC
GACCTCACACAAAAAGAAATCCGGACCCTGGAGAGCAAGCTGGTGAAGTACTTCAGCCGG
CAGCTGTCCTGCAAAAAGAAGGTAGCCTTGCAGGAGCGCAACGCGGAGCTGGACGGCTTC
CCCCAGCTACGGCACTGGTTCCGAATCGTCGATGTGCGCAAGGAGGTCCTGGAGGAAATC
TCCCCCGGCCAGCTGAGCCTGGAGGACCTCTTGGAGATGACGGATGAACAGGTGTGCGAG
ACTGTGGAGAAATACGGAGCCAACCGGGAGGAGTGTGCCCGCCTCAACGCCTCCCTCTCC
TGCCTCAGGAATGTCCACATGTCAGGAGGCAACCTTTCCAAACAAGACTGGACCATCCAG
TGGCCCACGACAGAGACGGGGAAGGAGAACAATCCCGTGTGCCCCCCGGAGCCCACCCCG
TGGATCCGCACCCATCTCTCCCAGAGCCCCAGGGTCCCGTCCAAGTGCGTCCAGCACTAT
TGTCACACCAGCCCCACTCCCGGGGCCCCTGTGTACACCCACGTGGACAGGCTTACCGTG
GACGCCTACCCGGGCTTGTGCCCGCCCCCGCCACTGGAGTCGGGCCACCGTTCCCTGCCC
CCATCGCCCCGGCAGCGGCACGCGGTCCGCACCCCGCCGCGCACCCCCAACATCGTCACC
ACCGTGACCCCGCCGGGCACGCCGCCCATGAGGAAGAAGAACAAGCTGAAGCCCCCGGGG
ACCCCACCGCCCTCCTCCCGAAAACTGATACACTTGATCCCGGGATTCACCGCGCTGCAT
CGGAGCAAATCCCACGAGTTCCAGCTGGGGCACCGCGTGGACGAGGCCCACACGCCCAAA
GCCAAGAAGAAGAGCAAACCCTTGAACCTCAAGATCCACAGCAGCGTAGGCAGCTGCGAG
AACATCCCCTCTCAGCAGCGCTCCCCGCTGCTGTCCGAGCGCTCCCTCCGCTCCTTCTTT
GTGGGACACGCACCTTTCCTGCCTTCCACCCCTCCTGTTCACACTGAGGCCAACTTCTCT
GCAAACACACTGTCAGTGCCACGCTGGTCCCCGCAGATCCCTCGCAGAGATCTCGGCAAC
TCCATCAAGCACAGGTTTTCCACCAAGTACTGGATGTCTCAGACGTGCACAGTCTGTGGG
AAAGGGATGCTTTTTGGCCTCAAGTGTAAAAACTGCAAGTTAAAGTGCCACAACAAATGC
ACCAAAGAAGCCCCACCCTGTCATCTTCTGATCATCCACCGAGGAGATCCAGCAAGGTTA
GTCCGGACAGAGTCCGTTCCGTGTGACATCAACAACCCTCTACGGAAGCCACCTCGCTAT
TCAGACCTGCACATCAGTCAGACGCTCCCCAAAACCAACAAAATCAACAAGGACCACATC
CCTGTCCCTTACCAGCCAGACTCCAGCAGCAACCCCTCCTCCACGACGTCCTCCACGCCC
TCCTCGCCAGCACCCCCCCTCCCTCCTAGTGCCACGCCGCCTTCTCCCCTACACCCTTCC
CCACAGTGCACACGGCAGCAGAAGAACTTCAACCTGCCAGCATCCCACTACTACAAATAC
AAGCAGCAGTTCATCTTCCCAGATGTGGTGCCGGTGCCGGAGACGCCGACCCGGGCGCCC
CAGGTCATCCTGCATCCGGTGACCTCGAATCCAATCTTGGAAGGAAATCCATTACTTCAA
ATTGAAGTGGAGCCAACGTCGGAGAATGAAGAGGTCCATGATGAGGCCGAAGAGTCAGAG
GATGACTTCGAGGAGATGAACCTGTCCCTCCTCTCGGCCCGGAGCTTCCCACGCAAGGCC
AGCCAGACCAGCATCTTCCTTCAGGAGTGGGACATCCCCTTTGAGCAGCTGGAGATCGGC
GAGCTCATTGGAAAGGGCCGCTTTGGGCAAGTGTACCACGGCCGCTGGCATGGCGAGGTG
GCCATCCGGCTGATTGACATTGAGAGGGACAACGAGGACCAGCTCAAGGCCTTCAAGCGG
GAGGTGATGGCCTACAGGCAGACACGGCATGAGAACGTGGTGCTTTTCATGGGTGCCTGC
ATGAGCCCGCCTCACCTGGCCATCATCACCAGCCTCTGTAAGGGACGGACGCTCTATTCC
GTTGTGAGGGATGCCAAAATCGTTTTGGATGTCAACAAAACCAGGCAGATTGCTCAAGAA
ATTGTGAAGGGCATGGGCTACCTCCACGCCAAGGGAATCCTACACAAGGACCTCAAGTCA
AAGAACGTCTTCTATGACAACGGCAAAGTGGTCATCACGGACTTTGGACTCTTCAGCATT
TCTGGGGTGCTGCAGGCTGGCAGGCGGGAGGACAAACTGCGCATCCAGAATGGCTGGCTA
TGCCACCTGGCACCAGAGATCATCCGCCAGCTGTCCCCCGACACAGAGGAGGATAAGCTC
CCCTTCTCCAAGCACTCTGACGTCTTTGCCCTTGGCACAATCTGGTATGAACTCCACGCC
AGGGAATGGCCTTTCAAGACCCAACCAGCAGAGGCAATAATCTGGCAAATGGGCACAGGC
ATGAAACCCAACCTCAGCCAGATTGGCATGGGAAAAGAAATCTCGGACATTCTTCTCTTC
TGCTGGGCCTTTGAACAAGAAGAGAGACCTACCTTCACCAAGCTCATGGACATGCTGGAG
AAACTGCCAAAGCGAAACCGTCGCCTGTCTCACCCTGGACATTTCTGGAAGTCTGCAGAG
CTGTGA
Enzyme 103 GenBank Gene ID Not Available
Enzyme 103 GeneCard ID KSR2 Link Image
Enzyme 103 GenAtlas ID KSR2 Link Image
Enzyme 103 HGNC ID HGNC:18610 Link Image
Enzyme 103 Chromosome Location 1
Enzyme 103 Locus 12q24.22-q24.23
Enzyme 103 SNPs SNPJam Report Link Image
Enzyme 103 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. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  3. Channavajhala PL, Wu L, Cuozzo JW, Hall JP, Liu W, Lin LL, Zhang Y: Identification of a novel human kinase supporter of Ras (hKSR-2) that functions as a negative regulator of Cot (Tpl2) signaling. J Biol Chem. 2003 Nov 21;278(47):47089-97. Epub 2003 Sep 15. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Channavajhala PL, Rao VR, Spaulding V, Lin LL, Zhang YG: hKSR-2 inhibits MEKK3-activated MAP kinase and NF-kappaB pathways in inflammation. Biochem Biophys Res Commun. 2005 Sep 9;334(4):1214-8. [PubMed Link Image]
  6. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 103 Metabolite References Not Available
Enzyme 104 [top]
Enzyme 104 ID 17244
Enzyme 104 Name cDNA FLJ76797, highly similar to Homo sapiens protein kinase C, zeta (PRKCZ), mRNA
Enzyme 104 Synonyms Not Available
Enzyme 104 Gene Name Not Available
Enzyme 104 Protein Sequence >cDNA FLJ76797, highly similar to Homo sapiens protein kinase C, zeta (PRKCZ), mRNA
MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKW
VDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGAR
RWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTC
RKHMDSVMPSQEPPVDDRNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDG
IKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTE
KHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEI
CIALNLLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAP
EILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRF
LSVKASHVLKGFLNKDPKEGLGCRPQTGFSDIKSHAFFRSIGWDLLEKKQALPPFQPQIT
DDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV
Enzyme 104 Number of Residues 592
Enzyme 104 Molecular Weight 67498
Enzyme 104 Theoretical pI 5.52
Enzyme 104 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • atypical protein kinase C activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • nucleotide binding
  • phorbol ester receptor activity
  • protein kinase C activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleotide binding
  • receptor activity
  • signal transducer activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • zinc ion binding
Process
  • biopolymer metabolism
  • biopolymer modification
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid phosphorylation
  • protein modification
  • signal transduction
Component
Enzyme 104 General Function Not Available
Enzyme 104 Specific Function ATP + a protein = ADP + a phosphoprotein
Enzyme 104 Pathways Not Available
Enzyme 104 Reactions Not Available
Enzyme 104 Pfam Domain Function
Enzyme 104 Signals
  • None
Enzyme 104 Transmembrane Regions
  • None
Enzyme 104 Essentiality Not Available
Enzyme 104 GenBank ID Protein Not Available
Enzyme 104 UniProtKB/Swiss-Prot ID A8K4N0 Link Image
Enzyme 104 UniProtKB/Swiss-Prot Entry Name A8K4N0_HUMAN Link Image
Enzyme 104 PDB ID Not Available
Enzyme 104 Cellular Location Not Available
Enzyme 104 Gene Sequence Not Available
Enzyme 104 GenBank Gene ID AK290995 Link Image
Enzyme 104 GeneCard ID Not Available
Enzyme 104 GenAtlas ID Not Available
Enzyme 104 HGNC ID HGNC:9412 Link Image
Enzyme 104 Chromosome Location Not Available
Enzyme 104 Locus Not Available
Enzyme 104 SNPs Not Available
Enzyme 104 General References Not Available
Enzyme 104 Metabolite References Not Available
Enzyme 105 [top]
Enzyme 105 ID 17245
Enzyme 105 Name cDNA FLJ60459, highly similar to Protein kinase C theta type (EC 2.7.11.13)
Enzyme 105 Synonyms Not Available
Enzyme 105 Gene Name Not Available
Enzyme 105 Protein Sequence >cDNA FLJ60459, highly similar to Protein kinase C theta type (EC 2.7.11.13)
MDTKDMNEFETEGFFALHQRRGAIKQAKVHHVKCHEFTATFFPQPTFCSVCHEFVWGLNK
QGYQCRQCNAAIHKKCIDKVIAKCTGSAINSRETMFHKERFKIDMPHRFKVYNYKSPTFC
EHCGTLLWGLARQGLKCDACGMNVHHRCQTKVANLCGINQKLMAEALAMIESTQQARCLR
DTEQIFREGPVEIGLPCSIKNEARPPCLPTPGKREPQGISWESPLDEVDKMCHLPEPELN
KERPSLQIKLKIEDFILHKMLGKGSFGKVFLAEFKKTNQFFAIKALKKDVVLMDDDVECT
MVEKRVLSLAWEHPFLTHMFCTFQTKENLFFVMEYLNGGDLMYHIQSCHKFDLSRATFYA
AEIILGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKTNTFCGTPDY
IAPEILLGQKYNHSVDWWSFGVLLYEMLIGQSPFHGQDEEELFHSIRMDNPFYPRWLEKE
AKDLLVKLFVREPEKRLGVRGDIRQHPLFREINWEELERKEIDPPFRPKVKSPFDCSNFD
KEFLNEKPRLSFADRALINSMDQNMFRNFSFMNPGMERLIS
Enzyme 105 Number of Residues 581
Enzyme 105 Molecular Weight 67559.7
Enzyme 105 Theoretical pI 7.60
Enzyme 105 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 105 General Function Involved in protein serine/threonine kinase activity
Enzyme 105 Specific Function ATP + a protein = ADP + a phosphoprotein
Enzyme 105 Pathways Not Available
Enzyme 105 Reactions Not Available
Enzyme 105 Pfam Domain Function
Enzyme 105 Signals
  • None
Enzyme 105 Transmembrane Regions
  • None
Enzyme 105 Essentiality Not Available
Enzyme 105 GenBank ID Protein 194375938 Link Image
Enzyme 105 UniProtKB/Swiss-Prot ID B4DF52 Link Image
Enzyme 105 UniProtKB/Swiss-Prot Entry Name B4DF52_HUMAN Link Image
Enzyme 105 PDB ID 1XJD Link Image
Enzyme 105 PDB File Show
Enzyme 105 3D Structure
Enzyme 105 Cellular Location Not Available
Enzyme 105 Gene Sequence >1746 bp
ATGGACACAAAGGACATGAATGAATTTGAGACGGAAGGCTTCTTTGCTTTGCATCAGCGC
CGGGGTGCCATCAAGCAGGCAAAGGTCCACCACGTCAAGTGCCACGAGTTCACTGCCACC
TTCTTCCCACAGCCCACATTTTGCTCTGTCTGCCACGAGTTTGTCTGGGGCCTGAACAAA
CAGGGCTACCAGTGCCGACAATGCAATGCAGCAATTCACAAGAAGTGTATTGATAAAGTT
ATAGCAAAGTGCACAGGATCAGCTATCAATAGCCGAGAAACCATGTTCCACAAGGAGAGA
TTCAAAATTGACATGCCACACAGATTTAAAGTCTACAATTACAAGAGCCCGACCTTCTGT
GAACACTGTGGGACCCTGCTGTGGGGACTGGCACGGCAAGGACTCAAGTGTGATGCATGT
GGCATGAATGTGCATCATAGATGCCAGACAAAGGTGGCCAACCTTTGTGGCATAAACCAG
AAGCTAATGGCTGAAGCGCTGGCCATGATTGAGAGCACTCAACAGGCTCGCTGCTTAAGA
GATACTGAACAGATCTTCAGAGAAGGTCCGGTTGAAATTGGTCTCCCATGCTCCATCAAA
AATGAAGCAAGGCCGCCATGTTTACCGACACCGGGAAAAAGAGAGCCTCAGGGCATTTCC
TGGGAGTCTCCGTTGGATGAGGTGGATAAAATGTGCCATCTTCCAGAACCTGAACTGAAC
AAAGAAAGACCATCTCTGCAGATTAAACTAAAAATTGAGGATTTTATCTTGCACAAAATG
TTGGGGAAAGGAAGTTTTGGCAAGGTCTTCCTGGCAGAATTCAAGAAAACCAATCAATTT
TTCGCAATAAAGGCCTTAAAGAAAGATGTGGTCTTGATGGACGATGATGTTGAGTGCACG
ATGGTAGAGAAGAGAGTTCTTTCCTTGGCCTGGGAGCATCCGTTTCTGACGCACATGTTT
TGTACATTCCAGACCAAGGAAAACCTCTTTTTTGTGATGGAGTACCTCAACGGAGGGGAC
TTAATGTACCACATCCAAAGCTGCCACAAGTTCGACCTTTCCAGAGCGACGTTTTATGCT
GCTGAAATCATTCTTGGTCTGCAGTTCCTTCATTCCAAAGGAATAGTCTACAGGGACCTG
AAGCTAGATAACATCCTGTTAGACAAAGATGGACATATCAAGATCGCGGATTTTGGAATG
TGCAAGGAGAACATGTTAGGAGATGCCAAGACGAATACCTTCTGTGGGACACCTGACTAC
ATCGCCCCAGAGATCTTGCTGGGTCAGAAATACAACCACTCTGTGGACTGGTGGTCCTTC
GGGGTTCTCCTTTATGAAATGCTGATTGGTCAGTCGCCTTTCCACGGGCAGGATGAGGAG
GAGCTCTTCCACTCCATCCGCATGGACAATCCCTTTTACCCACGGTGGCTGGAGAAGGAA
GCAAAGGACCTTCTGGTGAAGCTCTTCGTGCGAGAACCTGAGAAGAGGCTGGGCGTGAGG
GGAGACATCCGCCAGCACCCTTTGTTTCGGGAGATCAACTGGGAGGAACTTGAACGGAAG
GAGATTGACCCACCGTTCCGGCCGAAAGTGAAATCACCATTTGACTGCAGCAATTTCGAC
AAAGAATTCTTAAACGAGAAGCCCCGGCTGTCATTTGCCGACAGAGCACTGATCAACAGC
ATGGACCAGAATATGTTCAGGAACTTTTCCTTCATGAACCCCGGGATGGAGCGGCTGATA
TCCTGA
Enzyme 105 GenBank Gene ID AK293935 Link Image
Enzyme 105 GeneCard ID Not Available
Enzyme 105 GenAtlas ID Not Available
Enzyme 105 HGNC ID HGNC:9410 Link Image
Enzyme 105 Chromosome Location Not Available
Enzyme 105 Locus Not Available
Enzyme 105 SNPs Not Available
Enzyme 105 General References Not Available
Enzyme 105 Metabolite References Not Available
Enzyme 106 [top]
Enzyme 106 ID 17246
Enzyme 106 Name Tensin-like C1 domain-containing phosphatase
Enzyme 106 Synonyms
  1. C1 domain-containing phosphatase and tensin homolog
  2. C1-TEN
  3. Tensin-2
Enzyme 106 Gene Name TENC1
Enzyme 106 Protein Sequence >Tensin-like C1 domain-containing phosphatase
MKSSGPVERLLRALGRRDSSRAASRPRKAEPHSFREKVFRKKPPVCAVCKVTIDGTGVSC
RVCKVATHRKCEAKVTSACQALPPVELRRNTAPVRRIEHLGSTKSLNHSKQRSTLPRSFS
LDPLMERRWDLDLTYVTERILAAAFPARPDEQRHRGHLRELAHVLQSKHRDKYLLFNLSE
KRHDLTRLNPKVQDFGWPELHAPPLDKLCSICKAMETWLSADPQHVVVLYCKGNKGKLGV
IVSAYMHYSKISAGADQALATLTMRKFCEDKVATELQPSQRRYISYFSGLLSGSIRMNSS
PLFLHYVLIPMLPAFEPGTGFQPFLKIYQSMQLVYTSGVYHIAGPGPQQLCISLEPALLL
KGDVMVTCYHKGGRGTDRTLVFRVQFHTCTIHGPQLTFPKDQLDEAWTDERFPFQASVEF
VFSSSPEKIKGSTPRNDPSVSVDYNTTEPAVRWDSYENFNQHHEDSVDGSLTHTRGPLDG
SPYAQVQRPPRQTPPAPSPEPPPPPMLSVSSDSGHSSTLTTEPAAESPGRPPPTAAERQE
LDRLLGGCGVASGGRGAGRETAILDDEEQPTVGGGPHLGVYPGHRPGLSRHCSCRQGYRE
PCGVPNGGYYRPEGTLERRRLAYGGYEGSPQGYAEASMEKRRLCRSLSEGLYPYPPEMGK
PATGDFGYRAPGYREVVILEDPGLPALYPCPACEEKLALPTAALYGLRLEREAGEGWASE
AGKPLLHPVRPGHPLPLLLPACGHHHAPMPDYSCLKPPKAGEEGHEGCSYTMCPEGRYGH
PGYPALVTYSYGGAVPSYCPAYGRVPHSCGSPGEGRGYPSPGAHSPRAGSISPGSPPYPQ
SRKLSYEIPTEEGGDRYPLPGHLASAGPLASAESLEPVSWREGPSGHSTLPRSPRDAPCS
ASSELSGPSTPLHTSSPVQGKESTRRQDTRSPTSAPTQRLSPGEALPPVSQAGTGKAPEL
PSGSGPEPLAPSPVSPTFPPSSPSDWPQERSPGGHSDGASPRSPVPTTLPGLRHAPWQGP
RGPPDSPDGSPLTPVPSQMPWLVASPEPPQSSPTPAFPLAASYDTNGLSQPPLPEKRHLP
GPGQQPGPWGPEQASSPARGISHHVTFAPLLSDNVPQTPEPPTQESQSNVKFVQDTSKFW
YKPHLSRDQAIALLKDKDPGAFLIRDSHSFQGAYGLALKVATPPPSAQPWKGDPVEQLVR
HFLIETGPKGVKIKGCPSEPYFGSLSALVSQHSISPISLPCCLRIPSKDPLEETPEAPVP
TNMSTAADLLRQGAACSVLYLTSVETESLTGPQAVARASSAALSCSPRPTPAVVHFKVSA
QGITLTDNQRKLFFRRHYPVNSITFSSTDPQDRRWTNPDGTTSKIFGFVAKKPGSPWENV
CHLFAELDPDQPAGAIVTFITKVLLGQRK
Enzyme 106 Number of Residues 1409
Enzyme 106 Molecular Weight 152579.0
Enzyme 106 Theoretical pI 8.42
Enzyme 106 GO Classification
Function
  • binding
  • protein binding
Process
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 106 General Function Involved in intracellular signaling pathway
Enzyme 106 Specific Function Regulates cell motility and proliferation. May have phosphatase activity. Reduces AKT1 phosphorylation. Lowers AKT1 kinase activity and interferes with AKT1 signaling
Enzyme 106 Pathways Not Available
Enzyme 106 Reactions Not Available
Enzyme 106 Pfam Domain Function
Enzyme 106 Signals
  • None
Enzyme 106 Transmembrane Regions
  • None
Enzyme 106 Essentiality Not Available
Enzyme 106 GenBank ID Protein 38787957 Link Image
Enzyme 106 UniProtKB/Swiss-Prot ID Q63HR2 Link Image
Enzyme 106 UniProtKB/Swiss-Prot Entry Name TENC1_HUMAN Link Image
Enzyme 106 PDB ID Not Available
Enzyme 106 Cellular Location Not Available
Enzyme 106 Gene Sequence >4230 bp
ATGAAGTCCAGCGGCCCTGTGGAGAGGCTGCTCAGAGCCCTGGGGAGGAGGGACAGCAGC
CGGGCCGCAAGCAGGCCTAGGAAAGCTGAGCCTCATAGCTTCCGGGAGAAGGTTTTCCGG
AAGAAACCTCCAGTCTGTGCAGTATGTAAGGTGACCATCGATGGGACAGGCGTTTCGTGC
AGAGTCTGCAAGGTGGCGACGCACAGAAAATGTGAAGCAAAGGTGACTTCAGCCTGTCAG
GCCTTGCCTCCCGTGGAGTTGCGGCGAAACACGGCCCCAGTCAGGCGCATAGAGCACCTG
GGATCCACCAAATCTCTGAACCACTCAAAGCAGCGCAGCACTCTGCCCAGGAGCTTCAGC
CTGGACCCGCTCATGGAGCGGCGCTGGGACTTAGACCTCACCTACGTGACGGAGCGCATC
TTGGCCGCCGCCTTCCCCGCGCGGCCCGATGAACAGCGGCACCGGGGCCACCTGCGCGAG
CTGGCCCATGTGCTGCAATCCAAGCACCGGGACAAGTACCTGCTCTTCAACCTTTCAGAG
AAAAGGCATGACCTGACCCGCTTAAACCCCAAGGTTCAAGACTTCGGCTGGCCTGAGCTG
CATGCTCCACCCCTGGACAAGCTGTGCTCCATCTGCAAAGCCATGGAGACATGGCTCAGT
GCTGACCCACAGCACGTGGTCGTACTATACTGCAAGGGAAACAAGGGCAAGCTTGGGGTC
ATCGTTTCTGCCTACATGCACTACAGCAAGATCTCTGCAGGGGCGGACCAGGCACTGGCC
ACTCTTACCATGCGGAAATTCTGCGAGGACAAGGTGGCCACAGAACTGCAGCCCTCCCAG
CGTCGATATATCAGCTACTTCAGTGGGCTGCTATCTGGCTCCATCAGAATGAACAGCAGC
CCTCTCTTCCTGCACTATGTGCTCATCCCCATGCTGCCAGCCTTTGAACCTGGCACAGGC
TTCCAGCCCTTCCTTAAAATCTACCAGTCCATGCAGCTTGTCTACACATCTGGAGTCTAT
CACATTGCAGGCCCTGGTCCCCAGCAGCTTTGCATCAGCCTGGAGCCAGCCCTCCTCCTC
AAAGGCGATGTCATGGTAACATGTTATCACAAGGGTGGCCGGGGCACAGACCGGACCCTC
GTGTTCCGAGTCCAGTTCCACACCTGCACCATCCACGGACCACAGCTCACTTTCCCCAAG
GACCAGCTTGACGAGGCCTGGACTGATGAGAGGTTCCCCTTCCAAGCCTCCGTGGAGTTT
GTCTTCTCCTCCAGCCCCGAGAAGATCAAAGGCAGCACTCCACGGAACGACCCCTCGGTC
TCTGTCGACTACAACACCACTGAGCCAGCCGTGCGCTGGGACTCCTATGAGAACTTCAAC
CAGCACCACGAGGACAGTGTGGATGGCTCCTTGACCCACACCCGGGGTCCCCTGGATGGC
AGTCCTTATGCCCAGGTGCAGCGGCCTCCCCGGCAGACCCCCCCGGCACCCTCTCCAGAG
CCTCCACCACCCCCCATGCTCTCTGTCAGCAGCGACTCAGGCCATTCCTCCACGCTGACC
ACAGAGCCGGCTGCTGAGTCCCCTGGCCGGCCGCCCCCTACAGCTGCTGAACGGCAGGAG
CTGGATCGCCTCCTAGGAGGCTGCGGAGTGGCCAGTGGGGGCCGGGGAGCTGGGCGCGAG
ACGGCCATCCTAGATGACGAAGAGCAGCCCACTGTGGGCGGAGGCCCCCACCTCGGAGTG
TATCCAGGCCATAGGCCTGGCCTCAGCCGCCACTGCTCCTGCCGCCAGGGCTACCGGGAG
CCCTGCGGGGTTCCCAATGGGGGCTACTACCGGCCAGAGGGAACCCTGGAGAGGAGGCGA
CTGGCCTACGGGGGCTATGAGGGATCCCCCCAGGGCTACGCCGAGGCCTCGATGGAGAAG
AGGCGCCTCTGCCGATCGCTGTCAGAGGGGCTATACCCCTACCCACCTGAGATGGGGAAA
CCAGCCACTGGGGACTTTGGCTACCGCGCCCCAGGCTACCGGGAGGTGGTCATCCTGGAG
GACCCTGGGCTGCCTGCCCTATACCCATGCCCAGCCTGCGAGGAGAAGCTGGCGCTGCCT
ACAGCAGCCTTGTATGGACTGCGGCTGGAGAGGGAGGCTGGAGAAGGGTGGGCAAGTGAG
GCTGGCAAGCCTCTCCTGCACCCAGTGCGGCCTGGGCACCCGCTGCCTCTGCTCTTGCCT
GCCTGTGGGCATCACCATGCCCCGATGCCTGACTACAGCTGCCTGAAGCCACCCAAGGCA
GGCGAGGAAGGGCACGAGGGCTGCTCCTACACCATGTGCCCCGAAGGCAGGTATGGGCAT
CCAGGGTACCCTGCCCTGGTGACATACAGCTATGGAGGAGCAGTTCCCAGTTACTGCCCA
GCATATGGCCGTGTGCCTCATAGCTGTGGCTCTCCAGGAGAGGGCAGAGGGTATCCCAGC
CCTGGTGCCCACTCCCCACGGGCTGGCTCCATTTCCCCGGGCAGCCCGCCCTATCCACAA
TCTAGGAAGCTGAGCTACGAGATCCCTACGGAGGAGGGAGGGGACAGGTACCCATTGCCT
GGGCACCTGGCCTCAGCAGGACCTTTGGCATCTGCAGAGTCGCTGGAGCCGGTGTCCTGG
AGGGAGGGCCCCAGTGGGCACAGCACACTGCCTCGGTCTCCCCGAGATGCCCCATGCAGT
GCTTCGTCAGAGTTGTCTGGTCCCTCCACGCCCCTGCACACCAGCAGTCCAGTCCAGGGC
AAGGAAAGCACCCGGCGACAGGACACCAGGTCCCCCACCTCAGCGCCCACTCAGAGACTG
AGTCCTGGCGAGGCCTTGCCCCCTGTTTCCCAGGCAGGCACCGGAAAGGCCCCTGAGCTG
CCGTCGGGAAGTGGGCCTGAGCCTCTGGCCCCTAGCCCAGTCTCTCCGACCTTCCCTCCC
AGCTCGCCCAGTGACTGGCCTCAGGAAAGGAGTCCAGGGGGCCACTCAGATGGCGCCAGT
CCTCGGAGCCCTGTGCCCACCACACTTCCTGGCCTCCGCCACGCCCCCTGGCAAGGCCCT
CGAGGCCCCCCCGACAGCCCAGATGGGTCTCCCCTCACTCCTGTGCCTTCCCAGATGCCC
TGGCTTGTGGCCAGCCCAGAGCCGCCTCAGAGCTCACCTACACCTGCTTTCCCCCTGGCT
GCCTCCTATGACACCAATGGCCTTAGCCAGCCCCCACTTCCTGAGAAACGCCACCTGCCC
GGGCCGGGGCAACAGCCAGGACCCTGGGGCCCAGAGCAGGCATCATCGCCAGCCAGAGGC
ATCAGTCACCATGTCACCTTCGCACCTCTGCTCTCAGATAATGTCCCCCAAACCCCAGAG
CCTCCTACACAAGAGAGCCAAAGCAATGTCAAGTTTGTCCAGGATACATCCAAGTTCTGG
TACAAGCCACACCTGTCCCGTGACCAAGCCATTGCCCTGCTGAAGGACAAGGACCCTGGG
GCCTTCCTGATCAGGGACAGTCATTCATTCCAAGGAGCTTATGGGCTGGCCCTCAAGGTG
GCCACACCGCCACCCAGTGCCCAGCCCTGGAAAGGGGACCCCGTGGAACAGCTGGTCCGC
CATTTCCTCATCGAGACTGGGCCCAAAGGGGTGAAGATCAAGGGCTGCCCCAGTGAGCCC
TACTTTGGCAGCCTGTCCGCCTTGGTCTCCCAGCACTCCATCTCCCCCATCTCCCTGCCC
TGCTGCCTGCGCATTCCCAGCAAAGATCCTCTGGAAGAGACCCCAGAGGCTCCAGTGCCC
ACCAACATGAGCACAGCGGCAGACCTCCTGCGTCAGGGTGCTGCCTGCAGCGTGCTCTAC
TTGACCTCAGTGGAGACAGAGTCACTGACGGGCCCCCAAGCTGTGGCCCGGGCCAGCTCT
GCAGCTCTGAGCTGTAGCCCCCGCCCGACACCAGCTGTTGTCCACTTCAAGGTGTCAGCC
CAGGGCATTACACTGACGGACAACCAAAGGAAGCTCTTCTTTCGCCGCCATTATCCAGTG
AACAGCATCACCTTCTCCAGCACTGACCCTCAAGACCGGAGATGGACCAACCCAGACGGG
ACCACCTCCAAGATCTTTGGTTTCGTGGCCAAGAAGCCGGGAAGCCCCTGGGAGAATGTG
TGTCACCTCTTTGCAGAGCTTGACCCAGATCAGCCTGCTGGCGCCATTGTCACCTTCATC
ACCAAAGTTCTACTGGGCCAGAGAAAATGA
Enzyme 106 GenBank Gene ID NM_170754.2 Link Image
Enzyme 106 GeneCard ID TENC1 Link Image
Enzyme 106 GenAtlas ID TENC1 Link Image
Enzyme 106 HGNC ID HGNC:19737 Link Image
Enzyme 106 Chromosome Location 1
Enzyme 106 Locus 12q13.13
Enzyme 106 SNPs SNPJam Report Link Image
Enzyme 106 General References
  1. Hafizi S, Alindri F, Karlsson R, Dahlback B: Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1 domain-containing protein with homology to tensin. Biochem Biophys Res Commun. 2002 Dec 20;299(5):793-800. [PubMed Link Image]
  2. Chen H, Duncan IC, Bozorgchami H, Lo SH: Tensin1 and a previously undocumented family member, tensin2, positively regulate cell migration. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):733-8. Epub 2002 Jan 15. [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. 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. 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. 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. Hafizi S, Ibraimi F, Dahlback B: C1-TEN is a negative regulator of the Akt/PKB signal transduction pathway and inhibits cell survival, proliferation, and migration. FASEB J. 2005 Jun;19(8):971-3. Epub 2005 Apr 7. [PubMed Link Image]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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 106 Metabolite References Not Available
Enzyme 107 [top]
Enzyme 107 ID 17247
Enzyme 107 Name Protein kinase C, alpha variant
Enzyme 107 Synonyms Not Available
Enzyme 107 Gene Name Not Available
Enzyme 107 Protein Sequence >Protein kinase C, alpha variant
DPTHSPKDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPS
LCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESK
QKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKM
PASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSN
NLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKR
VLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYVAEISI
GLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEI
IAYQPYGKSVDWWAYGVLLYEMLAGQVMFCYIFMFVYCCVM
Enzyme 107 Number of Residues 461
Enzyme 107 Molecular Weight 52975.9
Enzyme 107 Theoretical pI 7.12
Enzyme 107 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 107 General Function Involved in intracellular signaling pathway
Enzyme 107 Specific Function ATP + a protein = ADP + a phosphoprotein
Enzyme 107 Pathways Not Available
Enzyme 107 Reactions Not Available
Enzyme 107 Pfam Domain Function
Enzyme 107 Signals
  • None
Enzyme 107 Transmembrane Regions
  • None
Enzyme 107 Essentiality Not Available
Enzyme 107 GenBank ID Protein 62088530 Link Image
Enzyme 107 UniProtKB/Swiss-Prot ID Q59FI5 Link Image
Enzyme 107 UniProtKB/Swiss-Prot Entry Name Q59FI5_HUMAN Link Image
Enzyme 107 PDB ID 1DSY Link Image
Enzyme 107 PDB File Show
Enzyme 107 3D Structure
Enzyme 107 Cellular Location Not Available
Enzyme 107 Gene Sequence >1386 bp
GATCCTACTCACTCTCCGAAGGACCCCAGGAGCAAGCACAAGTTCAAAATCCACACTTAC
GGAAGCCCCACCTTCTGCGATCACTGTGGGTCACTGCTCTATGGACTTATCCATCAAGGG
ATGAAATGTGACACCTGCGATATGAACGTTCACAAGCAATGCGTCATCAATGTCCCCAGC
CTCTGCGGAATGGATCACACTGAGAAGAGGGGGCGGATTTACCTAAAGGCTGAGGTTGCT
GATGAAAAGCTCCATGTCACAGTACGAGATGCAAAAAATCTAATCCCTATGGATCCAAAC
GGGCTTTCAGATCCTTATGTGAAGCTGAAACTTATTCCTGATCCCAAGAATGAAAGCAAG
CAAAAAACCAAAACCATCCGCTCCACACTAAATCCGCAGTGGAATGAGTCCTTTACATTC
AAATTGAAACCTTCAGACAAAGACCGACGACTGTCTGTAGAAATCTGGGACTGGGATCGA
ACAACAAGGAATGACTTCATGGGATCCCTTTCCTTTGGAGTTTCGGAGCTGATGAAGATG
CCGGCCAGTGGATGGTACAAGTTGCTTAACCAAGAAGAAGGTGAGTACTACAACGTACCC
ATTCCGGAAGGGGACGAGGAAGGAAACATGGAACTCAGGCAGAAATTCGAGAAAGCCAAA
CTTGGCCCTGCTGGCAACAAAGTCATCAGTCCCTCTGAAGACAGGAAACAACCTTCCAAC
AACCTTGACCGAGTGAAACTCACGGACTTCAATTTCCTCATGGTGTTGGGAAAGGGGAGT
TTTGGAAAGGTGATGCTTGCCGACAGGAAGGGCACAGAAGAACTGTATGCAATCAAAATC
CTGAAGAAGGATGTGGTGATTCAGGATGATGACGTGGAGTGCACCATGGTAGAAAAGCGA
GTCTTGGCCCTGCTTGACAAACCCCCGTTCTTGACGCAGCTGCACTCCTGCTTCCAGACA
GTGGATCGGCTGTACTTCGTCATGGAATATGTCAACGGTGGGGACCTCATGTACCACATT
CAGCAAGTAGGAAAATTTAAGGAACCACAAGCAGTATTCTATGTGGCAGAGATTTCCATC
GGATTGTTCTTTCTTCATAAAAGAGGAATCATTTATAGGGATCTGAAGTTAGATAACGTC
ATGTTGGATTCAGAAGGACATATCAAAATTGCTGACTTTGGGATGTGCAAGGAACACATG
ATGGATGGAGTCACGACCAGGACCTTCTGTGGGACTCCAGATTATATCGCCCCAGAGATA
ATCGCTTATCAGCCGTATGGAAAATCTGTGGACTGGTGGGCCTATGGCGTCCTGTTGTAT
GAAATGCTTGCCGGGCAGGTAATGTTTTGCTACATTTTCATGTTTGTTTATTGCTGTGTT
ATGTGA
Enzyme 107 GenBank Gene ID AB209475 Link Image
Enzyme 107 GeneCard ID Not Available
Enzyme 107 GenAtlas ID Not Available
Enzyme 107 HGNC ID HGNC:9393 Link Image
Enzyme 107 Chromosome Location Not Available
Enzyme 107 Locus Not Available
Enzyme 107 SNPs Not Available
Enzyme 107 General References Not Available
Enzyme 107 Metabolite References Not Available
Enzyme 108 [top]
Enzyme 108 ID 17248
Enzyme 108 Name Kinase suppressor of Ras 1
Enzyme 108 Synonyms Not Available
Enzyme 108 Gene Name KSR1
Enzyme 108 Protein Sequence >Kinase suppressor of Ras 1
MDRAALRAAAMGEKKEGGGGGDAAEGGAGAAASRALQQCGQLQKLIDISIGSLRGLRTKC
AVSNDLTQQEIRTLEAKLVRYICKQRQCKLSVAPGERTPELNSYPRFSDWLYTFNVRPEV
VQEIPRDLTLDALLEMNEAKVKETLRRCGASGDECGRLQYALTCLRKVTGLGGEHKEDSS
WSSLDARRESGSGPSTDTLSAASLPWPPGSSQLGRAGNSAQGPRSISVSALPASDSPTPS
FSEGLSDTCIPLHASGRLTPRALHSFITPPTTPQLRRHTKLKPPRTPPPPSRKVFQLLPS
FPTLTRSKSHESQLGNRIDDVSSMRFDLSHGSPQMVRRDIGLSVTHRFSTKSWLSQVCHV
CQKSMIFGVKCKHCRLKCHNKCTKEAPACRISFLPLTRLRRTESVPSDINNPVDRAAEPH
FGTLPKALTKKEHPPAMNHLDSSSNPSSTTSSTPSSPAPFPTSSNPSSATTPPNPSPGQR
DSRFNFPAAYFIHHRQQFIFPVPSAGHCWKCLLIAESLKENAFNISAFAHAAPLPEAADG
TRLDDQPKADVLEAHEAEAEEPEAGKSEAEDDEDEVDDLPSSRRPWRGPISRKASQTSVY
LQEWDIPFEQVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYR
QTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMG
YLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREGRRENQLKLSHDWLCYLAPE
IVREMTPGKDEDQLPFSKAADVYAFGTVWYELQARDWPLKNQAAEASIWQIGSGEGMKRV
LTSVSLGKEVSEILSACWAFDLQERPSFSLLMDMLEKLPKLNRRLSHPGHFWKSAEINSS
KVVPRFERFGLGVLESSNPKM
Enzyme 108 Number of Residues 921
Enzyme 108 Molecular Weight 102030.8
Enzyme 108 Theoretical pI 8.83
Enzyme 108 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 108 General Function Involved in intracellular signaling pathway
Enzyme 108 Specific Function Location-regulated scaffolding protein connecting MEK to RAF. Promotes MEK and RAF phosphorylation and activity through assembly of an activated signaling complex. By itself, it has no demonstrated kinase activity
Enzyme 108 Pathways Not Available
Enzyme 108 Reactions Not Available
Enzyme 108 Pfam Domain Function
Enzyme 108 Signals
  • None
Enzyme 108 Transmembrane Regions
  • None
Enzyme 108 Essentiality Not Available
Enzyme 108 GenBank ID Protein 75677325 Link Image
Enzyme 108 UniProtKB/Swiss-Prot ID Q8IVT5 Link Image
Enzyme 108 UniProtKB/Swiss-Prot Entry Name KSR1_HUMAN Link Image
Enzyme 108 PDB ID Not Available
Enzyme 108 Cellular Location Not Available
Enzyme 108 Gene Sequence Not Available
Enzyme 108 GenBank Gene ID Not Available
Enzyme 108 GeneCard ID KSR1 Link Image
Enzyme 108 GenAtlas ID KSR1 Link Image
Enzyme 108 HGNC ID HGNC:6465 Link Image
Enzyme 108 Chromosome Location 1
Enzyme 108 Locus 17q11.1-q11.2
Enzyme 108 SNPs SNPJam Report Link Image
Enzyme 108 General References
  1. 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]
  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. Therrien M, Chang HC, Solomon NM, Karim FD, Wassarman DA, Rubin GM: KSR, a novel protein kinase required for RAS signal transduction. Cell. 1995 Dec 15;83(6):879-88. [PubMed Link Image]
  4. Roy F, Therrien M: MAP kinase module: the Ksr connection. Curr Biol. 2002 Apr 30;12(9):R325-7. [PubMed Link Image]
  5. 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]
  6. 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]
  7. 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]
  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. 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]
  10. 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]
  11. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 108 Metabolite References Not Available
Enzyme 109 [top]
Enzyme 109 ID 17249
Enzyme 109 Name cDNA, FLJ94469, highly similar to Homo sapiens protein kinase C, epsilon (PRKCE), mRNA
Enzyme 109 Synonyms Not Available
Enzyme 109 Gene Name Not Available
Enzyme 109 Protein Sequence >cDNA, FLJ94469, highly similar to Homo sapiens protein kinase C, epsilon (PRKCE), mRNA
MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKT
NSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLE
PEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQP
TYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVN
MPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIA
KVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELE
NNIRKALPFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFG
KVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKD
RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL
DAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEM
MAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGED
AIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQI
NQEEFKGFSYFGEDLMP
Enzyme 109 Number of Residues 737
Enzyme 109 Molecular Weight 83683.2
Enzyme 109 Theoretical pI 7.13
Enzyme 109 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase C activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 109 General Function Involved in protein serine/threonine kinase activity
Enzyme 109 Specific Function ATP + a protein = ADP + a phosphoprotein
Enzyme 109 Pathways Not Available
Enzyme 109 Reactions Not Available
Enzyme 109 Pfam Domain Function
Enzyme 109 Signals
  • None
Enzyme 109 Transmembrane Regions
  • None
Enzyme 109 Essentiality Not Available
Enzyme 109 GenBank ID Protein 189054067 Link Image
Enzyme 109 UniProtKB/Swiss-Prot ID B2R9M7 Link Image
Enzyme 109 UniProtKB/Swiss-Prot Entry Name B2R9M7_HUMAN Link Image
Enzyme 109 PDB ID Not Available
Enzyme 109 Cellular Location Not Available
Enzyme 109 Gene Sequence >2214 bp
ATGGTAGTGTTCAATGGCCTTCTTAAGATCAAAATCTGCGAGGCCGTGAGCTTGAAGCCC
ACAGCCTGGTCGCTGCGCCATGCGGTGGGACCCCGGCCGCAGACTTTCCTTCTCGACCCC
TACATTGCCCTCAATGTGGACGACTCGCGCATCGGCCAAACGGCCACCAAGCAGAAGACC
AACAGCCCGGCCTGGCACGACGAGTTCGTCACCGATGTGTGCAACGGACGCAAGATCGAG
CTGGCTGTCTTTCACGATGCCCCCATAGGCTACGACGACTTCGTGGCCAACTGCACCATC
CAGTTTGAGGAGCTGCTGCAGAACGGGAGCCGCCACTTCGAGGACTGGATTGATCTGGAG
CCAGAAGGAAGAGTGTATGTGATCATCGATCTCTCAGGGTCGTCGGGTGAAGCCCCTAAA
GACAATGAAGAGCGTGTGTTCAGGGAACGCATGCGGCCGAGGAAGCGGCAGGGGGCCGTC
AGGCGCAGGGTCCATCAGGTCAACGGCCACAAGTTCATGGCCACCTATCTTCGGCAGCCC
ACCTACTGCTCCCATTGCAGAGACTTCATCTGGGGTGTCATAGGAAAGCAGGGATACCAG
TGTCAAGTCTGCACCTGCGTGGTCCACAAGCGGTGCCACGAGCTCATAATCACAAAGTGT
GCTGGGTTAAAGAAGCAGGAGACCCCCGACCAGGTGGGCTCCCAGCGGTTCAGCGTCAAC
ATGCCCCACAAGTTCGGTATCCACAACTACAAGGTCCCTACCTTCTGCGATCACTGTGGG
TCCCTGCTCTGGGGACTCTTGCGGCAGGGTTTGCAGTGTAAAGTCTGCAAAATGAATGTT
CACCGTCGATGTGAGACCAACGTGGCTCCCAACTGTGGAGTGGATGCCAGAGGAATCGCC
AAAGTACTGGCCGACCTGGGCGTTACCCCAGACAAAATCACCAACAGCGGCCAGAGAAGG
AAAAAGCTCATTGCTGGTGCCGAGTCCCCGCAGCCTGCTTCTGGAAGCTCACCATCTGAG
GAAGATCGATCCAAGTCAGCACCCACCTCCCCTTGTGACCAGGAAATAAAAGAACTTGAG
AACAACATTCGGAAAGCCTTGCCATTTGACAACCGAGGAGAGGAGCACCGGGCAGCATCG
TCTCCTGATGGCCAGCTGATGAGCCCCGGTGAGAATGGCGAAGTCCGGCAAGGCCAGGCC
AAGCGCCTGGGCCTGGATGAGTTCAACTTCATCAAGGTGTTGGGCAAAGGCAGCTTTGGC
AAGGTCATGTTGGCAGAACTCAAGGGCAAAGATGAAGTATATGCTGTGAAGGTCTTAAAG
AAGGACGTCATCCTTCAGGATGATGACGTGGACTGCACAATGACAGAGAAGAGGATTTTG
GCTCTGGCACGGAAACACCCGTACCTTACCCAACTCTACTGCTGCTTCCAGACCAAGGAC
CGCCTCTTTTTCGTCATGGAATATGTAAATGGTGGAGACCTCATGTTTCAGATTCAGCGC
TCCCGAAAATTCGACGAGCCTCGTTCACGGTTCTATGCTGCAGAGGTCACATCGGCCCTC
ATGTTCCTCCATCAGCATGGAGTCATCTACAGGGATTTGAAACTGGACAACATCCTTCTG
GATGCAGAAGGTCACTGCAAGCTGGCTGACTTCGGGATGTGCAAGGAAGGGATTCTGAAT
GGTGTGACGACCACCACGTTCTGTGGGACTCCTGACTACATAGCTCCTGAGATCCTGCAG
GAGTTGGAGTATGGCCCCTCCGTGGACTGGTGGGCCCTGGGGGTGCTGATGTACGAGATG
ATGGCTGGACAGCCTCCCTTTGAGGCCGACAATGAGGACGACCTATTTGAGTCCATCCTC
CATGACGACGTGCTGTACCCAGTCTGGCTCAGCAAGGAGGCTGTCAGCATCTTGAAAGCT
TTCATGACGAAGAATCCCCACAAGCGCCTGGGCTGTGTGGCGTCGCAGAATGGCGAGGAC
GCCATCAAGCAGCACCCATTCTTCAAAGAGATTGACTGGGTGCTCCTGGAGCAGAAGAAG
ATCAAGCCACCCTTCAAACCACGCATTAAAACCAAAAGAGACGTCAATAATTTTGACCAA
GACTTTACCCGGGAAGAGCCGGTACTCACCCTTGTGGACGAAGCAATTGTAAAGCAGATC
AACCAGGAGGAATTCAAAGGTTTCTCCTACTTTGGTGAAGACCTGATGCCCTGA
Enzyme 109 GenBank Gene ID AK313842 Link Image
Enzyme 109 GeneCard ID Not Available
Enzyme 109 GenAtlas ID Not Available
Enzyme 109 HGNC ID HGNC:9401 Link Image
Enzyme 109 Chromosome Location Not Available
Enzyme 109 Locus Not Available
Enzyme 109 SNPs Not Available
Enzyme 109 General References Not Available
Enzyme 109 Metabolite References Not Available
Enzyme 110 [top]
Enzyme 110 ID 17250
Enzyme 110 Name Protein kinase C, eta, isoform CRA_a
Enzyme 110 Synonyms
  1. SubName: cDNA FLJ57944, highly similar to Protein kinase C eta type (EC 2.7.11.13)
Enzyme 110 Gene Name PRKCH
Enzyme 110 Protein Sequence >Protein kinase C, eta, isoform CRA_a
MRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTA
CTCQNNINKVDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKM
NVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNG
IGVNSSNRLGIDNFEFIRVLGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTM
TEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAA
EIISALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYI
APEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDA
TGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDV
SNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP
Enzyme 110 Number of Residues 522
Enzyme 110 Molecular Weight 59520.3
Enzyme 110 Theoretical pI 7.48
Enzyme 110 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 110 General Function Involved in protein serine/threonine kinase activity
Enzyme 110 Specific Function ATP + a protein = ADP + a phosphoprotein
Enzyme 110 Pathways Not Available
Enzyme 110 Reactions Not Available
Enzyme 110 Pfam Domain Function
Enzyme 110 Signals
  • None
Enzyme 110 Transmembrane Regions
  • None
Enzyme 110 Essentiality Not Available
Enzyme 110 GenBank ID Protein 194382284 Link Image
Enzyme 110 UniProtKB/Swiss-Prot ID B4DJN5 Link Image
Enzyme 110 UniProtKB/Swiss-Prot Entry Name B4DJN5_HUMAN Link Image
Enzyme 110 PDB ID Not Available
Enzyme 110 Cellular Location Not Available
Enzyme 110 Gene Sequence >1569 bp
ATGCGAAGGCGAGTCCACCAGATCAATGGACACAAGTTCATGGCCACGTATCTGAGGCAG
CCCACCTACTGCTCTCACTGCAGGGAGTTTATCTGGGGAGTGTTTGGGAAACAGGGTTAT
CAGTGCCAAGTGTGCACCTGTGTCGTCCATAAACGCTGCCATCATCTAATTGTTACAGCC
TGTACTTGCCAAAACAATATTAACAAAGTGGATTCAAAGATTGCAGAACAGAGGTTCGGG
ATCAACATCCCACACAAGTTCAGCATCCACAACTACAAAGTGCCAACATTCTGCGATCAC
TGTGGCTCACTGCTCTGGGGAATAATGCGACAAGGACTTCAGTGTAAAATATGTAAAATG
AATGTGCATATTCGATGTCAAGCGAACGTGGCCCCTAACTGTGGGGTAAATGCGGTGGAA
CTTGCCAAGACCCTGGCAGGGATGGGTCTCCAACCCGGAAATATTTCTCCAACCTCGAAA
CTCGTTTCCAGATCGACCCTAAGACGACAGGGAAAGGAGAGCAGCAAAGAAGGAAATGGG
ATTGGGGTTAATTCTTCCAACCGACTTGGTATCGACAACTTTGAGTTCATCCGAGTGTTG
GGGAAGGGGAGTTTTGGGAAGGTGATGCTTGCAAGAGTAAAAGAAACAGGAGACCTCTAT
GCTGTGAAGGTGCTGAAGAAGGACGTGATTCTGCAGGATGATGATGTGGAATGCACCATG
ACCGAGAAAAGGATCCTGTCTCTGGCCCGCAATCACCCCTTCCTCACTCAGTTGTTCTGC
TGCTTTCAGACCCCCGATCGTCTGTTTTTTGTGATGGAGTTTGTGAATGGGGGTGACTTG
ATGTTCCACATTCAGAAGTCTCGTCGTTTTGATGAAGCACGAGCTCGCTTCTATGCTGCA
GAAATCATTTCGGCTCTCATGTTCCTCCATGATAAAGGAATCATCTATAGAGATCTGAAA
CTGGACAATGTCCTGTTGGACCACGAGGGTCACTGTAAACTGGCAGACTTCGGAATGTGC
AAGGAGGGGATTTGCAATGGTGTCACCACGGCCACATTCTGTGGCACGCCAGACTATATC
GCTCCAGAGATCCTCCAGGAAATGCTGTACGGGCCTGCAGTAGACTGGTGGGCAATGGGC
GTGTTGCTCTATGAGATGCTCTGTGGTCACGCGCCTTTTGAGGCAGAGAATGAAGATGAC
CTCTTTGAGGCCATACTGAATGATGAGGTGGTCTACCCTACCTGGCTCCATGAAGATGCC
ACAGGGATCCTAAAATCTTTCATGACCAAGAACCCCACCATGCGCTTGGGCAGCCTGACT
CAGGGAGGCGAGCACGCCATCTTGAGACATCCTTTTTTTAAGGAAATCGACTGGGCCCAG
CTGAACCATCGCCAAATAGAACCGCCTTTCAGACCCAGAATCAAATCCCGAGAAGATGTC
AGTAATTTTGACCCTGACTTCATAAAGGAAGAGCCAGTTTTAACTCCAATTGATGAGGGA
CATCTTCCAATGATTAACCAGGATGAGTTTAGAAACTTTTCCTATGTGTCTCCAGAATTG
CAACCATAG
Enzyme 110 GenBank Gene ID AK296158 Link Image
Enzyme 110 GeneCard ID PRKCH Link Image
Enzyme 110 GenAtlas ID PRKCH Link Image
Enzyme 110 HGNC ID HGNC:9403 Link Image
Enzyme 110 Chromosome Location 1
Enzyme 110 Locus 14q23.1
Enzyme 110 SNPs SNPJam Report Link Image
Enzyme 110 General References
  1. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 110 Metabolite References Not Available
Enzyme 111 [top]
Enzyme 111 ID 17251
Enzyme 111 Name cDNA, FLJ96384, highly similar to Homo sapiens protein kinase C, iota (PRKCI), mRNA
Enzyme 111 Synonyms Not Available
Enzyme 111 Gene Name Not Available
Enzyme 111 Protein Sequence >cDNA, FLJ96384, highly similar to Homo sapiens protein kinase C, iota (PRKCI), mRNA
MSHTVAGGGSGDHSHQVRVKAYYRGDIMITHFEPSISFEGLCNEVRDMCSFDNEQLFTMK
WIDEEGDPCTVSSQLELEEAFRLYELNKDSELLIHVFPCVPERPGMPCPGEDKSIYRRGA
RRWRKLYCANGHTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHKKCHKLVTIE
CGRHSLPQEPVMPMDQSSMHSDHAQTVIPYNPSSHESLDQVGEEKEAMNTRESGKASSSL
GLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQTEKHVFEQA
SNHPFLVGLHSCFQTESRLFFVIEHVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYL
HERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGED
YGFSVDWWALGVLMFEMVAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKA
ASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEFGL
DNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV
Enzyme 111 Number of Residues 587
Enzyme 111 Molecular Weight 67199.7
Enzyme 111 Theoretical pI 5.76
Enzyme 111 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • metal ion binding
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • zinc ion binding
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 111 General Function Involved in protein serine/threonine kinase activity
Enzyme 111 Specific Function ATP + a protein = ADP + a phosphoprotein
Enzyme 111 Pathways Not Available
Enzyme 111 Reactions Not Available
Enzyme 111 Pfam Domain Function
Enzyme 111 Signals
  • None
Enzyme 111 Transmembrane Regions
  • None
Enzyme 111 Essentiality Not Available
Enzyme 111 GenBank ID Protein 189067482 Link Image
Enzyme 111 UniProtKB/Swiss-Prot ID B2RCZ4 Link Image
Enzyme 111 UniProtKB/Swiss-Prot Entry Name B2RCZ4_HUMAN Link Image
Enzyme 111 PDB ID Not Available
Enzyme 111 Cellular Location Not Available
Enzyme 111 Gene Sequence >1764 bp
ATGTCCCACACGGTCGCAGGCGGCGGCAGCGGGGACCATTCCCACCAGGTCCGGGTGAAA
GCCTACTACCGCGGGGATATCATGATAACACATTTTGAACCTTCCATCTCCTTTGAGGGC
CTTTGCAATGAGGTTCGAGACATGTGTTCTTTTGACAACGAACAGCTCTTCACCATGAAA
TGGATAGATGAGGAAGGAGACCCGTGTACAGTATCATCTCAGTTGGAGTTAGAAGAAGCC
TTTAGACTTTATGAGCTAAACAAGGATTCTGAACTCTTGATTCATGTGTTCCCTTGTGTA
CCAGAACGTCCTGGGATGCCTTGTCCAGGAGAAGATAAATCCATCTACCGTAGAGGTGCA
CGCCGCTGGAGAAAGCTTTATTGTGCCAATGGCCACACTTTCCAAGCCAAGCGTTTCAAC
AGGCGTGCTCACTGTGCCATCTGCACAGACCGAATATGGGGACTTGGACGCCAAGGATAT
AAGTGCATCAACTGCAAACTCTTGGTTCATAAGAAGTGCCATAAACTCGTCACAATTGAA
TGTGGGCGGCATTCTTTGCCACAGGAACCAGTGATGCCCATGGATCAGTCATCCATGCAT
TCTGACCATGCACAGACAGTAATTCCATATAATCCTTCAAGTCATGAGAGTTTGGATCAA
GTTGGTGAAGAAAAAGAGGCAATGAACACCAGGGAAAGTGGCAAAGCTTCATCCAGTCTA
GGTCTTCAGGATTTTGATTTGCTCCGGGTAATAGGAAGAGGAAGTTATGCCAAAGTACTG
TTGGTTCGATTAAAAAAAACAGATCGTATTTATGCAATGAAAGTTGTGAAAAAAGAGCTT
GTTAATGATGATGAGGATATTGATTGGGTACAGACAGAGAAGCATGTGTTTGAGCAGGCA
TCCAATCATCCTTTCCTTGTTGGGCTGCATTCTTGCTTTCAGACAGAAAGCAGATTGTTC
TTTGTTATAGAGCATGTAAATGGAGGAGACCTAATGTTTCATATGCAGCGACAAAGAAAA
CTTCCTGAAGAACATGCCAGATTTTACTCTGCAGAAATCAGTCTAGCATTAAATTATCTT
CATGAGCGAGGGATAATTTATAGAGATTTGAAACTGGACAATGTATTACTGGACTCTGAA
GGCCACATTAAACTCACTGACTACGGCATGTGTAAGGAAGGATTACGGCCAGGAGATACA
ACCAGCACTTTCTGTGGTACTCCTAATTACATTGCTCCTGAAATTTTAAGAGGAGAAGAT
TATGGTTTCAGTGTTGACTGGTGGGCTCTTGGAGTGCTCATGTTTGAGATGGTGGCAGGA
AGGTCTCCATTTGATATTGTTGGGAGCTCCGATAACCCTGACCAGAACACAGAGGATTAT
CTCTTCCAAGTTATTTTGGAAAAACAAATTCGCATACCACGTTCTCTGTCTGTAAAAGCT
GCAAGTGTTCTGAAGAGTTTTCTTAATAAGGACCCTAAGGAACGATTGGGTTGTCATCCT
CAAACAGGATTTGCTGATATTCAGGGACACCCGTTCTTCCGAAATGTTGATTGGGATATG
ATGGAGCAAAAACAGGTGGTACCTCCCTTTAAACCAAATATTTCTGGGGAATTTGGTTTG
GACAACTTTGATTCTCAGTTTACTAATGAACCTGTCCAGCTCACTCCAGATGACGATGAC
ATTGTGAGGAAGATTGATCAGTCTGAATTTGAAGGTTTTGAGTATATCAATCCTCTTTTG
ATGTCTGCAGAAGAATGTGTCTGA
Enzyme 111 GenBank Gene ID AK315342 Link Image
Enzyme 111 GeneCard ID Not Available
Enzyme 111 GenAtlas ID Not Available
Enzyme 111 HGNC ID HGNC:9404 Link Image
Enzyme 111 Chromosome Location Not Available
Enzyme 111 Locus Not Available
Enzyme 111 SNPs Not Available
Enzyme 111 General References Not Available
Enzyme 111 Metabolite References Not Available
Enzyme 112 [top]
Enzyme 112 ID 17252
Enzyme 112 Name cDNA FLJ57052, highly similar to Protein kinase C delta type (EC 2.7.11.13)
Enzyme 112 Synonyms Not Available
Enzyme 112 Gene Name Not Available
Enzyme 112 Protein Sequence >cDNA FLJ57052, highly similar to Protein kinase C delta type (EC 2.7.11.13)
MRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRS
EDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCN
AAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWG
LVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIY
QGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGE
YFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGG
DLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFG
MCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDE
DELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEK
RRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHL
LED
Enzyme 112 Number of Residues 603
Enzyme 112 Molecular Weight 69155.8
Enzyme 112 Theoretical pI 7.83
Enzyme 112 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase C activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 112 General Function Involved in protein serine/threonine kinase activity
Enzyme 112 Specific Function ATP + a protein = ADP + a phosphoprotein
Enzyme 112 Pathways Not Available
Enzyme 112 Reactions Not Available
Enzyme 112 Pfam Domain Function
Enzyme 112 Signals
  • None
Enzyme 112 Transmembrane Regions
  • None
Enzyme 112 Essentiality Not Available
Enzyme 112 GenBank ID Protein 194376832 Link Image
Enzyme 112 UniProtKB/Swiss-Prot ID B4DFV1 Link Image
Enzyme 112 UniProtKB/Swiss-Prot Entry Name B4DFV1_HUMAN Link Image
Enzyme 112 PDB ID Not Available
Enzyme 112 Cellular Location Not Available
Enzyme 112 Gene Sequence >1812 bp
ATGCGGGCAGCAGAGGAGCCAGTGTCTGAGGTGACCGTGGGTGTGTCGGTGCTGGCCGAG
CGCTGCAAGAAGAACAATGGCAAGGCTGAGTTCTGGCTGGACCTGCAGCCTCAGGCCAAG
GTGTTGATGTCTGTTCAGTATTTCCTGGAGGACGTGGATTGCAAACAGTCTATGCGCAGT
GAGGACGAGGCCAAGTTCCCAACGATGAACCGCCGCGGAGCCATCAAACAGGCCAAAATC
CACTACATCAAGAACCATGAGTTTATCGCCACCTTCTTTGGGCAACCCACCTTCTGTTCT
GTGTGCAAAGACTTTGTCTGGGGCCTCAACAAGCAAGGCTACAAATGCAGGCAATGTAAC
GCTGCCATCCACAAGAAATGCATCGACAAGATCATCGGCAGATGCACTGGCACCGCGGCC
AACAGCCGGGACACTATATTCCAGAAAGAACGCTTCAACATCGACATGCCGCACCGCTTC
AAGGTTCACAACTACATGAGCCCCACCTTCTGTGACCACTGCGGCAGCCTGCTCTGGGGA
CTGGTGAAGCAGGGATTAAAGTGTGAAGACTGCGGCATGAATGTGCACCATAAATGCCGG
GAGAAGGTGGCCAACCTCTGCGGCATCAACCAGAAGCTTTTGGCTGAGGCCTTGAACCAA
GTCACCCAGAGAGCCTCCCGGAGATCAGACTCAGCCTCCTCAGAGCCTGTTGGGATATAT
CAGGGTTTCGAGAAGAAGACCGGAGTTGCTGGGGAGGACATGCAAGACAACAGTGGGACC
TACGGCAAGATCTGGGAGGGCAGCAGCAAGTGCAACATCAACAACTTCATCTTCCACAAG
GTCCTGGGCAAAGGCAGCTTCGGGAAGGTGCTGCTTGGAGAGCTGAAGGGCAGAGGAGAA
TACTTTGCCATCAAGGCCCTCAAGAAGGATGTGGTCCTGATCGACGACGACGTGGAGTGC
ACCATGGTTGAGAAGCGGGTGCTGACACTTGCCGCAGAGAATCCCTTTCTCACCCACCTC
ATCTGCACCTTCCAGACCAAGGACCACCTGTTCTTTGTGATGGAGTTCCTCAACGGGGGG
GACCTGATGTACCACATCCAGGACAAAGGCCGCTTTGAACTCTACCGTGCCACGTTTTAT
GCCGCTGAGATAATGTGTGGACTGCAGTTTCTACACAGCAAGGGCATCATTTACAGGGAC
CTCAAACTGGACAATGTGCTGCTGGACCGGGATGGCCACATCAAGATTGCCGACTTTGGG
ATGTGCAAAGAGAACATATTCGGGGAGAGCCGGGCCAGCACCTTCTGCGGCACCCCTGAC
TATATCGCCCCTGAGATCCTACAGGGCCTGAAGTACACATTCTCTGTGGACTGGTGGTCT
TTCGGGGTCCTTCTGTACGAGATGCTCATTGGCCAGTCCCCCTTCCATGGTGATGATGAG
GATGAACTCTTCGAGTCCATCCGTGTGGACACGCCACATTATCCCCGCTGGATCACCAAG
GAGTCCAAGGACATCCTGGAGAAGCTCTTTGAAAGGGAACCAACCAAGAGGCTGGGAGTG
ACGGGAAACATCAAAATCCACCCCTTCTTCAAGACCATAAACTGGACTCTGCTGGAAAAG
CGGAGGTTGGAGCCACCCTTCAGGCCCAAAGTGAAGTCACCCAGAGACTACAGTAACTTT
GACCAGGAGTTCCTGAACGAGAAGGCGCGCCTCTCCTACAGCGACAAGAACCTCATCGAC
TCCATGGACCAGTCTGCATTCGCTGGCTTCTCCTTTGTGAACCCCAAATTCGAGCACCTC
CTGGAAGATTGA
Enzyme 112 GenBank Gene ID AK294272 Link Image
Enzyme 112 GeneCard ID Not Available
Enzyme 112 GenAtlas ID Not Available
Enzyme 112 HGNC ID HGNC:9399 Link Image
Enzyme 112 Chromosome Location Not Available
Enzyme 112 Locus Not Available
Enzyme 112 SNPs Not Available
Enzyme 112 General References Not Available
Enzyme 112 Metabolite References Not Available
Enzyme 113 [top]
Enzyme 113 ID 17253
Enzyme 113 Name Protein kinase C, gamma variant
Enzyme 113 Synonyms Not Available
Enzyme 113 Gene Name Not Available
Enzyme 113 Protein Sequence >Protein kinase C, gamma variant
DPGPCYVSGAMAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCS
HCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSS
PTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTA
DEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVL
Enzyme 113 Number of Residues 239
Enzyme 113 Molecular Weight 26658.6
Enzyme 113 Theoretical pI 8.93
Enzyme 113 GO Classification
Function
Process
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 113 General Function Involved in intracellular signaling pathway
Enzyme 113 Specific Function Not Available
Enzyme 113 Pathways Not Available
Enzyme 113 Reactions Not Available
Enzyme 113 Pfam Domain Function
Enzyme 113 Signals
  • None
Enzyme 113 Transmembrane Regions
  • None
Enzyme 113 Essentiality Not Available
Enzyme 113 GenBank ID Protein 62088922 Link Image
Enzyme 113 UniProtKB/Swiss-Prot ID Q59EZ0 Link Image
Enzyme 113 UniProtKB/Swiss-Prot Entry Name Q59EZ0_HUMAN Link Image
Enzyme 113 PDB ID 1TBO Link Image
Enzyme 113 PDB File Show
Enzyme 113 3D Structure
Enzyme 113 Cellular Location Not Available
Enzyme 113 Gene Sequence >720 bp
GATCCTGGTCCCTGCTACGTTTCTGGGGCCATGGCTGGTCTGGGCCCCGGCGTAGGCGAT
TCAGAGGGGGGACCCCGGCCCCTGTTTTGCAGAAAGGGGGCTCTGAGGCAGAAGGTGGTC
CACGAAGTCAAGAGCCACAAGTTCACCGCTCGCTTCTTCAAGCAGCCCACCTTCTGCAGC
CACTGCACCGACTTCATCTGGGGTATCGGAAAGCAGGGCCTGCAATGTCAAGTCTGCAGC
TTTGTGGTTCATCGACGATGCCACGAATTTGTGACCTTCGAGTGTCCAGGCGCTGGGAAG
GGCCCCCAGACGGACGACCCCCGGAACAAACACAAGTTCCGCCTGCATAGCTACAGCAGC
CCCACCTTCTGCGACCACTGTGGCTCCCTCCTCTACGGGCTTGTGCACCAGGGCATGAAA
TGCTCCTGCTGCGAGATGAACGTGCACCGGCGCTGTGTGCGTAGCGTGCCCTCCCTGTGC
GGTGTGGACCACACCGAGCGCCGCGGGCGCCTGCAGCTGGAGATCCGGGCTCCCACAGCA
GATGAGATCCACGTAACTGTTGGCGAGGCCCGTAACCTAATTCCTATGGACCCCAATGGT
CTCTCTGATCCCTATGTGAAACTGAAGCTCATCCCAGACCCTCGGAACCTGACGAAACAG
AAGACCCGAACGGTGAAAGCCACGCTAAACCCTGTGTGGAATGAGACCTTTGTGTTGTGA
Enzyme 113 GenBank Gene ID AB209671 Link Image
Enzyme 113 GeneCard ID Not Available
Enzyme 113 GenAtlas ID Not Available
Enzyme 113 HGNC ID HGNC:9402 Link Image
Enzyme 113 Chromosome Location Not Available
Enzyme 113 Locus Not Available
Enzyme 113 SNPs Not Available
Enzyme 113 General References Not Available
Enzyme 113 Metabolite References Not Available
Enzyme 114 [top]
Enzyme 114 ID 17254
Enzyme 114 Name CDC42-binding protein kinase beta
Enzyme 114 Synonyms Not Available
Enzyme 114 Gene Name CDC42BPA
Enzyme 114 Protein Sequence >CDC42-binding protein kinase beta
MSGEVRLRQLEQFILDGPAQTNGQCFSVETLLDILICLYDECNNSPLRREKNILEYLEWA
KPFTSKVKQMRLHREDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETA
CFREERDVLVNGDNKWITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFEDRLPEDMARF
YLAEMVIAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAVGT
PDYISPEILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKER
FQFPAQVTDVSENAKDPIRRLICGREHRLGQSGIEDFKKHPFFSGIDWDNIRNCEAPYIP
EVSSPTDTSNFDVDDDCLKNSETMPPPTHTAFSGHHLPFVGFTYTSSCVLSDRSCLRVTA
GPTSLDLDVNVQRTLDNNLATEAYERRIKRLEQEKLELSRKLQESTQTVQALQYSTVDGP
LTASKDLEIKNLKEVIEKLRKQVTESSHLEQQLEEANAVRQELDDAFRQIKAYEKQIKTL
QQEREDLNKLEVHTEALAAEASKDRKLREQSEHYSKQLENELEGLKQKQISYSPGVCSIE
HQQEITKLKTDLEKKSIFYEEELSKREGIHANEIKNLKKELHDSEGQQLALNKEIMILKD
KLEKTRRESQSEREEFESEFKQQYEREKVLLTEENKKLTSELDKLTTLYENLSIHNQQLE
EEVKDLADKKESVAHWEAQITEIIQWVSDEKDARGYLQALASKMTEELEALRNSSLGTRA
TDMPWKMRRFAKLDMSARLELQSALDAEIRAKQAIQEELNKVKASNIITECKLKDSEKKN
LELLSEIEQLIKDTEELRSEKGIEHQDSQHSFLAFLNTPTDALDQFETVDSTPLSVHTPT
LRKKGCPGSTGFPPKRKTHQFFVKSFTTPTKCHQCTSLMVGLIRQGCSCEVCGFSCHITC
VNKAPTTCPVPPEQTKGPLGIDPQKGIGTAYEGHVRIPKPAGVKKGWQRALAIVCDFKLF
LYDIAEGKASQPSVVISQVIDMRDEEFSVSSVLASDVIHASRKDIPCIFRVTASQLSASN
NKCSILMLADTENEKNKWVGVLSELHKILKKNKFRDRSVYVPKEAYDSTLPLIKTTQAAA
IIDHERIALGNEEGLFVVHVTKDEIIRVGDNKKIHQIELIPNDQLVAVISGRNRHVRLFP
MSALDGRETDFYKLSETKGCQTVTSGKVRHGALTCLCVAMKRQVLCYELFQSKTRHRKFK
EIQVPYNVQWMAIFSEQLCVGFQSGFLRYPLNGEGNPYSMLHSNDHTLSFIAHQPMDAIC
AVEISSKEYLLCFNSIGIYTDCQGRRSRQQELMWPANPSSCCYNAPYLSVYSENAVDIFD
VNSMEWIQTLPLKKVRPLNNEGSLNLLGLETIRLIYFKNKMAEGDELVVPETSDNSRKQM
VRNINNKRRYSFRVPEEERMQQRREMLRDPEMRNKLISNPTNFNHIAHMGPGDGIQILKD
LPMNPRPQESRTVFSGSVSIPSITKSRPEPGRSMSASSGLSARSSAQNGSALKREFSGGS
YSAKRQPMPSPSEGSLSSGGMDQGSDAPARDFDGEDSDSPRHSTASNSSNLSSPPSPVSP
RKTKSLSLESTDRGSWDP
Enzyme 114 Number of Residues 1638
Enzyme 114 Molecular Weight 186036.4
Enzyme 114 Theoretical pI 6.31
Enzyme 114 GO Classification
Function
  • ATP binding
  • GTPase regulator activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • enzyme regulator activity
  • kinase activity
  • nucleoside binding
  • nucleoside-triphosphatase regulator activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • small GTPase regulator activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 114 General Function Involved in protein serine/threonine kinase activity
Enzyme 114 Specific Function ATP + a protein = ADP + a phosphoprotein
Enzyme 114 Pathways Not Available
Enzyme 114 Reactions Not Available
Enzyme 114 Pfam Domain Function
Enzyme 114 Signals
  • None
Enzyme 114 Transmembrane Regions
  • None
Enzyme 114 Essentiality Not Available
Enzyme 114 GenBank ID Protein 27261723 Link Image
Enzyme 114 UniProtKB/Swiss-Prot ID Q8IWQ7 Link Image
Enzyme 114 UniProtKB/Swiss-Prot Entry Name Q8IWQ7_HUMAN Link Image
Enzyme 114 PDB ID Not Available
Enzyme 114 Cellular Location Not Available
Enzyme 114 Gene Sequence >4917 bp
ATGTCTGGAGAAGTGCGTTTGAGGCAGTTGGAGCAGTTTATTTTGGACGGGCCCGCTCAG
ACCAATGGGCAGTGCTTCAGTGTGGAGACGTTACTGGATATACTCATCTGCCTTTATGAT
GAATGCAATAATTCTCCATTGAGAAGAGAGAAGAACATTCTCGAATACCTAGAATGGGCT
AAACCATTTACTTCTAAAGTGAAACAAATGCGATTACATAGAGAAGACTTTGAAATATTA
AAGGTGATTGGTCGAGGAGCTTTTGGGGAGGTTGCTGTAGTAAAACTAAAAAATGCAGAT
AAAGTGTTTGCCATGAAAATATTGAATAAATGGGAAATGCTGAAAAGAGCTGAGACAGCA
TGTTTTCGTGAAGAAAGGGATGTATTAGTGAATGGAGACAATAAATGGATTACAACCTTG
CACTATGCTTTCCAGGATGACAATAACTTATACCTGGTTATGGATTATTATGTTGGTGGG
GATTTGCTTACTCTACTCAGCAAATTTGAAGATAGATTGCCTGAAGATATGGCTAGATTT
TACTTGGCTGAGATGGTGATAGCAATTGACTCAGTTCATCAGCTACATTATGTACACAGA
GACATTAAACCTGACAATATACTGATGGATATGAATGGACATATTCGGTTAGCAGATTTT
GGTTCTTGTCTGAAGCTGATGGAAGATGGAACGGTTCAGTCCTCAGTGGCTGTAGGAACT
CCAGATTATATCTCTCCTGAAATCCTTCAAGCCATGGAAGATGGAAAAGGGAGATATGGA
CCTGAATGTGACTGGTGGTCTTTGGGGGTCTGTATGTATGAAATGCTTTACGGAGAAACA
CCATTTTATGCAGAATCGCTGGTGGAGACATACGGAAAAATCATGAACCACAAAGAGAGG
TTTCAGTTTCCAGCCCAAGTGACTGATGTGTCTGAAAATGCTAAGGATCCTATTCGAAGG
CTCATTTGTGGCAGAGAACATCGACTTGGTCAAAGTGGAATAGAAGACTTTAAGAAACAC
CCATTTTTCAGTGGAATTGACTGGGATAATATTCGGAACTGTGAAGCACCTTATATTCCA
GAAGTTAGTAGCCCAACAGATACATCGAATTTTGATGTAGATGATGATTGTTTAAAAAAT
TCTGAAACGATGCCCCCACCAACACATACTGCATTTTCTGGCCACCATCTGCCATTTGTT
GGTTTTACATATACTAGTAGCTGTGTACTTTCTGATCGGAGCTGTTTAAGAGTTACGGCT
GGTCCCACCTCACTGGATCTTGATGTTAATGTTCAGAGGACTCTAGACAACAACTTAGCA
ACTGAAGCTTATGAAAGAAGAATTAAGCGCCTTGAGCAAGAAAAACTTGAACTCAGTAGA
AAACTTCAAGAGTCAACACAGACTGTCCAAGCTCTGCAGTATTCAACTGTTGATGGTCCA
CTAACAGCAAGCAAAGATTTAGAAATAAAAAACTTAAAAGAAGTAATTGAAAAACTAAGA
AAACAAGTAACAGAATCAAGTCATTTGGAACAGCAACTTGAAGAAGCTAATGCTGTGAGG
CAAGAACTAGATGATGCTTTTAGACAAATCAAGGCTTATGAAAAACAAATCAAAACGTTA
CAACAAGAAAGAGAAGATCTAAATAAGCTGGAAGTTCATACAGAAGCTCTAGCTGCTGAA
GCATCTAAAGACAGGAAGCTACGTGAACAGAGTGAGCACTATTCTAAGCAACTGGAAAAT
GAATTGGAGGGACTGAAGCAAAAACAAATTAGTTACTCACCAGGAGTATGCAGCATAGAA
CATCAGCAAGAGATAACCAAACTAAAGACTGATTTGGAAAAGAAAAGTATCTTTTATGAA
GAAGAATTATCTAAAAGAGAAGGAATACATGCAAATGAAATAAAAAATCTTAAGAAAGAA
CTGCATGATTCAGAAGGTCAGCAACTTGCTCTCAACAAAGAAATTATGATTTTAAAAGAC
AAATTGGAAAAAACCAGAAGAGAAAGTCAAAGTGAAAGGGAGGAATTTGAAAGTGAGTTC
AAACAACAATATGAACGAGAAAAAGTGTTGTTAACTGAAGAAAATAAAAAGCTGACGAGT
GAACTTGATAAGCTTACTACTTTGTATGAGAACTTAAGTATACACAACCAGCAGTTAGAA
GAAGAGGTTAAAGATCTAGCAGACAAGAAAGAATCAGTTGCACATTGGGAAGCCCAAATC
ACAGAAATAATTCAGTGGGTCAGCGATGAAAAGGATGCACGAGGGTATCTTCAGGCCTTA
GCTTCTAAAATGACTGAAGAATTGGAGGCATTAAGAAATTCCAGCTTGGGTACACGAGCA
ACAGATATGCCCTGGAAAATGCGTCGTTTTGCGAAACTGGATATGTCAGCTAGACTGGAG
TTGCAGTCGGCTCTGGATGCAGAAATAAGAGCCAAACAGGCCATCCAAGAAGAGTTGAAT
AAAGTTAAAGCATCTAATATCATAACAGAATGTAAACTAAAAGATTCAGAGAAGAAGAAC
TTGGAACTACTCTCAGAAATCGAACAGCTGATAAAGGACACTGAAGAGCTTAGATCTGAA
AAGGGTATAGAGCACCAAGACTCACAGCATTCTTTCTTGGCATTTTTGAATACGCCTACC
GATGCTCTGGATCAATTTGAAACTGTAGACTCCACTCCACTTTCAGTTCACACACCAACC
TTAAGGAAAAAAGGATGTCCTGGTTCAACTGGCTTTCCACCTAAGCGCAAGACTCACCAG
TTTTTTGTAAAATCTTTTACTACTCCTACCAAGTGTCATCAGTGTACCTCCTTGATGGTG
GGTTTAATAAGACAGGGCTGTTCATGTGAAGTGTGTGGATTCTCATGCCATATAACTTGT
GTAAACAAAGCTCCAACCACTTGTCCAGTTCCTCCTGAACAGACAAAAGGTCCCCTGGGT
ATAGATCCTCAGAAAGGAATAGGAACAGCATATGAAGGTCATGTCAGGATTCCTAAGCCA
GCTGGAGTGAAGAAAGGGTGGCAGAGAGCACTGGCTATAGTGTGTGACTTCAAACTCTTT
CTGTACGATATTGCTGAAGGAAAAGCATCTCAGCCCAGTGTTGTCATTAGTCAAGTGATT
GACATGAGGGATGAAGAATTTTCTGTGAGTTCAGTCTTGGCTTCTGATGTTATCCATGCA
AGTCGGAAAGATATACCCTGTATATTTAGGGTCACAGCTTCCCAGCTCTCAGCATCTAAT
AACAAATGTTCAATCCTGATGCTAGCAGACACTGAGAATGAGAAGAATAAGTGGGTGGGA
GTGCTGAGTGAATTGCACAAGATTTTGAAGAAAAACAAATTCAGAGACCGCTCAGTCTAT
GTTCCCAAAGAGGCTTATGACAGCACTCTACCCCTCATTAAAACAACCCAGGCAGCCGCA
ATCATAGATCATGAAAGAATTGCTTTGGGAAACGAAGAAGGGTTATTTGTTGTACATGTC
ACCAAAGATGAAATTATTAGAGTTGGTGACAATAAGAAGATTCATCAGATTGAACTCATT
CCAAATGATCAGCTTGTTGCTGTGATCTCAGGACGAAATCGTCATGTACGACTTTTTCCT
ATGTCAGCATTGGATGGGCGAGAGACCGATTTTTACAAGCTGTCAGAAACTAAAGGGTGT
CAAACCGTAACTTCTGGAAAGGTGCGCCATGGAGCTCTCACATGCCTGTGTGTGGCTATG
AAAAGGCAGGTCCTCTGTTATGAACTATTTCAGAGCAAGACCCGTCACAGAAAATTTAAA
GAAATTCAAGTCCCATATAATGTCCAGTGGATGGCAATCTTCAGTGAACAACTCTGTGTG
GGATTCCAGTCAGGATTTCTAAGATACCCCTTGAATGGAGAAGGAAATCCATACAGTATG
CTCCATTCAAATGACCATACACTATCATTTATTGCACATCAACCAATGGATGCTATCTGC
GCAGTTGAGATCTCCAGTAAAGAATATCTGCTGTGTTTTAACAGCATTGGGATATACACT
GACTGCCAGGGCCGAAGATCTAGACAACAGGAATTGATGTGGCCAGCAAATCCTTCCTCT
TGTTGTTACAATGCACCATATCTCTCGGTGTACAGTGAAAATGCAGTTGATATCTTTGAT
GTGAACTCCATGGAATGGATTCAGACTCTTCCTCTCAAAAAGGTTCGACCCTTAAACAAT
GAAGGATCATTAAATCTTTTAGGGTTGGAGACCATTAGATTAATATATTTCAAAAATAAG
ATGGCAGAAGGGGACGAACTGGTAGTACCTGAAACATCAGATAATAGTCGGAAACAAATG
GTTAGAAACATTAACAATAAGCGGCGTTATTCCTTCAGAGTCCCAGAAGAGGAAAGGATG
CAGCAGAGGAGGGAAATGCTACGAGATCCAGAAATGAGAAATAAATTAATTTCTAATCCA
ACTAATTTTAATCACATAGCACACATGGGTCCTGGAGATGGAATACAGATCCTGAAAGAT
CTGCCCATGAACCCTCGGCCTCAGGAAAGTCGGACAGTATTCAGTGGCTCAGTCAGTATT
CCATCTATCACCAAATCCCGCCCTGAGCCAGGCCGCTCCATGAGTGCTAGCAGTGGCTTG
TCAGCAAGGTCATCCGCACAGAATGGCAGCGCATTAAAGAGGGAATTCTCTGGAGGAAGC
TACAGTGCCAAGCGGCAGCCCATGCCCTCCCCGTCAGAGGGCTCTTTGTCCTCCGGAGGC
ATGGACCAAGGAAGTGATGCCCCAGCGAGGGACTTTGACGGAGAGGACTCTGACTCTCCG
AGGCATTCCACAGCTTCCAACAGTTCCAACCTAAGCAGCCCCCCAAGCCCAGTTTCACCC
CGAAAAACCAAGAGCCTCTCCCTGGAGAGCACTGACCGCGGGAGCTGGGACCCGTGA
Enzyme 114 GenBank Gene ID AY166586 Link Image
Enzyme 114 GeneCard ID CDC42BPA Link Image
Enzyme 114 GenAtlas ID CDC42BPA Link Image
Enzyme 114 HGNC ID HGNC:1737 Link Image
Enzyme 114 Chromosome Location 1
Enzyme 114 Locus 1q42.11
Enzyme 114 SNPs SNPJam Report Link Image
Enzyme 114 General References Not Available
Enzyme 114 Metabolite References Not Available
Enzyme 115 [top]
Enzyme 115 ID 17260
Enzyme 115 Name PRKCA protein
Enzyme 115 Synonyms Not Available
Enzyme 115 Gene Name PRKCA
Enzyme 115 Protein Sequence >PRKCA protein
ASQRLRLPLPLRAAPARLSPAPAAPPRRDLGHRPAPRARGRPEPAPLPRRPRPPGPPRPQ
LPGGGKRWLGGTMADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPT
FCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHT
YGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEV
ADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFT
FKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNV
PIPEGDEEGNMELRQKFEWR
Enzyme 115 Number of Residues 380
Enzyme 115 Molecular Weight 43185.1
Enzyme 115 Theoretical pI 9.76
Enzyme 115 GO Classification
Function
Process
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 115 General Function Involved in intracellular signaling pathway
Enzyme 115 Specific Function Not Available
Enzyme 115 Pathways Not Available
Enzyme 115 Reactions Not Available
Enzyme 115 Pfam Domain Function
Enzyme 115 Signals
  • None
Enzyme 115 Transmembrane Regions
  • None
Enzyme 115 Essentiality Not Available
Enzyme 115 GenBank ID Protein 31544941 Link Image
Enzyme 115 UniProtKB/Swiss-Prot ID Q7Z727 Link Image
Enzyme 115 UniProtKB/Swiss-Prot Entry Name Q7Z727_HUMAN Link Image
Enzyme 115 PDB ID 1DSY Link Image
Enzyme 115 PDB File Show
Enzyme 115 3D Structure
Enzyme 115 Cellular Location Not Available
Enzyme 115 Gene Sequence >1143 bp
GCGAGCCAGCGGCTCCGGCTCCCGCTCCCGCTCCGCGCAGCACCAGCCCGACTCTCCCCG
GCCCCCGCCGCGCCCCCTCGCCGCGACCTCGGCCACCGGCCCGCGCCCCGCGCCCGGGGT
CGCCCCGAGCCCGCACCTCTCCCCCGCCGCCCCCGCCCACCCGGCCCTCCGCGGCCGCAG
CTCCCCGGCGGAGGCAAGAGGTGGTTGGGGGGGACCATGGCTGACGTTTTCCCGGGCAAC
GACTCCACGGCGTCTCAGGACGTGGCCAACCGCTTCGCCCGCAAAGGGGCGCTGAGGCAG
AAGAACGTGCACGAGGTGAAGGACCACAAATTCATCGCGCGCTTCTTCAAGCAGCCCACC
TTCTGCAGCCACTGCACCGACTTCATCTGGGGGTTTGGGAAACAAGGCTTCCAGTGCCAA
GTTTGCTGTTTTGTGGTCCACAAGAGGTGCCATGAATTTGTTACTTTTTCTTGTCCGGGT
GCGGATAAGGGACCCGACACTGATGACCCCAGGAGCAAGCACAAGTTCAAAATCCACACT
TACGGAAGCCCCACCTTCTGCGATCACTGTGGGTCACTGCTCTATGGACTTATCCATCAA
GGGATGAAATGTGACACCTGCGATATGAACGTTCACAAGCAATGCGTCATCAATGTCCCC
AGCCTCTGCGGAATGGATCACACTGAGAAGAGGGGGCGGATTTACCTAAAGGCTGAGGTT
GCTGATGAAAAGCTCCATGTCACAGTACGAGATGCAAAAAATCTAATCCCTATGGATCCA
AACGGGCTTTCAGATCCTTATGTGAAGCTGAAACTTATTCCTGATCCCAAGAATGAAAGC
AAGCAAAAAACCAAAACCATCCGCTCCACACTAAATCCGCAGTGGAATGAGTCCTTTACA
TTCAAATTGAAACCTTCAGACAAAGACCGACGACTGTCTGTAGAAATCTGGGACTGGGAT
CGAACAACAAGGAATGACTTCATGGGATCCCTTTCCTTTGGAGTTTCGGAGCTGATGAAG
ATGCCGGCCAGTGGATGGTACAAGTTACTTAACCAAGAAGAAGGTGAGTACTACAACGTA
CCCATTCCGGAAGGGGACGAGGAAGGAAACATGGAACTCAGGCAGAAATTCGAGTGGAGA
TGA
Enzyme 115 GenBank Gene ID BC053321 Link Image
Enzyme 115 GeneCard ID PRKCA Link Image
Enzyme 115 GenAtlas ID Not Available
Enzyme 115 HGNC ID Not Available
Enzyme 115 Chromosome Location 1
Enzyme 115 Locus 17q22-q23.2
Enzyme 115 SNPs SNPJam Report Link Image
Enzyme 115 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 115 Metabolite References Not Available
Enzyme 116 [top]
Enzyme 116 ID 17261
Enzyme 116 Name SH3 and cysteine-rich domain-containing protein 3
Enzyme 116 Synonyms Not Available
Enzyme 116 Gene Name STAC3
Enzyme 116 Protein Sequence >SH3 and cysteine-rich domain-containing protein 3
MTEKEVLESPKPSFPAETRQSGLQRLKQLLRKGSTGTKEMELPPEPQANGEAVGAGGGPI
YYIYEEEEEEEEEEEEPPPEPPKLVNDKPHKFKDHFFKKPKFCDVCARMIVLNNKFGLRC
KNCKTNIHEHCQSYVEMQRCFGKIPPGFHRAYSSPLYSNQQYACVKDLSAANRNDPVFET
LRTGVIMANKERKKGQADKKNPVAAMMEEEPESARPEEGKPQDGNPEGDKKAEKKTPDDK
HKQPGFQQSHYFVALYRFKALEKDDLDFPPGEKITVIDDSNEEWWRGKIGEKVGFFPPNF
IIRVRAGERVHRVTRSFVGNREIGQITLKKDQIVVQKGDEAGGYVKVYTGRKVGLFPTDF
LEEI
Enzyme 116 Number of Residues 364
Enzyme 116 Molecular Weight 41506.8
Enzyme 116 Theoretical pI 6.94
Enzyme 116 GO Classification
Function
Process
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 116 General Function Involved in intracellular signaling pathway
Enzyme 116 Specific Function Not Available
Enzyme 116 Pathways Not Available
Enzyme 116 Reactions Not Available
Enzyme 116 Pfam Domain Function
Enzyme 116 Signals
  • None
Enzyme 116 Transmembrane Regions
  • None
Enzyme 116 Essentiality Not Available
Enzyme 116 GenBank ID Protein 16552576 Link Image
Enzyme 116 UniProtKB/Swiss-Prot ID Q96MF2 Link Image
Enzyme 116 UniProtKB/Swiss-Prot Entry Name STAC3_HUMAN Link Image
Enzyme 116 PDB ID Not Available
Enzyme 116 Cellular Location Not Available
Enzyme 116 Gene Sequence >1095 bp
ATGACAGAAAAGGAGGTGCTGGAGTCCCCTAAGCCCTCCTTCCCAGCAGAGACTCGGCAA
AGTGGGCTACAGCGGCTAAAGCAGTTACTCAGGAAGGGTTCTACAGGGACAAAGGAGATG
GAACTTCCCCCAGAGCCCCAGGCCAATGGGGAGGCAGTGGGAGCTGGGGGTGGGCCCATC
TACTACATCTATGAGGAAGAGGAAGAGGAAGAAGAGGAGGAGGAGGAGCCACCCCCAGAA
CCTCCTAAGCTGGTCAACGATAAGCCCCACAAATTCAAAGATCACTTCTTCAAGAAGCCA
AAGTTCTGTGATGTCTGTGCCCGGATGATTGTTCTCAACAACAAGTTTGGGCTTCGCTGT
AAGAACTGCAAAACCAACATCCATGAACACTGTCAGTCCTATGTGGAAATGCAGAGATGC
TTCGGCAAGATCCCACCTGGTTTCCATCGGGCCTATAGTTCCCCACTCTACAGCAACCAG
CAGTACGCTTGTGTCAAAGATCTCTCTGCTGCCAATCGCAATGATCCTGTGTTTGAAACC
CTGCGCACTGGGGTGATCATGGCAAACAAGGAACGGAAGAAGGGACAGGCAGATAAGAAA
AATCCTGTAGCAGCCATGATGGAGGAGGAGCCAGAGTCGGCCAGACCAGAGGAAGGCAAA
CCCCAGGATGGAAACCCTGAAGGGGATAAGAAGGCTGAGAAGAAGACACCTGATGACAAG
CACAAGCAGCCTGGCTTCCAGCAGTCTCATTACTTTGTGGCTCTCTATCGGTTCAAAGCC
CTGGAGAAGGACGATCTGGATTTCCCGCCAGGAGAGAAGATCACAGTCATTGATGACTCC
AATGAAGAATGGTGGCGGGGGAAAATCGGGGAGAAGGTCGGATTTTTCCCTCCAAACTTC
ATCATTCGGGTCCGGGCTGGAGAACGTGTGCACCGCGTGACGAGATCCTTCGTGGGGAAC
CGCGAGATAGGGCAGATCACTCTCAAGAAGGACCAGATCGTGGTGCAGAAAGGAGACGAA
GCGGGCGGCTACGTCAAGGTCTACACCGGCCGCAAGGTGGGGCTGTTTCCCACCGACTTT
CTAGAGGAAATTTAG
Enzyme 116 GenBank Gene ID AK057013 Link Image
Enzyme 116 GeneCard ID STAC3 Link Image
Enzyme 116 GenAtlas ID STAC3 Link Image
Enzyme 116 HGNC ID HGNC:28423 Link Image
Enzyme 116 Chromosome Location 1
Enzyme 116 Locus 12q13.3
Enzyme 116 SNPs SNPJam Report Link Image
Enzyme 116 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]
Enzyme 116 Metabolite References Not Available
Enzyme 117 [top]
Enzyme 117 ID 17262
Enzyme 117 Name GEM-interacting protein
Enzyme 117 Synonyms
  1. GMIP
Enzyme 117 Gene Name GMIP
Enzyme 117 Protein Sequence >GEM-interacting protein
MDAAEPGLPPGPEGRKRYSDIFRSLDNLEISLGNVTLEMLAGDPLLSEDPEPDKTPTATV
TNEASCWSGPSPEGPVPLTGEELDLRLIRTKGGVDAALEYAKTWSRYAKELLAWTEKRAS
YELEFAKSTMKIAEAGKVSIQQQSHMPLQYIYTLFLEHDLSLGTLAMETVAQQKRDYYQP
LAAKRTEIEKWRKEFKEQWMKEQKRMNEAVQALRRAQLQYVQRSEDLRARSQGSPEDSAP
QASPGPSKQQERRRRSREEAQAKAQEAEALYQACVREANARQQDLEIAKQRIVSHVRKLV
FQGDEVLRRVTLSLFGLRGAQAERGPRAFAALAECCAPFEPGQRYQEFVRALRPEAPPPP
PPAFSFQEFLPSLNSSPLDIRKKLSGPLPPRLDENSAEPGPWEDPGTGWRWQGTPGPTPG
SDVDSVGGGSESRSLDSPTSSPGAGTRQLVKASSTGTESSDDFEERDPDLGDGLENGLGS
PFGKWTLSSAAQTHQLRRLRGPAKCRECEAFMVSGTECEECFLTCHKRCLETLLILCGHR
RLPARTPLFGVDFLQLPRDFPEEVPFVVTKCTAEIEHRALDVQGIYRVSGSRVRVERLCQ
AFENGRALVELSGNSPHDVSSVLKRFLQELTEPVIPFHLYDAFISLAKTLHADPGDDPGT
PSPSPEVIRSLKTLLVQLPDSNYNTLRHLVAHLFRVAARFMENKMSANNLGIVFGPTLLR
PPDGPRAASAIPVTCLLDSGHQAQLVEFLIVHYEQIFGMDELPQATEPPPQDSSPAPGPL
TTSSQPPPPHLDPDSQPPVLASDPGPDPQHHSTLEQHPTATPTEIPTPQSDQREDVAEDT
KDGGGEVSSQGPEDSLLGTQSRGHFSRQPVKYPRGGVRPVTHQLSSLALVASKLCEETPI
TSVPRGSLRGRGPSPAAASPEGSPLRRTPLPKHFEITQETARLLSKLDSEAVPRATCCPD
VQPEEAEDHL
Enzyme 117 Number of Residues 970
Enzyme 117 Molecular Weight 106681.8
Enzyme 117 Theoretical pI 5.46
Enzyme 117 GO Classification
Function
Process
  • biological regulation
  • intracellular signaling pathway
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
Enzyme 117 General Function Involved in intracellular signaling pathway
Enzyme 117 Specific Function Stimulates, in vitro and in vivo, the GTPase activity of RhoA
Enzyme 117 Pathways Not Available
Enzyme 117 Reactions Not Available
Enzyme 117 Pfam Domain Function
Enzyme 117 Signals
  • None
Enzyme 117 Transmembrane Regions
  • None
Enzyme 117 Essentiality Not Available
Enzyme 117 GenBank ID Protein 7380947 Link Image
Enzyme 117 UniProtKB/Swiss-Prot ID Q9P107 Link Image
Enzyme 117 UniProtKB/Swiss-Prot Entry Name GMIP_HUMAN Link Image
Enzyme 117 PDB ID Not Available
Enzyme 117 Cellular Location Not Available
Enzyme 117 Gene Sequence >2913 bp
ATGGACGCAGCAGAGCCGGGACTCCCCCCAGGTCCTGAGGGCAGGAAGAGGTACAGTGAC
ATCTTCCGGAGCCTGGACAACCTCGAAATCTCACTGGGGAACGTGACCCTTGAGATGCTG
GCTGGAGACCCTCTACTCTCAGAAGACCCAGAACCTGACAAGACCCCTACAGCCACTGTT
ACCAACGAAGCCAGCTGTTGGAGCGGCCCCTCCCCAGAGGGTCCTGTACCCCTCACAGGG
GAGGAACTGGACTTGCGGCTCATTCGGACAAAGGGGGGTGTGGACGCAGCCCTGGAATAT
GCCAAGACCTGGAGCCGCTATGCCAAGGAACTGCTTGCCTGGACTGAAAAGAGAGCCAGC
TATGAGCTGGAGTTTGCTAAGAGCACCATGAAGATCGCTGAAGCTGGCAAGGTGTCCATT
CAACAGCAGAGCCACATGCCTCTGCAGTACATCTACACCCTGTTTCTGGAGCACGATCTC
AGCCTGGGAACCCTGGCCATGGAGACAGTGGCCCAGCAGAAAAGAGACTACTACCAGCCC
CTCGCCGCCAAACGGACTGAGATTGAGAAGTGGCGGAAGGAGTTCAAGGAGCAGTGGATG
AAGGAGCAGAAGCGGATGAATGAGGCGGTGCAGGCACTGCGGCGCGCCCAGCTGCAGTAT
GTGCAACGCAGCGAGGACCTGCGGGCACGCTCCCAGGGGTCCCCTGAGGACTCGGCCCCC
CAGGCCTCGCCGGGACCTAGCAAGCAGCAGGAGCGGCGGCGGCGCTCGCGAGAGGAGGCC
CAGGCCAAGGCGCAGGAGGCCGAGGCGCTGTACCAGGCCTGTGTCCGCGAGGCCAACGCG
CGGCAGCAGGACCTGGAGATCGCCAAGCAGCGAATCGTGTCGCACGTGCGCAAGCTGGTG
TTTCAGGGGGATGAAGTGCTGAGGCGGGTGACGCTGAGTCTCTTCGGGCTGCGGGGGGCG
CAGGCAGAGCGTGGCCCCCGCGCCTTCGCCGCCCTGGCCGAGTGCTGTGCGCCCTTTGAG
CCGGGCCAGCGCTACCAGGAGTTTGTACGGGCGCTGCGGCCCGAGGCCCCGCCGCCCCCG
CCGCCCGCCTTCTCCTTCCAGGAGTTCCTTCCCTCCTTGAACAGCTCCCCTCTGGACATC
AGAAAGAAGCTCTCTGGGCCTCTTCCTCCAAGGCTGGATGAGAATTCAGCTGAGCCAGGC
CCTTGGGAGGATCCGGGCACAGGCTGGCGCTGGCAAGGGACTCCAGGCCCCACTCCGGGC
AGCGATGTGGACAGCGTGGGTGGCGGCAGCGAGTCTCGGTCCCTGGACTCACCCACTTCC
AGCCCAGGCGCTGGCACGAGGCAGCTGGTGAAGGCTTCGTCCACAGGCACTGAGTCCTCA
GATGACTTTGAGGAGCGAGACCCTGACCTGGGAGACGGGCTGGAGAATGGGCTGGGCAGC
CCCTTCGGGAAGTGGACACTGTCCAGCGCGGCTCAGACCCACCAGCTGCGGCGACTGCGG
GGCCCAGCCAAGTGCCGCGAGTGCGAAGCCTTCATGGTCAGCGGGACGGAGTGTGAGGAG
TGCTTTCTGACCTGCCACAAGCGCTGCCTGGAGACTCTCCTGATCCTCTGTGGACACAGG
CGGCTCCCAGCCCGGACACCCCTTTTTGGGGTTGACTTCCTGCAGCTACCCAGGGACTTC
CCGGAGGAGGTACCCTTTGTGGTCACGAAGTGCACGGCTGAGATAGAACACCGTGCCCTG
GATGTGCAGGGCATTTACCGGGTCAGCGGGTCCCGGGTCCGTGTGGAGCGGCTGTGCCAG
GCTTTCGAGAATGGCCGAGCGTTGGTGGAGCTGTCGGGGAACTCGCCTCATGACGTCTCG
AGTGTCCTCAAGCGATTTCTTCAGGAGCTCACCGAGCCCGTGATCCCCTTCCACCTCTAC
GACGCCTTCATCTCTCTGGCTAAGACCTTGCATGCAGACCCTGGGGACGACCCTGGGACC
CCCAGCCCCAGCCCTGATGTTATCCGCTCGCTGAAGACCCTCTTGGTACAGCTGCCTGAC
TCTAACTACAACACCCTGCGGCACCTGGTGGCCCATCTGTTCAGGGTGGCTGCACGATTT
ATGGAAAACAAGATGTCTGCCAACAACCTGGGCATTGTGTTTGGGCCGACACTGCTGCGG
CCGCCGGACGGCCCGCGGGCAGCCAGCGCCATCCCTGTCACCTGCCTGCTGGACTCTGGG
CATCAGGCCCAGCTTGTGGAGTTCCTCATCGTGCACTACGAGCAGATCTTTGGGATGGAT
GAGCTCCCCCAGGCCACTGAGCCCCCGCCCCAAGACTTCAGCCCAGCCCCTGGGCCCCTC
ACAACCAGCTCCCAACCGCCACCCCCGCACCTTGACCCAGACTCCCAGCCCCCAGTCCTA
GCCTCAGACCCCGGCCCAGACCCCCAGCACCACAGTACCCTGGAGCAGCATCCCACGGCC
ACACCTACCGAGATTCCAACTCCACAGAGTGACCAGAGAGAGGACGTGGCTGAAGACACC
AAAGATGGGGGAGGGGAAGTGTCCAGCCAAGGCCCAGAGGACTCACTCCTGGGGACACAG
TCTCGTGGCCACTTCAGCCGCCAGCCATGTAAGTATCCCCGGGGCGGTGTGAGGCCTGTA
ACCCACCAGCTGTCCAGTCTGGCCCTGGTGGCTTCCAAGCTGTGCGAGGAGACCCCCATC
ACATCAGTGCCCAGAGGGAGTTTGCGGGGGCGGGGGCCCAGCCCTGCAGCTGCCTCCCCT
GAGGGCAGCCCCCTGCGCCGCACCCCGCTGCCCAAGCATTTTGAGATTACCCAGGAGACA
GCCCGGCTACTCTCGAAATTGGACAGCGAGGCTGTGCCCAGGGCCACCTGCTGCCCGGAC
GTCCAGCCTGAGGAAGCCGAGGACCATCTCTGA
Enzyme 117 GenBank Gene ID AF132541 Link Image
Enzyme 117 GeneCard ID GMIP Link Image
Enzyme 117 GenAtlas ID GMIP Link Image
Enzyme 117 HGNC ID HGNC:24852 Link Image
Enzyme 117 Chromosome Location 1
Enzyme 117 Locus 19p13.11
Enzyme 117 SNPs SNPJam Report Link Image
Enzyme 117 General References
  1. Aresta S, de Tand-Heim MF, Beranger F, de Gunzburg J: A novel Rho GTPase-activating-protein interacts with Gem, a member of the Ras superfamily of GTPases. Biochem J. 2002 Oct 1;367(Pt 1):57-65. [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. 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]
  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. 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. 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]
  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 117 Metabolite References Not Available
Enzyme 118 [top]
Enzyme 118 ID 17263
Enzyme 118 Name Differentially expressed in FDCP 8 homolog
Enzyme 118 Synonyms
  1. DEF-8
Enzyme 118 Gene Name DEF8
Enzyme 118 Protein Sequence >Differentially expressed in FDCP 8 homolog
MAILSLRAPGPWQAMQVWADRTLLTPHTGVTSQVLGVAAAVMTPLPGGHAAGRTREARWD
AMEYDEKLARFRQAHLNPFNKQSGPRQHEQGPGEEVPDVTPEEALPELPPGEPEFRCPER
VMDLGLSEDHFSRPVGLFLASDVQQLRQAIEECKQVILELPEQSEKQKDAVVRLIHLRLK
LQELKDPNEDEPNIRVLLEHRFYKEKSKSVKQTCDKCNTIIWGLIQTWYTCTGCYYRCHS
KCLNLISKPCVSSKVSHQAEYELNICPETGLDSQDYRCAECRAPISLRGVPSEARQCDYT
GQYYCSHCHWNDLAVIPARVVHNWDFEPRKVSRCSMRYLALMVSRPVLRLREINPLLFSY
VEELVEIRKLRQDILLMKPYFITCREAMEARLLLQLQDRQHFVENDEMYSVQDLLDVHAG
RLGCSLTEIHTLFAKHIKLDCERCQAKGFVCELCREGDVLFPFDSHTSVCADCSAVFHRD
CYYDNSTTCPKCARLSLRKQSLFQEPGPDVEA
Enzyme 118 Number of Residues 512
Enzyme 118 Molecular Weight 58709.7
Enzyme 118 Theoretical pI 6.50
Enzyme 118 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • protein binding
  • transition metal ion binding
  • zinc ion binding
Process
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 118 General Function Involved in intracellular signaling pathway
Enzyme 118 Specific Function Not Available
Enzyme 118 Pathways Not Available
Enzyme 118 Reactions Not Available
Enzyme 118 Pfam Domain Function
Enzyme 118 Signals
  • None
Enzyme 118 Transmembrane Regions
  • None
Enzyme 118 Essentiality Not Available
Enzyme 118 GenBank ID Protein 46447820 Link Image
Enzyme 118 UniProtKB/Swiss-Prot ID Q6ZN54 Link Image
Enzyme 118 UniProtKB/Swiss-Prot Entry Name DEFI8_HUMAN Link Image
Enzyme 118 PDB ID Not Available
Enzyme 118 Cellular Location Not Available
Enzyme 118 Gene Sequence >1539 bp
ATGGCCATCCTGTCCCTGCGAGCCCCTGGGCCCTGGCAGGCGATGCAGGTATGGGCAGAC
AGGACGCTGTTGACTCCGCACACCGGCGTGACTTCTCAGGTTCTCGGGGTGGCAGCTGCA
GTGATGACACCGCTTCCTGGTGGTCACGCCGCGGGCAGGACGCGGGAGGCCAGGTGGGAT
GCTATGGAATATGATGAGAAGCTGGCCCGTTTCCGGCAGGCCCACCTCAACCCCTTCAAC
AAGCAGTCTGGGCCGAGACAGCATGAGCAGGGCCCTGGGGAGGAGGTCCCGGACGTCACT
CCTGAAGAGGCCCTGCCTGAGCTGCCCCCTGGGGAGCCGGAATTCCGCTGCCCTGAACGC
GTGATGGATCTCGGCCTGTCTGAGGACCACTTCTCCCGCCCTGTGGGTCTGTTCCTGGCC
TCTGACGTCCAGCAGCTGCGGCAGGCGATCGAGGAGTGCAAGCAGGTGATTCTGGAGCTG
CCCGAGCAGTCGGAGAAGCAGAAGGATGCCGTGGTGCGACTCATCCACCTCCGGCTGAAG
CTCCAGGAGCTGAAGGACCCCAATGAGGATGAGCCAAACATCCGAGTGCTCCTTGAGCAC
CGCTTTTACAAGGAGAAGAGCAAGAGCGTCAAGCAGACCTGTGACAAGTGTAACACCATC
ATCTGGGGGCTCATTCAGACCTGGTACACCTGCACAGGGTGTTATTACCGCTGTCACAGT
AAGTGCTTGAACCTCATCTCCAAGCCCTGTGTGAGCTCCAAAGTCAGCCACCAAGCTGAA
TACGAACTGAACATCTGCCCTGAGACAGGGCTGGACAGCCAGGATTACCGCTGTGCCGAG
TGCCGGGCGCCCATCTCTCTGCGGGGTGTGCCCAGTGAGGCCAGGCAGTGCGACTACACC
GGCCAGTACTACTGCAGCCACTGCCACTGGAACGACCTGGCTGTGATCCCTGCACGCGTT
GTACACAACTGGGACTTTGAGCCTCGAAAGGTTTCTCGCTGCAGCATGCGCTACCTGGCG
CTGATGGTGTCTCGGCCCGTACTCAGGCTCCGGGAGATCAACCCTCTGCTGTTCAGCTAC
GTGGAGGAGCTGGTGGAGATTCGCAAGCTGCGCCAGGACATCCTGCTCATGAAGCCGTAC
TTCATCACCTGCAGGGAGGCCATGGAGGCTCGTCTGCTGCTGCAGCTCCAGGATCGGCAG
CATTTTGTGGAGAACGACGAGATGTACTCTGTCCAGGACCTCCTGGACGTGCATGCCGGC
CGCCTGGGCTGCTCGCTCACCGAGATCCACACGCTCTTCGCCAAGCACATCAAGCTGGAC
TGCGAGCGGTGCCAGGCCAAGGGCTTCGTGTGTGAGCTCTGCAGAGAGGGCGACGTGCTG
TTCCCGTTCGACAGCCACACGTCTGTGTGCGCCGACTGCTCCGCGGTCTTCCACAGGGAC
TGCTACTACGACAACTCCACCACTTGTCCCAAGTGTGCCCGGCTCAGCCTGAGGAAGCAG
TCGCTCTTCCAGGAGCCAGGTCCCGATGTGGAGGCCTAG
Enzyme 118 GenBank Gene ID NM_207514.1 Link Image
Enzyme 118 GeneCard ID DEF8 Link Image
Enzyme 118 GenAtlas ID DEF8 Link Image
Enzyme 118 HGNC ID HGNC:25969 Link Image
Enzyme 118 Chromosome Location 1
Enzyme 118 Locus 16q24.3
Enzyme 118 SNPs SNPJam Report Link Image
Enzyme 118 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]
Enzyme 118 Metabolite References Not Available
Enzyme 119 [top]
Enzyme 119 ID 17264
Enzyme 119 Name Rho GTPase-activating protein 29
Enzyme 119 Synonyms
  1. PTPL1-associated RhoGAP protein 1
  2. Rho-type GTPase-activating protein 29
Enzyme 119 Gene Name ARHGAP29
Enzyme 119 Protein Sequence >Rho GTPase-activating protein 29
MIAHKQKKTKKKRAWASGQLSTDITTSEMGLKSLSSNSIFDPDYIKELVNDIRKFSHMLL
YLKEAIFSDCFKEVIHIRLEELLRVLKSIMNKHQNLNSVDLQNAAEMLTAKVKAVNFTEV
NEENKNDLFQEVFSSIETLAFTFGNILTNFLMGDVGNDSLLRLPVSRETKSFENVSVESV
DSSSEKGNFSPLELDNVLLKNTDSIELALSYAKTWSKYTKNIVSWVEKKLNLELESTRNM
VKLAEATRTNIGIQEFMPLQSLFTNALLNDIESSHLLQQTIAALQANKFVQPLLGRKNEM
EKQRKEIKELWKQEQNKMLEAENALKKAKLLCMQRQDEYEKAKSSMFRAEEEHLSSSGGL
AKNLNKQLEKKRRLEEEALQKVEEANELYKVCVTNVEERRNDLENTKREILAQLRTLVFQ
CDLTLKAVTVNLFHMQHLQAASLADSLQSLCDSAKLYDPGQEYSEFVKATNSTEEEKVDG
NVNKHLNSSQPSGFGPANSLEDVVRLPDSSNKIEEDRCSNSADITGPSFIRSWTFGMFSD
SESTGGSSESRSLDSESISPGDFHRKLPRTPSSGTMSSADDLDEREPPSPSETGPNSLGT
FKKTLMSKAALTHKFRKLRSPTKCRDCEGIVVFQGVECEECLLVCHRKCLENLVIICGHQ
KLPGKIHLFGAEFTQVAKKEPDGIPFILKICASEIENRALCLQGIYRVCGNKIKTEKLCQ
ALENGMHLVDISEFSSHDICDVLKLYLRQLPEPFILFRLYKEFIDLAKEIQHVNEEQETK
KNSLEDKKWPNMCIEINRILLKSKDLLRQLPASNFNSLHFLIVHLKRVVDHAEENKMNSK
NLGVIFGPSLIRPRPTTAPITISSLAEYSNQARLVEFLITYSQKIFDGSLQPQDVMCSIG
VVDQGCFPKPLLSPEERDIERSMKSLFFSSKEDIHTSESESKIFERATSFEESERKQNAL
GKCDACLSDKAQLLLDQEAESASQKIEDGKTPKPLSLKSDRSTNNVERHTPRTKIRPVSL
PVDRLLLASPPNERNGRNMGNVNLDKFCKNPAFEGVNRKDAATTVCSKFNGFDQQTLQKI
QDKQYEQNSLTAKTTMIMPSALQEKGVTTSLQISGDHSINATQPSKPYAEPVRSVREASE
RRSSDSYPLAPVRAPRTLQPQHWTTFYKPHAPIISIRGNEEKPASPSAAVPPGTDHDPHG
LVVKSMPDPDKASACPGQATGQPKEDSEELGLPDVNPMCQRPRLKRMQQFEDLEGEIPQF
V
Enzyme 119 Number of Residues 1261
Enzyme 119 Molecular Weight 142062.2
Enzyme 119 Theoretical pI 6.72
Enzyme 119 GO Classification
Function
Process
  • biological regulation
  • intracellular signaling pathway
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
Enzyme 119 General Function Involved in intracellular signaling pathway
Enzyme 119 Specific Function GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. May act as a specific effector of RAP2A to regulate Rho
Enzyme 119 Pathways Not Available
Enzyme 119 Reactions Not Available
Enzyme 119 Pfam Domain Function
Enzyme 119 Signals
  • None
Enzyme 119 Transmembrane Regions
  • None
Enzyme 119 Essentiality Not Available
Enzyme 119 GenBank ID Protein 134304853 Link Image
Enzyme 119 UniProtKB/Swiss-Prot ID Q52LW3 Link Image
Enzyme 119 UniProtKB/Swiss-Prot Entry Name RHG29_HUMAN Link Image
Enzyme 119 PDB ID Not Available
Enzyme 119 Cellular Location Not Available
Enzyme 119 Gene Sequence >3786 bp
ATGATTGCTCACAAACAGAAAAAGACAAAGAAAAAACGTGCTTGGGCATCAGGTCAACTC
TCTACTGATATTACAACTTCTGAAATGGGGCTCAAGTCCTTAAGTTCCAACTCTATTTTT
GATCCGGATTACATCAAGGAGTTGGTGAATGATATCAGGAAGTTCTCCCACATGTTACTA
TATTTGAAAGAAGCCATATTTTCAGACTGTTTTAAAGAAGTTATTCATATACGTCTAGAG
GAACTGCTCCGTGTTTTAAAGTCTATAATGAATAAACATCAGAACCTCAATTCTGTTGAT
CTTCAAAATGCTGCAGAAATGCTCACTGCAAAAGTGAAAGCTGTGAACTTCACAGAAGTT
AATGAAGAAAACAAAAACGATCTCTTCCAGGAAGTGTTTTCTTCTATTGAAACTTTGGCA
TTTACCTTTGGAAATATCCTTACAAACTTCCTTATGGGAGATGTAGGCAATGATTCATTA
TTGCGACTGCCTGTTTCTCGAGAAACTAAGTCGTTTGAAAATGTTTCTGTGGAATCAGTG
GACTCATCCAGTGAAAAAGGAAATTTTTCCCCTTTAGAACTAGACAACGTGCTGTTAAAG
AACACTGACTCTATCGAGCTGGCTTTGTCATATGCTAAAACTTGGTCAAAATATACTAAG
AACATAGTTTCATGGGTTGAAAAAAAGCTTAACTTGGAATTGGAGTCCACTAGAAATATG
GTCAAGTTGGCAGAGGCAACTAGAACTAACATTGGAATTCAGGAGTTCATGCCACTGCAG
TCTCTGTTTACTAATGCTCTTCTTAATGATATAGAAAGCAGTCACCTTTTACAACAAACA
ATTGCAGCTCTCCAGGCTAACAAATTTGTGCAGCCTCTACTTGGAAGGAAAAATGAAATG
GAAAAACAAAGGAAAGAAATAAAAGAGCTTTGGAAACAGGAGCAAAATAAAATGCTTGAA
GCAGAGAATGCTCTCAAAAAGGCAAAATTATTATGCATGCAACGTCAAGATGAATATGAG
AAAGCAAAGTCTTCCATGTTTCGTGCAGAAGAGGAGCATCTGTCTTCAAGTGGCGGATTA
GCAAAAAATCTCAACAAGCAACTAGAAAAAAAGCGAAGGTTGGAAGAGGAGGCTCTCCAA
AAAGTAGAAGAAGCAAATGAACTTTACAAAGTTTGTGTGACAAATGTTGAAGAAAGAAGA
AATGATCTAGAAAATACCAAAAGAGAAATTTTAGCACAACTCCGGACACTTGTTTTCCAG
TGTGATCTTACCCTTAAAGCTGTAACAGTTAACCTCTTCCACATGCAGCATCTGCAGGCT
GCTTCCCTTGCAGACAGTTTACAGTCTCTCTGTGATAGTGCCAAACTCTATGACCCAGGC
CAAGAGTACAGTGAATTTGTCAAGGCCACAAATTCAACTGAAGAAGAAAAAGTTGATGGA
AATGTAAATAAACATTTAAATAGTTCCCAACCTTCAGGATTTGGACCTGCCAACTCTTTA
GAGGATGTTGTACGCCTTCCTGACAGTTCTAATAAAATTGAAGAGGACAGATGCTCTAAC
AGTGCAGATATAACAGGTCCTTCCTTTATAAGATCATGGACATTTGGGATGTTTAGTGAT
TCTGAGAGCACTGGAGGGAGCAGCGAATCTAGATCTCTGGATTCAGAATCTATAAGTCCA
GGAGACTTTCATCGAAAACTTCCACGAACACCATCCAGTGGAACTATGTCCTCTGCAGAT
GATCTAGATGAAAGAGAGCCACCTTCCCCTTCAGAAACTGGACCCAATTCCCTTGGAACA
TTTAAGAAAACATTGATGTCAAAGGCAGCTCTCACACACAAGTTTCGCAAATTGAGATCC
CCCACGAAATGTAGGGATTGTGAAGGCATTGTAGTGTTCCAAGGTGTTGAATGTGAAGAG
TGTCTCCTTGTTTGTCATCGAAAGTGTTTGGAAAATTTAGTCATTATTTGTGGTCATCAG
AAACTTCCAGGAAAAATACACTTATTTGGAGCAGAATTCACACAAGTTGCAAAAAAGGAA
CCAGATGGTATCCCTTTTATACTCAAAATATGTGCCTCAGAGATTGAAAATAGAGCTTTG
TGTCTACAGGGAATTTATCGTGTGTGTGGAAACAAAATAAAAACTGAAAAATTGTGTCAA
GCTTTGGAAAATGGAATGCACTTGGTAGATATTTCAGAATTTAGTTCACATGATATCTGT
GACGTCTTGAAATTATACCTTCGGCAGCTCCCAGAACCATTTATTTTATTTCGATTGTAC
AAGGAATTTATAGACCTTGCAAAAGAGATCCAACATGTAAATGAAGAACAAGAGACAAAA
AAGAATAGTCTTGAAGACAAAAAATGGCCAAATATGTGTATAGAAATAAACCGAATTCTT
CTAAAAAGCAAAGACCTTCTAAGACAATTGCCAGCATCAAATTTTAACAGTCTTCATTTC
CTTATAGTACATCTAAAGCGGGTAGTAGATCATGCAGAAGAAAACAAGATGAACTCCAAA
AACTTGGGGGTGATATTTGGACCAAGTCTCATTAGGCCAAGGCCCACAACTGCTCCTATC
ACCATCTCCTCCCTTGCAGAGTATTCAAATCAAGCACGCTTGGTAGAGTTTCTCATTACT
TACTCACAGAAGATCTTCGATGGGTCCCTACAACCACAAGATGTTATGTGTAGCATAGGT
GTTGTTGATCAAGGCTGTTTTCCAAAGCCTCTGTTATCACCAGAAGAAAGAGACATTGAA
CGTTCCATGAAGTCACTATTTTTTTCTTCAAAGGAAGATATCCATACTTCAGAGAGTGAA
AGCAAAATTTTTGAACGAGCTACATCATTTGAGGAATCAGAACGCAAGCAAAATGCGTTA
GGAAAATGTGATGCATGTCTCAGTGACAAAGCACAGTTGCTTCTAGACCAAGAGGCTGAA
TCAGCATCCCAAAAGATAGAAGATGGTAAAACCCCTAAGCCACTTTCTCTGAAATCTGAT
AGGTCAACAAACAATGTGGAGAGGCATACTCCAAGGACCAAGATTAGACCTGTAAGTTTG
CCTGTAGATAGACTACTTCTTGCAAGTCCTCCTAATGAGAGAAATGGCAGAAATATGGGA
AATGTAAATTTAGACAAGTTTTGCAAGAATCCTGCCTTTGAAGGAGTTAATAGAAAAGAC
GCTGCTACTACTGTTTGTTCCAAATTTAATGGCTTTGACCAGCAAACTCTACAGAAAATT
CAGGACAAACAGTATGAACAAAACAGCCTAACTGCCAAGACTACAATGATCATGCCCAGT
GCACTCCAGGAAAAAGGAGTGACAACAAGCCTCCAGATTAGTGGGGACCATTCTATCAAT
GCCACTCAACCCAGTAAGCCATATGCAGAGCCAGTCAGGTCAGTGAGAGAGGCATCTGAG
AGACGGTCTTCAGATTCCTACCCTCTCGCTCCTGTCAGAGCACCCAGAACACTGCAGCCT
CAACATTGGACAACATTTTATAAACCACATGCTCCCATCATCAGTATCAGGGGGAATGAG
GAGAAGCCAGCTTCACCCTCAGCAGCAGTGCCTCCTGGCACAGATCACGATCCCCACGGT
CTCGTGGTGAAGTCAATGCCAGACCCAGACAAAGCATCAGCTTGTCCTGGGCAAGCAACT
GGTCAACCTAAAGAAGACTCTGAGGAGCTTGGCTTGCCTGATGTGAATCCAATGTGTCAG
AGACCAAGGCTAAAACGAATGCAACAGTTTGAAGACCTCGAAGGTGAAATTCCACAATTT
GTGTAG
Enzyme 119 GenBank Gene ID NM_004815.3 Link Image
Enzyme 119 GeneCard ID ARHGAP29 Link Image
Enzyme 119 GenAtlas ID ARHGAP29 Link Image
Enzyme 119 HGNC ID HGNC:30207 Link Image
Enzyme 119 Chromosome Location 1
Enzyme 119 Locus 1p22.1
Enzyme 119 SNPs SNPJam Report Link Image
Enzyme 119 General References
  1. Saras J, Franzen P, Aspenstrom P, Hellman U, Gonez LJ, Heldin CH: A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1. J Biol Chem. 1997 Sep 26;272(39):24333-8. [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. Mariani L, Beaudry C, McDonough WS, Hoelzinger DB, Demuth T, Ross KR, Berens T, Coons SW, Watts G, Trent JM, Wei JS, Giese A, Berens ME: Glioma cell motility is associated with reduced transcription of proapoptotic and proliferation genes: a cDNA microarray analysis. J Neurooncol. 2001 Jun;53(2):161-76. [PubMed Link Image]
  5. Myagmar BE, Umikawa M, Asato T, Taira K, Oshiro M, Hino A, Takei K, Uezato H, Kariya K: PARG1, a protein-tyrosine phosphatase-associated RhoGAP, as a putative Rap2 effector. Biochem Biophys Res Commun. 2005 Apr 15;329(3):1046-52. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Ripperger T, von Neuhoff N, Kamphues K, Emura M, Lehmann U, Tauscher M, Schraders M, Groenen P, Skawran B, Rudolph C, Callet-Bauchu E, van Krieken JH, Schlegelberger B, Steinemann D: Promoter methylation of PARG1, a novel candidate tumor suppressor gene in mantle-cell lymphomas. Haematologica. 2007 Apr;92(4):460-8. [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]
  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 119 Metabolite References Not Available
Enzyme 120 [top]
Enzyme 120 ID 17265
Enzyme 120 Name Pleckstrin homology domain-containing family M member 3
Enzyme 120 Synonyms
  1. PH domain-containing family M member 3
Enzyme 120 Gene Name PLEKHM3
Enzyme 120 Protein Sequence >Pleckstrin homology domain-containing family M member 3
MEALEVDDISPALEVTEEFFSTLDSNLEKAVQQAEVYGIQEVPELVGHEVLSNITDNGAM
RNVTSLGKGGMIWDHCKSRLLETKAQNVFPAKEQFMVQRGTTPDNLSWMEQKEASTFNFF
NICQRRRDRPRSVNDLLDETSTFKPGHARSRSDITQVDWRVVLKTTPLQQQQQQQPLLQG
PHVTRPSFLLPSPNKIEDAQGNTEHKQTFPNILKKGYLEIRKDHDSYWQSCYAELSPYNL
YFYSLDSSGNQNLYATYQLSHFQSISVLGNLEARMVDTVLYDNTQLQLKAESPWEALDWG
QKLWEVVHAAVPGYMGRQNELTISPGLGHHDDYTQNHSFQKKTSGLLPPSPVLDSSKQYQ
NILKSGTLYRLTVQNNWKAFTFVLSRAYLMAFQPGKLDEDPLLSYNVDVCLAVQMDNLDG
CDSCFQVIFPQDVLRLRAETRQRAQEWMEALKIAANVARSSEQNLQVTLRNKPKDQMGGH
ELRKNKRQSVTTSFLSILTTLSLERGLTAQSFKCAGCQRSIGLSNGKAKVCNYSGWYYCS
SCHVDDSFLIPARIVHNWDTSKYKVSKQAKEFLEYVYEEPLIDIQQENAMLYHHAEPLAA
VLRLRQRLKSLRAYLFSCRAAVAEDLRRRIFPREYLLQQIHLYSLADLQQVIEGKLAPFL
GKVIKFATSHVYSCSLCSQKGFICEICNNGEILYPFEDISTSRCESCGAVFHSECKEKSV
PCPRCVRRELQKKQKSFWQRLNMDESLEEACTMFELSYQNT
Enzyme 120 Number of Residues 761
Enzyme 120 Molecular Weight 87165.2
Enzyme 120 Theoretical pI 7.10
Enzyme 120 GO Classification
Function
Process
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
Enzyme 120 General Function Involved in intracellular signaling pathway
Enzyme 120 Specific Function Not Available
Enzyme 120 Pathways Not Available
Enzyme 120 Reactions Not Available
Enzyme 120 Pfam Domain Function