|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5452 |
| Enzyme 1 Name |
Diacylglycerol kinase theta |
| Enzyme 1 Synonyms |
- DAG kinase theta
- Diglyceride kinase theta
- 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 |
- Glycerolipid Metabolism (map00561
)
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
40806175  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P52824  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
DGKQ_HUMAN  |
| 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  |
| Enzyme 1 GeneCard ID |
DGKQ  |
| Enzyme 1 GenAtlas ID |
DGKQ  |
| Enzyme 1 HGNC ID |
HGNC:2856  |
| Enzyme 1 Chromosome Location |
4 |
| Enzyme 1 Locus |
4p16.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5453 |
| Enzyme 2 Name |
Pancreatic triacylglycerol lipase |
| Enzyme 2 Synonyms |
- PL
- 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 |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
Not Available |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P16233  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
LIPP_HUMAN  |
| Enzyme 2 PDB ID |
1N8S  |
| 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  |
| Enzyme 2 GeneCard ID |
PNLIP  |
| Enzyme 2 GenAtlas ID |
PNLIP  |
| Enzyme 2 HGNC ID |
HGNC:9155  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
10q26.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- Winkler FK, D'Arcy A, Hunziker W: Structure of human pancreatic lipase. Nature. 1990 Feb 22;343(6260):771-4. [PubMed
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- PLC-154
- Phosphoinositide phospholipase C-beta-1
- Phospholipase C-I
- PLC-I
- Phospholipase C-beta-1
- 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 |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
12083581  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q9NQ66  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
PLCB1_HUMAN  |
| 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  |
| Enzyme 3 GeneCard ID |
PLCB1  |
| Enzyme 3 GenAtlas ID |
PLCB1  |
| Enzyme 3 HGNC ID |
HGNC:15917  |
| Enzyme 3 Chromosome Location |
2 |
| Enzyme 3 Locus |
20p12 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Phosphoinositide phospholipase C-beta-4
- Phospholipase C-beta-4
- 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 |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
57284038  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q15147  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
PLCB4_HUMAN  |
| 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  |
| Enzyme 4 GeneCard ID |
PLCB4  |
| Enzyme 4 GenAtlas ID |
PLCB4  |
| Enzyme 4 HGNC ID |
HGNC:9059  |
| Enzyme 4 Chromosome Location |
2 |
| Enzyme 4 Locus |
20p12 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Phosphoinositide phospholipase C-beta-2
- Phospholipase C-beta-2
- 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 |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
95147333  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q00722  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
PLCB2_HUMAN  |
| 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  |
| Enzyme 5 GeneCard ID |
PLCB2  |
| Enzyme 5 GenAtlas ID |
PLCB2  |
| Enzyme 5 HGNC ID |
HGNC:9055  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
15q15 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5457 |
| Enzyme 6 Name |
Diacylglycerol kinase gamma |
| Enzyme 6 Synonyms |
- DAG kinase gamma
- Diglyceride kinase gamma
- 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 |
- Glycerolipid Metabolism (map00561
)
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
124256476  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P49619  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
DGKG_HUMAN  |
| 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  |
| Enzyme 6 GeneCard ID |
DGKG  |
| Enzyme 6 GenAtlas ID |
DGKG  |
| Enzyme 6 HGNC ID |
HGNC:2853  |
| Enzyme 6 Chromosome Location |
3 |
| Enzyme 6 Locus |
3q27.2-q27.3 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5458 |
| Enzyme 7 Name |
Hepatic triacylglycerol lipase |
| Enzyme 7 Synonyms |
- HL
- Hepatic lipase
- 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 |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
194097335  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P11150  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
LIPC_HUMAN  |
| 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  |
| Enzyme 7 GeneCard ID |
LIPC  |
| Enzyme 7 GenAtlas ID |
LIPC  |
| Enzyme 7 HGNC ID |
HGNC:6619  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
15q21-q23 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- Hegele RA, Tu L, Connelly PW: Human hepatic lipase mutations and polymorphisms. Hum Mutat. 1992;1(4):320-4. [PubMed
]
- 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
]
- 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
]
|
| 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 |
- Phosphoinositide phospholipase C-beta-3
- Phospholipase C-beta-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 |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
148745659  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q01970  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
PLCB3_HUMAN  |
| 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  |
| Enzyme 8 GeneCard ID |
PLCB3  |
| Enzyme 8 GenAtlas ID |
PLCB3  |
| Enzyme 8 HGNC ID |
HGNC:9056  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
11q13 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5461 |
| Enzyme 9 Name |
Pancreatic lipase-related protein 1 |
| Enzyme 9 Synonyms |
- 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 |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
5453920  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P54315  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
LIPR1_HUMAN  |
| 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  |
| Enzyme 9 GeneCard ID |
PNLIPRP1  |
| Enzyme 9 GenAtlas ID |
PNLIPRP1  |
| Enzyme 9 HGNC ID |
HGNC:9156  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
10q25.3 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Phosphoinositide phospholipase C-gamma-2
- Phospholipase C-IV
- PLC-IV
- Phospholipase C-gamma-2
- 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 |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
117320537  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P16885  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
PLCG2_HUMAN  |
| 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  |
| Enzyme 10 GeneCard ID |
PLCG2  |
| Enzyme 10 GenAtlas ID |
PLCG2  |
| Enzyme 10 HGNC ID |
HGNC:9066  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
16q24.1 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5463 |
| Enzyme 11 Name |
Lipid phosphate phosphohydrolase 2 |
| Enzyme 11 Synonyms |
- PAP2-gamma
- PAP2-G
- Phosphatidate phosphohydrolase type 2c
- Phosphatidic acid phosphatase 2c
- PAP-2c
- 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 |
|
| Process |
| — |
| Component |
|
|
| 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 |
|
| 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  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
O43688  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
LPP2_HUMAN  |
| 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  |
| Enzyme 11 GeneCard ID |
PPAP2C  |
| Enzyme 11 GenAtlas ID |
PPAP2C  |
| Enzyme 11 HGNC ID |
HGNC:9230  |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
19p13 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Acylglycerol O-acyltransferase
- Adiponutrin
- Calcium-independent phospholipase A2-epsilon
- 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 |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
17059636  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q9NST1  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
PLPL3_HUMAN  |
| 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  |
| Enzyme 12 GeneCard ID |
PNPLA3  |
| Enzyme 12 GenAtlas ID |
PNPLA3  |
| Enzyme 12 HGNC ID |
HGNC:18590  |
| Enzyme 12 Chromosome Location |
2 |
| Enzyme 12 Locus |
22q13.31 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5465 |
| Enzyme 13 Name |
Diacylglycerol kinase alpha |
| Enzyme 13 Synonyms |
- DAG kinase alpha
- 80 kDa diacylglycerol kinase
- Diglyceride kinase alpha
- 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 |
- Glycerolipid Metabolism (map00561
)
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
30823  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
P23743  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
DGKA_HUMAN  |
| Enzyme 13 PDB ID |
1TUZ  |
| 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  |
| Enzyme 13 GeneCard ID |
DGKA  |
| Enzyme 13 GenAtlas ID |
DGKA  |
| Enzyme 13 HGNC ID |
HGNC:2849  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
12q13.3 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
5466 |
| Enzyme 14 Name |
Diacylglycerol kinase delta |
| Enzyme 14 Synonyms |
- DAG kinase delta
- 130 kDa diacylglycerol kinase
- Diglyceride kinase delta
- 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 |
- Glycerolipid Metabolism (map00561
)
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
22773821  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q16760  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
DGKD_HUMAN  |
| Enzyme 14 PDB ID |
1R79  |
| 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  |
| Enzyme 14 GeneCard ID |
DGKD  |
| Enzyme 14 GenAtlas ID |
DGKD  |
| Enzyme 14 HGNC ID |
HGNC:2851  |
| Enzyme 14 Chromosome Location |
2 |
| Enzyme 14 Locus |
2q37.1 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
5467 |
| Enzyme 15 Name |
Diacylglycerol kinase epsilon |
| Enzyme 15 Synonyms |
- DAG kinase epsilon
- Diglyceride kinase epsilon
- 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 |
- Glycerolipid Metabolism (map00561
)
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
4503313  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P52429  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
DGKE_HUMAN  |
| 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  |
| Enzyme 15 GeneCard ID |
DGKE  |
| Enzyme 15 GenAtlas ID |
DGKE  |
| Enzyme 15 HGNC ID |
HGNC:2852  |
| Enzyme 15 Chromosome Location |
1 |
| Enzyme 15 Locus |
17q22 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- 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
]
- 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
]
- 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
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
5468 |
| Enzyme 16 Name |
Gastric triacylglycerol lipase |
| Enzyme 16 Synonyms |
- GL
- 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 |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
758063  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P07098  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
LIPG_HUMAN  |
| Enzyme 16 PDB ID |
1HLG  |
| 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  |
| Enzyme 16 GeneCard ID |
LIPF  |
| Enzyme 16 GenAtlas ID |
LIPF  |
| Enzyme 16 HGNC ID |
HGNC:6622  |
| Enzyme 16 Chromosome Location |
1 |
| Enzyme 16 Locus |
10q23.31 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
5469 |
| Enzyme 17 Name |
Lipid phosphate phosphohydrolase 1 |
| Enzyme 17 Synonyms |
- PAP2-alpha
- Phosphatidate phosphohydrolase type 2a
- Phosphatidic acid phosphatase 2a
- PAP-2a
- 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 |
|
| Process |
| — |
| Component |
|
|
| 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 |
|
| 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  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
O14494  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
LPP1_HUMAN  |
| 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  |
| Enzyme 17 GeneCard ID |
PPAP2A  |
| Enzyme 17 GenAtlas ID |
PPAP2A  |
| Enzyme 17 HGNC ID |
HGNC:9228  |
| Enzyme 17 Chromosome Location |
5 |
| Enzyme 17 Locus |
5q11 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
5470 |
| Enzyme 18 Name |
Diacylglycerol kinase beta |
| Enzyme 18 Synonyms |
- DAG kinase beta
- 90 kDa diacylglycerol kinase
- Diglyceride kinase beta
- 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 |
- Glycerolipid Metabolism (map00561
)
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
22027632  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q9Y6T7  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
DGKB_HUMAN  |
| 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  |
| Enzyme 18 GeneCard ID |
DGKB  |
| Enzyme 18 GenAtlas ID |
DGKB  |
| Enzyme 18 HGNC ID |
HGNC:2850  |
| Enzyme 18 Chromosome Location |
7 |
| Enzyme 18 Locus |
7p21.2 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
5471 |
| Enzyme 19 Name |
Endothelial lipase |
| Enzyme 19 Synonyms |
- Endothelial cell-derived lipase
- EDL
- 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 |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
4836419  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9Y5X9  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
LIPE_HUMAN  |
| 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  |
| Enzyme 19 GeneCard ID |
LIPG  |
| Enzyme 19 GenAtlas ID |
LIPG  |
| Enzyme 19 HGNC ID |
HGNC:6623  |
| Enzyme 19 Chromosome Location |
1 |
| Enzyme 19 Locus |
18q21.1 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
5472 |
| Enzyme 20 Name |
Diacylglycerol kinase iota |
| Enzyme 20 Synonyms |
- DAG kinase iota
- Diglyceride kinase iota
- 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 |
- Glycerolipid Metabolism (map00561
)
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
3676530  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
O75912  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
DGKI_HUMAN  |
| 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  |
| Enzyme 20 GeneCard ID |
DGKI  |
| Enzyme 20 GenAtlas ID |
DGKI  |
| Enzyme 20 HGNC ID |
HGNC:2855  |
| Enzyme 20 Chromosome Location |
7 |
| Enzyme 20 Locus |
7q32.3-q33 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
5473 |
| Enzyme 21 Name |
Bile salt-activated lipase |
| Enzyme 21 Synonyms |
- BAL
- Bile salt-stimulated lipase
- BSSL
- Bucelipase
- Carboxyl ester lipase
- Cholesterol esterase
- Pancreatic lysophospholipase
- 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 |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
148536848  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
P19835  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
CEL_HUMAN  |
| Enzyme 21 PDB ID |
1F6W  |
| 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  |
| Enzyme 21 GenAtlas ID |
CEL  |
| Enzyme 21 HGNC ID |
HGNC:1848  |
| Enzyme 21 Chromosome Location |
9 |
| Enzyme 21 Locus |
9q34.3 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
5474 |
| Enzyme 22 Name |
Lipid phosphate phosphohydrolase 3 |
| Enzyme 22 Synonyms |
- PAP2-beta
- Phosphatidate phosphohydrolase type 2b
- Phosphatidic acid phosphatase 2b
- PAP-2b
- PAP2b
- Vascular endothelial growth factor and type I collagen-inducible protein
- 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 |
|
| Process |
| — |
| Component |
|
|
| 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 |
|
| 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  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
LPP3_HUMAN  |
| 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  |
| Enzyme 22 GeneCard ID |
PPAP2B  |
| Enzyme 22 GenAtlas ID |
PPAP2B  |
| Enzyme 22 HGNC ID |
HGNC:9229  |
| Enzyme 22 Chromosome Location |
1 |
| Enzyme 22 Locus |
1pter-p22.1 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
5475 |
| Enzyme 23 Name |
Diacylglycerol O-acyltransferase 1 |
| Enzyme 23 Synonyms |
- ACAT-related gene product 1
- 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 |
|
| 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  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
O75907  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
DGAT1_HUMAN  |
| 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  |
| Enzyme 23 GeneCard ID |
DGAT1  |
| Enzyme 23 GenAtlas ID |
DGAT1  |
| Enzyme 23 HGNC ID |
HGNC:2843  |
| Enzyme 23 Chromosome Location |
8 |
| Enzyme 23 Locus |
8q24.3 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- 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
]
- 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
]
|
| 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 |
- PLC-148
- Phosphoinositide phospholipase C-gamma-1
- Phospholipase C-II
- PLC-II
- Phospholipase C-gamma-1
- 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 |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
3336979  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
P19174  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
PLCG1_HUMAN  |
| 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  |
| Enzyme 24 GeneCard ID |
PLCG1  |
| Enzyme 24 GenAtlas ID |
PLCG1  |
| Enzyme 24 HGNC ID |
HGNC:9065  |
| Enzyme 24 Chromosome Location |
2 |
| Enzyme 24 Locus |
20q12-q13.1 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
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- 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
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- 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
]
- 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
]
- 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
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
5477 |
| Enzyme 25 Name |
Pancreatic lipase-related protein 2 |
| Enzyme 25 Synonyms |
- 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 |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
Not Available |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
P54317  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
LIPR2_HUMAN  |
| 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  |
| Enzyme 25 GeneCard ID |
PNLIPRP2  |
| Enzyme 25 GenAtlas ID |
PNLIPRP2  |
| Enzyme 25 HGNC ID |
HGNC:9157  |
| Enzyme 25 Chromosome Location |
1 |
| Enzyme 25 Locus |
10q25.3 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
5478 |
| Enzyme 26 Name |
Diacylglycerol kinase zeta |
| Enzyme 26 Synonyms |
- DAG kinase zeta
- Diglyceride kinase zeta
- 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 |
- Glycerolipid Metabolism (map00561
)
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
157688564  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
Q13574  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
DGKZ_HUMAN  |
| 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  |
| Enzyme 26 GeneCard ID |
DGKZ  |
| Enzyme 26 GenAtlas ID |
DGKZ  |
| Enzyme 26 HGNC ID |
HGNC:2857  |
| Enzyme 26 Chromosome Location |
1 |
| Enzyme 26 Locus |
11p11.2 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Phosphoinositide phospholipase C-delta-1
- Phospholipase C-III
- PLC-III
- Phospholipase C-delta-1
- 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 |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
37572274  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
P51178  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
PLCD1_HUMAN  |
| 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  |
| Enzyme 27 GeneCard ID |
PLCD1  |
| Enzyme 27 GenAtlas ID |
PLCD1  |
| Enzyme 27 HGNC ID |
HGNC:9060  |
| Enzyme 27 Chromosome Location |
3 |
| Enzyme 27 Locus |
3p22-p21.3 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- 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
]
- 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
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
5545 |
| Enzyme 28 Name |
Lipoprotein lipase |
| Enzyme 28 Synonyms |
- 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 |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
189065397  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
P06858  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
LIPL_HUMAN  |
| 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  |
| Enzyme 28 GeneCard ID |
LPL  |
| Enzyme 28 GenAtlas ID |
LPL  |
| Enzyme 28 HGNC ID |
HGNC:6677  |
| Enzyme 28 Chromosome Location |
8 |
| Enzyme 28 Locus |
8p22 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- Zechner R: Rapid and simple isolation procedure for lipoprotein lipase from human milk. Biochim Biophys Acta. 1990 May 1;1044(1):20-5. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
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- 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
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- 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
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
5554 |
| Enzyme 29 Name |
Galactosylceramide sulfotransferase |
| Enzyme 29 Synonyms |
- GalCer sulfotransferase
- 3'-phosphoadenosine-5'-phosphosulfate:GalCer sulfotransferase
- 3'-phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase
- 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 |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
6714628  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
Q99999  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
G3ST1_HUMAN  |
| 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  |
| Enzyme 29 GeneCard ID |
GAL3ST1  |
| Enzyme 29 GenAtlas ID |
GAL3ST1  |
| Enzyme 29 HGNC ID |
HGNC:24240  |
| Enzyme 29 Chromosome Location |
2 |
| Enzyme 29 Locus |
22q12.2 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
5781 |
| Enzyme 30 Name |
Hormone-sensitive lipase |
| Enzyme 30 Synonyms |
- 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 |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
47124456  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
Q05469  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
LIPS_HUMAN  |
| 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  |
| Enzyme 30 GeneCard ID |
LIPE  |
| Enzyme 30 GenAtlas ID |
LIPE  |
| Enzyme 30 HGNC ID |
HGNC:6621  |
| Enzyme 30 Chromosome Location |
1 |
| Enzyme 30 Locus |
19q13.2 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
6021 |
| Enzyme 31 Name |
Phosphatidate cytidylyltransferase 2 |
| Enzyme 31 Synonyms |
- CDP-DAG synthase 2
- CDP-DG synthase 2
- CDP-diacylglycerol synthase 2
- CDS 2
- CDP-diglyceride pyrophosphorylase 2
- CDP-diglyceride synthase 2
- 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 |
|
|
| 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 |
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 31 Reactions |
- CTP + phosphatidate = diphosphate + CDP-diacylglycerol [RN:R01799]
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| 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  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
O95674  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
CDS2_HUMAN  |
| 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  |
| Enzyme 31 GeneCard ID |
CDS2  |
| Enzyme 31 GenAtlas ID |
CDS2  |
| Enzyme 31 HGNC ID |
HGNC:1801  |
| Enzyme 31 Chromosome Location |
2 |
| Enzyme 31 Locus |
20p13 |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
6030 |
| Enzyme 32 Name |
Choline-phosphate cytidylyltransferase A |
| Enzyme 32 Synonyms |
- CCT-alpha
- CTP:phosphocholine cytidylyltransferase A
- CCT A
- CT A
- 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 |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
28204946  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
P49585  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
PCY1A_HUMAN  |
| Enzyme 32 PDB ID |
1PEH  |
| 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  |
| Enzyme 32 GeneCard ID |
PCYT1A  |
| Enzyme 32 GenAtlas ID |
PCYT1A  |
| Enzyme 32 HGNC ID |
HGNC:8754  |
| Enzyme 32 Chromosome Location |
3 |
| Enzyme 32 Locus |
3q29 |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
- 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
]
- 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
]
- Johnson JE, Cornell RB: Membrane-binding amphipathic alpha-helical peptide derived from CTP:phosphocholine cytidylyltransferase. Biochemistry. 1994 Apr 12;33(14):4327-35. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
6040 |
| Enzyme 33 Name |
Phosphatidate cytidylyltransferase 1 |
| Enzyme 33 Synonyms |
- CDP-DAG synthase 1
- CDP-DG synthase 1
- CDP-diacylglycerol synthase 1
- CDS 1
- CDP-diglyceride pyrophosphorylase 1
- CDP-diglyceride synthase 1
- 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 |
|
|
| 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 |
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 33 Reactions |
- CTP + phosphatidate = diphosphate + CDP-diacylglycerol [RN:R01799]
|
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| 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  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
Q92903  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
CDS1_HUMAN  |
| 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  |
| Enzyme 33 GeneCard ID |
CDS1  |
| Enzyme 33 GenAtlas ID |
CDS1  |
| Enzyme 33 HGNC ID |
HGNC:1800  |
| Enzyme 33 Chromosome Location |
4 |
| Enzyme 33 Locus |
4q21.23 |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
6049 |
| Enzyme 34 Name |
Phosphatidylcholine:ceramide cholinephosphotransferase 2 |
| Enzyme 34 Synonyms |
- 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 |
|
| Process |
| — |
| Component |
|
|
| 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 |
|
| 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  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
SMS2_HUMAN  |
| 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  |
| Enzyme 34 GeneCard ID |
SGMS2  |
| Enzyme 34 GenAtlas ID |
SGMS2  |
| Enzyme 34 HGNC ID |
HGNC:28395  |
| Enzyme 34 Chromosome Location |
4 |
| Enzyme 34 Locus |
4q25 |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
6050 |
| Enzyme 35 Name |
CDP-diacylglycerol--inositol 3-phosphatidyltransferase |
| Enzyme 35 Synonyms |
- Phosphatidylinositol synthase
- PI synthase
- 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 |
|
|
| 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 |
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 35 Reactions |
- CDP-diacylglycerol + myo-inositol = CMP + phosphatidyl-1D-myo-inositol [RN:R01802]
|
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| 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  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
CDIPT_HUMAN  |
| 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  |
| Enzyme 35 GeneCard ID |
CDIPT  |
| Enzyme 35 GenAtlas ID |
CDIPT  |
| Enzyme 35 HGNC ID |
HGNC:1769  |
| Enzyme 35 Chromosome Location |
1 |
| Enzyme 35 Locus |
16p11.2 |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 General References |
- 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
]
- 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
]
- 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
]
- Antonsson BE: Purification and characterization of phosphatidylinositol synthase from human placenta. Biochem J. 1994 Feb 1;297 ( Pt 3):517-22. [PubMed
]
|
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
6054 |
| Enzyme 36 Name |
Phosphatidylcholine:ceramide cholinephosphotransferase 1 |
| Enzyme 36 Synonyms |
- Medulla oblongata-derived protein
- Protein Mob
- Sphingomyelin synthase 1
- 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 |
|
| Process |
| — |
| Component |
|
|
| 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 |
|
| 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  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
Q86VZ5  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
SMS1_HUMAN  |
| 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  |
| Enzyme 36 GenAtlas ID |
SGMS1  |
| Enzyme 36 HGNC ID |
HGNC:29799  |
| Enzyme 36 Chromosome Location |
1 |
| Enzyme 36 Locus |
10q11.2 |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Neural RAP guanine nucleotide exchange protein
- nRap GEP
- PDZ domain-containing guanine nucleotide exchange factor 1
- PDZ-GEF1
- 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 |
|
|
| 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 |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
7657261  |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
Q9Y4G8  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
RPGF2_HUMAN  |
| 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  |
| Enzyme 37 GeneCard ID |
RAPGEF2  |
| Enzyme 37 GenAtlas ID |
RAPGEF2  |
| Enzyme 37 HGNC ID |
HGNC:16854  |
| Enzyme 37 Chromosome Location |
4 |
| Enzyme 37 Locus |
4q32.1 |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Proto-oncogene c-RAF
- cRaf
- 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 |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
35842  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
P04049  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
RAF1_HUMAN  |
| 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  |
| Enzyme 38 GeneCard ID |
RAF1  |
| Enzyme 38 GenAtlas ID |
RAF1  |
| Enzyme 38 HGNC ID |
HGNC:9829  |
| Enzyme 38 Chromosome Location |
3 |
| Enzyme 38 Locus |
3p25 |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
6476 |
| Enzyme 39 Name |
Protein kinase C alpha type |
| Enzyme 39 Synonyms |
- PKC-A
- 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 |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
35483  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
P17252  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
KPCA_HUMAN  |
| 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  |
| Enzyme 39 GeneCard ID |
PRKCA  |
| Enzyme 39 GenAtlas ID |
PRKCA  |
| Enzyme 39 HGNC ID |
HGNC:9393  |
| Enzyme 39 Chromosome Location |
1 |
| Enzyme 39 Locus |
17q22-q23.2 |
| Enzyme 39 SNPs |
SNPJam Report  |
| Enzyme 39 General References |
- Finkenzeller G, Marme D, Hug H: Sequence of human protein kinase C alpha. Nucleic Acids Res. 1990 Apr 25;18(8):2183. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Proto-oncogene A-Raf
- Proto-oncogene A-Raf-1
- 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 |
|
| Enzyme 40 Transmembrane Regions |
|
| Enzyme 40 Essentiality |
Not Available |
| Enzyme 40 GenBank ID Protein |
1340152  |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
P10398  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
ARAF_HUMAN  |
| 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  |
| Enzyme 40 GeneCard ID |
ARAF  |
| Enzyme 40 GenAtlas ID |
ARAF  |
| Enzyme 40 HGNC ID |
HGNC:646  |
| Enzyme 40 Chromosome Location |
Not Available |
| Enzyme 40 Locus |
Not Available |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
6633 |
| Enzyme 41 Name |
Citron Rho-interacting kinase |
| Enzyme 41 Synonyms |
- CRIK
- 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 |
|
| Enzyme 41 Transmembrane Regions |
|
| Enzyme 41 Essentiality |
Not Available |
| Enzyme 41 GenBank ID Protein |
32698688  |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
O14578  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
CTRO_HUMAN  |
| 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  |
| Enzyme 41 GeneCard ID |
CIT  |
| Enzyme 41 GenAtlas ID |
CIT  |
| Enzyme 41 HGNC ID |
HGNC:1985  |
| Enzyme 41 Chromosome Location |
1 |
| Enzyme 41 Locus |
12q24 |
| Enzyme 41 SNPs |
SNPJam Report  |
| Enzyme 41 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
6668 |
| Enzyme 42 Name |
Protein kinase C beta type |
| Enzyme 42 Synonyms |
- PKC-B
- 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 |
|
| Enzyme 42 Transmembrane Regions |
|
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
47157322  |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
P05771  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
KPCB_HUMAN  |
| 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  |
| Enzyme 42 GeneCard ID |
PRKCB  |
| Enzyme 42 GenAtlas ID |
PRKCB  |
| Enzyme 42 HGNC ID |
HGNC:9395  |
| Enzyme 42 Chromosome Location |
1 |
| Enzyme 42 Locus |
16p11.2 |
| Enzyme 42 SNPs |
SNPJam Report  |
| Enzyme 42 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
6670 |
| Enzyme 43 Name |
Protein kinase C zeta type |
| Enzyme 43 Synonyms |
- 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 |
|
| Enzyme 43 Transmembrane Regions |
|
| Enzyme 43 Essentiality |
Not Available |
| Enzyme 43 GenBank ID Protein |
158255426  |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
Q05513  |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
KPCZ_HUMAN  |
| 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  |
| Enzyme 43 GeneCard ID |
PRKCZ  |
| Enzyme 43 GenAtlas ID |
PRKCZ  |
| Enzyme 43 HGNC ID |
HGNC:9412  |
| Enzyme 43 Chromosome Location |
1 |
| Enzyme 43 Locus |
1p36.33-p36.2 |
| Enzyme 43 SNPs |
SNPJam Report  |
| Enzyme 43 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
6732 |
| Enzyme 44 Name |
Protein kinase C iota type |
| Enzyme 44 Synonyms |
- Atypical protein kinase C-lambda/iota
- PRKC-lambda/iota
- aPKC-lambda/iota
- 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 |
|
| Enzyme 44 Transmembrane Regions |
|
| Enzyme 44 Essentiality |
Not Available |
| Enzyme 44 GenBank ID Protein |
133908623  |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
P41743  |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
KPCI_HUMAN  |
| 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  |
| Enzyme 44 GeneCard ID |
PRKCI  |
| Enzyme 44 GenAtlas ID |
PRKCI  |
| Enzyme 44 HGNC ID |
HGNC:9404  |
| Enzyme 44 Chromosome Location |
3 |
| Enzyme 44 Locus |
3q26.3 |
| Enzyme 44 SNPs |
SNPJam Report  |
| Enzyme 44 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 44 Metabolite References |
Not Available |
|
Enzyme 45
[top]
|
| Enzyme 45 ID |
6751 |
| Enzyme 45 Name |
Rho-associated protein kinase 1 |
| Enzyme 45 Synonyms |
- Renal carcinoma antigen NY-REN-35
- Rho-associated, coiled-coil-containing protein kinase 1
- p160 ROCK-1
- 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 |
|
|
| 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 |
|
| Enzyme 45 Transmembrane Regions |
|
| Enzyme 45 Essentiality |
Not Available |
| Enzyme 45 GenBank ID Protein |
Not Available |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
Q13464  |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
ROCK1_HUMAN  |
| 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  |
| Enzyme 45 GeneCard ID |
ROCK1  |
| Enzyme 45 GenAtlas ID |
ROCK1  |
| Enzyme 45 HGNC ID |
HGNC:10251  |
| Enzyme 45 Chromosome Location |
1 |
| Enzyme 45 Locus |
18q11.1 |
| Enzyme 45 SNPs |
SNPJam Report  |
| Enzyme 45 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- Riento K, Ridley AJ: Rocks: multifunctional kinases in cell behaviour. Nat Rev Mol Cell Biol. 2003 Jun;4(6):446-56. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 45 Metabolite References |
Not Available |
|
Enzyme 46
[top]
|
| Enzyme 46 ID |
6767 |
| Enzyme 46 Name |
Serine/threonine-protein kinase D1 |
| Enzyme 46 Synonyms |
- Protein kinase C mu type
- Protein kinase D
- nPKC-D1
- 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 |
|
| Enzyme 46 Transmembrane Regions |
|
| Enzyme 46 Essentiality |
Not Available |
| Enzyme 46 GenBank ID Protein |
189054333  |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
Q15139  |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
KPCD1_HUMAN  |
| 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  |
| Enzyme 46 GeneCard ID |
PRKD1  |
| Enzyme 46 GenAtlas ID |
PRKD1  |
| Enzyme 46 HGNC ID |
HGNC:9407  |
| Enzyme 46 Chromosome Location |
1 |
| Enzyme 46 Locus |
14q11 |
| Enzyme 46 SNPs |
SNPJam Report  |
| Enzyme 46 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 46 Metabolite References |
Not Available |
|
Enzyme 47
[top]
|
| Enzyme 47 ID |
6775 |
| Enzyme 47 Name |
Protein kinase C gamma type |
| Enzyme 47 Synonyms |
- 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 |
|
| Enzyme 47 Transmembrane Regions |
|
| Enzyme 47 Essentiality |
Not Available |
| Enzyme 47 GenBank ID Protein |
Not Available |
| Enzyme 47 UniProtKB/Swiss-Prot ID |
P05129  |
| Enzyme 47 UniProtKB/Swiss-Prot Entry Name |
KPCG_HUMAN  |
| 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  |
| Enzyme 47 GeneCard ID |
PRKCG  |
| Enzyme 47 GenAtlas ID |
PRKCG  |
| Enzyme 47 HGNC ID |
HGNC:9402  |
| Enzyme 47 Chromosome Location |
1 |
| Enzyme 47 Locus |
19q13.4 |
| Enzyme 47 SNPs |
SNPJam Report  |
| Enzyme 47 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 47 Metabolite References |
Not Available |
|
Enzyme 48
[top]
|
| Enzyme 48 ID |
6814 |
| Enzyme 48 Name |
Rho-associated protein kinase 2 |
| Enzyme 48 Synonyms |
- Rho kinase 2
- Rho-associated, coiled-coil-containing protein kinase 2
- 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 |
|
| Enzyme 48 Transmembrane Regions |
|
| Enzyme 48 Essentiality |
Not Available |
| Enzyme 48 GenBank ID Protein |
41872583  |
| Enzyme 48 UniProtKB/Swiss-Prot ID |
O75116  |
| Enzyme 48 UniProtKB/Swiss-Prot Entry Name |
ROCK2_HUMAN  |
| 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  |
| Enzyme 48 GeneCard ID |
ROCK2  |
| Enzyme 48 GenAtlas ID |
ROCK2  |
| Enzyme 48 HGNC ID |
HGNC:10252  |
| Enzyme 48 Chromosome Location |
2 |
| Enzyme 48 Locus |
2p24 |
| Enzyme 48 SNPs |
SNPJam Report  |
| Enzyme 48 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 48 Metabolite References |
Not Available |
|
Enzyme 49
[top]
|
| Enzyme 49 ID |
7218 |
| Enzyme 49 Name |
Protein kinase C delta type |
| Enzyme 49 Synonyms |
- 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 |
|
| Enzyme 49 Transmembrane Regions |
|
| Enzyme 49 Essentiality |
Not Available |
| Enzyme 49 GenBank ID Protein |
189053779  |
| Enzyme 49 UniProtKB/Swiss-Prot ID |
Q05655  |
| Enzyme 49 UniProtKB/Swiss-Prot Entry Name |
KPCD_HUMAN  |
| 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  |
| Enzyme 49 GeneCard ID |
PRKCD  |
| Enzyme 49 GenAtlas ID |
PRKCD  |
| Enzyme 49 HGNC ID |
HGNC:9399  |
| Enzyme 49 Chromosome Location |
3 |
| Enzyme 49 Locus |
3p21.31 |
| Enzyme 49 SNPs |
SNPJam Report  |
| Enzyme 49 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 49 Metabolite References |
Not Available |
|
Enzyme 50
[top]
|
| Enzyme 50 ID |
7219 |
| Enzyme 50 Name |
Serine/threonine-protein kinase D3 |
| Enzyme 50 Synonyms |
- Protein kinase C nu type
- Protein kinase EPK2
- 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 |
|
| Enzyme 50 Transmembrane Regions |
|
| Enzyme 50 Essentiality |
Not Available |
| Enzyme 50 GenBank ID Protein |
4115769  |
| Enzyme 50 UniProtKB/Swiss-Prot ID |
O94806  |
| Enzyme 50 UniProtKB/Swiss-Prot Entry Name |
KPCD3_HUMAN  |
| 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  |
| Enzyme 50 GeneCard ID |
PRKD3  |
| Enzyme 50 GenAtlas ID |
PRKD3  |
| Enzyme 50 HGNC ID |
HGNC:9408  |
| Enzyme 50 Chromosome Location |
2 |
| Enzyme 50 Locus |
2p21 |
| Enzyme 50 SNPs |
SNPJam Report  |
| Enzyme 50 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 50 Metabolite References |
Not Available |
|
Enzyme 51
[top]
|
| Enzyme 51 ID |
7220 |
| Enzyme 51 Name |
Protein kinase C theta type |
| Enzyme 51 Synonyms |
- 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 |
|
| Enzyme 51 Transmembrane Regions |
|
| Enzyme 51 Essentiality |
Not Available |
| Enzyme 51 GenBank ID Protein |
55957459  |
| Enzyme 51 UniProtKB/Swiss-Prot ID |
Q04759  |
| Enzyme 51 UniProtKB/Swiss-Prot Entry Name |
KPCT_HUMAN  |
| Enzyme 51 PDB ID |
1XJD  |
| 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  |
| Enzyme 51 GeneCard ID |
PRKCQ  |
| Enzyme 51 GenAtlas ID |
PRKCQ  |
| Enzyme 51 HGNC ID |
HGNC:9410  |
| Enzyme 51 Chromosome Location |
1 |
| Enzyme 51 Locus |
10p15 |
| Enzyme 51 SNPs |
SNPJam Report  |
| Enzyme 51 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 51 Metabolite References |
Not Available |
|
Enzyme 52
[top]
|
| Enzyme 52 ID |
7221 |
| Enzyme 52 Name |
Protein kinase C eta type |
| Enzyme 52 Synonyms |
- PKC-L
- 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 |
|
| Enzyme 52 Transmembrane Regions |
|
| Enzyme 52 Essentiality |
Not Available |
| Enzyme 52 GenBank ID Protein |
158261389  |
| Enzyme 52 UniProtKB/Swiss-Prot ID |
P24723  |
| Enzyme 52 UniProtKB/Swiss-Prot Entry Name |
KPCL_HUMAN  |
| 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  |
| Enzyme 52 GeneCard ID |
PRKCH  |
| Enzyme 52 GenAtlas ID |
PRKCH  |
| Enzyme 52 HGNC ID |
HGNC:9403  |
| Enzyme 52 Chromosome Location |
1 |
| Enzyme 52 Locus |
14q23.1 |
| Enzyme 52 SNPs |
SNPJam Report  |
| Enzyme 52 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Phosphoinositide phospholipase C-eta-2
- Phosphoinositide phospholipase C-like 4
- PLC-L4
- Phospholipase C-like protein 4
- Phospholipase C-eta-2
- 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 |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 53 Transmembrane Regions |
|
| Enzyme 53 Essentiality |
Not Available |
| Enzyme 53 GenBank ID Protein |
Not Available |
| Enzyme 53 UniProtKB/Swiss-Prot ID |
O75038  |
| Enzyme 53 UniProtKB/Swiss-Prot Entry Name |
PLCH2_HUMAN  |
| 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  |
| Enzyme 53 GeneCard ID |
PLCH2  |
| Enzyme 53 GenAtlas ID |
PLCH2  |
| Enzyme 53 HGNC ID |
HGNC:29037  |
| Enzyme 53 Chromosome Location |
1 |
| Enzyme 53 Locus |
1p36.32 |
| Enzyme 53 SNPs |
SNPJam Report  |
| Enzyme 53 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 53 Metabolite References |
Not Available |
|
Enzyme 54
[top]
|
| Enzyme 54 ID |
7223 |
| Enzyme 54 Name |
Protein kinase C epsilon type |
| Enzyme 54 Synonyms |
- 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 |
|
| Enzyme 54 Transmembrane Regions |
|
| Enzyme 54 Essentiality |
Not Available |
| Enzyme 54 GenBank ID Protein |
4885563  |
| Enzyme 54 UniProtKB/Swiss-Prot ID |
Q02156  |
| Enzyme 54 UniProtKB/Swiss-Prot Entry Name |
KPCE_HUMAN  |
| 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  |
| Enzyme 54 GeneCard ID |
PRKCE  |
| Enzyme 54 GenAtlas ID |
PRKCE  |
| Enzyme 54 HGNC ID |
HGNC:9401  |
| Enzyme 54 Chromosome Location |
2 |
| Enzyme 54 Locus |
2p21 |
| Enzyme 54 SNPs |
SNPJam Report  |
| Enzyme 54 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
|
| 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 |
|
| Enzyme 55 Transmembrane Regions |
|
| Enzyme 55 Essentiality |
Not Available |
| Enzyme 55 GenBank ID Protein |
25777684  |
| Enzyme 55 UniProtKB/Swiss-Prot ID |
Q9NS23  |
| Enzyme 55 UniProtKB/Swiss-Prot Entry Name |
RASF1_HUMAN  |
| 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  |
| Enzyme 55 GeneCard ID |
RASSF1  |
| Enzyme 55 GenAtlas ID |
RASSF1  |
| Enzyme 55 HGNC ID |
HGNC:9882  |
| Enzyme 55 Chromosome Location |
3 |
| Enzyme 55 Locus |
3p21.3 |
| Enzyme 55 SNPs |
SNPJam Report  |
| Enzyme 55 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Proto-oncogene B-Raf
- p94
- 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 |
|
| Enzyme 56 Transmembrane Regions |
|
| Enzyme 56 Essentiality |
Not Available |
| Enzyme 56 GenBank ID Protein |
33188459  |
| Enzyme 56 UniProtKB/Swiss-Prot ID |
P15056  |
| Enzyme 56 UniProtKB/Swiss-Prot Entry Name |
BRAF_HUMAN  |
| Enzyme 56 PDB ID |
1UWJ  |
| 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  |
| Enzyme 56 GeneCard ID |
BRAF  |
| Enzyme 56 GenAtlas ID |
BRAF  |
| Enzyme 56 HGNC ID |
HGNC:1097  |
| Enzyme 56 Chromosome Location |
7 |
| Enzyme 56 Locus |
7q34 |
| Enzyme 56 SNPs |
SNPJam Report  |
| Enzyme 56 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
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- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
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- 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
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- 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
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- 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
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- 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
]
- 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
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- 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
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- 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
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- 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
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- 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
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- 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
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- 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
]
- 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
]
- 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
]
|
| 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 |
- TrpC3
- Transient receptor protein 3
- TRP-3
- hTrp-3
- 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 |
|
| 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  |
| Enzyme 57 UniProtKB/Swiss-Prot Entry Name |
TRPC3_HUMAN  |
| 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  |
| Enzyme 57 GeneCard ID |
TRPC3  |
| Enzyme 57 GenAtlas ID |
TRPC3  |
| Enzyme 57 HGNC ID |
HGNC:12335  |
| Enzyme 57 Chromosome Location |
4 |
| Enzyme 57 Locus |
4q27 |
| Enzyme 57 SNPs |
SNPJam Report  |
| Enzyme 57 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 57 Metabolite References |
Not Available |
|
Enzyme 58
[top]
|
| Enzyme 58 ID |
8362 |
| Enzyme 58 Name |
Cholinephosphotransferase 1 |
| Enzyme 58 Synonyms |
- hCPT1
- AAPT1-like protein
- 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 |
|
|
| 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 |
|
| 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  |
| Enzyme 58 UniProtKB/Swiss-Prot ID |
Q8WUD6  |
| Enzyme 58 UniProtKB/Swiss-Prot Entry Name |
CHPT1_HUMAN  |
| 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  |
| Enzyme 58 GeneCard ID |
CHPT1  |
| Enzyme 58 GenAtlas ID |
CHPT1  |
| Enzyme 58 HGNC ID |
HGNC:17852  |
| Enzyme 58 Chromosome Location |
1 |
| Enzyme 58 Locus |
12q |
| Enzyme 58 SNPs |
SNPJam Report  |
| Enzyme 58 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- PLC-L1
- Phospholipase C-deleted in lung carcinoma
- Phospholipase C-related but catalytically inactive protein
- 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 |
|
| Enzyme 59 Transmembrane Regions |
|
| Enzyme 59 Essentiality |
Not Available |
| Enzyme 59 GenBank ID Protein |
254939661  |
| Enzyme 59 UniProtKB/Swiss-Prot ID |
Q15111  |
| Enzyme 59 UniProtKB/Swiss-Prot Entry Name |
PLCL1_HUMAN  |
| 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  |
| Enzyme 59 GeneCard ID |
PLCL1  |
| Enzyme 59 GenAtlas ID |
PLCL1  |
| Enzyme 59 HGNC ID |
HGNC:9063  |
| Enzyme 59 Chromosome Location |
2 |
| Enzyme 59 Locus |
2q33 |
| Enzyme 59 SNPs |
SNPJam Report  |
| Enzyme 59 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 59 Metabolite References |
Not Available |
|
Enzyme 60
[top]
|
| Enzyme 60 ID |
8626 |
| Enzyme 60 Name |
2-acylglycerol O-acyltransferase 2 |
| Enzyme 60 Synonyms |
- Acyl-CoA:monoacylglycerol acyltransferase 2
- MGAT2
- hMGAT2
- Diacylglycerol O-acyltransferase candidate 5
- hDC5
- Diacylglycerol acyltransferase 2-like protein 5
- 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 |
|
| Enzyme 60 Transmembrane Regions |
|
| Enzyme 60 Essentiality |
Not Available |
| Enzyme 60 GenBank ID Protein |
37537527  |
| Enzyme 60 UniProtKB/Swiss-Prot ID |
Q3SYC2  |
| Enzyme 60 UniProtKB/Swiss-Prot Entry Name |
MOGT2_HUMAN  |
| 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  |
| Enzyme 60 GeneCard ID |
MOGAT2  |
| Enzyme 60 GenAtlas ID |
MOGAT2  |
| Enzyme 60 HGNC ID |
HGNC:23248  |
| Enzyme 60 Chromosome Location |
1 |
| Enzyme 60 Locus |
11q13.5 |
| Enzyme 60 SNPs |
SNPJam Report  |
| Enzyme 60 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- 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 |
|
| Enzyme 61 Transmembrane Regions |
|
| Enzyme 61 Essentiality |
Not Available |
| Enzyme 61 GenBank ID Protein |
158260799  |
| Enzyme 61 UniProtKB/Swiss-Prot ID |
P41247  |
| Enzyme 61 UniProtKB/Swiss-Prot Entry Name |
PLPL4_HUMAN  |
| 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  |
| Enzyme 61 GeneCard ID |
PNPLA4  |
| Enzyme 61 GenAtlas ID |
PNPLA4  |
| Enzyme 61 HGNC ID |
HGNC:24887  |
| Enzyme 61 Chromosome Location |
Not Available |
| Enzyme 61 Locus |
Not Available |
| Enzyme 61 SNPs |
SNPJam Report  |
| Enzyme 61 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Phosphatidylglycerophosphate synthase 1
- 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 |
|
| Enzyme 62 Transmembrane Regions |
|
| Enzyme 62 Essentiality |
Not Available |
| Enzyme 62 GenBank ID Protein |
Not Available |
| Enzyme 62 UniProtKB/Swiss-Prot ID |
Q32NB8  |
| Enzyme 62 UniProtKB/Swiss-Prot Entry Name |
PGPS1_HUMAN  |
| 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  |
| Enzyme 62 GeneCard ID |
PGS1  |
| Enzyme 62 GenAtlas ID |
PGS1  |
| Enzyme 62 HGNC ID |
HGNC:30029  |
| Enzyme 62 Chromosome Location |
1 |
| Enzyme 62 Locus |
17q25.3 |
| Enzyme 62 SNPs |
SNPJam Report  |
| Enzyme 62 General References |
- 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
]
- 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
]
- 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
]
|
| Enzyme 62 Metabolite References |
Not Available |
|
Enzyme 63
[top]
|
| Enzyme 63 ID |
9821 |
| Enzyme 63 Name |
Diacylglycerol kinase eta |
| Enzyme 63 Synonyms |
- DAG kinase eta
- Diglyceride kinase eta
- 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 |
- Glycerolipid Metabolism (map00561
)
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 63 Transmembrane Regions |
|
| Enzyme 63 Essentiality |
Not Available |
| Enzyme 63 GenBank ID Protein |
29788751  |
| Enzyme 63 UniProtKB/Swiss-Prot ID |
Q86XP1  |
| Enzyme 63 UniProtKB/Swiss-Prot Entry Name |
DGKH_HUMAN  |
| Enzyme 63 PDB ID |
1R79  |
| 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  |
| Enzyme 63 GeneCard ID |
DGKH  |
| Enzyme 63 GenAtlas ID |
DGKH  |
| Enzyme 63 HGNC ID |
HGNC:2854  |
| Enzyme 63 Chromosome Location |
1 |
| Enzyme 63 Locus |
13q14.11 |
| Enzyme 63 SNPs |
SNPJam Report  |
| Enzyme 63 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- hPLCD4
- Phosphoinositide phospholipase C-delta-4
- Phospholipase C-delta-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 |
|
| Enzyme 64 Transmembrane Regions |
|
| Enzyme 64 Essentiality |
Not Available |
| Enzyme 64 GenBank ID Protein |
62897967  |
| Enzyme 64 UniProtKB/Swiss-Prot ID |
Q9BRC7  |
| Enzyme 64 UniProtKB/Swiss-Prot Entry Name |
PLCD4_HUMAN  |
| 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  |
| Enzyme 64 GeneCard ID |
PLCD4  |
| Enzyme 64 GenAtlas ID |
PLCD4  |
| Enzyme 64 HGNC ID |
HGNC:9062  |
| Enzyme 64 Chromosome Location |
2 |
| Enzyme 64 Locus |
2q35 |
| Enzyme 64 SNPs |
SNPJam Report  |
| Enzyme 64 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Phosphoinositide phospholipase C-eta-1
- Phospholipase C-eta-1
- PLC-eta-1
- Phospholipase C-like protein 3
- 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 |
|
| Enzyme 65 Transmembrane Regions |
|
| Enzyme 65 Essentiality |
Not Available |
| Enzyme 65 GenBank ID Protein |
195972871  |
| Enzyme 65 UniProtKB/Swiss-Prot ID |
Q4KWH8  |
| Enzyme 65 UniProtKB/Swiss-Prot Entry Name |
PLCH1_HUMAN  |
| 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  |
| Enzyme 65 GeneCard ID |
PLCH1  |
| Enzyme 65 GenAtlas ID |
PLCH1  |
| Enzyme 65 HGNC ID |
HGNC:29185  |
| Enzyme 65 Chromosome Location |
3 |
| Enzyme 65 Locus |
3q25.31 |
| Enzyme 65 SNPs |
SNPJam Report  |
| Enzyme 65 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Pancreas-enriched phospholipase C
- Phosphoinositide phospholipase C-epsilon-1
- Phospholipase C-epsilon-1
- 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 |
|
|
| 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 |
|
| Enzyme 66 Transmembrane Regions |
|
| Enzyme 66 Essentiality |
Not Available |
| Enzyme 66 GenBank ID Protein |
117168250  |
| Enzyme 66 UniProtKB/Swiss-Prot ID |
Q9P212  |
| Enzyme 66 UniProtKB/Swiss-Prot Entry Name |
PLCE1_HUMAN  |
| 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  |
| Enzyme 66 GeneCard ID |
PLCE1  |
| Enzyme 66 GenAtlas ID |
PLCE1  |
| Enzyme 66 HGNC ID |
HGNC:17175  |
| Enzyme 66 Chromosome Location |
1 |
| Enzyme 66 Locus |
10q23 |
| Enzyme 66 SNPs |
SNPJam Report  |
| Enzyme 66 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Phosphoinositide phospholipase C-delta-3
- Phospholipase C-delta-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 |
|
| Enzyme 67 Transmembrane Regions |
|
| Enzyme 67 Essentiality |
Not Available |
| Enzyme 67 GenBank ID Protein |
Not Available |
| Enzyme 67 UniProtKB/Swiss-Prot ID |
Q8N3E9  |
| Enzyme 67 UniProtKB/Swiss-Prot Entry Name |
PLCD3_HUMAN  |
| 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  |
| Enzyme 67 GeneCard ID |
PLCD3  |
| Enzyme 67 GenAtlas ID |
PLCD3  |
| Enzyme 67 HGNC ID |
HGNC:9061  |
| Enzyme 67 Chromosome Location |
1 |
| Enzyme 67 Locus |
17q21.31 |
| Enzyme 67 SNPs |
SNPJam Report  |
| Enzyme 67 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 67 Metabolite References |
Not Available |
|
Enzyme 68
[top]
|
| Enzyme 68 ID |
10076 |
| Enzyme 68 Name |
Diacylglycerol O-acyltransferase 2 |
| Enzyme 68 Synonyms |
- 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 |
|
| Enzyme 68 Transmembrane Regions |
|
| Enzyme 68 Essentiality |
Not Available |
| Enzyme 68 GenBank ID Protein |
22506631  |
| Enzyme 68 UniProtKB/Swiss-Prot ID |
Q96PD7  |
| Enzyme 68 UniProtKB/Swiss-Prot Entry Name |
DGAT2_HUMAN  |
| 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  |
| Enzyme 68 GeneCard ID |
DGAT2  |
| Enzyme 68 GenAtlas ID |
DGAT2  |
| Enzyme 68 HGNC ID |
HGNC:16940  |
| Enzyme 68 Chromosome Location |
1 |
| Enzyme 68 Locus |
11q13.5 |
| Enzyme 68 SNPs |
SNPJam Report  |
| Enzyme 68 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 68 Metabolite References |
Not Available |
|
Enzyme 69
[top]
|
| Enzyme 69 ID |
10239 |
| Enzyme 69 Name |
2-acylglycerol O-acyltransferase 1 |
| Enzyme 69 Synonyms |
- Acyl-CoA:monoacylglycerol acyltransferase 1
- MGAT1
- Diacylglycerol O-acyltransferase candidate 2
- hDC2
- Diacylglycerol acyltransferase 2-like protein 1
- 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 |
|
| Enzyme 69 Transmembrane Regions |
|
| Enzyme 69 Essentiality |
Not Available |
| Enzyme 69 GenBank ID Protein |
148746191  |
| Enzyme 69 UniProtKB/Swiss-Prot ID |
Q96PD6  |
| Enzyme 69 UniProtKB/Swiss-Prot Entry Name |
MOGT1_HUMAN  |
| 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  |
| Enzyme 69 GeneCard ID |
MOGAT1  |
| Enzyme 69 GenAtlas ID |
MOGAT1  |
| Enzyme 69 HGNC ID |
HGNC:18210  |
| Enzyme 69 Chromosome Location |
2 |
| Enzyme 69 Locus |
2q36.1 |
| Enzyme 69 SNPs |
SNPJam Report  |
| Enzyme 69 General References |
- 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
]
- 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
]
- 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
]
|
| 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 |
- Diacylglycerol O-acyltransferase 2-like protein 3
- Diacylglycerol acyltransferase 2
- 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 |
|
| Enzyme 70 Transmembrane Regions |
|
| Enzyme 70 Essentiality |
Not Available |
| Enzyme 70 GenBank ID Protein |
123227401  |
| Enzyme 70 UniProtKB/Swiss-Prot ID |
Q58HT5  |
| Enzyme 70 UniProtKB/Swiss-Prot Entry Name |
AWAT1_HUMAN  |
| 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  |
| Enzyme 70 GeneCard ID |
AWAT1  |
| Enzyme 70 GenAtlas ID |
AWAT1  |
| Enzyme 70 HGNC ID |
HGNC:23252  |
| Enzyme 70 Chromosome Location |
Not Available |
| Enzyme 70 Locus |
Not Available |
| Enzyme 70 SNPs |
SNPJam Report  |
| Enzyme 70 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Diacylglycerol O-acyltransferase 2-like protein 4
- Diacylglycerol O-acyltransferase candidate 4
- hDC4
- Long-chain-alcohol O-fatty-acyltransferase 2
- Multifunctional O-acyltransferase
- Wax synthase
- 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 |
|
| Enzyme 71 Transmembrane Regions |
|
| Enzyme 71 Essentiality |
Not Available |
| Enzyme 71 GenBank ID Protein |
49854214  |
| Enzyme 71 UniProtKB/Swiss-Prot ID |
Q6E213  |
| Enzyme 71 UniProtKB/Swiss-Prot Entry Name |
AWAT2_HUMAN  |
| 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  |
| Enzyme 71 GeneCard ID |
AWAT2  |
| Enzyme 71 GenAtlas ID |
AWAT2  |
| Enzyme 71 HGNC ID |
HGNC:23251  |
| Enzyme 71 Chromosome Location |
Not Available |
| Enzyme 71 Locus |
Not Available |
| Enzyme 71 SNPs |
SNPJam Report  |
| Enzyme 71 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Diacylglycerol O-acyltransferase candidate 3
- 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 |
|
| Enzyme 72 Transmembrane Regions |
|
| Enzyme 72 Essentiality |
Not Available |
| Enzyme 72 GenBank ID Protein |
34526048  |
| Enzyme 72 UniProtKB/Swiss-Prot ID |
Q6ZPD8  |
| Enzyme 72 UniProtKB/Swiss-Prot Entry Name |
DG2L6_HUMAN  |
| 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  |
| Enzyme 72 GeneCard ID |
DGAT2L6  |
| Enzyme 72 GenAtlas ID |
DGAT2L6  |
| Enzyme 72 HGNC ID |
HGNC:23250  |
| Enzyme 72 Chromosome Location |
Not Available |
| Enzyme 72 Locus |
Not Available |
| Enzyme 72 SNPs |
SNPJam Report  |
| Enzyme 72 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
|
| Enzyme 73 Transmembrane Regions |
|
| Enzyme 73 Essentiality |
Not Available |
| Enzyme 73 GenBank ID Protein |
Not Available |
| Enzyme 73 UniProtKB/Swiss-Prot ID |
Q6IED9  |
| Enzyme 73 UniProtKB/Swiss-Prot Entry Name |
DG2L7_HUMAN  |
| 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  |
| 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  |
| Enzyme 73 General References |
- 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
]
- 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
]
|
| Enzyme 73 Metabolite References |
Not Available |
|
Enzyme 74
[top]
|
| Enzyme 74 ID |
12901 |
| Enzyme 74 Name |
Sn1-specific diacylglycerol lipase alpha |
| Enzyme 74 Synonyms |
- DGL-alpha
- 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 |
|
| Enzyme 74 Transmembrane Regions |
- 23-43
61-81
102-122
137-157
|
| Enzyme 74 Essentiality |
Not Available |
| Enzyme 74 GenBank ID Protein |
27262632  |
| Enzyme 74 UniProtKB/Swiss-Prot ID |
Q9Y4D2  |
| Enzyme 74 UniProtKB/Swiss-Prot Entry Name |
DGLA_HUMAN  |
| 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  |
| Enzyme 74 GeneCard ID |
DAGLA  |
| Enzyme 74 GenAtlas ID |
DAGLA  |
| Enzyme 74 HGNC ID |
HGNC:1165  |
| Enzyme 74 Chromosome Location |
1 |
| Enzyme 74 Locus |
11q12.2 |
| Enzyme 74 SNPs |
SNPJam Report  |
| Enzyme 74 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 74 Metabolite References |
Not Available |
|
Enzyme 75
[top]
|
| Enzyme 75 ID |
12902 |
| Enzyme 75 Name |
Sn1-specific diacylglycerol lipase beta |
| Enzyme 75 Synonyms |
- DGL-beta
- 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 |
|
| Enzyme 75 Transmembrane Regions |
- 18-38
59-79
103-123
133-153
|
| Enzyme 75 Essentiality |
Not Available |
| Enzyme 75 GenBank ID Protein |
17864023  |
| Enzyme 75 UniProtKB/Swiss-Prot ID |
Q8NCG7  |
| Enzyme 75 UniProtKB/Swiss-Prot Entry Name |
DGLB_HUMAN  |
| 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  |
| Enzyme 75 GeneCard ID |
DAGLB  |
| Enzyme 75 GenAtlas ID |
DAGLB  |
| Enzyme 75 HGNC ID |
HGNC:28923  |
| Enzyme 75 Chromosome Location |
7 |
| Enzyme 75 Locus |
7p22.1 |
| Enzyme 75 SNPs |
SNPJam Report  |
| Enzyme 75 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 75 Metabolite References |
Not Available |
|
Enzyme 76
[top]
|
| Enzyme 76 ID |
12903 |
| Enzyme 76 Name |
2-acylglycerol O-acyltransferase 3 |
| Enzyme 76 Synonyms |
- Acyl-CoA:monoacylglycerol acyltransferase 3
- MGAT3
- Diacylglycerol O-acyltransferase candidate 7
- hDC7
- Diacylglycerol acyltransferase 2-like protein 7
- 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 |
|
| Enzyme 76 Transmembrane Regions |
|
| Enzyme 76 Essentiality |
Not Available |
| Enzyme 76 GenBank ID Protein |
29124967  |
| Enzyme 76 UniProtKB/Swiss-Prot ID |
Q86VF5  |
| Enzyme 76 UniProtKB/Swiss-Prot Entry Name |
MOGT3_HUMAN  |
| 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  |
| Enzyme 76 GeneCard ID |
MOGAT3  |
| Enzyme 76 GenAtlas ID |
MOGAT3  |
| Enzyme 76 HGNC ID |
HGNC:23249  |
| Enzyme 76 Chromosome Location |
7 |
| Enzyme 76 Locus |
7q22.1 |
| Enzyme 76 SNPs |
SNPJam Report  |
| Enzyme 76 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 76 Metabolite References |
Not Available |
|
Enzyme 77
[top]
|
| Enzyme 77 ID |
12904 |
| Enzyme 77 Name |
Diacylglycerol kinase kappa |
| Enzyme 77 Synonyms |
- DAG kinase kappa
- 142 kDa diacylglycerol kinase
- Diglyceride kinase kappa
- 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 |
- Glycerolipid Metabolism (map00561
)
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 77 Transmembrane Regions |
|
| Enzyme 77 Essentiality |
Not Available |
| Enzyme 77 GenBank ID Protein |
57753888  |
| Enzyme 77 UniProtKB/Swiss-Prot ID |
Q5KSL6  |
| Enzyme 77 UniProtKB/Swiss-Prot Entry Name |
DGKK_HUMAN  |
| 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  |
| Enzyme 77 GeneCard ID |
DGKK  |
| Enzyme 77 GenAtlas ID |
DGKK  |
| Enzyme 77 HGNC ID |
HGNC:32395  |
| Enzyme 77 Chromosome Location |
Not Available |
| Enzyme 77 Locus |
Not Available |
| Enzyme 77 SNPs |
SNPJam Report  |
| Enzyme 77 General References |
- 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
]
- 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
]
|
| Enzyme 77 Metabolite References |
Not Available |
|
Enzyme 78
[top]
|
| Enzyme 78 ID |
12905 |
| Enzyme 78 Name |
Serine/threonine-protein kinase D2 |
| Enzyme 78 Synonyms |
- 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 |
|
| Enzyme 78 Transmembrane Regions |
|
| Enzyme 78 Essentiality |
Not Available |
| Enzyme 78 GenBank ID Protein |
120659782  |
| Enzyme 78 UniProtKB/Swiss-Prot ID |
Q9BZL6  |
| Enzyme 78 UniProtKB/Swiss-Prot Entry Name |
KPCD2_HUMAN  |
| 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  |
| Enzyme 78 GeneCard ID |
PRKD2  |
| Enzyme 78 GenAtlas ID |
PRKD2  |
| Enzyme 78 HGNC ID |
HGNC:17293  |
| Enzyme 78 Chromosome Location |
1 |
| Enzyme 78 Locus |
19q13.3 |
| Enzyme 78 SNPs |
SNPJam Report  |
| Enzyme 78 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- PLC-L(2)
- PLC-L2
- Phospholipase C-L2
- Phospholipase C-epsilon-2
- 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 |
|
| Enzyme 79 Transmembrane Regions |
|
| Enzyme 79 Essentiality |
Not Available |
| Enzyme 79 GenBank ID Protein |
221219000  |
| Enzyme 79 UniProtKB/Swiss-Prot ID |
Q9UPR0  |
| Enzyme 79 UniProtKB/Swiss-Prot Entry Name |
PLCL2_HUMAN  |
| 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  |
| Enzyme 79 GeneCard ID |
PLCL2  |
| Enzyme 79 GenAtlas ID |
PLCL2  |
| Enzyme 79 HGNC ID |
HGNC:9064  |
| Enzyme 79 Chromosome Location |
3 |
| Enzyme 79 Locus |
3p24.3 |
| Enzyme 79 SNPs |
SNPJam Report  |
| Enzyme 79 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Drosophila retinal degeneration B homolog
- Phosphatidylinositol transfer protein, membrane-associated 1
- PITPnm 1
- Pyk2 N-terminal domain-interacting receptor 2
- 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 |
|
|
| 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 |
|
| Enzyme 80 Transmembrane Regions |
|
| Enzyme 80 Essentiality |
Not Available |
| Enzyme 80 GenBank ID Protein |
12667436  |
| Enzyme 80 UniProtKB/Swiss-Prot ID |
O00562  |
| Enzyme 80 UniProtKB/Swiss-Prot Entry Name |
PITM1_HUMAN  |
| 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  |
| Enzyme 80 GeneCard ID |
PITPNM1  |
| Enzyme 80 GenAtlas ID |
PITPNM1  |
| Enzyme 80 HGNC ID |
HGNC:9003  |
| Enzyme 80 Chromosome Location |
1 |
| Enzyme 80 Locus |
11q13 |
| Enzyme 80 SNPs |
SNPJam Report  |
| Enzyme 80 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Phosphoinositide phospholipase C-zeta-1
- Phospholipase C-zeta-1
- PLC-zeta-1
- 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 |
|
| Enzyme 81 Transmembrane Regions |
|
| Enzyme 81 Essentiality |
Not Available |
| Enzyme 81 GenBank ID Protein |
25053795  |
| Enzyme 81 UniProtKB/Swiss-Prot ID |
Q86YW0  |
| Enzyme 81 UniProtKB/Swiss-Prot Entry Name |
PLCZ1_HUMAN  |
| 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  |
| Enzyme 81 GeneCard ID |
PLCZ1  |
| Enzyme 81 GenAtlas ID |
PLCZ1  |
| Enzyme 81 HGNC ID |
HGNC:19218  |
| Enzyme 81 Chromosome Location |
1 |
| Enzyme 81 Locus |
12p12.3 |
| Enzyme 81 SNPs |
SNPJam Report  |
| Enzyme 81 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Adipose triglyceride lipase
- Calcium-independent phospholipase A2
- Desnutrin
- IPLA2-zeta
- Pigment epithelium-derived factor
- TTS2.2
- Transport-secretion protein 2
- 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 |
|
| Enzyme 82 Transmembrane Regions |
|
| Enzyme 82 Essentiality |
Not Available |
| Enzyme 82 GenBank ID Protein |
32698724  |
| Enzyme 82 UniProtKB/Swiss-Prot ID |
Q96AD5  |
| Enzyme 82 UniProtKB/Swiss-Prot Entry Name |
PLPL2_HUMAN  |
| 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  |
| Enzyme 82 GeneCard ID |
PNPLA2  |
| Enzyme 82 GenAtlas ID |
PNPLA2  |
| Enzyme 82 HGNC ID |
HGNC:30802  |
| Enzyme 82 Chromosome Location |
1 |
| Enzyme 82 Locus |
11p15.5 |
| Enzyme 82 SNPs |
SNPJam Report  |
| Enzyme 82 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 82 Metabolite References |
Not Available |
|
Enzyme 83
[top]
|
| Enzyme 83 ID |
13145 |
| Enzyme 83 Name |
A-kinase anchor protein 13 |
| Enzyme 83 Synonyms |
- AKAP-13
- AKAP-Lbc
- Breast cancer nuclear receptor-binding auxiliary protein
- Guanine nucleotide exchange factor Lbc
- Human thyroid-anchoring protein 31
- Lymphoid blast crisis oncogene
- LBC oncogene
- Non-oncogenic Rho GTPase-specific GTP exchange factor
- Protein kinase A-anchoring protein 13
- 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 |
|
|
| 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 |
|
| Enzyme 83 Transmembrane Regions |
|
| Enzyme 83 Essentiality |
Not Available |
| Enzyme 83 GenBank ID Protein |
15207794  |
| Enzyme 83 UniProtKB/Swiss-Prot ID |
Q12802  |
| Enzyme 83 UniProtKB/Swiss-Prot Entry Name |
AKP13_HUMAN  |
| 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  |
| Enzyme 83 GeneCard ID |
AKAP13  |
| Enzyme 83 GenAtlas ID |
AKAP13  |
| Enzyme 83 HGNC ID |
HGNC:371  |
| Enzyme 83 Chromosome Location |
1 |
| Enzyme 83 Locus |
15q24-q25 |
| Enzyme 83 SNPs |
SNPJam Report  |
| Enzyme 83 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 83 Metabolite References |
Not Available |
|
Enzyme 84
[top]
|
| Enzyme 84 ID |
13428 |
| Enzyme 84 Name |
RAS guanyl-releasing protein 1 |
| Enzyme 84 Synonyms |
- Calcium and DAG-regulated guanine nucleotide exchange factor II
- CalDAG-GEFII
- 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 |
|
|
| 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 |
|
| Enzyme 84 Transmembrane Regions |
|
| Enzyme 84 Essentiality |
Not Available |
| Enzyme 84 GenBank ID Protein |
190684644  |
| Enzyme 84 UniProtKB/Swiss-Prot ID |
O95267  |
| Enzyme 84 UniProtKB/Swiss-Prot Entry Name |
GRP1_HUMAN  |
| 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  |
| Enzyme 84 GeneCard ID |
RASGRP1  |
| Enzyme 84 GenAtlas ID |
RASGRP1  |
| Enzyme 84 HGNC ID |
HGNC:9878  |
| Enzyme 84 Chromosome Location |
1 |
| Enzyme 84 Locus |
15q14 |
| Enzyme 84 SNPs |
SNPJam Report  |
| Enzyme 84 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 84 Metabolite References |
Not Available |
|
Enzyme 85
[top]
|
| Enzyme 85 ID |
13429 |
| Enzyme 85 Name |
RAS guanyl-releasing protein 2 |
| Enzyme 85 Synonyms |
- Calcium and DAG-regulated guanine nucleotide exchange factor I
- CalDAG-GEFI
- Cdc25-like protein
- hCDC25L
- 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 |
|
|
| 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 |
|
| Enzyme 85 Transmembrane Regions |
|
| Enzyme 85 Essentiality |
Not Available |
| Enzyme 85 GenBank ID Protein |
149158727  |
| Enzyme 85 UniProtKB/Swiss-Prot ID |
Q7LDG7  |
| Enzyme 85 UniProtKB/Swiss-Prot Entry Name |
GRP2_HUMAN  |
| 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  |
| Enzyme 85 GeneCard ID |
RASGRP2  |
| Enzyme 85 GenAtlas ID |
RASGRP2  |
| Enzyme 85 HGNC ID |
HGNC:9879  |
| Enzyme 85 Chromosome Location |
1 |
| Enzyme 85 Locus |
11q13 |
| Enzyme 85 SNPs |
SNPJam Report  |
| Enzyme 85 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 85 Metabolite References |
Not Available |
|
Enzyme 86
[top]
|
| Enzyme 86 ID |
13538 |
| Enzyme 86 Name |
Myosin-IXb |
| Enzyme 86 Synonyms |
- 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 |
|
| Enzyme 86 Transmembrane Regions |
|
| Enzyme 86 Essentiality |
Not Available |
| Enzyme 86 GenBank ID Protein |
33356170  |
| Enzyme 86 UniProtKB/Swiss-Prot ID |
Q13459  |
| Enzyme 86 UniProtKB/Swiss-Prot Entry Name |
MYO9B_HUMAN  |
| 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  |
| Enzyme 86 GeneCard ID |
MYO9B  |
| Enzyme 86 GenAtlas ID |
MYO9B  |
| Enzyme 86 HGNC ID |
HGNC:7609  |
| Enzyme 86 Chromosome Location |
1 |
| Enzyme 86 Locus |
19p13.1 |
| Enzyme 86 SNPs |
SNPJam Report  |
| Enzyme 86 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- TrpC6
- Transient receptor protein 6
- 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 |
|
| 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  |
| Enzyme 87 UniProtKB/Swiss-Prot Entry Name |
TRPC6_HUMAN  |
| 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  |
| Enzyme 87 GeneCard ID |
TRPC6  |
| Enzyme 87 GenAtlas ID |
TRPC6  |
| Enzyme 87 HGNC ID |
HGNC:12338  |
| Enzyme 87 Chromosome Location |
1 |
| Enzyme 87 Locus |
11q22.1 |
| Enzyme 87 SNPs |
SNPJam Report  |
| Enzyme 87 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- TrpC7
- Transient receptor protein 7
- TRP-7
- 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 |
|
| 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  |
| Enzyme 88 UniProtKB/Swiss-Prot ID |
Q9HCX4  |
| Enzyme 88 UniProtKB/Swiss-Prot Entry Name |
TRPC7_HUMAN  |
| 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  |
| Enzyme 88 GeneCard ID |
TRPC7  |
| Enzyme 88 GenAtlas ID |
TRPC7  |
| Enzyme 88 HGNC ID |
HGNC:20754  |
| Enzyme 88 Chromosome Location |
5 |
| Enzyme 88 Locus |
5q31.1 |
| Enzyme 88 SNPs |
SNPJam Report  |
| Enzyme 88 General References |
- 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
]
- 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
]
- 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
]
|
| Enzyme 88 Metabolite References |
Not Available |
|
Enzyme 89
[top]
|
| Enzyme 89 ID |
13805 |
| Enzyme 89 Name |
Protein unc-13 homolog A |
| Enzyme 89 Synonyms |
- 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 |
|
| Enzyme 89 Transmembrane Regions |
|
| Enzyme 89 Essentiality |
Not Available |
| Enzyme 89 GenBank ID Protein |
283837842  |
| Enzyme 89 UniProtKB/Swiss-Prot ID |
Q9UPW8  |
| Enzyme 89 UniProtKB/Swiss-Prot Entry Name |
UN13A_HUMAN  |
| Enzyme 89 PDB ID |
1Y8F  |
| 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  |
| Enzyme 89 GeneCard ID |
UNC13A  |
| Enzyme 89 GenAtlas ID |
UNC13A  |
| Enzyme 89 HGNC ID |
HGNC:23150  |
| Enzyme 89 Chromosome Location |
1 |
| Enzyme 89 Locus |
19p13.11 |
| Enzyme 89 SNPs |
SNPJam Report  |
| Enzyme 89 General References |
- 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
]
- 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
]
- 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
]
|
| Enzyme 89 Metabolite References |
Not Available |
|
Enzyme 90
[top]
|
| Enzyme 90 ID |
13806 |
| Enzyme 90 Name |
Protein unc-13 homolog B |
| Enzyme 90 Synonyms |
- Munc13-2
- 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 |
|
| Enzyme 90 Transmembrane Regions |
|
| Enzyme 90 Essentiality |
Not Available |
| Enzyme 90 GenBank ID Protein |
2432000  |
| Enzyme 90 UniProtKB/Swiss-Prot ID |
O14795  |
| Enzyme 90 UniProtKB/Swiss-Prot Entry Name |
UN13B_HUMAN  |
| Enzyme 90 PDB ID |
1Y8F  |
| 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  |
| Enzyme 90 GeneCard ID |
UNC13B  |
| Enzyme 90 GenAtlas ID |
UNC13B  |
| Enzyme 90 HGNC ID |
HGNC:12566  |
| Enzyme 90 Chromosome Location |
9 |
| Enzyme 90 Locus |
9p13.3 |
| Enzyme 90 SNPs |
SNPJam Report  |
| Enzyme 90 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 90 Metabolite References |
Not Available |
|
Enzyme 91
[top]
|
| Enzyme 91 ID |
13807 |
| Enzyme 91 Name |
Protein unc-13 homolog C |
| Enzyme 91 Synonyms |
- 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 |
|
| Enzyme 91 Transmembrane Regions |
|
| Enzyme 91 Essentiality |
Not Available |
| Enzyme 91 GenBank ID Protein |
122937514  |
| Enzyme 91 UniProtKB/Swiss-Prot ID |
Q8NB66  |
| Enzyme 91 UniProtKB/Swiss-Prot Entry Name |
UN13C_HUMAN  |
| Enzyme 91 PDB ID |
1Y8F  |
| 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  |
| Enzyme 91 GeneCard ID |
UNC13C  |
| Enzyme 91 GenAtlas ID |
UNC13C  |
| Enzyme 91 HGNC ID |
HGNC:23149  |
| Enzyme 91 Chromosome Location |
1 |
| Enzyme 91 Locus |
15q21.3 |
| Enzyme 91 SNPs |
SNPJam Report  |
| Enzyme 91 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Guanine nucleotide exchange factor H1
- GEF-H1
- Microtubule-regulated Rho-GEF
- 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 |
|
|
| 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 |
|
| Enzyme 92 Transmembrane Regions |
|
| Enzyme 92 Essentiality |
Not Available |
| Enzyme 92 GenBank ID Protein |
253735775  |
| Enzyme 92 UniProtKB/Swiss-Prot ID |
Q92974  |
| Enzyme 92 UniProtKB/Swiss-Prot Entry Name |
ARHG2_HUMAN  |
| 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  |
| Enzyme 92 GeneCard ID |
ARHGEF2  |
| Enzyme 92 GenAtlas ID |
ARHGEF2  |
| Enzyme 92 HGNC ID |
HGNC:682  |
| Enzyme 92 Chromosome Location |
1 |
| Enzyme 92 Locus |
1q21-q22 |
| Enzyme 92 SNPs |
SNPJam Report  |
| Enzyme 92 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
|
|
| 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 |
|
| Enzyme 93 Transmembrane Regions |
|
| Enzyme 93 Essentiality |
Not Available |
| Enzyme 93 GenBank ID Protein |
26051258  |
| Enzyme 93 UniProtKB/Swiss-Prot ID |
Q8TDF6  |
| Enzyme 93 UniProtKB/Swiss-Prot Entry Name |
GRP4_HUMAN  |
| 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  |
| Enzyme 93 GeneCard ID |
RASGRP4  |
| Enzyme 93 GenAtlas ID |
RASGRP4  |
| Enzyme 93 HGNC ID |
HGNC:18958  |
| Enzyme 93 Chromosome Location |
1 |
| Enzyme 93 Locus |
19q13.1 |
| Enzyme 93 SNPs |
SNPJam Report  |
| Enzyme 93 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- CDC42-binding protein kinase alpha
- DMPK-like alpha
- Myotonic dystrophy kinase-related CDC42-binding kinase alpha
- MRCK alpha
- 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 |
|
| Enzyme 94 Transmembrane Regions |
|
| Enzyme 94 Essentiality |
Not Available |
| Enzyme 94 GenBank ID Protein |
30089962  |
| Enzyme 94 UniProtKB/Swiss-Prot ID |
Q5VT25  |
| Enzyme 94 UniProtKB/Swiss-Prot Entry Name |
MRCKA_HUMAN  |
| 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  |
| Enzyme 94 GeneCard ID |
CDC42BPA  |
| Enzyme 94 GenAtlas ID |
CDC42BPA  |
| Enzyme 94 HGNC ID |
HGNC:1737  |
| Enzyme 94 Chromosome Location |
1 |
| Enzyme 94 Locus |
1q42.11 |
| Enzyme 94 SNPs |
SNPJam Report  |
| Enzyme 94 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- CDC42-binding protein kinase beta
- DMPK-like beta
- Myotonic dystrophy kinase-related CDC42-binding kinase beta
- MRCK beta
- 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 |
|
| Enzyme 95 Transmembrane Regions |
|
| Enzyme 95 Essentiality |
Not Available |
| Enzyme 95 GenBank ID Protein |
115527097  |
| Enzyme 95 UniProtKB/Swiss-Prot ID |
Q9Y5S2  |
| Enzyme 95 UniProtKB/Swiss-Prot Entry Name |
MRCKB_HUMAN  |
| 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  |
| Enzyme 95 GeneCard ID |
CDC42BPB  |
| Enzyme 95 GenAtlas ID |
CDC42BPB  |
| Enzyme 95 HGNC ID |
HGNC:1738  |
| Enzyme 95 Chromosome Location |
1 |
| Enzyme 95 Locus |
14q32.3 |
| Enzyme 95 SNPs |
SNPJam Report  |
| Enzyme 95 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- CDC42-binding protein kinase gamma
- DMPK-like gamma
- Myotonic dystrophy kinase-related CDC42-binding kinase gamma
- MRCK gamma
- Myotonic dystrophy protein kinase-like gamma
- 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 |
|
| Enzyme 96 Transmembrane Regions |
|
| Enzyme 96 Essentiality |
Not Available |
| Enzyme 96 GenBank ID Protein |
156766068  |
| Enzyme 96 UniProtKB/Swiss-Prot ID |
Q6DT37  |
| Enzyme 96 UniProtKB/Swiss-Prot Entry Name |
MRCKG_HUMAN  |
| 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  |
| Enzyme 96 GeneCard ID |
CDC42BPG  |
| Enzyme 96 GenAtlas ID |
CDC42BPG  |
| Enzyme 96 HGNC ID |
HGNC:29829  |
| Enzyme 96 Chromosome Location |
1 |
| Enzyme 96 Locus |
11q13.1 |
| Enzyme 96 SNPs |
SNPJam Report  |
| Enzyme 96 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 96 Metabolite References |
Not Available |
|
Enzyme 97
[top]
|
| Enzyme 97 ID |
14330 |
| Enzyme 97 Name |
Guanine nucleotide exchange factor VAV3 |
| Enzyme 97 Synonyms |
- 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 |
|
|
| 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 |
|
| Enzyme 97 Transmembrane Regions |
|
| Enzyme 97 Essentiality |
Not Available |
| Enzyme 97 GenBank ID Protein |
3928847  |
| Enzyme 97 UniProtKB/Swiss-Prot ID |
Q9UKW4  |
| Enzyme 97 UniProtKB/Swiss-Prot Entry Name |
VAV3_HUMAN  |
| 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  |
| Enzyme 97 GeneCard ID |
VAV3  |
| Enzyme 97 GenAtlas ID |
VAV3  |
| Enzyme 97 HGNC ID |
HGNC:12659  |
| Enzyme 97 Chromosome Location |
1 |
| Enzyme 97 Locus |
1p13.3 |
| Enzyme 97 SNPs |
SNPJam Report  |
| Enzyme 97 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 97 Metabolite References |
Not Available |
|
Enzyme 98
[top]
|
| Enzyme 98 ID |
14426 |
| Enzyme 98 Name |
Acylglycerol kinase, mitochondrial |
| Enzyme 98 Synonyms |
- hAGK
- Multiple substrate lipid kinase
- HsMuLK
- MuLK
- 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 |
- Glycerolipid Metabolism (map00561
)
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| 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 |
|
| Enzyme 98 Transmembrane Regions |
|
| Enzyme 98 Essentiality |
Not Available |
| Enzyme 98 GenBank ID Protein |
8922701  |
| Enzyme 98 UniProtKB/Swiss-Prot ID |
Q53H12  |
| Enzyme 98 UniProtKB/Swiss-Prot Entry Name |
AGK_HUMAN  |
| 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  |
| Enzyme 98 GeneCard ID |
AGK  |
| Enzyme 98 GenAtlas ID |
AGK  |
| Enzyme 98 HGNC ID |
HGNC:21869  |
| Enzyme 98 Chromosome Location |
7 |
| Enzyme 98 Locus |
7q34 |
| Enzyme 98 SNPs |
SNPJam Report  |
| Enzyme 98 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
|
| Enzyme 99 Transmembrane Regions |
|
| Enzyme 99 Essentiality |
Not Available |
| Enzyme 99 GenBank ID Protein |
Not Available |
| Enzyme 99 UniProtKB/Swiss-Prot ID |
B0LPH7  |
| Enzyme 99 UniProtKB/Swiss-Prot Entry Name |
B0LPH7_HUMAN  |
| Enzyme 99 PDB ID |
Not Available |
| Enzyme 99 Cellular Location |
Not Available |
| Enzyme 99 Gene Sequence |
Not Available |
| Enzyme 99 GenBank Gene ID |
EU332867  |
| Enzyme 99 GeneCard ID |
B0LPH7  |
| 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  |
| 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 |
- 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 |
|
| Enzyme 100 Transmembrane Regions |
|
| Enzyme 100 Essentiality |
Not Available |
| Enzyme 100 GenBank ID Protein |
190341077  |
| Enzyme 100 UniProtKB/Swiss-Prot ID |
Q17RR3  |
| Enzyme 100 UniProtKB/Swiss-Prot Entry Name |
LIPR3_HUMAN  |
| 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  |
| Enzyme 100 GeneCard ID |
PNLIPRP3  |
| Enzyme 100 GenAtlas ID |
PNLIPRP3  |
| Enzyme 100 HGNC ID |
HGNC:23492  |
| Enzyme 100 Chromosome Location |
1 |
| Enzyme 100 Locus |
10q25.3 |
| Enzyme 100 SNPs |
SNPJam Report  |
| Enzyme 100 General References |
- 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
]
- 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
]
- 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
]
|
| 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 |
|
| Enzyme 101 Transmembrane Regions |
|
| Enzyme 101 Essentiality |
Not Available |
| Enzyme 101 GenBank ID Protein |
161611364  |
| Enzyme 101 UniProtKB/Swiss-Prot ID |
A9JR72  |
| Enzyme 101 UniProtKB/Swiss-Prot Entry Name |
A9JR72_HUMAN  |
| 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  |
| Enzyme 101 GeneCard ID |
CDC42BPB  |
| 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  |
| Enzyme 101 General References |
- 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
]
|
| 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 |
|
| Enzyme 102 Transmembrane Regions |
|
| Enzyme 102 Essentiality |
Not Available |
| Enzyme 102 GenBank ID Protein |
189065389  |
| Enzyme 102 UniProtKB/Swiss-Prot ID |
B2R5T1  |
| Enzyme 102 UniProtKB/Swiss-Prot Entry Name |
B2R5T1_HUMAN  |
| 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  |
| Enzyme 102 GeneCard ID |
Not Available |
| Enzyme 102 GenAtlas ID |
Not Available |
| Enzyme 102 HGNC ID |
HGNC:9402  |
| 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 |
- 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 |
|
| Enzyme 103 Transmembrane Regions |
|
| Enzyme 103 Essentiality |
Not Available |
| Enzyme 103 GenBank ID Protein |
167621456  |
| Enzyme 103 UniProtKB/Swiss-Prot ID |
Q6VAB6  |
| Enzyme 103 UniProtKB/Swiss-Prot Entry Name |
KSR2_HUMAN  |
| 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  |
| Enzyme 103 GenAtlas ID |
KSR2  |
| Enzyme 103 HGNC ID |
HGNC:18610  |
| Enzyme 103 Chromosome Location |
1 |
| Enzyme 103 Locus |
12q24.22-q24.23 |
| Enzyme 103 SNPs |
SNPJam Report  |
| Enzyme 103 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
|
| Enzyme 104 Transmembrane Regions |
|
| Enzyme 104 Essentiality |
Not Available |
| Enzyme 104 GenBank ID Protein |
Not Available |
| Enzyme 104 UniProtKB/Swiss-Prot ID |
A8K4N0  |
| Enzyme 104 UniProtKB/Swiss-Prot Entry Name |
A8K4N0_HUMAN  |
| Enzyme 104 PDB ID |
Not Available |
| Enzyme 104 Cellular Location |
Not Available |
| Enzyme 104 Gene Sequence |
Not Available |
| Enzyme 104 GenBank Gene ID |
AK290995  |
| Enzyme 104 GeneCard ID |
Not Available |
| Enzyme 104 GenAtlas ID |
Not Available |
| Enzyme 104 HGNC ID |
HGNC:9412  |
| 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 |
|
| Enzyme 105 Transmembrane Regions |
|
| Enzyme 105 Essentiality |
Not Available |
| Enzyme 105 GenBank ID Protein |
194375938  |
| Enzyme 105 UniProtKB/Swiss-Prot ID |
B4DF52  |
| Enzyme 105 UniProtKB/Swiss-Prot Entry Name |
B4DF52_HUMAN  |
| Enzyme 105 PDB ID |
1XJD  |
| 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  |
| Enzyme 105 GeneCard ID |
Not Available |
| Enzyme 105 GenAtlas ID |
Not Available |
| Enzyme 105 HGNC ID |
HGNC:9410  |
| 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 |
- C1 domain-containing phosphatase and tensin homolog
- C1-TEN
- 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 |
|
| 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 |
|
| Enzyme 106 Transmembrane Regions |
|
| Enzyme 106 Essentiality |
Not Available |
| Enzyme 106 GenBank ID Protein |
38787957  |
| Enzyme 106 UniProtKB/Swiss-Prot ID |
Q63HR2  |
| Enzyme 106 UniProtKB/Swiss-Prot Entry Name |
TENC1_HUMAN  |
| 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  |
| Enzyme 106 GeneCard ID |
TENC1  |
| Enzyme 106 GenAtlas ID |
TENC1  |
| Enzyme 106 HGNC ID |
HGNC:19737  |
| Enzyme 106 Chromosome Location |
1 |
| Enzyme 106 Locus |
12q13.13 |
| Enzyme 106 SNPs |
SNPJam Report  |
| Enzyme 106 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
|
| Enzyme 107 Transmembrane Regions |
|
| Enzyme 107 Essentiality |
Not Available |
| Enzyme 107 GenBank ID Protein |
62088530  |
| Enzyme 107 UniProtKB/Swiss-Prot ID |
Q59FI5  |
| Enzyme 107 UniProtKB/Swiss-Prot Entry Name |
Q59FI5_HUMAN  |
| Enzyme 107 PDB ID |
1DSY  |
| 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  |
| Enzyme 107 GeneCard ID |
Not Available |
| Enzyme 107 GenAtlas ID |
Not Available |
| Enzyme 107 HGNC ID |
HGNC:9393  |
| 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 |
|
| Enzyme 108 Transmembrane Regions |
|
| Enzyme 108 Essentiality |
Not Available |
| Enzyme 108 GenBank ID Protein |
75677325  |
| Enzyme 108 UniProtKB/Swiss-Prot ID |
Q8IVT5  |
| Enzyme 108 UniProtKB/Swiss-Prot Entry Name |
KSR1_HUMAN  |
| 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  |
| Enzyme 108 GenAtlas ID |
KSR1  |
| Enzyme 108 HGNC ID |
HGNC:6465  |
| Enzyme 108 Chromosome Location |
1 |
| Enzyme 108 Locus |
17q11.1-q11.2 |
| Enzyme 108 SNPs |
SNPJam Report  |
| Enzyme 108 General References |
- 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
]
- 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
]
- 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
]
- Roy F, Therrien M: MAP kinase module: the Ksr connection. Curr Biol. 2002 Apr 30;12(9):R325-7. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
|
| Enzyme 109 Transmembrane Regions |
|
| Enzyme 109 Essentiality |
Not Available |
| Enzyme 109 GenBank ID Protein |
189054067  |
| Enzyme 109 UniProtKB/Swiss-Prot ID |
B2R9M7  |
| Enzyme 109 UniProtKB/Swiss-Prot Entry Name |
B2R9M7_HUMAN  |
| 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  |
| Enzyme 109 GeneCard ID |
Not Available |
| Enzyme 109 GenAtlas ID |
Not Available |
| Enzyme 109 HGNC ID |
HGNC:9401  |
| 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 |
- 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 |
|
| Enzyme 110 Transmembrane Regions |
|
| Enzyme 110 Essentiality |
Not Available |
| Enzyme 110 GenBank ID Protein |
194382284  |
| Enzyme 110 UniProtKB/Swiss-Prot ID |
B4DJN5  |
| Enzyme 110 UniProtKB/Swiss-Prot Entry Name |
B4DJN5_HUMAN  |
| 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  |
| Enzyme 110 GeneCard ID |
PRKCH  |
| Enzyme 110 GenAtlas ID |
PRKCH  |
| Enzyme 110 HGNC ID |
HGNC:9403  |
| Enzyme 110 Chromosome Location |
1 |
| Enzyme 110 Locus |
14q23.1 |
| Enzyme 110 SNPs |
SNPJam Report  |
| Enzyme 110 General References |
- 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
]
|
| 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 |
|
| Enzyme 111 Transmembrane Regions |
|
| Enzyme 111 Essentiality |
Not Available |
| Enzyme 111 GenBank ID Protein |
189067482  |
| Enzyme 111 UniProtKB/Swiss-Prot ID |
B2RCZ4  |
| Enzyme 111 UniProtKB/Swiss-Prot Entry Name |
B2RCZ4_HUMAN  |
| 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  |
| Enzyme 111 GeneCard ID |
Not Available |
| Enzyme 111 GenAtlas ID |
Not Available |
| Enzyme 111 HGNC ID |
HGNC:9404  |
| 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 |
|
| Enzyme 112 Transmembrane Regions |
|
| Enzyme 112 Essentiality |
Not Available |
| Enzyme 112 GenBank ID Protein |
194376832  |
| Enzyme 112 UniProtKB/Swiss-Prot ID |
B4DFV1  |
| Enzyme 112 UniProtKB/Swiss-Prot Entry Name |
B4DFV1_HUMAN  |
| 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  |
| Enzyme 112 GeneCard ID |
Not Available |
| Enzyme 112 GenAtlas ID |
Not Available |
| Enzyme 112 HGNC ID |
HGNC:9399  |
| 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 |
|
| Enzyme 113 Transmembrane Regions |
|
| Enzyme 113 Essentiality |
Not Available |
| Enzyme 113 GenBank ID Protein |
62088922  |
| Enzyme 113 UniProtKB/Swiss-Prot ID |
Q59EZ0  |
| Enzyme 113 UniProtKB/Swiss-Prot Entry Name |
Q59EZ0_HUMAN  |
| Enzyme 113 PDB ID |
1TBO  |
| 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  |
| Enzyme 113 GeneCard ID |
Not Available |
| Enzyme 113 GenAtlas ID |
Not Available |
| Enzyme 113 HGNC ID |
HGNC:9402  |
| 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 |
|
| Enzyme 114 Transmembrane Regions |
|
| Enzyme 114 Essentiality |
Not Available |
| Enzyme 114 GenBank ID Protein |
27261723  |
| Enzyme 114 UniProtKB/Swiss-Prot ID |
Q8IWQ7  |
| Enzyme 114 UniProtKB/Swiss-Prot Entry Name |
Q8IWQ7_HUMAN  |
| 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  |
| Enzyme 114 GeneCard ID |
CDC42BPA  |
| Enzyme 114 GenAtlas ID |
CDC42BPA  |
| Enzyme 114 HGNC ID |
HGNC:1737  |
| Enzyme 114 Chromosome Location |
1 |
| Enzyme 114 Locus |
1q42.11 |
| Enzyme 114 SNPs |
SNPJam Report  |
| 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 |
|
| Enzyme 115 Transmembrane Regions |
|
| Enzyme 115 Essentiality |
Not Available |
| Enzyme 115 GenBank ID Protein |
31544941  |
| Enzyme 115 UniProtKB/Swiss-Prot ID |
Q7Z727  |
| Enzyme 115 UniProtKB/Swiss-Prot Entry Name |
Q7Z727_HUMAN  |
| Enzyme 115 PDB ID |
1DSY  |
| 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  |
| Enzyme 115 GeneCard ID |
PRKCA  |
| 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  |
| Enzyme 115 General References |
- 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
]
|
| 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 |
|
| Enzyme 116 Transmembrane Regions |
|
| Enzyme 116 Essentiality |
Not Available |
| Enzyme 116 GenBank ID Protein |
16552576  |
| Enzyme 116 UniProtKB/Swiss-Prot ID |
Q96MF2  |
| Enzyme 116 UniProtKB/Swiss-Prot Entry Name |
STAC3_HUMAN  |
| 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  |
| Enzyme 116 GeneCard ID |
STAC3  |
| Enzyme 116 GenAtlas ID |
STAC3  |
| Enzyme 116 HGNC ID |
HGNC:28423  |
| Enzyme 116 Chromosome Location |
1 |
| Enzyme 116 Locus |
12q13.3 |
| Enzyme 116 SNPs |
SNPJam Report  |
| Enzyme 116 General References |
- 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
]
- 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
]
|
| Enzyme 116 Metabolite References |
Not Available |
|
Enzyme 117
[top]
|
| Enzyme 117 ID |
17262 |
| Enzyme 117 Name |
GEM-interacting protein |
| Enzyme 117 Synonyms |
- 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 |
|
|
| 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 |
|
| Enzyme 117 Transmembrane Regions |
|
| Enzyme 117 Essentiality |
Not Available |
| Enzyme 117 GenBank ID Protein |
7380947  |
| Enzyme 117 UniProtKB/Swiss-Prot ID |
Q9P107  |
| Enzyme 117 UniProtKB/Swiss-Prot Entry Name |
GMIP_HUMAN  |
| 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  |
| Enzyme 117 GeneCard ID |
GMIP  |
| Enzyme 117 GenAtlas ID |
GMIP  |
| Enzyme 117 HGNC ID |
HGNC:24852  |
| Enzyme 117 Chromosome Location |
1 |
| Enzyme 117 Locus |
19p13.11 |
| Enzyme 117 SNPs |
SNPJam Report  |
| Enzyme 117 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- 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 |
|
| Enzyme 118 Transmembrane Regions |
|
| Enzyme 118 Essentiality |
Not Available |
| Enzyme 118 GenBank ID Protein |
46447820  |
| Enzyme 118 UniProtKB/Swiss-Prot ID |
Q6ZN54  |
| Enzyme 118 UniProtKB/Swiss-Prot Entry Name |
DEFI8_HUMAN  |
| 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  |
| Enzyme 118 GeneCard ID |
DEF8  |
| Enzyme 118 GenAtlas ID |
DEF8  |
| Enzyme 118 HGNC ID |
HGNC:25969  |
| Enzyme 118 Chromosome Location |
1 |
| Enzyme 118 Locus |
16q24.3 |
| Enzyme 118 SNPs |
SNPJam Report  |
| Enzyme 118 General References |
- 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
]
- 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
]
|
| Enzyme 118 Metabolite References |
Not Available |
|
Enzyme 119
[top]
|
| Enzyme 119 ID |
17264 |
| Enzyme 119 Name |
Rho GTPase-activating protein 29 |
| Enzyme 119 Synonyms |
- PTPL1-associated RhoGAP protein 1
- 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 |
|
|
| 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 |
|
| Enzyme 119 Transmembrane Regions |
|
| Enzyme 119 Essentiality |
Not Available |
| Enzyme 119 GenBank ID Protein |
134304853  |
| Enzyme 119 UniProtKB/Swiss-Prot ID |
Q52LW3  |
| Enzyme 119 UniProtKB/Swiss-Prot Entry Name |
RHG29_HUMAN  |
| 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  |
| Enzyme 119 GeneCard ID |
ARHGAP29  |
| Enzyme 119 GenAtlas ID |
ARHGAP29  |
| Enzyme 119 HGNC ID |
HGNC:30207  |
| Enzyme 119 Chromosome Location |
1 |
| Enzyme 119 Locus |
1p22.1 |
| Enzyme 119 SNPs |
SNPJam Report  |
| Enzyme 119 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- 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 |
|