|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5454 |
| Enzyme 1 Name |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1 |
| Enzyme 1 Synonyms |
- PLC-154
- Phosphoinositide phospholipase C-beta-1
- Phospholipase C-I
- PLC-I
- Phospholipase C-beta-1
- PLC-beta-1
|
| Enzyme 1 Gene Name |
PLCB1 |
| Enzyme 1 Protein Sequence |
>1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1
MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKE
TELLDLSLVKDARCGRHAKAPKDPKLRELLDVGNIGRLEQRMITVVYGPDLVNISHLNLV
AFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSA
DRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYL
TVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLARKGQISVDGFMRYLS
GEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCV
ELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQ
QAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKK
KLSEQASNTYSDSSSMFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEM
SNLVNYIQPVKFESFEISKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPK
GTRVDSSNYMPQLFWNAGCQMVALNFQTMDLAMQINMGMYEYNGKSGYRLKPEFMRRPDK
HFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQG
NAVNPVWEEEPIVFKKVVLPTLACLRIAVYEEGGKFIGHRILPVQAIRPGYHYICLRNER
NQPLTLPAVFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKK
EADPGETPSEAPSEARTTPAENGVNHTTTLTPKPPSQALHSQPAPGSVKAPAKTEDLIQS
VLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTTKYNEIQNDYL
RRRAALEKSAKKDSKKKSEPSSPDHGSSTIEQDLAALDAEMTQKLIDLKDKQQQQLLNLR
QEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKI
TEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHKEIRQQILDEKP
KLQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPLSLSSDPGKVNHKTPSS
EELGGDIPGKEFDTPL
|
| Enzyme 1 Number of Residues |
1216 |
| Enzyme 1 Molecular Weight |
138565.8 |
| Enzyme 1 Theoretical pI |
6.12 |
| Enzyme 1 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- lipase activity
- metal ion binding
- phosphoinositide phospholipase C activity
- phospholipase C activity
- phospholipase activity
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- biological regulation
- intracellular signaling pathway
- lipid catabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
- regulation of biological process
- regulation of cellular process
- signal transduction
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in calcium ion binding |
| Enzyme 1 Specific Function |
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes |
| Enzyme 1 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 1 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
12083581  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q9NQ66  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
PLCB1_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>3651 bp
ATGGCCGGGGCTCAACCCGGAGTGCACGCCTTGCAACTCAAGCCCGTGTGCGTGTCCGAC
AGCCTCAAGAAGGGCACCAAATTCGTCAAGTGGGATGATGACTCAACTATTGTTACTCCA
ATTATTTTGAGGACTGACCCTCAGGGATTTTTCTTTTACTGGACAGATCAAAACAAGGAG
ACAGAGCTACTGGATCTCAGCCTTGTCAAAGATGCCAGATGTGGGAGACACGCCAAAGCT
CCCAAGGACCCCAAATTACGTGAACTTTTGGATGTGGGGAACATCGGGCGCCTGGAGCAG
CGCATGATCACAGTGGTGTATGGGCCTGACCTCGTGAACATCTCCCATTTGAATCTCGTG
GCTTTCCAAGAAGAAGTGGCCAAGGAATGGACAAATGAGGTTTTCAGTTTGGCAACAAAC
CTGCTGGCCCAAAACATGTCCAGGGATGCATTTCTGGAAAAAGCCTATACTAAACTTAAG
CTGCAAGTCACTCCAGAAGGGCGTATTCCTCTCAAAAACATATATCGCTTGTTTTCAGCA
GATCGGAAGCGAGTTGAAACTGCTTTAGAGGCTTGTAGTCTTCCATCTTCAAGGAATGAT
TCAATACCTCAAGAAGATTTCACTCCAGAAGTGTACAGAGTTTTCCTCAACAACCTTTGC
CCTCGACCTGAAATTGATAACATCTTTTCAGAATTTGGTGCAAAAAGCAAACCATATCTT
ACCGTTGATCAGATGATGGATTTTATCAACCTTAAGCAGCGAGATCCTCGGCTTAATGAA
ATACTTTATCCACCTCTAAAACAAGAGCAAGTCCAAGTATTGATTGAGAAGTATGAACCC
AACAACAGCCTCGCCAGAAAAGGACAAATATCAGTGGATGGGTTCATGCGCTATCTGAGT
GGAGAAGAAAACGGAGTCGTTTCACCTGAGAAACTGGATTTGAATGAAGACATGTCTCAG
CCCCTTTCTCACTATTTCATTAATTCCTCGCACAACACCTACCTCACAGCTGGCCAACTG
GCTGGAAACTCCTCTGTTGAGATGTATCGCCAAGTGCTCCTGTCTGGTTGTCGCTGTGTG
GAGCTGGACTGCTGGAAGGGACGGACTGCAGAAGAGGAACCTGTCATCACCCATGGCTTC
ACCATGACAACTGAAATATCTTTCAAGGAAGTGATAGAAGCAATTGCGGAGTGTGCATTT
AAGACTTCACCTTTTCCAATTCTCCTTTCGTTTGAGAACCATGTGGATTCCCCAAAGCAG
CAAGCCAAGATGGCGGAGTACTGCCGACTGATCTTTGGGGATGCCCTTCTCATGGAGCCC
CTGGAAAAATATCCACTGGAATCTGGAGTTCCTCTTCCAAGCCCTATGGATTTAATGTAT
AAAATTTTGGTGAAAAATAAGAAGAAATCACACAAGTCATCAGAAGGAAGCGGCAAAAAG
AAGCTCTCAGAACAAGCCTCCAACACCTACAGTGACTCCTCCAGCATGTTCGAGCCCTCA
TCCCCAGGAGCCGGAGAAGCTGATACGGAAAGTGACGACGACGATGATGATGATGACTGT
AAAAAATCTTCAATGGATGAGGGGACTGCTGGAAGTGAGGCTATGGCCACAGAAGAAATG
TCTAATCTGGTGAACTATATTCAGCCAGTCAAGTTTGAGTCATTTGAAATTTCAAAAAAA
AGAAATAAAAGTTTTGAAATGTCTTCCTTCGTGGAAACCAAAGGACTTGAACAACTCACC
AAGTCTCCAGTGGAATTTGTAGAATATAACAAAATGCAGCTTAGCAGGATATATCCAAAA
GGAACACGTGTGGATTCATCCAACTATATGCCTCAGCTCTTCTGGAATGCAGGTTGTCAG
ATGGTGGCACTTAATTTCCAGACAATGGACCTGGCTATGCAAATAAATATGGGGATGTAT
GAATACAACGGGAAGAGTGGCTACAGATTGAAGCCAGAGTTCATGAGGAGGCCTGACAAG
CATTTTGATCCATTTACTGAAGGCATCGTAGATGGGATAGTGGCAAACACTTTGTCTGTT
AAGATTATTTCAGGTCAGTTTCTTTCTGATAAGAAAGTTGGGACTTACGTGGAAGTAGAT
ATGTTTGGTTTGCCTGTGGATACAAGGAGGAAGGCATTTAAGACCAAAACATCCCAAGGA
AATGCTGTGAATCCTGTCTGGGAAGAAGAACCTATTGTGTTCAAAAAGGTGGTTCTTCCT
ACTCTGGCCTGTTTGAGAATAGCAGTTTATGAAGAAGGAGGTAAATTCATTGGCCACCGT
ATCTTGCCAGTGCAAGCCATTCGGCCAGGCTATCACTATATCTGTCTAAGGAATGAAAGG
AACCAGCCTCTGACGCTGCCTGCTGTCTTTGTCTACATAGAAGTGAAAGACTATGTGCCA
GACACATATGCAGATGTCATCGAAGCTTTATCAAACCCAATCCGATATGTGAACCTGATG
GAACAGAGAGCTAAGCAATTGGCTGCTTTGACACTGGAAGATGAAGAAGAAGTAAAGAAA
GAGGCTGATCCTGGAGAAACACCATCAGAGGCTCCAAGTGAAGCGAGAACGACTCCAGCA
GAAAATGGGGTGAATCACACTACAACCCTGACACCCAAGCCACCCTCCCAGGCTCTCCAC
AGCCAGCCAGCTCCAGGTTCTGTAAAGGCACCTGCCAAAACAGAAGATCTTATTCAGAGT
GTCTTAACAGAAGTGGAAGCACAGACCATCGAAGAACTAAAGCAACAGAAATCGTTTGTG
AAACTTCAAAAGAAACACTACAAAGAAATGAAAGACCTGGTTAAGAGACACCACAAGAAA
ACCACTGACCTTATCAAAGAACACACTACCAAGTATAATGAAATTCAGAATGACTACTTG
AGAAGGAGAGCCGCTTTGGAAAAGTCCGCCAAAAAGGACAGTAAGAAAAAATCGGAACCC
AGCAGCCCTGATCATGGTTCATCAACGATTGAGCAAGACCTCGCTGCTCTGGATGCTGAA
ATGACCCAAAAGTTAATAGACTTGAAGGACAAACAACAGCAGCAGCTGCTTAATCTTCGG
CAAGAACAGTATTATAGTGAAAAATACCAGAAGCGAGAACATATTAAACTGCTTATTCAA
AAGTTGACGGATGTCGCAGAAGAGTGTCAGAACAATCAGTTAAAGAAGCTCAAAGAAATC
TGTGAGAAAGAAAAGAAAGAATTAAAGAAGAAAATGGATAAAAAGAGGCAGGAGAAGATA
ACAGAAGCTAAATCCAAAGACAAAAGTCAGATGGAAGAGGAGAAGACAGAGATGATCCGG
TCATATATCCAGGAAGTGGTGCAGTATATCAAGAGGCTAGAAGAAGCGCAAAGTAAACGG
CAAGAAAAACTCGTAGAGAAACACAAGGAAATACGTCAGCAGATCCTGGATGAAAAGCCC
AAGCTGCAGGTGGAGCTGGAGCAAGAATACCAAGACAAATTCAAAAGACTGCCCCTCGAG
ATTTTGGAATTCGTGCAGGAAGCCATGAAAGGAAAGATCAGTGAAGACAGCAATCACGGT
TCTGCCCCTCTCTCCCTGTCCTCAGACCCTGGAAAAGTGAACCACAAGACTCCCTCCAGT
GAGGAGCTGGGAGGAGACATCCCAGGAAAAGAATTTGATACTCCTCTGTGA
|
| Enzyme 1 GenBank Gene ID |
NM_015192.2  |
| Enzyme 1 GeneCard ID |
PLCB1  |
| Enzyme 1 GenAtlas ID |
PLCB1  |
| Enzyme 1 HGNC ID |
HGNC:15917  |
| Enzyme 1 Chromosome Location |
2 |
| Enzyme 1 Locus |
20p12 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 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 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5455 |
| Enzyme 2 Name |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4 |
| Enzyme 2 Synonyms |
- Phosphoinositide phospholipase C-beta-4
- Phospholipase C-beta-4
- PLC-beta-4
|
| Enzyme 2 Gene Name |
PLCB4 |
| Enzyme 2 Protein Sequence |
>1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4
MAKPYEFNWQKEVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWRSEGKEGQVL
ECSLINSIRSGAIPKDPKILAALEAVGKSENDLEGRIVCVCSGTDLVNISFTYMVAENPE
VTKQWVEGLRSIIHNFRANNVSPMTCLKKHWMKLAFMTNTNGKIPVRSITRTFASGKTEK
VIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVD
QLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE
NAPVFLDRLELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELD
CWDGKGEDQEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKM
SKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRLKPEVEKKQLEALRSM
MEAGESASPANILEDDNEEEIESADQEEEAHPEFKFGNELSADDLGHKEAVANSVKKGLV
TVEDEQAWMASYKYVGATTNIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVG
LGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQL
NQGKFEYNGSCGYLLKPDFMRRPDRTFDPFSETPVDGVIAATCSVQVISGQFLSDKKIGT
YVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNK
LIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNIVLKTYVPDGFGDIVDALSDPKK
FLSITEKRADQMRAMGIETSDIADVPSDTSKNDKKGKANTAKANVTPQSSSELRPTTTAA
LASGVEAKKGIELIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHCTQ
VDKIVAQYDKEKSTHEKILEKAMKKKGGSNCLEMKKETEIKIQTLTSDHKSKVKEIVAQH
TKEWSEMINTHSAEEQEIRDLHLSQQCELLKKLLINAHEQQTQQLKLSHDRESKEMRAHQ
AKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQ
LEHLEFLEKQNEQAKEMQQMVKLEAEMDRRPATVV
|
| Enzyme 2 Number of Residues |
1175 |
| Enzyme 2 Molecular Weight |
134462.6 |
| Enzyme 2 Theoretical pI |
6.90 |
| Enzyme 2 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- lipase activity
- metal ion binding
- phosphoinositide phospholipase C activity
- phospholipase C activity
- phospholipase activity
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- biological regulation
- intracellular signaling pathway
- lipid metabolic process
- metabolic process
- primary metabolic process
- regulation of biological process
- regulation of cellular process
- signal transduction
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in calcium ion binding |
| Enzyme 2 Specific Function |
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This form has a role in retina signal transduction |
| Enzyme 2 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 2 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
57284038  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q15147  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PLCB4_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>3528 bp
ATGGCCAAACCTTATGAATTTAACTGGCAGAAGGAAGTTCCCTCCTTTTTGCAAGAAGGA
GCAGTTTTTGACAGATACGAGGAGGAATCCTTTGTGTTTGAACCCAACTGCCTCTTCAAA
GTGGATGAGTTTGGCTTCTTTCTGACATGGAGAAGTGAAGGCAAGGAAGGACAGGTGCTA
GAATGCTCCCTCATCAACAGTATTCGGTCGGGAGCCATACCAAAGGATCCCAAAATCTTG
GCTGCTCTTGAAGCTGTTGGAAAATCAGAAAATGATCTGGAAGGGCGGATAGTTTGTGTC
TGCAGTGGCACAGATCTAGTGAACATTAGTTTTACCTACATGGTGGCTGAAAATCCAGAA
GTAACTAAGCAATGGGTAGAAGGCCTGAGATCAATCATACACAACTTCAGGGCCAACAAC
GTCAGTCCAATGACATGCCTCAAGAAACACTGGATGAAATTGGCATTTATGACCAACACA
AATGGTAAAATTCCAGTTAGGAGTATTACTAGAACATTTGCATCGGGAAAAACAGAAAAG
GTGATCTTTCAAGCACTCAAGGAGTTAGGTCTTCCCAGTGGAAAGAATGATGAAATTGAG
CCCACAGCATTTTCTTATGAAAAGTTCTATGAACTGACACAAAAGATTTGTCCTCGGACA
GATATAGAAGATCTTTTCAAAAAAATCAATGGAGACAAAACTGATTATTTAACGGTAGAC
CAATTAGTGAGCTTTCTAAATGAACATCAACGAGATCCTCGATTGAATGAAATTTTATTT
CCATTTTATGATGCCAAAAGGGCAATGCAGATCATTGAGATGTATGAACCTGATGAAGAT
TTGAAGAAAAAAGGCCTTATATCAAGTGATGGGTTTTGCAGATATCTGATGTCAGATGAA
AACGCCCCAGTCTTCCTAGATCGTTTAGAACTTTACCAAGAAATGGACCATCCTCTGGCT
CACTACTTCATCAGTTCTTCCCATAACACTTATCTCACTGGCAGACAGTTCGGCGGGAAG
TCTTCGGTAGAAATGTACAGACAGGTTCTCCTGGCTGGTTGCAGATGTGTTGAACTTGAC
TGCTGGGATGGAAAAGGTGAAGACCAAGAACCAATAATAACTCATGGAAAAGCAATGTGT
ACAGATATCCTTTTTAAGGATGTAATTCAAGCCATCAAGGAAACTGCATTTGTCACATCA
GAATATCCTGTAATTCTCTCCTTTGAAAATCACTGCAGCAAATATCAACAGTACAAGATG
TCCAAATATTGCGAAGATCTATTTGGGGATCTCCTGTTGAAACAAGCACTTGAATCACAT
CCACTTGAACCAGGCAGGGCTTTGCCATCCCCCAATGACCTCAAAAGAAAAATACTCATA
AAAAACAAGCGGCTGAAACCTGAAGTTGAAAAAAAACAGCTGGAAGCTTTGAGAAGCATG
ATGGAAGCTGGAGAATCTGCCTCCCCAGCAAACATCTTAGAGGACGATAATGAAGAGGAG
ATCGAAAGTGCTGACCAAGAGGAGGAAGCTCACCCCGAATTCAAATTTGGAAATGAACTT
TCTGCTGATGACTTGGGTCACAAGGAAGCTGTTGCAAATAGCGTCAAGAAGGGCCTGGTC
ACTGTAGAAGATGAGCAGGCGTGGATGGCATCTTATAAATATGTAGGTGCTACCACTAAT
ATCCATCCATATTTGTCCACAATGATCAACTACGCCCAGCCTGTAAAGTTTCAAGGTTTC
CATGTGGCAGAAGAACGCAATATTCATTATAACATGTCTTCTTTTAATGAATCAGTCGGT
CTTGGCTACTTGAAGACACATGCAATTGAATTTGTCAATTATAACAAACGGCAAATGAGT
CGCATTTACCCCAAGGGAGGCCGAGTCGATTCCAGTAATTACATGCCTCAGATTTTCTGG
AACGCTGGCTGCCAGATGGTTTCACTGAACTATCAAACCCCAGATTTAGCGATGCAATTG
AATCAGGGAAAATTTGAGTATAATGGATCGTGCGGGTACCTTCTCAAACCAGATTTCATG
AGGCGGCCTGATCGAACATTTGACCCCTTCTCTGAAACTCCTGTTGATGGTGTTATTGCA
GCCACTTGCTCAGTGCAGGTTATATCAGGTCAATTCTTATCAGATAAGAAAATTGGCACC
TACGTAGAGGTGGATATGTATGGGTTGCCCACTGACACCATACGTAAGGAATTCCGAACT
CGCATGGTTATGAATAATGGACTCAATCCAGTTTACAATGAAGAGTCATTTGTATTTCGG
AAGGTGATCCTGCCGGACCTGGCTGTCTTGAGAATAGCTGTGTATGATGATAACAACAAG
CTGATTGGCCAGAGGATCCTCCCGCTTGATGGCCTCCAAGCCGGATATCGACACATTTCC
CTTCGAAATGAGGGAAATAAACCATTATCACTACCAACAATTTTCTGCAATATTGTTCTT
AAAACATATGTGCCTGATGGATTTGGAGATATCGTGGATGCTTTATCAGATCCAAAGAAA
TTTCTCTCAATTACAGAAAAGAGAGCAGACCAAATGAGAGCTATGGGCATTGAAACTAGT
GACATAGCCGACGTGCCCAGTGACACTTCCAAAAATGACAAGAAAGGAAAGGCCAACACC
GCCAAAGCAAATGTGACCCCTCAGAGTAGCTCTGAGCTCAGACCAACCACCACGGCTGCC
CTGGCCTCTGGTGTGGAAGCCAAGAAAGGTATTGAACTTATCCCTCAAGTAAGGATAGAA
GACTTAAAGCAGATGAAGGCTTACTTGAAGCATTTAAAGAAACAGCAGAAGGAGCTAAAT
TCTTTAAAGAAGAAACATGCAAAGGAACACAGTACCATGCAGAAGTTACACTGCACGCAA
GTTGACAAAATTGTGGCACAGTATGACAAAGAGAAGTCGACTCATGAGAAAATCCTAGAG
AAGGCAATGAAGAAGAAGGGGGGAAGTAATTGTCTCGAAATGAAAAAAGAAACAGAAATC
AAAATTCAGACGCTGACATCAGATCACAAATCTAAGGTCAAAGAGATTGTAGCACAGCAC
ACAAAGGAATGGTCAGAAATGATCAATACCCACAGTGCTGAGGAGCAAGAAATCCGAGAC
CTGCACCTCAGCCAGCAGTGTGAGCTGCTGAAAAAGCTACTCATCAATGCCCACGAGCAG
CAAACCCAGCAGCTGAAACTGTCCCATGACAGGGAAAGCAAGGAAATGCGAGCACACCAG
GCTAAGATTTCTATGGAAAATAGCAAAGCCATCAGCCAAGATAAATCTATCAAGAATAAA
GCAGAACGGGAAAGGCGAGTCAGGGAGTTAAACAGCAGCAACACTAAAAAGTTTCTGGAA
GAAAGAAAGAGACTTGCCATGAAGCAGTCCAAAGAAATGGATCAGTTGAAAAAAGTCCAG
CTTGAACATCTAGAATTCCTAGAGAAACAGAATGAGCAGGCGAAGGAGATGCAGCAGATG
GTGAAATTGGAAGCCGAGATGGACCGCAGACCAGCAACAGTAGTATGA
|
| Enzyme 2 GenBank Gene ID |
AL023805  |
| Enzyme 2 GeneCard ID |
PLCB4  |
| Enzyme 2 GenAtlas ID |
PLCB4  |
| Enzyme 2 HGNC ID |
HGNC:9059  |
| Enzyme 2 Chromosome Location |
2 |
| Enzyme 2 Locus |
20p12 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 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 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5456 |
| Enzyme 3 Name |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2 |
| Enzyme 3 Synonyms |
- Phosphoinositide phospholipase C-beta-2
- Phospholipase C-beta-2
- PLC-beta-2
|
| Enzyme 3 Gene Name |
PLCB2 |
| Enzyme 3 Protein Sequence |
>1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2
MSLLNPVLLPPKVKAYLSQGERFIKWDDETTVASPVILRVDPKGYYLYWTYQSKEMEFLD
ITSIRDTRFGKFAKMPKSQKLRDVFNMDFPDNSFLLKTLTVVSGPDMVDLTFHNFVSYKE
NVGKAWAEDVLALVKHPLTANASRSTFLDKILVKLKMQLNSEGKIPVKNFFQMFPADRKR
VEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSYHAKAKPYMTKEH
LTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPEN
SVLAQDKLLLHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDC
WKGKPPDEEPIITHGFTMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVDSPRQQAKM
AEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKNQFSGPTSSSKDTGGE
AEGSSPPSAPAGEGTVWAGEEGTELEEEEVEEEEEEESGNLDEEEIKKMQSDEGTAGLEV
TAYEEMSSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQM
SRIYPKGTRMDSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEF
MRRPDKQFNPFSVDRIDVVVATTLSITVISGQFLSERSVRTYVEVELFGLPGDPKRRYRT
KLSPSTNSINPVWKEEPFVFEKILMPELASLRVAVMEEGNKFLGHRIIPINALNSGYHHL
CLHSESNMPLTMPALFIFLEMKDYIPGAWADLTVALANPIKFFSAHDTKSVKLKEAMGGL
PEKPFPLASPVASQVNGALAPTSNGSPAARAGAREEAMKEAAEPRTASLEELRELKGVVK
LQRRHEKELRELERRGARRWEELLQRGAAQLAELGPPGVGGVGACKLGPGKGSRKKRSLP
REESAGAAPGEGPEGVDGRVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMEL
AREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNSHI
QEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAEVKE
SVRACLRTCFPSEAKDKPERACECPPELCEQDPLIAKADAQESRL
|
| Enzyme 3 Number of Residues |
1185 |
| Enzyme 3 Molecular Weight |
134023.2 |
| Enzyme 3 Theoretical pI |
6.21 |
| Enzyme 3 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- lipase activity
- metal ion binding
- phosphoinositide phospholipase C activity
- phospholipase C activity
- phospholipase activity
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- biological regulation
- intracellular signaling pathway
- lipid catabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
- regulation of biological process
- regulation of cellular process
- signal transduction
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in calcium ion binding |
| Enzyme 3 Specific Function |
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes |
| Enzyme 3 Pathways |
- 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 |
95147333  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q00722  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
PLCB2_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>3558 bp
ATGTCTCTGCTCAACCCTGTCCTGCTGCCCCCCAAGGTGAAGGCCTATCTGAGCCAAGGG
GAGCGCTTCATCAAATGGGATGATGAAACTACAGTTGCCTCTCCAGTTATCCTCCGTGTG
GATCCTAAGGGCTACTACTTATACTGGACGTATCAAAGTAAGGAGATGGAGTTTCTGGAT
ATCACCAGCATCCGGGATACTCGCTTTGGGAAGTTTGCCAAGATGCCCAAGAGCCAGAAG
CTCCGGGACGTCTTCAACATGGACTTTCCTGATAACAGTTTCCTGCTGAAGACACTCACG
GTGGTGTCCGGCCCGGACATGGTGGACCTCACCTTCCACAACTTCGTCTCCTACAAGGAG
AACGTGGGCAAGGCCTGGGCTGAGGACGTACTGGCCCTAGTCAAACATCCGCTGACGGCC
AACGCCTCCCGCAGCACCTTCCTGGACAAGATCCTTGTGAAGCTCAAGATGCAGCTCAAC
TCTGAAGGGAAGATTCCGGTGAAGAACTTTTTCCAGATGTTTCCTGCTGACCGCAAGCGG
GTGGAAGCTGCTCTCAGTGCCTGCCACCTCCCCAAAGGCAAAAATGACGCCATCAATCCT
GAGGACTTCCCAGAACCTGTCTACAAGAGTTTCCTCATGAGCCTCTGTCCTCGGCCAGAA
ATAGATGAGATCTTCACTTCTTACCATGCTAAGGCCAAACCCTACATGACGAAGGAGCAC
CTGACCAAATTCATCAACCAGAAACAGCGGGACTCCCGGCTTAACTCCCTGCTGTTCCCG
CCAGCACGGCCTGACCAGGTGCAGGGCCTCATCGACAAGTATGAGCCCAGTGGCATCAAT
GCACAGAGGGGCCAGCTGTCACCTGAAGGCATGGTCTGGTTTCTCTGTGGGCCAGAGAAC
AGCGTGCTGGCCCAGGACAAGCTGCTGCTCCACCACGACATGACGCAGCCACTCAATCAT
TACTTCATCAACTCGTCCCACAACACCTACCTGACAGCCGGCCAGTTCTCAGGCCTCTCC
TCGGCTGAGATGTACCGCCAGGTGCTGCTCTCTGGCTGCCGTTGCGTGGAGCTAGACTGC
TGGAAGGGGAAACCCCCTGACGAGGAGCCCATTATCACCCATGGCTTCACCATGACCACA
GACATCTTCTTCAAAGAAGCAATTGAGGCTATTGCAGAAAGCGCCTTTAAGACCTCCCCC
TATCCCATCATCCTGTCGTTTGAGAACCATGTGGACTCACCCCGCCAGCAGGCTAAGATG
GCTGAGTATTGCCGGACGATCTTTGGGGATATGCTGCTCACAGAGCCCCTGGAAAAGTTC
CCACTAAAACCAGGTGTCCCCCTGCCCAGCCCTGAGGATCTCAGGGGCAAGATCCTCATC
AAGAACAAGAAGAACCAGTTTTCTGGCCCCACCTCCTCCAGTAAGGATACTGGTGGGGAG
GCTGAGGGCAGCAGCCCACCCAGTGCCCCTGCAGGTGAGGGCACAGTGTGGGCTGGCGAG
GAAGGGACTGAGCTGGAGGAGGAGGAGGTGGAAGAGGAAGAGGAGGAGGAGTCAGGAAAC
CTGGATGAAGAAGAGATTAAGAAGATGCAGTCGGATGAGGGCACAGCGGGCCTGGAAGTG
ACGGCTTATGAGGAGATGTCCAGCCTAGTCAATTACATCCAGCCCACCAAGTTCGTCTCC
TTTGAGTTCTCTGCCCAAAAGAACCGAAGTTATGTCATCTCGTCCTTCACAGAGCTCAAG
GCATATGACCTGCTCTCCAAGGCCTCGGTGCAGTTTGTGGACTACAACAAGCGCCAGATG
AGCCGCATTTACCCCAAGGGAACCCGCATGGACTCCTCCAACTACATGCCCCAGATGTTC
TGGAATGCTGGATGCCAGATGGTTGCCCTCAACTTCCAGACGATGGACTTGCCCATGCAG
CAGAACATGGCAGTATTTGAGTTCAACGGGCAGAGCGGCTACCTCCTCAAGCATGAGTTC
ATGCGCCGGCCGGACAAGCAGTTCAACCCCTTCTCAGTGGACCGCATCGACGTGGTGGTG
GCCACCACCCTTTCCATTACGGTGATCTCTGGGCAGTTCCTGTCAGAACGCAGCGTGCGC
ACCTATGTAGAAGTGGAGCTGTTTGGCCTTCCTGGGGACCCCAAGAGGCGCTATCGAACT
AAGCTGTCACCCAGTACTAACTCCATCAATCCTGTCTGGAAGGAGGAGCCCTTTGTCTTT
GAGAAGATCTTGATGCCTGAGCTGGCCTCCCTCAGAGTGGCTGTGATGGAGGAAGGCAAC
AAGTTTCTTGGACACCGCATCATCCCCATCAATGCCCTAAATTCTGGGTACCACCACCTG
TGCCTGCACAGTGAGAGCAACATGCCCCTCACCATGCCTGCGCTCTTCATCTTCCTGGAG
ATGAAGGACTACATACCTGGTGCTTGGGCAGATCTCACTGTGGCCCTCGCCAACCCCATT
AAGTTCTTCAGTGCCCATGACACGAAGTCTGTGAAGCTCAAGGAGGCCATGGGAGGTCTG
CCTGAGAAGCCCTTCCCACTGGCGAGTCCAGTTGCCAGCCAGGTCAATGGGGCGTTGGCC
CCAACGAGCAATGGGTCACCAGCAGCCAGGGCCGGGGCCAGGGAAGAGGCTATGAAAGAA
GCTGCGGAGCCGCGGACCGCCAGCCTGGAGGAGCTCCGGGAGCTAAAGGGCGTGGTGAAG
CTGCAGCGGCGGCACGAGAAGGAGCTGCGAGAGTTGGAGCGGCGCGGAGCGCGGCGCTGG
GAGGAGCTGCTGCAGCGGGGCGCGGCGCAGCTGGCGGAGCTCGGGCCACCGGGCGTGGGG
GGCGTCGGGGCCTGCAAGCTCGGTCCCGGCAAGGGCTCTCGCAAGAAGAGGAGCCTGCCC
CGCGAGGAGAGCGCCGGAGCCGCGCCGGGCGAGGGCCCTGAGGGCGTGGACGGGCGCGTG
CGGGAGCTGAAAGACAGGCTGGAGCTGGAGCTGCTGCGGCAGGGCGAGGAGCAGTACGAG
TGCGTTCTGAAGCGCAAGGAGCAGCACGTGGCCGAGCAAATCTCCAAAATGATGGAGCTG
GCCAGAGAGAAACAGGCGGCAGAGCTGAAGGCCCTGAAGGAGACGTCGGAGAACGACACC
AAAGAGATGAAGAAAAAGCTGGAGACAAAGAGACTGGAGCGGATCCAGGGCATGACCAAA
GTCACCACAGACAAGATGGCCCAGGAGAGGTTGAAGAGAGAGATTAACAACTCCCACATC
CAGGAAGTAGTGCAGGTGATCAAGCAGATGACGGAGAACTTGGAGAGGCACCAGGAGAAG
CTGGAGGAGAAGCAGGCGGCTTGCCTGGAACAGATACGGGAGATGGAAAAGCAGTTCCAG
AAGGAGGCGCTGGCAGAGTACGAGGCCAGGATGAAGGGTCTGGAGGCAGAGGTGAAGGAG
TCGGTGAGGGCCTGCCTCAGGACCTGCTTTCCCTCCGAGGCCAAGGACAAGCCTGAGAGG
GCCTGCGAGTGCCCCCCAGAGCTGTGTGAGCAGGACCCACTCATAGCAAAGGCAGATGCC
CAGGAGAGCCGCCTCTGA
|
| Enzyme 3 GenBank Gene ID |
NM_004573.2  |
| Enzyme 3 GeneCard ID |
PLCB2  |
| Enzyme 3 GenAtlas ID |
PLCB2  |
| Enzyme 3 HGNC ID |
HGNC:9055  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
15q15 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 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 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5460 |
| Enzyme 4 Name |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3 |
| Enzyme 4 Synonyms |
- Phosphoinositide phospholipase C-beta-3
- Phospholipase C-beta-3
- PLC-beta-3
|
| Enzyme 4 Gene Name |
PLCB3 |
| Enzyme 4 Protein Sequence |
>1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3
MAGAQPGVHALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNME
VDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNF
MAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFS
ADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPY
LTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYL
GGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRC
VELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAK
QQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPDS
AGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGD
EGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPV
KFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYM
PQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIV
DGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEP
FDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLI
YTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQL
GSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRGH
KALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVED
TKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQF
KRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLE
EAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGLG
DGPLVACASNGHAPGSSGHLSGADSESQEENTQL
|
| Enzyme 4 Number of Residues |
1234 |
| Enzyme 4 Molecular Weight |
138797.7 |
| Enzyme 4 Theoretical pI |
5.66 |
| Enzyme 4 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- lipase activity
- metal ion binding
- phosphoinositide phospholipase C activity
- phospholipase C activity
- phospholipase activity
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- biological regulation
- intracellular signaling pathway
- lipid catabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
- regulation of biological process
- regulation of cellular process
- signal transduction
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in calcium ion binding |
| Enzyme 4 Specific Function |
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes |
| Enzyme 4 Pathways |
- 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 |
148745659  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q01970  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
PLCB3_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>3705 bp
ATGGCGGGCGCCCAGCCCGGCGTCCACGCGCTGCAGTTGGAGCCGCCCACCGTGGTGGAG
ACCCTGCGGCGCGGGAGTAAGTTCATCAAATGGGACGAGGAGACCTCCAGTCGGAACCTG
GTGACCCTGCGTGTGGACCCCAATGGCTTCTTCTTGTACTGGACGGGCCCCAACATGGAG
GTGGACACACTGGACATCAGTTCCATCAGGGACACACGGACAGGCCGGTACGCCCGCCTG
CCCAAGGACCCCAAGATCCGGGAAGTTCTGGGCTTTGGGGGTCCCGATGCCCGGCTGGAG
GAGAAGCTGATGACGGTGGTGTCTGGGCCAGACCCGGTGAACACAGTGTTCTTGAACTTC
ATGGCCGTGCAGGATGACACAGCCAAGGTCTGGTCTGAGGAGCTATTCAAGCTGGCTATG
AACATCCTGGCTCAGAACGCCTCCCGGAACACCTTCCTGCGCAAAGCATACACGAAGCTG
AAGCTGCAGGTGAACCAGGATGGTCGGATCCCCGTCAAGAACATCCTGAAGATGTTCTCA
GCAGACAAGAAGCGGGTGGAGACTGCGCTGGAATCCTGTGGCCTCAAATTCAACCGGAGT
GAGTCCATCCGGCCTGATGAGTTTTCCTTGGAAATCTTTGAGCGGTTCCTGAACAAGCTG
TGTCTGCGGCCGGACATTGACAAGATCCTGCTGGAGATAGGCGCCAAGGGCAAGCCATAC
CTGACGCTGGAGCAGCTCATGGACTTCATCAACCAGAAGCAACGCGACCCGAGACTCAAC
GAAGTGCTGTACCCGCCCCTGCGGCCCTCCCAGGCCCGGCTGCTCATCGAAAAGTATGAG
CCCAACCAGCAGTTTCTGGAGCGAGACCAGATGTCCATGGAGGGCTTTAGCCGCTACCTG
GGAGGCGAGGAGAATGGCATCCTGCCCCTGGAAGCCCTGGATCTGAGCACGGACATGACC
CAGCCACTGAGTGCCTACTTCATCAACTCCTCGCATAACACCTATCTCACTGCGGGGCAG
CTGGCTGGGACCTCGTCGGTGGAGATGTACCGCCAGGCACTACTATGGGGCTGCCGCTGC
GTGGAGCTGGACGTGTGGAAGGGACGGCCGCCTGAGGAGGAACCCTTCATTACCCACGGC
TTCACCATGACCACAGAGGTGCCTCTGCGCGACGTGCTGGAGGCCATTGCCGAGACTGCC
TTCAAGACCTCGCCCTACCCCGTCATCCTCTCCTTCGAGAACCATGTGGACTCGGCAAAG
CAACAGGCAAAGATGGCTGAGTACTGCCGCTCCATCTTTGGAGACGCGCTACTCATCGAG
CCTCTGGACAAGTACCCGCTGGCCCCAGGCGTTCCCCTGCCCAGCCCCCAGGACCTGATG
GGCCGTATCCTGGTGAAGAACAAGAAGCGGCACCGACCCAGCGCAGGTGGCCCAGACAGC
GCCGGGCGCAAGCGGCCCCTGGAGCAGAGCAATTCTGCCCTGAGCGAGAGCTCCGCGGCC
ACCGAGCCCTCCTCCCCGCAGCTGGGGTCTCCCAGCTCTGACAGCTGCCCAGGCCTGAGC
AATGGGGAGGAGGTAGGGCTTGAGAAGCCCAGCCTGGAGCCTCAGAAGTCTCTGGGTGAC
GAGGGCCTGAACCGAGGCCCCTATGTTCTTGGACCTGCTGACCGTGAGGATGAGGAGGAA
GATGAGGAAGAGGAGGAACAGACAGACCCCAAAAAGCCAACTACAGATGAGGGCACAGCC
AGCAGCGAGGTGAATGCCACTGAGGAGATGTCCACGCTTGTCAACTACATCGAACCTGTC
AAGTTCAAGTCCTTTGAGGCTGCTCGAAAGAGGAACAAATGCTTCGAGATGTCGTCCTTT
GTGGAGACCAAGGCCATGGAGCAACTGACCAAGAGCCCCATGGAGTTTGTGGAATACAAC
AAGCAGCAGCTCAGCCGCATCTACCCCAAGGGCACCCGCGTGGACTCCTCCAACTACATG
CCCCAGCTCTTCTGGAACGTAGGGTGCCAGCTTGTTGCGCTCAACTTCCAGACCCTCGAT
GTGGCGATGCAGCTCAACGCGGGCGTTTTTGAGTACAACGGGCGCAGCGGGTACCTGCTC
AAGCCGGAGTTCATGCGGCGGCCGGACAAGTCCTTCGACCCCTTCACTGAGGTCATCGTG
GATGGCATCGTGGCCAATGCCTTGCGGGTCAAGGTGATCTCAGGGCAGTTCCTGTCCGAC
AGGAAGGTGGGCATCTACGTGGAGGTGGACATGTTTGGCCTCCCTGTTGATACGCGGCGC
AAGTACCGCACCCGGACCTCTCAGGGGAACTCGTTCAACCCCGTGTGGGACGAAGAGCCC
TTCGACTTCCCCAAGGTGGTGCTGCCCACGCTGGCTTCACTTCGCATTGCAGCCTTTGAG
GAGGGGGGTAAATTCGTAGGGCACCGGATCCTGCCTGTCTCTGCCATCCGCTCCGGATAC
CACTACGTCTGCCTGCGGAACGAGGCCAACCAACCGCTGTGCCTGCCGGCCCTGCTCATC
TACACCGAAGCCTCGGACTACATTCCTGACGACCACCAGGACTATGCGGAGGCCCTGATC
AACCCCATTAAGCACGTCAGCCTGATGGACCAGAGGGCCCGGCAGCTGGCCGCCCTCATT
GGGGAGAGTGAGGCTCAGGCTGGCCAAGAGACGTGCCAGGACACCCAGTCTCAGCAGCTG
GGGTCTCAGCCGTCCTCAAACCCCACCCCCAGCCCACTGGATGCCTCCCCCCGCCGGCCC
CCTGGCCCCACCACCTCCCCTGCCAGCACCTCCCTCAGCAGCCCAGGGCAGCGTGATGAT
CTCATCGCCAGCATCCTCTCAGAGGTGGCCCCCACCCCGCTGGATGAGCTCCGAGGTCAC
AAGGCTCTGGTCAAGCTCCGGAGCCGGCAAGAGCGAGACCTGCGGGAGCTGCGCAAGAAG
CATCAGCGGAAGGCAGTCACCCTCACCCGCCGCCTGCTGGATGGCCTGGCTCAGGCACAG
GCTGAGGGCAGGTGCCGGCTGCGGCCAGGTGCCCTAGGTGGGGCCGCTGATGTGGAGGAC
ACGAAGGAGGGGGAGGACGAGGCAAAGCGGTATCAGGAGTTCCAGAACAGACAGGTGCAG
AGCCTGCTGGAGCTGCGGGAGGCCCAGGTGGACGCAGAGGCCCAGCGGAGGCTGGAACAC
CTGAGACAGGCTCTGCAGCGGCTCAGGGAGGTCGTCCTTGATGCAAACACAACTCAGTTC
AAGAGGCTGAAAGAGATGAACGAGAGGGAGAAGAAGGAGCTGCAGAAGATCCTGGACAGA
AAGCGCCATAACAGCATCTCGGAGGCCAAGATGAGGGACAAGCATAAGAAGGAGGCGGAA
CTGACGGAGATTAACCGTCGGCACATCACTGAGTCAGTCAACTCCATCCGTCGGCTGGAG
GAGGCCCAGAAGCAGCGGCATGACCGTCTTGTGGCTGGGCAGCAGCAGGTCCTGCAACAG
CTGGCAGAAGAGGAGCCCAAGCTGCTGGCCCAGCTGGCCCAGGAGTGTCAGGAGCAGCGG
GCGAGGCTCCCCCAGGAGATCCGCCGGAGCCTGCTGGGCGAGATGCCAGAGGGGCTGGGG
GACGGGCCTCTGGTGGCCTGTGCCAGCAACGGTCACGCACCCGGGAGCAGCGGGCACCTG
TCGGGCGCTGACTCGGAGAGCCAGGAGGAGAACACGCAGCTCTGA
|
| Enzyme 4 GenBank Gene ID |
BC142681  |
| Enzyme 4 GeneCard ID |
PLCB3  |
| Enzyme 4 GenAtlas ID |
PLCB3  |
| Enzyme 4 HGNC ID |
HGNC:9056  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
11q13 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 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 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5462 |
| Enzyme 5 Name |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2 |
| Enzyme 5 Synonyms |
- Phosphoinositide phospholipase C-gamma-2
- Phospholipase C-IV
- PLC-IV
- Phospholipase C-gamma-2
- PLC-gamma-2
|
| Enzyme 5 Gene Name |
PLCG2 |
| Enzyme 5 Protein Sequence |
>1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2
MSTTVNVDSLAEYEKSQIKRALELGTVMTVFSFRKSTPERRTVQVIMETRQVAWSKTADK
IEGFLDIMEIKEIRPGKNSKDFERAKAVRQKEDCCFTILYGTQFVLSTLSLAADSKEDAV
NWLSGLKILHQEAMNASTPTIIESWLRKQIYSVDQTRRNSISLRELKTILPLINFKVSSA
KFLKDKFVEIGAHKDELSFEQFHLFYKKLMFEQQKSILDEFKKDSSVFILGNTDRPDASA
VYLHDFQRFLIHEQQEHWAQDLNKVRERMTKFIDDTMRETAEPFLFVDEFLTYLFSRENS
IWDEKYDAVDMQDMNNPLSHYWISSSHNTYLTGDQLRSESSPEAYIRCLRMGCRCIELDC
WDGPDGKPVIYHGWTRTTKIKFDDVVQAIKDHAFVTSSFPVILSIEEHCSVEQQRHMAKA
FKEVFGDLLLTKPTEASADQLPSPSQLREKIIIKHKKLGPRGDVDVNMEDKKDEHKQQGE
LYMWDSIDQKWTRHYCAIADAKLSFSDDIEQTMEEEVPQDIPPTELHFGEKWFHKKVEKR
TSAEKLLQEYCMETGGKDGTFLVRESETFPNDYTLSFWRSGRVQHCRIRSTMEGGTLKYY
LTDNLTFSSIYALIQHYRETHLRCAEFELRLTDPVPNPNPHESKPWYYDSLSRGEAEDML
MRIPRDGAFLIRKREGSDSYAITFRARGKVKHCRINRDGRHFVLGTSAYFESLVELVSYY
EKHSLYRKMRLRYPVTPELLERYNMERDINSLYDVSRMYVDPSEINPSMPQRTVKALYDY
KAKRSDELSFCRGALIHNVSKEPGGWWKGDYGTRIQQYFPSNYVEDISTADFEELEKQII
EDNPLGSLCRGILDLNTYNVVKAPQGKNQKSFVFILEPKQQGDPPVEFATDRVEELFEWF
QSIREITWKIDTKENNMKYWEKNQSIAIELSDLVVYCKPTSKTKDNLENPDFREIRSFVE
TKADSIIRQKPVDLLKYNQKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTADKY
MQMNHALFSLNGRTGYVLQPESMRTEKYDPMPPESQRKILMTLTVKVLGARHLPKLGRSI
ACPFVEVEICGAEYDNNKFKTTVVNDNGLSPIWAPTQEKVTFEIYDPNLAFLRFVVYEED
MFSDPNFLAHATYPIKAVKSGFRSVPLKNGYSEDIELASLLVFCEMRPVLESEEELYSSC
RQLRRRQEELNNQLFLYDTHQNLRNANRDALVKEFSVNENQLQLYQEKCNKRLREKRVSN
SKFYS
|
| Enzyme 5 Number of Residues |
1265 |
| Enzyme 5 Molecular Weight |
147868.7 |
| Enzyme 5 Theoretical pI |
6.60 |
| Enzyme 5 GO Classification |
| Function |
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipase activity
- molecular transducer activity
- phosphoinositide phospholipase C activity
- phospholipase C activity
- phospholipase activity
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
- protein binding
- signal transducer activity
|
| Process |
- biological regulation
- intracellular signaling pathway
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid catabolic process
- phospholipid metabolic process
- primary metabolic process
- regulation of biological process
- regulation of cellular process
- signal transduction
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in phosphoinositide phospholipase C activity |
| Enzyme 5 Specific Function |
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling |
| Enzyme 5 Pathways |
- 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 |
117320537  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P16885  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
PLCG2_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>3798 bp
ATGTCCACCACGGTCAATGTAGATTCCCTTGCGGAATATGAGAAGAGCCAGATCAAGAGA
GCCCTGGAGCTGGGGACGGTGATGACTGTGTTCAGCTTCCGCAAGTCCACCCCCGAGCGG
AGAACCGTCCAGGTGATCATGGAGACGCGGCAGGTGGCCTGGAGCAAGACCGCCGACAAG
ATCGAGGGCTTCTTGGATATCATGGAAATAAAAGAAATCCGCCCAGGGAAGAACTCCAAA
GATTTCGAGCGAGCAAAAGCAGTTCGCCAGAAAGAAGACTGCTGCTTCACCATCCTATAT
GGCACTCAGTTCGTCCTCAGCACGCTCAGCTTGGCAGCTGACTCTAAAGAGGATGCAGTT
AACTGGCTCTCTGGCTTGAAAATCTTACACCAGGAAGCGATGAATGCGTCCACGCCCACC
ATTATCGAGAGTTGGCTGAGAAAGCAGATATATTCTGTGGATCAAACCAGAAGAAACAGC
ATCAGTCTCCGAGAGTTGAAGACCATCTTGCCCCTGATCAACTTTAAAGTGAGCAGTGCC
AAGTTCCTTAAAGATAAGTTTGTGGAAATAGGAGCACACAAAGATGAGCTCAGCTTTGAA
CAGTTCCATCTCTTCTATAAAAAACTTATGTTTGAACAGCAAAAATCGATTCTCGATGAA
TTCAAAAAGGATTCGTCCGTGTTCATCCTGGGGAACACTGACAGGCCGGATGCCTCTGCT
GTTTACCTGCATGACTTCCAGAGGTTTCTCATACATGAACAGCAGGAGCATTGGGCTCAG
GATCTGAACAAAGTCCGTGAGCGGATGACAAAGTTCATTGATGACACCATGCGTGAAACT
GCTGAGCCTTTCTTGTTTGTGGATGAGTTCCTCACGTACCTGTTTTCACGAGAAAACAGC
ATCTGGGATGAGAAGTATGACGCGGTGGACATGCAGGACATGAACAACCCCCTGTCTCAT
TACTGGATCTCCTCGTCACATAACACGTACCTTACAGGTGACCAGCTGCGGAGCGAGTCG
TCCCCAGAAGCTTACATCCGCTGCCTGCGCATGGGCTGTCGCTGCATTGAACTGGACTGC
TGGGACGGGCCCGATGGGAAGCCGGTCATCTACCATGGCTGGACGCGGACTACCAAGATC
AAGTTTGACGACGTCGTGCAGGCCATCAAAGACCACGCCTTTGTTACCTCGAGCTTCCCA
GTGATCCTGTCCATCGAGGAGCACTGCAGCGTGGAGCAACAGCGTCACATGGCCAAGGCC
TTCAAGGAAGTATTTGGCGACCTGCTGTTGACGAAGCCCACGGAGGCCAGTGCTGACCAG
CTGCCCTCGCCCAGCCAGCTGCGGGAGAAGATCATCATCAAGCATAAGAAGCTGGGCCCC
CGAGGCGATGTGGATGTCAACATGGAGGACAAGAAGGACGAACACAAGCAACAGGGGGAG
CTGTACATGTGGGATTCCATTGACCAGAAATGGACTCGGCACTACTGCGCCATTGCCGAT
GCCAAGCTGTCCTTCAGTGATGACATTGAACAGACTATGGAGGAGGAAGTGCCCCAGGAT
ATACCCCCTACAGAACTACATTTTGGGGAGAAATGGTTCCACAAGAAGGTGGAGAAGAGG
ACGAGTGCCGAGAAGTTGCTGCAGGAATACTGCATGGAGACGGGGGGCAAGGATGGCACC
TTCCTGGTTCGGGAGAGCGAGACCTTCCCCAATGACTACACCCTGTCCTTCTGGCGGTCA
GGCCGGGTCCAGCACTGCCGGATCCGCTCCACCATGGAGGGCGGGACCCTGAAATACTAC
TTGACTGACAACCTCACCTTCAGCAGCATCTATGCCCTCATCCAGCACTACCGCGAGACG
CACCTGCGCTGCGCCGAGTTCGAGCTGCGGCTCACGGACCCTGTGCCCAACCCCAACCCC
CACGAGTCCAAGCCGTGGTACTATGACAGCCTGAGCCGCGGAGAGGCAGAGGACATGCTG
ATGAGGATTCCCCGGGACGGGGCCTTCCTGATCCGGAAGCGAGAGGGGAGCGACTCCTAT
GCCATCACCTTCAGGGCTAGGGGCAAGGTAAAGCATTGTCGCATCAACCGGGACGGCCGG
CACTTTGTGCTGGGGACCTCCGCCTATTTTGAGAGTCTGGTGGAGCTCGTCAGTTACTAC
GAGAAGCATTCACTCTACCGAAAGATGAGACTGCGCTACCCCGTGACCCCCGAGCTCCTG
GAGCGCTACAATATGGAAAGAGATATAAACTCCCTCTACGACGTCAGCAGAATGTATGTG
GATCCCAGTGAAATCAATCCGTCCATGCCTCAGAGAACCGTGAAAGCTCTGTATGACTAC
AAAGCCAAGCGAAGCGATGAGCTGAGCTTCTGCCGTGGTGCCCTCATCCACAATGTCTCC
AAGGAGCCCGGGGGCTGGTGGAAAGGAGACTATGGAACCAGGATCCAGCAGTACTTCCCA
TCCAACTACGTCGAGGACATCTCAACTGCAGACTTCGAGGAGCTAGAAAAGCAGATTATT
GAAGACAATCCCTTAGGGTCTCTTTGCAGAGGAATATTGGACCTCAATACCTATAACGTC
GTGAAAGCCCCTCAGGGAAAAAACCAGAAGTCCTTTGTCTTCATCCTGGAGCCCAAGCAG
CAGGGCGATCCTCCGGTGGAGTTTGCCACAGACAGGGTGGAGGAGCTCTTTGAGTGGTTT
CAGAGCATCCGAGAGATCACCTGGAAGATTGACACCAAGGAGAACAACATGAAGTACTGG
GAGAAGAACCAGTCCATCGCCATCGAGCTCTCTGACCTGGTTGTCTACTGCAAACCAACC
AGCAAAACCAAGGACAACTTAGAAAATCCTGACTTCCGAGAAATCCGCTCCTTTGTGGAG
ACGAAGGCTGACAGCATCATCAGACAGAAGCCCGTCGACCTCCTGAAGTACAATCAAAAG
GGCCTGACCCGCGTCTACCCAAAGGGACAAAGAGTTGACTCTTCAAACTACGACCCCTTC
CGCCTCTGGCTGTGCGGTTCTCAGATGGTGGCACTCAATTTCCAGACGGCAGATAAGTAC
ATGCAGATGAATCACGCATTGTTTTCTCTCAATGGGCGCACGGGCTACGTTCTGCAGCCT
GAGAGCATGAGGACAGAGAAATATGACCCGATGCCACCCGAGTCCCAGAGGAAGATCCTG
ATGACGCTGACAGTCAAGGTTCTCGGTGCTCGCCATCTCCCCAAACTTGGACGAAGTATT
GCCTGTCCCTTTGTAGAAGTGGAGATCTGTGGAGCCGAGTATGACAACAACAAGTTCAAG
ACGACGGTTGTGAATGATAATGGCCTCAGCCCTATCTGGGCTCCAACACAGGAGAAGGTG
ACATTTGAAATTTATGACCCAAACCTGGCATTTCTGCGCTTTGTGGTTTATGAAGAAGAT
ATGTTCAGCGATCCCAACTTTCTTGCTCATGCCACTTACCCCATTAAAGCAGTCAAATCA
GGATTCAGGTCCGTTCCTCTGAAGAATGGGTACAGCGAGGACATAGAGCTGGCTTCCCTC
CTGGTTTTCTGTGAGATGCGGCCAGTCCTGGAGAGCGAAGAGGAACTTTACTCCTCCTGT
CGCCAGCTGAGGAGGCGGCAAGAAGAACTGAACAACCAGCTCTTTCTGTATGACACACAC
CAGAACTTGCGCAATGCCAACCGGGATGCCCTGGTTAAAGAGTTCAGTGTTAATGAGAAC
CAGCTCCAGCTGTACCAGGAGAAATGCAACAAGAGGTTAAGAGAGAAGAGAGTCAGCAAC
AGCAAGTTTTACTCATAG
|
| Enzyme 5 GenBank Gene ID |
NM_002661.2  |
| Enzyme 5 GeneCard ID |
PLCG2  |
| Enzyme 5 GenAtlas ID |
PLCG2  |
| Enzyme 5 HGNC ID |
HGNC:9066  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
16q24.1 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 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 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6439 |
| Enzyme 6 Name |
Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta isoform |
| Enzyme 6 Synonyms |
- PI3-kinase subunit delta
- PI3K-delta
- PtdIns-3-kinase subunit delta
- Phosphatidylinositol-4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta
- PtdIns-3-kinase subunit p110-delta
|
| Enzyme 6 Gene Name |
PIK3CD |
| Enzyme 6 Protein Sequence |
>Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta isoform
MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFH
MLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLL
IGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGP
GTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYT
LQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPR
AKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSS
SEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAW
ANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAP
HPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQE
HFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSL
RKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSV
ALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMR
QEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKN
GDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLN
KSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIM
IRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYC
ERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFN
EALRESWKTKVNWLAHNVSKDNRQ
|
| Enzyme 6 Number of Residues |
1044 |
| Enzyme 6 Molecular Weight |
119478.1 |
| Enzyme 6 Theoretical pI |
7.18 |
| Enzyme 6 GO Classification |
| Function |
- 1-phosphatidylinositol-3-kinase activity
- binding
- catalytic activity
- inositol or phosphatidylinositol kinase activity
- kinase activity
- lipid kinase activity
- phosphatidylinositol-4,5-bisphosphate 3-kinase activity
- phosphoinositide 3-kinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biological regulation
- glycerophospholipid metabolic process
- intracellular signal transduction
- metabolic process
- organophosphate metabolic process
- phosphoinositide metabolic process
- phosphoinositide phosphorylation
- phosphoinositide-mediated signaling
- phospholipid metabolic process
- regulation of biological process
- regulation of cellular process
- second-messenger-mediated signaling
- signal transduction
|
| Component |
- macromolecular complex
- phosphoinositide 3-kinase complex
- protein complex
|
|
| Enzyme 6 General Function |
Involved in binding |
| Enzyme 6 Specific Function |
ATP + 1-phosphatidyl-1D-myo-inositol 4,5- bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5- trisphosphate |
| Enzyme 6 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 6 Reactions |
- ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate [RN:R04545]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
37496959  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
O00329  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
PK3CD_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>3135 bp
ATGCCCCCTGGGGTGGACTGCCCCATGGAATTCTGGACCAAGGAGGAGAATCAGAGCGTT
GTGGTTGACTTCCTGCTGCCCACAGGGGTCTACCTGAACTTCCCTGTGTCCCGCAATGCC
AACCTCAGCACCATCAAGCAGCTGCTGTGGCACCGCGCCCAGTATGAGCCGCTCTTCCAC
ATGCTCAGTGGCCCCGAGGCCTATGTGTTCACCTGCATCAACCAGACAGCGGAGCAGCAA
GAGCTGGAGGACGAGCAACGGCGTCTGTGTGACGTGCAGCCCTTCCTGCCCGTCCTGCGC
CTGGTGGCCCGTGAGGGCGACCGCGTGAAGAAGCTCATCAACTCACAGATCAGCCTCCTC
ATCGGCAAAGGCCTCCACGAGTTTGACTCCTTGTGCGACCCAGAAGTGAACGACTTTCGC
GCCAAGATGTGCCAATTCTGCGAGGAGGCGGCCGCCCGCCGGCAGCAGCTGGGCTGGGAG
GCCTGGCTGCAGTACAGTTTCCCCCTGCAGCTGGAGCCCTCGGCTCAAACCTGGGGGCCT
GGTACCCTGCGGCTCCCGAACCGGGCCCTTCTGGTCAACGTTAAGTTTGAGGGCAGCGAG
GAGAGCTTCACCTTCCAGGTGTCCACCAAGGACGTGCCGCTGGCGCTGATGGCCTGTGCC
CTGCGGAAGAAGGCCACAGTGTTCCGGCAGCCGCTGGTGGAGCAGCCGGAAGACTACACG
CTGCAGGTGAACGGCAGGCATGAGTACCTGTATGGCAGCTACCCGCTCTGCCAGTTCCAG
TACATCTGCAGCTGCCTGCACAGTGGGTTGACCCCTCACCTGACCATGGTCCATTCCTCC
TCCATCCTCGCCATGCGGGATGAGCAGAGCAACCCTGCCCCCCAGGTCCAGAAACCGCGT
GCCAAACCACCTCCCATTCCTGCGAAGAAGCCTTCCTCTGTGTCCCTGTGGTCCCTGGAG
CAGCCGTTCCGCATCGAGCTCATCCAGGGCAGCAAAGTGAACGCCGACGAGCGGATGAAG
CTGGTGGTGCAGGCCGGGCTTTTCCACGGCAACGAGATGCTGTGCAAGACGGTGTCCAGC
TCGGAGGTGAGCGTGTGCTCGGAGCCCGTGTGGAAGCAGCGGCTGGAGTTCGACATCAAC
ATCTGCGACCTGCCCCGCATGGCCCGTCTCTGCTTTGCGCTGTACGCCGTGATCGAGAAA
GCCAAGAAGGCTCGCTCCACCAAGAAGAAGTCCAAGAAGGCGGACTGCCCCATTGCCTGG
GCCAACCTCATGCTGTTTGACTACAAGGACCAGCTTAAGACCGGGGAACGCTGCCTCTAC
ATGTGGCCCTCCGTCCCAGATGAGAAGGGCGAGCTGCTGAACCCCACGGGCACTGTGCGC
AGTAACCCCAACACGGATAGCGCCGCTGCCCTGCTCATCTGCCTGCCCGAGGTGGCCCCG
CACCCCGTGTACTACCCCGCCCTGGAGAAGATCTTGGAGCTGGGGCGACACAGCGAGTGT
GTGCATGTCACCGAGGAGGAGCAGCTGCAGCTGCGGGAAATCCTGGAGCGGCGGGGGTCT
GGGGAGCTGTATGAGCACGAGAAGGACCTGGTGTGGAAGCTGCGGCATGAAGTCCAGGAG
CACTTCCCGGAGGCGCTAGCCCGGCTGCTGCTGGTCACCAAGTGGAACAAGCATGAGGAT
GTGGCCCAGATGCTCTACCTGCTGTGCTCCTGGCCGGAGCTGCCCGTCCTGAGCGCCCTG
GAGCTGCTAGACTTCAGCTTCCCCGATTGCCACGTAGGCTCCTTCGCCATCAAGTCGCTG
CGGAAACTGACGGACGATGAGCTGTTCCAGTACCTGCTGCAGCTGGTGCAGGTGCTCAAG
TACGAGTCCTACCTGGACTGCGAGCTGACCAAATTCCTGCTGGACCGGGCCCTGGCCAAC
CGCAAGATCGGCCACTTCCTTTTCTGGCACCTCCGCTCCGAGATGCACGTGCCGTCGGTG
GCCCTGCGCTTCGGCCTCATCCTGGAGGCCTACTGCAGGGGCAGCACCCACCACATGAAG
GTGCTGATGAAGCAGGGGGAAGCACTGAGCAAACTGAAGGCCCTGAATGACTTCGTCAAG
CTGAGCTCTCAGAAGACCCCCAAGCCCCAGACCAAGGAGCTGATGCACTTGTGCATGCGG
CAGGAGGCCTACCTAGAGGCCCTCTCCCACCTGCAGTCCCCACTCGACCCCAGCACCCTG
CTGGCTGAAGTCTGCGTGGAGCAGTGCACCTTCATGGACTCCAAGATGAAGCCCCTGTGG
ATCATGTACAGCAACGAGGAGGCAGGCAGCGGCGGCAGCGTGGGCATCATCTTTAAGAAC
GGGGATGACCTCCGGCAGGACATGCTGACCCTGCAGATGATCCAGCTCATGGACGTCCTG
TGGAAGCAGGAGGGGCTGGACCTGAGGATGACCCCCTATGGCTGCCTCCCCACCGGGGAC
CGCACAGGCCTCATTGAGGTGGTACTCCGTTCAGACACCATCGCCAACATCCAACTCAAC
AAGAGCAACATGGCAGCCACAGCCGCCTTCAACAAGGATGCCCTGCTCAACTGGCTGAAG
TCCAAGAACCCGGGGGAGGCCCTGGATCGAGCCATTGAGGAGTTCACCCTCTCCTGTGCT
GGCTATTGTGTGGCCACATATGTGCTGGGCATTGGCGATCGGCACAGCGACAACATCATG
ATCCGAGAGAGTGGGCAGCTGTTCCACATTGATTTTGGCCACTTTCTGGGGAATTTCAAG
ACCAAGTTTGGAATCAACCGCGAGCGTGTCCCATTCATCCTCACCTACGACTTTGTCCAT
GTGATTCAGCAGGGGAAGACTAATAATAGTGAGAAATTTGAACGGTTCCGGGGCTACTGT
GAAAGGGCCTACACCATCCTGCGGCGCCACGGGCTTCTCTTCCTCCACCTCTTTGCCCTG
ATGCGGGCGGCAGGCCTGCCTGAGCTCAGCTGCTCCAAAGACATCCAGTATCTCAAGGAC
TCCCTGGCACTGGGGAAAACAGAGGAGGAGGCACTGAAGCACTTCCGAGTGAAGTTTAAC
GAAGCCCTCCGTGAGAGCTGGAAAACCAAAGTGAACTGGCTGGCCCACAACGTGTCCAAA
GACAACAGGCAGTAG
|
| Enzyme 6 GenBank Gene ID |
Y10055  |
| Enzyme 6 GeneCard ID |
PIK3CD  |
| Enzyme 6 GenAtlas ID |
PIK3CD  |
| Enzyme 6 HGNC ID |
HGNC:8977  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
1p36.2 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Vanhaesebroeck B, Welham MJ, Kotani K, Stein R, Warne PH, Zvelebil MJ, Higashi K, Volinia S, Downward J, Waterfield MD: P110delta, a novel phosphoinositide 3-kinase in leukocytes. Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4330-5. [PubMed
]
- Chantry D, Vojtek A, Kashishian A, Holtzman DA, Wood C, Gray PW, Cooper JA, Hoekstra MF: p110delta, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes. J Biol Chem. 1997 Aug 1;272(31):19236-41. [PubMed
]
- 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
]
- Vanhaesebroeck B, Higashi K, Raven C, Welham M, Anderson S, Brennan P, Ward SG, Waterfield MD: Autophosphorylation of p110delta phosphoinositide 3-kinase: a new paradigm for the regulation of lipid kinases in vitro and in vivo. EMBO J. 1999 Mar 1;18(5):1292-302. [PubMed
]
- 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
]
- 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 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6498 |
| Enzyme 7 Name |
Phosphatidylinositol-5-phosphate 4-kinase type-2 alpha |
| Enzyme 7 Synonyms |
- 1-phosphatidylinositol-5-phosphate 4-kinase 2-alpha
- Diphosphoinositide kinase 2-alpha
- PIP5KIII
- Phosphatidylinositol-5-phosphate 4-kinase type II alpha
- PI(5)P 4-kinase type II alpha
- PIP4KII-alpha
- PtdIns(4)P-5-kinase B isoform
- PtdIns(4)P-5-kinase C isoform
- PtdIns(5)P-4-kinase isoform 2-alpha
|
| Enzyme 7 Gene Name |
PIP4K2A |
| Enzyme 7 Protein Sequence |
>Phosphatidylinositol-5-phosphate 4-kinase type-2 alpha
MATPGNLGSSVLASKTKTKKKHFVAQKVKLFRASDPLLSVLMWGVNHSINELSHVQIPVM
LMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSA
PLPNDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVECHGITLLPQFLG
MYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFIN
EGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVECEENDGEE
EGESDGTHPVGTPPDSPGNTLNSSPPLAPGEFDPNIDVYGIKCHENSPRKEVYFMAIIDI
LTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGHILT
|
| Enzyme 7 Number of Residues |
406 |
| Enzyme 7 Molecular Weight |
46224.3 |
| Enzyme 7 Theoretical pI |
7.00 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- kinase activity
- lipid kinase activity
- phosphatidylinositol phosphate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- glycerophospholipid metabolic process
- metabolic process
- organophosphate metabolic process
- phosphatidylinositol metabolic process
- phosphoinositide metabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in phosphatidylinositol phosphate kinase activity |
| Enzyme 7 Specific Function |
Catalyzes the phosphorylation of phosphatidylinositol-5- phosphate on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol-4,5-biphosphate |
| Enzyme 7 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 7 Reactions |
- ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [RN:R05803]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
57160667  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P48426  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
PI42A_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1221 bp
ATGGCGACCCCCGGCAACCTAGGGTCCTCTGTCCTGGCGAGCAAGACCAAGACCAAGAAG
AAGCACTTCGTAGCGCAGAAAGTGAAGCTGTTTCGGGCCAGCGACCCGCTGCTCAGCGTC
CTCATGTGGGGGGTAAACCACTCGATCAATGAACTGAGCCATGTTCAAATCCCTGTTATG
TTGATGCCAGATGACTTCAAAGCCTATTCAAAAATAAAGGTGGACAATCACCTTTTTAAC
AAAGAAAACATGCCGAGCCATTTCAAGTTTAAGGAATACTGCCCGATGGTCTTCCGTAAC
CTGCGGGAGAGGTTTGGAATTGATGATCAAGATTTCCAGAATTCCCTGACCAGGAGCGCA
CCCCTCCCCAACGACTCCCAGGCCCGCAGTGGAGCTCGTTTTCACACTTCCTACGACAAA
AGATACATCATCAAGACTATTACCAGTGAAGACGTGGCCGAAATGCACAACATCCTGAAG
AAATACCACCAGTACATAGTGGAATGTCATGGGATCACCCTTCTTCCCCAGTTCTTGGGC
ATGTACCGGCTTAATGTTGATGGAGTTGAAATATATGTGATAGTTACAAGAAATGTATTC
AGCCACCGTTTGTCTGTGTATAGGAAATACGACTTAAAGGGCTCTACAGTGGCTAGAGAA
GCTAGTGACAAAGAAAAGGCCAAAGAACTGCCAACTCTGAAAGATAATGATTTCATTAAT
GAGGGCCAAAAGATTTATATTGATGACAACAACAAGAAGGTCTTCCTGGAAAAACTAAAA
AAGGATGTTGAGTTTCTGGCCCAGCTGAAGCTCATGGACTACAGTCTGCTGGTGGGAATT
CATGATGTGGAGAGAGCCGAACAGGAGGAAGTGGAGTGTGAGGAGAACGATGGGGAGGAG
GAGGGCGAGAGCGATGGCACCCACCCGGTGGGAACCCCCCCAGATAGCCCCGGGAATACA
CTGAACAGCTCACCACCCCTGGCTCCCGGGGAGTTCGATCCGAACATCGACGTCTATGGA
ATTAAGTGCCATGAAAACTCGCCTAGGAAGGAGGTGTACTTCATGGCAATTATTGACATC
CTTACTCATTATGATGCAAAAAAGAAAGCTGCCCATGCTGCAAAAACTGTTAAACATGGC
GCTGGCGCGGAGATCTCCACCGTGAACCCAGAACAGTATTCAAAGCGCTTTTTGGACTTT
ATTGGCCACATCTTGACGTAA
|
| Enzyme 7 GenBank Gene ID |
AL157707  |
| Enzyme 7 GeneCard ID |
PIP4K2A  |
| Enzyme 7 GenAtlas ID |
PIP4K2A  |
| Enzyme 7 HGNC ID |
HGNC:8997  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
10p12.2 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Boronenkov IV, Anderson RA: The sequence of phosphatidylinositol-4-phosphate 5-kinase defines a novel family of lipid kinases. J Biol Chem. 1995 Feb 17;270(7):2881-4. [PubMed
]
- Divecha N, Truong O, Hsuan JJ, Hinchliffe KA, Irvine RF: The cloning and sequence of the C isoform of PtdIns4P 5-kinase. Biochem J. 1995 Aug 1;309 ( Pt 3):715-9. [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
]
- Rameh LE, Tolias KF, Duckworth BC, Cantley LC: A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate. Nature. 1997 Nov 13;390(6656):192-6. [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
]
- 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
]
- 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 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6504 |
| Enzyme 8 Name |
Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform |
| Enzyme 8 Synonyms |
- PI3-kinase subunit beta
- PI3K-beta
- PtdIns-3-kinase subunit beta
- Phosphatidylinositol-4,5-bisphosphate 3-kinase 110 kDa catalytic subunit beta
- PtdIns-3-kinase subunit p110-beta
|
| Enzyme 8 Gene Name |
PIK3CB |
| Enzyme 8 Protein Sequence |
>Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform
MCFSFIMPPAMADILDIWAVDSQIASDGSIPVDFLLPTGIYIQLEVPREATISYIKQMLW
KQVHNYPMFNLLMDIDSYMFACVNQTAVYEELEDETRRLCDVRPFLPVLKLVTRSCDPGE
KLDSKIGVLIGKGLHEFDSLKDPEVNEFRRKMRKFSEEKILSLVGLSWMDWLKQTYPPEH
EPSIPENLEDKLYGGKLIVAVHFENCQDVFSFQVSPNMNPIKVNELAIQKRLTIHGKEDE
VSPYDYVLQVSGRVEYVFGDHPLIQFQYIRNCVMNRALPHFILVECCKIKKMYEQEMIAI
EAAINRNSSNLPLPLPPKKTRIISHVWENNNPFQIVLVKGNKLNTEETVKVHVRAGLFHG
TELLCKTIVSSEVSGKNDHIWNEPLEFDINICDLPRMARLCFAVYAVLDKVKTKKSTKTI
NPSKYQTIRKAGKVHYPVAWVNTMVFDFKGQLRTGDIILHSWSSFPDELEEMLNPMGTVQ
TNPYTENATALHVKFPENKKQPYYYPPFDKIIEKAAEIASSDSANVSSRGGKKFLPVLKE
ILDRDPLSQLCENEMDLIWTLRQDCREIFPQSLPKLLLSIKWNKLEDVAQLQALLQIWPK
LPPREALELLDFNYPDQYVREYAVGCLRQMSDEELSQYLLQLVQVLKYEPFLDCALSRFL
LERALGNRRIGQFLFWHLRSEVHIPAVSVQFGVILEAYCRGSVGHMKVLSKQVEALNKLK
TLNSLIKLNAVKLNRAKGKEAMHTCLKQSAYREALSDLQSPLNPCVILSELYVEKCKYMD
SKMKPLWLVYNNKVFGEDSVGVIFKNGDDLRQDMLTLQMLRLMDLLWKEAGLDLRMLPYG
CLATGDRSGLIEVVSTSETIADIQLNSSNVAAAAAFNKDALLNWLKEYNSGDDLDRAIEE
FTLSCAGYCVASYVLGIGDRHSDNIMVKKTGQLFHIDFGHILGNFKSKFGIKRERVPFIL
TYDFIHVIQQGKTGNTEKFGRFRQCCEDAYLILRRHGNLFITLFALMLTAGLPELTSVKD
IQYLKDSLALGKSEEEALKQFKQKFDEALRESWTTKVNWMAHTVRKDYRS
|
| Enzyme 8 Number of Residues |
1070 |
| Enzyme 8 Molecular Weight |
122761.2 |
| Enzyme 8 Theoretical pI |
7.09 |
| Enzyme 8 GO Classification |
| Function |
- 1-phosphatidylinositol-3-kinase activity
- binding
- catalytic activity
- inositol or phosphatidylinositol kinase activity
- kinase activity
- lipid kinase activity
- phosphatidylinositol-4,5-bisphosphate 3-kinase activity
- phosphoinositide 3-kinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biological regulation
- glycerophospholipid metabolic process
- intracellular signal transduction
- metabolic process
- organophosphate metabolic process
- phosphoinositide metabolic process
- phosphoinositide phosphorylation
- phosphoinositide-mediated signaling
- phospholipid metabolic process
- regulation of biological process
- regulation of cellular process
- second-messenger-mediated signaling
- signal transduction
|
| Component |
- macromolecular complex
- phosphoinositide 3-kinase complex
- protein complex
|
|
| Enzyme 8 General Function |
Involved in binding |
| Enzyme 8 Specific Function |
Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2 with a preference for PtdIns(4,5)P2 |
| Enzyme 8 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 8 Reactions |
- ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate [RN:R04545]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
Not Available |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P42338  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
PK3CB_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>3213 bp
ATGTGCTTCAGTTTCATAATGCCTCCTGCTATGGCAGACATCCTTGACATCTGGGCGGTG
GATTCACAGATAGCATCTGATGGCTCCATACCTGTGGATTTCCTTTTGCCCACTGGGATT
TATATCCAGTTGGAGGTACCTCGGGAAGCTACCATTTCTTATATTAAGCAGATGTTATGG
AAGCAAGTTCACAATTACCCAATGTTCAACCTCCTTATGGATATTGACTCCTATATGTTT
GCATGTGTGAATCAGACTGCTGTATATGAGGAGCTTGAAGATGAAACACGAAGACTCTGT
GATGTCAGACCTTTTCTTCCAGTTCTCAAATTAGTGACAAGAAGTTGTGACCCAGGGGAA
AAATTAGACTCAAAAATTGGAGTCCTTATAGGAAAAGGTCTGCATGAATTTGATTCCTTG
AAGGATCCTGAAGTAAATGAATTTCGAAGAAAAATGCGCAAATTCAGCGAGGAAAAAATC
CTGTCACTTGTGGGATTGTCTTGGATGGACTGGCTAAAACAAACATATCCACCAGAGCAT
GAACCATCCATCCCTGAAAACTTAGAAGATAAACTTTATGGGGGAAAGCTCATCGTAGCT
GTTCATTTTGAAAACTGCCAGGACGTGTTTAGCTTTCAAGTGTCTCCTAATATGAATCCT
ATCAAAGTAAATGAATTGGCAATCCAAAAACGTTTGACTATTCATGGGAAGGAAGATGAA
GTTAGCCCCTATGATTATGTGTTGCAAGTCAGCGGGAGAGTAGAATATGTTTTTGGTGAT
CATCCACTAATTCAGTTCCAGTATATCCGGAACTGTGTGATGAACAGAGCCCTGCCCCAT
TTTATACTTGTGGAATGCTGCAAGATCAAGAAAATGTATGAACAAGAAATGATTGCCATA
GAGGCTGCCATAAATCGAAATTCATCTAATCTTCCTCTTCCATTACCACCAAAGAAAACA
CGAATTATTTCTCATGTTTGGGAAAATAACAACCCTTTCCAAATTGTCTTGGTTAAGGGA
AATAAACTTAACACAGAGGAAACTGTAAAAGTTCATGTCAGGGCTGGTCTTTTTCATGGT
ACTGAGCTCCTGTGTAAAACCATCGTAAGCTCAGAGGTATCAGGGAAAAATGATCATATT
TGGAATGAACCACTGGAATTTGATATTAATATTTGTGACTTACCAAGAATGGCTCGATTA
TGTTTTGCTGTTTATGCAGTTTTGGATAAAGTAAAAACGAAGAAATCAACGAAAACTATT
AATCCCTCTAAATATCAGACCATCAGGAAAGCTGGAAAAGTGCATTATCCTGTAGCGTGG
GTAAATACGATGGTTTTTGACTTTAAAGGACAATTGAGAACTGGAGACATAATATTACAC
AGCTGGTCTTCATTTCCTGATGAACTCGAAGAAATGTTGAATCCAATGGGAACTGTTCAA
ACAAATCCATATACTGAAAATGCAACAGCTTTGCATGTTAAATTTCCAGAGAATAAAAAA
CAACCTTATTATTACCCTCCCTTCGATAAGATTATTGAAAAGGCAGCTGAGATTGCAAGC
AGTGATAGTGCTAATGTGTCAAGTCGAGGTGGAAAAAAGTTTCTTCCTGTATTGAAAGAA
ATCTTGGACAGGGATCCCTTGTCTCAACTGTGTGAAAATGAAATGGATCTTATTTGGACT
TTGCGACAAGACTGCCGAGAGATTTTCCCACAATCACTGCCAAAATTACTGCTGTCAATC
AAGTGGAATAAACTTGAGGATGTTGCTCAGCTTCAGGCGCTGCTTCAGATTTGGCCTAAA
CTGCCCCCCCGGGAGGCCCTAGAGCTTCTGGATTTCAACTATCCAGACCAGTACGTTCGA
GAATATGCTGTAGGCTGCCTGCGACAGATGAGTGATGAAGAACTTTCTCAATATCTTTTA
CAACTGGTGCAAGTGTTAAAATATGAGCCTTTTCTTGATTGTGCCCTCTCTAGATTCCTA
TTAGAAAGAGCACTTGGTAATCGGAGGATAGGGCAGTTTCTATTTTGGCATCTTAGGTCA
GAAGTGCACATTCCTGCTGTCTCAGTACAATTTGGTGTCATCCTTGAAGCATACTGCCGG
GGAAGTGTGGGGCACATGAAAGTGCTTTCTAAGCAGGTTGAAGCACTCAATAAGTTAAAA
ACTTTAAATAGTTTAATCAAACTGAATGCCGTGAAGTTAAACAGAGCCAAAGGGAAGGAG
GCCATGCATACCTGTTTAAAACAGAGTGCTTACCGGGAAGCCCTCTCTGACCTGCAGTCA
CCCCTGAACCCATGTGTTATCCTCTCAGAACTCTATGTTGAAAAGTGCAAATACATGGAT
TCCAAAATGAAGCCTTTGTGGCTGGTATACAATAACAAGGTATTTGGTGAGGATTCAGTT
GGAGTGATTTTTAAAAATGGTGATGATTTACGACAGGATATGTTGACACTCCAAATGTTG
CGCTTGATGGATTTACTCTGGAAAGAAGCTGGTTTGGATCTTCGGATGTTGCCTTATGGC
TGTTTAGCAACAGGAGATCGCTCTGGCCTCATTGAAGTTGTGAGCACCTCTGAAACAATT
GCTGACATTCAGCTGAACAGTAGCAATGTGGCTGCTGCAGCAGCCTTCAACAAAGATGCC
CTTCTGAACTGGCTTAAAGAATACAACTCTGGGGATGACCTGGACCGAGCCATTGAGGAA
TTTACACTGTCCTGTGCTGGCTACTGTGTAGCTTCTTATGTCCTTGGGATTGGTGACAGA
CATAGTGACAACATCATGGTCAAAAAAACTGGCCAGCTCTTCCACATTGACTTTGGACAT
ATTCTTGGAAATTTCAAATCTAAGTTTGGCATTAAAAGGGAGCGAGTGCCTTTTATTCTT
ACCTATGATTTCATCCATGTCATTCAACAAGGAAAAACAGGAAATACAGAAAAGTTTGGC
CGGTTCCGCCAGTGTTGTGAGGATGCATATCTGATTTTACGACGGCATGGGAATCTCTTC
ATCACTCTCTTTGCGCTGATGTTGACTGCAGGGCTTCCTGAACTCACATCAGTCAAAGAT
ATACAGTATCTTAAGGACTCTCTTGCATTAGGGAAGAGTGAAGAAGAAGCACTCAAACAG
TTTAAGCAAAAATTTGATGAGGCGCTCAGGGAAAGCTGGACTACTAAAGTGAACTGGATG
GCCCACACAGTTCGGAAAGACTACAGATCTTAA
|
| Enzyme 8 GenBank Gene ID |
S67334  |
| Enzyme 8 GeneCard ID |
PIK3CB  |
| Enzyme 8 GenAtlas ID |
PIK3CB  |
| Enzyme 8 HGNC ID |
HGNC:8976  |
| Enzyme 8 Chromosome Location |
3 |
| Enzyme 8 Locus |
3q22.3 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Hu P, Mondino A, Skolnik EY, Schlessinger J: Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85. Mol Cell Biol. 1993 Dec;13(12):7677-88. [PubMed
]
- Kossila M, Sinkovic M, Karkkainen P, Laukkanen MO, Miettinen R, Rissanen J, Kekalainen P, Kuusisto J, Yla-Herttuala S, Laakso M: Gene encoding the catalytic subunit p110beta of human phosphatidylinositol 3-kinase: cloning, genomic structure, and screening for variants in patients with type 2 diabetes. Diabetes. 2000 Oct;49(10):1740-3. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, 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 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
6532 |
| Enzyme 9 Name |
Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha isoform |
| Enzyme 9 Synonyms |
- PI3-kinase subunit alpha
- PI3K-alpha
- PtdIns-3-kinase subunit alpha
- Phosphatidylinositol-4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha
- PtdIns-3-kinase subunit p110-alpha
|
| Enzyme 9 Gene Name |
PIK3CA |
| Enzyme 9 Protein Sequence |
>Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
MPPRPSSGELWGIHLMPPRILVECLLPNGMIVTLECLREATLITIKHELFKEARKYPLHQ
LLQDESSYIFVSVTQEAEREEFFDETRRLCDLRLFQPFLKVIEPVGNREEKILNREIGFA
IGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKH
IYNKLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLK
LCVLEYQGKYILKVCGCDEYFLEKYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPMD
CFTMPSYSRRISTATPYMNGETSTKSLWVINSALRIKILCATYVNVNIRDIDKIYVRTGI
YHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHC
PLAWGNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNPNKETPCLELEFDWF
SSVVKFPDMSVIEEHANWSVSREAGFSYSHAGLSNRLARDNELRENDKEQLKAISTRDPL
SEITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMYCLVKDWPPIKPEQAME
LLDCNYPDPMVRGFAVRCLEKYLTDDKLSQYLIQLVQVLKYEQYLDNLLVRFLLKKALTN
QRIGHFFFWHLKSEMHNKTVSQRFGLLLESYCRACGMYLKHLNRQVEAMEKLINLTDILK
QEKKDETQKVQMKFLVEQMRRPDFMDALQGFLSPLNPAHQLGNLRLEECRIMSSAKRPLW
LNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLS
IGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRS
CAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDF
LIVISKGAQECTKTREFERFQEMCYKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIA
YIRKTLALDKTEQEALEYFMKQMNDAHHGGWTTKMDWIFHTIKQHALN
|
| Enzyme 9 Number of Residues |
1068 |
| Enzyme 9 Molecular Weight |
124283.0 |
| Enzyme 9 Theoretical pI |
7.23 |
| Enzyme 9 GO Classification |
| Function |
- 1-phosphatidylinositol-3-kinase activity
- binding
- catalytic activity
- inositol or phosphatidylinositol kinase activity
- kinase activity
- lipid kinase activity
- phosphatidylinositol-4,5-bisphosphate 3-kinase activity
- phosphoinositide 3-kinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biological regulation
- glycerophospholipid metabolic process
- intracellular signal transduction
- metabolic process
- organophosphate metabolic process
- phosphoinositide metabolic process
- phosphoinositide phosphorylation
- phosphoinositide-mediated signaling
- phospholipid metabolic process
- regulation of biological process
- regulation of cellular process
- second-messenger-mediated signaling
- signal transduction
|
| Component |
- macromolecular complex
- phosphoinositide 3-kinase complex
- protein complex
|
|
| Enzyme 9 General Function |
Involved in binding |
| Enzyme 9 Specific Function |
Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2 with a preference for PtdIns(4,5)P2 |
| Enzyme 9 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 9 Reactions |
- ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate [RN:R04545]
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
472991  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P42336  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
PK3CA_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>3207 bp
ATGCCTCCAAGACCATCATCAGGTGAACTGTGGGGCATCCACTTGATGCCCCCAAGAATC
CTAGTGGAATGTTTACTACCAAATGGAATGATAGTGACTTTAGAATGCCTCCGTGAGGCT
ACATTAGTAACTATAAAGCATGAACTATTTAAAGAAGCAAGAAAATACCCTCTCCATCAA
CTTCTTCAAGATGAATCTTCTTACATTTTCGTAAGTGTTACCCAAGAAGCAGAAAGGGAA
GAATTTTTTGATGAAACAAGACGACTTTGTGATCTTCGGCTTTTTCAACCATTTTTAAAA
GTAATTGAACCAGTAGGCAACCGTGAAGAAAAGATCCTCAATCGAGAAATTGGTTTTGCT
ATCGGCATGCCAGTGTGCGAATTTGATATGGTTAAAGATCCTGAAGTACAGGACTTCCGA
AGAAATATTCTTAATGTTTGTAAAGAAGCTGTGGATCTTAGGGATCTTAATTCACCTCAT
AGTAGAGCAATGTATGTCTATCCGCCACATGTAGAATCTTCACCAGAGCTGCCAAAGCAC
ATATATAATAAATTGGATAGAGGCCAAATAATAGTGGTGATTTGGGTAATAGTTTCTCCA
AATAATGACAAGCAGAAGTATACTCTGAAAATCAACCATGACTGTGTGCCAGAACAAGTA
ATTGCTGAAGCAATCAGGAAAAAAACTAGAAGTATGTTGCTATCATCTGAACAATTAAAA
CTCTGTGTTTTAGAATATCAGGGCAAGTACATTTTAAAAGTGTGTGGATGTGATGAATAC
TTCCTAGAAAAATATCCTCTGAGTCAGTATAAGTATATAAGAAGCTGTATAATGCTTGGG
AGGATGCCCAATTTGAAGATGATGGCTAAAGAAAGCCTTTATTCTCAACTGCCAATGGAC
TGTTTTACAATGCCATCTTATTCCAGACGCATTTCCACAGCTACACCATATATGAATGGA
GAAACATCTACAAAATCCCTTTGGGTTATAAATAGAGCACTCAGAATAAAAATTCTTTGT
GCAACCTACGTGAATCTAAATATTCGAGACATTGACAAGATTTATGTTCGAACAGGTATC
TACCATGGAGGAGAACCCTTATGTGACAATGTGAACACTCAAAGAGTACCTTGTTCCAAT
CCCAGGTGGAATGAATGGCTGAATTATGATATATACATTCCTGATCTTCCTCGTGCTGCT
CGACTTTGCCTTTCCATTTGCTCTGTTAAAGGCCGAAAGGGTGCTAAAGAGGAACACTGT
CCATTGGCATGGGGAAATATAAACTTGTTTGATTACACAGACACTCTAGTATCTGGAAAA
ATGGCTTTGAATCTTTGGCCAGTACCTCATGGATTAGAAGATTTGCTGAACCCTATTGGT
GTTACTGGATCAAATCCAAATAAAGAAACTCCATGCTTAGAGTTGGAGTTTGACTGGTTC
AGCAGTGTGGTAAAGTTCCCAGATATGTCAGTGATTGAAGAGCATGCCAATTGGTCTGTA
TCCCGAGAAGCAGGATTTAGCTATTCCCACGCAGGACTGAGTAACAGACTAGCTAGAGAC
AATGAATTAAGGGAAAATGACAAAGAACAGCTCAAAGCAATTTCTACACGAGATCCTCTC
TCTGAAATCACTGAGCAGGAGAAAGATTTTCTATGGAGTCACAGACACTATTGTGTAACT
ATCCCCGAAATTCTACCCAAATTGCTTCTGTCTGTTAAATGGAATTCTAGAGATGAAGTA
GCCCAGATGTATTGCTTGGTAAAAGATTGGCCTCCAATCAAACCTGAACAGGCTATGGAA
CTTCTGGACTGTAATTACCCAGATCCTATGGTTCGAGGTTTTGCTGTTCGGTGCTTGGAA
AAATATTTAACAGATGACAAACTTTCTCAGTATTTAATTCAGCTAGTACAGGTCCTAAAA
TATGAACAATATTTGGATAACTTGCTTGTGAGATTTTTACTGAAGAAAGCATTGACTAAT
CAAAGGATTGGGCACTTTTTCTTTTGGCATTTAAAATCTGAGATGCACAATAAAACAGTT
AGCCAGAGGTTTGGCCTGCTTTTGGAGTCCTATTGTCGTGCATGTGGGATGTATTTGAAG
CACCTGAATAGGCAAGTCGAGGCAATGGAAAAGCTCATTAACTTAACTGACATTCTCAAA
CAGGAGAGGAAGGATGAAACACAAAAGGTACAGATGAAGTTTTTAGTTGAGCAAATGAGG
CGACCAGATTTCATGGATGCCCTACAGGGCTTGCTGTCTCCTCTAAACCCTGCTCATCAA
CTAGGAAACCTCAGGCTTAAAGAGTGTCGAATTATGTCTTCTGCAAAAAGGCCACTGTGG
TTGAATTGGGAGAACCCAGACATCATGTCAGAGTTACTGTTTCAGAACAATGAGATCATC
TTTAAAAATGGGGATGATTTACGGCAAGATATGCTAACACTTCAAATTATTCGTATTATG
GAAAATATCTGGCAAAATCAAGGTCTTGATCTTCGAATGTTACCTTATGGTTGTCTGTCA
ATCGGTGACTGTGTGGGACTTATTGAGGTGGTGCGAAATTCTCACACTATTATGCAAATT
CAGTGCAAAGGCGGCTTGAAAGGTGCACTGCAGTTCAACAGCCACACACTACATCAGTGG
CTCAAAGACAAGAACAAAGGAGAAATATATGATGCAGCCATTGACCTGTTTACACGTTCA
TGTGCTGGATACTGTGTAGCTACCTTCATTTTGGGAATTGGAGATCGTCACAATAGTAAC
ATCATGGTGAAAGACGATGGACAACTGTTTCATATAGATTTTGGACACTTTTTGGATCAC
AAGAAGAAAAAATTTGGTTATAAACGAGAACGTGTGCCATTTGTTTTGACACAGGATTTC
TTAATAGTGATTAGTAAAGGAGCCCAAGAATGCACAAAGACAAGAGAATTTGAGAGGTTT
CAGGAGATGTGTTACAAGGCTTATCTAGCTATTCGACAGCATGCCAATCTCTTCATAAAT
CTTTTCTCAATGATGCTTGGCTCTGGAATGCCAGAACTACAATCTTTTGATGACATTGCA
TACATTCGAAAGACCCTAGCCTTAGATAAAACTGAGCAAGAGGCTTTGGAGTATTTCATG
AAACAAATGAATGATGCACATCATGGTGGCTGGACAACAAAAATGGATTGGATCTTCCAC
ACAATTAAACAGCATGCATTGAACTGA
|
| Enzyme 9 GenBank Gene ID |
Z29090  |
| Enzyme 9 GeneCard ID |
PIK3CA  |
| Enzyme 9 GenAtlas ID |
PIK3CA  |
| Enzyme 9 HGNC ID |
HGNC:8975  |
| Enzyme 9 Chromosome Location |
3 |
| Enzyme 9 Locus |
3q26.3 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Volinia S, Hiles I, Ormondroyd E, Nizetic D, Antonacci R, Rocchi M, Waterfield MD: Molecular cloning, cDNA sequence, and chromosomal localization of the human phosphatidylinositol 3-kinase p110 alpha (PIK3CA) gene. Genomics. 1994 Dec;24(3):472-7. [PubMed
]
- Stirdivant SM, Ahern J, Conroy RR, Barnett SF, Ledder LM, Oliff A, Heimbrook DC: Cloning and mutagenesis of the p110 alpha subunit of human phosphoinositide 3'-hydroxykinase. Bioorg Med Chem. 1997 Jan;5(1):65-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Broderick DK, Di C, Parrett TJ, Samuels YR, Cummins JM, McLendon RE, Fults DW, Velculescu VE, Bigner DD, Yan H: Mutations of PIK3CA in anaplastic oligodendrogliomas, high-grade astrocytomas, and medulloblastomas. Cancer Res. 2004 Aug 1;64(15):5048-50. [PubMed
]
- Campbell IG, Russell SE, Choong DY, Montgomery KG, Ciavarella ML, Hooi CS, Cristiano BE, Pearson RB, Phillips WA: Mutation of the PIK3CA gene in ovarian and breast cancer. Cancer Res. 2004 Nov 1;64(21):7678-81. [PubMed
]
- Samuels Y, Wang Z, Bardelli A, Silliman N, Ptak J, Szabo S, Yan H, Gazdar A, Powell SM, Riggins GJ, Willson JK, Markowitz S, Kinzler KW, Vogelstein B, Velculescu VE: High frequency of mutations of the PIK3CA gene in human cancers. Science. 2004 Apr 23;304(5670):554. Epub 2004 Mar 11. [PubMed
]
- Hartmann C, Bartels G, Gehlhaar C, Holtkamp N, von Deimling A: PIK3CA mutations in glioblastoma multiforme. Acta Neuropathol. 2005 Jun;109(6):639-42. Epub 2005 May 28. [PubMed
]
- Li VS, Wong CW, Chan TL, Chan AS, Zhao W, Chu KM, So S, Chen X, Yuen ST, Leung SY: Mutations of PIK3CA in gastric adenocarcinoma. BMC Cancer. 2005 Mar 23;5:29. [PubMed
]
- Ikenoue T, Kanai F, Hikiba Y, Obata T, Tanaka Y, Imamura J, Ohta M, Jazag A, Guleng B, Tateishi K, Asaoka Y, Matsumura M, Kawabe T, Omata M: Functional analysis of PIK3CA gene mutations in human colorectal cancer. Cancer Res. 2005 Jun 1;65(11):4562-7. [PubMed
]
- Oda K, Stokoe D, Taketani Y, McCormick F: High frequency of coexistent mutations of PIK3CA and PTEN genes in endometrial carcinoma. Cancer Res. 2005 Dec 1;65(23):10669-73. [PubMed
]
- Velho S, Oliveira C, Ferreira A, Ferreira AC, Suriano G, Schwartz S Jr, Duval A, Carneiro F, Machado JC, Hamelin R, Seruca R: The prevalence of PIK3CA mutations in gastric and colon cancer. Eur J Cancer. 2005 Jul;41(11):1649-54. [PubMed
]
- Wang Y, Helland A, Holm R, Kristensen GB, Borresen-Dale AL: PIK3CA mutations in advanced ovarian carcinomas. Hum Mutat. 2005 Mar;25(3):322. [PubMed
]
- Lee JW, Soung YH, Kim SY, Lee HW, Park WS, Nam SW, Kim SH, Lee JY, Yoo NJ, Lee SH: PIK3CA gene is frequently mutated in breast carcinomas and hepatocellular carcinomas. Oncogene. 2005 Feb 17;24(8):1477-80. [PubMed
]
- Qiu W, Schonleben F, Li X, Ho DJ, Close LG, Manolidis S, Bennett BP, Su GH: PIK3CA mutations in head and neck squamous cell carcinoma. Clin Cancer Res. 2006 Mar 1;12(5):1441-6. [PubMed
]
- Or YY, Hui AB, To KF, Lam CN, Lo KW: PIK3CA mutations in nasopharyngeal carcinoma. Int J Cancer. 2006 Feb 15;118(4):1065-7. [PubMed
]
- Buttitta F, Felicioni L, Barassi F, Martella C, Paolizzi D, Fresu G, Salvatore S, Cuccurullo F, Mezzetti A, Campani D, Marchetti A: PIK3CA mutation and histological type in breast carcinoma: high frequency of mutations in lobular carcinoma. J Pathol. 2006 Feb;208(3):350-5. [PubMed
]
- Bader AG, Kang S, Vogt PK: Cancer-specific mutations in PIK3CA are oncogenic in vivo. Proc Natl Acad Sci U S A. 2006 Jan 31;103(5):1475-9. Epub 2006 Jan 23. [PubMed
]
- Hafner C, Lopez-Knowles E, Luis NM, Toll A, Baselga E, Fernandez-Casado A, Hernandez S, Ribe A, Mentzel T, Stoehr R, Hofstaedter F, Landthaler M, Vogt T, Pujol RM, Hartmann A, Real FX: Oncogenic PIK3CA mutations occur in epidermal nevi and seborrheic keratoses with a characteristic mutation pattern. Proc Natl Acad Sci U S A. 2007 Aug 14;104(33):13450-4. Epub 2007 Aug 2. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6572 |
| Enzyme 10 Name |
1-phosphatidylinositol-3-phosphate 5-kinase |
| Enzyme 10 Synonyms |
- Phosphatidylinositol-3-phosphate 5-kinase
- FYVE finger-containing phosphoinositide kinase
- PIKfyve
- Phosphatidylinositol-3-phosphate 5-kinase type III
- PIPkin-III
- Type III PIP kinase
|
| Enzyme 10 Gene Name |
PIKFYVE |
| Enzyme 10 Protein Sequence |
>1-phosphatidylinositol-3-phosphate 5-kinase
MATDDKTSPTLDSANDLPRSPTSPSHLTHFKPLTPDQDEPPFKSAYSSFVNLFRFNKERA
EGGQGEQQPLSGSWTSPQLPSRTQSVRSPTPYKKQLNEELQRRSSALDTRRKAEPTFGGH
DPRTAVQLRSLSTVLKRLKEIMEGKSQDSDLKQYWMPDSQCKECYDCSEKFTTFRRRHHC
RLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYCRKIALSYAHSTDSNSIGEDLNALSDSA
CSVSVLDPSEPRTPVGSRKASRNIFLEDDLAWQSLIHPDSSNTPLSTRLVSVQEDAGKSP
ARNRSASITNLSLDRSGSPMVPSYETSVSPQANRTYVRTETTEDERKILLDSVQLKDLWK
KICHHSSGMEFQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLD
CVSHHDQLFRDEYALYRPLQSTEFSETPSPDSDSVNSVEGHSEPSWFKDIKFDDSDTEQI
AEEGDDNLANSASPSKRTSVSSFQSTVDSDSAASISLNVELDNVNFHIKKPSKYPHVPPH
PADQKEYLISDTGGQQLSISDAFIKESLFNRRVEEKSKELPFTPLGWHHNNLELLREENG
EKQAMERLLSANHNHMMALLQQLLHSDSLSSSWRDIIVSLVCQVVQTVRPDVKNQDDDMD
IRQFVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIEYLYREETK
FTCIDPIVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVL
ERISRMTQGDLVMSMDQLLTKPHLGTCHKFYMQIFQLPNEQTKTLMFFEGCPQHLGCTIK
LRGGSDYELARVKEILIFMICVAYHSQLEISFLMDEFAMPPTLMQNPSFHSLIEGRGHEG
AVQEQYGGGSIPWDPDIPPESLPCDDSSLLELRIVFEKGEQENKNLPQAVASVKHQEHST
TACPAGLPCAFFAPVPESLLPLPVDDQQDALGSEQPETLQQTVVLQDPKSQIRAFRDPLQ
DDTGLYVTEEVTSSEDKRKTYSLAFKQELKDVILCISPVITFREPFLLTEKGMRCSTRDY
FAEQVYWSPLLNKEFKEMENRRKKQLLRDLSGLQGMNGSIQAKSIQVLPSHELVSTRIAE
HLGDSQSLGRMLADYRARGGRIQPKNSDPFAHSKDASSTSSGQSGSKNEGDEERGLILSD
AVWSTKVDCLNPINHQRLCVLFSSSSAQSSNAPSACVSPWIVTMEFYGKNDLTLGIFLER
YCFRPSYQCPSMFCDTPMVHHIRRFVHGQGCVQIILKELDSPVPGYQHTILTYSWCRICK
QVTPVVALSNESWSMSFAKYLELRFYGHQYTRRANAEPCGHSIHHDYHQYFSYNQMVASF
SYSPIRLLEVCVPLPKIFIKRQAPLKVSLLQDLKDFFQKVSQVYVAIDERLASLKTDTFS
KTREEKMEDIFAQKEMEEGEFKNWIEKMQARLMSSSVDTPQQLQSVFESLIAKKQSLCEV
LQAWNNRLQDLFQQEKGRKRPSVPPSPGRLRQGEESKISAMDASPRNISPGLQNGEKEDR
FLTTLSSQSSTSSTHLQLPTPPEVMSEQSVGGPPELDTASSSEDVFDGHLLGSTDSQVKE
KSTMKAIFANLLPGNSYNPIPFPFDPDKHYLMYEHERVPIAVCEKEPSSIIAFALSCKEY
RNALEELSKATQWNSAEEGLPTNSTSDSRPKSSSPIRLPEMSGGQTNRTTETEPQPTKKA
SGMLSFFRGTAGKSPDLSSQKRETLRGADSAYYQVGQTGKEGTENQGVEPQDEVDGGDTQ
KKQLINPHVELQFSDANAKFYCRLYYAGEFHKMREVILDSSEEDFIRSLSHSSPWQARGG
KSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYITNAVQQKRPTALAKILGVYRIG
YKNSQNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKTDTGKESCDVVLLDENLL
KMVRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDTSNELVVGIIDYIRT
FTWDKKLEMVVKSTGILGGQGKMPTVVSPELYRTRFCEAMDKYFLMVPDHWTGLGLNC
|
| Enzyme 10 Number of Residues |
2098 |
| Enzyme 10 Molecular Weight |
237134.1 |
| Enzyme 10 Theoretical pI |
6.67 |
| Enzyme 10 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- ion binding
- kinase activity
- lipid kinase activity
- metal ion binding
- nucleoside binding
- phosphatidylinositol phosphate kinase activity
- protein binding
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- cellular protein metabolic process
- glycerophospholipid metabolic process
- intracellular signaling pathway
- macromolecule metabolic process
- metabolic process
- organophosphate metabolic process
- phosphatidylinositol metabolic process
- phosphoinositide metabolic process
- phospholipid metabolic process
- protein metabolic process
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in protein binding |
| Enzyme 10 Specific Function |
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol-3-phosphate on the fifth hydroxyl of the myo- inositol ring, to form phosphatidylinositol-3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. Plays a role in the biogenesis of endosome carrier vesicles (ECV)/ multivesicular bodies (MVB) transport intermediates from early endosomes |
| Enzyme 10 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 10 Reactions |
- ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate [RN:R05802]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
121583483  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q9Y2I7  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
FYV1_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>6297 bp
ATGGCCACAGATGATAAGACGTCCCCAACACTGGACTCTGCTAATGATTTGCCTCGATCT
CCTACTAGTCCTTCTCATCTCACACACTTTAAACCTTTGACTCCTGATCAAGATGAGCCC
CCTTTTAAATCAGCTTATAGTTCTTTTGTAAATCTCTTTCGTTTTAACAAAGAGAGAGCA
GAAGGAGGCCAGGGAGAACAGCAGCCTTTGAGTGGAAGTTGGACCAGCCCTCAGCTCCCT
TCGAGGACACAGTCTGTTAGGTCACCCACACCTTATAAAAAGCAGCTTAATGAGGAACTC
CAGCGGCGCTCTTCAGCATTAGACACAAGAAGGAAAGCAGAACCTACCTTTGGAGGTCAT
GACCCTCGTACAGCTGTTCAGCTTCGAAGCCTCAGCACAGTATTAAAACGCCTCAAGGAA
ATCATGGAGGGGAAAAGCCAGGATAGTGACCTGAAACAATACTGGATGCCAGATAGCCAA
TGTAAAGAGTGCTATGACTGTAGTGAGAAATTTACAACCTTTAGGCGCAGACACCATTGC
CGACTATGTGGGCAGATTTTCTGCAGTCGTTGCTGTAATCAAGAAATCCCTGGAAAATTT
ATGGGCTATACAGGAGACCTCCGAGCTTGCACATATTGTAGAAAAATAGCCTTAAGTTAT
GCTCATTCCACAGACAGTAATTCTATTGGGGAAGACTTGAATGCTCTTTCAGATTCTGCT
TGCTCTGTGTCTGTGCTTGATCCAAGTGAACCCCGAACACCTGTTGGGAGTAGGAAAGCC
AGCCGTAACATATTTTTAGAGGATGATTTGGCCTGGCAAAGTTTGATTCATCCAGATTCC
TCAAATACTCCTCTTTCAACAAGACTTGTATCTGTGCAAGAGGATGCTGGGAAATCTCCT
GCTCGAAATAGATCAGCCAGCATTACTAACCTGTCACTGGATAGATCTGGTTCTCCTATG
GTACCTTCATATGAGACATCTGTCAGTCCCCAGGCTAACCGAACATATGTTAGGACAGAG
ACCACTGAGGATGAACGCAAAATTCTTCTGGACAGTGTGCAGTTAAAAGACCTGTGGAAA
AAAATCTGCCATCACAGCAGTGGAATGGAGTTTCAGGATCACCGCTACTGGTTGAGAACG
CATCCCAACTGCATTGTAGGAAAGGAATTAGTCAACTGGCTAATCCGAAATGGGCATATT
GCCACAAGGGCACAAGCTATAGCAATTGGACAAGCAATGGTTGATGGACGTTGGCTGGAT
TGTGTTAGTCATCACGACCAGCTTTTCAGAGATGAGTATGCGCTGTATAGACCACTGCAG
AGTACAGAATTTTCTGAGACGCCTTCTCCCGACAGTGACTCAGTGAACTCCGTGGAAGGA
CACTCTGAGCCATCCTGGTTTAAAGACATAAAGTTTGATGACAGTGACACAGAACAGATA
GCTGAAGAAGGTGACGATAATTTGGCTAATTCTGCCAGTCCTAGCAAGCGCACATCAGTC
AGCAGTTTCCAGTCCACAGTGGACAGTGACTCAGCCGCTTCTATCAGCCTGAACGTGGAG
CTGGACAACGTGAACTTCCATATCAAGAAGCCCTCCAAGTACCCACATGTGCCCCCTCAC
CCTGCTGACCAAAAAGAGTATTTGATTTCTGACACTGGAGGACAACAGCTCTCAATAAGT
GACGCTTTCATCAAAGAATCCTTATTTAATCGCCGAGTAGAGGAAAAATCCAAAGAGCTG
CCTTTCACACCTTTGGGCTGGCATCATAACAACCTGGAGCTCCTGAGGGAGGAGAATGGG
GAGAAACAAGCCATGGAGAGGTTGCTTTCAGCTAATCATAACCACATGATGGCACTACTC
CAGCAGTTGCTCCATAGTGACTCACTGTCATCATCTTGGAGGGACATCATCGTGTCATTG
GTCTGCCAGGTTGTTCAGACAGTCCGACCTGATGTCAAGAACCAGGATGATGACATGGAT
ATCCGTCAGTTTGTCCACATCAAAAAAATCCCAGGTGGAAAGAAGTTTGATTCTGTGGTT
GTCAATGGCTTTGTTTGTACCAAGAACATTGCACATAAAAAGATGAGTTCTTGTATTAAA
AACCCCAAAATTCTTCTGTTGAAGTGTTCCATTGAGTATCTCTACAGAGAAGAAACTAAG
TTTACTTGCATTGATCCTATTGTGCTTCAGGAAAGGGAATTCTTGAAGAATTATGTCCAG
CGAATAGTTGATGTTCGACCCACCTTGGTTCTTGTTGAGAAAACAGTGTCTCGGATTGCC
CAGGACATGTTATTGGAACATGGCATTACTTTGGTCATTAATGTAAAGTCACAAGTTTTG
GAACGAATCAGTCGAATGACCCAAGGTGATTTAGTGATGTCAATGGACCAGCTGCTTACG
AAACCACACCTGGGCACTTGTCACAAATTTTATATGCAGATATTTCAGTTGCCTAATGAA
CAAACCAAGACACTGATGTTTTTTGAAGGTTGTCCACAGCACCTAGGCTGTACAATCAAG
CTAAGAGGAGGCTCTGATTATGAGCTGGCTCGAGTTAAGGAGATCCTAATATTTATGATC
TGTGTTGCTTATCATTCTCAACTAGAAATATCCTTTCTCATGGATGAATTTGCTATGCCT
CCCACATTAATGCAAAACCCTTCATTCCATTCCCTGATTGAGGGACGAGGGCATGAGGGG
GCTGTCCAAGAGCAGTACGGTGGAGGTTCCATCCCCTGGGATCCTGACATCCCTCCTGAG
TCTCTGCCCTGTGATGATAGCAGTTTGCTGGAATTGAGGATTGTGTTTGAGAAGGGTGAG
CAGGAAAATAAAAATCTTCCGCAGGCTGTTGCCTCTGTGAAGCATCAAGAACATAGCACA
ACAGCTTGCCCGGCGGGTCTCCCTTGTGCTTTCTTTGCACCTGTACCGGAATCATTGTTG
CCACTCCCTGTGGATGACCAACAAGATGCTTTAGGCAGCGAGCAGCCAGAGACTTTGCAG
CAAACAGTTGTGCTGCAGGATCCCAAAAGCCAGATAAGAGCCTTTAGAGACCCTCTACAG
GATGACACTGGATTATATGTTACTGAGGAAGTCACCTCCTCTGAAGATAAACGAAAGACT
TATTCTTTGGCCTTTAAGCAGGAATTAAAAGATGTGATCCTCTGTATCTCCCCAGTAATC
ACATTCCGAGAACCCTTTCTTTTAACTGAAAAGGGGATGAGATGCTCTACCCGAGATTAT
TTTGCAGAGCAGGTTTACTGGTCTCCTCTCCTCAATAAAGAATTCAAAGAAATGGAGAAC
AGGAGGAAGAAACAGCTGCTCAGGGATCTCTCTGGACTTCAGGGCATGAATGGAAGTATT
CAGGCCAAGTCTATTCAAGTCTTACCCTCACATGAGCTAGTGAGCACTAGAATTGCTGAG
CATCTGGGCGATAGCCAGAGCTTGGGTAGAATGCTGGCCGATTATCGAGCCAGAGGAGGA
AGAATTCAGCCCAAAAATTCAGACCCTTTTGCTCATTCAAAGGATGCATCAAGTACTTCA
AGTGGCCAATCAGGAAGCAAAAATGAGGGTGATGAAGAGAGAGGGCTTATTCTGAGTGAT
GCTGTGTGGTCAACAAAGGTGGACTGTCTGAATCCCATTAATCACCAGAGACTTTGTGTG
CTCTTCAGCAGCTCTTCTGCCCAGTCCAGCAATGCTCCTAGTGCCTGTGTCAGTCCTTGG
ATTGTAACAATGGAATTTTATGGAAAGAATGATCTTACATTAGGAATATTTTTAGAGAGA
TACTGTTTCAGGCCTTCTTATCAGTGTCCAAGCATGTTCTGTGATACCCCCATGGTACAT
CATATTCGGCGCTTTGTTCATGGCCAAGGCTGTGTGCAGATAATCCTGAAGGAGTTGGAT
TCTCCAGTACCTGGATATCAGCATACAATTCTTACATATTCCTGGTGTAGAATCTGCAAA
CAGGTAACACCAGTTGTTGCTCTTTCCAATGAGTCCTGGTCTATGTCATTTGCAAAATAC
CTTGAACTTAGGTTTTATGGGCACCAGTATACTCGCAGAGCCAACGCTGAGCCCTGTGGT
CACTCCATCCATCATGATTATCACCAGTATTTCTCCTATAACCAGATGGTGGCGTCTTTC
AGTTATTCTCCCATTCGGCTTCTTGAAGTATGTGTTCCACTCCCCAAAATATTCATTAAG
CGTCAGGCCCCATTAAAAGTGTCCCTTCTTCAGGATCTGAAGGACTTCTTTCAAAAAGTT
TCACAGGTATATGTTGCCATTGATGAAAGACTTGCATCTTTGAAAACTGATACATTTAGT
AAAACAAGAGAGGAAAAAATGGAAGATATTTTTGCACAGAAAGAGATGGAAGAAGGTGAG
TTCAAGAACTGGATTGAGAAGATGCAAGCAAGGCTCATGTCTTCCTCTGTAGATACCCCT
CAGCAACTGCAGTCGGTCTTTGAGTCACTCATTGCCAAGAAACAAAGTCTCTGTGAAGTG
CTGCAAGCTTGGAATAACAGGTTGCAGGACCTTTTCCAACAGGAAAAGGGTAGAAAGAGA
CCTTCAGTTCCTCCAAGTCCTGGAAGACTGAGACAAGGGGAAGAAAGCAAGATAAGTGCG
ATGGATGCATCTCCACGGAATATTTCTCCAGGACTTCAGAATGGAGAAAAAGAGGATCGC
TTCTTAACAACTTTGTCCAGCCAGAGCTCCACCAGTTCTACTCATCTCCAATTGCCTACG
CCACCTGAAGTCATGTCTGAACAGTCAGTGGGAGGGCCCCCTGAGCTAGATACAGCCAGC
AGTTCCGAAGATGTGTTTGATGGGCATTTGCTGGGATCCACAGACAGCCAAGTGAAGGAA
AAGTCAACCATGAAAGCCATCTTTGCAAATTTGCTTCCAGGAAATAGCTATAATCCTATT
CCATTTCCTTTTGATCCAGATAAACACTACTTAATGTATGAACATGAACGAGTGCCCATT
GCAGTCTGCGAGAAGGAACCCAGCTCCATCATTGCTTTTGCTCTCAGTTGTAAAGAATAC
CGAAATGCCTTAGAGGAATTGTCTAAAGCGACTCAGTGGAACAGTGCCGAAGAAGGGCTT
CCAACAAATAGTACTTCAGATAGCAGACCAAAGAGTAGCAGCCCTATCAGATTACCTGAA
ATGAGTGGAGGACAGACAAATCGTACAACAGAAACAGAACCACAACCAACCAAAAAGGCT
TCTGGAATGTTGTCCTTCTTCAGAGGGACAGCAGGGAAAAGCCCCGATCTCTCTTCCCAG
AAGAGAGAGACCTTACGTGGAGCAGATAGTGCTTACTACCAGGTTGGGCAGACGGGCAAG
GAGGGGACCGAGAATCAAGGCGTTGAGCCTCAAGATGAAGTAGATGGAGGAGATACACAA
AAGAAGCAACTCATAAATCCTCATGTGGAACTTCAATTTTCAGATGCTAATGCCAAGTTT
TACTGTCGGCTCTACTATGCGGGAGAGTTTCATAAGATGCGTGAAGTGATTCTGGACAGC
AGTGAAGAAGATTTCATTCGTTCCCTCTCCCACTCATCACCCTGGCAGGCCCGGGGAGGC
AAATCAGGAGCTGCCTTCTATGCAACTGAGGATGATAGATTTATTTTGAAGCAAATGCCT
CGTCTGGAAGTCCAGTCCTTCCTCGACTTTGCACCACATTACTTCAATTATATTACAAAT
GCTGTTCAACAAAAGAGGCCCACGGCGTTGGCCAAAATTCTTGGAGTTTACAGAATTGGT
TATAAGAACTCTCAGAACAACACTGAGAAGAAGTTAGATCTCCTTGTCATGGAAAATCTT
TTCTACGGGAGAAAGATGGCACAGGTTTTTGATTTGAAGGGCTCTCTTAGGAATCGGAAT
GTAAAAACTGACACTGGAAAAGAGAGTTGTGATGTGGTCCTGCTAGATGAAAATCTCCTA
AAGATGGTTCGAGACAACCCTCTATATATTCGTTCTCATTCCAAAGCTGTGCTGAGAACC
TCGATCCATAGTGACTCCCATTTCCTTTCTAGCCACCTCATTATAGATTATTCTTTGCTG
GTTGGGCGAGATGATACTAGCAATGAGCTAGTAGTTGGAATTATAGATTATATTCGAACA
TTTACATGGGACAAAAAGCTTGAGATGGTTGTGAAATCAACAGGAATTTTAGGTGGACAA
GGTAAAATGCCAACAGTGGTGTCTCCGGAGTTGTACAGGACTAGGTTTTGTGAGGCAATG
GACAAGTATTTCCTAATGGTACCAGACCACTGGACAGGCTTGGGTCTGAATTGCTGA
|
| Enzyme 10 GenBank Gene ID |
NM_015040.3  |
| Enzyme 10 GeneCard ID |
PIKFYVE  |
| Enzyme 10 GenAtlas ID |
PIKFYVE  |
| Enzyme 10 HGNC ID |
HGNC:23785  |
| Enzyme 10 Chromosome Location |
2 |
| Enzyme 10 Locus |
2q34 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- 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
]
- 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
]
- 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
]
- Sbrissa D, Ikonomov OC, Shisheva A: Phosphatidylinositol 3-phosphate-interacting domains in PIKfyve. Binding specificity and role in PIKfyve. Endomenbrane localization. J Biol Chem. 2002 Feb 22;277(8):6073-9. Epub 2001 Nov 12. [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
]
- 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
]
- Sbrissa D, Ikonomov OC, Fu Z, Ijuin T, Gruenberg J, Takenawa T, Shisheva A: Core protein machinery for mammalian phosphatidylinositol 3,5-bisphosphate synthesis and turnover that regulates the progression of endosomal transport. Novel Sac phosphatase joins the ArPIKfyve-PIKfyve complex. J Biol Chem. 2007 Aug 17;282(33):23878-91. Epub 2007 Jun 7. [PubMed
]
- Sbrissa D, Ikonomov OC, Fenner H, Shisheva A: ArPIKfyve homomeric and heteromeric interactions scaffold PIKfyve and Sac3 in a complex to promote PIKfyve activity and functionality. J Mol Biol. 2008 Dec 26;384(4):766-79. Epub 2008 Oct 11. [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
]
- Li S, Tiab L, Jiao X, Munier FL, Zografos L, Frueh BE, Sergeev Y, Smith J, Rubin B, Meallet MA, Forster RK, Hejtmancik JF, Schorderet DF: Mutations in PIP5K3 are associated with Francois-Neetens mouchetee fleck corneal dystrophy. Am J Hum Genet. 2005 Jul;77(1):54-63. Epub 2005 May 18. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6650 |
| Enzyme 11 Name |
Phosphatidylinositol-5-phosphate 4-kinase type-2 beta |
| Enzyme 11 Synonyms |
- 1-phosphatidylinositol-5-phosphate 4-kinase 2-beta
- Diphosphoinositide kinase 2-beta
- Phosphatidylinositol-5-phosphate 4-kinase type II beta
- PI(5)P 4-kinase type II beta
- PIP4KII-beta
- PtdIns(5)P-4-kinase isoform 2-beta
|
| Enzyme 11 Gene Name |
PIP4K2B |
| Enzyme 11 Protein Sequence |
>Phosphatidylinositol-5-phosphate 4-kinase type-2 beta
MSSNCTSTTAVAVAPLSASKTKTKKKHFVCQKVKLFRASEPILSVLMWGVNHTINELSNV
PVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNS
VTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLL
PQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKD
NDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDRAEQEEMEVEE
RAEDEECENDGVGGNLLCSYGTPPDSPGNLLSFPRFFGPGEFDPSVDVYAMKSHESSPKK
EVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSNILT
|
| Enzyme 11 Number of Residues |
416 |
| Enzyme 11 Molecular Weight |
47377.6 |
| Enzyme 11 Theoretical pI |
7.37 |
| Enzyme 11 GO Classification |
| Function |
- catalytic activity
- kinase activity
- lipid kinase activity
- phosphatidylinositol phosphate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- glycerophospholipid metabolic process
- metabolic process
- organophosphate metabolic process
- phosphatidylinositol metabolic process
- phosphoinositide metabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 11 General Function |
Involved in phosphatidylinositol phosphate kinase activity |
| Enzyme 11 Specific Function |
Participates in the biosynthesis of phosphatidylinositol-4,5-bisphosphate |
| Enzyme 11 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 11 Reactions |
- ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [RN:R05803]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
4505819  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
P78356  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
PI42B_HUMAN  |
| Enzyme 11 PDB ID |
1BO1  |
| Enzyme 11 PDB File |
Show |
| Enzyme 11 3D Structure |
|
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1251 bp
ATGTCGTCCAACTGCACCAGCACCACGGCGGTGGCGGTGGCGCCGCTCAGCGCCAGCAAG
ACCAAGACCAAGAAGAAGCATTTCGTGTGCCAGAAAGTGAAGCTATTCCGGGCCAGCGAG
CCGATCCTCAGCGTCCTGATGTGGGGGGTGAACCACACGATCAATGAGCTGAGCAATGTT
CCTGTTCCTGTCATGCTAATGCCAGATGACTTCAAAGCCTACAGCAAGATCAAGGTGGAC
AATCATCTCTTCAATAAGGAGAACCTGCCCAGCCGCTTTAAGTTTAAGGAGTATTGCCCC
ATGGTGTTCCGAAACCTTCGGGAGAGGTTTGGAATTGATGATCAGGATTACCAGAATTCA
GTGACGCGCAGCGCCCCCATCAACAGTGACAGCCAGGGTCGGTGTGGCACGCGTTTCCTC
ACCACCTACGACCGGCGCTTTGTCATCAAGACTGTGTCCAGCGAGGACGTGGCGGAGATG
CACAACATCTTAAAGAAATACCACCAGTTTATAGTGGAGTGTCATGGCAACACGCTTTTG
CCACAGTTCCTGGGCATGTACCGCCTGACCGTGGATGGTGTGGAAACCTACATGGTGGTT
ACCAGGAACGTGTTCAGCCATCGGCTCACTGTGCATCGCAAGTATGACCTCAAGGGTTCT
ACGGTTGCCAGAGAAGCGAGCGACAAGGAGAAGGCCAAGGACTTGCCAACATTCAAAGAC
AATGACTTCCTCAATGAAGGGCAGAAGCTGCATGTGGGAGAGGAGAGTAAAAAGAACTTC
CTGGAGAAACTGAAGCGGGACGTTGAGTTCTTGGCACAGCTGAAGATCATGGACTACAGC
CTGCTGGTGGGCATCCACGACGTGGACCGGGCAGAGCAGGAGGAGATGGAGGTGGAGGAG
CGGGCAGAGGACGAGGAGTGTGAGAATGATGGGGTGGGTGGCAACCTACTCTGCTCCTAT
GGCACACCTCCGGACAGCCCTGGCAACCTCCTCAGCTTTCCTCGGTTCTTTGGTCCTGGG
GAATTCGACCCCTCTGTTGACGTCTATGCCATGAAAAGCCATGAAAGTTCCCCCAAGAAG
GAGGTGTATTTCATGGCCATCATTGATATCCTCACGCCATACGATACAAAGAAGAAAGCT
GCACATGCTGCCAAAACGGTGAAACACGGGGCAGGGGCCGAGATCTCGACTGTGAACCCT
GAGCAGTACTCCAAACGCTTCAACGAGTTTATGTCCAACATCCTGACGTAG
|
| Enzyme 11 GenBank Gene ID |
NM_003559.4  |
| Enzyme 11 GeneCard ID |
PIP4K2B  |
| Enzyme 11 GenAtlas ID |
PIP4K2B  |
| Enzyme 11 HGNC ID |
HGNC:8998  |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
17q12 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Castellino AM, Parker GJ, Boronenkov IV, Anderson RA, Chao MV: A novel interaction between the juxtamembrane region of the p55 tumor necrosis factor receptor and phosphatidylinositol-4-phosphate 5-kinase. J Biol Chem. 1997 Feb 28;272(9):5861-70. [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
]
- 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
]
- 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
]
- Rao VD, Misra S, Boronenkov IV, Anderson RA, Hurley JH: Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation. Cell. 1998 Sep 18;94(6):829-39. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6707 |
| Enzyme 12 Name |
Phosphatidylinositol 4-kinase alpha |
| Enzyme 12 Synonyms |
- PI4-kinase alpha
- PI4K-alpha
- PtdIns-4-kinase alpha
|
| Enzyme 12 Gene Name |
PI4KA |
| Enzyme 12 Protein Sequence |
>Phosphatidylinositol 4-kinase alpha
MCPVDFHGIFQLDERRRDAVIALGIFLIESDLQHKDCVVPYLLRLLKGLPKVYWVEESTA
RKGRGALPVAESFSFCLVTLLSDVAYRDPSLRDEILEVLLQVLHVLLGMCQALEIQDKEY
LCKYAIPCLIGISRAFGRYSNMEESLLSKLFPKIPPHSLRVLEELEGVRRRSFNDFRSIL
PSNLLTVCQEGTLKRKTSSVSSISQVSPERGMPPPSSPGGSAFHYFEASCLPDGTALEPE
YYFSTISSSFSVSPLFNGVTYKEFNIPLEMLRELLNLVKKIVEEAVLKSLDAIVASVMEA
NPSADLYYTSFSDPLYLTMFKMLRDTLYYMKDLPTSFVKEIHDFVLEQFNTSQGELQKIL
HDADRIHNELSPLKLRCQANAACVDLMVWAVKDEQGAENLCIKLSEKLQSKTSSKVIIAH
LPLLICCLQGLGRLCERFPVVVHSVTPSLRDFLVIPSPVLVKLYKYHSQYHTVAGNDIKI
SVTNEHSESTLNVMSGKKSQPSMYEQLRDIAIDNICRCLKAGLTVDPVIVEAFLASLSNR
LYISQESDKDAHLIPDHTIRALGHIAVALRDTPKVMEPILQILQQKFCQPPSPLDVLIID
QLGCLVITGNQYIYQEVWNLFQQISVKASSVVYSATKDYKDHGYRHCSLAVINALANIAA
NIQDEHLVDELLMNLLELFVQLGLEGKRASERASEKGPALKASSSAGNLGVLIPVIAVLT
RRLPPIKEAKPRLQKLFRDFWLYSVLMGFAVEGSGLWPEEWYEGVCEIATKSPLLTFPSK
EPLRSVLQYNSAMKNDTVTPAELSELRSTIINLLDPPPEVSALINKLDFAMSTYLLSVYR
LEYMRVLRSTDPDRFQVMFCYFEDKAIQKDKSGMMQCVIAVADKVFDAFLNMMADKAKTK
ENEEELERHAQFLLVNFNHIHKRIRRVADKYLSGLVDKFPHLLWSGTVLKTMLDILQTLS
LSLSADIHKDQPYYDIPDAPYRITVPDTYEARESIVKDFAARCGMILQEAMKWAPTVTKS
HLQEYLNKHQNWVSGLSQHTGLAMATESILHFAGYNKQNTTLGATQLSERPACVKKDYSN
FMASLNLRNRYAGEVYGMIRFSGTTGQMSDLNKMMVQDLHSALDRSHPQHYTQAMFKLTA
MLISSKDCDPQLLHHLCWGPLRMFNEHGMETALACWEWLLAGKDGVEVPFMREMAGAWHM
TVEQKFGLFSAEIKEADPLAASEASQPKPCPPEVTPHYIWIDFLVQRFEIAKYCSSDQVE
IFSSLLQRSMSLNIGGAKGSMNRHVAAIGPRFKLLTLGLSLLHADVVPNATIRNVLREKI
YSTAFDYFSCPPKFPTQGEKRLREDISIMIKFWTAMFSDKKYLTASQLVPPDNQDTRSNL
DITVGSRQQATQGWINTYPLSSGMSTISKKSGMSKKTNRGSQLHKYYMKRRTLLLSLLAT
EIERLITWYNPLSAPELELDQAGENSVANWRSKYISLSEKQWKDNVNLAWSISPYLAVQL
PARFKNTEAIGNEVTRLVRLDPGAVSDVPEAIKFLVTWHTIDADAPELSHVLCWAPTDPP
TGLSYFSSMYPPHPLTAQYGVKVLRSFPPDAILFYIPQIVQALRYDKMGYVREYILWAAS
KSQLLAHQFIWNMKTNIYLDEEGHQKDPDIGDLLDQLVEEITGSLSGPAKDFYQREFDFF
NKITNVSAIIKPYPKGDERKKACLSALSEVKVQPGCYLPSNPEAIVLDIDYKSGTPMQSA
AKAPYLAKFKVKRCGVSELEKEGLRCRSDSEDECSTQEADGQKISWQAAIFKVGDDCRQD
MLALQIIDLFKNIFQLVGLDLFVFPYRVVATAPGCGVIECIPDCTSRDQLGRQTDFGMYD
YFTRQYGDESTLAFQQARYNFIRSMAAYSLLLFLLQIKDRHNGNIMLDKKGHIIHIDFGF
MFESSPGGNLGWEPDIKLTDEMVMIMGGKMEATPFKWFMEMCVRGYLAVRPYMDAVVSLV
TLMLDTGLPCFRGQTIKLLKHRFSPNMTEREAANFIMKVIQSCFLSNRSRTYDMIQYYQN
DIPY
|
| Enzyme 12 Number of Residues |
2044 |
| Enzyme 12 Molecular Weight |
231316.9 |
| Enzyme 12 Theoretical pI |
6.86 |
| Enzyme 12 GO Classification |
| Function |
- binding
- catalytic activity
- inositol or phosphatidylinositol kinase activity
- kinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biological regulation
- glycerophospholipid metabolic process
- intracellular signal transduction
- metabolic process
- organophosphate metabolic process
- phosphoinositide metabolic process
- phosphoinositide phosphorylation
- phosphoinositide-mediated signaling
- phospholipid metabolic process
- regulation of biological process
- regulation of cellular process
- second-messenger-mediated signaling
- signal transduction
|
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in binding |
| Enzyme 12 Specific Function |
Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol- 1,4,5,-trisphosphate |
| Enzyme 12 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 12 Reactions |
- ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate [RN:R03361]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
155030226  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P42356  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
PI4KA_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>6135 bp
ATGTGTCCAGTGGATTTCCATGGGATCTTCCAGTTAGATGAAAGACGGAGAGATGCAGTG
ATTGCATTGGGCATTTTTCTGATTGAATCTGATCTTCAGCACAAAGATTGTGTGGTTCCT
TACCTTCTTCGACTTCTCAAAGGTCTTCCAAAAGTGTATTGGGTAGAAGAAAGCACAGCT
CGGAAAGGCAGAGGTGCCCTCCCGGTTGCAGAGAGCTTCAGCTTCTGCTTGGTAACTCTG
CTGTCTGATGTGGCCTATAGGGATCCTTCACTTAGGGATGAGATTTTAGAGGTGCTTTTG
CAGGTTTTGCATGTCCTCTTGGGGATGTGCCAGGCCTTGGAGATTCAAGACAAAGAATAC
CTTTGCAAGTATGCTATCCCATGCCTGATAGGAATCTCGCGAGCATTTGGGCGTTACAGC
AACATGGAAGAGTCTCTCCTCTCAAAGCTCTTTCCCAAAATCCCTCCTCATTCCCTCCGT
GTCCTGGAAGAGCTTGAAGGTGTTCGAAGGCGTTCCTTTAATGACTTCCGCTCCATCCTC
CCCAGCAATCTGCTGACTGTCTGTCAGGAGGGTACCCTGAAGAGGAAAACCAGCAGTGTG
TCCAGCATCTCTCAGGTCAGCCCTGAACGCGGCATGCCCCCTCCCAGTTCCCCTGGAGGA
TCTGCCTTTCACTACTTTGAAGCCTCCTGCTTGCCCGATGGGACTGCCCTAGAGCCTGAG
TACTACTTTTCAACCATCAGCTCCAGCTTCTCAGTCTCTCCCCTTTTCAACGGTGTCACA
TATAAGGAGTTTAACATTCCATTGGAAATGCTTCGGGAACTCTTAAACCTGGTGAAGAAG
ATCGTTGAGGAGGCTGTTCTCAAATCTTTGGATGCCATTGTAGCCAGTGTGATGGAGGCC
AACCCCAGTGCTGATCTCTACTACACTTCCTTCAGTGACCCTCTCTACCTGACCATGTTC
AAGATGCTGCGTGACACTCTGTACTACATGAAGGACCTCCCGACCTCTTTTGTGAAGGAG
ATCCATGATTTTGTGCTGGAGCAGTTCAACACGAGCCAGGGGGAGCTCCAGAAGATTCTA
CATGACGCAGACCGGATCCACAATGAGCTGAGCCCCCTCAAACTGCGCTGTCAGGCGAAT
GCTGCCTGTGTGGACCTCATGGTGTGGGCTGTGAAGGACGAGCAGGGTGCAGAAAACCTT
TGCATCAAGCTATCTGAGAAGCTGCAGTCCAAGACGTCCAGCAAAGTCATTATTGCTCAC
TTGCCCCTGCTGATCTGCTGTCTGCAGGGTTTGGGCCGCCTGTGCGAGAGGTTCCCGGTG
GTGGTGCACTCTGTGACACCGTCCTTGCGAGACTTCCTGGTCATCCCGTCCCCAGTTCTG
GTGAAGCTCTACAAGTACCACAGTCAGTACCACACAGTTGCTGGCAATGATATAAAAATC
AGTGTGACCAATGAGCATTCCGAGTCAACCCTGAACGTCATGTCGGGTAAGAAGAGCCAG
CCCTCCATGTACGAGCAGCTCCGAGACATCGCTATTGACAACATCTGCAGGTGCCTGAAG
GCTGGATTGACGGTGGACCCAGTGATTGTGGAGGCGTTCTTGGCCAGCCTGTCCAACCGG
CTCTACATCTCTCAGGAGAGCGACAAGGACGCTCACTTGATTCCCGACCACACAATCCGA
GCCTTGGGACACATTGCGGTGGCCTTGAGGGACACCCCGAAGGTCATGGAGCCCATTCTG
CAGATCCTACAGCAGAAATTCTGCCAGCCACCCTCCCCCCTCGATGTGCTGATTATTGAC
CAGCTGGGCTGCCTGGTTATCACCGGAAATCAATACATCTATCAGGAAGTGTGGAACCTC
TTCCAGCAGATCAGTGTGAAGGCCAGCTCCGTTGTATACTCAGCCACCAAAGATTACAAG
GACCACGGCTATAGGCATTGCTCCCTGGCAGTGATTAATGCCCTGGCCAACATCGCGGCC
AACATCCAAGACGAGCACCTGGTGGATGAGCTGCTCATGAACCTGTTGGAGTTGTTTGTG
CAGCTGGGGCTGGAGGGGAAGCGAGCCAGCGAGAGGGCAAGCGAGAAGGGCCCTGCCCTA
AAGGCTTCTAGCAGTGCAGGGAACTTGGGAGTACTCATTCCTGTAATAGCTGTGCTCACC
CGACGACTGCCACCCATCAAAGAAGCTAAGCCTCGGTTACAGAAGCTCTTCCGAGACTTC
TGGCTGTATTCCGTTCTGATGGGATTCGCTGTGGAGGGCTCAGGACTCTGGCCAGAAGAA
TGGTACGAGGGGGTCTGTGAAATAGCCACTAAGTCCCCCTTGCTCACCTTTCCCAGCAAG
GAGCCACTGCGGTCCGTCCTCCAGTATAACTCAGCCATGAAGAATGACACGGTCACCCCC
GCTGAGCTGAGTGAGCTCCGCAGCACTATCATCAACCTGCTGGACCCCCCTCCCGAGGTG
TCCGCACTCATCAACAAGCTGGACTTCGCCATGTCCACCTACCTCCTCTCTGTGTACCGG
CTGGAGTACATGAGGGTACTGCGTTCAACAGATCCTGATCGCTTCCAGGTAATGTTCTGC
TACTTTGAGGATAAAGCTATTCAGAAAGACAAATCTGGGATGATGCAGTGTGTGATTGCA
GTCGCGGACAAAGTATTCGATGCCTTCCTGAACATGATGGCGGATAAAGCCAAGACCAAG
GAGAACGAGGAGGAGCTGGAGCGGCACGCTCAGTTCCTGTTGGTGAACTTCAACCACATC
CACAAGAGGATAAGGAGGGTGGCAGACAAGTATCTATCTGGTCTGGTGGATAAGTTTCCC
CACTTGCTCTGGAGCGGGACTGTGCTGAAGACCATGCTGGACATCCTGCAGACCCTGTCA
CTGTCACTGAGCGCTGATATTCACAAGGATCAGCCTTACTATGACATCCCCGACGCCCCC
TACCGGATCACGGTTCCTGACACGTACGAAGCCCGTGAGAGCATTGTGAAGGACTTCGCT
GCACGCTGTGGGATGATCCTCCAGGAGGCCATGAAGTGGGCACCTACCGTCACCAAGTCC
CACCTGCAGGAATATCTGAACAAACATCAGAACTGGGTATCGGGACTGTCCCAGCACACG
GGGCTGGCCATGGCCACTGAGAGCATCCTTCACTTTGCTGGCTACAACAAGCAGAACACA
ACTCTTGGGGCAACTCAGCTGAGCGAGCGCCCGGCCTGTGTGAAGAAAGACTACTCCAAC
TTCATGGCATCCCTGAATCTGCGCAACCGCTACGCGGGCGAGGTGTATGGAATGATTCGG
TTCTCAGGCACCACAGGCCAGATGTCTGACCTGAACAAAATGATGGTCCAGGATCTACAT
TCAGCTTTAGACCGCAGTCATCCTCAGCACTACACGCAGGCCATGTTCAAGCTGACCGCA
ATGCTCATTAGCAGTAAAGATTGTGACCCGCAGCTCCTTCATCATCTGTGCTGGGGTCCC
CTCCGGATGTTCAATGAGCATGGCATGGAGACGGCCCTGGCCTGCTGGGAGTGGCTGCTG
GCTGGCAAGGATGGAGTGGAAGTGCCGTTCATGCGGGAGATGGCAGGGGCCTGGCACATG
ACGGTGGAGCAGAAATTTGGCCTGTTTTCTGCTGAGATAAAGGAAGCAGACCCCCTGGCT
GCCTCGGAAGCAAGTCAACCCAAACCCTGTCCCCCCGAAGTGACCCCCCACTACATCTGG
ATCGACTTCCTGGTGCAGCGGTTTGAGATCGCCAAGTACTGCAGCTCTGACCAAGTGGAG
ATCTTCTCCAGCCTGCTGCAGCGCTCCATGTCCCTGAACATCGGCGGGGCCAAGGGGAGC
ATGAACCGGCACGTGGCGGCCATCGGGCCCCGCTTCAAGCTGCTGACCCTGGGGCTGTCC
CTCCTGCATGCCGATGTGGTTCCAAATGCAACCATCCGCAATGTGCTTCGCGAGAAGATC
TACTCCACTGCCTTTGACTACTTCAGCTGTCCCCCAAAGTTCCCTACTCAAGGAGAGAAG
CGGCTGCGTGAAGACATAAGCATCATGATTAAATTTTGGACCGCCATGTTCTCAGATAAG
AAGTACCTGACCGCCAGCCAGCTTGTTCCCCCAGATAATCAGGACACCCGGAGCAACCTG
GACATAACTGTCGGCTCTCGGCAACAAGCCACCCAAGGCTGGATCAACACATACCCCCTG
TCCAGCGGCATGTCCACCATCTCCAAGAAATCAGGCATGTCTAAGAAAACCAACCGGGGC
TCCCAGCTGCACAAATACTACATGAAGCGCAGGACGCTGCTGCTGTCCCTGCTGGCCACT
GAGATCGAGCGTCTCATCACATGGTACAACCCGCTGTCAGCCCCGGAACTGGAACTAGAC
CAGGCCGGAGAGAACAGCGTGGCCAACTGGAGATCTAAGTACATCAGCCTGAGTGAGAAG
CAGTGGAAGGACAACGTGAACCTCGCCTGGAGCATCTCTCCCTACCTAGCCGTGCAGCTG
CCTGCCAGGTTTAAGAACACAGAAGCCATTGGGAACGAAGTGACCCGTCTCGTTCGGTTG
GACCCGGGAGCCGTTAGTGATGTGCCTGAAGCAATCAAGTTCCTGGTCACCTGGCACACC
ATCGACGCCGATGCTCCAGAGCTCAGCCATGTGCTGTGCTGGGCGCCCACGGACCCACCC
ACAGGCCTCTCCTACTTCTCCAGCATGTACCCGCCGCACCCTCTCACGGCGCAGTACGGG
GTGAAAGTCCTGCGGTCCTTCCCTCCGGACGCCATCCTCTTCTACATCCCCCAGATTGTG
CAGGCCCTCAGGTACGACAAGATGGGCTATGTGCGGGAGTATATTCTGTGGGCAGCGTCT
AAATCCCAGCTTCTGGCACACCAGTTCATCTGGAACATGAAGACTAACATTTATCTAGAT
GAAGAGGGCCACCAGAAAGACCCTGACATCGGCGACCTCCTGGATCAGTTGGTAGAGGAG
ATCACAGGCTCCTTGTCCGGCCCAGCGAAGGACTTTTACCAGCGGGAGTTTGATTTCTTT
AACAAGATCACCAACGTGTCGGCTATCATCAAGCCCTACCCTAAAGGCGACGAGAGAAAG
AAGGCTTGTCTGTCGGCCCTGTCTGAAGTGAAGGTGCAGCCGGGCTGCTACCTGCCCAGC
AACCCTGAGGCCATTGTGCTGGACATCGACTACAAGTCTGGGACCCCGATGCAGAGTGCT
GCAAAAGCCCCATATCTGGCCAAGTTCAAGGTGAAGCGATGTGGAGTTAGTGAACTTGAA
AAAGAAGGTCTGCGGTGCCGCTCAGACTCCGAGGATGAGTGCAGCACGCAGGAGGCCGAC
GGCCAGAAGATCTCCTGGCAGGCAGCCATCTTCAAGGTGGGAGACGACTGCCGGCAGGAC
ATGCTGGCCCTGCAGATCATCGACCTCTTCAAGAACATCTTCCAGCTGGTCGGCCTGGAC
CTCTTTGTTTTTCCCTACCGCGTGGTGGCCACTGCCCCTGGGTGCGGGGTGATCGAGTGC
ATCCCCGACTGCACCTCCCGGGACCAGCTGGGCCGCCAGACAGACTTCGGCATGTACGAC
TACTTCACACGCCAGTACGGGGATGAGTCCACTCTGGCCTTCCAGCAGGCCCGCTACAAC
TTCATCCGAAGCATGGCCGCCTACAGCCTCCTGCTGTTCCTGCTGCAGATCAAGGACAGA
CACAACGGCAACATTATGCTGGACAAGAAGGGTCATATCATCCACATCGACTTTGGCTTC
ATGTTTGAAAGCTCGCCGGGCGGCAATCTCGGCTGGGAACCCGACATCAAGCTGACGGAT
GAGATGGTGATGATCATGGGGGGCAAGATGGAGGCCACACCCTTCAAGTGGTTCATGGAG
ATGTGTGTCCGAGGCTACCTGGCTGTGCGGCCCTACATGGACGCGGTCGTCTCCCTGGTC
ACTCTCATGTTGGACACGGGCCTGCCCTGTTTTCGCGGCCAGACAATCAAGCTCTTGAAG
CACAGGTTTAGCCCCAACATGACTGAGCGCGAGGCTGCAAATTTCATCATGAAGGTCATC
CAGAGCTGCTTCCTCAGCAACAGGAGCCGGACCTACGACATGATCCAGTACTATCAGAAT
GACATCCCCTACTGA
|
| Enzyme 12 GenBank Gene ID |
NM_058004.2  |
| Enzyme 12 GeneCard ID |
PI4KA  |
| Enzyme 12 GenAtlas ID |
PI4KA  |
| Enzyme 12 HGNC ID |
HGNC:8983  |
| Enzyme 12 Chromosome Location |
2 |
| Enzyme 12 Locus |
22q11.21 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Wong K, Cantley LC: Cloning and characterization of a human phosphatidylinositol 4-kinase. J Biol Chem. 1994 Nov 18;269(46):28878-84. [PubMed
]
- Gehrmann T, Gulkan H, Suer S, Herberg FW, Balla A, Vereb G, Mayr GW, Heilmeyer LM Jr: Functional expression and characterisation of a new human phosphatidylinositol 4-kinase PI4K230. Biochim Biophys Acta. 1999 Mar 25;1437(3):341-56. [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
]
- 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
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6865 |
| Enzyme 13 Name |
Inositol polyphosphate 5-phosphatase OCRL-1 |
| Enzyme 13 Synonyms |
- Lowe oculocerebrorenal syndrome protein
|
| Enzyme 13 Gene Name |
OCRL |
| Enzyme 13 Protein Sequence |
>Inositol polyphosphate 5-phosphatase OCRL-1
MEPPLPVGAQPLATVEGMEMKGPLREPCALTLAQRNGQYELIIQLHEKEQHVQDIIPINS
HFRCVQEAEETLLIDIASNSGCKIRVQGDWIRERRFEIPDEEHCLKFLSAVLAAQKAQSQ
LLVPEQKDSSSWYQKLDTKDKPSVFSGLLGFEDNFSSMNLDKKINSQNQPTGIHREPPPP
PFSVNKMLPREKEASNKEQPKVTNTMRKLFVPNTQSGQREGLIKHILAKREKEYVNIQTF
RFFVGTWNVNGQSPDSGLEPWLNCDPNPPDIYCIGFQELDLSTEAFFYFESVKEQEWSMA
VERGLHSKAKYKKVQLVRLVGMMLLIFARKDQCRYIRDIATETVGTGIMGKMGNKGGVAV
RFVFHNTTFCIVNSHLAAHVEDFERRNQDYKDICARMSFVVPNQTLPQLNIMKHEVVIWL
GDLNYRLCMPDANEVKSLINKKDLQRLLKFDQLNIQRTQKKAFVDFNEGEIKFIPTYKYD
SKTDRWDSSGKCRVPAWCDRILWRGTNVNQLNYRSHMELKTSDHKPVSALFHIGVKVVDE
RRYRKVFEDSVRIMDRMENDFLPSLELSRREFVFENVKFRQLQKEKFQISNNGQVPCHFS
FIPKLNDSQYCKPWLRAEPFEGYLEPNETVDISLDVYVSKDSVTILNSGEDKIEDILVLH
LDRGKDYFLTISGNYLPSCFGTSLEALCRMKRPIREVPVTKLIDLEEDSFLEKEKSLLQM
VPLDEGASERPLQVPKEIWLLVDHLFKYACHQEDLFQTPGMQEELQQIIDCLDTSIPETI
PGSNHSVAEALLIFLEALPEPVICYELYQRCLDSAYDPRICRQVISQLPRCHRNVFRYLM
AFLRELLKFSEYNSVNANMIATLFTSLLLRPPPNLMARQTPSDRQRAIQFLLGFLLGSEE
D
|
| Enzyme 13 Number of Residues |
901 |
| Enzyme 13 Molecular Weight |
104203.8 |
| Enzyme 13 Theoretical pI |
6.51 |
| Enzyme 13 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
- biological regulation
- regulation of biological process
- regulation of cellular process
- signal transduction
|
| Component |
|
|
| Enzyme 13 General Function |
Involved in inositol or phosphatidylinositol phosphatase activity |
| Enzyme 13 Specific Function |
Converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate. Also converts inositol 1,4,5- trisphosphate to inositol 1,4-bisphosphate and inositol 1,3,4,5- tetrakisphosphate to inositol 1,3,4-trisphosphate. May function in lysosomal membrane trafficking by regulating the specific pool of phosphatidylinositol 4,5-bisphosphate that is associated with lysosomes |
| Enzyme 13 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 13 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate [RN:R04404]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
66347006  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q01968  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
OCRL_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>2706 bp
ATGGAGCCGCCGCTCCCGGTCGGAGCCCAGCCGCTTGCCACTGTCGAGGGTATGGAGATG
AAGGGTCCTCTCCGGGAGCCCTGCGCCCTGACCCTAGCCCAGAGGAACGGGCAATATGAG
TTAATAATCCAGTTGCATGAGAAGGAACAGCATGTTCAAGATATCATTCCTATAAATAGC
CACTTCAGATGTGTTCAAGAAGCAGAAGAAACTCTTTTGATTGACATAGCTTCTAACAGT
GGCTGCAAAATTCGGGTTCAGGGGGACTGGATCAGAGAGCGCCGCTTTGAAATCCCTGAT
GAGGAACACTGTTTGAAGTTCCTCTCAGCTGTCCTTGCTGCTCAGAAAGCTCAGTCACAG
CTTCTTGTTCCAGAGCAAAAGGACTCATCTAGCTGGTACCAGAAATTAGACACTAAGGAC
AAACCTTCTGTTTTTTCAGGGCTTCTTGGATTTGAAGACAATTTTTCTTCTATGAATTTG
GACAAGAAAATAAATTCACAAAATCAGCCTACTGGGATTCATCGGGAACCCCCACCTCCA
CCCTTTTCAGTGAATAAAATGCTTCCACGTGAAAAAGAAGCTTCTAACAAGGAGCAGCCC
AAAGTGACCAACACCATGCGGAAGCTCTTTGTACCAAATACCCAATCTGGGCAGCGGGAG
GGTCTCATCAAACATATCCTGGCAAAGCGAGAGAAAGAATATGTCAACATTCAGACTTTC
AGATTTTTTGTTGGAACTTGGAATGTGAATGGCCAGTCTCCAGATAGCGGGTTAGAACCT
TGGCTGAACTGTGATCCCAATCCTCCTGATATCTACTGCATTGGATTCCAAGAACTGGAC
TTGAGCACAGAAGCCTTCTTCTACTTTGAATCTGTGAAGGAACAAGAATGGTCCATGGCT
GTAGAGAGAGGTTTGCATTCCAAAGCCAAGTATAAGAAAGTTCAACTGGTGCGCCTTGTT
GGGATGATGCTTCTTATATTTGCCAGAAAGGATCAGTGTCGATACATTCGTGATATTGCT
ACAGAAACAGTTGGAACTGGAATCATGGGGAAAATGGGAAACAAAGGTGGGGTAGCTGTG
AGATTTGTATTTCACAACACCACCTTTTGCATTGTCAATTCCCATCTGGCTGCACACGTG
GAGGACTTTGAGAGAAGGAATCAAGATTATAAGGACATTTGTGCGAGAATGAGTTTTGTG
GTCCCAAATCAGACCCTCCCGCAGTTGAACATCATGAAACATGAGGTTGTCATTTGGTTG
GGAGATTTGAATTATAGACTTTGCATGCCTGATGCCAATGAGGTGAAAAGTCTTATTAAT
AAGAAAGACCTTCAGAGACTCTTGAAATTCGACCAGCTAAATATTCAGCGCACACAGAAA
AAAGCTTTTGTTGACTTCAATGAAGGGGAAATCAAGTTCATCCCCACTTATAAGTATGAC
TCTAAAACAGACCGGTGGGATTCCAGTGGGAAATGCCGGGTTCCAGCCTGGTGTGACCGA
ATTCTTTGGAGAGGAACAAATGTTAATCAGCTTAATTATCGGAGTCACATGGAACTGAAA
ACCAGCGACCACAAGCCTGTTAGCGCCCTCTTCCATATTGGGGTGAAGGTTGTGGATGAA
CGAAGGTACCGGAAAGTCTTTGAAGATAGTGTACGCATCATGGACAGAATGGAAAATGAC
TTCCTTCCTTCCTTAGAACTCAGCAGGAGGGAGTTTGTGTTTGAAAATGTGAAGTTTCGG
CAACTACAAAAGGAGAAGTTCCAGATCAGCAACAATGGACAGGTTCCCTGCCATTTTTCT
TTCATCCCTAAACTTAATGACAGCCAGTACTGCAAGCCATGGCTTCGGGCTGAACCTTTT
GAGGGCTACTTGGAGCCAAATGAGACAGTGGACATTTCTCTTGATGTGTATGTCAGCAAA
GACTCTGTAACCATCCTGAACTCGGGAGAAGATAAGATTGAAGATATTCTCGTCCTTCAC
CTGGATCGAGGCAAAGATTACTTCTTGACTATCAGTGGAAATTACCTCCCAAGTTGTTTT
GGCACATCCTTAGAGGCTCTGTGCCGTATGAAAAGACCAATCCGAGAAGTTCCTGTTACC
AAACTCATAGACTTGGAAGAAGACAGCTTCCTAGAAAAGGAGAAATCCCTTCTGCAAATG
GTTCCTTTGGATGAAGGTGCCAGTGAGAGACCCCTTCAGGTTCCCAAGGAGATCTGGCTT
CTAGTAGATCACCTATTCAAATACGCCTGTCACCAGGAGGACCTGTTCCAGACCCCTGGA
ATGCAGGAAGAGCTCCAGCAGATCATTGATTGTCTGGATACCAGCATTCCTGAGACAATC
CCTGGCAGCAACCACTCTGTGGCTGAAGCACTGCTCATTTTCTTGGAAGCCCTGCCAGAG
CCAGTCATCTGTTACGAGCTGTATCAGCGATGTCTTGACTCTGCTTATGATCCCCGGATC
TGCCGACAGGTGATCTCCCAGCTTCCGAGATGCCATAGAAATGTTTTCCGTTACTTGATG
GCATTCCTTCGAGAACTCTTAAAATTCTCTGAATACAATAGCGTCAATGCCAACATGATC
GCTACTCTCTTCACTAGTCTTCTCCTGAGGCCTCCACCCAACCTTATGGCAAGACAGACT
CCAAGTGACCGCCAGCGTGCTATTCAGTTCCTTCTGGGCTTTCTGCTTGGGAGCGAAGAA
GACTAA
|
| Enzyme 13 GenBank Gene ID |
AL022162  |
| Enzyme 13 GeneCard ID |
OCRL  |
| Enzyme 13 GenAtlas ID |
OCRL  |
| Enzyme 13 HGNC ID |
HGNC:8108  |
| Enzyme 13 Chromosome Location |
Not Available |
| Enzyme 13 Locus |
Not Available |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Attree O, Olivos IM, Okabe I, Bailey LC, Nelson DL, Lewis RA, McInnes RR, Nussbaum RL: The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase. Nature. 1992 Jul 16;358(6383):239-42. [PubMed
]
- Nussbaum RL, Orrison BM, Janne PA, Charnas L, Chinault AC: Physical mapping and genomic structure of the Lowe syndrome gene OCRL1. Hum Genet. 1997 Feb;99(2):145-50. [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
]
- Leahey AM, Charnas LR, Nussbaum RL: Nonsense mutations in the OCRL-1 gene in patients with the oculocerebrorenal syndrome of Lowe. Hum Mol Genet. 1993 Apr;2(4):461-3. [PubMed
]
- Zhang X, Jefferson AB, Auethavekiat V, Majerus PW: The protein deficient in Lowe syndrome is a phosphatidylinositol-4,5-bisphosphate 5-phosphatase. Proc Natl Acad Sci U S A. 1995 May 23;92(11):4853-6. [PubMed
]
- Zhang X, Hartz PA, Philip E, Racusen LC, Majerus PW: Cell lines from kidney proximal tubules of a patient with Lowe syndrome lack OCRL inositol polyphosphate 5-phosphatase and accumulate phosphatidylinositol 4,5-bisphosphate. J Biol Chem. 1998 Jan 16;273(3):1574-82. [PubMed
]
- Lin T, Orrison BM, Leahey AM, Suchy SF, Bernard DJ, Lewis RA, Nussbaum RL: Spectrum of mutations in the OCRL1 gene in the Lowe oculocerebrorenal syndrome. Am J Hum Genet. 1997 Jun;60(6):1384-8. [PubMed
]
- Lin T, Orrison BM, Suchy SF, Lewis RA, Nussbaum RL: Mutations are not uniformly distributed throughout the OCRL1 gene in Lowe syndrome patients. Mol Genet Metab. 1998 May;64(1):58-61. [PubMed
]
- Kawano T, Indo Y, Nakazato H, Shimadzu M, Matsuda I: Oculocerebrorenal syndrome of Lowe: three mutations in the OCRL1 gene derived from three patients with different phenotypes. Am J Med Genet. 1998 Jun 5;77(5):348-55. [PubMed
]
- Kubota T, Sakurai A, Arakawa K, Shimazu M, Wakui K, Furihata K, Fukushima Y: Identification of two novel mutations in the OCRL1 gene in Japanese families with Lowe syndrome. Clin Genet. 1998 Sep;54(3):199-202. [PubMed
]
- Monnier N, Satre V, Lerouge E, Berthoin F, Lunardi J: OCRL1 mutation analysis in French Lowe syndrome patients: implications for molecular diagnosis strategy and genetic counseling. Hum Mutat. 2000;16(2):157-65. [PubMed
]
- Roschinger W, Muntau AC, Rudolph G, Roscher AA, Kammerer S: Carrier assessment in families with lowe oculocerebrorenal syndrome: novel mutations in the OCRL1 gene and correlation of direct DNA diagnosis with ocular examination. Mol Genet Metab. 2000 Mar;69(3):213-22. [PubMed
]
- Hoopes RR Jr, Shrimpton AE, Knohl SJ, Hueber P, Hoppe B, Matyus J, Simckes A, Tasic V, Toenshoff B, Suchy SF, Nussbaum RL, Scheinman SJ: Dent Disease with mutations in OCRL1. Am J Hum Genet. 2005 Feb;76(2):260-7. Epub 2004 Dec 30. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
6866 |
| Enzyme 14 Name |
Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN |
| Enzyme 14 Synonyms |
- Mutated in multiple advanced cancers 1
- Phosphatase and tensin homolog
|
| Enzyme 14 Gene Name |
PTEN |
| Enzyme 14 Protein Sequence |
>Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSK
HKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVA
AIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSY
LLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMY
FEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEI
DSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEAS
SSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV
|
| Enzyme 14 Number of Residues |
403 |
| Enzyme 14 Molecular Weight |
47165.9 |
| Enzyme 14 Theoretical pI |
6.33 |
| Enzyme 14 GO Classification |
| Function |
- PDZ domain binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- ion binding
- magnesium ion binding
- metal ion binding
- phosphatase activity
- phosphatidylinositol bisphosphate phosphatase activity
- phosphatidylinositol trisphosphate phosphatase activity
- phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity
- phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity
- phosphoprotein phosphatase activity
- phosphoric ester hydrolase activity
- protein binding
- protein domain specific binding
- protein tyrosine phosphatase activity
- protein tyrosine/serine/threonine phosphatase activity
|
| Process |
- alcohol metabolic process
- biological regulation
- cellular metabolic process
- dephosphorylation
- glycerophospholipid metabolic process
- inositol metabolic process
- inositol phosphate dephosphorylation
- metabolic process
- negative regulation of cell migration
- negative regulation of cell proliferation
- negative regulation of cell-matrix adhesion
- negative regulation of focal adhesion assembly
- negative regulation of intracellular protein kinase cascade
- negative regulation of protein kinase B signaling cascade
- negative regulation of signal transduction
- organophosphate metabolic process
- phosphate metabolic process
- phosphoinositide dephosphorylation
- phosphoinositide metabolic process
- phospholipid metabolic process
- phosphorus metabolic process
- polyol metabolic process
- posttranscriptional regulation of gene expression
- protein amino acid dephosphorylation
- regulation of biological process
- regulation of cell adhesion
- regulation of cell communication
- regulation of cell migration
- regulation of cell motility
- regulation of cell proliferation
- regulation of cell-matrix adhesion
- regulation of cell-substrate adhesion
- regulation of cellular process
- regulation of gene expression
- regulation of locomotion
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein stability
- regulation of signal transduction
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Involved in magnesium ion binding |
| Enzyme 14 Specific Function |
Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine- phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3- phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K- AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability |
| Enzyme 14 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 14 Reactions |
- phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate [RN:R04513]
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
Not Available |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P60484  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
PTEN_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>1212 bp
ATGACAGCCATCATCAAAGAGATCGTTAGCAGAAACAAAAGGAGATATCAAGAGGATGGA
TTCGACTTAGACTTGACCTATATTTATCCAAACATTATTGCTATGGGATTTCCTGCAGAA
AGACTTGAAGGCGTATACAGGAACAATATTGATGATGTAGTAAGGTTTTTGGATTCAAAG
CATAAAAACCATTACAAGATATACAATCTTTGTGCTGAAAGACATTATGACACCGCCAAA
TTTAATTGCAGAGTTGCACAATATCCTTTTGAAGACCATAACCCACCACAGCTAGAACTT
ATCAAACCCTTTTGTGAAGATCTTGACCAATGGCTAAGTGAAGATGACAATCATGTTGCA
GCAATTCACTGTAAAGCTGGAAAGGGACGAACTGGTGTAATGATATGTGCATATTTATTA
CATCGGGGCAAATTTTTAAAGGCACAAGAGGCCCTAGATTTCTATGGGGAAGTAAGGACC
AGAGACAAAAAGGGAGTAACTATTCCCAGTCAGAGGCGCTATGTGTATTATTATAGCTAC
CTGTTAAAGAATCATCTGGATTATAGACCAGTGGCACTGTTGTTTCACAAGATGATGTTT
GAAACTATTCCAATGTTCAGTGGCGGAACTTGCAATCCTCAGTTTGTGGTCTGCCAGCTA
AAGGTGAAGATATATTCCTCCAATTCAGGACCCACACGACGGGAAGACAAGTTCATGTAC
TTTGAGTTCCCTCAGCCGTTACCTGTGTGTGGTGATATCAAAGTAGAGTTCTTCCACAAA
CAGAACAAGATGCTAAAAAAGGACAAAATGTTTCACTTTTGGGTAAATACATTCTTCATA
CCAGGACCAGAGGAAACCTCAGAAAAAGTAGAAAATGGAAGTCTATGTGATCAAGAAATC
GATAGCATTTGCAGTATAGAGCGTGCAGATAATGACAAGGAATATCTAGTACTTACTTTA
ACAAAAAATGATCTTGACAAAGCAAATAAAGACAAAGCCAACCGATACTTTTCTCCAAAT
TTTAAGGTGAAGCTGTACTTCACAAAAACAGTAGAGGAGCCGTCAAATCCAGAGGCTAGC
AGTTCAACTTCTGTAACACCAGATGTTAGTGACAATGAACCTGATCATTATAGATATTCT
GACACCACTGACTCTGATCCAGAGAATGAACCTTTTGATGAAGATCAGCATACACAAATT
ACAAAAGTCTGA
|
| Enzyme 14 GenBank Gene ID |
U96180  |
| Enzyme 14 GeneCard ID |
PTEN  |
| Enzyme 14 GenAtlas ID |
PTEN  |
| Enzyme 14 HGNC ID |
HGNC:9588  |
| Enzyme 14 Chromosome Location |
1 |
| Enzyme 14 Locus |
10q23.3 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Li DM, Sun H: TEP1, encoded by a candidate tumor suppressor locus, is a novel protein tyrosine phosphatase regulated by transforming growth factor beta. Cancer Res. 1997 Jun 1;57(11):2124-9. [PubMed
]
- Steck PA, Pershouse MA, Jasser SA, Yung WK, Lin H, Ligon AH, Langford LA, Baumgard ML, Hattier T, Davis T, Frye C, Hu R, Swedlund B, Teng DH, Tavtigian SV: Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers. Nat Genet. 1997 Apr;15(4):356-62. [PubMed
]
- Li J, Yen C, Liaw D, Podsypanina K, Bose S, Wang SI, Puc J, Miliaresis C, Rodgers L, McCombie R, Bigner SH, Giovanella BC, Ittmann M, Tycko B, Hibshoosh H, Wigler MH, Parsons R: PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science. 1997 Mar 28;275(5308):1943-7. [PubMed
]
- Hamilton JA, Stewart LM, Ajayi L, Gray IC, Gray NE, Roberts KG, Watson GJ, Kaisary AV, Snary D: The expression profile for the tumour suppressor gene PTEN and associated polymorphic markers. Br J Cancer. 2000 May;82(10):1671-6. [PubMed
]
- 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
]
- Myers MP, Stolarov JP, Eng C, Li J, Wang SI, Wigler MH, Parsons R, Tonks NK: P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase. Proc Natl Acad Sci U S A. 1997 Aug 19;94(17):9052-7. [PubMed
]
- Maehama T, Dixon JE: The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem. 1998 May 29;273(22):13375-8. [PubMed
]
- Myers MP, Pass I, Batty IH, Van der Kaay J, Stolarov JP, Hemmings BA, Wigler MH, Downes CP, Tonks NK: The lipid phosphatase activity of PTEN is critical for its tumor supressor function. Proc Natl Acad Sci U S A. 1998 Nov 10;95(23):13513-8. [PubMed
]
- Tamura M, Gu J, Matsumoto K, Aota S, Parsons R, Yamada KM: Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN. Science. 1998 Jun 5;280(5369):1614-7. [PubMed
]
- Georgescu MM, Kirsch KH, Akagi T, Shishido T, Hanafusa H: The tumor-suppressor activity of PTEN is regulated by its carboxyl-terminal region. Proc Natl Acad Sci U S A. 1999 Aug 31;96(18):10182-7. [PubMed
]
- Adey NB, Huang L, Ormonde PA, Baumgard ML, Pero R, Byreddy DV, Tavtigian SV, Bartel PL: Threonine phosphorylation of the MMAC1/PTEN PDZ binding domain both inhibits and stimulates PDZ binding. Cancer Res. 2000 Jan 1;60(1):35-7. [PubMed
]
- Wu Y, Dowbenko D, Spencer S, Laura R, Lee J, Gu Q, Lasky LA: Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase. J Biol Chem. 2000 Jul 14;275(28):21477-85. [PubMed
]
- Wu X, Hepner K, Castelino-Prabhu S, Do D, Kaye MB, Yuan XJ, Wood J, Ross C, Sawyers CL, Whang YE: Evidence for regulation of the PTEN tumor suppressor by a membrane-localized multi-PDZ domain containing scaffold protein MAGI-2. Proc Natl Acad Sci U S A. 2000 Apr 11;97(8):4233-8. [PubMed
]
- Vazquez F, Grossman SR, Takahashi Y, Rokas MV, Nakamura N, Sellers WR: Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex. J Biol Chem. 2001 Dec 28;276(52):48627-30. Epub 2001 Nov 13. [PubMed
]
- Miller SJ, Lou DY, Seldin DC, Lane WS, Neel BG: Direct identification of PTEN phosphorylation sites. FEBS Lett. 2002 Sep 25;528(1-3):145-53. [PubMed
]
- Valiente M, Andres-Pons A, Gomar B, Torres J, Gil A, Tapparel C, Antonarakis SE, Pulido R: Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases. J Biol Chem. 2005 Aug 12;280(32):28936-43. Epub 2005 Jun 10. [PubMed
]
- Wang X, Trotman LC, Koppie T, Alimonti A, Chen Z, Gao Z, Wang J, Erdjument-Bromage H, Tempst P, Cordon-Cardo C, Pandolfi PP, Jiang X: NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN. Cell. 2007 Jan 12;128(1):129-39. [PubMed
]
- Song MS, Salmena L, Carracedo A, Egia A, Lo-Coco F, Teruya-Feldstein J, Pandolfi PP: The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network. Nature. 2008 Oct 9;455(7214):813-7. Epub 2008 Aug 20. [PubMed
]
- Yim EK, Peng G, Dai H, Hu R, Li K, Lu Y, Mills GB, Meric-Bernstam F, Hennessy BT, Craven RJ, Lin SY: Rak functions as a tumor suppressor by regulating PTEN protein stability and function. Cancer Cell. 2009 Apr 7;15(4):304-14. [PubMed
]
- 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
]
- Mund T, Pelham HR: Regulation of PTEN/Akt and MAP kinase signaling pathways by the ubiquitin ligase activators Ndfip1 and Ndfip2. Proc Natl Acad Sci U S A. 2010 Jun 22;107(25):11429-34. Epub 2010 Jun 7. [PubMed
]
- Lee JO, Yang H, Georgescu MM, Di Cristofano A, Maehama T, Shi Y, Dixon JE, Pandolfi P, Pavletich NP: Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Cell. 1999 Oct 29;99(3):323-34. [PubMed
]
- Tsou HC, Teng DH, Ping XL, Brancolini V, Davis T, Hu R, Xie XX, Gruener AC, Schrager CA, Christiano AM, Eng C, Steck P, Ott J, Tavtigian SV, Peacocke M: The role of MMAC1 mutations in early-onset breast cancer: causative in association with Cowden syndrome and excluded in BRCA1-negative cases. Am J Hum Genet. 1997 Nov;61(5):1036-43. [PubMed
]
- Lynch ED, Ostermeyer EA, Lee MK, Arena JF, Ji H, Dann J, Swisshelm K, Suchard D, MacLeod PM, Kvinnsland S, Gjertsen BT, Heimdal K, Lubs H, Moller P, King MC: Inherited mutations in PTEN that are associated with breast cancer, cowden disease, and juvenile polyposis. Am J Hum Genet. 1997 Dec;61(6):1254-60. [PubMed
]
- Wang SI, Puc J, Li J, Bruce JN, Cairns P, Sidransky D, Parsons R: Somatic mutations of PTEN in glioblastoma multiforme. Cancer Res. 1997 Oct 1;57(19):4183-6. [PubMed
]
- Nelen MR, van Staveren WC, Peeters EA, Hassel MB, Gorlin RJ, Hamm H, Lindboe CF, Fryns JP, Sijmons RH, Woods DG, Mariman EC, Padberg GW, Kremer H: Germline mutations in the PTEN/MMAC1 gene in patients with Cowden disease. Hum Mol Genet. 1997 Aug;6(8):1383-7. [PubMed
]
- Liaw D, Marsh DJ, Li J, Dahia PL, Wang SI, Zheng Z, Bose S, Call KM, Tsou HC, Peacocke M, Eng C, Parsons R: Germline mutations of the PTEN gene in Cowden disease, an inherited breast and thyroid cancer syndrome. Nat Genet. 1997 May;16(1):64-7. [PubMed
]
- Marsh DJ, Dahia PL, Zheng Z, Liaw D, Parsons R, Gorlin RJ, Eng C: Germline mutations in PTEN are present in Bannayan-Zonana syndrome. Nat Genet. 1997 Aug;16(4):333-4. [PubMed
]
- Maxwell GL, Risinger JI, Gumbs C, Shaw H, Bentley RC, Barrett JC, Berchuck A, Futreal PA: Mutation of the PTEN tumor suppressor gene in endometrial hyperplasias. Cancer Res. 1998 Jun 15;58(12):2500-3. [PubMed
]
- Chi SG, Kim HJ, Park BJ, Min HJ, Park JH, Kim YW, Dong SH, Kim BH, Lee JI, Chang YW, Chang R, Kim WK, Yang MH: Mutational abrogation of the PTEN/MMAC1 gene in gastrointestinal polyps in patients with Cowden disease. Gastroenterology. 1998 Nov;115(5):1084-9. [PubMed
]
- Tsou HC, Ping XL, Xie XX, Gruener AC, Zhang H, Nini R, Swisshelm K, Sybert V, Diamond TM, Sutphen R, Peacocke M: The genetic basis of Cowden's syndrome: three novel mutations in PTEN/MMAC1/TEP1. Hum Genet. 1998 Apr;102(4):467-73. [PubMed
]
- Marsh DJ, Coulon V, Lunetta KL, Rocca-Serra P, Dahia PL, Zheng Z, Liaw D, Caron S, Duboue B, Lin AY, Richardson AL, Bonnetblanc JM, Bressieux JM, Cabarrot-Moreau A, Chompret A, Demange L, Eeles RA, Yahanda AM, Fearon ER, Fricker JP, Gorlin RJ, Hodgson SV, Huson S, Lacombe D, Eng C, et al.: Mutation spectrum and genotype-phenotype analyses in Cowden disease and Bannayan-Zonana syndrome, two hamartoma syndromes with germline PTEN mutation. Hum Mol Genet. 1998 Mar;7(3):507-15. [PubMed
]
- Scala S, Bruni P, Lo Muzio L, Mignogna M, Viglietto G, Fusco A: Novel mutation of the PTEN gene in an Italian Cowden's disease kindred. Int J Oncol. 1998 Oct;13(4):665-8. [PubMed
]
- Marsh DJ, Dahia PL, Caron S, Kum JB, Frayling IM, Tomlinson IP, Hughes KS, Eeles RA, Hodgson SV, Murday VA, Houlston R, Eng C: Germline PTEN mutations in Cowden syndrome-like families. J Med Genet. 1998 Nov;35(11):881-5. [PubMed
]
- Olschwang S, Serova-Sinilnikova OM, Lenoir GM, Thomas G: PTEN germ-line mutations in juvenile polyposis coli. Nat Genet. 1998 Jan;18(1):12-4. [PubMed
]
- Kurose K, Araki T, Matsunaka T, Takada Y, Emi M: Variant manifestation of Cowden disease in Japan: hamartomatous polyposis of the digestive tract with mutation of the PTEN gene. Am J Hum Genet. 1999 Jan;64(1):308-10. [PubMed
]
- Sutphen R, Diamond TM, Minton SE, Peacocke M, Tsou HC, Root AW: Severe Lhermitte-Duclos disease with unique germline mutation of PTEN. Am J Med Genet. 1999 Feb 12;82(4):290-3. [PubMed
]
- Nelen MR, Kremer H, Konings IB, Schoute F, van Essen AJ, Koch R, Woods CG, Fryns JP, Hamel B, Hoefsloot LH, Peeters EA, Padberg GW: Novel PTEN mutations in patients with Cowden disease: absence of clear genotype-phenotype correlations. Eur J Hum Genet. 1999 Apr;7(3):267-73. [PubMed
]
- Marsh DJ, Kum JB, Lunetta KL, Bennett MJ, Gorlin RJ, Ahmed SF, Bodurtha J, Crowe C, Curtis MA, Dasouki M, Dunn T, Feit H, Geraghty MT, Graham JM Jr, Hodgson SV, Hunter A, Korf BR, Manchester D, Miesfeldt S, Murday VA, Nathanson KL, Parisi M, Pober B, Romano C, Eng C, et al.: PTEN mutation spectrum and genotype-phenotype correlations in Bannayan-Riley-Ruvalcaba syndrome suggest a single entity with Cowden syndrome. Hum Mol Genet. 1999 Aug;8(8):1461-72. [PubMed
]
- Han SY, Kato H, Kato S, Suzuki T, Shibata H, Ishii S, Shiiba K, Matsuno S, Kanamaru R, Ishioka C: Functional evaluation of PTEN missense mutations using in vitro phosphoinositide phosphatase assay. Cancer Res. 2000 Jun 15;60(12):3147-51. [PubMed
]
- De Vivo I, Gertig DM, Nagase S, Hankinson SE, O'Brien R, Speizer FE, Parsons R, Hunter DJ: Novel germline mutations in the PTEN tumour suppressor gene found in women with multiple cancers. J Med Genet. 2000 May;37(5):336-41. [PubMed
]
- Celebi JT, Shendrik I, Silvers DN, Peacocke M: Identification of PTEN mutations in metastatic melanoma specimens. J Med Genet. 2000 Sep;37(9):653-7. [PubMed
]
- Weng LP, Brown JL, Eng C: PTEN coordinates G(1) arrest by down-regulating cyclin D1 via its protein phosphatase activity and up-regulating p27 via its lipid phosphatase activity in a breast cancer model. Hum Mol Genet. 2001 Mar 15;10(6):599-604. [PubMed
]
- Reardon W, Zhou XP, Eng C: A novel germline mutation of the PTEN gene in a patient with macrocephaly, ventricular dilatation, and features of VATER association. J Med Genet. 2001 Dec;38(12):820-3. [PubMed
]
- Marsh DJ, Theodosopoulos G, Howell V, Richardson AL, Benn DE, Proos AL, Eng C, Robinson BG: Rapid mutation scanning of genes associated with familial cancer syndromes using denaturing high-performance liquid chromatography. Neoplasia. 2001 May-Jun;3(3):236-44. [PubMed
]
- Staal FJ, van der Luijt RB, Baert MR, van Drunen J, van Bakel H, Peters E, de Valk I, van Amstel HK, Taphoorn MJ, Jansen GH, van Veelen CW, Burgering B, Staal GE: A novel germline mutation of PTEN associated with brain tumours of multiple lineages. Br J Cancer. 2002 May 20;86(10):1586-91. [PubMed
]
- Poetsch M, Lorenz G, Kleist B: Detection of new PTEN/MMAC1 mutations in head and neck squamous cell carcinomas with loss of chromosome 10. Cancer Genet Cytogenet. 2002 Jan 1;132(1):20-4. [PubMed
]
- Smith JM, Kirk EP, Theodosopoulos G, Marshall GM, Walker J, Rogers M, Field M, Brereton JJ, Marsh DJ: Germline mutation of the tumour suppressor PTEN in Proteus syndrome. J Med Genet. 2002 Dec;39(12):937-40. [PubMed
]
- Butler MG, Dasouki MJ, Zhou XP, Talebizadeh Z, Brown M, Takahashi TN, Miles JH, Wang CH, Stratton R, Pilarski R, Eng C: Subset of individuals with autism spectrum disorders and extreme macrocephaly associated with germline PTEN tumour suppressor gene mutations. J Med Genet. 2005 Apr;42(4):318-21. [PubMed
]
- Balciuniene J, Feng N, Iyadurai K, Hirsch B, Charnas L, Bill BR, Easterday MC, Staaf J, Oseth L, Czapansky-Beilman D, Avramopoulos D, Thomas GH, Borg A, Valle D, Schimmenti LA, Selleck SB: Recurrent 10q22-q23 deletions: a genomic disorder on 10q associated with cognitive and behavioral abnormalities. Am J Hum Genet. 2007 May;80(5):938-47. Epub 2007 Mar 20. [PubMed
]
- Tekin M, Hismi BO, Fitoz S, Yalcinkaya F, Ekim M, Kansu A, Ertem M, Deda G, Tutar E, Arsan S, Zhou XP, Pilarski R, Eng C, Akar N: A germline PTEN mutation with manifestations of prenatal onset and verrucous epidermal nevus. Am J Med Genet A. 2006 Jul 1;140(13):1472-5. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
6867 |
| Enzyme 15 Name |
Synaptojanin-2 |
| Enzyme 15 Synonyms |
- Synaptic inositol-1,4,5-trisphosphate 5-phosphatase 2
|
| Enzyme 15 Gene Name |
SYNJ2 |
| Enzyme 15 Protein Sequence |
>Synaptojanin-2
MALSKGLRLLGRLGAEGDCSVLLEARGRDDCLLFEAGTVATLAPEEKEVIKGQYGKLTDA
YGCLGELRLKSGGTSLSFLVLVTGCTSVGRIPDAEIYKITATDFYPLQEEAKEEERLIAL
KKILSSGVFYFSWPNDGSRFDLTVRTQKQGDDSSEWGNSFFWNQLLHVPLRQHQVSCCDW
LLKIICGVVTIRTVYASHKQAKACLVSRVSCERTGTRFHTRGVNDDGHVSNFVETEQMIY
MDDGVSSFVQIRGSVPLFWEQPGLQVGSHHLRLHRGLEANAPAFDRHMVLLKEQYGQQVV
VNLLGSRGGEEVLNRAFKKLLWASCHAGDTPMINFDFHQFAKGGKLEKLETLLRPQLKLH
WEDFDVFTKGENVSPRFQKGTLRMNCLDCLDRTNTVQSFIALEVLHLQLKTLGLSSKPIV
DRFVESFKAMWSLNGHSLSKVFTGSRALEGKAKVGKLKDGARSMSRTIQSNFFDGVKQEA
IKLLLVGDVYGEEVADKGGMLLDSTALLVTPRILKAMTERQSEFTNFKRIRIAMGTWNVN
GGKQFRSNVLRTAELTDWLLDSPQLSGATDSQDDSSPADIFAVGFEEMVELSAGNIVNAS
TTNKKMWGEQLQKAISRSHRYILLTSAQLVGVCLYIFVRPYHVPFIRDVAIDTVKTGMGG
KAGNKGAVGIRFQFHSTSFCFICSHLTAGQSQVKERNEDYKEITQKLCFPMGRNVFSHDY
VFWCGDFNYRIDLTYEEVFYFVKRQDWKKLLEFDQLQLQKSSGKIFKDFHEGAINFGPTY
KYDVGSAAYDTSDKCRTPAWTDRVLWWRKKHPFDKTAGELNLLDSDLDVDTKVRHTWSPG
ALQYYGRAELQASDHRPVLAIVEVEVQEVDVGARERVFQEVSSFQGPLDATVVVNLQSPT
LEEKNEFPEDLRTELMQTLGSYGTIVLVRINQGQMLVTFADSHSALSVLDVDGMKVKGRA
VKIRPKTKDWLKGLREEIIRKRDSMAPVSPTANSCLLEENFDFTSLDYESEGDILEDDED
YLVDEFNQPGVSDSELGGDDLSDVPGPTALAPPSKSPALTKKKQHPTYKDDADLVELKRE
LEAVGEFRHRSPSRSLSVPNRPRPPQPPQRPPPPTGLMVKKSASDASISSGTHGQYSILQ
TARLLPGAPQQPPKARTGISKPYNVKQIKTTNAQEAEAAIRCLLEARGGASEEALSAVAP
RDLEASSEPEPTPGAAKPETPQAPPLLPRRPPPRVPAIKKPTLRRTGKPLSPEEQFEQQT
VHFTIGPPETSVEAPPVVTAPRVPPVPKPRTFQPGKAAERPSHRKPASDEAPPGAGASVP
PPLEAPPLVPKVPPRRKKSAPAAFHLQVLQSNSQLLQGLTYNSSDSPSGHPPAAGTVFPQ
GDFLSTSSATSPDSDGTKAMKPEAAPLLGDYQDPFWNLLHHPKLLNNTWLSKSSDPLDSG
TRSPKRDPIDPVSAGASAAKAELPPDHEHKTLGHWVTISDQEKRTALQVFDPLAKT
|
| Enzyme 15 Number of Residues |
1496 |
| Enzyme 15 Molecular Weight |
165536.6 |
| Enzyme 15 Theoretical pI |
7.36 |
| Enzyme 15 GO Classification |
| Function |
- RNA binding
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- nucleic acid binding
- phosphatase activity
- phosphatidylinositol bisphosphate phosphatase activity
- phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
- cellular metabolic process
- dephosphorylation
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Involved in nucleotide binding |
| Enzyme 15 Specific Function |
Inositol 5-phosphatase which may be involved in distinct membrane trafficking and signal transduction pathways. May mediate the inhibitory effect of Rac1 on endocytosis |
| Enzyme 15 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 15 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate [RN:R04404]
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
26190608  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
O15056  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
SYNJ2_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>4491 bp
ATGGCCCTGAGCAAAGGGCTGCGGCTGCTGGGGCGCCTGGGGGCCGAGGGGGACTGTAGC
GTGCTGCTGGAGGCGCGCGGCCGCGACGACTGCCTGCTGTTCGAGGCCGGCACGGTGGCC
ACGCTGGCTCCAGAAGAAAAGGAAGTCATTAAAGGACAGTATGGCAAGCTCACGGACGCG
TACGGCTGCCTGGGGGAGCTGAGGCTGAAATCTGGTGGCACGTCTCTGAGCTTCCTGGTG
TTGGTGACAGGCTGCACATCTGTGGGCAGAATTCCAGATGCTGAAATCTACAAAATCACT
GCCACTGACTTTTACCCTCTTCAGGAAGAGGCCAAGGAGGAGGAACGCCTCATAGCTTTG
AAGAAAATCCTCAGCTCGGGGGTGTTCTATTTCTCATGGCCAAACGATGGGTCTCGCTTT
GACCTGACTGTCCGCACGCAGAAGCAGGGGGATGACAGCTCTGAATGGGGGAACTCCTTC
TTCTGGAACCAGCTGTTGCACGTGCCCTTGAGGCAGCACCAGGTGAGCTGCTGTGACTGG
CTGCTGAAGATCATCTGCGGGGTGGTCACCATCCGCACCGTGTATGCCTCCCACAAGCAG
GCCAAGGCCTGCCTCGTCTCTCGCGTTAGCTGTGAGCGCACAGGCACTCGCTTCCACACC
CGTGGCGTGAACGACGACGGCCATGTGTCCAACTTCGTGGAGACAGAGCAGATGATTTAC
ATGGACGATGGAGTGTCATCTTTTGTCCAGATCAGAGGCTCCGTTCCGCTGTTCTGGGAA
CAGCCAGGGCTTCAGGTTGGCTCCCATCATCTGAGACTCCACAGAGGCCTGGAAGCCAAT
GCCCCTGCTTTCGACAGGCACATGGTGCTTCTGAAGGAGCAGTACGGGCAGCAGGTGGTC
GTGAACCTTCTGGGAAGCAGAGGCGGAGAGGAGGTGCTCAACAGAGCCTTCAAGAAGCTG
CTCTGGGCTTCTTGCCACGCGGGCGACACGCCTATGATCAATTTTGACTTCCATCAGTTT
GCCAAAGGTGGGAAGCTAGAGAAATTGGAGACCCTCTTGAGGCCACAGTTAAAGCTGCAC
TGGGAAGACTTCGATGTGTTCACAAAGGGGGAGAACGTCAGTCCACGTTTTCAGAAAGGC
ACTTTGCGGATGAACTGTCTTGACTGCCTGGACCGAACCAACACTGTGCAGAGCTTCATC
GCGCTCGAGGTCCTGCATCTGCAGCTCAAGACCCTGGGGCTGAGTTCAAAACCCATCGTT
GACCGCTTTGTGGAGTCCTTCAAAGCCATGTGGTCTCTGAATGGCCACAGCCTGAGCAAG
GTGTTCACAGGCAGCAGAGCCCTGGAAGGGAAGGCCAAGGTGGGGAAGCTGAAGGATGGA
GCCCGGTCCATGTCTCGAACCATCCAGTCCAACTTCTTCGACGGGGTGAAGCAGGAGGCC
ATCAAGCTGCTGCTGGTTGGGGACGTCTACGGCGAGGAGGTGGCAGACAAAGGGGGCATG
CTGCTGGACAGCACGGCGCTCCTGGTGACTCCCAGGATCCTGAAAGCTATGACTGAGCGT
CAGTCCGAATTCACAAATTTCAAGCGGATCCGGATTGCTATGGGGACCTGGAACGTGAAC
GGAGGAAAGCAGTTCCGGAGCAACGTGCTCAGGACGGCGGAGCTGACAGACTGGCTGCTC
GACTCGCCCCAGCTCTCGGGAGCTACCGACTCCCAGGATGACAGCAGCCCAGCTGACATA
TTTGCTGTGGGGTTTGAAGAGATGGTGGAATTGAGCGCAGGGAATATTGTCAATGCCAGT
ACTACCAACAAGAAGATGTGGGGTGAACAGCTTCAGAAAGCCATCTCACGCTCTCATAGA
TACATTCTGTTGACTTCGGCACAGCTGGTGGGCGTCTGTCTTTATATCTTTGTACGTCCA
TACCATGTCCCGTTCATCAGGGACGTAGCCATCGACACAGTGAAGACGGGCATGGGGGGC
AAGGCGGGGAACAAGGGCGCCGTCGGCATCCGCTTCCAGTTCCACAGCACCAGCTTCTGC
TTCATATGTAGTCACCTGACGGCCGGGCAGTCCCAGGTGAAGGAGCGGAATGAAGACTAC
AAGGAGATCACCCAGAAACTCTGCTTCCCAATGGGGAGAAATGTTTTTTCTCATGATTAT
GTATTTTGGTGTGGCGATTTCAACTACCGCATTGATCTTACTTATGAAGAAGTCTTCTAT
TTTGTTAAACGCCAAGACTGGAAGAAACTTCTGGAATTTGATCAACTACAGCTACAGAAA
TCAAGTGGAAAAATTTTTAAGGACTTTCACGAAGGAGCCATTAACTTTGGACCCACCTAC
AAGTATGACGTTGGCTCAGCCGCCTACGATACAAGCGACAAATGCCGCACCCCCGCCTGG
ACAGACAGGGTGCTGTGGTGGAGGAAGAAACATCCCTTTGATAAAACAGCTGGAGAACTC
AACCTTCTAGACAGTGATCTAGATGTTGACACCAAAGTCAGACACACCTGGTCTCCTGGT
GCCCTGCAGTATTATGGTCGTGCGGAGCTACAAGCGTCTGATCACAGACCTGTGCTGGCG
ATCGTGGAGGTGGAAGTTCAGGAAGTCGATGTGGGTGCTCGGGAGAGGGTTTTCCAGGAA
GTGTCCTCCTTCCAGGGCCCCCTGGATGCCACTGTTGTAGTAAACCTTCAATCACCGACC
TTAGAAGAGAAAAACGAGTTTCCAGAGGACCTGCGTACTGAGCTCATGCAGACCTTGGGG
AGTTATGGGACAATTGTTCTTGTCAGGATCAACCAAGGGCAGATGCTGGTAACTTTTGCA
GACAGTCACTCGGCTCTCAGTGTCCTGGACGTGGACGGTATGAAGGTGAAAGGCAGAGCA
GTGAAGATTAGACCGAAGACCAAGGACTGGCTGAAAGGTTTGCGAGAGGAGATCATTCGG
AAACGAGACAGCATGGCCCCCGTGTCTCCCACTGCCAACTCCTGTTTGCTGGAGGAAAAC
TTTGACTTCACAAGTTTGGACTATGAGTCAGAAGGGGATATTCTTGAAGACGATGAAGAC
TACTTGGTGGATGAATTCAATCAGCCTGGAGTCTCGGACAGTGAACTCGGGGGAGACGAC
CTCTCTGATGTCCCCGGCCCCACAGCACTGGCTCCTCCCAGCAAGTCACCTGCTCTCACC
AAAAAGAAGCAGCATCCAACGTACAAAGATGACGCGGACCTGGTGGAGCTCAAGCGGGAG
CTGGAAGCCGTCGGGGAGTTCCGCCACCGTTCTCCGAGCAGGTCTCTGTCGGTCCCCAAC
CGGCCTCGGCCACCTCAACCCCCGCAGAGACCCCCCCCTCCAACCGGTTTAATGGTGAAA
AAGTCGGCTTCAGATGCGTCCATCTCCTCCGGCACCCATGGACAGTATTCAATTTTGCAG
ACGGCAAGACTTCTACCAGGAGCACCTCAGCAACCTCCCAAGGCTCGGACTGGAATAAGT
AAACCTTATAATGTCAAGCAGATCAAAACCACCAATGCCCAGGAGGCAGAAGCAGCAATC
CGGTGTCTCCTGGAAGCCAGAGGAGGTGCCTCCGAAGAAGCCCTAAGTGCCGTGGCCCCA
AGGGACCTTGAAGCATCCTCTGAACCAGAGCCCACACCGGGGGCAGCCAAACCAGAGACC
CCACAGGCGCCCCCACTCCTTCCCCGTCGGCCCCCACCCAGAGTTCCTGCCATCAAGAAG
CCAACCTTGAGAAGGACAGGAAAGCCCCTGTCACCGGAAGAACAGTTTGAGCAACAGACT
GTCCATTTTACAATCGGGCCCCCGGAGACAAGCGTTGAGGCCCCTCCTGTCGTGACAGCC
CCTCGAGTCCCTCCTGTTCCCAAACCAAGAACATTTCAGCCTGGGAAAGCTGCAGAGAGG
CCAAGCCACAGGAAGCCAGCATCAGACGAAGCCCCTCCTGGGGCAGGAGCCTCTGTGCCA
CCACCTCTGGAGGCGCCGCCTCTTGTGCCCAAGGTACCCCCGAGGAGGAAGAAGTCAGCC
CCCGCAGCCTTCCACCTGCAGGTCCTGCAGAGCAACAGCCAGCTTCTCCAGGGCCTCACT
TACAATAGCAGTGACAGCCCCTCTGGGCACCCACCTGCCGCGGGCACCGTCTTCCCACAA
GGGGACTTTCTCAGCACTTCATCTGCTACAAGCCCCGACAGCGATGGCACCAAAGCGATG
AAGCCAGAGGCAGCCCCACTTCTTGGTGATTATCAGGACCCCTTCTGGAACCTTCTTCAC
CACCCTAAACTGTTGAATAACACTTGGCTTTCTAAGAGCTCAGACCCTTTGGACTCAGGA
ACCAGGAGCCCCAAAAGAGATCCCATAGACCCAGTGTCAGCTGGCGCTTCAGCTGCCAAG
GCAGAGCTGCCACCAGATCATGAACACAAAACCTTAGGTCACTGGGTGACAATCAGTGAC
CAAGAAAAGAGGACAGCACTGCAGGTGTTTGACCCACTGGCAAAAACATGA
|
| Enzyme 15 GenBank Gene ID |
NM_003898.3  |
| Enzyme 15 GeneCard ID |
SYNJ2  |
| Enzyme 15 GenAtlas ID |
SYNJ2  |
| Enzyme 15 HGNC ID |
HGNC:11504  |
| Enzyme 15 Chromosome Location |
6 |
| Enzyme 15 Locus |
6q25.3 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Malecz N, McCabe PC, Spaargaren C, Qiu R, Chuang Y, Symons M: Synaptojanin 2, a novel Rac1 effector that regulates clathrin-mediated endocytosis. Curr Biol. 2000 Nov 2;10(21):1383-6. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Nemoto Y, Wenk MR, Watanabe M, Daniell L, Murakami T, Ringstad N, Yamada H, Takei K, De Camilli P: Identification and characterization of a synaptojanin 2 splice isoform predominantly expressed in nerve terminals. J Biol Chem. 2001 Nov 2;276(44):41133-42. Epub 2001 Aug 9. [PubMed
]
- 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
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [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
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
6868 |
| Enzyme 16 Name |
72 kDa inositol polyphosphate 5-phosphatase |
| Enzyme 16 Synonyms |
- Phosphatidylinositol polyphosphate 5-phosphatase type IV
- Phosphatidylinositol-4,5-bisphosphate 5-phosphatase
|
| Enzyme 16 Gene Name |
INPP5E |
| Enzyme 16 Protein Sequence |
>72 kDa inositol polyphosphate 5-phosphatase
MPSKAENLRPSEPAPQPPEGRTLQGQLPGAPPAQRAGSPPDAPGSESPALACSTPATPSG
EDPPARAAPIAPRPPARPRLERALSLDDKGWRRRRFRGSQEDLEARNGTSPSRGSVQSEG
PGAPAHSCSPPCLSTSLQEIPKSRGVLSSERGSPSSGGNPLSGVASSSPNLPHRDAAVAG
SSPRLPSLLPPRPPPALSLDIASDSLRTANKVDSDLADYKLRAQPLLVRAHSSLGPGRPR
SPLACDDCSLRSAKSSFSLLAPIRSKDVRSRSYLEGSLLASGALLGADELARYFPDRNVA
LFVATWNMQGQKELPPSLDEFLLPAEADYAQDLYVIGVQEGCSDRREWETRLQETLGPHY
VLLSSAAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLF
ITSHFTSGDGKVAERLLDYTRTVQALVLPRNVPDTNPYRSSAADVTTRFDEVFWFGDFNF
RLSGGRTVVDALLCQGLVVDVPALLQHDQLIREMRKGSIFKGFQEPDIHFLPSYKFDIGK
DTYDSTSKQRTPSYTDRVLYRSRHKGDICPVSYSSCPGIKTSDHRPVYGLFRVKVRPGRD
NIPLAAGKFDRELYLLGIKRRISKEIQRQQALQSQNSSTICSVS
|
| Enzyme 16 Number of Residues |
644 |
| Enzyme 16 Molecular Weight |
70204.4 |
| Enzyme 16 Theoretical pI |
9.18 |
| Enzyme 16 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 16 General Function |
Involved in inositol-polyphosphate 5-phosphatase activity |
| Enzyme 16 Specific Function |
Converts phosphatidylinositol-3,4,5-triphosphate (PtdIns 3,4,5-P3) to PtdIns-P2. Specific for lipid substrates, inactive towards water soluble inositol phosphates |
| Enzyme 16 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 16 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate [RN:R04404]
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
8925284  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q9NRR6  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
INP5E_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1935 bp
ATGCCGTCCAAGGCGGAGAATCTGCGGCCCTCCGAGCCGGCCCCGCAGCCGCCGGAAGGG
AGGACGCTCCAAGGACAGCTTCCCGGCGCTCCGCCGGCCCAGCGCGCGGGGTCCCCACCC
GATGCTCCGGGCTCCGAGAGCCCCGCGCTTGCCTGCAGCACTCCGGCCACGCCCAGCGGC
GAGGACCCGCCAGCCCGAGCAGCACCCATCGCCCCGCGGCCCCCCGCCAGGCCTCGACTG
GAGCGAGCCCTGTCCCTGGACGACAAGGGCTGGAGGAGGAGGCGTTTTCGAGGCAGCCAG
GAGGACCTGGAAGCCCGGAATGGGACCAGTCCCTCCAGGGGCTCAGTGCAGAGCGAGGGC
CCCGGGGCCCCCGCCCACAGCTGCTCCCCGCCCTGCCTGAGCACCTCCTTGCAGGAAATC
CCCAAGTCCCGCGGGGTCCTGAGCAGTGAGAGAGGGAGCCCGTCCTCGGGGGGTAACCCT
CTCTCTGGGGTGGCCAGCAGCTCCCCGAACCTCCCGCACAGAGACGCCGCCGTGGCGGGG
AGCTCGCCCAGGCTGCCCAGCCTGCTGCCCCCGCGCCCACCGCCTGCCCTGAGCCTGGAC
ATCGCCTCCGACTCCCTGAGGACAGCAAACAAGGTCGACTCGGATCTTGCAGACTACAAG
CTCCGCGCGCAGCCGCTCCTGGTGCGGGCCCACAGCAGCCTGGGCCCCGGCCGGCCGCGG
AGCCCCCTGGCCTGCGACGACTGTTCCCTTCGCTCGGCCAAATCCTCCTTCAGCCTCCTG
GCGCCCATCCGCAGCAAGGACGTCCGCAGCAGGAGTTACCTGGAGGGCAGCCTCCTGGCC
AGCGGGGCCCTGTTGGGGGCGGATGAGCTGGCCCGCTACTTCCCAGACCGGAACGTGGCA
CTCTTCGTGGCCACCTGGAACATGCAGGGCCAGAAGGAGCTCCCGCCCAGCCTGGACGAG
TTCCTGCTCCCAGCCGAGGCCGACTATGCCCAGGACCTGTATGTCATCGGGGTCCAGGAG
GGCTGTTCTGACACGCGGGAGTGGGAGACTCGTCTGCAGGAGACGCTGGGCCCGCACTAT
GTGCTGCTGTCCTCGGCGGCCCACGGCGTGCTCTACATGTCGCTCTTCATCCGCAGGGAC
CTCATCTGGTTCTGCTCAGAGGTGGAGTGCTCCACGGTGACCACACGCATCGTGTCTCAG
ATCAAGACCAAGGGGGCCTTGGGCATCAGCTTCACCTTTTTTGGCACTTCCTTCCTCTTC
ATCACGTCCCACTTCACCTCAGGTGACGGGAAGGTGGCGGAGCGGCTGCTGGACTACACC
AGGACTGTACAAGCCCTGGTCCTGCCCAGAAATGTGCCCGACACCAACCCCTATCGCTCC
AGCGCAGCGGACGTCACCACCCGCTTCGATGAGGTGTTCTGGTTTGGAGACTTCAACTTC
CGCCTGAGTGGCGGGCGCACAGTCGTGGACGCCCTCCTGTGCCAGGGCCTGGTGGTGGAC
GTGCCGGCGCTGCTGCAGCACGACCAGCTCATCCGGGAGATGCGGAAAGGGTCCATCTTC
AAGGGCTTCCAGGAGCCGGACATCCACTTCCTCCCATCATACAAGTTTGACATCGGGAAG
GACACGTACGACAGCACCTCCAAGCAGAGGACGCCCTCATACACGGACCGCGTCTTGTAC
AGAAGCCGCCACAAGGGTGACATCTGTCCTGTGAGCTACTCTTCCTGCCCCGGGATCAAG
ACGTCCGACCACCGCCCTGTGTATGGCCTCTTCCGGGTGAAAGTGAGGCCGGGGCGAGAC
AACATTCCGTTGGCAGCTGGCAAATTTGATAGAGAACTGTACTTACTAGGAATTAAAAGA
CGGATTTCGAAGGAGATTCAGAGGCAGCAAGCACTACAGAGTCAGAACTCCAGCACCATC
TGCTCCGTTTCTTGA
|
| Enzyme 16 GenBank Gene ID |
AF187891  |
| Enzyme 16 GeneCard ID |
INPP5E  |
| Enzyme 16 GenAtlas ID |
Not Available |
| Enzyme 16 HGNC ID |
Not Available |
| Enzyme 16 Chromosome Location |
9 |
| Enzyme 16 Locus |
9q34.3 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Kisseleva MV, Wilson MP, Majerus PW: The isolation and characterization of a cDNA encoding phospholipid-specific inositol polyphosphate 5-phosphatase. J Biol Chem. 2000 Jun 30;275(26):20110-6. [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
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [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
]
- 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
]
- Jacoby M, Cox JJ, Gayral S, Hampshire DJ, Ayub M, Blockmans M, Pernot E, Kisseleva MV, Compere P, Schiffmann SN, Gergely F, Riley JH, Perez-Morga D, Woods CG, Schurmans S: INPP5E mutations cause primary cilium signaling defects, ciliary instability and ciliopathies in human and mouse. Nat Genet. 2009 Sep;41(9):1027-31. Epub 2009 Aug 9. [PubMed
]
- Bielas SL, Silhavy JL, Brancati F, Kisseleva MV, Al-Gazali L, Sztriha L, Bayoumi RA, Zaki MS, Abdel-Aleem A, Rosti RO, Kayserili H, Swistun D, Scott LC, Bertini E, Boltshauser E, Fazzi E, Travaglini L, Field SJ, Gayral S, Jacoby M, Schurmans S, Dallapiccola B, Majerus PW, Valente EM, Gleeson JG: Mutations in INPP5E, encoding inositol polyphosphate-5-phosphatase E, link phosphatidyl inositol signaling to the ciliopathies. Nat Genet. 2009 Sep;41(9):1032-6. Epub 2009 Aug 9. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
6869 |
| Enzyme 17 Name |
Synaptojanin-1 |
| Enzyme 17 Synonyms |
- Synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1
|
| Enzyme 17 Gene Name |
SYNJ1 |
| Enzyme 17 Protein Sequence |
>Synaptojanin-1
MAFSKGFRIYHKLDPPPFSLIVETRHKEECLMFESGAVAVLSSAEKEAIKGTYSKVLDAY
GLLGVLRLNLGDTMLHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRIDSSDEDRISEVR
KVLNSGNFYFAWSASGISLDLSLNAHRSMQEQTTDNRFFWNQSLHLHLKHYGVNCDDWLL
RLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVVYLD
DSVSSFIQIRGSVPLFWEQPGLQVGSHRVRMSRGFEANAPAFDRHFRTLKNLYGKQIIVN
LLGSKEGEHMLSKAFQSHLKASEHAADIQMVNFDYHQMVKGGKAEKLHSVLKPQVQKFLD
YGFFYFNGSEVQRCQSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAEKPQLVTR
FQEVFRSMWSVNGDSISKIYAGTGALEGKAKLKDGARSVTRTIQNNFFDSSKQEAIDVLL
LGNTLNSDLADKARALLTTGSLRVSEQTLQSASSKVLKSMCENFYKYSKPKKIRVCVGTW
NVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNI
VSASTTNQKLWAVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKT
GMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFIEIARKLSFPMGRMLF
SHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRGFLEGKVTF
APTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYT
WTPGTLLHYGRAELKTSDHRPVVALIDIDIFEVEAEERQNIYKEVIAVQGPPDGTVLVSI
KSSLPENNFFDDALIDELLQQFASFGEVILIRFVEDKMWVTFLEGSSALNVLSLNGKELL
NRTITIALKSPDWIKNLEEEMSLEKISIALPSSTSSTLLGEDAEVAADFDMEGDVDDYSA
EVEELLPQHLQPSSSSGLGTSPSSSPRTSPCQSPTISEGPVPSLPIRPSRAPSRTPGPPS
AQSSPIDAQPATPLPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPPPPSGARSPAPTRK
EFGGIGAPPSPGVARREMEAPKSPGTTRKDNIGRSQPSPQAGLAGPGPAGYSTARPTIPP
RAGVISAPQSHARASAGRLTPESQSKTSETSKGSTFLPEPLKPQAAFPPQSSLPPPAQRL
QEPLVPVAAPMPQSGPQPNLETPPQPPPRSRSSHSLPSEASSQPQVKTNGISDGKRESPL
KIDPFEDLSFNLLAVSKAQLSVQTSPVPTPDPKRLIQLPSATQSNVLSSVSCMPTMPPIP
ARSQSQENMRSSPNPFITGLTRTNPFSDRTAAPGNPFRAKSEESEATSWFSKEEPVTISP
FPSLQPLGHNKSRASSSLDGFKDSFDLQGQSTLKISNPKGWVTFEEEEDFGVKGKSKSAC
SDLLGNQPSSFSGSNLTLNDDWNKGTNVSFCVLPSRRPPPPPVPLLPPGTSPPVDPFTTL
ASKASPTLDFTER
|
| Enzyme 17 Number of Residues |
1573 |
| Enzyme 17 Molecular Weight |
173101.4 |
| Enzyme 17 Theoretical pI |
7.44 |
| Enzyme 17 GO Classification |
| Function |
- RNA binding
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- nucleic acid binding
- phosphatase activity
- phosphatidylinositol bisphosphate phosphatase activity
- phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
- cellular metabolic process
- dephosphorylation
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
|
| Component |
| — |
|
| Enzyme 17 General Function |
Cell cycle control, cell division, chromosome partitioning |
| Enzyme 17 Specific Function |
Inositol 5-phosphatase which has a role in clathrin- mediated endocytosis |
| Enzyme 17 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 17 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate [RN:R04404]
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
237757310  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
O43426  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
SYNJ1_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>4839 bp
ATGCGGAAGAGATGGGCCTGCTGGAGCGGAAGTGACGCTCCCGGCGGCTGTGGCGGCGGC
TGCGGGAGAAGGAGGAGGAGGAGCCGGAGGAAGAGGGCTGCCTCCGAAGAAAGGAGAATG
GCGTTCAGTAAAGGATTCCGGATCTATCACAAATTGGATCCCCCACCTTTCAGCCTCATA
GTGGAAACTAGGCATAAGGAAGAATGTCTCATGTTCGAGTCTGGGGCTGTCGCTGTGCTC
TCATCTGCAGAAAAAGAGGCAATCAAGGGTACATACTCCAAAGTACTGGATGCATATGGA
CTCTTAGGTGTTCTGCGGTTAAATCTTGGTGATACTATGTTACATTATCTGGTCCTAGTC
ACTGGATGTATGTCTGTTGGAAAAATTCAAGAATCTGAAGTTTTCCGAGTTACTTCCACT
GAGTTTATATCACTGCGAATCGATTCTTCAGATGAGGATCGCATTTCAGAAGTGCGGAAA
GTTTTGAATTCAGGAAACTTTTATTTTGCATGGTCTGCATCTGGCATCAGTTTAGATTTG
AGTCTTAATGCGCATCGTAGCATGCAAGAACAGACAACTGATAATAGATTTTTCTGGAAT
CAGTCTTTGCATTTGCATCTCAAACACTATGGCGTGAATTGTGATGACTGGTTATTACGT
CTTATGTGTGGAGGAGTAGAAATCAGAACAATTTATGCTGCTCATAAACAGGCGAAGGCT
TGCCTCATTTCAAGATTAAGCTGTGAACGAGCTGGGACCAGGTTTAATGTCCGGGGAACA
AATGATGATGGTCATGTTGCCAATTTTGTAGAAACAGAACAGGTTGTGTACTTAGATGAC
TCAGTTTCTTCCTTCATACAAATCCGAGGATCTGTTCCATTGTTCTGGGAGCAACCAGGG
TTGCAAGTGGGATCTCATCGTGTCCGTATGTCAAGGGGATTTGAAGCCAATGCACCTGCT
TTTGACAGGCATTTTAGAACACTTAAGAACTTATATGGTAAACAAATAATAGTAAATTTG
CTTGGATCTAAGGAAGGTGAACATATGCTAAGTAAAGCTTTCCAGAGTCATTTGAAAGCT
TCTGAACATGCTGCTGATATCCAGATGGTGAATTTTGACTATCATCAAATGGTTAAGGGA
GGAAAGGCAGAAAAATTACATAGTGTTCTTAAACCTCAAGTCCAGAAGTTTCTAGATTAT
GGATTTTTTTATTTCAATGGAAGTGAAGTTCAAAGATGCCAGAGTGGTACAGTTCGAACA
AACTGCTTGGATTGTCTTGATAGAACAAATAGTGTGCAGGCATTTCTTGGCTTAGAGATG
CTAGCTAAACAGTTGGAAGCTCTTGGTTTAGCTGAAAAGCCTCAGTTGGTGACTCGCTTT
CAAGAAGTTTTTCGGTCAATGTGGTCCGTGAATGGTGATTCAATCAGTAAGATATATGCA
GGAACTGGAGCTCTTGAAGGGAAAGCGAAGTTAAAAGATGGTGCTCGCTCTGTTACCCGA
ACAATTCAGAATAACTTCTTTGACAGCTCCAAGCAAGAGGCCATTGATGTTTTGCTACTG
GGAAATACTCTGAATAGTGATTTAGCTGACAAAGCTCGAGCACTTTTAACTACTGGAAGT
TTGCGTGTTTCTGAGCAGACATTACAGTCAGCATCTTCTAAAGTACTAAAGAGCATGTGT
GAGAATTTCTACAAATATTCAAAGCCTAAGAAAATTCGAGTATGTGTCGGAACCTGGAAT
GTGAATGGTGGGAAGCAATTTCGCAGCATAGCTTTTAAGAATCAGACACTCACTGACTGG
CTTCTTGATGCACCCAAGTTAGCTGGCATCCAGGAGTTTCAAGATAAAAGAAGTAAGCCA
ACTGATATATTTGCAATTGGTTTTGAAGAAATGGTAGAATTGAATGCTGGAAACATTGTG
AGTGCAAGCACAACAAATCAGAAGCTCTGGGCTGTAGAACTTCAGAAGACAATCTCCAGA
GACAACAAGTATGTGCTGCTGGCTTCTGAACAGTTGGTGGGCGTCTGTTTGTTTGTTTTT
ATCAGACCACAGCATGCTCCTTTTATCAGGGATGTTGCAGTTGATACTGTGAAGACTGGA
ATGGGAGGTGCAACTGGAAATAAGGGAGCAGTTGCAATCCGAATGCTCTTCCATACAACC
AGCCTTTGCTTCGTCTGTAGCCACTTTGCTGCAGGGCAGTCACAAGTCAAAGAAAGAAAT
GAAGATTTTATAGAAATAGCACGAAAATTGAGTTTTCCTATGGGAAGGATGCTATTTTCC
CATGACTATGTATTTTGGTGTGGTGATTTCAACTATCGAATCGATCTCCCTAACGAAGAA
GTTAAAGAGCTCATAAGACAGCAAAATTGGGATTCTCTTATAGCAGGAGATCAACTTATC
AATCAGAAAAATGCTGGACAGGTTTTTAGAGGATTTTTAGAAGGAAAGGTAACCTTTGCT
CCGACATATAAGTATGACTTGTTTTCTGACGACTATGACACCAGTGAAAAGTGCCGCACC
CCTGCCTGGACAGACCGTGTCCTTTGGAGAAGGAGGAAATGGCCTTTTGATAGATCAGCT
GAAGATCTAGATCTTCTAAATGCTAGTTTTCAAGATGAAAGCAAAATTCTGTACACGTGG
ACTCCAGGCACTTTGCTGCACTATGGAAGAGCTGAGCTGAAGACTTCTGACCACAGGCCT
GTCGTTGCCCTGATTGATATAGATATATTTGAAGTTGAAGCTGAAGAGAGGCAAAACATT
TATAAAGAAGTAATTGCAGTTCAGGGTCCACCAGATGGTACAGTATTGGTCTCAATCAAA
AGTTCTTTACCAGAAAATAATTTTTTTGATGATGCCTTGATTGATGAGCTTCTGCAGCAG
TTTGCAAGTTTTGGTGAAGTTATACTTATAAGATTTGTAGAAGATAAAATGTGGGTTACA
TTTTTGGAGGGAAGCTCTGCCTTGAATGTTCTGAGCCTAAATGGTAAAGAGTTATTGAAT
CGGACTATAACTATTGCTTTAAAAAGTCCAGACTGGATCAAAAATTTGGAAGAAGAAATG
AGTTTAGAGAAAATTAGCATTGCATTGCCATCATCAACAAGCTCTACCCTGCTTGGTGAA
GATGCAGAGGTTGCAGCAGATTTTGATATGGAAGGTGATGTTGATGACTATAGTGCTGAA
GTGGAGGAACTTCTTCCTCAGCATCTCCAGCCATCTTCAAGTTCCGGCCTTGGTACTTCC
CCCAGCTCTTCACCCCGAACTAGTCCCTGCCAGTCACCTACAATATCAGAGGGTCCTGTA
CCTTCCCTTCCCATCAGACCAAGCCGAGCACCGTCAAGAACTCCTGGGCCTCCCAGTGCA
CAGAGTTCTCCTATTGACGCGCAGCCAGCAACGCCGCTGCCGCAGAAAGACCCCGCCCAG
CCCTTGGAGCCCAAGCGGCCGCCGCCGCCCCGCCCGGTCGCCCCTCCCACACGCCCGGCT
CCCCCACAGAGACCTCCTCCGCCTTCAGGGGCTAGGAGTCCTGCACCCACTAGAAAGGAA
TTTGGAGGTATTGGAGCCCCTCCCAGTCCTGGGGTAGCTAGGAGAGAGATGGAAGCACCC
AAAAGCCCTGGAACAACAAGGAAAGATAATATAGGACGCAGTCAGCCTTCACCTCAAGCA
GGACTTGCAGGCCCAGGACCTGCTGGATACAGTACAGCCAGACCGACGATTCCTCCTCGT
GCTGGAGTTATCAGTGCCCCACAGAGCCACGCGCGGGCATCTGCTGGAAGACTGACTCCT
GAAAGCCAAAGCAAAACATCAGAAACGTCGAAAGGTTCAACTTTCCTTCCTGAACCACTG
AAGCCTCAGGCTGCTTTTCCTCCGCAGTCTTCTTTGCCCCCGCCTGCTCAAAGGTTGCAA
GAGCCTCTTGTCCCTGTGGCAGCACCTATGCCTCAGTCTGGCCCCCAGCCAAATTTGGAA
ACCCCACCACAACCACCACCTCGAAGCAGGTCATCCCATAGCTTGCCTTCAGAAGCTTCC
TCACAACCGCAAGTAAAAACAAATGGAATCTCTGATGGCAAAAGAGAATCACCATTAAAG
ATTGACCCATTTGAAGATCTGTCATTTAATCTGCTTGCTGTATCAAAGGCTCAGCTATCT
GTTCAAACGTCACCTGTTCCCACCCCAGACCCAAAGAGGTTGATTCAGTTGCCTTCTGCA
ACGCAAAGTAATGTTTTGAGTTCTGTAAGTTGCATGCCAACAATGCCTCCAATTCCAGCT
CGGAGTCAATCCCAGGAAAATATGCGAAGTTCTCCAAACCCATTTATTACTGGCTTGACC
AGGACAAATCCTTTCAGTGACAGGACTGCTGCTCCTGGAAACCCATTTAGAGCCAAGTCT
GAAGAATCAGAGGCAACTTCATGGTTCTCCAAAGAAGAGCCCGTTACTATCAGTCCTTTC
CCTTCTCTGCAGCCTCTTGGTCATAACAAAAGCAGGGCTTCATCTTCACTTGATGGCTTT
AAGGACAGTTTTGATCTACAGGGCCAGTCTACATTAAAAATTAGCAACCCGAAAGGATGG
GTAACCTTCGAGGAAGAAGAGGATTTTGGTGTGAAAGGGAAGTCAAAGTCAGCTTGTTCA
GACTTACTGGGTAATCAGCCAAGTTCATTTTCTGGCTCCAACCTGACATTGAATGATGAC
TGGAATAAAGGTACAAATGTCTCCTTCTGTGTGTTGCCGTCAAGAAGACCTCCTCCACCT
CCTGTCCCTCTGCTCCCGCCCGGCACCAGCCCTCCAGTAGATCCTTTCACGACCTTGGCC
TCTAAGGCTTCACCCACACTGGACTTTACAGAAAGATAA
|
| Enzyme 17 GenBank Gene ID |
NM_003895  |
| Enzyme 17 GeneCard ID |
SYNJ1  |
| Enzyme 17 GenAtlas ID |
Not Available |
| Enzyme 17 HGNC ID |
Not Available |
| Enzyme 17 Chromosome Location |
2 |
| Enzyme 17 Locus |
21q22.2 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Haffner C, Takei K, Chen H, Ringstad N, Hudson A, Butler MH, Salcini AE, Di Fiore PP, De Camilli P: Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15. FEBS Lett. 1997 Dec 15;419(2-3):175-80. [PubMed
]
- 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. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [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
]
- Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Cestra G, Castagnoli L, Dente L, Minenkova O, Petrelli A, Migone N, Hoffmuller U, Schneider-Mergener J, Cesareni G: The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity. J Biol Chem. 1999 Nov 5;274(45):32001-7. [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 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
7254 |
| Enzyme 18 Name |
Type II inositol-1,4,5-trisphosphate 5-phosphatase |
| Enzyme 18 Synonyms |
- 75 kDa inositol polyphosphate-5-phosphatase
- Phosphoinositide 5-phosphatase
- 5PTase
|
| Enzyme 18 Gene Name |
INPP5B |
| Enzyme 18 Protein Sequence |
>Type II inositol-1,4,5-trisphosphate 5-phosphatase
MDQSVAIQETLAEGEYCVIAVQGVLCEGDSRQSRLLGLVRYRLEHGGQEHALFLYTHRRM
AITGDDVSLDQIVPVSRDFTLEEVSPDGELYILGSDVTVQLDTAELSLVFQLPFGSQTRM
FLHEVARACPGFDSATRDPEFLWLSRYRCAELELEMPTPRGCNSALVTWPGYATIGGGRY
PSRKKRWGLEEARPQGAGSVLFWGGAMEKTGFRLMERAHGGGFVWGRSARDGRRDEELEE
AGREMSAAAGSRERNTAGGSNFDGLRPNGKGVPMDQSSRGQDKPESLQPRQNKSKSEITD
MVRSSTITVSDKAHILSMQKFGLRDTIVKSHLLQKEEDYTYIQNFRFFAGTYNVNGQSPK
ECLRLWLSNGIQAPDVYCVGFQELDLSKEAFFFHDTPKEEEWFKAVSEGLHPDAKYAKVK
LIRLVGIMLLLYVKQEHAAYISEVEAETVGTGIMGRMGNKGGVAIRFQFHNTSICVVNSH
LAAHIEEYERRNQDYKDICSRMQFCQPDPSLPPLTISNHDVILWLGDLNYRIEELDVEKV
KKLIEEKDFQMLYAYDQLKIQVAAKTVFEGFTEGELTFQPTYKYDTGSDDWDTSEKCRAP
AWCDRILWKGKNITQLSYQSHMALKTSDHKPVSSVFDIGVRVVNDELYRKTLEEIVRSLD
KMENANIPSVSLSKREFCFQNVKYMQLKVESFTIHNGQVPCHFEFINKPDEESYCKQWLN
ANPSRGFLLPDSDVEIDLELFVNKMTATKLNSGEDKIEDILVLHLDRGKDYFLSVSGNYL
PSCFGSPIHTLCYMREPILDLPLETISELTLMPVWTGDDGSQLDSPMEIPKELWMMVDYL
YRNAVQQEDLFQQPGLRSEFEHIRDCLDTGMIDNLSASNHSVAEALLLFLESLPEPVICY
STYHNCLECSGNYTASKQVISTLPIFHKNVFHYLMAFLRELLKNSAKNHLDENILASIFG
SLLLRNPAGHQKLDMTEKKKAQEFIHQFLCNPL
|
| Enzyme 18 Number of Residues |
993 |
| Enzyme 18 Molecular Weight |
112851.2 |
| Enzyme 18 Theoretical pI |
5.27 |
| Enzyme 18 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
- biological regulation
- regulation of biological process
- regulation of cellular process
- signal transduction
|
| Component |
|
|
| Enzyme 18 General Function |
Involved in inositol or phosphatidylinositol phosphatase activity |
| Enzyme 18 Specific Function |
Hydrolyzes the calcium-mobilizing second messenger Ins(1,4,5)P3, this is a signal-terminating reaction |
| Enzyme 18 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 18 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate [RN:R04404]
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
55665969  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
P32019  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
I5P2_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>2982 bp
ATGGACCAGTCTGTGGCAATCCAGGAGACGCTGGCTGAGGGGGAATACTGCGTCATCGCG
GTGCAAGGTGTGCTGTGTGAGGGGGACAGCCGGCAGAGCCGCCTCCTGGGACTCGTGCGC
TACCGCCTGGAGCACGGCGGCCAGGAACACGCTCTCTTCCTCTATACGCACCGGAGGATG
GCCATTACCGGGGACGATGTCTCTCTGGACCAGATAGTGCCAGTCTCGCGGGATTTTACG
CTGGAAGAAGTGTCCCCAGATGGTGAACTCTACATCCTTGGCTCAGATGTGACCGTCCAG
CTGGACACAGCAGAGCTTAGCCTCGTATTCCAACTGCCCTTTGGTTCACAAACCAGGATG
TTCCTCCACGAAGTTGCCAGGGCCTGTCCAGGCTTCGATTCTGCGACCCGGGATCCTGAA
TTCCTGTGGCTGTCTCGGTATAGGTGCGCAGAGCTGGAGCTGGAGATGCCAACGCCGCGC
GGTTGTAACTCGGCCCTAGTTACCTGGCCAGGGTACGCGACAATTGGCGGAGGCAGGTAT
CCGTCCCGGAAGAAACGGTGGGGATTGGAGGAGGCCCGGCCACAGGGGGCGGGCTCCGTT
CTGTTTTGGGGCGGAGCGATGGAGAAGACAGGCTTTCGATTGATGGAGCGGGCACACGGG
GGCGGGTTCGTCTGGGGGCGGAGCGCGCGGGACGGGCGGCGGGATGAGGAGCTTGAGGAA
GCAGGCAGGGAAATGTCTGCCGCCGCCGGCTCTCGGGAGCGCAACACTGCAGGTGGTTCT
AACTTTGATGGTTTGAGACCAAATGGGAAGGGAGTGCCTATGGACCAAAGCTCCAGGGGT
CAAGATAAACCAGAAAGCTTGCAACCAAGACAGAATAAATCCAAGTCCGAAATTACTGAC
ATGGTTCGCTCCTCCACTATCACAGTGTCGGACAAGGCTCATATTTTATCCATGCAGAAG
TTTGGACTGCGAGATACAATTGTGAAATCACATCTACTACAGAAAGAAGAGGATTACACC
TATATCCAGAACTTCAGGTTTTTTGCGGGAACATACAATGTAAATGGGCAGTCCCCCAAA
GAATGCCTCCGGCTGTGGCTGAGCAATGGTATCCAGGCCCCAGATGTCTATTGTGTAGGG
TTCCAGGAGCTTGATCTGAGTAAGGAAGCTTTTTTCTTTCACGATACCCCAAAGGAGGAA
GAGTGGTTCAAAGCTGTGTCAGAGGGTCTTCATCCAGATGCCAAATATGCAAAGGTGAAG
CTTATCCGACTGGTTGGGATTATGCTGCTGTTATATGTCAAACAGGAGCATGCAGCTTAT
ATCTCAGAAGTGGAAGCCGAGACTGTGGGGACAGGAATCATGGGGAGGATGGGCAACAAG
GGAGGCGTGGCGATCAGGTTCCAGTTCCACAACACCAGCATCTGCGTTGTGAATTCTCAC
TTGGCAGCCCACATTGAAGAGTATGAGAGGAGGAACCAGGACTATAAGGACATTTGTTCT
CGAATGCAGTTTTGTCAGCCTGACCCAAGCCTTCCCCCTCTCACCATCAGCAACCATGAT
GTGATCTTGTGGCTGGGGGACCTCAACTACAGGATAGAAGAGCTGGATGTGGAAAAAGTG
AAAAAGCTCATCGAAGAGAAGGACTTTCAAATGCTGTATGCATATGATCAGCTGAAAATT
CAGGTGGCCGCAAAGACTGTCTTTGAAGGCTTCACAGAGGGTGAGCTCACATTCCAGCCT
ACTTACAAGTATGATACGGGCTCTGACGACTGGGATACCAGTGAGAAGTGCCGTGCTCCT
GCCTGGTGTGATCGGATTCTCTGGAAAGGGAAGAACATCACTCAGCTGAGTTACCAGAGC
CACATGGCCCTGAAGACCAGTGACCACAAGCCTGTCAGCTCAGTGTTTGACATCGGGGTG
AGGGTCGTAAATGACGAGCTTTACCGGAAGACACTGGAGGAAATTGTTCGCTCCCTGGAT
AAGATGGAAAATGCCAACATTCCTTCTGTGTCCCTGTCCAAGCGAGAGTTCTGTTTTCAG
AATGTGAAGTACATGCAATTGAAAGTAGAATCCTTTACAATTCATAATGGACAAGTACCC
TGTCATTTTGAATTCATCAACAAGCCTGATGAAGAGTCTTACTGTAAGCAGTGGCTGAAT
GCCAACCCCAGCAGAGGCTTCCTCCTGCCAGATTCTGATGTTGAGATTGACTTGGAGCTC
TTCGTAAATAAGATGACAGCTACAAAGCTCAACTCGGGTGAAGACAAAATTGAGGACATT
CTGGTTCTGCACTTGGACAGGGGAAAGGATTACTTTTTGTCTGTGTCTGGGAACTACCTG
CCCAGCTGTTTTGGGTCTCCCATTCATACACTGTGTTACATGAGAGAGCCAATCTTGGAC
CTACCACTTGAAACCATTAGTGAGCTGACTCTGATGCCAGTATGGACTGGAGATGATGGG
AGCCAGTTGGATAGCCCCATGGAAATCCCCAAAGAGCTCTGGATGATGGTTGATTACCTG
TACCGAAATGCTGTCCAGCAGGAAGATCTGTTTCAGCAACCAGGCCTGAGGTCAGAATTT
GAACATATCAGGGACTGCTTGGATACTGGAATGATTGATAACCTCTCTGCCAGCAATCAT
TCTGTAGCCGAAGCCCTGCTGCTTTTCCTGGAGAGCCTTCCAGAGCCTGTCATCTGTTAC
AGCACCTACCATAACTGCTTGGAGTGTTCTGGCAACTACACAGCAAGCAAACAGGTCATT
TCTACTCTCCCCATATTCCACAAAAATGTCTTCCACTACTTGATGGCGTTTTTGCGAGAA
CTGCTGAAAAATTCAGCAAAAAATCATTTGGATGAGAATATTCTAGCTAGCATATTTGGC
AGCTTATTGCTTCGAAACCCAGCTGGTCACCAAAAGCTTGATATGACAGAGAAGAAGAAG
GCTCAAGAATTTATTCACCAGTTCCTCTGCAACCCACTCTGA
|
| Enzyme 18 GenBank Gene ID |
AL603790  |
| Enzyme 18 GeneCard ID |
INPP5B  |
| Enzyme 18 GenAtlas ID |
INPP5B  |
| Enzyme 18 HGNC ID |
HGNC:6077  |
| Enzyme 18 Chromosome Location |
1 |
| Enzyme 18 Locus |
1p34 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Jefferson AB, Majerus PW: Properties of type II inositol polyphosphate 5-phosphatase. J Biol Chem. 1995 Apr 21;270(16):9370-7. [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
]
- 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
]
- Ross TS, Jefferson AB, Mitchell CA, Majerus PW: Cloning and expression of human 75-kDa inositol polyphosphate-5-phosphatase. J Biol Chem. 1991 Oct 25;266(30):20283-9. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
8868 |
| Enzyme 19 Name |
Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma |
| Enzyme 19 Synonyms |
- PIP5K1-gamma
- PtdIns(4)P-5-kinase 1 gamma
- Phosphatidylinositol-4-phosphate 5-kinase type I gamma
- PIP5KIgamma
|
| Enzyme 19 Gene Name |
PIP5K1C |
| Enzyme 19 Protein Sequence |
>Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma
MELEVPDEAESAEAGAVPSEAAWAAESGAAAGLAQKKAAPTEVLSMTAQPGPGHGKKLGH
RGVDASGETTYKKTTSSTLKGAIQLGIGYTVGHLSSKPERDVLMQDFYVVESIFFPSEGS
NLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSLFYVT
SDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNN
ILPRVVKMHLKFDLKGSTYKRRASKKEKEKSFPTYKDLDFMQDMPEGLLLDADTFSALVK
TLQRDCLVLESFKIMDYSLLLGVHNIDQHERERQAQGAQSTSDEKRPVGQKALYSTAMES
IQGGAARGEAIESDDTMGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVHDG
DTVSVHRPSFYAERFFKFMSNTVFRKNSSLKSSPSKKGRGGALLAVKPLGPTAAFSASQI
PSEREEAQYDLRGARSYPTLEDEGRPDLLPCTPPSFEEATTASIATTLSSTSLSIPERSP
SETSEQPRYRRRTQSSGQDGRPQEEPPAEEDLQQITVQVEPACSVEIVVPKEEDAGVEAS
PAGASAAVEVETASQASDEEGAPASQASDEEDAPATDIYFPTDERSWVYSPLHYSAQAPP
ASDGESDT
|
| Enzyme 19 Number of Residues |
668 |
| Enzyme 19 Molecular Weight |
73259.3 |
| Enzyme 19 Theoretical pI |
4.94 |
| Enzyme 19 GO Classification |
| Function |
- catalytic activity
- kinase activity
- lipid kinase activity
- phosphatidylinositol phosphate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- glycerophospholipid metabolic process
- metabolic process
- organophosphate metabolic process
- phosphatidylinositol metabolic process
- phosphoinositide metabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 19 General Function |
Involved in phosphatidylinositol phosphate kinase activity |
| Enzyme 19 Specific Function |
Plays a role in membrane ruffling and assembly of clathrin-coated pits at the synapse. Mediates RAC1-dependent reorganization of actin filaments. Participates in the biosynthesis of phosphatidylinositol-4,5-bisphosphate |
| Enzyme 19 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 19 Reactions |
- ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [RN:R03469]
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
31317309  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
O60331  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
PI51C_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>2007 bp
ATGGAGCTGGAGGTACCGGACGAGGCGGAGAGCGCTGAGGCGGGGGCCGTGCCCTCGGAG
GCGGCGTGGGCGGCAGAGAGCGGGGCGGCGGCAGGTTTGGCTCAGAAGAAGGCGGCCCCA
ACAGAGGTTCTGTCCATGACGGCACAGCCGGGCCCTGGCCATGGGAAGAAGTTGGGCCAT
CGAGGTGTGGACGCATCCGGCGAAACCACCTACAAGAAGACCACCTCCTCCACCCTGAAG
GGTGCCATCCAGCTGGGCATCGGCTACACCGTGGGCCACCTGAGCTCCAAGCCCGAACGC
GACGTGCTCATGCAGGACTTCTACGTGGTGGAGAGCATCTTCTTCCCCAGCGAAGGCAGC
AACCTCACCCCCGCCCACCACTTCCAGGACTTCCGCTTCAAGACCTATGCACCTGTCGCC
TTCCGCTACTTCCGGGAGCTCTTTGGGATCCGGCCAGATGATTACTTGTACTCCCTGTGC
AATGAGCCGCTGATCGAGCTGTCCAACCCGGGCGCCAGTGGCTCCCTCTTCTACGTCACC
AGCGACGACGAGTTCATCATCAAGACCGTCATGCACAAGGAGGCCGAGTTCCTGCAGAAG
CTGCTCCCTGGCTACTACATGAACCTCAACCAGAACCCGCGGACGCTGCTGCCCAAGTTC
TATGGGCTGTACTGCGTGCAGTCGGGGGGCAAGAACATCCGCGTCGTGGTCATGAACAAC
ATCCTGCCCCGCGTGGTCAAGATGCACCTCAAGTTCGACCTCAAGGGCTCCACCTACAAG
CGGCGCGCCAGCAAGAAGGAGAAGGAGAAGAGCTTCCCCACCTACAAGGACCTGGACTTC
ATGCAGGACATGCCCGAGGGGCTCCTGCTGGACGCCGACACCTTCAGCGCCCTGGTCAAG
ACGCTGCAGCGGGACTGCCTGGTCCTGGAAAGTTTCAAGATCATGGACTACAGCCTGCTG
CTGGGCGTGCACAACATCGACCAGCACGAGCGCGAGCGGCAGGCGCAGGGCGCCCAGAGC
ACCTCAGATGAGAAGCGGCCTGTGGGCCAGAAGGCGCTCTACTCCACGGCCATGGAGTCC
ATCCAGGGTGGCGCCGCGCGCGGGGAGGCCATCGAATCGGATGACACGATGGGCGGGATC
CCCGCTGTGAACGGCCGCGGGGAGCGGCTGCTGCTGCACATTGGCATCATCGACATCCTG
CAGTCCTACAGGTTCATCAAGAAACTGGAGCACACCTGGAAGGCCCTCGTCCACGATGGG
GACACGGTGTCCGTCCACCGCCCCAGCTTCTATGCCGAGCGCTTTTTCAAGTTCATGAGC
AACACGGTCTTTCGGAAGAACTCCTCCCTGAAGTCCTCGCCCTCCAAGAAGGGGCGCGGC
GGAGCCTTGCTAGCTGTGAAACCGCTGGGGCCCACCGCTGCCTTCTCGGCCAGCCAGATC
CCTAGCGAGCGGGAGGAGGCCCAGTACGACCTGCGGGGGGCCCGCAGCTACCCCACGCTG
GAGGACGAAGGCCGGCCCGACCTCCTGCCCTGCACGCCACCTTCTTTCGAAGAAGCCACT
ACAGCCTCCATTGCCACGACTCTGTCATCCACATCCCTCTCCATTCCTGAGCGGTCCCCC
TCGGAGACGTCGGAGCAGCCGCGGTACAGGCGGCGCACACAGTCGTCTGGACAGGATGGC
AGGCCGCAGGAGGAGCCACCCGCGGAAGAGGATCTGCAGCAGATTACAGTGCAGGTGGAG
CCTGCGTGCAGCGTGGAGATTGTGGTCCCCAAAGAGGAGGACGCAGGGGTGGAGGCTTCC
CCGGCCGGTGCCTCTGCTGCTGTTGAAGTAGAAACTGCCAGCCAGGCCTCAGACGAGGAG
GGCGCACCTGCCAGCCAGGCCTCGGACGAGGAGGACGCGCCCGCCACCGACATCTACTTT
CCCACCGATGAGAGGAGCTGGGTGTACTCCCCGCTCCACTATAGCGCCCAGGCCCCCCCG
GCCTCCGACGGCGAGAGCGACACATAA
|
| Enzyme 19 GenBank Gene ID |
NM_012398.2  |
| Enzyme 19 GeneCard ID |
PIP5K1C  |
| Enzyme 19 GenAtlas ID |
PIP5K1C  |
| Enzyme 19 HGNC ID |
HGNC:8996  |
| Enzyme 19 Chromosome Location |
1 |
| Enzyme 19 Locus |
19p13.3 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- 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
]
- 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
]
- Di Paolo G, Pellegrini L, Letinic K, Cestra G, Zoncu R, Voronov S, Chang S, Guo J, Wenk MR, De Camilli P: Recruitment and regulation of phosphatidylinositol phosphate kinase type 1 gamma by the FERM domain of talin. Nature. 2002 Nov 7;420(6911):85-9. [PubMed
]
- Doughman RL, Firestone AJ, Wojtasiak ML, Bunce MW, Anderson RA: Membrane ruffling requires coordination between type Ialpha phosphatidylinositol phosphate kinase and Rac signaling. J Biol Chem. 2003 Jun 20;278(25):23036-45. Epub 2003 Apr 6. [PubMed
]
- Krauss M, Kinuta M, Wenk MR, De Camilli P, Takei K, Haucke V: ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Igamma. J Cell Biol. 2003 Jul 7;162(1):113-24. [PubMed
]
- Narkis G, Ofir R, Landau D, Manor E, Volokita M, Hershkowitz R, Elbedour K, Birk OS: Lethal contractural syndrome type 3 (LCCS3) is caused by a mutation in PIP5K1C, which encodes PIPKI gamma of the phophatidylinsitol pathway. Am J Hum Genet. 2007 Sep;81(3):530-9. Epub 2007 Jul 24. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
9581 |
| Enzyme 20 Name |
Phosphatidylinositol 3-kinase catalytic subunit type 3 |
| Enzyme 20 Synonyms |
- PI3-kinase type 3
- PI3K type 3
- PtdIns-3-kinase type 3
- Phosphatidylinositol 3-kinase p100 subunit
- Phosphoinositide-3-kinase class 3
- hVps34
|
| Enzyme 20 Gene Name |
PIK3C3 |
| Enzyme 20 Protein Sequence |
>Phosphatidylinositol 3-kinase catalytic subunit type 3
MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVT
CQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAV
PVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTK
AHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDG
DESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIV
SYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDV
EDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKK
DSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLI
SRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRS
LLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVK
IRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRK
ENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAE
VMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLN
KEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVK
KVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK
|
| Enzyme 20 Number of Residues |
887 |
| Enzyme 20 Molecular Weight |
101548.6 |
| Enzyme 20 Theoretical pI |
6.79 |
| Enzyme 20 GO Classification |
| Function |
- 1-phosphatidylinositol-3-kinase activity
- binding
- catalytic activity
- inositol or phosphatidylinositol kinase activity
- kinase activity
- lipid kinase activity
- phosphoinositide 3-kinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biological regulation
- glycerophospholipid metabolic process
- intracellular signal transduction
- metabolic process
- organophosphate metabolic process
- phosphoinositide metabolic process
- phosphoinositide phosphorylation
- phosphoinositide-mediated signaling
- phospholipid metabolic process
- regulation of biological process
- regulation of cellular process
- second-messenger-mediated signaling
- signal transduction
|
| Component |
- macromolecular complex
- phosphoinositide 3-kinase complex
- protein complex
|
|
| Enzyme 20 General Function |
Involved in binding |
| Enzyme 20 Specific Function |
Catalytic subunit of the PI3K complex. Involved in the transport of lysosomal enzyme precursors to lysosomes |
| Enzyme 20 Pathways |
|
| Enzyme 20 Reactions |
- ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate [RN:R03362]
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
987948  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q8NEB9  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
PK3C3_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>2664 bp
ATGGGGGAAGCAGAGAAGTTTCACTACATCTATAGTTGTGACCTGGATATCAACGTCCAG
CTTAAGATAGGAAGCTTGGAAGGGAAGAGAGAACAAAAGAGTTATAACGCTGTCCTGGAA
GACCCAATGTTGAAGTTCTCAGGACTATATCAAGAGACATGCTCTGATCTTTATGTTACT
TGTCAAGTTTTTGCAGAAGGGAAGCCTTCGGCCTTGCCAGTGAGAACATCCTACAAAGCA
TTTAGTACAAGATGGAACTGGAATGAATGGCTGAAACTACCAGTAAAATACCCTGACCTG
CCCAGGAATGCCCAAGTGGCCCTCACCATATGGGATGTGTATGGTCCCGGAAAAGCAGTG
CCTGTAGGAGGAACAACGGTTTCGCTCTTTGGAAAATACGGCATGTCTCGCCAAGGGATG
CATGACTTGAAAGTCTGGCCTAATGTAGAAGCAGATGGATCAGAACCCACAAATACTCCT
GGCAGAACAAGTAGCACTCTCTCAGAAGATCAGATGAGCCGTCTTGCCAAGCTCACCAAA
GCTCATCGACAAGGACACATGGTGAAAGTAGATTGGCTGGATAGATTGACATTTAGAGAA
ATAGAAATGATAAATGAGAGTGTGAAACGAAGTTCTAATTTCATGTACCTGATGGGTGGA
TTTCGATGTGTCAAGTGTGATGATAAGGAATATGGTATTGTTTATTATGAAAAGGACGGT
GATGAATCATCTCCAATTTTAACAAGTTTTGAATTAGTGAAAGTTCCTGACCCCCAGATG
TCCCTGGAGAATTTAGTTGAGAGCAAACACCACAACCTTCCCCGGAGTTTAAGAAGTGGA
CCTTCTGACCACGATCTGAAACCCTATCCTTCCCCGAGAGATCAGTTAAAAAATATTGTG
AGTTATCCTCCATCCAAGCCACCCACATATGAAGAACAAGATCTTGTTTGGGAGTTTAGA
TATTATCTTACGAATCAAGATAAAGCCTTGACCAAAATCCTGACATCTGTTATTTGGGAT
CTACCTCAGGGGGCCAAACAGGCCTTGGCACTTCTGGGGAAATGGAACCCGATGGATGTA
GAGGACTCCTTGGAGCTGATATCCTCTCATTACACCAACCCAACTGTGAGGCGTTATGCT
GTTGCCCGGTTGCGACAGGCCGATGATGAGGATTTGTTGATGTACCTATCACAATTGGTC
CAGGCTCTCAAATATGAAAATTTTGATGATATAAAGAATGGATTGGAACCTACCAAGAAG
GATAGTCAGAGTTCAGTGTCAGGAAATGTGTCAAATTCTGGAATAAATTCTGCAGAAATA
GATAGCTCCCAAATTATAACCAGCCCCCTTCCTTCAGTCTCTTCACCTCCTCCTGCATCA
AAAACAAAAGAAGTTCCAGATGGCGAAAATCTGGAACAAGATCTCTGTACCTTCTTGATA
TCGAGAGCCTCCAAAAACTCAACACTGGCTAATTATTTATACTGGTATGTGATAGTGGAA
TGTGAAGATCAAGATACTCAGCAGAGAGATCCAAAGACCCATGAGATGTACTTGAACGTA
ATGAGAAGATTCAGCCAAGCATTGTTGAAGGGTGATAAGTCTGTCAGAGTTATGCGTTCT
TTGCTGGCTGCACAACAGACATTTGTAGATCGGTTGGTGCATCTAATGAAGGCAGTACAA
CGCGAAAGTGGAAATCGTAAGAAAAAGAATGAGAGACTACAGGCATTGCTTGGAGATAAT
GAAAAGATGAATTTGTCAGATGTGGAACTTATCCCGTTGCCTTTAGAACCCCAAGTGAAA
ATTAGAGGAATAATTCCGGAAACAGCTACACTGTTTAAAAGTGCCCTTATGCCTGCACAG
TTGTTTTTTAAGACGGAAGATGGAGGCAAATATCCAGTTATATTTAAGCATGGAGATGAT
TTACGTCAAGATCAACTTATTCTTCAAATCATTTCACTCATGGACAAGCTGTTACGGAAA
GAAAATCTGGACTTGAAATTGACACCTTATAAGGTGTTAGCCACCAGTACAAAACATGGC
TTCATGCAGTTTATCCAGTCAGTTCCTGTGGCTGAAGTTCTTGATACAGAGGGAAGCATT
CAGAACTTTTTTAGAAAATATGCACCAAGTGAGAATGGGCCAAATGGGATTAGTGCTGAG
GTCATGGACACTTACGTTAAAAGCTGTGCTGGATATTGCGTGATCACCTATATACTTGGA
GTTGGAGACAGGCACCTGGATAACCTTGTGCTAACAAAAACAGGCAAACTCTTCCACATA
GACTTTGGATATATTTTGGGTCGGGATCCAAAGCCTCTTCCTCCACCAATGAAGCTGAAT
AAAGAAATGGTAGAAGGAATGGGGGGCACACAGAGTGAGCAGTACCAAGAGTTCCGTAAA
CAGTGTTACACGGCTTTCCTCCACCTGCGGAGGTATTCTAATCTGATTTTGAACTTGTTT
TCCTTGATGGTTGATCCAAACATTCCAGATATTGCACTTGAACCAGATAAAACTGTGAAA
AAGGTTCAGGATAAATTCCGCTTAGACCTGTCGGATGAAGAGGCTGTGCATTACATGCAG
AGTCTGATTGATGAGAGTGTCCATGCTCTTTTTGCTGCAGTGGTGGAACAGATTCACAAG
TTTGCCCAGTACTGGAGAAAATGA
|
| Enzyme 20 GenBank Gene ID |
Z46973  |
| Enzyme 20 GeneCard ID |
PIK3C3  |
| Enzyme 20 GenAtlas ID |
PIK3C3  |
| Enzyme 20 HGNC ID |
HGNC:8974  |
| Enzyme 20 Chromosome Location |
1 |
| Enzyme 20 Locus |
18q12.3 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Volinia S, Dhand R, Vanhaesebroeck B, MacDougall LK, Stein R, Zvelebil MJ, Domin J, Panaretou C, Waterfield MD: A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system. EMBO J. 1995 Jul 17;14(14):3339-48. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [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
]
- Sun Q, Fan W, Chen K, Ding X, Chen S, Zhong Q: Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase. Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19211-6. Epub 2008 Dec 2. [PubMed
]
- 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
]
- Matsunaga K, Saitoh T, Tabata K, Omori H, Satoh T, Kurotori N, Maejima I, Shirahama-Noda K, Ichimura T, Isobe T, Akira S, Noda T, Yoshimori T: Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages. Nat Cell Biol. 2009 Apr;11(4):385-96. Epub 2009 Mar 8. [PubMed
]
- 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 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
9668 |
| Enzyme 21 Name |
Phosphatidylinositol-5-phosphate 4-kinase type-2 gamma |
| Enzyme 21 Synonyms |
- Phosphatidylinositol-5-phosphate 4-kinase type II gamma
- PI(5)P 4-kinase type II gamma
- PIP4KII-gamma
|
| Enzyme 21 Gene Name |
PIP4K2C |
| Enzyme 21 Protein Sequence |
>Phosphatidylinositol-5-phosphate 4-kinase type-2 gamma
MASSSVPPATVSAATAGPGPGFGFASKTKKKHFVQQKVKVFRAADPLVGVFLWGVAHSIN
ELSQVPPPVMLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFGIDDQ
DYLVSLTRNPPSESEGSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNT
LLPQFLGMYRVSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTL
KDMDFLNKNQKVYIGEEEKKIFLEKLKRDVEFLVQLKIMDYSLLLGIHDIIRGSEPEEEG
PVREDESEVDGDCSLTGPPALVGSYGTSPEGIGGYIHSHRPLGPGEFESFIDVYAIRSAE
GAPQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITNIF
A
|
| Enzyme 21 Number of Residues |
421 |
| Enzyme 21 Molecular Weight |
47285.5 |
| Enzyme 21 Theoretical pI |
6.84 |
| Enzyme 21 GO Classification |
| Function |
- catalytic activity
- kinase activity
- lipid kinase activity
- phosphatidylinositol phosphate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- glycerophospholipid metabolic process
- metabolic process
- organophosphate metabolic process
- phosphatidylinositol metabolic process
- phosphoinositide metabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 21 General Function |
Involved in phosphatidylinositol phosphate kinase activity |
| Enzyme 21 Specific Function |
May play an important role in the production of Phosphatidylinositol bisphosphate (PIP2), in the endoplasmic reticulum |
| Enzyme 21 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
- Regulation of actin cytoskeleton (map04810
)
|
| Enzyme 21 Reactions |
- ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [RN:R05803]
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
226371739  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q8TBX8  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
PI42C_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>1266 bp
ATGGCGTCCTCCTCGGTCCCACCAGCCACGGTATCGGCGGCGACAGCAGGCCCCGGCCCA
GGTTTCGGCTTCGCCTCCAAGACCAAGAAGAAGCATTTCGTGCAGCAGAAGGTGAAGGTG
TTCCGGGCGGCCGACCCGCTGGTGGGTGTGTTCCTGTGGGGCGTAGCCCACTCGATCAAT
GAGCTCAGCCAGGTGCCTCCCCCGGTGATGCTGCTGCCAGATGACTTTAAGGCCAGCTCC
AAGATCAAGGTCAACAATCACCTTTTCCACAGGGAAAATCTGCCCAGTCATTTCAAGTTC
AAGGAGTATTGTCCCCAGGTCTTCAGGAACCTCCGTGATCGATTTGGCATTGATGACCAA
GATTACTTGGTGTCCCTTACCCGAAACCCCCCCAGCGAAAGTGAAGGCAGTGATGGTCGC
TTCCTTATCTCCTACGATCGGACTCTGGTCATCAAAGAAGTATCCAGTGAGGACATTGCT
GACATGCATAGCAACCTCTCCAACTATCACCAGTACATTGTGAAGTGCCATGGCAACACG
CTTCTGCCCCAGTTCCTGGGGATGTACCGAGTCAGTGTGGACAACGAAGACAGCTACATG
CTTGTGATGCGCAATATGTTTAGCCACCGTCTTCCTGTGCACAGGAAGTATGACCTCAAG
GGTTCCCTAGTGTCCCGGGAAGCCAGCGATAAGGAAAAGGTTAAAGAATTGCCCACCCTT
AAGGATATGGACTTTCTCAACAAGAACCAGAAAGTATATATTGGTGAAGAGGAGAAGAAA
ATATTTCTGGAGAAGCTGAAGAGAGATGTGGAGTTTCTAGTGCAGCTGAAGATCATGGAC
TACAGCCTTCTGCTAGGCATCCACGACATCATTCGGGGCTCTGAACCAGAGGAGGAAGCG
CCCGTGCGGGAGGATGAGTCAGAGGTGGATGGGGACTGCAGCCTGACTGGACCTCCTGCT
CTGGTGGGCTCCTATGGCACCTCCCCAGAGGGTATCGGAGGCTACATCCATTCCCATCGG
CCCCTGGGCCCAGGAGAGTTTGAGTCCTTCATTGATGTCTATGCCATCCGGAGTGCTGAA
GGAGCCCCCCAGAAGGAGGTCTACTTCATGGGCCTCATTGATATCCTTACACAGTATGAT
GCCAAGAAGAAAGCAGCTCATGCAGCCAAAACTGTCAAGCATGGGGCTGGGGCAGAGATC
TCTACTGTCCATCCGGAGCAGTATGCTAAGCGATTCCTGGATTTTATTACCAACATCTTT
GCCTAA
|
| Enzyme 21 GenBank Gene ID |
NM_001146258.1  |
| Enzyme 21 GeneCard ID |
PIP4K2C  |
| Enzyme 21 GenAtlas ID |
PIP4K2C  |
| Enzyme 21 HGNC ID |
HGNC:23786  |
| Enzyme 21 Chromosome Location |
1 |
| Enzyme 21 Locus |
12q13.3 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 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
]
- 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
]
- 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 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
10047 |
| Enzyme 22 Name |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4 |
| Enzyme 22 Synonyms |
- hPLCD4
- Phosphoinositide phospholipase C-delta-4
- Phospholipase C-delta-4
- PLC-delta-4
|
| Enzyme 22 Gene Name |
PLCD4 |
| Enzyme 22 Protein Sequence |
>1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
MASLLQDQLTTDQDLLLMQEGMPMRKVRSKSWKKLRYFRLQNDGMTVWHARQARGSAKPS
FSISDVETIRNGHDSELLRSLAEELPLEQGFTIVFHGRRSNLDLMANSVEEAQIWMRGLQ
LLVDLVTSMDHQERLDQWLSDWFQRGDKNQDGKMSFQEVQRLLHLMNVEMDQEYAFSLFQ
AADTSQSGTLEGEEFVQFYKALTKRAEVQELFESFSADGQKLTLLEFLDFLQEEQKERDC
TSELALELIDRYEPSDSGKLRHVLSMDGFLSYLCSKDGDIFNPACLPIYQDMTQPLNHYF
ICSSHNTYLVGDQLCGQSSVEGYIRALKRGCRCVEVDVWDGPSGEPVVYHGHTLTSRILF
KDVVATVAQYAFQTSDYPVILSLETHCSWEQQQTMARHLTEILGEQLLSTTLDGVLPTQL
PSPEELRRKILVKGKKLTLEEDLEYEEEEAEPELEESELALESQFETEPEPQEQNLQNKD
KKKKSKPILCPALSSLVIYLKSVSFRSFTHSKEHYHFYEISSFSETKAKRLIKEAGNEFV
QHNTWQLSRVYPSGLRTDSSNYNPQELWNAGCQMVAMNMQTAGLEMDICDGHFRQNGGCG
YVLKPDFLRDIQSSFHPEKPISPFKAQTLLIQVISGQQLPKVDKTKEGSIVDPLVKVQIF
GVRLDTARQETNYVENNGFNPYWGQTLCFRVLVPELAMLRFVVMDYDWKSRNDFIGQYTL
PWTCMQQGYRHIHLLSKDGISLRPASIFVYICIQEGLEGDES
|
| Enzyme 22 Number of Residues |
762 |
| Enzyme 22 Molecular Weight |
87584.5 |
| Enzyme 22 Theoretical pI |
4.85 |
| Enzyme 22 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 22 General Function |
Involved in calcium ion binding |
| Enzyme 22 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 22 Pathways |
|
| Enzyme 22 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
62897967  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q9BRC7  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
PLCD4_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 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 22 GenBank Gene ID |
AK223203  |
| Enzyme 22 GeneCard ID |
PLCD4  |
| Enzyme 22 GenAtlas ID |
PLCD4  |
| Enzyme 22 HGNC ID |
HGNC:9062  |
| Enzyme 22 Chromosome Location |
2 |
| Enzyme 22 Locus |
2q35 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 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 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
10050 |
| Enzyme 23 Name |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3 |
| Enzyme 23 Synonyms |
- Phosphoinositide phospholipase C-delta-3
- Phospholipase C-delta-3
- PLC-delta-3
|
| Enzyme 23 Gene Name |
PLCD3 |
| Enzyme 23 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 23 Number of Residues |
789 |
| Enzyme 23 Molecular Weight |
89257.5 |
| Enzyme 23 Theoretical pI |
6.97 |
| Enzyme 23 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 23 General Function |
Involved in calcium ion binding |
| Enzyme 23 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 23 Pathways |
|
| Enzyme 23 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
Not Available |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q8N3E9  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
PLCD3_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 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 23 GenBank Gene ID |
AK074240  |
| Enzyme 23 GeneCard ID |
PLCD3  |
| Enzyme 23 GenAtlas ID |
PLCD3  |
| Enzyme 23 HGNC ID |
HGNC:9061  |
| Enzyme 23 Chromosome Location |
1 |
| Enzyme 23 Locus |
17q21.31 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 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 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
13065 |
| Enzyme 24 Name |
Protein-tyrosine phosphatase mitochondrial 1 |
| Enzyme 24 Synonyms |
- PTEN-like phosphatase
- Phosphoinositide lipid phosphatase
|
| Enzyme 24 Gene Name |
PTPMT1 |
| Enzyme 24 Protein Sequence |
>Protein-tyrosine phosphatase mitochondrial 1
MAATALLEAGLARVLFYPTLLYTLFRGKVPGRAHRDWYHRIDPTVLLGALPLRSLTRQLV
QDENVRGVITMNEEYETRFLCNSSQEWKRLGVEQLRLSTVDMTGIPTLDNLQKGVQFALK
YQSLGQCVYVHCKAGRSRSATMVAAYLIQVHKWSPEEAVRAIAKIRSYIHIRPGQLDVLK
EFHKQITARATKDGTFVISKT
|
| Enzyme 24 Number of Residues |
201 |
| Enzyme 24 Molecular Weight |
22843.4 |
| Enzyme 24 Theoretical pI |
10.24 |
| Enzyme 24 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphatase activity
- phosphoprotein phosphatase activity
- phosphoric ester hydrolase activity
- protein tyrosine phosphatase activity
- protein tyrosine/serine/threonine phosphatase activity
|
| Process |
- cellular metabolic process
- dephosphorylation
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- protein amino acid dephosphorylation
|
| Component |
| — |
|
| Enzyme 24 General Function |
Involved in phosphatase activity |
| Enzyme 24 Specific Function |
Protein phosphatase that specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production. Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues. Probably involved in regulation of insulin secretion in pancreatic beta cells |
| Enzyme 24 Pathways |
- Epithelial cell signaling in Helicobacter pylori infection (map05120
)
- Insulin signaling pathway (map04910
)
- Leukocyte transendothelial migration (map04670
)
- MAPK signaling pathway (map04010
)
- Natural killer cell mediated cytotoxicity (map04650
)
- Progesterone-mediated oocyte maturation (map04914
)
- Cell cycle (map04110
)
- Cell cycle - yeast (map04111
)
- Cell adhesion molecules (CAMs) (map04514
)
- Adherens junction (map04520
)
- Jak-STAT signaling pathway (map04630
)
- T cell receptor signaling pathway (map04660
)
- B cell receptor signaling pathway (map04662
)
- Adipocytokine signaling pathway (map04920
)
- Type I diabetes mellitus (map04940
)
- Renal cell carcinoma (map05211
)
- Chronic myeloid leukemia (map05220
)
|
| Enzyme 24 Reactions |
- protein tyrosine phosphate + H2O = protein tyrosine + phosphate [RN:R02585]
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
148224884  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q8WUK0  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
PTPM1_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>606 bp
ATGGCGGCCACCGCGCTGCTGGAGGCCGGCCTGGCGCGGGTGCTCTTCTACCCGACGCTG
CTCTACACCCTGTTCCGCGGGAAGGTGCCGGGTCGGGCGCACCGGGACTGGTACCACCGC
ATCGACCCCACCGTGCTGCTGGGCGCGCTGCCGTTGCGGAGCTTGACGCGCCAGCTGGTA
CAGGACGAGAACGTGCGCGGGGTGATCACCATGAACGAGGAGTACGAGACGAGGTTCCTG
TGCAACTCTTCACAGGAGTGGAAGAGACTAGGAGTCGAGCAGCTGCGGCTCAGCACAGTA
GACATGACTGGGATCCCCACCTTGGACAACCTCCAGAAGGGAGTCCAATTTGCTCTCAAG
TACCAGTCGCTGGGCCAGTGTGTTTACGTGCATTGTAAGGCTGGGCGCTCCAGGAGTGCC
ACTATGGTGGCAGCATACCTGATTCAGGTGCACAAATGGAGTCCAGAGGAGGCTGTAAGA
GCCATCGCCAAGATCCGGTCATACATCCACATCAGGCCTGGCCAGCTGGATGTTCTTAAA
GAGTTCCACAAGCAGATTACTGCACGGGCAACAAAGGATGGGACTTTTGTCATTTCAAAG
ACATGA
|
| Enzyme 24 GenBank Gene ID |
NM_175732.2  |
| Enzyme 24 GeneCard ID |
PTPMT1  |
| Enzyme 24 GenAtlas ID |
PTPMT1  |
| Enzyme 24 HGNC ID |
HGNC:26965  |
| Enzyme 24 Chromosome Location |
1 |
| Enzyme 24 Locus |
11p11.2 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 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 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
15318 |
| Enzyme 25 Name |
cDNA FLJ76965, highly similar to Homo sapiens phosphatidylinositol-4- phosphate 5-kinase, type I, beta (PIP5K1B), transcript variant 2, mRNA (Phosphatidylinositol-4-phosphate 5-kinase, type I, beta, isoform CRA_a) |
| Enzyme 25 Synonyms |
Not Available |
| Enzyme 25 Gene Name |
PIP5K1B |
| Enzyme 25 Protein Sequence |
>cDNA FLJ76965, highly similar to Homo sapiens phosphatidylinositol-4- phosphate 5-kinase, type I, beta (PIP5K1B), transcript variant 2, mRNA (Phosphatidylinositol-4-phosphate 5-kinase, type I, beta, isoform CRA_a)
MSSAAENGEAAPGKQNEEKTYKKTASSAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVV
ESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNP
GASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGG
INIRIVVMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQDMHEGLYF
DTETYNALMKTLQRDCRVLESFKIMDYSLLLGIHFLDHSLKEKEEETPQNVPDAKRTGMQ
KVLYSTAMESIQGPGKSGDGIITENPDTMGGIPAKSHRGEKLLLFMGIIDILQSYRLMKK
LEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKIQALKASPSKKRCNSIAALKAT
SQEIVSSISQEWKDEKRDLLTEGQSFSSLDEEALGSRHRPDLVPSTPSLFEAASLATTIS
SSSLYVNEHYPHDRPTLYSNSKGLPSSSTFTLEEGTIYLTAEPNTLEVQDDNASVLDVYL
|
| Enzyme 25 Number of Residues |
540 |
| Enzyme 25 Molecular Weight |
61037 |
| Enzyme 25 Theoretical pI |
6.85 |
| Enzyme 25 GO Classification |
Not Available |
| Enzyme 25 General Function |
Not Available |
| Enzyme 25 Specific Function |
Not Available |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
Not Available |
| Enzyme 25 Pfam Domain Function |
Not Available |
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
158258905  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
A8K9L9  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
A8K9L9_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>1623 bp
ATGTCTTCTGCTGCTGAAAATGGAGAGGCAGCACCTGGAAAACAAAATGAAGAAAAAACC
TATAAAAAGACTGCATCATCTGCTATTAAAGGTGCTATTCAGCTGGGAATAGGATACACA
GTGGGTAATCTCACTTCCAAGCCAGAACGAGATGTTCTTATGCAAGACTTTTATGTGGTG
GAAAGTGTGTTCCTACCCAGCGAAGGGAGCAATCTGACCCCAGCACATCACTACCCAGAC
TTTAGATTTAAGACATACGCTCCATTAGCATTCCGATATTTCAGAGAACTTTTTGGTATC
AAGCCTGATGATTACTTGTATTCCATCTGCAGTGAACCTCTAATAGAACTGTCTAACCCT
GGAGCCAGTGGATCCTTGTTTTTTGTGACCAGTGATGATGAATTTATCATCAAAACAGTT
CAGCACAAAGAAGCTGAGTTTCTTCAGAAGCTACTGCCAGGCTATTACATGAATTTAAAC
CAGAATCCAAGGACTCTTTTGCCAAAATTTTACGGACTGTATTGTATGCAATCAGGAGGC
ATTAATATCAGGATTGTGGTGATGAACAACGTTTTGCCACGCTCCATGAGAATGCACTTT
ACATATGACTTGAAAGGCTCAACGTATAAGCGAAGAGCATCCCGTAAAGAGAGAGAGAAA
TCCAACCCCACATTTAAGGACTTAGATTTCCTGCAAGACATGCACGAAGGGTTGTATTTT
GATACGGAAACATACAACGCGCTTATGAAAACACTTCAGAGAGACTGCCGGGTGCTAGAA
AGCTTCAAGATCATGGATTATAGCCTTCTGTTGGGAATTCATTTCCTGGACCATTCCCTC
AAAGAGAAAGAGGAGGAGACCCCACAAAATGTGCCTGATGCTAAGCGGACTGGGATGCAG
AAGGTTCTCTACTCAACAGCCATGGAATCTATCCAGGGTCCAGGGAAATCTGGAGATGGG
ATAATCACAGAGAACCCAGACACAATGGGAGGCATTCCAGCTAAAAGCCATAGGGGAGAA
AAACTACTTTTATTTATGGGCATTATTGACATTCTGCAATCATATAGGTTAATGAAGAAG
TTAGAACATTCCTGGAAAGCTCTTGTTTATGATGGGGACACTGTTTCTGTTCATAGACCA
AGCTTTTATGCAGACAGATTTCTTAAGTTCATGAATTCCAGAGTTTTCAAGAAAATTCAA
GCTTTGAAGGCTTCACCGTCTAAGAAACGGTGCAATTCAATCGCCGCCCTAAAGGCCACT
TCACAGGAGATTGTGTCCTCAATTAGCCAGGAATGGAAGGATGAGAAGCGGGATTTGCTG
ACTGAAGGACAAAGTTTTAGCAGCCTTGATGAAGAAGCCCTGGGATCCCGACACAGGCCA
GACCTGGTCCCTAGCACTCCATCACTGTTTGAAGCTGCTTCCTTGGCAACCACAATTTCA
TCTTCTTCCTTATACGTCAATGAGCACTATCCACACGACAGGCCTACACTCTATTCAAAC
AGCAAAGGGTTACCTTCCAGTTCAACATTTACCTTGGAAGAGGGGACCATCTACTTGACC
GCTGAGCCCAACACTCTGGAAGTGCAGGATGACAATGCTTCTGTGCTTGACGTCTATTTA
TAA
|
| Enzyme 25 GenBank Gene ID |
AK292734  |
| Enzyme 25 GeneCard ID |
A8K9L9  |
| Enzyme 25 GenAtlas ID |
Not Available |
| Enzyme 25 HGNC ID |
Not Available |
| Enzyme 25 Chromosome Location |
Not Available |
| Enzyme 25 Locus |
Not Available |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
Not Available |
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
15320 |
| Enzyme 26 Name |
Phosphoinositide-3-kinase, catalytic, gamma polypeptide |
| Enzyme 26 Synonyms |
- SubName: Phosphoinositide-3-kinase, catalytic, gamma polypeptide, isoform CRA_a
|
| Enzyme 26 Gene Name |
PIK3CG |
| Enzyme 26 Protein Sequence |
>Phosphoinositide-3-kinase, catalytic, gamma polypeptide
MELENYKQPVVLREDNCRRRRRMKPRSAAASLSSMELIPIEFVLPTSQRKCKSPETALLH
VAGHGNVEQMKAQVWLRALETSVAADFYHRLGPHHFLLLYQKKGQWYEIYDKYQVVQTLD
CLRYWKATHRSPGQIHLVQRHPPSEESQAFQRQLTALIGYDVTDVSNVHDDELEFTRRGL
VTPRMAEVASRDPKLYAMHPWVTSKPLPEYLWKKIANNCIFIVIHRSTTSQTIKVSPDDT
PGAILQSFFTKMAKKKSLMDIPESQSEQDFVLRVCGRDEYLVGETPIKNFQWVRHCLKNG
EEIHVVLDTPPDPALDEVRKEEWPLVDDCTGVTGYHEQLTIHGKDHESVFTVSLWDCDRK
FRVKIRGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNVWLEFSIKI
KDLPKGALLNLQIYCGKAPALSSKASAESPSSESKGKVQLLYYVNLLLIDHRFLLRRGEY
VLHMWQISGKGEDQGSFNADKLTSATNPDKENSMSISILLDNYCHPIALPKHQPTPDPEG
DRVRAEMPNQLRKQLEAIIATDPLNPLTAEDKELLWHFRYESLKHPKAYPKLFSSVKWGQ
QEIVAKTYQLLARREVWDQSALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYL
LQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLRSEIAQSRHYQQRFAVILEAY
LRGCGTAMLHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLP
ESFRVPYDPGLKAGALAIEKCKVMASKKKPLWLEFKCADPTALSNETIGIIFKHGDDLRQ
DMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTVGNTG
AFKDEVLNHWLKEKSPTEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNL
FHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSPHFQKFQDICVKAYLAL
RHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKNEEDAKKYFLDQIEVCRDKGW
TVQFNWFLHLVLGIKQGEKHSA
|
| Enzyme 26 Number of Residues |
1102 |
| Enzyme 26 Molecular Weight |
126452.6 |
| Enzyme 26 Theoretical pI |
7.53 |
| Enzyme 26 GO Classification |
| Function |
- 1-phosphatidylinositol-3-kinase activity
- binding
- catalytic activity
- inositol or phosphatidylinositol kinase activity
- kinase activity
- lipid kinase activity
- phosphoinositide 3-kinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biological regulation
- glycerophospholipid metabolic process
- intracellular signal transduction
- metabolic process
- organophosphate metabolic process
- phosphoinositide metabolic process
- phosphoinositide phosphorylation
- phosphoinositide-mediated signaling
- phospholipid metabolic process
- regulation of biological process
- regulation of cellular process
- second-messenger-mediated signaling
- signal transduction
|
| Component |
- macromolecular complex
- phosphoinositide 3-kinase complex
- protein complex
|
|
| Enzyme 26 General Function |
Involved in binding |
| Enzyme 26 Specific Function |
Not Available |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
Not Available |
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
21237725  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
A4D0Q6  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
A4D0Q6_HUMAN  |
| Enzyme 26 PDB ID |
1E8Z  |
| Enzyme 26 PDB File |
Show |
| Enzyme 26 3D Structure |
|
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>3309 bp
ATGGAGCTGGAGAACTATAAACAGCCCGTGGTGCTGAGAGAGGACAACTGCCGAAGGCGC
CGGAGGATGAAGCCGCGCAGTGCTGCGGCCAGCCTGTCCTCCATGGAGCTCATCCCCATC
GAGTTCGTGCTGCCCACCAGCCAGCGCAAATGCAAGAGCCCCGAAACGGCGCTGCTGCAC
GTGGCCGGCCACGGCAACGTGGAGCAGATGAAGGCCCAGGTGTGGCTGCGAGCGCTGGAG
ACCAGCGTGGCGGCGGACTTCTACCACCGGCTGGGACCGCATCACTTCCTCCTGCTCTAT
CAGAAGAAGGGGCAGTGGTACGAGATCTACGACAAGTACCAGGTGGTGCAGACTCTGGAC
TGCCTGCGCTACTGGAAGGCCACGCACCGGAGCCCGGGCCAGATCCACCTGGTGCAGCGG
CACCCGCCCTCCGAGGAGTCCCAAGCCTTCCAGCGGCAGCTCACGGCGCTGATTGGCTAT
GACGTCACTGACGTCAGCAACGTGCACGACGATGAGCTGGAGTTCACGCGCCGTGGCTTG
GTGACCCCGCGCATGGCGGAGGTGGCCAGCCGCGACCCCAAGCTCTACGCCATGCACCCG
TGGGTGACGTCCAAGCCCCTCCCGGAGTACCTGTGGAAGAAGATTGCCAACAACTGCATC
TTCATCGTCATTCACCGCAGCACCACCAGCCAGACCATTAAGGTCTCACCCGACGACACC
CCCGGCGCCATCCTGCAGAGCTTCTTCACCAAGATGGCCAAGAAGAAATCTCTGATGGAT
ATTCCCGAAAGCCAAAGCGAACAGGATTTTGTGCTGCGCGTCTGTGGCCGGGATGAGTAC
CTGGTGGGCGAAACGCCCATCAAAAACTTCCAGTGGGTGAGGCACTGCCTCAAGAACGGA
GAAGAGATTCACGTGGTACTGGACACGCCTCCAGACCCGGCCCTAGACGAGGTGAGGAAG
GAAGAGTGGCCGCTGGTGGATGACTGCACGGGAGTCACCGGCTACCATGAGCAGCTTACC
ATCCACGGCAAGGACCACGAGAGTGTGTTCACCGTGTCCCTGTGGGACTGCGACCGCAAG
TTCAGGGTCAAGATCAGAGGCATTGATATCCCCGTCCTGCCTCGGAACACCGACCTCACA
GTTTTTGTAGAGGCAAACATCCAGCATGGGCAACAAGTCCTTTGCCAAAGGAGAACCAGC
CCCAAACCCTTCACAGAGGAGGTGCTGTGGAATGTGTGGCTTGAGTTCAGTATCAAAATC
AAAGACTTGCCCAAAGGGGCTCTACTGAACCTCCAGATCTACTGCGGTAAAGCTCCAGCA
CTGTCCAGCAAGGCCTCTGCAGAGTCCCCCAGTTCTGAGTCCAAGGGCAAAGTTCAGCTT
CTCTATTATGTGAACCTGCTGCTGATAGACCACCGTTTCCTCCTGCGCCGTGGAGAATAC
GTCCTCCACATGTGGCAGATATCTGGGAAGGGAGAAGACCAAGGAAGCTTCAATGCTGAC
AAACTCACGTCTGCAACTAACCCAGACAAGGAGAACTCAATGTCCATCTCCATTCTTCTG
GACAATTACTGCCACCCGATAGCCCTGCCTAAGCATCAGCCCACCCCTGACCCGGAAGGG
GACCGGGTTCGAGCAGAAATGCCCAACCAGCTTCGCAAGCAATTGGAGGCGATCATAGCC
ACTGATCCACTTAACCCTCTCACAGCAGAGGACAAAGAATTGCTCTGGCATTTTAGATAC
GAAAGCCTTAAGCACCCAAAAGCATATCCTAAGCTATTTAGTTCAGTGAAATGGGGACAG
CAAGAAATTGTGGCCAAAACATACCAATTGTTGGCCAGAAGGGAAGTCTGGGATCAAAGT
GCTTTGGATGTTGGGTTAACAATGCAGCTCCTGGACTGCAACTTCTCAGATGAAAATGTA
AGAGCCATTGCAGTTCAGAAACTGGAGAGCTTGGAGGACGATGATGTTCTGCATTACCTT
CTACAATTGGTCCAGGCTGTGAAATTTGAACCATACCATGATAGCGCCCTTGCCAGATTT
CTGCTGAAGCGTGGTTTAAGAAACAAAAGAATTGGTCACTTTTTGTTTTGGTTCTTGAGA
AGTGAGATAGCCCAGTCCAGACACTATCAGCAGAGGTTCGCTGTGATTCTGGAAGCCTAT
CTGAGGGGCTGTGGCACAGCCATGCTGCACGACTTTACCCAACAAGTCCAAGTAATCGAG
ATGTTACAAAAAGTCACCCTTGATATTAAATCGCTCTCTGCTGAAAAGTATGACGTCAGT
TCCCAAGTTATTTCACAACTTAAACAAAAGCTTGAAAACCTGCAGAATTCTCAACTCCCC
GAAAGCTTTAGAGTTCCATATGATCCTGGACTGAAAGCAGGAGCGCTGGCAATTGAAAAA
TGTAAAGTAATGGCCTCCAAGAAAAAACCACTATGGCTTGAGTTTAAATGTGCCGATCCT
ACAGCCCTATCAAATGAAACAATTGGAATTATCTTTAAACATGGTGATGATCTGCGCCAA
GACATGCTTATTTTACAGATTCTACGAATCATGGAGTCTATTTGGGAGACTGAATCTTTG
GATCTATGCCTCCTGCCATATGGTTGCATTTCAACTGGTGACAAAATAGGAATGATCGAG
ATTGTGAAAGACGCCACGACAATTGCCAAAATTCAGCAAAGCACAGTGGGCAACACGGGA
GCATTTAAAGATGAAGTCCTGAATCACTGGCTCAAAGAAAAATCCCCTACTGAAGAAAAG
TTTCAGGCAGCAGTGGAGAGATTTGTTTATTCCTGTGCAGGCTACTGTGTGGCAACCTTT
GTTCTTGGAATAGGCGACAGACACAATGACAATATTATGATCACCGAGACAGGAAACCTA
TTTCATATTGACTTCGGGCACATTCTTGGGAATTACAAAAGTTTCCTGGGCATTAATAAA
GAGAGAGTGCCATTTGTGCTAACCCCTGACTTCCTCTTTGTGATGGGAACTTCTGGAAAG
AAGACAAGCCCACACTTCCAGAAATTTCAGGACATCTGTGTTAAGGCTTATCTAGCCCTT
CGTCATCACACAAACCTACTGATCATCCTGTTCTCCATGATGCTGATGACAGGAATGCCC
CAGTTAACAAGCAAAGAAGACATTGAATATATCCGGGATGCCCTCACAGTGGGGAAAAAT
GAGGAGGATGCTAAAAAGTATTTTCTTGATCAGATCGAAGTTTGCAGAGACAAAGGATGG
ACTGTGCAGTTTAATTGGTTTCTACATCTTGTTCTTGGCATCAAACAAGGAGAGAAACAT
TCAGCCTAA
|
| Enzyme 26 GenBank Gene ID |
NM_002649.2  |
| Enzyme 26 GeneCard ID |
PIK3CG  |
| Enzyme 26 GenAtlas ID |
PIK3CG  |
| Enzyme 26 HGNC ID |
HGNC:8978  |
| Enzyme 26 Chromosome Location |
7 |
| Enzyme 26 Locus |
7q22.3 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- 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
]
- 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 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
16047 |
| Enzyme 27 Name |
Phospholipase C, beta 3 (Phosphatidylinositol-specific) (Phospholipase C, beta 3 (Phosphatidylinositol-specific), isoform CRA_a) |
| Enzyme 27 Synonyms |
Not Available |
| Enzyme 27 Gene Name |
PLCB3 |
| Enzyme 27 Protein Sequence |
>Phospholipase C, beta 3 (Phosphatidylinositol-specific) (Phospholipase C, beta 3 (Phosphatidylinositol-specific), isoform CRA_a)
MAGAQPGVHALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNME
VDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNF
MAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFS
ADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPY
LTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYL
GGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRC
VELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAK
QQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPDS
AGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGD
EGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPV
KFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYM
PQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIV
DGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEP
FDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLI
YTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQL
GSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRGH
KALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVED
TKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQF
KRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLE
EAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGLG
DGPLVACASNGHAPGSSGHLSGADSESQEENTQL
|
| Enzyme 27 Number of Residues |
1234 |
| Enzyme 27 Molecular Weight |
138801 |
| Enzyme 27 Theoretical pI |
5.66 |
| Enzyme 27 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylic ester hydrolase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphodiesterase activity
- ion binding
- lipase activity
- phosphoinositide phospholipase C activity
- phospholipase C activity
- phospholipase activity
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- cell communication
- cellular process
- intracellular signaling cascade
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
- signal transduction
|
| Component |
| — |
|
| Enzyme 27 General Function |
Not Available |
| Enzyme 27 Specific Function |
Not Available |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
Not Available |
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
Not Available |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
A5PKZ6  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
A5PKZ6_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
Not Available |
| Enzyme 27 GenBank Gene ID |
BC142681  |
| Enzyme 27 GeneCard ID |
A5PKZ6  |
| Enzyme 27 GenAtlas ID |
Not Available |
| Enzyme 27 HGNC ID |
Not Available |
| Enzyme 27 Chromosome Location |
11 |
| Enzyme 27 Locus |
11q13 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
16048 |
| Enzyme 28 Name |
Phospholipase C, gamma 1 |
| Enzyme 28 Synonyms |
- SubName: Phospholipase C, gamma 1, isoform CRA_b
|
| Enzyme 28 Gene Name |
PLCG1 |
| Enzyme 28 Protein Sequence |
>Phospholipase C, gamma 1
MAGAASPCANGCGPGAPSDAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQI
TWSRGADKIEGAIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTL
SLQATSEDEVNMWIKGLTWLMEDTLQAPTPLQIERWLRKQFYSVDRNREDRISAKDLKNM
LSQVNYRVPNMRFLRERLTDLEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLEASTLRA
GERPELCRVSLPEFQQFLLDYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDEFVT
FLFSKENSVWNSQLDAVCPDTMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMG
CRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIA
QQRNMAQYFKKVLGDTLLTKPVEISADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSMM
YSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEVSS
STELHSNEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFW
RNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQT
NAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQE
GQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNP
GFYVEANPMPTFKCAVKALFDYKAQREDELTFIKSAIIQNVEKQEGGWWRGDYGGKKQLW
FPSNYVEEMVNPVALEPEREHLDENSPLGDLLRGVLDVPACQIAIRPEGKNNRLFVFSIS
MASVAHWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKIMERRKKIALELSELVVYC
RPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDS
SNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMTGRHCGYVLQPSTMRDEAFDPFDKS
SLRGLEPCAISIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVW
PAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDL
ELASLLIKIDIFPAKQENGDLSPFSGTSLRERGSDASGQLFHGRAREGSFESRYQQPFED
FRISQEHLADHFDSRERRAPRRTRVNGDNRL
|
| Enzyme 28 Number of Residues |
1291 |
| Enzyme 28 Molecular Weight |
148658.9 |
| Enzyme 28 Theoretical pI |
5.91 |
| Enzyme 28 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 28 General Function |
Involved in calcium ion binding |
| Enzyme 28 Specific Function |
Not Available |
| Enzyme 28 Pathways |
Not Available |
| Enzyme 28 Reactions |
Not Available |
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
123228952  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
A2A284  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
A2A284_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>3876 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
GAGTTGGCCTCCCTGCTGATCAAGATTGACATTTTCCCTGCCAAGCAGGAGAATGGTGAC
CTCAGTCCCTTCAGTGGTACGTCCCTGCGGGAGCGGGGCTCAGATGCCTCAGGCCAGCTG
TTTCATGGCCGAGCCCGGGAAGGCTCCTTTGAATCCCGCTACCAGCAGCCGTTTGAGGAC
TTCCGCATCTCCCAGGAGCATCTCGCAGACCATTTTGACAGTCGAGAACGAAGGGCCCCA
AGAAGGACTCGGGTCAATGGAGACAACCGCCTCTAG
|
| Enzyme 28 GenBank Gene ID |
AL022394  |
| Enzyme 28 GeneCard ID |
PLCG1  |
| Enzyme 28 GenAtlas ID |
PLCG1  |
| Enzyme 28 HGNC ID |
HGNC:9065  |
| Enzyme 28 Chromosome Location |
2 |
| Enzyme 28 Locus |
20q12-q13.1 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
Not Available |
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
16574 |
| Enzyme 29 Name |
Phosphatidylinositol-4-phosphate 5-kinase type-2 alpha variant 1 (Phosphatidylinositol-4-phosphate 5-kinase, type II, alpha, isoform CRA_a) (Phosphatidylinositol-4-phosphate 5-kinase type-2 alpha variant 2) |
| Enzyme 29 Synonyms |
Not Available |
| Enzyme 29 Gene Name |
PIP5K2A |
| Enzyme 29 Protein Sequence |
>Phosphatidylinositol-4-phosphate 5-kinase type-2 alpha variant 1 (Phosphatidylinositol-4-phosphate 5-kinase, type II, alpha, isoform CRA_a) (Phosphatidylinositol-4-phosphate 5-kinase type-2 alpha variant 2)
MATPGNLGSSVLASKTKTKKKHFVAQKVKLFRASDPLLSVLMWGVNHSINELSHVQIPVM
LMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSA
PLPNDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVECHGITLLPQFLG
MYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFIN
EGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVECEENDGEE
EGESDGTHPVGTPPDSPGNTLNSSPPLAPGEFDPNIDVYGIKCHENSPRKEVYFMAIIDI
LTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGHILT
|
| Enzyme 29 Number of Residues |
406 |
| Enzyme 29 Molecular Weight |
46225 |
| Enzyme 29 Theoretical pI |
7.00 |
| Enzyme 29 GO Classification |
| Function |
- 1-phosphatidylinositol-4-phosphate 5-kinase activity
- catalytic activity
- kinase activity
- lipid kinase activity
- phosphatidylinositol phosphate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 29 General Function |
Not Available |
| Enzyme 29 Specific Function |
Not Available |
| Enzyme 29 Pathways |
Not Available |
| Enzyme 29 Reactions |
Not Available |
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
Not Available |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
B0YJ66  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
B0YJ66_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
Not Available |
| Enzyme 29 GenBank Gene ID |
EF445009  |
| Enzyme 29 GeneCard ID |
B0YJ66  |
| Enzyme 29 GenAtlas ID |
Not Available |
| Enzyme 29 HGNC ID |
Not Available |
| Enzyme 29 Chromosome Location |
10 |
| Enzyme 29 Locus |
10p12.2 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
Not Available |
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
16633 |
| Enzyme 30 Name |
cDNA, FLJ94145, Homo sapiens phosphatase and tensin homolog (mutated in multipleadvanced cancers 1) (PTEN), mRNA (Phosphatase and tensin homolog (Mutated in multiple advanced cancers 1), isoform CRA_c) |
| Enzyme 30 Synonyms |
Not Available |
| Enzyme 30 Gene Name |
PTEN |
| Enzyme 30 Protein Sequence |
>cDNA, FLJ94145, Homo sapiens phosphatase and tensin homolog (mutated in multipleadvanced cancers 1) (PTEN), mRNA (Phosphatase and tensin homolog (Mutated in multiple advanced cancers 1), isoform CRA_c)
MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSK
HKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVA
AIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSY
LLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMY
FEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEI
DSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEAS
SSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV
|
| Enzyme 30 Number of Residues |
403 |
| Enzyme 30 Molecular Weight |
47167 |
| Enzyme 30 Theoretical pI |
6.33 |
| Enzyme 30 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoprotein phosphatase activity
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
- protein tyrosine/serine/threonine phosphatase activity
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid dephosphorylation
- protein modification
|
| Component |
| — |
|
| Enzyme 30 General Function |
Signal transduction mechanisms |
| Enzyme 30 Specific Function |
Not Available |
| Enzyme 30 Pathways |
Not Available |
| Enzyme 30 Reactions |
Not Available |
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
Not Available |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
B2R904  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
B2R904_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
Not Available |
| Enzyme 30 GenBank Gene ID |
AK313581  |
| Enzyme 30 GeneCard ID |
B2R904  |
| Enzyme 30 GenAtlas ID |
Not Available |
| Enzyme 30 HGNC ID |
Not Available |
| Enzyme 30 Chromosome Location |
10 |
| Enzyme 30 Locus |
10q23.3 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
Not Available |
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
16778 |
| Enzyme 31 Name |
cDNA FLJ33455 fis, clone BRAMY2000354, highly similar to 1-phosphatidylinositol-4,5-bisphosphatephosphodiesterase delta 1 (EC 3.1.4.11) |
| Enzyme 31 Synonyms |
Not Available |
| Enzyme 31 Gene Name |
Not Available |
| Enzyme 31 Protein Sequence |
>cDNA FLJ33455 fis, clone BRAMY2000354, highly similar to 1-phosphatidylinositol-4,5-bisphosphatephosphodiesterase delta 1 (EC 3.1.4.11)
MQCLGIRSRSRSRELYLQERSLKVAALNGRRLGLQDDEDLQALLKGSQLLKVKSSSWRRE
RFYKLQEDCKTIWQESRKVMRTPESQLFSIEDIQEVRMGHRTEGLEKFARDVPEDRCFSI
VFKDQRNTLDLIAPSPADAQHWVLGLHKIIHHSGSMDQRQKLQHWIHSCLRKADKNKDNK
MSFKELQNFLKELNIQVDDSYARKIFRECDHSQTDSLEDEEIEAFYKMLTQRVEIDRTFA
EAAGSGETLSVDQLVTFLQHQQREEAAGPALALSLIERYEPSETAKAQRQMTKDGFLMYL
LSADGSAFSLAHRRVYQDMGQPLSHYLVSSSHNTYLLEDQLAGPSSTEAYIRALCKGCRC
LELDCWDGPNQEPIIYHGYTFTSKILFCDVLRAIRDYAFKASPYPVILSLENHCTLEQQR
VMARHLHAILGPMLLNRPLDGVTNSLPSPEQLKGKILLKGKKLGGLLPPGGEGGPEATVV
SDEDEAAEMEDEAVRSRVQHKPKEDKLRLAQELSDMVIYCKSVHFGGFSSPGTPGQAFYE
MASFSENRALRLLQESGNGFVRHNVGHLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNF
QTPGPEMDVYQGRFQDNGACGYVLKPAFLRDPNGTFNPRALAQGPWWARKRLNIRVISGQ
QLPKVNKNKNSIVDPKVTVEIHGVSRDVASRQTAVITNNGFNPWWDTEFAFEVVVPDLAL
IRFLVEDYDASSKNDFIGQSTIPLNSLKQGYRHVHLMSKNGDQHPSATLFVKISLQD
|
| Enzyme 31 Number of Residues |
777 |
| Enzyme 31 Molecular Weight |
88134.2 |
| Enzyme 31 Theoretical pI |
7.23 |
| Enzyme 31 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 31 General Function |
Involved in calcium ion binding |
| Enzyme 31 Specific Function |
Not Available |
| Enzyme 31 Pathways |
Not Available |
| Enzyme 31 Reactions |
Not Available |
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
193786903  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
B3KR14  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
B3KR14_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>2334 bp
ATGCAGTGCCTGGGGATCCGGAGCCGGAGCCGCTCCAGGGAGCTCTACCTGCAGGAGCGG
AGCCTTAAGGTGGCGGCGCTCAATGGACGGAGGCTGGGCCTACAGGATGATGAGGATCTA
CAGGCGCTGCTGAAGGGCAGCCAGCTCCTGAAGGTGAAGTCCAGCTCATGGAGGAGAGAG
CGCTTCTACAAGTTGCAGGAGGACTGCAAGACCATCTGGCAGGAGTCCCGCAAGGTCATG
CGGACCCCGGAGTCCCAGCTGTTCTCCATCGAGGACATTCAGGAGGTGCGAATGGGGCAC
CGCACGGAGGGTCTGGAGAAGTTCGCCCGTGATGTGCCCGAGGACCGCTGCTTCTCCATT
GTCTTCAAGGACCAGCGCAATACACTAGACCTCATCGCCCCATCGCCAGCTGATGCCCAG
CACTGGGTGCTGGGGCTGCACAAGATCATCCACCACTCAGGCTCCATGGACCAGCGTCAG
AAGCTACAGCACTGGATTCACTCCTGCTTGCGAAAAGCTGACAAAAACAAGGACAACAAG
ATGAGCTTCAAGGAGCTGCAGAACTTCCTGAAGGAGCTCAACATCCAGGTGGACGACAGC
TATGCCCGGAAGATCTTCAGGGAGTGTGACCACTCCCAGACAGACTCCCTGGAGGACGAG
GAGATTGAGGCCTTCTACAAGATGCTGACCCAGCGGGTGGAGATCGACCGCACCTTCGCC
GAGGCCGCGGGCTCAGGGGAGACTCTGTCGGTGGATCAGTTAGTGACGTTCCTGCAGCAC
CAGCAGCGGGAGGAGGCGGCAGGGCCTGCGCTGGCCCTCTCCCTCATTGAGCGCTACGAG
CCCAGCGAGACTGCCAAGGCGCAGCGGCAGATGACCAAGGACGGCTTCCTCATGTACTTA
CTGTCGGCTGACGGCAGCGCCTTCAGCCTGGCACACCGCCGTGTCTACCAGGACATGGGC
CAGCCACTTAGCCACTACCTGGTGTCCTCTTCACACAACACCTACCTGCTGGAGGACCAG
CTAGCCGGGCCCAGCAGCACTGAAGCCTACATCCGGGCACTGTGCAAAGGCTGCCGATGC
CTGGAGCTTGACTGCTGGGACGGGCCCAACCAGGAACCAATCATCTACCACGGCTATACT
TTCACTTCCAAGATCCTCTTCTGCGATGTGCTCAGGGCCATCCGGGACTATGCCTTCAAG
GCGTCCCCCTACCCTGTCATCCTATCCCTGGAGAACCACTGCACACTGGAGCAGCAGCGC
GTGATGGCGCGGCACCTGCATGCCATCCTGGGCCCCATGCTGTTGAACCGACCACTGGAT
GGGGTCACCAACAGCCTGCCCTCCCCTGAGCAACTGAAGGGGAAGATCCTGCTGAAGGGG
AAGAAGCTCGGGGGGCTCCTGCCCCCTGGAGGGGAGGGTGGCCCTGAGGCCACTGTGGTG
TCAGACGAAGACGAGGCTGCTGAGATGGAGGATGAGGCAGTGAGGAGCCGTGTGCAGCAC
AAGCCCAAGGAGGACAAGCTCAGGCTAGCACAGGAGCTCTCTGACATGGTCATTTACTGC
AAGAGTGTCCACTTTGGGGGCTTCTCCAGTCCTGGCACCCCTGGACAGGCCTTCTACGAG
ATGGCGTCCTTCTCTGAGAACCGTGCCCTTCGACTGCTCCAAGAATCAGGAAACGGCTTT
GTCCGCCACAACGTGGGGCACCTGAGCAGAATCTACCCGGCTGGATGGAGAACAGACTCC
TCCAACTACAGCCCCGTGGAGATGTGGAATGGGGGCTGCCAGATCGTGGCCCTGAATTTC
CAGACACCTGGGCCAGAGATGGACGTGTACCAGGGCCGCTTCCAGGACAACGGGGCCTGT
GGGTACGTGCTGAAGCCCGCCTTCCTGCGAGACCCCAACGGCACCTTTAACCCCCGCGCC
CTGGCTCAGGGGCCCTGGTGGGCACGGAAGCGGCTCAACATCAGGGTCATTTCGGGGCAG
CAGCTGCCAAAAGTCAACAAGAATAAGAATTCAATTGTGGACCCCAAAGTGACAGTGGAG
ATCCATGGCGTGAGCCGGGACGTGGCCAGCCGCCAGACTGCTGTCATCACCAACAATGGT
TTCAACCCATGGTGGGACACGGAGTTTGCGTTTGAGGTAGTTGTGCCTGACCTTGCCCTC
ATCCGCTTCTTGGTGGAAGATTATGATGCCTCCTCCAAGAATGACTTCATTGGCCAGAGT
ACCATCCCCTTGAACAGCCTCAAGCAAGGATACCGCCATGTCCACCTCATGTCTAAGAAC
GGGGACCAGCATCCATCAGCCACCCTCTTTGTGAAGATCTCCCTCCAGGACTAG
|
| Enzyme 31 GenBank Gene ID |
AK090774  |
| Enzyme 31 GeneCard ID |
Not Available |
| Enzyme 31 GenAtlas ID |
Not Available |
| Enzyme 31 HGNC ID |
Not Available |
| Enzyme 31 Chromosome Location |
Not Available |
| Enzyme 31 Locus |
Not Available |
| Enzyme 31 SNPs |
Not Available |
| Enzyme 31 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
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| Enzyme 31 Metabolite References |
Not Available |