UniProt ID | PTP2_YEAST | |
---|---|---|
UniProt AC | P29461 | |
Protein Name | Tyrosine-protein phosphatase 2 | |
Gene Name | PTP2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 750 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | Major phosphatase responsible with PTP3 for tyrosine dephosphorylation of MAP kinase HOG1 to inactivate its activity. May also be involved in the regulation of MAP kinase FUS3. May be implicated in the ubiquitin-mediated protein degradation.. | |
Protein Sequence | MDRIAQQYRNGKRDNNGNRMASSAISEKGHIQVNQTRTPGQMPVYRGETINLSNLPQNQIKPCKDLDDVNIRRNNSNRHSKILLLDLCAGPNTNSFLGNTNAKDITVLSLPLPSTLVKRSNYPFENLLKNYLGSDEKYIEFTKIIKDYDIFIFSDSFSRISSCLKTTFCLIEKFKKFICHFFPSPYLKFFLLEGSLNDSKAPSLGKNKKNCILPKLDLNLNVNLTSRSTLNLRINIPPPNDSNKIFLQSLKKDLIHYSPNSLQKFFQFNMPADLAPNDTILPNWLKFCSVKENEKVILKKLFNNFETLENFEMQRLEKCLKFKKKPLHQKQLSQKQRGPQSTDDSKLYSLTSLQRQYKSSLKSNIQKNQKLKLIIPKNNTSSSPSPLSSDDTIMSPINDYELTEGIQSFTKNRYSNILPYEHSRVKLPHSPKPPAVSEASTTETKTDKSYPMCPVDAKNHSCKPNDYINANYLKLTQINPDFKYIATQAPLPSTMDDFWKVITLNKVKVIISLNSDDELNLRKWDIYWNNLSYSNHTIKLQNTWENICNINGCVLRVFQVKKTAPQNDNISQDCDLPHNGDLTSITMAVSEPFIVYQLQYKNWLDSCGVDMNDIIKLHKVKNSLLFNPQSFITSLEKDVCKPDLIDDNNSELHLDTANSSPLLVHCSAGCGRTGVFVTLDFLLSILSPTTNHSNKIDVWNMTQDLIFIIVNELRKQRISMVQNLTQYIACYEALLNYFALQKQIKNALPC | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
22 | Phosphorylation | NNGNRMASSAISEKG CCCCCCCHHHHHHCC | 15.80 | 28889911 | |
23 | Phosphorylation | NGNRMASSAISEKGH CCCCCCHHHHHHCCC | 21.78 | 28889911 | |
26 | Phosphorylation | RMASSAISEKGHIQV CCCHHHHHHCCCEEE | 32.73 | 28889911 | |
257 | Phosphorylation | LKKDLIHYSPNSLQK HHHHHHCCCCCHHHH | 20.87 | 19823750 | |
258 | Phosphorylation | KKDLIHYSPNSLQKF HHHHHCCCCCHHHHH | 11.93 | 25521595 | |
261 | Phosphorylation | LIHYSPNSLQKFFQF HHCCCCCHHHHHHHC | 35.25 | 19823750 | |
349 | Phosphorylation | TDDSKLYSLTSLQRQ CCHHHHHHHHHHHHH | 35.29 | 27214570 | |
395 | Phosphorylation | SSDDTIMSPINDYEL CCCCCEECCCCCHHH | 20.83 | 28889911 | |
430 | Phosphorylation | SRVKLPHSPKPPAVS CCCCCCCCCCCCCCC | 32.45 | 17330950 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of PTP2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PTP2_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of PTP2_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND MASSSPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND MASSSPECTROMETRY. | |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-430, ANDMASS SPECTROMETRY. |