UniProt ID | PWP1_YEAST | |
---|---|---|
UniProt AC | P21304 | |
Protein Name | Periodic tryptophan protein 1 | |
Gene Name | PWP1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 576 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MISATNWVPRGFSSEFPEKYVLDDEEVERINQLAQLNLDDAKATLEEAEGESGVEDDAATGSSNKLKDQLDIDDDLKEYNLEEYDDEEIADNEGGKDVSMFPGLSNDSDVKFHEGEKGEDPYISLPNQEDSQEEKQELQVYPSDNLVLAARTEDDVSYLDIYVYDDGAGFHSSDIPVEEGDEADPDVARGLVRDPALYVHHDLMLPAFPLCVEWLDYKVGSNSEEAANYAAIGTFDPQIEIWNLDCVDKAFPDMILGEPLDNSMVSLKSKKKKKKSKTGHITTHHTDAVLSMAHNKYFRSVLASTSADHTVKLWDLNSGNAARSLASIHSNKNVSSSEWHMLNGSILLTGGYDSRVALTDVRISDESQMSKYWSAMAGEEIETVTFASENIILCGTDSGNVYSFDIRNNENRKPVWTLKAHDAGISTLCSNKFIPGMMSTGAMGEKTVKLWKFPLDDATNTKGPSMVLSRDFDVGNVLTSSFAPDIEVAGTMVIGGVNKVLKLWDVFTNRSVRKSFKSELENVQARAKEEAQKIGKSSRIARKYTSNDNPDTVITIDDQGEDEEEREGGDEHDDMA | |
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 |
---|---|---|---|---|---|
5 | Phosphorylation | ---MISATNWVPRGF ---CCCCCCCCCCCC | 23.87 | 19779198 | |
13 | Phosphorylation | NWVPRGFSSEFPEKY CCCCCCCCCCCCCCC | 31.61 | 30377154 | |
19 | Acetylation | FSSEFPEKYVLDDEE CCCCCCCCCCCCHHH | 40.68 | 24489116 | |
44 | Phosphorylation | NLDDAKATLEEAEGE CHHHHHHHHHHHCCC | 33.71 | 22890988 | |
52 | Phosphorylation | LEEAEGESGVEDDAA HHHHCCCCCCCCCCC | 60.02 | 22369663 | |
60 | Phosphorylation | GVEDDAATGSSNKLK CCCCCCCCCCCHHHH | 39.04 | 22890988 | |
62 | Phosphorylation | EDDAATGSSNKLKDQ CCCCCCCCCHHHHHH | 26.78 | 22890988 | |
63 | Phosphorylation | DDAATGSSNKLKDQL CCCCCCCCHHHHHHC | 39.05 | 22890988 | |
99 | Phosphorylation | NEGGKDVSMFPGLSN CCCCCCCCCCCCCCC | 25.49 | 22369663 | |
105 | Phosphorylation | VSMFPGLSNDSDVKF CCCCCCCCCCCCCCE | 44.50 | 22369663 | |
108 | Phosphorylation | FPGLSNDSDVKFHEG CCCCCCCCCCCEECC | 48.86 | 22369663 | |
124 | Phosphorylation | KGEDPYISLPNQEDS CCCCCCCCCCCCCCC | 31.75 | 28889911 | |
131 | Phosphorylation | SLPNQEDSQEEKQEL CCCCCCCCHHHHHHC | 38.45 | 22369663 | |
263 | Phosphorylation | LGEPLDNSMVSLKSK CCCCCCCCCCCCCCC | 21.89 | 22369663 | |
266 | Phosphorylation | PLDNSMVSLKSKKKK CCCCCCCCCCCCCCC | 22.80 | 22369663 | |
330 | Phosphorylation | RSLASIHSNKNVSSS HHHHHHHCCCCCCHH | 48.07 | 27017623 | |
336 | Phosphorylation | HSNKNVSSSEWHMLN HCCCCCCHHHEEECC | 28.17 | 27017623 | |
337 | Phosphorylation | SNKNVSSSEWHMLNG CCCCCCHHHEEECCC | 36.88 | 27017623 | |
354 | Phosphorylation | LLTGGYDSRVALTDV EEECCCCCCEEEEEE | 21.85 | 19779198 | |
502 | Ubiquitination | GGVNKVLKLWDVFTN CCHHHHHHHHHHHCC | 50.98 | 23749301 | |
511 | Phosphorylation | WDVFTNRSVRKSFKS HHHHCCHHHHHHHHH | 28.48 | 27017623 | |
515 | Phosphorylation | TNRSVRKSFKSELEN CCHHHHHHHHHHHHH | 27.61 | 23749301 | |
517 | Acetylation | RSVRKSFKSELENVQ HHHHHHHHHHHHHHH | 50.54 | 24489116 | |
518 | Phosphorylation | SVRKSFKSELENVQA HHHHHHHHHHHHHHH | 45.46 | 24961812 | |
537 | Phosphorylation | EAQKIGKSSRIARKY HHHHHCHHHHHHHHH | 21.45 | 19823750 | |
538 | Phosphorylation | AQKIGKSSRIARKYT HHHHCHHHHHHHHHC | 31.06 | 19823750 | |
545 | Phosphorylation | SRIARKYTSNDNPDT HHHHHHHCCCCCCCC | 24.88 | 17563356 | |
546 | Phosphorylation | RIARKYTSNDNPDTV HHHHHHCCCCCCCCE | 38.81 | 17563356 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of PWP1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PWP1_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 PWP1_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-52; SER-62; SER-131;SER-263 AND SER-266, AND MASS SPECTROMETRY. | |
"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-52; THR-545 AND SER-546,AND MASS SPECTROMETRY. | |
"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-52, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND MASSSPECTROMETRY. |