UniProt ID | HSP79_YEAST | |
---|---|---|
UniProt AC | P32590 | |
Protein Name | Heat shock protein homolog SSE2 | |
Gene Name | SSE2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 693 | |
Subcellular Localization | ||
Protein Description | Has a calcium-dependent calmodulin-binding activity.. | |
Protein Sequence | MSTPFGLDLGNNNSVLAVARNRGIDVVVNEVSNRSTPSLVGFGPRNRYLGESGKTKQTSNVKNTVENLKRIIGLKFKDPEFDIENKFFTSKLVQLKNGKVGVEVEFGGKTHVFSATQLTAMFIDKVKHTVQEETKSSITDVCLAVPVWYSEEQRYNIADAARIAGLNPVRIVNDVTAAAVSYGVFKNDLPGPEEKPRIIGLVDIGHSTYTCSIMAFRKGEMKVLGTAYDKHFGGRDFDRAITEHFADQFKDKYKIDIRKNPKAYNRILIAAEKLKKVLSANTTAPFSVESVMDDIDVSSQLSREELEELVEPLLKRVTYPITNALAQAKLTVNDIDFVEIIGGTTRIPVLKKSISDVFGKPLSSTLNQDEAVAKGAAFICAIHSPTLRVRPFKFEDIDPYSVSYTWDKQVDDEDRLEVFPANSSYPSTKLITLHRTGDFSMKAVYTHPSKLPKGTSTTIAKWSFTGVKVPKDQDFIPVKVKLRCDPSGLHIIENAYTTEDITVQEPVPLPEDAPEDAEPQFKEVTKTIKKDVLGMTAKTFALNPVELNDLIEKENELRNQDKLVAETEDRKNALEEYIYTLRAKLDDEYSDFASDAEKEKLKNMLATTENWLYGDGDDSTKAKYIAKYEELASLGNIIRGRYLAKEEEKRQALRANQETSKMNDIAEKLAEQRRARAASDDSDDNNDENMDLD | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSTPFGLDL ------CCCCCCEEC | 44.80 | 28152593 | |
3 | Phosphorylation | -----MSTPFGLDLG -----CCCCCCEECC | 22.72 | 28152593 | |
35 | Phosphorylation | VNEVSNRSTPSLVGF EEECCCCCCCCCCCC | 49.25 | 27214570 | |
75 | Acetylation | LKRIIGLKFKDPEFD HHHHHCCEECCCCCC | 45.19 | 24489116 | |
77 | Acetylation | RIIGLKFKDPEFDIE HHHCCEECCCCCCCC | 71.44 | 24489116 | |
86 | Acetylation | PEFDIENKFFTSKLV CCCCCCCCCEEEEEE | 29.12 | 24489116 | |
91 | Acetylation | ENKFFTSKLVQLKNG CCCCEEEEEEECCCC | 50.01 | 24489116 | |
226 | Phosphorylation | GEMKVLGTAYDKHFG CCEEEEEEECCCCCC | 20.20 | 30377154 | |
230 | Acetylation | VLGTAYDKHFGGRDF EEEEECCCCCCCCCH | 28.32 | 24489116 | |
250 | Acetylation | EHFADQFKDKYKIDI HHHHHHCCHHCCCCC | 47.91 | 24489116 | |
273 | Acetylation | RILIAAEKLKKVLSA HHHHHHHHHHHHHCC | 61.96 | 24489116 | |
355 | Phosphorylation | PVLKKSISDVFGKPL EHHHHHHHHHHCCCH | 34.51 | 28889911 | |
384 | Phosphorylation | AFICAIHSPTLRVRP HEEEEECCCCEEECC | 17.29 | 22369663 | |
386 | Phosphorylation | ICAIHSPTLRVRPFK EEEECCCCEEECCCC | 30.15 | 22369663 | |
432 | Phosphorylation | YPSTKLITLHRTGDF CCCCEEEEEEECCCC | 27.27 | 24961812 | |
436 | Phosphorylation | KLITLHRTGDFSMKA EEEEEEECCCCCEEE | 30.29 | 21440633 | |
440 | Phosphorylation | LHRTGDFSMKAVYTH EEECCCCCEEEEEEC | 24.90 | 24961812 | |
442 | Acetylation | RTGDFSMKAVYTHPS ECCCCCEEEEEECCC | 33.24 | 24489116 | |
449 | Phosphorylation | KAVYTHPSKLPKGTS EEEEECCCCCCCCCC | 38.94 | 28889911 | |
455 | Phosphorylation | PSKLPKGTSTTIAKW CCCCCCCCCCEEEEE | 29.09 | 21126336 | |
471 | Acetylation | FTGVKVPKDQDFIPV EECEECCCCCCCEEE | 71.64 | 24489116 | |
584 | Acetylation | YIYTLRAKLDDEYSD HHHHHHHHCCHHHCC | 46.12 | 24489116 | |
600 | Acetylation | ASDAEKEKLKNMLAT CCHHHHHHHHHHHHH | 75.68 | 24489116 | |
623 | Ubiquitination | GDDSTKAKYIAKYEE CCCCHHHHHHHCHHH | 38.45 | 22817900 | |
627 | Ubiquitination | TKAKYIAKYEELASL HHHHHHHCHHHHHHC | 43.57 | 24961812 | |
633 | Phosphorylation | AKYEELASLGNIIRG HCHHHHHHCHHHHHH | 49.81 | 30377154 | |
642 | Phosphorylation | GNIIRGRYLAKEEEK HHHHHHHHHCCHHHH | 17.52 | 22369663 | |
645 | Acetylation | IRGRYLAKEEEKRQA HHHHHHCCHHHHHHH | 64.16 | 25381059 | |
661 | Ubiquitination | RANQETSKMNDIAEK HHHHHHHHHHHHHHH | 49.49 | 23749301 | |
668 | Ubiquitination | KMNDIAEKLAEQRRA HHHHHHHHHHHHHHH | 43.93 | 23749301 | |
668 | Acetylation | KMNDIAEKLAEQRRA HHHHHHHHHHHHHHH | 43.93 | 24489116 | |
679 | Phosphorylation | QRRARAASDDSDDNN HHHHHHCCCCCCCCC | 40.75 | 19823750 | |
682 | Phosphorylation | ARAASDDSDDNNDEN HHHCCCCCCCCCCCC | 52.43 | 19823750 |
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 HSP79_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HSP79_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 HSP79_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
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-384 AND THR-386, ANDMASS 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-384, 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-384, AND MASSSPECTROMETRY. |