UniProt ID | HRR25_YEAST | |
---|---|---|
UniProt AC | P29295 | |
Protein Name | Casein kinase I homolog HRR25 | |
Gene Name | HRR25 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 494 | |
Subcellular Localization | Cytoplasm . Nucleus, nucleolus . Nucleus, nucleoplasm . | |
Protein Description | Associated with repair of damaged DNA and meiosis. Phosphorylates serine and threonine. Can use casein as a substrate.. | |
Protein Sequence | MDLRVGRKFRIGRKIGSGSFGDIYHGTNLISGEEVAIKLESIRSRHPQLDYESRVYRYLSGGVGIPFIRWFGREGEYNAMVIDLLGPSLEDLFNYCHRRFSFKTVIMLALQMFCRIQYIHGRSFIHRDIKPDNFLMGVGRRGSTVHVIDFGLSKKYRDFNTHRHIPYRENKSLTGTARYASVNTHLGIEQSRRDDLESLGYVLIYFCKGSLPWQGLKATTKKQKYDRIMEKKLNVSVETLCSGLPLEFQEYMAYCKNLKFDEKPDYLFLARLFKDLSIKLEYHNDHLFDWTMLRYTKAMVEKQRDLLIEKGDLNANSNAASASNSTDNKSETFNKIKLLAMKKFPTHFHYYKNEDKHNPSPEEIKQQTILNNNAASSLPEELLNALDKGMENLRQQQPQQQVQSSQPQPQPQQLQQQPNGQRPNYYPEPLLQQQQRDSQEQQQQVPMATTRATQYPPQINSNNFNTNQASVPPQMRSNPQQPPQDKPAGQSIWL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
14 | Ubiquitination | RKFRIGRKIGSGSFG CEEECCCEECCCCCC | 46.32 | 23749301 | |
24 | Phosphorylation | SGSFGDIYHGTNLIS CCCCCCCCCCCCCCC | 10.03 | 23749301 | |
143 | Phosphorylation | MGVGRRGSTVHVIDF ECCCCCCCEEEEEEC | 25.99 | 17330950 | |
144 | Phosphorylation | GVGRRGSTVHVIDFG CCCCCCCEEEEEECC | 19.91 | 25752575 | |
153 | Phosphorylation | HVIDFGLSKKYRDFN EEEECCCCHHCCCCC | 27.73 | 19779198 | |
179 | Phosphorylation | SLTGTARYASVNTHL CCCCCCEEEECCHHC | 10.77 | 25371407 | |
181 | Phosphorylation | TGTARYASVNTHLGI CCCCEEEECCHHCCC | 13.63 | 25371407 | |
219 | Phosphorylation | PWQGLKATTKKQKYD CCCCHHHHCCHHHHH | 37.25 | 28152593 | |
220 | Phosphorylation | WQGLKATTKKQKYDR CCCHHHHCCHHHHHH | 40.90 | 24961812 | |
225 | Phosphorylation | ATTKKQKYDRIMEKK HHCCHHHHHHHHHHH | 14.14 | 27717283 | |
259 | Acetylation | MAYCKNLKFDEKPDY HHHHHCCCCCCCCCH | 61.23 | 24489116 | |
259 | Ubiquitination | MAYCKNLKFDEKPDY HHHHHCCCCCCCCCH | 61.23 | 24961812 | |
263 | Acetylation | KNLKFDEKPDYLFLA HCCCCCCCCCHHHHH | 45.06 | 24489116 | |
274 | Acetylation | LFLARLFKDLSIKLE HHHHHHHCHHCCEEE | 63.45 | 24489116 | |
310 | Ubiquitination | QRDLLIEKGDLNANS HHHHHHHCCCCCCCC | 51.21 | 23749301 | |
317 | Phosphorylation | KGDLNANSNAASASN CCCCCCCCCCCCCCC | 25.99 | 28889911 | |
321 | Phosphorylation | NANSNAASASNSTDN CCCCCCCCCCCCCCC | 29.80 | 22369663 | |
323 | Phosphorylation | NSNAASASNSTDNKS CCCCCCCCCCCCCCH | 28.90 | 22369663 | |
325 | Phosphorylation | NAASASNSTDNKSET CCCCCCCCCCCCHHH | 34.34 | 22369663 | |
326 | Phosphorylation | AASASNSTDNKSETF CCCCCCCCCCCHHHH | 48.09 | 22369663 | |
329 | Ubiquitination | ASNSTDNKSETFNKI CCCCCCCCHHHHHHH | 53.10 | 23749301 | |
330 | Phosphorylation | SNSTDNKSETFNKIK CCCCCCCHHHHHHHH | 48.39 | 22369663 | |
332 | Phosphorylation | STDNKSETFNKIKLL CCCCCHHHHHHHHHH | 39.33 | 22369663 | |
376 | Phosphorylation | ILNNNAASSLPEELL HCCCCHHHCCCHHHH | 29.96 | 30377154 | |
377 | Phosphorylation | LNNNAASSLPEELLN CCCCHHHCCCHHHHH | 43.12 | 21440633 | |
438 | Phosphorylation | LQQQQRDSQEQQQQV HHHHHHHCHHHHHHC | 37.49 | 28889911 |
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 HRR25_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HRR25_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 HRR25_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-143, 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-330, 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-143, AND MASSSPECTROMETRY. |