UniProt ID | RAD7_YEAST | |
---|---|---|
UniProt AC | P06779 | |
Protein Name | DNA repair protein RAD7 | |
Gene Name | RAD7 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 565 | |
Subcellular Localization | ||
Protein Description | Component of the global genome repair (GGR) complex which promotes global genome nucleotide excision repair (GG-NER) which removes DNA damage from nontranscribing DNA. This protein is one of 10 proteins (RAD1, 2,3,4,7,10,14, 16,23 and MMS19) involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents.. | |
Protein Sequence | MYRSRNRPKRGGENEVKGPNSALTQFLREEGISAENIKQKWYQRQSKKQEDATDEKKGKAEDDSFTAEISRVVEDEEIDEIGTGSGTETERAQVSYDARMKLVPADSDEEEYETSHISDTPVSLSSANDRESLTKKRQNTAKIIQNRRRKRKRAADLLDRRVNKVSSLQSLCITKISENISKWQKEADESSKLVFNKLRDVLGGVSTANLNNLAKALSKNRALNDHTLQLFLKTDLKRLTFSDCSKISFDGYKTLAIFSPHLTELSLQMCGQLNHESLLYIAEKLPNLKSLNLDGPFLINEDTWEKFFVIMKGRLEEFHISNTHRFTDKSLSNLLINCGSTLVSLGLSRLDSISNYALLPQYLVNDEFHSLCIEYPFNEEDVNDEIIINLLGQIGRTLRKLVLNGCIDLTDSMIINGLTAFIPEKCPLEVLSLEESDQITTDSLSYFFSKVELNNLIECSFRRCLQLGDMAIIELLLNGARDSLRSLNLNSLKELTKEAFVALACPNLTYLDLGFVRCVDDSVIQMLGEQNPNLTVIDVFGDNLVTEKATMRPGLTLIGRQSDSI | |
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 |
---|---|---|---|---|---|
33 | Phosphorylation | FLREEGISAENIKQK HHHHCCCCHHHHHHH | 40.15 | 30377154 | |
64 | Phosphorylation | KGKAEDDSFTAEISR CCCCCCCCHHHHHHE | 36.50 | 22369663 | |
66 | Phosphorylation | KAEDDSFTAEISRVV CCCCCCHHHHHHEEE | 27.60 | 22369663 | |
70 | Phosphorylation | DSFTAEISRVVEDEE CCHHHHHHEEECHHH | 15.55 | 29688323 | |
83 | Phosphorylation | EEIDEIGTGSGTETE HHCCCCCCCCCCCCE | 33.56 | 22369663 | |
85 | Phosphorylation | IDEIGTGSGTETERA CCCCCCCCCCCCEEE | 42.24 | 22369663 | |
87 | Phosphorylation | EIGTGSGTETERAQV CCCCCCCCCCEEEEE | 41.24 | 22369663 | |
89 | Phosphorylation | GTGSGTETERAQVSY CCCCCCCCEEEEECC | 30.52 | 22369663 | |
95 | Phosphorylation | ETERAQVSYDARMKL CCEEEEECCCCCCCE | 12.76 | 23749301 | |
96 | Phosphorylation | TERAQVSYDARMKLV CEEEEECCCCCCCEE | 18.11 | 28889911 | |
107 | Phosphorylation | MKLVPADSDEEEYET CCEEECCCCHHHHHH | 49.37 | 21551504 | |
112 | Phosphorylation | ADSDEEEYETSHISD CCCCHHHHHHCCCCC | 27.99 | 21440633 | |
114 | Phosphorylation | SDEEEYETSHISDTP CCHHHHHHCCCCCCC | 25.38 | 19779198 | |
115 | Phosphorylation | DEEEYETSHISDTPV CHHHHHHCCCCCCCC | 13.59 | 21440633 | |
118 | Phosphorylation | EYETSHISDTPVSLS HHHHCCCCCCCCCCC | 29.97 | 20377248 | |
120 | Phosphorylation | ETSHISDTPVSLSSA HHCCCCCCCCCCCCC | 20.85 | 21551504 | |
123 | Phosphorylation | HISDTPVSLSSANDR CCCCCCCCCCCCCCH | 24.60 | 21551504 | |
125 | Phosphorylation | SDTPVSLSSANDRES CCCCCCCCCCCCHHH | 21.65 | 26447709 | |
126 | Phosphorylation | DTPVSLSSANDRESL CCCCCCCCCCCHHHH | 36.06 | 19779198 | |
321 | Phosphorylation | RLEEFHISNTHRFTD CEEEEEECCCCCCCC | 27.40 | 27017623 |
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 RAD7_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAD7_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 RAD7_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-64; SER-85 AND TYR-96,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-107, AND MASSSPECTROMETRY. |