UniProt ID | RAD1_YEAST | |
---|---|---|
UniProt AC | P06777 | |
Protein Name | DNA repair protein RAD1 | |
Gene Name | RAD1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1100 | |
Subcellular Localization | Nucleus. | |
Protein Description | Involved in nucleotide excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Along with RAD10 forms an endonuclease that specifically degrades single-stranded DNA.. | |
Protein Sequence | MSQLFYQGDSDDELQEELTRQTTQASQSSKIKNEDEPDDSNHLNEVENEDSKVLDDDAVLYPLIPNEPDDIETSKPNINDIRPVDIQLTLPLPFQQKVVENSLITEDALIIMGKGLGLLDIVANLLHVLATPTSINGQLKRALVLVLNAKPIDNVRIKEALEELSWFSNTGKDDDDTAVESDDELFERPFNVVTADSLSIEKRRKLYISGGILSITSRILIVDLLSGIVHPNRVTGMLVLNADSLRHNSNESFILEIYRSKNTWGFIKAFSEAPETFVMEFSPLRTKMKELRLKNVLLWPRFRVEVSSCLNATNKTSHNKVIEVKVSLTNSMSQIQFGLMECLKKCIAELSRKNPELALDWWNMENVLDINFIRSIDSVMVPNWHRISYESKQLVKDIRFLRHLLKMLVTSDAVDFFGEIQLSLDANKPSVSRKYSESPWLLVDEAQLVISYAKKRIFYKNEYTLEENPKWEQLIHILHDISHERMTNHLQGPTLVACSDNLTCLELAKVLNASNKKRGVRQVLLNKLKWYRKQREETKKLVKEVQSQDTFPENATLNVSSTFSKEQVTTKRRRTRGASQVAAVEKLRNAGTNVDMEVVFEDHKLSEEIKKGSGDDLDDGQEENAANDSKIFEIQEQENEILIDDGDAEFDNGELEYVGDLPQHITTHFNKDLWAEHCNEYEYVDRQDEILISTFKSLNDNCSLQEMMPSYIIMFEPDISFIRQIEVYKAIVKDLQPKVYFMYYGESIEEQSHLTAIKREKDAFTKLIRENANLSHHFETNEDLSHYKNLAERKLKLSKLRKSNTRNAGGQQGFHNLTQDVVIVDTREFNASLPGLLYRYGIRVIPCMLTVGDYVITPDICLERKSISDLIGSLQNNRLANQCKKMLKYYAYPTLLIEFDEGQSFSLEPFSERRNYKNKDISTVHPISSKLSQDEIQLKLAKLVLRFPTLKIIWSSSPLQTVNIILELKLGREQPDPSNAVILGTNKVRSDFNSTAKGLKDGDNESKFKRLLNVPGVSKIDYFNLRKKIKSFNKLQKLSWNEINELINDEDLTDRIYYFLRTEKEEQEQESTDENLESPGKTTDDNALHDHHNDVPEAPV | |
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 | ------MSQLFYQGD ------CCCCCCCCC | 47.06 | 30377154 | |
6 | Phosphorylation | --MSQLFYQGDSDDE --CCCCCCCCCCCHH | 21.85 | 30377154 | |
10 | Phosphorylation | QLFYQGDSDDELQEE CCCCCCCCCHHHHHH | 54.51 | 28152593 | |
26 | Phosphorylation | TRQTTQASQSSKIKN HHHHHHHHHHHCCCC | 22.30 | 27214570 | |
40 | Phosphorylation | NEDEPDDSNHLNEVE CCCCCCCCCCHHHHC | 33.26 | 25704821 | |
51 | Phosphorylation | NEVENEDSKVLDDDA HHHCCCCCCCCCCCC | 20.63 | 28889911 | |
181 | Phosphorylation | DDDTAVESDDELFER CCCCCCCCCHHHHHC | 43.70 | 28889911 | |
592 | Phosphorylation | EKLRNAGTNVDMEVV HHHHHCCCCCCEEEE | 29.65 | 28889911 | |
613 | Phosphorylation | SEEIKKGSGDDLDDG HHHHHCCCCCCCCCC | 48.18 | 23749301 | |
629 | Phosphorylation | EENAANDSKIFEIQE CCCCCCCCCCEEEHH | 27.71 | 21551504 | |
1062 | Phosphorylation | RIYYFLRTEKEEQEQ HHHHHHHCHHHHHHH | 54.26 | 30377154 | |
1071 | Phosphorylation | KEEQEQESTDENLES HHHHHHHCCCCCCCC | 40.63 | 17563356 | |
1072 | Phosphorylation | EEQEQESTDENLESP HHHHHHCCCCCCCCC | 46.72 | 17563356 | |
1078 | Phosphorylation | STDENLESPGKTTDD CCCCCCCCCCCCCCC | 41.96 | 21551504 |
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 RAD1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAD1_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 RAD1_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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-1071 AND THR-1072, ANDMASS SPECTROMETRY. |