| Tag | Content |
|---|
| CPLM ID | CPLM-006193 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | UV excision repair protein RAD23 |
Protein Synonyms/Alias | |
Gene Name | RAD23 |
Gene Synonyms/Alias | YEL037C; SYGP-ORF29 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 13 | FKNFKKEKVPLDLEP | ubiquitination | [1] | | 30 | TILETKTKLAQSISC | ubiquitination | [1] | | 49 | IKLIYSGKVLQDSKT | ubiquitination | [1, 2] | | 55 | GKVLQDSKTVSECGL | ubiquitination | [1] | | 81 | QKKSTKTKVTEPPIA | ubiquitination | [1] |
|
Reference | [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J. Nat Methods. 2013 Jul;10(7):676-82. [ PMID: 23749301] [2] Sites of ubiquitin attachment in Saccharomyces cerevisiae. Starita LM, Lo RS, Eng JK, von Haller PD, Fields S. Proteomics. 2012 Jan;12(2):236-40. [ PMID: 22106047] |
Functional Description | Plays a central role both in proteasomal degradation of misfolded proteins and DNA repair. Central component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol. Involved in DNA excision repair. May play a part in DNA damage recognition and/or in altering chromatin structure to allow access by damage- processing enzymes. |
Sequence Annotation | DOMAIN 1 77 Ubiquitin-like.
DOMAIN 146 186 UBA 1.
DOMAIN 355 395 UBA 2.
MOD_RES 94 94 Phosphothreonine.
MOD_RES 121 121 Phosphoserine.
MOD_RES 139 139 Phosphothreonine. |
Keyword | 3D-structure; Complete proteome; Cytoplasm; DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation pathway. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 398 AA |
Protein Sequence | MVSLTFKNFK KEKVPLDLEP SNTILETKTK LAQSISCEES QIKLIYSGKV LQDSKTVSEC 60
GLKDGDQVVF MVSQKKSTKT KVTEPPIAPE SATTPGRENS TEASPSTDAS AAPAATAPEG 120
SQPQEEQTAT TERTESASTP GFVVGTERNE TIERIMEMGY QREEVERALR AAFNNPDRAV 180
EYLLMGIPEN LRQPEPQQQT AAAAEQPSTA ATTAEQPAED DLFAQAAQGG NASSGALGTT 240
GGATDAAQGG PPGSIGLTVE DLLSLRQVVS GNPEALAPLL ENISARYPQL REHIMANPEV 300
FVSMLLEAVG DNMQDVMEGA DDMVEGEDIE VTGEAAAAGL GQGEGEGSFQ VDYTPEDDQA 360
ISRLCELGFE RDLVIQVYFA CDKNEEAAAN ILFSDHAD 398 |
Gene Ontology | GO:0005739; C:mitochondrion; IDA:SGD. GO:0000111; C:nucleotide-excision repair factor 2 complex; IDA:SGD. GO:0000502; C:proteasome complex; IMP:SGD. GO:0003684; F:damaged DNA binding; IDA:SGD. GO:0043130; F:ubiquitin binding; IDA:SGD. GO:0030433; P:ER-associated protein catabolic process; IMP:SGD. GO:0000715; P:nucleotide-excision repair, DNA damage recognition; TAS:SGD. GO:0006517; P:protein deglycosylation; IDA:SGD. |
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Pfam | |
SMART | |
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PRINTS | |