| Tag | Content |
|---|
| CPLM ID | CPLM-024796 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | SprT-like domain-containing protein Spartan |
Protein Synonyms/Alias | Protein with SprT-like domain at the N terminus; Spartan |
Gene Name | Sprtn |
Gene Synonyms/Alias | Gm505 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 342 | RVSVANQKAFRNVNG | ubiquitination | [1] | | 432 | RTALDTIKEQTQSGG | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Regulator of UV-induced DNA damage response: acts as a 'reader' of ubiquitinated PCNA that enhances RAD18-mediated PCNA ubiquitination and translesion DNA synthesis (TLS). Recruited to sites of UV damage and interacts with ubiquitinated PCNA and RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA. Facilitates chromatin association of RAD18 and is required for efficient PCNA monoubiquitination, promoting a feed-forward loop to enhance PCNA ubiquitination and translesion DNA synthesis. Acts as a regulator of TLS by recruiting VCP/p97 to sites of DNA damage, possibly leading to extraction of DNA polymerase eta (POLH) by VCP/p97 to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage (By similarity). |
Sequence Annotation | DOMAIN 46 213 SprT-like.
ZN_FING 462 485 UBZ-type.
MOTIF 254 262 SHP-box.
MOTIF 326 333 PIP-box. |
Keyword | Chromosome; Complete proteome; DNA damage; DNA repair; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 497 AA |
Protein Sequence | MDEDLVVALR LQEEWDVQMA RRAAAAREPV SLVDASWELV DPTPDLQALF LQFNDRFFWG 60
QLEAVEVKWS VRMTLCAGIC TYEGRGGMCS IRLSEPLLKL RPRKDLVETL LHEMIHAYLF 120
VTNNDKDREG HGPEFCKHMH RINQLTGANI TVYHTFHDEV DEYRRHWWRC NGPCQHRQPY 180
YGYVKRATNR APSVHDYWWA DHQKTCGGTY IKIKEPENYS KKGRGKTKAD KQPASAVENK 240
DKLCRGEAQL LIPFSGKGYV LGDASTCPSA GKLNTSYMVN EAKGLSSQDH SVSGLRLNSN 300
AEVKCEQNCL PKKPHLVSPL PTASHQSVLS SYFPRVSVAN QKAFRNVNGS PVKNGTTGDG 360
TKRPASGGSQ RKVPPSRASL RNTSKVTAPA SATVTSAAGT SATISREESG SEDQFLNKRP 420
RLEDRTALDT IKEQTQSGGD LRSSSQPTAA SAPQSLSSQR RLVNCPVCQG VVVESQINEH 480
LDRCLEGNKT NLRPRRV 497 |
Gene Ontology | GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. GO:0016607; C:nuclear speck; IEA:Compara. GO:0005634; C:nucleus; ISS:UniProtKB. GO:0070530; F:K63-linked polyubiquitin binding; ISS:UniProtKB. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB. GO:0009411; P:response to UV; ISS:UniProtKB. GO:0019985; P:translesion synthesis; ISS:UniProtKB. |
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Pfam | |
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PRINTS | |