Rev1
entrez
56210
canonical
uniprot
Q920Q2
canonical
ensembl
ENSMUSG00000026082
resolver
ensp
ENSMUSP00000027251
resolver
ensp
ENSMUSP00000199806
resolver
ensp
ENSMUSP00000199807
resolver
ensp
ENSMUSP00000199809
resolver
ensp
ENSMUSP00000199811
resolver
ensp
ENSMUSP00000199814
resolver
ensp
ENSMUSP00000199821
resolver
ensp
ENSMUSP00000199825
resolver
ensp
ENSMUSP00000199842
resolver
enst
ENSMUST00000027251
resolver
genesymbol
Rev1
resolver
genesymbol_syn
Rev1l
resolver
uniprot
Q9QXV2
resolver
uniprot_entry
REV1_MOUSE
resolver
uniprot_sec
Q9QXV2
resolver
amino_acid_sequence
MRRGGWRKRTENDGWEKWGGYMAAKVQKLEEQFRTDAANQKDGTASAIFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLLSSAPYQLYTKPSAAQKSLNFNPVCKPEDPGPGPSNRAKQLNNRVNHIIKKIETESEVKANGLSSWNEDGVNDDFSFEDLEHTFPGRKQNGVMHPRDTAVIFNGHTHSSNGALKTQDCLVPVGNSVASRLSLDSTQEEKRAEKSNADFRDCTVQHLQHSTRSADALRSPHRTNSLSPSLHSNTKINGAHHSTVQGPSSTKSTSVLTLSKVAPSVPSKPSDCNFISDFYSRSRLHHISTWKCELTEFVNTLQRQSSGIFPGREKLKKVKTGRSSLVVTDTGTMSVLSSPRHQSCVMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGTAPLRPGANPQLEWQYYQNRALRGKAADIPDSSVWENQDSTQTNGIDSVLSKAEIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKIMVRKPGAPIETAKFGGHGICDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQVNQLVPANSNLSTCSSRPSAQSSLFSGRPHSVRDLFQLQKAKKPTEEEHKEVFLAAVDLEVSSTSRACGLLSPLSAHLAASVSPDTNSGECSRKWNGLHSPVSGQSRLNLSIEVPSPSQIDQSVLEALPLDLREQIEQVCAAQQGEPRGKKKEPVNGCSSGVLPHPVGTVLLQIPEPQEPCNSDSKISVIALPAFSQVDPDVFAALPAELQKELKAAYDQRQRQGEDTTHQQPTSTSVPKNPLLQLKPPAMKDKRNKRKNLIGSPRKSPLKNKLLSSPAKTLPGAYGSPQKLMDGFLQHEGMASERPLEEVSASTPGAQDLSSLLPGQSSCFRPAAPNLAGAVEFSDVKTLLKEWITTISDPMEEDILQVVRYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT
uniprot
proteins
ec_number
2.7.7.-
uniprot
proteins
function
FUNCTION: Bifunctional protein involved in the maintenance of genome stability through translesion DNA synthesis (TLS) and antibody diversification via somatic hypermutation (PubMed:14657033, PubMed:16476771, PubMed:22859295). Functions as a molecular adapter protein at stalled DNA replication, coordinating polymerases recruitment, selection, and switching, in a manner independent of its deoxycytidyl transferase activity (PubMed:14657033, PubMed:22859295). At the site of DNA lesion, recruits and mediates the switch between low-fidelity inserter DNA polymerases, such as POLK, that incorporate nucleotides opposite lesions and the extender DNA polymerase zeta complex which continues DNA synthesis from distorted primer termini (PubMed:14657033, PubMed:22859295). In vitro, acts as a template-dependent deoxycytidyl transferase that preferentially incorporates deoxycytidine residues from dCTP to the 3'-end of a DNA primer opposite apurinic/apyrimidinic (AP) site, uracil, undamaged DNA templates (G > A > C > T) and a variety of damaged DNA templates (PubMed:11711549). Opposite template guanine, efficiently incorporates not only dCMP but also non-complementary dGMP and dTMP, with lower efficiency for dAMP, demonstrating low fidelity on undamaged DNA (PubMed:11711549). This catalytic activity has been implicated in somatic hypermutation, likely achieved by incorporation of deoxycytidine opposite abasic sites, generated at cytidines via activation-induced deoxycytidine deaminase (AID)-mediated deamination and uracil DNA glycosylase (UNG) activity, respectively (PubMed:16476771). In addition, exhibits a 5'-deoxyribose-5-phosphate lyase activity in vitro, though its necessity in vivo is not confirmed (PubMed:16476771). {ECO:0000269|PubMed:11711549, ECO:0000269|PubMed:14657033, ECO:0000269|PubMed:16476771, ECO:0000269|PubMed:22859295}.
uniprot
proteins
mass_dalton
137341
uniprot
proteins
mutagenesis
MUTAGEN 1199; /note="K->E: Fails to complement the cisplatin-induced DNA damage in chicken DT40 cells lacking the REV1 gene. Does not affect protein expression level."; /evidence="ECO:0000269|PubMed:22859295"; MUTAGEN 1242; /note="Y->A: Loss of interaction with MAD2L2."; /evidence="ECO:0000269|PubMed:22859295"; MUTAGEN 1246; /note="L->A: Loss of interaction with MAD2L2."; /evidence="ECO:0000269|PubMed:22859295"; MUTAGEN 1247; /note="K->E: Loss of interaction with MAD2L2."; /evidence="ECO:0000269|PubMed:22859295
uniprot
proteins
post_translational_modification
PTM: Monoubiquitinated (PubMed:16982685). Undergoes a ubiquitination-deubiquitination cycle. The monoubiquitination is not required for FAAP20 interaction but enhances it, contributing to the stable association of the two proteins at DNA lesions in response to replication stress (By similarity). {ECO:0000250|UniProtKB:Q9UBZ9, ECO:0000269|PubMed:16982685}.
uniprot
proteins
protein_family
DNA polymerase type-Y family
uniprot
proteins
pubmed
11711549
uniprot
proteins
pubmed
14657033
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16476771
uniprot
proteins
pubmed
16857592
uniprot
proteins
pubmed
16982685
uniprot
proteins
pubmed
22700975
uniprot
proteins
pubmed
22859295
uniprot
proteins
pubmed
27683219
uniprot
proteins
sequence_length
1249
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16857592, ECO:0000269|PubMed:16982685}. Note=In response to replication stress, is recruited to stalled DNA replication through recognition of monoubiquitinated PCNA, and accumulates in nuclear foci in a process facilitated by FAAP20 binding (By similarity). Nuclear foci localization likely reflects the recruitment of REV1 to DNA lesions in response to replication stress, and depends on its ubiquitin-binding motif (UBM) domains (PubMed:16857592, PubMed:16982685). {ECO:0000250|UniProtKB:Q9UBZ9, ECO:0000269|PubMed:16857592, ECO:0000269|PubMed:16982685}.
uniprot
proteins