REV1
entrez
51455
canonical
uniprot
Q9UBZ9
canonical
ensembl
ENSG00000135945
resolver
ensp
ENSP00000258428
resolver
ensp
ENSP00000377091
resolver
ensp
ENSP00000549722
resolver
ensp
ENSP00000549723
resolver
ensp
ENSP00000549724
resolver
ensp
ENSP00000590336
resolver
ensp
ENSP00000619124
resolver
ensp
ENSP00000707885
resolver
genesymbol
REV1
resolver
genesymbol_syn
REV1L
resolver
hgnc
HGNC:14060
resolver
uniprot
O95941
resolver
uniprot
Q49AI5
resolver
uniprot
Q53SI7
resolver
uniprot
Q9C0J4
resolver
uniprot
Q9NUP2
resolver
uniprot_entry
Q49AI5_HUMAN
resolver
uniprot_entry
REV1_HUMAN
resolver
uniprot_sec
O95941
resolver
uniprot_sec
Q53SI7
resolver
uniprot_sec
Q9C0J4
resolver
uniprot_sec
Q9NUP2
resolver
amino_acid_sequence
MRRGGWRKRAENDGWETWGGYMAAKVQKLEEQFRSDAAMQKDGTSSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLLSYIPYQLYTKQSSVQKGLSFNPVCRPEDPLPGPSNIAKQLNNRVNHIVKKIETENEVKVNGMNSWNEEDENNDFSFVDLEQTSPGRKQNGIPHPRGSTAIFNGHTPSSNGALKTQDCLVPMVNSVASRLSPAFSQEEDKAEKSSTDFRDCTLQQLQQSTRNTDALRNPHRTNSFSLSPLHSNTKINGAHHSTVQGPSSTKSTSSVSTFSKAAPSVPSKPSDCNFISNFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPGREKLKKMKTGRSALVVTDTGDMSVLNSPRHQSCIMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRAPLRPGANPQLEWQYYQNKILKGKAADIPDSSLWENPDSAQANGIDSVLSRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQLVPTNLNPSTCPSRPSVQSSHFPSGSYSVRDVFQVQKAKKSTEEEHKEVFRAAVDLEISSASRTCTFLPPFPAHLPTSPDTNKAESSGKWNGLHTPVSVQSRLNLSIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQAESHGDKKKEPVNGCNTGILPQPVGTVLLQIPEPQESNSDAGINLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQRQGENSTHQQSASASVPKNPLLHLKAAVKEKKRNKKKKTIGSPKRIQSPLNNKLLNSPAKTLPGACGSPQKLIDGFLKHEGPPAEKPLEELSASTSGVPGLSSLQSDPAGCVRPPAPNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT
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:16263170, PubMed:23143872). 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:23143872). 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:23143872). 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:10536157, PubMed:11278384, PubMed:38612916). 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:10536157, PubMed:11711549, PubMed:38612916). 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:16263170). In addition, exhibits a 5'-deoxyribose-5-phosphate lyase activity in vitro, though its necessity in vivo is not confirmed (By similarity). {ECO:0000250|UniProtKB:Q920Q2, ECO:0000269|PubMed:10536157, ECO:0000269|PubMed:11278384, ECO:0000269|PubMed:11711549, ECO:0000269|PubMed:16263170, ECO:0000269|PubMed:23143872, ECO:0000269|PubMed:38612916}.
uniprot
proteins
mass_dalton
138248
uniprot
proteins
mutagenesis
MUTAGEN 570..571; /note="DE->AA: Loss of deoxycytidyl transferase activity."; /evidence="ECO:0000269|PubMed:11711549"; MUTAGEN 570; /note="D->A: Abolishes transferase activity; when associated with A-571."; /evidence="ECO:0000269|PubMed:11278384"; MUTAGEN 571; /note="E->A: Abolishes transferase activity; when associated with A-570."; /evidence="ECO:0000269|PubMed:11278384"; MUTAGEN 946; /note="L->A: Loss of monoubiquitination; when associated with A-947, A-1024 and A-1025."; /evidence="ECO:0000269|PubMed:22266823"; MUTAGEN 947; /note="P->A: Loss of monoubiquitination; when associated with A-946, A-1024 and A-1025."; /evidence="ECO:0000269|PubMed:22266823"; MUTAGEN 958; /note="C->S: Does not affect UBB binding; when associated with A-977."; /evidence="ECO:0000269|PubMed:29864443"; MUTAGEN 977; /note="C->A: Does not affect UBB binding; when associated with A-977."; /evidence="ECO:0000269|PubMed:29864443"; MUTAGEN 1024; /note="L->A: Loss of monoubiquitination; when associated with A-946, A-947 and A-1025."; /evidence="ECO:0000269|PubMed:22266823"; MUTAGEN 1025; /note="P->A: Loss of monoubiquitination; when associated with A-946, A-947 and A-1024."; /evidence="ECO:0000269|PubMed:22266823
uniprot
proteins
post_translational_modification
PTM: Monoubiquitinated (PubMed:22266823). Undergoes a ubiquitination-deubiquitination cycle (PubMed:22266823). 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 (PubMed:22266823). {ECO:0000269|PubMed:22266823}.
uniprot
proteins
protein_family
DNA polymerase type-Y family
uniprot
proteins
pubmed
10094488
uniprot
proteins
pubmed
10536157
uniprot
proteins
pubmed
10760286
uniprot
proteins
pubmed
11278384
uniprot
proteins
pubmed
11485998
uniprot
proteins
pubmed
11711549
uniprot
proteins
pubmed
12529368
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16263170
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19464298
uniprot
proteins
pubmed
20164194
uniprot
proteins
pubmed
22266823
uniprot
proteins
pubmed
22691049
uniprot
proteins
pubmed
23143872
uniprot
proteins
pubmed
26982350
uniprot
proteins
pubmed
29778604
uniprot
proteins
pubmed
29864443
uniprot
proteins
pubmed
38612916
uniprot
proteins
sequence_length
1251
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22266823}. 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 (PubMed:22266823). 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:22266823). {ECO:0000269|PubMed:22266823}.
uniprot
proteins