{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9UBZ9","secondaryAccessions":["O95941","Q53SI7","Q9C0J4","Q9NUP2"],"uniProtkbId":"REV1_HUMAN","entryAudit":{"firstPublicDate":"2005-02-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2000-05-01","entryVersion":193,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Translesion synthesis protein REV1"}},"alternativeNames":[{"fullName":{"value":"Alpha integrin-binding protein 80"},"shortNames":[{"value":"AIBP80"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22691049"}],"value":"Molecular adapter protein REV1"}},{"fullName":{"value":"Rev1-like terminal deoxycytidyl transferase"}},{"fullName":{"value":"Reversionless protein 1 homolog"},"shortNames":[{"value":"REV1 homolog"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Template-dependent deoxycytidyl transferase REV1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10536157"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11278384"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11711549"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16263170"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38612916"}],"value":"2.7.7.-"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:14060"}],"value":"REV1"},"synonyms":[{"value":"REV1L"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q920Q2"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10536157"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11278384"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11711549"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16263170"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23143872"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38612916"}],"value":"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)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"DNA(n) + dCTP = DNA(n)-C + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:86319"},{"database":"Rhea","id":"RHEA-COMP:17339"},{"database":"Rhea","id":"RHEA-COMP:20773"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61481"},{"database":"ChEBI","id":"CHEBI:173112"},{"database":"ChEBI","id":"CHEBI:235524"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10536157"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11278384"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11711549"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38612916"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:86320"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10536157"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11278384"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11711549"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38612916"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P12689"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":0.04,"unit":"uM","substrate":"dCMP (with guanine template nucleotide)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38612916"}]},{"constant":10.13,"unit":"uM","substrate":"dCMP (with 8-oxoguanine lesion template nucleotide)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38612916"}]},{"constant":0.06,"unit":"uM","substrate":"dCMP (with guanine template nucleotide)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38612916"}]},{"constant":2.92,"unit":"uM","substrate":"dCMP (with 6-O-methylguanine lesion template nucleotide)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38612916"}]},{"constant":10.6,"unit":"uM","substrate":"dCMP (with adenine template nucleotide)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38612916"}]},{"constant":56.81,"unit":"uM","substrate":"dCMP (with 7-deaza-adenine artificial lesion template nucleotide)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38612916"}]},{"constant":72.02,"unit":"uM","substrate":"dCMP (with adenine template nucleotide)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38612916"}]},{"constant":2.18,"unit":"uM","substrate":"dCMP (with 1,N6-ethenoadenine lesion template nucleotide)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38612916"}]},{"constant":301.73,"unit":"uM","substrate":"dCMP (with thymine template nucleotide)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38612916"}]},{"constant":1.08,"unit":"uM","substrate":"dCMP (with thymine glycol lersion template nucleotide)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38612916"}]}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q920Q2"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10094488"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11485998"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12529368"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19464298"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20164194"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22266823"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22691049"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23143872"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26982350"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29778604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29864443"}],"value":"Monomer (By similarity). Homodimer (PubMed:23143872). Homotetramer (PubMed:19464298). Interacts (via C-terminal domain) with the DNA polymerase zeta complex which is composed of REV3L and MAD2L2; the interaction with MAD2L2 is direct, and REV3L forms and stabilizes the DNA polymerase zeta complex before being recruited by REV1 to the DNA lesion site (PubMed:11485998, PubMed:12529368, PubMed:20164194, PubMed:23143872). Forms a quaternary complex with POLK, MAD2L2 and REV3L, where REV3L-bound MAD2L2 and POLK are able to bind simultaneously to REV1 forming the stable translesion synthesis (TLS) machinery therefore bridging the inserter and extender polymerases (PubMed:23143872). May bind ITGA3 (PubMed:10094488). Interacts with FAAP20 (via UBZ2-type zinc finger); this interaction contributes to the stable association of the two proteins in nuclear foci in response to replication stress (PubMed:22266823). Interacts (via C-terminal domain) with POLH (PubMed:22691049). Interacts (via C-terminal domain) with POLD3 (PubMed:26982350). Interacts with UBB (PubMed:29778604, PubMed:29864443). Interacts (via C-terminal domain) with POLK; POLK competes with MAD2L2 for binding to REV1 (By similarity). Interacts (via C-terminal domain) with POLI (By similarity). Interacts (via BRCT domain) with PCNA; this interaction is enhanced with a monoubiquitinated form of PCNA and mediates the recruitment of REV1 to stalled DNA replication (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q9UBZ9","intActId":"EBI-7353917"},"interactantTwo":{"uniProtKBAccession":"Q6NZ36","geneName":"FAAP20","intActId":"EBI-2817693"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22266823"}],"value":"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)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22266823"}],"value":"Nucleus","id":"SL-0191"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"synonyms":[{"value":"REV1"}],"isoformIds":["Q9UBZ9-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"synonyms":[{"value":"REV1S"}],"isoformIds":["Q9UBZ9-2"],"sequenceIds":["VSP_012812"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["Q9UBZ9-3"],"sequenceIds":["VSP_012809","VSP_012810","VSP_012811"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10536157"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11278384"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11485998"}],"value":"Ubiquitous"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16263170"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22691049"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23143872"}],"value":"The C-terminal domain mediates interaction with the major translesion synthesis (TLS) polymerases, POLH, POLI, and POLK, and the adapter subunit MAD2L2 of DNA polymerase zeta complex and is essential for tolerance of DNA damage caused by a number of mutagens (PubMed:16263170, PubMed:22691049, PubMed:23143872). The C-terminal domain can binds simultaneously both POLK and the MAD2L2 subunit of DNA polymerase zeta complex, bridging the inserter and extender polymerases during TLS (PubMed:23143872)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q920Q2"}],"value":"The BRCT domain promotes resistance to DNA damage by mediating interaction with PCNA and localization to nuclear foci"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q920Q2"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29778604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29864443"}],"value":"Ubiquitin-binding motif (UBM) domains contribute to DNA damage tolerance and damage-induced mutagenesis by enhancing both REV1's interaction with monoubiquitinated PCNA and association with replication foci (By similarity). Only the UBM2 domain mediates UBB binding (PubMed:29778604, PubMed:29864443)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22266823"}],"value":"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)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the DNA polymerase type-Y family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1251,"modifier":"EXACT"}},"description":"Translesion synthesis protein 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