ID REV1_HUMAN Reviewed; 1251 AA.
AC Q9UBZ9; O95941; Q53SI7; Q9C0J4; Q9NUP2;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 183.
DE RecName: Full=DNA repair protein REV1;
DE EC=2.7.7.-;
DE AltName: Full=Alpha integrin-binding protein 80;
DE Short=AIBP80;
DE AltName: Full=Rev1-like terminal deoxycytidyl transferase;
GN Name=REV1; Synonyms=REV1L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow, Leukocyte, and T-cell;
RX PubMed=10536157; DOI=10.1093/nar/27.22.4468;
RA Lin W., Xin H., Zhang X., Wu X., Yuan F., Wang Z.;
RT "The human REV1 gene codes for a DNA template-dependent dCMP transferase.";
RL Nucleic Acids Res. 27:4468-4475(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ROLE IN UV-INDUCED MUTAGENESIS.
RC TISSUE=Brain;
RX PubMed=10760286; DOI=10.1073/pnas.97.8.4186;
RA Gibbs P.E.M., Wang X.-D., Li Z., McManus T.P., McGregor W.G.,
RA Lawrence C.W., Maher V.M.;
RT "The function of the human homolog of Saccharomyces cerevisiae REV1 is
RT required for mutagenesis induced by UV light.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4186-4191(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, MUTAGENESIS OF
RP ASP-570 AND GLU-571, AND TISSUE SPECIFICITY.
RC TISSUE=Mammary cancer, and Testis;
RX PubMed=11278384; DOI=10.1074/jbc.m008082200;
RA Masuda Y., Takahashi M., Tsunekuni N., Minami T., Sumii M., Miyagawa K.,
RA Kamiya K.;
RT "Deoxycytidyl transferase activity of the human REV1 protein is closely
RT associated with the conserved polymerase domain.";
RL J. Biol. Chem. 276:15051-15058(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH REV3L AND MAD2L2.
RC TISSUE=Testis;
RX PubMed=11485998; DOI=10.1074/jbc.m102051200;
RA Murakumo Y., Ogura Y., Ishii H., Numata S., Ichihara M., Croce C.M.,
RA Fishel R., Takahashi M.;
RT "Interactions in the error-prone postreplication repair proteins hREV1,
RT hREV3, and hREV7.";
RL J. Biol. Chem. 276:35644-35651(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 479-1251 (ISOFORM 2), AND INTERACTION WITH
RP ITGA3.
RC TISSUE=Placenta;
RX PubMed=10094488; DOI=10.1016/s0014-5793(99)00151-9;
RA Wixler V., Laplantine E., Geerts D., Sonnenberg A., Petersohn D., Eckes B.,
RA Paulsson M., Aumailley M.;
RT "Identification of novel interaction partners for the conserved membrane
RT proximal region of alpha-integrin cytoplasmic domains.";
RL FEBS Lett. 445:351-355(1999).
RN [8]
RP INTERACTION WITH MAD2L2.
RX PubMed=12529368; DOI=10.1074/jbc.m211765200;
RA Masuda Y., Ohmae M., Masuda K., Kamiya K.;
RT "Structure and enzymatic properties of a stable complex of the human REV1
RT and REV7 proteins.";
RL J. Biol. Chem. 278:12356-12360(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP INTERACTION WITH DNA POLYMERASE ZETA.
RX PubMed=20164194; DOI=10.1074/jbc.m109.092403;
RA Hara K., Hashimoto H., Murakumo Y., Kobayashi S., Kogame T., Unzai S.,
RA Akashi S., Takeda S., Shimizu T., Sato M.;
RT "Crystal structure of human REV7 in complex with a human REV3 fragment and
RT structural implication of the interaction between DNA polymerase zeta and
RT REV1.";
RL J. Biol. Chem. 285:12299-12307(2010).
RN [11]
RP FUNCTION, AND INTERACTION WITH C1ORF86.
RX PubMed=22266823; DOI=10.1038/nsmb.2222;
RA Kim H., Yang K., Dejsuphong D., D'Andrea A.D.;
RT "Regulation of Rev1 by the Fanconi anemia core complex.";
RL Nat. Struct. Mol. Biol. 19:164-170(2012).
RN [12]
RP STRUCTURE BY NMR OF 43-133.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the BRCT domain from human DNA repair protein
RT REV1.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Deoxycytidyl transferase involved in DNA repair. Transfers a
CC dCMP residue from dCTP to the 3'-end of a DNA primer in a template-
CC dependent reaction. May assist in the first step in the bypass of
CC abasic lesions by the insertion of a nucleotide opposite the lesion.
CC Required for normal induction of mutations by physical and chemical
CC agents. {ECO:0000269|PubMed:10536157, ECO:0000269|PubMed:10760286,
CC ECO:0000269|PubMed:11278384, ECO:0000269|PubMed:11485998,
CC ECO:0000269|PubMed:22266823}.
CC -!- SUBUNIT: Monomer. Interacts with the DNA polymerase zeta which is
CC composed of REV3L and MAD2L2; the interaction with MAD2L2 is direct and
CC requires that REV3L is in its closed conformation. Interacts with POLH,
CC POLI and POLK. May bind ITGA3. Interacts with FAAP20/C1orf86.
CC {ECO:0000269|PubMed:10094488, ECO:0000269|PubMed:11485998,
CC ECO:0000269|PubMed:12529368, ECO:0000269|PubMed:20164194,
CC ECO:0000269|PubMed:22266823}.
CC -!- INTERACTION:
CC Q9UBZ9; Q6NZ36: FAAP20; NbExp=2; IntAct=EBI-7353917, EBI-2817693;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=REV1;
CC IsoId=Q9UBZ9-1; Sequence=Displayed;
CC Name=2; Synonyms=REV1S;
CC IsoId=Q9UBZ9-2; Sequence=VSP_012812;
CC Name=3;
CC IsoId=Q9UBZ9-3; Sequence=VSP_012809, VSP_012810, VSP_012811;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10536157,
CC ECO:0000269|PubMed:11278384, ECO:0000269|PubMed:11485998}.
CC -!- DOMAIN: The C-terminal domain is necessary for protein interactions.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK43708.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF151538; AAF06731.1; -; mRNA.
DR EMBL; AF206019; AAF18986.1; -; mRNA.
DR EMBL; AB047646; BAB21441.1; -; mRNA.
DR EMBL; AF357886; AAK43708.1; ALT_INIT; mRNA.
DR EMBL; AK002087; BAA92079.1; -; mRNA.
DR EMBL; AC018690; AAY24314.1; -; Genomic_DNA.
DR EMBL; AJ131720; CAB38231.1; -; mRNA.
DR CCDS; CCDS2045.1; -. [Q9UBZ9-1]
DR CCDS; CCDS42722.1; -. [Q9UBZ9-2]
DR RefSeq; NP_001032961.1; NM_001037872.2. [Q9UBZ9-2]
DR RefSeq; NP_001308383.1; NM_001321454.1.
DR RefSeq; NP_001308384.1; NM_001321455.1.
DR RefSeq; NP_001308387.1; NM_001321458.1.
DR RefSeq; NP_001308388.1; NM_001321459.1.
DR RefSeq; NP_001308389.1; NM_001321460.1.
DR RefSeq; NP_057400.1; NM_016316.3. [Q9UBZ9-1]
DR PDB; 2EBW; NMR; -; A=44-133.
DR PDB; 2LSI; NMR; -; A=1156-1251.
DR PDB; 2LSK; NMR; -; A=1158-1251.
DR PDB; 2LSY; NMR; -; A=1158-1251.
DR PDB; 2N1G; NMR; -; A=1158-1251.
DR PDB; 3GQC; X-ray; 2.50 A; A/B/C/D=330-833.
DR PDB; 3VU7; X-ray; 2.80 A; H=1140-1251.
DR PDB; 4BA9; X-ray; 2.73 A; A/B/C/D/E/F=1158-1242.
DR PDB; 4EXT; X-ray; 1.90 A; A=1156-1251.
DR PDB; 4GK0; X-ray; 2.70 A; E/F=1117-1251.
DR PDB; 4GK5; X-ray; 3.21 A; E/F=1117-1251.
DR PDB; 5VZM; NMR; -; B=933-1040.
DR PDB; 6ASR; X-ray; 2.36 A; B=998-1040.
DR PDB; 6AXD; NMR; -; A=998-1040.
DR PDB; 6WS0; X-ray; 2.24 A; HHH=1158-1251.
DR PDB; 6WS5; X-ray; 2.47 A; HHH=1158-1251.
DR PDBsum; 2EBW; -.
DR PDBsum; 2LSI; -.
DR PDBsum; 2LSK; -.
DR PDBsum; 2LSY; -.
DR PDBsum; 2N1G; -.
DR PDBsum; 3GQC; -.
DR PDBsum; 3VU7; -.
DR PDBsum; 4BA9; -.
DR PDBsum; 4EXT; -.
DR PDBsum; 4GK0; -.
DR PDBsum; 4GK5; -.
DR PDBsum; 5VZM; -.
DR PDBsum; 6ASR; -.
DR PDBsum; 6AXD; -.
DR PDBsum; 6WS0; -.
DR PDBsum; 6WS5; -.
DR AlphaFoldDB; Q9UBZ9; -.
DR BMRB; Q9UBZ9; -.
DR SMR; Q9UBZ9; -.
DR BioGRID; 119551; 35.
DR CORUM; Q9UBZ9; -.
DR IntAct; Q9UBZ9; 7.
DR MINT; Q9UBZ9; -.
DR STRING; 9606.ENSP00000258428; -.
DR BindingDB; Q9UBZ9; -.
DR ChEMBL; CHEMBL4295973; -.
DR CarbonylDB; Q9UBZ9; -.
DR GlyGen; Q9UBZ9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UBZ9; -.
DR PhosphoSitePlus; Q9UBZ9; -.
DR BioMuta; REV1; -.
DR DMDM; 59798439; -.
DR EPD; Q9UBZ9; -.
DR jPOST; Q9UBZ9; -.
DR MassIVE; Q9UBZ9; -.
DR MaxQB; Q9UBZ9; -.
DR PaxDb; 9606-ENSP00000258428; -.
DR PeptideAtlas; Q9UBZ9; -.
DR ProteomicsDB; 84105; -. [Q9UBZ9-1]
DR ProteomicsDB; 84106; -. [Q9UBZ9-2]
DR ProteomicsDB; 84107; -. [Q9UBZ9-3]
DR Antibodypedia; 32824; 185 antibodies from 29 providers.
DR DNASU; 51455; -.
DR Ensembl; ENST00000258428.8; ENSP00000258428.3; ENSG00000135945.10. [Q9UBZ9-1]
DR Ensembl; ENST00000393445.7; ENSP00000377091.3; ENSG00000135945.10. [Q9UBZ9-2]
DR GeneID; 51455; -.
DR KEGG; hsa:51455; -.
DR MANE-Select; ENST00000258428.8; ENSP00000258428.3; NM_016316.4; NP_057400.1.
DR UCSC; uc002tac.4; human. [Q9UBZ9-1]
DR AGR; HGNC:14060; -.
DR CTD; 51455; -.
DR DisGeNET; 51455; -.
DR GeneCards; REV1; -.
DR HGNC; HGNC:14060; REV1.
DR HPA; ENSG00000135945; Low tissue specificity.
DR MIM; 606134; gene.
DR neXtProt; NX_Q9UBZ9; -.
DR OpenTargets; ENSG00000135945; -.
DR PharmGKB; PA162401120; -.
DR VEuPathDB; HostDB:ENSG00000135945; -.
DR eggNOG; KOG2093; Eukaryota.
DR GeneTree; ENSGT00940000156374; -.
DR HOGENOM; CLU_003901_0_1_1; -.
DR InParanoid; Q9UBZ9; -.
DR OMA; IKNGMWM; -.
DR OrthoDB; 169741at2759; -.
DR PhylomeDB; Q9UBZ9; -.
DR TreeFam; TF314488; -.
DR PathwayCommons; Q9UBZ9; -.
DR Reactome; R-HSA-110312; Translesion synthesis by REV1.
DR Reactome; R-HSA-5655862; Translesion synthesis by POLK.
DR Reactome; R-HSA-5656121; Translesion synthesis by POLI.
DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR SignaLink; Q9UBZ9; -.
DR SIGNOR; Q9UBZ9; -.
DR BioGRID-ORCS; 51455; 76 hits in 1154 CRISPR screens.
DR ChiTaRS; REV1; human.
DR EvolutionaryTrace; Q9UBZ9; -.
DR GeneWiki; REV1; -.
DR GenomeRNAi; 51455; -.
DR Pharos; Q9UBZ9; Tbio.
DR PRO; PR:Q9UBZ9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UBZ9; Protein.
DR Bgee; ENSG00000135945; Expressed in secondary oocyte and 195 other cell types or tissues.
DR ExpressionAtlas; Q9UBZ9; baseline and differential.
DR Genevisible; Q9UBZ9; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc.
DR GO; GO:0017125; F:deoxycytidyl transferase activity; IBA:GO_Central.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR GO; GO:0070987; P:error-free translesion synthesis; IBA:GO_Central.
DR GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR CDD; cd17719; BRCT_Rev1; 1.
DR CDD; cd01701; PolY_Rev1; 1.
DR CDD; cd12145; Rev1_C; 1.
DR CDD; cd19318; Rev1_UBM2; 2.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.1170.60; -; 1.
DR Gene3D; 6.10.250.1490; -; 1.
DR Gene3D; 6.10.250.1630; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 1.
DR Gene3D; 1.20.58.1280; DNA repair protein Rev1, C-terminal domain; 1.
DR IDEAL; IID00284; -.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR InterPro; IPR012112; REV1.
DR InterPro; IPR031991; Rev1_C.
DR InterPro; IPR038401; Rev1_C_sf.
DR InterPro; IPR047346; Rev1_UBM1/2.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR PANTHER; PTHR45990; DNA REPAIR PROTEIN REV1; 1.
DR PANTHER; PTHR45990:SF1; DNA REPAIR PROTEIN REV1; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF00817; IMS; 2.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF21704; POLH-Rev1_HhH; 1.
DR Pfam; PF16727; REV1_C; 1.
DR Pfam; PF14377; UBM; 2.
DR PIRSF; PIRSF036573; REV1; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50173; UMUC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA damage; DNA repair; DNA synthesis;
KW DNA-binding; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..1251
FT /note="DNA repair protein REV1"
FT /id="PRO_0000173992"
FT DOMAIN 44..131
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 419..653
FT /note="UmuC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT REGION 206..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..362
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 653..656
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 709..717
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 1035..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1249
FT /note="Protein interaction domain; mediates interaction
FT with DNA polymerase zeta"
FT MOTIF 1071..1078
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1039..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1082
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 357
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 423..427
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 423
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 510..516
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 522
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 570
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 570
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 571
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT SITE 770
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 783
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012809"
FT VAR_SEQ 406..413
FT /note="DMSVLNSP -> RYLLKLSS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012810"
FT VAR_SEQ 414..1251
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012811"
FT VAR_SEQ 479
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10094488,
FT ECO:0000303|PubMed:11278384"
FT /id="VSP_012812"
FT VARIANT 138
FT /note="V -> M (in dbSNP:rs3087403)"
FT /id="VAR_021249"
FT VARIANT 257
FT /note="F -> S (in dbSNP:rs3087386)"
FT /id="VAR_021250"
FT VARIANT 306
FT /note="N -> D (in dbSNP:rs28382882)"
FT /id="VAR_029193"
FT VARIANT 373
FT /note="N -> S (in dbSNP:rs3087399)"
FT /id="VAR_021251"
FT VARIANT 656
FT /note="M -> V (in dbSNP:rs3087394)"
FT /id="VAR_029194"
FT VARIANT 660
FT /note="L -> W (in dbSNP:rs3087398)"
FT /id="VAR_029195"
FT VARIANT 700
FT /note="D -> N (in dbSNP:rs28382941)"
FT /id="VAR_029196"
FT VARIANT 704
FT /note="R -> Q (in dbSNP:rs28382942)"
FT /id="VAR_029197"
FT VARIANT 902
FT /note="P -> H (in dbSNP:rs28382961)"
FT /id="VAR_029199"
FT VARIANT 902
FT /note="P -> S (in dbSNP:rs28382960)"
FT /id="VAR_029198"
FT VARIANT 921
FT /note="S -> I (in dbSNP:rs3087396)"
FT /id="VAR_029200"
FT VARIANT 1003
FT /note="A -> T (in dbSNP:rs3087401)"
FT /id="VAR_024436"
FT VARIANT 1060
FT /note="P -> T (in dbSNP:rs3087388)"
FT /id="VAR_029201"
FT VARIANT 1074
FT /note="N -> K (in dbSNP:rs3087393)"
FT /id="VAR_029202"
FT VARIANT 1091
FT /note="N -> T (in dbSNP:rs3087392)"
FT /id="VAR_029203"
FT VARIANT 1102
FT /note="L -> P (in dbSNP:rs3087400)"
FT /id="VAR_029204"
FT MUTAGEN 570
FT /note="D->A: Abolishes transferase activity; when
FT associated with A-571."
FT /evidence="ECO:0000269|PubMed:11278384"
FT MUTAGEN 571
FT /note="E->A: Abolishes transferase activity; when
FT associated with A-570."
FT /evidence="ECO:0000269|PubMed:11278384"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:2EBW"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:2EBW"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:2EBW"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2EBW"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2EBW"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:2EBW"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2EBW"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:2EBW"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2EBW"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 357..375
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:3GQC"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 427..432
FT /evidence="ECO:0007829|PDB:3GQC"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:3GQC"
FT TURN 437..441
FT /evidence="ECO:0007829|PDB:3GQC"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 463..471
FT /evidence="ECO:0007829|PDB:3GQC"
FT TURN 472..475
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:3GQC"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 513..516
FT /evidence="ECO:0007829|PDB:3GQC"
FT TURN 517..519
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 526..532
FT /evidence="ECO:0007829|PDB:3GQC"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 543..558
FT /evidence="ECO:0007829|PDB:3GQC"
FT STRAND 564..568
FT /evidence="ECO:0007829|PDB:3GQC"
FT STRAND 571..575
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 577..583
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 587..602
FT /evidence="ECO:0007829|PDB:3GQC"
FT STRAND 606..613
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 614..624
FT /evidence="ECO:0007829|PDB:3GQC"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 634..636
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 637..643
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 646..648
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 654..662
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 668..671
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 676..683
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 685..694
FT /evidence="ECO:0007829|PDB:3GQC"
FT TURN 695..697
FT /evidence="ECO:0007829|PDB:3GQC"
FT STRAND 712..716
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 725..745
FT /evidence="ECO:0007829|PDB:3GQC"
FT STRAND 748..760
FT /evidence="ECO:0007829|PDB:3GQC"
FT STRAND 776..790
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 793..805
FT /evidence="ECO:0007829|PDB:3GQC"
FT HELIX 811..813
FT /evidence="ECO:0007829|PDB:3GQC"
FT STRAND 814..826
FT /evidence="ECO:0007829|PDB:3GQC"
FT STRAND 936..939
FT /evidence="ECO:0007829|PDB:5VZM"
FT HELIX 940..943
FT /evidence="ECO:0007829|PDB:5VZM"
FT HELIX 948..955
FT /evidence="ECO:0007829|PDB:5VZM"
FT HELIX 960..963
FT /evidence="ECO:0007829|PDB:5VZM"
FT TURN 973..979
FT /evidence="ECO:0007829|PDB:5VZM"
FT HELIX 985..987
FT /evidence="ECO:0007829|PDB:5VZM"
FT HELIX 1004..1009
FT /evidence="ECO:0007829|PDB:6ASR"
FT HELIX 1013..1015
FT /evidence="ECO:0007829|PDB:6ASR"
FT HELIX 1018..1022
FT /evidence="ECO:0007829|PDB:6ASR"
FT HELIX 1026..1037
FT /evidence="ECO:0007829|PDB:6ASR"
FT STRAND 1160..1162
FT /evidence="ECO:0007829|PDB:3VU7"
FT HELIX 1165..1178
FT /evidence="ECO:0007829|PDB:4EXT"
FT HELIX 1184..1199
FT /evidence="ECO:0007829|PDB:4EXT"
FT HELIX 1203..1218
FT /evidence="ECO:0007829|PDB:4EXT"
FT HELIX 1223..1243
FT /evidence="ECO:0007829|PDB:4EXT"
FT STRAND 1245..1248
FT /evidence="ECO:0007829|PDB:4EXT"
SQ SEQUENCE 1251 AA; 138248 MW; 010E261D537DBA80 CRC64;
MRRGGWRKRA ENDGWETWGG YMAAKVQKLE EQFRSDAAMQ KDGTSSTIFS GVAIYVNGYT
DPSAEELRKL MMLHGGQYHV YYSRSKTTHI IATNLPNAKI KELKGEKVIR PEWIVESIKA
GRLLSYIPYQ LYTKQSSVQK GLSFNPVCRP EDPLPGPSNI AKQLNNRVNH IVKKIETENE
VKVNGMNSWN EEDENNDFSF VDLEQTSPGR KQNGIPHPRG STAIFNGHTP SSNGALKTQD
CLVPMVNSVA SRLSPAFSQE EDKAEKSSTD FRDCTLQQLQ QSTRNTDALR NPHRTNSFSL
SPLHSNTKIN GAHHSTVQGP SSTKSTSSVS TFSKAAPSVP SKPSDCNFIS NFYSHSRLHH
ISMWKCELTE FVNTLQRQSN GIFPGREKLK KMKTGRSALV VTDTGDMSVL NSPRHQSCIM
HVDMDCFFVS VGIRNRPDLK GKPVAVTSNR GTGRAPLRPG ANPQLEWQYY QNKILKGKAA
DIPDSSLWEN PDSAQANGID SVLSRAEIAS CSYEARQLGI KNGMFFGHAK QLCPNLQAVP
YDFHAYKEVA QTLYETLASY THNIEAVSCD EALVDITEIL AETKLTPDEF ANAVRMEIKD
QTKCAASVGI GSNILLARMA TRKAKPDGQY HLKPEEVDDF IRGQLVTNLP GVGHSMESKL
ASLGIKTCGD LQYMTMAKLQ KEFGPKTGQM LYRFCRGLDD RPVRTEKERK SVSAEINYGI
RFTQPKEAEA FLLSLSEEIQ RRLEATGMKG KRLTLKIMVR KPGAPVETAK FGGHGICDNI
ARTVTLDQAT DNAKIIGKAM LNMFHTMKLN ISDMRGVGIH VNQLVPTNLN PSTCPSRPSV
QSSHFPSGSY SVRDVFQVQK AKKSTEEEHK EVFRAAVDLE ISSASRTCTF LPPFPAHLPT
SPDTNKAESS GKWNGLHTPV SVQSRLNLSI EVPSPSQLDQ SVLEALPPDL REQVEQVCAV
QQAESHGDKK KEPVNGCNTG ILPQPVGTVL LQIPEPQESN SDAGINLIAL PAFSQVDPEV
FAALPAELQR ELKAAYDQRQ RQGENSTHQQ SASASVPKNP LLHLKAAVKE KKRNKKKKTI
GSPKRIQSPL NNKLLNSPAK TLPGACGSPQ KLIDGFLKHE GPPAEKPLEE LSASTSGVPG
LSSLQSDPAG CVRPPAPNLA GAVEFNDVKT LLREWITTIS DPMEEDILQV VKYCTDLIEE
KDLEKLDLVI KYMKRLMQQS VESVWNMAFD FILDNVQVVL QQTYGSTLKV T
//
