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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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. DR Genevisible; Q9UBZ9; HS. 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 //