REV3L_HUMAN
ID REV3L_HUMAN Reviewed; 3130 AA.
AC O60673; O43214; Q5TC33;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=DNA polymerase zeta catalytic subunit;
DE EC=2.7.7.7;
DE AltName: Full=Protein reversionless 3-like;
DE Short=REV3-like;
DE Short=hREV3;
GN Name=REV3L; Synonyms=POLZ, REV3;
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), AND VARIANT ILE-1224.
RC TISSUE=Fetal brain;
RX PubMed=9618506; DOI=10.1073/pnas.95.12.6876;
RA Gibbs P.E.M., McGregor W.G., Maher V.M., Nisson P., Lawrence C.W.;
RT "A human homolog of the Saccharomyces cerevisiae REV3 gene, which encodes
RT the catalytic subunit of DNA polymerase zeta.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6876-6880(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-1224.
RC TISSUE=Bone marrow, and Leukocyte;
RX PubMed=10102035; DOI=10.1016/s0921-8777(98)00065-2;
RA Lin W., Wu X., Wang Z.;
RT "A full-length cDNA of hREV3 is predicted to encode DNA polymerase zeta for
RT damage-induced mutagenesis in humans.";
RL Mutat. Res. 433:89-98(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-1224.
RA Murakumo Y., Rasio D., Roth T., Negrini M., Croce C.M., Fishel R.;
RT "Cloning and characterization of hREV3, the human homolog of S. cerevisiae
RT REV3.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS HIS-231; CYS-1156;
RP ILE-1224 AND GLU-1540.
RC TISSUE=Testis;
RX PubMed=9925914; DOI=10.1159/000015157;
RA Morelli C., Mungall A.J., Negrini M., Barbanti-Brodano G., Croce C.M.;
RT "Alternative splicing, genomic structure, and fine chromosome localization
RT of REV3L.";
RL Cytogenet. Cell Genet. 83:18-20(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-397; THR-693; GLN-962;
RP CYS-1156; ILE-1224; THR-1302; HIS-1309; THR-1339; PRO-1469; LEU-1576;
RP ASN-1713; THR-1724; SER-1791; HIS-1812; ARG-1923; HIS-1970; VAL-2015;
RP MET-2075; GLN-2762 AND ILE-3064.
RG NIEHS SNPs program;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 70-3130 (ISOFORM 1), VARIANTS HIS-231;
RP CYS-1156; ILE-1224 AND GLU-1540, AND INTERACTION WITH MAD2L2.
RX PubMed=10660610; DOI=10.1074/jbc.275.6.4391;
RA Murakumo Y., Roth T., Ishii H., Rasio D., Numata S., Croce C.M., Fishel R.;
RT "A human REV7 homolog that interacts with the polymerase zeta catalytic
RT subunit hREV3 and the spindle assembly checkpoint protein hMAD2.";
RL J. Biol. Chem. 275:4391-4397(2000).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1030 AND THR-1041, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1724 AND SER-1967, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP FUNCTION, IDENTIFICATION IN POL-ZETA COMPLEX, AND MUTAGENESIS OF ASP-2614
RP AND ASP-2783.
RX PubMed=24449906; DOI=10.1073/pnas.1324001111;
RA Lee Y.S., Gregory M.T., Yang W.;
RT "Human Pol zeta purified with accessory subunits is active in translesion
RT DNA synthesis and complements Pol eta in cisplatin bypass.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:2954-2959(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1847-1898 IN COMPLEX WITH MAD2L2.
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).
CC -!- FUNCTION: Catalytic subunit of the DNA polymerase zeta complex, an
CC error-prone polymerase specialized in translesion DNA synthesis (TLS).
CC Lacks an intrinsic 3'-5' exonuclease activity and thus has no
CC proofreading function. {ECO:0000269|PubMed:24449906}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P14284};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P14284};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.71 uM for dATP (for Pol-zeta2);
CC KM=1.17 uM for dATP (for Pol-zeta4);
CC Note=kcat is 0.31 min(-1) for DNA synthesis by Pol-zeta4. kcat is
CC 0.05 min(-1) for DNA synthesis by Pol-zeta2.
CC {ECO:0000269|PubMed:24449906};
CC -!- SUBUNIT: Heterodimer with MAD2L2. This dimer forms the minimal DNA
CC polymerase zeta complex (Pol-zeta2), with REV3L bearing DNA polymerase
CC catalytic activity, although its activity is very low in this context.
CC Component of the tetrameric Pol-zeta complex (Pol-zeta4), which
CC consists of REV3L, MAD2L2, POLD2 and POLD3; Pol-zeta4 is the fully
CC active form of DNA polymerase zeta. {ECO:0000269|PubMed:10660610,
CC ECO:0000269|PubMed:20164194, ECO:0000269|PubMed:24449906}.
CC -!- INTERACTION:
CC O60673; Q9UI95: MAD2L2; NbExp=5; IntAct=EBI-2871302, EBI-77889;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60673-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60673-2; Sequence=VSP_024121;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DOMAIN: Its C-terminal part could serve as the catalytic domain during
CC nucleotide polymerization, while its N-terminal part could provide
CC sites for protein-protein interactions with other factors during
CC translesion DNA synthesis.
CC -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC formation of polymerase complexes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rev3l/";
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DR EMBL; AF058701; AAC24357.1; -; mRNA.
DR EMBL; AF071798; AAC24009.1; -; mRNA.
DR EMBL; AF157476; AAD40184.1; -; mRNA.
DR EMBL; AF179428; AAG09402.1; -; mRNA.
DR EMBL; AF179429; AAG09403.1; -; mRNA.
DR EMBL; AF078695; AAC28460.1; -; mRNA.
DR EMBL; AY684169; AAT74627.1; -; Genomic_DNA.
DR EMBL; AL080317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF035537; AAB88486.1; -; mRNA.
DR CCDS; CCDS5091.2; -. [O60673-1]
DR CCDS; CCDS69177.1; -. [O60673-2]
DR RefSeq; NP_001273360.1; NM_001286431.1. [O60673-2]
DR RefSeq; NP_001273361.1; NM_001286432.1. [O60673-2]
DR RefSeq; NP_002903.3; NM_002912.4. [O60673-1]
DR PDB; 3ABD; X-ray; 1.90 A; X/Y=1847-1898.
DR PDB; 3ABE; X-ray; 2.60 A; Z=1847-1898.
DR PDB; 3VU7; X-ray; 2.80 A; Z=1847-1898.
DR PDB; 4EXT; X-ray; 1.90 A; B=1873-1895.
DR PDB; 4GK0; X-ray; 2.70 A; C/D=1847-1898.
DR PDB; 4GK5; X-ray; 3.21 A; C/D=1847-1898.
DR PDB; 5O8K; X-ray; 1.80 A; B=1873-1898.
DR PDB; 6BC8; X-ray; 1.68 A; B=1987-2014.
DR PDB; 6BCD; X-ray; 1.43 A; B=1987-2014.
DR PDB; 6BI7; X-ray; 2.80 A; B/D/F/H=1987-2014.
DR PDB; 6EKM; X-ray; 2.76 A; B=1989-2014.
DR PDB; 6KEA; X-ray; 2.35 A; A/B/C/D=1850-1872, A/B/C/D=1887-1894.
DR PDB; 6WS0; X-ray; 2.24 A; ZZZ=1847-1898.
DR PDB; 6WS5; X-ray; 2.47 A; ZZZ=1847-1898.
DR PDBsum; 3ABD; -.
DR PDBsum; 3ABE; -.
DR PDBsum; 3VU7; -.
DR PDBsum; 4EXT; -.
DR PDBsum; 4GK0; -.
DR PDBsum; 4GK5; -.
DR PDBsum; 5O8K; -.
DR PDBsum; 6BC8; -.
DR PDBsum; 6BCD; -.
DR PDBsum; 6BI7; -.
DR PDBsum; 6EKM; -.
DR PDBsum; 6KEA; -.
DR PDBsum; 6WS0; -.
DR PDBsum; 6WS5; -.
DR SASBDB; O60673; -.
DR SMR; O60673; -.
DR BioGRID; 111912; 39.
DR ComplexPortal; CPX-994; DNA polymerase zeta complex.
DR CORUM; O60673; -.
DR IntAct; O60673; 14.
DR MINT; O60673; -.
DR STRING; 9606.ENSP00000351697; -.
DR GlyGen; O60673; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60673; -.
DR PhosphoSitePlus; O60673; -.
DR BioMuta; REV3L; -.
DR CPTAC; CPTAC-3252; -.
DR CPTAC; CPTAC-3253; -.
DR CPTAC; CPTAC-944; -.
DR EPD; O60673; -.
DR jPOST; O60673; -.
DR MassIVE; O60673; -.
DR MaxQB; O60673; -.
DR PaxDb; O60673; -.
DR PeptideAtlas; O60673; -.
DR PRIDE; O60673; -.
DR ProteomicsDB; 49517; -. [O60673-1]
DR ProteomicsDB; 49518; -. [O60673-2]
DR Antibodypedia; 32376; 105 antibodies from 23 providers.
DR DNASU; 5980; -.
DR Ensembl; ENST00000358835.7; ENSP00000351697.3; ENSG00000009413.16. [O60673-1]
DR Ensembl; ENST00000368802.8; ENSP00000357792.3; ENSG00000009413.16. [O60673-1]
DR Ensembl; ENST00000435970.5; ENSP00000402003.1; ENSG00000009413.16. [O60673-2]
DR GeneID; 5980; -.
DR KEGG; hsa:5980; -.
DR MANE-Select; ENST00000368802.8; ENSP00000357792.3; NM_001372078.1; NP_001359007.1.
DR UCSC; uc003puy.6; human. [O60673-1]
DR CTD; 5980; -.
DR DisGeNET; 5980; -.
DR GeneCards; REV3L; -.
DR HGNC; HGNC:9968; REV3L.
DR HPA; ENSG00000009413; Tissue enhanced (brain).
DR MalaCards; REV3L; -.
DR MIM; 602776; gene.
DR neXtProt; NX_O60673; -.
DR OpenTargets; ENSG00000009413; -.
DR Orphanet; 570; Moebius syndrome.
DR PharmGKB; PA34337; -.
DR VEuPathDB; HostDB:ENSG00000009413; -.
DR eggNOG; KOG0968; Eukaryota.
DR GeneTree; ENSGT00940000156226; -.
DR HOGENOM; CLU_000203_1_0_1; -.
DR InParanoid; O60673; -.
DR OMA; PVSSCEN; -.
DR OrthoDB; 20210at2759; -.
DR PhylomeDB; O60673; -.
DR TreeFam; TF101072; -.
DR PathwayCommons; O60673; -.
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 SignaLink; O60673; -.
DR BioGRID-ORCS; 5980; 450 hits in 1083 CRISPR screens.
DR ChiTaRS; REV3L; human.
DR EvolutionaryTrace; O60673; -.
DR GeneWiki; REV3L; -.
DR GenomeRNAi; 5980; -.
DR Pharos; O60673; Tbio.
DR PRO; PR:O60673; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O60673; protein.
DR Bgee; ENSG00000009413; Expressed in calcaneal tendon and 204 other tissues.
DR ExpressionAtlas; O60673; baseline and differential.
DR Genevisible; O60673; HS.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016035; C:zeta DNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006261; P:DNA-templated DNA replication; TAS:ProtInc.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0042276; P:error-prone translesion synthesis; IDA:ComplexPortal.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 1.
DR IDEAL; IID00259; -.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR032757; DUF4683.
DR InterPro; IPR030559; PolZ_Rev3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR PANTHER; PTHR45812; PTHR45812; 2.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 2.
DR Pfam; PF15735; DUF4683; 1.
DR Pfam; PF14260; zf-C4pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Alternative splicing; DNA damage; DNA repair;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase; Iron;
KW Iron-sulfur; Metal-binding; Nucleotidyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..3130
FT /note="DNA polymerase zeta catalytic subunit"
FT /id="PRO_0000046468"
FT ZN_FING 3042..3057
FT /note="CysA-type"
FT REGION 263..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1537..1600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1845..1882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1847..1898
FT /note="Mediates interaction with MAD2L2"
FT /evidence="ECO:0000269|PubMed:10660610"
FT REGION 1962..1984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2017..2050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2080..2150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2216..2236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3086..3104
FT /note="CysB motif"
FT COMPBIAS 700..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1060
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1537..1565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1574..1588
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1845..1876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1962..1983
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2080..2096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2222..2236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3042
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 3045
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 3054
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 3057
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 3086
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 3089
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 3099
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 3104
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MOD_RES 1030
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1041
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1724
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1967
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..78
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9925914"
FT /id="VSP_024121"
FT VARIANT 231
FT /note="Q -> H (in dbSNP:rs1053911)"
FT /evidence="ECO:0000269|PubMed:10660610,
FT ECO:0000269|PubMed:9925914"
FT /id="VAR_008516"
FT VARIANT 389
FT /note="S -> T"
FT /id="VAR_008517"
FT VARIANT 397
FT /note="Q -> P (in dbSNP:rs3218579)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022226"
FT VARIANT 633
FT /note="S -> G (in dbSNP:rs3218598)"
FT /id="VAR_048883"
FT VARIANT 693
FT /note="M -> T (in dbSNP:rs3218593)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022227"
FT VARIANT 962
FT /note="R -> Q (in dbSNP:rs17539588)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022228"
FT VARIANT 1156
FT /note="Y -> C (in dbSNP:rs458017)"
FT /evidence="ECO:0000269|PubMed:10660610,
FT ECO:0000269|PubMed:9925914, ECO:0000269|Ref.5"
FT /id="VAR_022229"
FT VARIANT 1220
FT /note="S -> L (in dbSNP:rs3218600)"
FT /id="VAR_048884"
FT VARIANT 1224
FT /note="T -> I (in dbSNP:rs462779)"
FT /evidence="ECO:0000269|PubMed:10102035,
FT ECO:0000269|PubMed:10660610, ECO:0000269|PubMed:9618506,
FT ECO:0000269|PubMed:9925914, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.5"
FT /id="VAR_022230"
FT VARIANT 1284
FT /note="T -> P (in dbSNP:rs3218578)"
FT /id="VAR_048885"
FT VARIANT 1302
FT /note="S -> T (in dbSNP:rs3218597)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022231"
FT VARIANT 1309
FT /note="Q -> H (in dbSNP:rs3218595)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022232"
FT VARIANT 1339
FT /note="P -> T (in dbSNP:rs17539616)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022233"
FT VARIANT 1469
FT /note="Q -> P (in dbSNP:rs3218572)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022234"
FT VARIANT 1540
FT /note="K -> E (in dbSNP:rs1053913)"
FT /evidence="ECO:0000269|PubMed:10660610,
FT ECO:0000269|PubMed:9925914"
FT /id="VAR_008518"
FT VARIANT 1576
FT /note="S -> L (in dbSNP:rs3218582)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022235"
FT VARIANT 1713
FT /note="D -> N (in dbSNP:rs3218585)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022236"
FT VARIANT 1724
FT /note="S -> T (in dbSNP:rs17539644)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022237"
FT VARIANT 1791
FT /note="P -> S (in dbSNP:rs17539651)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022238"
FT VARIANT 1812
FT /note="D -> H (in dbSNP:rs3218599)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022239"
FT VARIANT 1923
FT /note="G -> R (in dbSNP:rs3218604)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022240"
FT VARIANT 1970
FT /note="R -> H (in dbSNP:rs3218606)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022241"
FT VARIANT 2015
FT /note="E -> V (in dbSNP:rs17539692)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022242"
FT VARIANT 2075
FT /note="I -> M (in dbSNP:rs17510963)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022243"
FT VARIANT 2607
FT /note="S -> T"
FT /id="VAR_008519"
FT VARIANT 2762
FT /note="R -> Q (in dbSNP:rs3218592)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022244"
FT VARIANT 3064
FT /note="V -> I (in dbSNP:rs3204953)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_016147"
FT MUTAGEN 2614
FT /note="D->N: Loss of DNA polymerase catalytic activity;
FT when associated with N-2783."
FT /evidence="ECO:0000269|PubMed:24449906"
FT MUTAGEN 2783
FT /note="D->N: Loss of DNA polymerase catalytic activity;
FT when associated with N-2614."
FT /evidence="ECO:0000269|PubMed:24449906"
FT CONFLICT 237
FT /note="E -> Q (in Ref. 4; AAC28460 and 7; AAB88486)"
FT /evidence="ECO:0000305"
FT STRAND 1877..1882
FT /evidence="ECO:0007829|PDB:5O8K"
FT HELIX 1887..1894
FT /evidence="ECO:0007829|PDB:5O8K"
FT STRAND 1991..1998
FT /evidence="ECO:0007829|PDB:6BCD"
FT HELIX 2003..2012
FT /evidence="ECO:0007829|PDB:6BCD"
SQ SEQUENCE 3130 AA; 352776 MW; 4FBAA214639DF3C6 CRC64;
MFSVRIVTAD YYMASPLQGL DTCQSPLTQA PVKKVPVVRV FGATPAGQKT CLHLHGIFPY
LYVPYDGYGQ QPESYLSQMA FSIDRALNVA LGNPSSTAQH VFKVSLVSGM PFYGYHEKER
HFMKIYLYNP TMVKRICELL QSGAIMNKFY QPHEAHIPYL LQLFIDYNLY GMNLINLAAV
KFRKARRKSN TLHATGSCKN HLSGNSLADT LFRWEQDEIP SSLILEGVEP QSTCELEVDA
VAADILNRLD IEAQIGGNPG LQAIWEDEKQ RRRNRNETSQ MSQPESQDHR FVPATESEKK
FQKRLQEILK QNDFSVTLSG SVDYSDGSQE FSAELTLHSE VLSPEMLQCT PANMVEVHKD
KESSKGHTRH KVEEALINEE AILNLMENSQ TFQPLTQRLS ESPVFMDSSP DEALVHLLAG
LESDGYRGER NRMPSPCRSF GNNKYPQNSD DEENEPQIEK EEMELSLVMS QRWDSNIEEH
CAKKRSLCRN THRSSTEDDD SSSGEEMEWS DNSLLLASLS IPQLDGTADE NSDNPLNNEN
SRTHSSVIAT SKLSVKPSIF HKDAATLEPS SSAKITFQCK HTSALSSHVL NKEDLIEDLS
QTNKNTEKGL DNSVTSFTNE STYSMKYPGS LSSTVHSENS HKENSKKEIL PVSSCESSIF
DYEEDIPSVT RQVPSRKYTN IRKIEKDSPF IHMHRHPNEN TLGKNSFNFS DLNHSKNKVS
SEGNEKGNST ALSSLFPSSF TENCELLSCS GENRTMVHSL NSTADESGLN KLKIRYEEFQ
EHKTEKPSLS QQAAHYMFFP SVVLSNCLTR PQKLSPVTYK LQPGNKPSRL KLNKRKLAGH
QETSTKSSET GSTKDNFIQN NPCNSNPEKD NALASDLTKT TRGAFENKTP TDGFIDCHFG
DGTLETEQSF GLYGNKYTLR AKRKVNYETE DSESSFVTHN SKISLPHPME IGESLDGTLK
SRKRRKMSKK LPPVIIKYII INRFRGRKNM LVKLGKIDSK EKQVILTEEK MELYKKLAPL
KDFWPKVPDS PATKYPIYPL TPKKSHRRKS KHKSAKKKTG KQQRTNNENI KRTLSFRKKR
SHAILSPPSP SYNAETEDCD LNYSDVMSKL GFLSERSTSP INSSPPRCWS PTDPRAEEIM
AAAEKEAMLF KGPNVYKKTV NSRIGKTSRA RAQIKKSKAK LANPSIVTKK RNKRNQTNKL
VDDGKKKPRA KQKTNEKGTS RKHTTLKDEK IKSQSGAEVK FVLKHQNVSE FASSSGGSQL
LFKQKDMPLM GSAVDHPLSA SLPTGINAQQ KLSGCFSSFL ESKKSVDLQT FPSSRDDLHP
SVVCNSIGPG VSKINVQRPH NQSAMFTLKE STLIQKNIFD LSNHLSQVAQ NTQISSGMSS
KIEDNANNIQ RNYLSSIGKL SEYRNSLESK LDQAYTPNFL HCKDSQQQIV CIAEQSKHSE
TCSPGNTASE ESQMPNNCFV TSLRSPIKQI AWEQKQRGFI LDMSNFKPER VKPRSLSEAI
SQTKALSQCK NRNVSTPSAF GEGQSGLAVL KELLQKRQQK AQNANTTQDP LSNKHQPNKN
ISGSLEHNKA NKRTRSVTSP RKPRTPRSTK QKEKIPKLLK VDSLNLQNSS QLDNSVSDDS
PIFFSDPGFE SCYSLEDSLS PEHNYNFDIN TIGQTGFCSF YSGSQFVPAD QNLPQKFLSD
AVQDLFPGQA IEKNEFLSHD NQKCDEDKHH TTDSASWIRS GTLSPEIFEK STIDSNENRR
HNQWKNSFHP LTTRSNSIMD SFCVQQAEDC LSEKSRLNRS SVSKEVFLSL PQPNNSDWIQ
GHTRKEMGQS LDSANTSFTA ILSSPDGELV DVACEDLELY VSRNNDMLTP TPDSSPRSTS
SPSQSKNGSF TPRTANILKP LMSPPSREEI MATLLDHDLS ETIYQEPFCS NPSDVPEKPR
EIGGRLLMVE TRLANDLAEF EGDFSLEGLR LWKTAFSAMT QNPRPGSPLR SGQGVVNKGS
SNSPKMVEDK KIVIMPCKCA PSRQLVQVWL QAKEEYERSK KLPKTKPTGV VKSAENFSSS
VNPDDKPVVP PKMDVSPCIL PTTAHTKEDV DNSQIALQAP TTGCSQTASE SQMLPPVASA
SDPEKDEDDD DNYYISYSSP DSPVIPPWQQ PISPDSKALN GDDRPSSPVE ELPSLAFENF
LKPIKDGIQK SPCSEPQEPL VISPINTRAR TGKCESLCFH STPIIQRKLL ERLPEAPGLS
PLSTEPKTQK LSNKKGSNTD TLRRVLLTQA KNQFAAVNTP QKETSQIDGP SLNNTYGFKV
SIQNLQEAKA LHEIQNLTLI SVELHARTRR DLEPDPEFDP ICALFYCISS DTPLPDTEKT
ELTGVIVIDK DKTVFSQDIR YQTPLLIRSG ITGLEVTYAA DEKALFHEIA NIIKRYDPDI
LLGYEIQMHS WGYLLQRAAA LSIDLCRMIS RVPDDKIENR FAAERDEYGS YTMSEINIVG
RITLNLWRIM RNEVALTNYT FENVSFHVLH QRFPLFTFRV LSDWFDNKTD LYRWKMVDHY
VSRVRGNLQM LEQLDLIGKT SEMARLFGIQ FLHVLTRGSQ YRVESMMLRI AKPMNYIPVT
PSVQQRSQMR APQCVPLIME PESRFYSNSV LVLDFQSLYP SIVIAYNYCF STCLGHVENL
GKYDEFKFGC TSLRVPPDLL YQVRHDITVS PNGVAFVKPS VRKGVLPRML EEILKTRFMV
KQSMKAYKQD RALSRMLDAR QLGLKLIANV TFGYTSANFS GRMPCIEVGD SIVHKARETL
ERAIKLVNDT KKWGARVVYG DTDSMFVLLK GATKEQSFKI GQEIAEAVTA TNPKPVKLKF
EKVYLPCVLQ TKKRYVGYMY ETLDQKDPVF DAKGIETVRR DSCPAVSKIL ERSLKLLFET
RDISLIKQYV QRQCMKLLEG KASIQDFIFA KEYRGSFSYK PGACVPALEL TRKMLTYDRR
SEPQVGERVP YVIIYGTPGV PLIQLVRRPV EVLQDPTLRL NATYYITKQI LPPLARIFSL
IGIDVFSWYH ELPRIHKATS SSRSEPEGRK GTISQYFTTL HCPVCDDLTQ HGICSKCRSQ
PQHVAVILNQ EIRELERQQE QLVKICKNCT GCFDRHIPCV SLNCPVLFKL SRVNRELSKA
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