GenomeNet

Database: UniProt
Entry: REV3L_HUMAN
LinkDB: REV3L_HUMAN
Original site: 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-JUL-2019, entry version 172.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   encodes 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
RT   zeta for 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.
RT   cerevisiae REV3.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS HIS-231;
RP   CYS-1156; ILE-1224 AND GLU-1540.
RC   TISSUE=Testis;
RX   PubMed=9925914;
RA   Morelli C., Mungall A.J., Negrini M., Barbanti-Brodano G., Croce C.M.;
RT   "Alternative splicing, genomic structure, and fine chromosome
RT   localization of REV3L.";
RL   Cytogenet. Cell Genet. 83:18-20(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-397; THR-693;
RP   GLN-962; CYS-1156; ILE-1224; THR-1302; HIS-1309; THR-1339; PRO-1469;
RP   LEU-1576; ASN-1713; THR-1724; SER-1791; HIS-1812; ARG-1923; HIS-1970;
RP   VAL-2015; 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.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   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.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA   Fishel R.;
RT   "A human REV7 homolog that interacts with the polymerase zeta
RT   catalytic subunit hREV3 and the spindle assembly checkpoint protein
RT   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
RP   ASP-2614 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
RT   translesion DNA synthesis and complements Pol eta in cisplatin
RT   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
RP   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
RT   and structural implication of the interaction between DNA polymerase
RT   zeta and 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
CC       (TLS). Lacks an intrinsic 3'-5' exonuclease activity and thus has
CC       no 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-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
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
CC         is 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
CC       polymerase catalytic activity, although its activity is very low
CC       in this context. Component of the tetrameric Pol-zeta complex
CC       (Pol-zeta4), which consists of REV3L, MAD2L2, POLD2 and POLD3;
CC       Pol-zeta4 is the fully active form of DNA polymerase zeta.
CC       {ECO:0000269|PubMed:10660610, ECO:0000269|PubMed:20164194,
CC       ECO:0000269|PubMed:24449906}.
CC   -!- INTERACTION:
CC       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
CC       during nucleotide polymerization, while its N-terminal part could
CC       provide sites for protein-protein interactions with other factors
CC       during translesion DNA synthesis.
CC   -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for
CC       the formation of polymerase complexes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/rev3l/";
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   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   SMR; O60673; -.
DR   BioGrid; 111912; 30.
DR   CORUM; O60673; -.
DR   IntAct; O60673; 12.
DR   MINT; O60673; -.
DR   STRING; 9606.ENSP00000351697; -.
DR   iPTMnet; O60673; -.
DR   PhosphoSitePlus; O60673; -.
DR   BioMuta; REV3L; -.
DR   jPOST; O60673; -.
DR   MaxQB; O60673; -.
DR   PaxDb; O60673; -.
DR   PeptideAtlas; O60673; -.
DR   PRIDE; O60673; -.
DR   ProteomicsDB; 49517; -.
DR   ProteomicsDB; 49518; -. [O60673-2]
DR   Ensembl; ENST00000358835; ENSP00000351697; ENSG00000009413. [O60673-1]
DR   Ensembl; ENST00000368802; ENSP00000357792; ENSG00000009413. [O60673-1]
DR   Ensembl; ENST00000368805; ENSP00000357795; ENSG00000009413. [O60673-1]
DR   Ensembl; ENST00000435970; ENSP00000402003; ENSG00000009413. [O60673-2]
DR   GeneID; 5980; -.
DR   KEGG; hsa:5980; -.
DR   UCSC; uc003puy.6; human. [O60673-1]
DR   CTD; 5980; -.
DR   DisGeNET; 5980; -.
DR   GeneCards; REV3L; -.
DR   H-InvDB; HIX0017582; -.
DR   HGNC; HGNC:9968; REV3L.
DR   HPA; HPA064853; -.
DR   HPA; HPA069382; -.
DR   MalaCards; REV3L; -.
DR   MIM; 602776; gene.
DR   neXtProt; NX_O60673; -.
DR   OpenTargets; ENSG00000009413; -.
DR   Orphanet; 570; Moebius syndrome.
DR   PharmGKB; PA34337; -.
DR   eggNOG; KOG0968; Eukaryota.
DR   eggNOG; COG0417; LUCA.
DR   GeneTree; ENSGT00940000156226; -.
DR   HOGENOM; HOG000112263; -.
DR   InParanoid; O60673; -.
DR   KO; K02350; -.
DR   OMA; CSKCRSQ; -.
DR   OrthoDB; 20210at2759; -.
DR   PhylomeDB; O60673; -.
DR   TreeFam; TF101072; -.
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   ChiTaRS; REV3L; human.
DR   EvolutionaryTrace; O60673; -.
DR   GeneWiki; REV3L; -.
DR   GenomeRNAi; 5980; -.
DR   PRO; PR:O60673; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000009413; Expressed in 227 organ(s), highest expression level in female reproductive system.
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: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; TAS:ProtInc.
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-dependent DNA replication; TAS:ProtInc.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 1.
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; IPR042087; DNA_pol_B_C.
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; 1.
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   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Alternative splicing; Complete proteome;
KW   DNA damage; DNA repair; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotidyltransferase; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   3130       DNA polymerase zeta catalytic subunit.
FT                                /FTId=PRO_0000046468.
FT   ZN_FING    3042   3057       CysA-type.
FT   REGION     1847   1898       Mediates interaction with MAD2L2.
FT                                {ECO:0000269|PubMed:10660610}.
FT   MOTIF      3086   3104       CysB motif.
FT   METAL      3042   3042       Zinc. {ECO:0000250}.
FT   METAL      3045   3045       Zinc. {ECO:0000250}.
FT   METAL      3054   3054       Zinc. {ECO:0000250}.
FT   METAL      3057   3057       Zinc. {ECO:0000250}.
FT   METAL      3086   3086       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL      3089   3089       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL      3099   3099       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL      3104   3104       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   MOD_RES    1030   1030       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES    1041   1041       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES    1724   1724       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1967   1967       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ       1     78       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:9925914}.
FT                                /FTId=VSP_024121.
FT   VARIANT     231    231       Q -> H (in dbSNP:rs1053911).
FT                                {ECO:0000269|PubMed:10660610,
FT                                ECO:0000269|PubMed:9925914}.
FT                                /FTId=VAR_008516.
FT   VARIANT     389    389       S -> T.
FT                                /FTId=VAR_008517.
FT   VARIANT     397    397       Q -> P (in dbSNP:rs3218579).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022226.
FT   VARIANT     633    633       S -> G (in dbSNP:rs3218598).
FT                                /FTId=VAR_048883.
FT   VARIANT     693    693       M -> T (in dbSNP:rs3218593).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022227.
FT   VARIANT     962    962       R -> Q (in dbSNP:rs17539588).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022228.
FT   VARIANT    1156   1156       Y -> C (in dbSNP:rs458017).
FT                                {ECO:0000269|PubMed:10660610,
FT                                ECO:0000269|PubMed:9925914,
FT                                ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022229.
FT   VARIANT    1220   1220       S -> L (in dbSNP:rs3218600).
FT                                /FTId=VAR_048884.
FT   VARIANT    1224   1224       T -> I (in dbSNP:rs462779).
FT                                {ECO:0000269|PubMed:10102035,
FT                                ECO:0000269|PubMed:10660610,
FT                                ECO:0000269|PubMed:9618506,
FT                                ECO:0000269|PubMed:9925914,
FT                                ECO:0000269|Ref.3, ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022230.
FT   VARIANT    1284   1284       T -> P (in dbSNP:rs3218578).
FT                                /FTId=VAR_048885.
FT   VARIANT    1302   1302       S -> T (in dbSNP:rs3218597).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022231.
FT   VARIANT    1309   1309       Q -> H (in dbSNP:rs3218595).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022232.
FT   VARIANT    1339   1339       P -> T (in dbSNP:rs17539616).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022233.
FT   VARIANT    1469   1469       Q -> P (in dbSNP:rs3218572).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022234.
FT   VARIANT    1540   1540       K -> E (in dbSNP:rs1053913).
FT                                {ECO:0000269|PubMed:10660610,
FT                                ECO:0000269|PubMed:9925914}.
FT                                /FTId=VAR_008518.
FT   VARIANT    1576   1576       S -> L (in dbSNP:rs3218582).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022235.
FT   VARIANT    1713   1713       D -> N (in dbSNP:rs3218585).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022236.
FT   VARIANT    1724   1724       S -> T (in dbSNP:rs17539644).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022237.
FT   VARIANT    1791   1791       P -> S (in dbSNP:rs17539651).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022238.
FT   VARIANT    1812   1812       D -> H (in dbSNP:rs3218599).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022239.
FT   VARIANT    1923   1923       G -> R (in dbSNP:rs3218604).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022240.
FT   VARIANT    1970   1970       R -> H (in dbSNP:rs3218606).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022241.
FT   VARIANT    2015   2015       E -> V (in dbSNP:rs17539692).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022242.
FT   VARIANT    2075   2075       I -> M (in dbSNP:rs17510963).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022243.
FT   VARIANT    2607   2607       S -> T.
FT                                /FTId=VAR_008519.
FT   VARIANT    2762   2762       R -> Q (in dbSNP:rs3218592).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_022244.
FT   VARIANT    3064   3064       V -> I (in dbSNP:rs3204953).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_016147.
FT   MUTAGEN    2614   2614       D->N: Loss of DNA polymerase catalytic
FT                                activity; when associated with N-2783.
FT                                {ECO:0000269|PubMed:24449906}.
FT   MUTAGEN    2783   2783       D->N: Loss of DNA polymerase catalytic
FT                                activity; when associated with N-2614.
FT                                {ECO:0000269|PubMed:24449906}.
FT   CONFLICT    237    237       E -> Q (in Ref. 4; AAC28460 and 7;
FT                                AAB88486). {ECO:0000305}.
FT   STRAND     1877   1882       {ECO:0000244|PDB:5O8K}.
FT   HELIX      1887   1894       {ECO:0000244|PDB:5O8K}.
FT   STRAND     1991   1998       {ECO:0000244|PDB:6BCD}.
FT   HELIX      2003   2012       {ECO:0000244|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
     PYLRQLLDQF
//
DBGET integrated database retrieval system