ID H0YBX1_HUMAN Unreviewed; 239 AA.
AC H0YBX1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU366014};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU366014};
DE Flags: Fragment;
GN Name=POLB {ECO:0000313|Ensembl:ENSP00000430478.1};
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 {ECO:0000313|Ensembl:ENSP00000430478.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000430478.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Glockner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [2] {ECO:0000313|Ensembl:ENSP00000430478.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: DNA polymerase that functions in several pathways of DNA
CC repair. Involved in base excision repair (BER) responsible for repair
CC of lesions that give rise to abasic (AP) sites in DNA. Also contributes
CC to DNA double-strand break repair by non-homologous end joining and
CC homologous recombination. Has both template-dependent and template-
CC independent (terminal transferase) DNA polymerase activities. Has also
CC a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
CC {ECO:0000256|RuleBase:RU366014}.
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 Evidence={ECO:0000256|ARBA:ARBA00024632,
CC ECO:0000256|RuleBase:RU366014};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU366014}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family.
CC {ECO:0000256|ARBA:ARBA00008323, ECO:0000256|RuleBase:RU366014}.
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DR EMBL; AC083973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR MassIVE; H0YBX1; -.
DR MaxQB; H0YBX1; -.
DR PeptideAtlas; H0YBX1; -.
DR ProteomicsDB; 36867; -.
DR Antibodypedia; 3175; 442 antibodies from 35 providers.
DR Ensembl; ENST00000518579.5; ENSP00000430478.1; ENSG00000070501.12.
DR UCSC; uc064mlp.1; human.
DR HGNC; HGNC:9174; POLB.
DR VEuPathDB; HostDB:ENSG00000070501; -.
DR GeneTree; ENSGT00940000156918; -.
DR HOGENOM; CLU_1168201_0_0_1; -.
DR ChiTaRS; POLB; human.
DR Proteomes; UP000005640; Chromosome 8.
DR Bgee; ENSG00000070501; Expressed in oocyte and 197 other cell types or tissues.
DR ExpressionAtlas; H0YBX1; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00141; NT_POLXc; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 1.
DR InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR InterPro; IPR019843; DNA_pol-X_BS.
DR InterPro; IPR028207; DNA_pol_B_palm_palm.
DR InterPro; IPR037160; DNA_Pol_thumb_sf.
DR InterPro; IPR022312; DNA_pol_X.
DR InterPro; IPR002008; DNA_pol_X_beta-like.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR029398; PolB_thumb.
DR PANTHER; PTHR11276:SF42; DNA POLYMERASE BETA; 1.
DR PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1.
DR Pfam; PF14792; DNA_pol_B_palm; 1.
DR Pfam; PF14791; DNA_pol_B_thumb; 1.
DR PRINTS; PR00869; DNAPOLX.
DR PRINTS; PR00870; DNAPOLXBETA.
DR SMART; SM00483; POLXc; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 1: Evidence at protein level;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU366014};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU366014};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU366014};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU366014}; Nucleus {ECO:0000256|RuleBase:RU366014};
KW Proteomics identification {ECO:0007829|EPD:H0YBX1,
KW ECO:0007829|MaxQB:H0YBX1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366014}.
FT DOMAIN 1..190
FT /note="DNA-directed DNA polymerase X"
FT /evidence="ECO:0000259|SMART:SM00483"
FT NON_TER 1
FT /evidence="ECO:0000313|Ensembl:ENSP00000430478.1"
SQ SEQUENCE 239 AA; 27131 MW; ACA92ECC209C868A CRC64;
XGDFEKRIPR EEMLQMQDIV LNEVKKVDSE YIATVCGSFR RGAESSGDMD VLLTHPSFTS
ESTKQPKLLH QVVEQLQKVH FITDTLSKGE TKFMGVCQLP SKNDEKEYPH RRIDIRLIPK
DQYYCGVLYF TGSDIFNKNM RAHALEKGFT INEYTIRPLG VTVLQATRED LMHNMLLGPQ
LKAIKELQEN PCQWIVKKTS LITSSGNTGN PRTGANEACI LPGRHNPIGV LIYFLTFAM
//
