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Q07864 (DPOE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA polymerase epsilon catalytic subunit A

EC=2.7.7.7
Alternative name(s):
DNA polymerase II subunit A
Gene names
Name:POLE
Synonyms:POLE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2286 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in DNA repair and in chromosomal DNA replication.

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactor

Binds 1 4Fe-4S cluster By similarity.

Subunit structure

Catalytic and central component of the epsilon DNA polymerase complex consisting of four subunits: POLE, POLE2, POLE3 and POLE4. Interacts with RAD17 and TOPBP1. Ref.5 Ref.6 Ref.7

Subcellular location

Nucleus.

Domain

The DNA polymerase activity domain resides in the N-terminal half of the protein, while the C-terminus is necessary for complexing subunits B and C. The C-terminus may also regulate the catalytic activities of the enzyme.

The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes By similarity.

Involvement in disease

Colorectal cancer 12 (CRCS12) [MIM:615083]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. CRCS12 is characterized by a high-penetrance predisposition to the development of colorectal adenomas and carcinomas, with a variable tendency to develop multiple and large tumors. Onset is usually before age 40 years. The histologic features of the tumors are unremarkable.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.12

Facial dysmorphism, immunodeficiency, livedo, and short stature (FILS) [MIM:615139]: A syndrome characterized by mild facial dysmorphism, mainly malar hypoplasia, livedo on the skin since birth, and immunodeficiency resulting in recurrent infections. Growth impairment is observed during early childhood and results in variable short stature in adulthood.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Sequence similarities

Belongs to the DNA polymerase type-B family.

Contains 1 CysA-type zinc finger.

Sequence caution

The sequence AAA15448.1 differs from that shown. Reason: Frameshift at positions 443 and 448.

The sequence AAA15448.1 differs from that shown. Reason:

Ontologies

Keywords
   Biological processDNA damage
DNA repair
DNA replication
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainZinc-finger
   Ligand4Fe-4S
DNA-binding
Iron
Iron-sulfur
Metal-binding
Zinc
   Molecular functionDNA-directed DNA polymerase
Nucleotidyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement. Source: Reactome

DNA replication

Inferred from mutant phenotype PubMed 16762037. Source: UniProtKB

DNA replication initiation

Traceable author statement. Source: Reactome

DNA synthesis involved in DNA repair

Inferred from mutant phenotype PubMed 1730053. Source: UniProtKB

G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 16762037. Source: UniProtKB

base-excision repair, gap-filling

Inferred from direct assay PubMed 10559260. Source: UniProtKB

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle

Traceable author statement. Source: Reactome

nucleotide-excision repair

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA gap filling

Inferred from mutant phenotype PubMed 20227374. Source: UniProtKB

telomere maintenance

Traceable author statement. Source: Reactome

telomere maintenance via recombination

Traceable author statement. Source: Reactome

telomere maintenance via semi-conservative replication

Traceable author statement. Source: Reactome

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

epsilon DNA polymerase complex

Inferred from direct assay Ref.5. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 16762037. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from direct assay PubMed 16762037. Source: UniProtKB

DNA-directed DNA polymerase activity

Inferred from mutant phenotype PubMed 16762037. Source: UniProtKB

chromatin binding

Inferred from direct assay PubMed 16762037. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22862286DNA polymerase epsilon catalytic subunit A
PRO_0000046455

Regions

Zinc finger2158 – 219033CysA-type
Motif2221 – 223818CysB motif

Sites

Metal binding21581Zinc By similarity
Metal binding21611Zinc By similarity
Metal binding21871Zinc By similarity
Metal binding21901Zinc By similarity
Metal binding22211Iron-sulfur (4Fe-4S) By similarity
Metal binding22241Iron-sulfur (4Fe-4S) By similarity
Metal binding22361Iron-sulfur (4Fe-4S) By similarity
Metal binding22381Iron-sulfur (4Fe-4S) By similarity

Amino acid modifications

Modified residue11841Phosphoserine Ref.9
Modified residue19401Phosphoserine Ref.8

Natural variations

Natural variant311A → S.
Corresponds to variant rs34047482 [ dbSNP | Ensembl ].
VAR_061138
Natural variant991P → L.
Corresponds to variant rs5744739 [ dbSNP | Ensembl ].
VAR_028429
Natural variant1891A → T Found in a colorectal sample; somatic mutation. Ref.12
VAR_069339
Natural variant2311R → H Found in a colorectal sample; somatic mutation. Ref.12
VAR_069340
Natural variant2521A → V.
Corresponds to variant rs5744751 [ dbSNP | Ensembl ].
VAR_020276
Natural variant2601R → Q.
Corresponds to variant rs5744752 [ dbSNP | Ensembl ].
VAR_028430
Natural variant2861P → H Found in a colorectal sample; somatic mutation. Ref.12
VAR_069341
Natural variant3361N → S.
Corresponds to variant rs5744760 [ dbSNP | Ensembl ].
VAR_020277
Natural variant3671F → S Found in a colorectal sample; somatic mutation. Ref.12
VAR_069342
Natural variant4111V → L Found in a colorectal sample; somatic mutation. Ref.12
VAR_069343
Natural variant4241L → V in CRCS12; associated with disease susceptibility. Ref.12
VAR_069344
Natural variant4361P → R Found in a colorectal sample; somatic mutation. Ref.12
VAR_069345
Natural variant4591S → F Found in a colorectal sample; somatic mutation. Ref.12
VAR_069346
Natural variant6951F → I.
Corresponds to variant rs5744799 [ dbSNP | Ensembl ].
VAR_020278
Natural variant7621R → W Found in a colorectal sample; somatic mutation. Ref.12
VAR_069347
Natural variant7771K → N Found in a colorectal sample; somatic mutation. Ref.12
VAR_069348
Natural variant10081K → N Found in a colorectal sample; somatic mutation. Ref.12
VAR_069349
Natural variant12551L → V Found in a colorectal sample; somatic mutation. Ref.12
VAR_069350
Natural variant13681V → M Found in a colorectal sample; somatic mutation. Ref.12
VAR_069351
Natural variant13821R → C.
Corresponds to variant rs5744904 [ dbSNP | Ensembl ].
VAR_028431
Natural variant13951Y → C.
Corresponds to variant rs5744933 [ dbSNP | Ensembl ].
VAR_020279
Natural variant13961N → S.
Corresponds to variant rs5744934 [ dbSNP | Ensembl ].
VAR_020280
Natural variant13991E → Q.
Corresponds to variant rs5744935 [ dbSNP | Ensembl ].
VAR_020281
Natural variant14211P → S. Ref.12
VAR_069352
Natural variant15771E → A.
Corresponds to variant rs5744948 [ dbSNP | Ensembl ].
VAR_028432
Natural variant17121A → V.
Corresponds to variant rs5744950 [ dbSNP | Ensembl ].
VAR_028433
Natural variant17521D → N Found in a colorectal sample; somatic mutation. Ref.12
VAR_069353
Natural variant18571K → R.
Corresponds to variant rs5744971 [ dbSNP | Ensembl ].
VAR_028434
Natural variant19351C → Y.
Corresponds to variant rs5744991 [ dbSNP | Ensembl ].
VAR_028435
Natural variant20131D → N. Ref.12
VAR_069354
Natural variant20401A → V.
Corresponds to variant rs5745021 [ dbSNP | Ensembl ].
VAR_020282
Natural variant20561A → T Found in a colorectal sample; somatic mutation. Ref.12
VAR_069355
Natural variant21401E → K.
Corresponds to variant rs5745066 [ dbSNP | Ensembl ].
VAR_048881
Natural variant21591R → C.
Corresponds to variant rs5745067 [ dbSNP | Ensembl ].
VAR_048882
Natural variant21651R → H.
Corresponds to variant rs5745068 [ dbSNP | Ensembl ].
VAR_020283
Natural variant22131A → V Found in a colorectal sample; somatic mutation. Ref.12
VAR_069356

Experimental info

Sequence conflict22371S → T in AAA15448. Ref.1
Sequence conflict22371S → T in AAC19148. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q07864 [UniParc].

Last modified October 17, 2006. Version 5.
Checksum: A213AE1EA8437DEC

FASTA2,286261,518
        10         20         30         40         50         60 
MSLRSGGRRR ADPGADGEAS RDDGATSSVS ALKRLERSQW TDKMDLRFGF ERLKEPGEKT 

        70         80         90        100        110        120 
GWLINMHPTE ILDEDKRLGS AVDYYFIQDD GSRFKVALPY KPYFYIATRK GCEREVSSFL 

       130        140        150        160        170        180 
SKKFQGKIAK VETVPKEDLD LPNHLVGLKR NYIRLSFHTV EDLVKVRKEI SPAVKKNREQ 

       190        200        210        220        230        240 
DHASDAYTAL LSSVLQRGGV ITDEEETSKK IADQLDNIVD MREYDVPYHI RLSIDLKIHV 

       250        260        270        280        290        300 
AHWYNVRYRG NAFPVEITRR DDLVERPDPV VLAFDIETTK LPLKFPDAET DQIMMISYMI 

       310        320        330        340        350        360 
DGQGYLITNR EIVSEDIEDF EFTPKPEYEG PFCVFNEPDE AHLIQRWFEH VQETKPTIMV 

       370        380        390        400        410        420 
TYNGDFFDWP FVEARAAVHG LSMQQEIGFQ KDSQGEYKAP QCIHMDCLRW VKRDSYLPVG 

       430        440        450        460        470        480 
SHNLKAAAKA KLGYDPVELD PEDMCRMATE QPQTLATYSV SDAVATYYLY MKYVHPFIFA 

       490        500        510        520        530        540 
LCTIIPMEPD EVLRKGSGTL CEALLMVQAF HANIIFPNKQ EQEFNKLTDD GHVLDSETYV 

       550        560        570        580        590        600 
GGHVEALESG VFRSDIPCRF RMNPAAFDFL LQRVEKTLRH ALEEEEKVPV EQVTNFEEVC 

       610        620        630        640        650        660 
DEIKSKLASL KDVPSRIECP LIYHLDVGAM YPNIILTNRL QPSAMVDEAT CAACDFNKPG 

       670        680        690        700        710        720 
ANCQRKMAWQ WRGEFMPASR SEYHRIQHQL ESEKFPPLFP EGPARAFHEL SREEQAKYEK 

       730        740        750        760        770        780 
RRLADYCRKA YKKIHITKVE ERLTTICQRE NSFYVDTVRA FRDRRYEFKG LHKVWKKKLS 

       790        800        810        820        830        840 
AAVEVGDAAE VKRCKNMEVL YDSLQLAHKC ILNSFYGYVM RKGARWYSME MAGIVCFTGA 

       850        860        870        880        890        900 
NIITQARELI EQIGRPLELD TDGIWCVLPN SFPENFVFKT TNVKKPKVTI SYPGAMLNIM 

       910        920        930        940        950        960 
VKEGFTNDQY QELAEPSSLT YVTRSENSIF FEVDGPYLAM ILPASKEEGK KLKKRYAVFN 

       970        980        990       1000       1010       1020 
EDGSLAELKG FEVKRRGELQ LIKIFQSSVF EAFLKGSTLE EVYGSVAKVA DYWLDVLYSK 

      1030       1040       1050       1060       1070       1080 
AANMPDSELF ELISENRSMS RKLEDYGEQK STSISTAKRL AEFLGDQMVK DAGLSCRYII 

      1090       1100       1110       1120       1130       1140 
SRKPEGSPVT ERAIPLAIFQ AEPTVRKHFL RKWLKSSSLQ DFDIRAILDW DYYIERLGSA 

      1150       1160       1170       1180       1190       1200 
IQKIITIPAA LQQVKNPVPR VKHPDWLHKK LLEKNDVYKQ KKISELFTLE GRRQVTMAEA 

      1210       1220       1230       1240       1250       1260 
SEDSPRPSAP DMEDFGLVKL PHPAAPVTVK RKRVLWESQE ESQDLTPTVP WQEILGQPPA 

      1270       1280       1290       1300       1310       1320 
LGTSQEEWLV WLRFHKKKWQ LQARQRLARR KRQRLESAEG VLRPGAIRDG PATGLGSFLR 

      1330       1340       1350       1360       1370       1380 
RTARSILDLP WQIVQISETS QAGLFRLWAL VGSDLHCIRL SIPRVFYVNQ RVAKAEEGAS 

      1390       1400       1410       1420       1430       1440 
YRKVNRVLPR SNMVYNLYEY SVPEDMYQEH INEINAELSA PDIEGVYETQ VPLLFRALVH 

      1450       1460       1470       1480       1490       1500 
LGCVCVVNKQ LVRHLSGWEA ETFALEHLEM RSLAQFSYLE PGSIRHIYLY HHAQAHKALF 

      1510       1520       1530       1540       1550       1560 
GIFIPSQRRA SVFVLDTVRS NQMPSLGALY SAEHGLLLEK VGPELLPPPK HTFEVRAETD 

      1570       1580       1590       1600       1610       1620 
LKTICRAIQR FLLAYKEERR GPTLIAVQSS WELKRLASEI PVLEEFPLVP ICVADKINYG 

      1630       1640       1650       1660       1670       1680 
VLDWQRHGAR RMIRHYLNLD TCLSQAFEMS RYFHIPIGNL PEDISTFGSD LFFARHLQRH 

      1690       1700       1710       1720       1730       1740 
NHLLWLSPTA RPDLGGKEAD DNCLVMEFDD QATVEINSSG CYSTVCVELD LQNLAVNTIL 

      1750       1760       1770       1780       1790       1800 
QSHHVNDMEG ADSMGISFDV IQQASLEDMI TGGQAASAPA SYDETALCSN TFRILKSMVV 

      1810       1820       1830       1840       1850       1860 
GWVKEITQYH NIYADNQVMH FYRWLRSPSS LLHDPALHRT LHNMMKKLFL QLIAEFKRLG 

      1870       1880       1890       1900       1910       1920 
SSVIYANFNR IILCTKKRRV EDAIAYVEYI TSSIHSKETF HSLTISFSRC WEFLLWMDPS 

      1930       1940       1950       1960       1970       1980 
NYGGIKGKVS SRIHCGLQDS QKAGGAEDEQ ENEDDEEERD GEEEEEAEES NVEDLLENNW 

      1990       2000       2010       2020       2030       2040 
NILQFLPQAA SCQNYFLMIV SAYIVAVYHC MKDGLRRSAP GSTPVRRRGA SQLSQEAEGA 

      2050       2060       2070       2080       2090       2100 
VGALPGMITF SQDYVANELT QSFFTITQKI QKKVTGSRNS TELSEMFPVL PGSHLLLNNP 

      2110       2120       2130       2140       2150       2160 
ALEFIKYVCK VLSLDTNITN QVNKLNRDLL RLVDVGEFSE EAQFRDPCRS YVLPEVICRS 

      2170       2180       2190       2200       2210       2220 
CNFCRDLDLC KDSSFSEDGA VLPQWLCSNC QAPYDSSAIE MTLVEVLQKK LMAFTLQDLV 

      2230       2240       2250       2260       2270       2280 
CLKCRGVKET SMPVYCSCAG DFALTIHTQV FMEQIGIFRN IAQHYGMSYL LETLEWLLQK 


NPQLGH 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the cDNA for the catalytic subunit of human DNA polymerase epsilon."
Kesti T., Frantti H., Syvaeoja J.E.
J. Biol. Chem. 268:10238-10245(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 48-51; 876-886 AND 1338-1344.
Tissue: T-cell.
[2]Syvaeoja J.E.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]Asahara H., Goldsmith J.S., Lee E., Linn S.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]NIEHS SNPs program
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-2286.
[5]"Identification and cloning of two histone fold motif-containing subunits of HeLa DNA polymerase epsilon."
Li Y., Pursell Z.F., Linn S.
J. Biol. Chem. 275:23247-23252(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN EPSILON DNA POLYMERASE COMPLEX.
Tissue: Cervix carcinoma.
[6]"BRCT domain-containing protein TopBP1 functions in DNA replication and damage response."
Maekiniemi M., Hillukkala T., Tuusa J., Reini K., Vaara M., Huang D., Pospiech H., Majuri I., Westerling T., Maekelae T.P., Syvaeoja J.E.
J. Biol. Chem. 276:30399-30406(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOPBP1.
[7]"The human checkpoint Rad protein Rad17 is chromatin-associated throughout the cell cycle, localizes to DNA replication sites, and interacts with DNA polymerase epsilon."
Post S.M., Tomkinson A.E., Lee E.Y.-H.P.
Nucleic Acids Res. 31:5568-5575(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAD17.
[8]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1940, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Polymerase epsilon1 mutation in a human syndrome with facial dysmorphism, immunodeficiency, livedo, and short stature (FILS syndrome)."
Pachlopnik Schmid J., Lemoine R., Nehme N., Cormier-Daire V., Revy P., Debeurme F., Debre M., Nitschke P., Bole-Feysot C., Legeai-Mallet L., Lim A., de Villartay J.P., Picard C., Durandy A., Fischer A., de Saint Basile G.
J. Exp. Med. 209:2323-2330(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN FILS.
[12]"Germline mutations affecting the proofreading domains of POLE and POLD1 predispose to colorectal adenomas and carcinomas."
CORGI Consortium, WGS500 Consortium
Palles C., Cazier J.B., Howarth K.M., Domingo E., Jones A.M., Broderick P., Kemp Z., Spain S.L., Guarino Almeida E., Salguero I., Sherborne A., Chubb D., Carvajal-Carmona L.G., Ma Y., Kaur K., Dobbins S., Barclay E., Gorman M. expand/collapse author list , Martin L., Kovac M.B., Humphray S., Lucassen A., Holmes C.C., Bentley D., Donnelly P., Taylor J., Petridis C., Roylance R., Sawyer E.J., Kerr D.J., Clark S., Grimes J., Kearsey S.E., Thomas H.J., McVean G., Houlston R.S., Tomlinson I.
Nat. Genet. 45:136-144(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CRCS12 VAL-424, VARIANTS THR-189; HIS-231; HIS-286; SER-367; LEU-411; ARG-436; PHE-459; TRP-762; ASN-777; ASN-1008; VAL-1255; MET-1368; SER-1421; ASN-1752; ASN-2013; THR-2056 AND VAL-2213.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S60080 mRNA. Translation: AAA15448.1. Sequence problems.
L09561 mRNA. Translation: AAC19148.1.
U49356 mRNA. Translation: AAA90924.1.
AY273166 Genomic DNA. Translation: AAP12650.1.
PIRG02434.
RefSeqNP_006222.2. NM_006231.3.
UniGeneHs.524871.

3D structure databases

ProteinModelPortalQ07864.
SMRQ07864. Positions 218-552, 776-1119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111422. 17 interactions.
DIPDIP-24243N.
IntActQ07864. 8 interactions.
MINTMINT-145475.
STRING9606.ENSP00000322570.

Chemistry

ChEMBLCHEMBL2363042.

PTM databases

PhosphoSiteQ07864.

Polymorphism databases

DMDM116241339.

Proteomic databases

PaxDbQ07864.
PRIDEQ07864.

Protocols and materials databases

DNASU5426.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320574; ENSP00000322570; ENSG00000177084.
GeneID5426.
KEGGhsa:5426.
UCSCuc001uks.1. human.

Organism-specific databases

CTD5426.
GeneCardsGC12M133200.
H-InvDBHIX0022184.
HGNCHGNC:9177. POLE.
HPAHPA058210.
MIM174762. gene.
615083. phenotype.
615139. phenotype.
neXtProtNX_Q07864.
Orphanet352712. Facial dysmorphism - immunodeficiency - livedo - short stature.
PharmGKBPA277.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0417.
HOVERGENHBG051398.
InParanoidQ07864.
KOK02324.
PhylomeDBQ07864.
TreeFamTF105017.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_216. DNA Repair.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressQ07864.
BgeeQ07864.
CleanExHS_POLE.
GenevestigatorQ07864.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
InterProIPR006172. DNA-dir_DNA_pol_B.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR013697. DNA_pol_e_suA_C.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF08490. DUF1744. 1 hit.
[Graphical view]
SMARTSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMSSF53098. SSF53098. 2 hits.
ProtoNetSearch...

Other

ChiTaRSPOLE. human.
GeneWikiPOLE_(enzyme).
GenomeRNAi5426.
NextBio20993.
PROQ07864.
SOURCESearch...

Entry information

Entry nameDPOE1_HUMAN
AccessionPrimary (citable) accession number: Q07864
Secondary accession number(s): Q13533, Q86VH9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 142 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM