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Q07864

- DPOE1_HUMAN

UniProt

Q07864 - DPOE1_HUMAN

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Protein

DNA polymerase epsilon catalytic subunit A

Gene

POLE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Participates in DNA repair and in chromosomal DNA replication.

Catalytic activityi

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

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi2158 – 21581ZincBy similarity
Metal bindingi2161 – 21611ZincBy similarity
Metal bindingi2187 – 21871ZincBy similarity
Metal bindingi2190 – 21901ZincBy similarity
Metal bindingi2221 – 22211Iron-sulfur (4Fe-4S)By similarity
Metal bindingi2224 – 22241Iron-sulfur (4Fe-4S)By similarity
Metal bindingi2236 – 22361Iron-sulfur (4Fe-4S)By similarity
Metal bindingi2238 – 22381Iron-sulfur (4Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri2158 – 219033CysA-typeAdd
BLAST

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. chromatin binding Source: UniProtKB
  3. DNA binding Source: UniProtKB
  4. DNA-directed DNA polymerase activity Source: UniProtKB
  5. nucleotide binding Source: InterPro
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. base-excision repair, gap-filling Source: UniProtKB
  2. DNA repair Source: Reactome
  3. DNA replication Source: UniProtKB
  4. DNA replication initiation Source: Reactome
  5. DNA synthesis involved in DNA repair Source: UniProtKB
  6. G1/S transition of mitotic cell cycle Source: UniProtKB
  7. in utero embryonic development Source: Ensembl
  8. mitotic cell cycle Source: Reactome
  9. nucleotide-excision repair Source: Reactome
  10. nucleotide-excision repair, DNA gap filling Source: UniProtKB
  11. telomere maintenance Source: Reactome
  12. telomere maintenance via recombination Source: Reactome
  13. telomere maintenance via semi-conservative replication Source: Reactome
  14. transcription-coupled nucleotide-excision repair Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, DNA replication

Keywords - Ligandi

4Fe-4S, DNA-binding, Iron, Iron-sulfur, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_2244. DNA replication initiation.
REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_7993. Telomere C-strand synthesis initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase epsilon catalytic subunit A (EC:2.7.7.7)
Alternative name(s):
DNA polymerase II subunit A
Gene namesi
Name:POLE
Synonyms:POLE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9177. POLE.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. epsilon DNA polymerase complex Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti424 – 4241L → V in CRCS12; associated with disease susceptibility. 1 Publication
VAR_069344
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615083. phenotype.
615139. phenotype.
Orphaneti352712. Facial dysmorphism - immunodeficiency - livedo - short stature.
PharmGKBiPA277.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22862286DNA polymerase epsilon catalytic subunit APRO_0000046455Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1184 – 11841Phosphoserine1 Publication
Modified residuei1940 – 19401Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ07864.
PaxDbiQ07864.
PRIDEiQ07864.

PTM databases

PhosphoSiteiQ07864.

Expressioni

Gene expression databases

BgeeiQ07864.
CleanExiHS_POLE.
ExpressionAtlasiQ07864. baseline and differential.
GenevestigatoriQ07864.

Organism-specific databases

HPAiHPA058210.

Interactioni

Subunit structurei

Catalytic and central component of the epsilon DNA polymerase complex consisting of four subunits: POLE, POLE2, POLE3 and POLE4. Interacts with RAD17 and TOPBP1.3 Publications

Protein-protein interaction databases

BioGridi111422. 23 interactions.
DIPiDIP-24243N.
IntActiQ07864. 9 interactions.
MINTiMINT-145475.
STRINGi9606.ENSP00000322570.

Structurei

3D structure databases

ProteinModelPortaliQ07864.
SMRiQ07864. Positions 218-552, 776-1119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2221 – 223818CysB motifAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the DNA polymerase type-B family.Curated
Contains 1 CysA-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri2158 – 219033CysA-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0417.
GeneTreeiENSGT00390000010194.
HOVERGENiHBG051398.
InParanoidiQ07864.
KOiK02324.
OMAiYETHSDN.
PhylomeDBiQ07864.
TreeFamiTF105017.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR006172. 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.
IPR029703. POL2.
IPR012337. RNaseH-like_dom.
[Graphical view]
PANTHERiPTHR10670:SF0. PTHR10670:SF0. 1 hit.
PfamiPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF08490. DUF1744. 1 hit.
[Graphical view]
SMARTiSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 2 hits.

Sequencei

Sequence statusi: Complete.

Q07864-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLRSGGRRR ADPGADGEAS RDDGATSSVS ALKRLERSQW TDKMDLRFGF
60 70 80 90 100
ERLKEPGEKT GWLINMHPTE ILDEDKRLGS AVDYYFIQDD GSRFKVALPY
110 120 130 140 150
KPYFYIATRK GCEREVSSFL SKKFQGKIAK VETVPKEDLD LPNHLVGLKR
160 170 180 190 200
NYIRLSFHTV EDLVKVRKEI SPAVKKNREQ DHASDAYTAL LSSVLQRGGV
210 220 230 240 250
ITDEEETSKK IADQLDNIVD MREYDVPYHI RLSIDLKIHV AHWYNVRYRG
260 270 280 290 300
NAFPVEITRR DDLVERPDPV VLAFDIETTK LPLKFPDAET DQIMMISYMI
310 320 330 340 350
DGQGYLITNR EIVSEDIEDF EFTPKPEYEG PFCVFNEPDE AHLIQRWFEH
360 370 380 390 400
VQETKPTIMV TYNGDFFDWP FVEARAAVHG LSMQQEIGFQ KDSQGEYKAP
410 420 430 440 450
QCIHMDCLRW VKRDSYLPVG SHNLKAAAKA KLGYDPVELD PEDMCRMATE
460 470 480 490 500
QPQTLATYSV SDAVATYYLY MKYVHPFIFA LCTIIPMEPD EVLRKGSGTL
510 520 530 540 550
CEALLMVQAF HANIIFPNKQ EQEFNKLTDD GHVLDSETYV GGHVEALESG
560 570 580 590 600
VFRSDIPCRF RMNPAAFDFL LQRVEKTLRH ALEEEEKVPV EQVTNFEEVC
610 620 630 640 650
DEIKSKLASL KDVPSRIECP LIYHLDVGAM YPNIILTNRL QPSAMVDEAT
660 670 680 690 700
CAACDFNKPG ANCQRKMAWQ WRGEFMPASR SEYHRIQHQL ESEKFPPLFP
710 720 730 740 750
EGPARAFHEL SREEQAKYEK RRLADYCRKA YKKIHITKVE ERLTTICQRE
760 770 780 790 800
NSFYVDTVRA FRDRRYEFKG LHKVWKKKLS AAVEVGDAAE VKRCKNMEVL
810 820 830 840 850
YDSLQLAHKC ILNSFYGYVM RKGARWYSME MAGIVCFTGA NIITQARELI
860 870 880 890 900
EQIGRPLELD TDGIWCVLPN SFPENFVFKT TNVKKPKVTI SYPGAMLNIM
910 920 930 940 950
VKEGFTNDQY QELAEPSSLT YVTRSENSIF FEVDGPYLAM ILPASKEEGK
960 970 980 990 1000
KLKKRYAVFN EDGSLAELKG FEVKRRGELQ LIKIFQSSVF EAFLKGSTLE
1010 1020 1030 1040 1050
EVYGSVAKVA DYWLDVLYSK AANMPDSELF ELISENRSMS RKLEDYGEQK
1060 1070 1080 1090 1100
STSISTAKRL AEFLGDQMVK DAGLSCRYII SRKPEGSPVT ERAIPLAIFQ
1110 1120 1130 1140 1150
AEPTVRKHFL RKWLKSSSLQ DFDIRAILDW DYYIERLGSA IQKIITIPAA
1160 1170 1180 1190 1200
LQQVKNPVPR VKHPDWLHKK LLEKNDVYKQ KKISELFTLE GRRQVTMAEA
1210 1220 1230 1240 1250
SEDSPRPSAP DMEDFGLVKL PHPAAPVTVK RKRVLWESQE ESQDLTPTVP
1260 1270 1280 1290 1300
WQEILGQPPA LGTSQEEWLV WLRFHKKKWQ LQARQRLARR KRQRLESAEG
1310 1320 1330 1340 1350
VLRPGAIRDG PATGLGSFLR RTARSILDLP WQIVQISETS QAGLFRLWAL
1360 1370 1380 1390 1400
VGSDLHCIRL SIPRVFYVNQ RVAKAEEGAS YRKVNRVLPR SNMVYNLYEY
1410 1420 1430 1440 1450
SVPEDMYQEH INEINAELSA PDIEGVYETQ VPLLFRALVH LGCVCVVNKQ
1460 1470 1480 1490 1500
LVRHLSGWEA ETFALEHLEM RSLAQFSYLE PGSIRHIYLY HHAQAHKALF
1510 1520 1530 1540 1550
GIFIPSQRRA SVFVLDTVRS NQMPSLGALY SAEHGLLLEK VGPELLPPPK
1560 1570 1580 1590 1600
HTFEVRAETD LKTICRAIQR FLLAYKEERR GPTLIAVQSS WELKRLASEI
1610 1620 1630 1640 1650
PVLEEFPLVP ICVADKINYG VLDWQRHGAR RMIRHYLNLD TCLSQAFEMS
1660 1670 1680 1690 1700
RYFHIPIGNL PEDISTFGSD LFFARHLQRH NHLLWLSPTA RPDLGGKEAD
1710 1720 1730 1740 1750
DNCLVMEFDD QATVEINSSG CYSTVCVELD LQNLAVNTIL QSHHVNDMEG
1760 1770 1780 1790 1800
ADSMGISFDV IQQASLEDMI TGGQAASAPA SYDETALCSN TFRILKSMVV
1810 1820 1830 1840 1850
GWVKEITQYH NIYADNQVMH FYRWLRSPSS LLHDPALHRT LHNMMKKLFL
1860 1870 1880 1890 1900
QLIAEFKRLG SSVIYANFNR IILCTKKRRV EDAIAYVEYI TSSIHSKETF
1910 1920 1930 1940 1950
HSLTISFSRC WEFLLWMDPS NYGGIKGKVS SRIHCGLQDS QKAGGAEDEQ
1960 1970 1980 1990 2000
ENEDDEEERD GEEEEEAEES NVEDLLENNW NILQFLPQAA SCQNYFLMIV
2010 2020 2030 2040 2050
SAYIVAVYHC MKDGLRRSAP GSTPVRRRGA SQLSQEAEGA VGALPGMITF
2060 2070 2080 2090 2100
SQDYVANELT QSFFTITQKI QKKVTGSRNS TELSEMFPVL PGSHLLLNNP
2110 2120 2130 2140 2150
ALEFIKYVCK VLSLDTNITN QVNKLNRDLL RLVDVGEFSE EAQFRDPCRS
2160 2170 2180 2190 2200
YVLPEVICRS CNFCRDLDLC KDSSFSEDGA VLPQWLCSNC QAPYDSSAIE
2210 2220 2230 2240 2250
MTLVEVLQKK LMAFTLQDLV CLKCRGVKET SMPVYCSCAG DFALTIHTQV
2260 2270 2280
FMEQIGIFRN IAQHYGMSYL LETLEWLLQK NPQLGH
Length:2,286
Mass (Da):261,518
Last modified:October 17, 2006 - v5
Checksum:iA213AE1EA8437DEC
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2237 – 22371S → T in AAA15448. (PubMed:8486689)Curated
Sequence conflicti2237 – 22371S → T in AAC19148. (PubMed:8486689)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti31 – 311A → S.
Corresponds to variant rs34047482 [ dbSNP | Ensembl ].
VAR_061138
Natural varianti99 – 991P → L.
Corresponds to variant rs5744739 [ dbSNP | Ensembl ].
VAR_028429
Natural varianti189 – 1891A → T Found in a colorectal sample; somatic mutation. 1 Publication
VAR_069339
Natural varianti231 – 2311R → H Found in a colorectal sample; somatic mutation. 1 Publication
VAR_069340
Natural varianti252 – 2521A → V.
Corresponds to variant rs5744751 [ dbSNP | Ensembl ].
VAR_020276
Natural varianti260 – 2601R → Q.
Corresponds to variant rs5744752 [ dbSNP | Ensembl ].
VAR_028430
Natural varianti286 – 2861P → H Found in a colorectal sample; somatic mutation. 1 Publication
VAR_069341
Natural varianti336 – 3361N → S.
Corresponds to variant rs5744760 [ dbSNP | Ensembl ].
VAR_020277
Natural varianti367 – 3671F → S Found in a colorectal sample; somatic mutation. 1 Publication
VAR_069342
Natural varianti411 – 4111V → L Found in a colorectal sample; somatic mutation. 1 Publication
VAR_069343
Natural varianti424 – 4241L → V in CRCS12; associated with disease susceptibility. 1 Publication
VAR_069344
Natural varianti436 – 4361P → R Found in a colorectal sample; somatic mutation. 1 Publication
VAR_069345
Natural varianti459 – 4591S → F Found in a colorectal sample; somatic mutation. 1 Publication
VAR_069346
Natural varianti695 – 6951F → I.
Corresponds to variant rs5744799 [ dbSNP | Ensembl ].
VAR_020278
Natural varianti762 – 7621R → W Found in a colorectal sample; somatic mutation. 1 Publication
VAR_069347
Natural varianti777 – 7771K → N Found in a colorectal sample; somatic mutation. 1 Publication
VAR_069348
Natural varianti1008 – 10081K → N Found in a colorectal sample; somatic mutation. 1 Publication
VAR_069349
Natural varianti1255 – 12551L → V Found in a colorectal sample; somatic mutation. 1 Publication
VAR_069350
Natural varianti1368 – 13681V → M Found in a colorectal sample; somatic mutation. 1 Publication
VAR_069351
Natural varianti1382 – 13821R → C.
Corresponds to variant rs5744904 [ dbSNP | Ensembl ].
VAR_028431
Natural varianti1395 – 13951Y → C.
Corresponds to variant rs5744933 [ dbSNP | Ensembl ].
VAR_020279
Natural varianti1396 – 13961N → S.
Corresponds to variant rs5744934 [ dbSNP | Ensembl ].
VAR_020280
Natural varianti1399 – 13991E → Q.
Corresponds to variant rs5744935 [ dbSNP | Ensembl ].
VAR_020281
Natural varianti1421 – 14211P → S.1 Publication
VAR_069352
Natural varianti1577 – 15771E → A.
Corresponds to variant rs5744948 [ dbSNP | Ensembl ].
VAR_028432
Natural varianti1712 – 17121A → V.
Corresponds to variant rs5744950 [ dbSNP | Ensembl ].
VAR_028433
Natural varianti1752 – 17521D → N Found in a colorectal sample; somatic mutation. 1 Publication
VAR_069353
Natural varianti1857 – 18571K → R.
Corresponds to variant rs5744971 [ dbSNP | Ensembl ].
VAR_028434
Natural varianti1935 – 19351C → Y.
Corresponds to variant rs5744991 [ dbSNP | Ensembl ].
VAR_028435
Natural varianti2013 – 20131D → N.1 Publication
VAR_069354
Natural varianti2040 – 20401A → V.
Corresponds to variant rs5745021 [ dbSNP | Ensembl ].
VAR_020282
Natural varianti2056 – 20561A → T Found in a colorectal sample; somatic mutation. 1 Publication
VAR_069355
Natural varianti2140 – 21401E → K.
Corresponds to variant rs5745066 [ dbSNP | Ensembl ].
VAR_048881
Natural varianti2159 – 21591R → C.
Corresponds to variant rs5745067 [ dbSNP | Ensembl ].
VAR_048882
Natural varianti2165 – 21651R → H.
Corresponds to variant rs5745068 [ dbSNP | Ensembl ].
VAR_020283
Natural varianti2213 – 22131A → V Found in a colorectal sample; somatic mutation. 1 Publication
VAR_069356

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S60080 mRNA. Translation: AAA15448.1. Sequence problems.
L09561 mRNA. Translation: AAC19148.1.
U49356 mRNA. Translation: AAA90924.1.
AY273166 Genomic DNA. Translation: AAP12650.1.
CCDSiCCDS9278.1.
PIRiG02434.
RefSeqiNP_006222.2. NM_006231.3.
UniGeneiHs.524871.

Genome annotation databases

EnsembliENST00000320574; ENSP00000322570; ENSG00000177084.
GeneIDi5426.
KEGGihsa:5426.
UCSCiuc001uks.1. human.

Polymorphism databases

DMDMi116241339.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S60080 mRNA. Translation: AAA15448.1 . Sequence problems.
L09561 mRNA. Translation: AAC19148.1 .
U49356 mRNA. Translation: AAA90924.1 .
AY273166 Genomic DNA. Translation: AAP12650.1 .
CCDSi CCDS9278.1.
PIRi G02434.
RefSeqi NP_006222.2. NM_006231.3.
UniGenei Hs.524871.

3D structure databases

ProteinModelPortali Q07864.
SMRi Q07864. Positions 218-552, 776-1119.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111422. 23 interactions.
DIPi DIP-24243N.
IntActi Q07864. 9 interactions.
MINTi MINT-145475.
STRINGi 9606.ENSP00000322570.

Chemistry

ChEMBLi CHEMBL2363042.
DrugBanki DB00242. Cladribine.

PTM databases

PhosphoSitei Q07864.

Polymorphism databases

DMDMi 116241339.

Proteomic databases

MaxQBi Q07864.
PaxDbi Q07864.
PRIDEi Q07864.

Protocols and materials databases

DNASUi 5426.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000320574 ; ENSP00000322570 ; ENSG00000177084 .
GeneIDi 5426.
KEGGi hsa:5426.
UCSCi uc001uks.1. human.

Organism-specific databases

CTDi 5426.
GeneCardsi GC12M133200.
H-InvDB HIX0022184.
HGNCi HGNC:9177. POLE.
HPAi HPA058210.
MIMi 174762. gene.
615083. phenotype.
615139. phenotype.
neXtProti NX_Q07864.
Orphaneti 352712. Facial dysmorphism - immunodeficiency - livedo - short stature.
PharmGKBi PA277.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0417.
GeneTreei ENSGT00390000010194.
HOVERGENi HBG051398.
InParanoidi Q07864.
KOi K02324.
OMAi YETHSDN.
PhylomeDBi Q07864.
TreeFami TF105017.

Enzyme and pathway databases

Reactomei REACT_1095. Activation of the pre-replicative complex.
REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_2244. DNA replication initiation.
REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_7993. Telomere C-strand synthesis initiation.

Miscellaneous databases

ChiTaRSi POLE. human.
GeneWikii POLE_(enzyme).
GenomeRNAii 5426.
NextBioi 20993.
PROi Q07864.
SOURCEi Search...

Gene expression databases

Bgeei Q07864.
CleanExi HS_POLE.
ExpressionAtlasi Q07864. baseline and differential.
Genevestigatori Q07864.

Family and domain databases

Gene3Di 3.30.420.10. 1 hit.
InterProi IPR006172. 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.
IPR029703. POL2.
IPR012337. RNaseH-like_dom.
[Graphical view ]
PANTHERi PTHR10670:SF0. PTHR10670:SF0. 1 hit.
Pfami PF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF08490. DUF1744. 1 hit.
[Graphical view ]
SMARTi SM00486. POLBc. 1 hit.
[Graphical view ]
SUPFAMi SSF53098. SSF53098. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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.

Entry informationi

Entry nameiDPOE1_HUMAN
AccessioniPrimary (citable) accession number: Q07864
Secondary accession number(s): Q13533, Q86VH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 17, 2006
Last modified: November 26, 2014
This is version 149 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3