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Protein

DNA polymerase epsilon subunit 4

Gene

POLE4

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

Functioni

May play a role in allowing polymerase epsilon to carry out its replication and/or repair function.

Catalytic activityi

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

GO - Molecular functioni

  1. DNA-directed DNA polymerase activity Source: ProtInc
  2. sequence-specific DNA binding Source: InterPro

GO - Biological processi

  1. DNA biosynthetic process Source: GOC
  2. histone H3 acetylation Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase epsilon subunit 4 (EC:2.7.7.7)
Alternative name(s):
DNA polymerase II subunit 4
DNA polymerase epsilon subunit p12
Gene namesi
Name:POLE4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:18755. POLE4.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. Ada2/Gcn5/Ada3 transcription activator complex Source: BHF-UCL
  2. epsilon DNA polymerase complex Source: UniProtKB
  3. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38677.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 117116DNA polymerase epsilon subunit 4PRO_0000191746Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei11 – 111Phosphothreonine1 Publication
Modified residuei25 – 251Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NR33.
PaxDbiQ9NR33.
PRIDEiQ9NR33.

PTM databases

PhosphoSiteiQ9NR33.

Expressioni

Gene expression databases

BgeeiQ9NR33.
CleanExiHS_POLE4.
GenevestigatoriQ9NR33.

Interactioni

Subunit structurei

Component of the epsilon DNA polymerase complex consisting of four subunits: POLE, POLE2, POLE3 and POLE4. Interaction with POLE3 is a prerequisite for further binding with POLE and POLE2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ORFQ9Q2G42EBI-867034,EBI-6248094From a different organism.
POLE3Q9NRF93EBI-867034,EBI-744901

Protein-protein interaction databases

BioGridi121168. 13 interactions.
IntActiQ9NR33. 6 interactions.
MINTiMINT-3072641.
STRINGi9606.ENSP00000420176.

Structurei

3D structure databases

ProteinModelPortaliQ9NR33.
SMRiQ9NR33. Positions 41-112.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG5208.
GeneTreeiENSGT00530000063560.
HOGENOMiHOG000007271.
HOVERGENiHBG051399.
InParanoidiQ9NR33.
KOiK03506.
OMAiPITRIKH.
OrthoDBiEOG7BGHNS.
PhylomeDBiQ9NR33.
TreeFamiTF103009.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR003958. CBFA_NFYB_domain.
IPR009072. Histone-fold.
[Graphical view]
PfamiPF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NR33-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAAAGSG TPREEEGPAG EAAASQPQAP TSVPGARLSR LPLARVKALV
60 70 80 90 100
KADPDVTLAG QEAIFILARA AELFVETIAK DAYCCAQQGK RKTLQRRDLD
110
NAIEAVDEFA FLEGTLD
Length:117
Mass (Da):12,209
Last modified:October 17, 2006 - v2
Checksum:i1F7273FFEC9D318C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171G → V.3 Publications
Corresponds to variant rs12366 [ dbSNP | Ensembl ].
VAR_028050

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF261688 Genomic DNA. Translation: AAF90132.1.
AC007400 Genomic DNA. Translation: AAY15030.1.
BC031331 mRNA. Translation: AAH31331.1.
CCDSiCCDS1957.1.
RefSeqiNP_063949.2. NM_019896.2.
UniGeneiHs.469060.

Genome annotation databases

EnsembliENST00000483063; ENSP00000420176; ENSG00000115350.
GeneIDi56655.
KEGGihsa:56655.
UCSCiuc002snf.3. human.

Polymorphism databases

DMDMi116241340.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF261688 Genomic DNA. Translation: AAF90132.1.
AC007400 Genomic DNA. Translation: AAY15030.1.
BC031331 mRNA. Translation: AAH31331.1.
CCDSiCCDS1957.1.
RefSeqiNP_063949.2. NM_019896.2.
UniGeneiHs.469060.

3D structure databases

ProteinModelPortaliQ9NR33.
SMRiQ9NR33. Positions 41-112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121168. 13 interactions.
IntActiQ9NR33. 6 interactions.
MINTiMINT-3072641.
STRINGi9606.ENSP00000420176.

Chemistry

DrugBankiDB00242. Cladribine.

PTM databases

PhosphoSiteiQ9NR33.

Polymorphism databases

DMDMi116241340.

Proteomic databases

MaxQBiQ9NR33.
PaxDbiQ9NR33.
PRIDEiQ9NR33.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000483063; ENSP00000420176; ENSG00000115350.
GeneIDi56655.
KEGGihsa:56655.
UCSCiuc002snf.3. human.

Organism-specific databases

CTDi56655.
GeneCardsiGC02P075185.
H-InvDBHIX0002198.
HGNCiHGNC:18755. POLE4.
MIMi607269. gene.
neXtProtiNX_Q9NR33.
PharmGKBiPA38677.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5208.
GeneTreeiENSGT00530000063560.
HOGENOMiHOG000007271.
HOVERGENiHBG051399.
InParanoidiQ9NR33.
KOiK03506.
OMAiPITRIKH.
OrthoDBiEOG7BGHNS.
PhylomeDBiQ9NR33.
TreeFamiTF103009.

Miscellaneous databases

GenomeRNAii56655.
NextBioi62121.
PROiQ9NR33.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NR33.
CleanExiHS_POLE4.
GenevestigatoriQ9NR33.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR003958. CBFA_NFYB_domain.
IPR009072. Histone-fold.
[Graphical view]
PfamiPF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION IN EPSILON DNA POLYMERASE COMPLEX, VARIANT VAL-17.
    Tissue: Cervix carcinoma.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-17.
    Tissue: Skin.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, VARIANT [LARGE SCALE ANALYSIS] VAL-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  6. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDPOE4_HUMAN
AccessioniPrimary (citable) accession number: Q9NR33
Secondary accession number(s): Q53TR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: October 17, 2006
Last modified: March 4, 2015
This is version 115 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.