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Q9NR33 (DPOE4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:POLE4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length117 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

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. Ref.1

Subcellular location

Nucleus Potential.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ORFQ9Q2G42EBI-867034,EBI-6248094From a different organism.
POLE3Q9NRF93EBI-867034,EBI-744901

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 117116DNA polymerase epsilon subunit 4
PRO_0000191746

Amino acid modifications

Modified residue21N-acetylalanine Ref.5 Ref.6 Ref.8
Modified residue111Phosphothreonine Ref.6
Modified residue251Phosphoserine Ref.4

Natural variations

Natural variant171G → V. Ref.1 Ref.3 Ref.4
Corresponds to variant rs12366 [ dbSNP | Ensembl ].
VAR_028050

Sequences

Sequence LengthMass (Da)Tools
Q9NR33 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 1F7273FFEC9D318C

FASTA11712,209
        10         20         30         40         50         60 
MAAAAAAGSG TPREEEGPAG EAAASQPQAP TSVPGARLSR LPLARVKALV KADPDVTLAG 

        70         80         90        100        110 
QEAIFILARA AELFVETIAK DAYCCAQQGK RKTLQRRDLD NAIEAVDEFA FLEGTLD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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-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].
Tissue: Cervix carcinoma.
[7]"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].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF261688 Genomic DNA. Translation: AAF90132.1.
AC007400 Genomic DNA. Translation: AAY15030.1.
BC031331 mRNA. Translation: AAH31331.1.
CCDSCCDS1957.1.
RefSeqNP_063949.2. NM_019896.2.
UniGeneHs.469060.

3D structure databases

ProteinModelPortalQ9NR33.
SMRQ9NR33. Positions 41-112.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121168. 12 interactions.
IntActQ9NR33. 6 interactions.
MINTMINT-3072641.
STRING9606.ENSP00000420176.

PTM databases

PhosphoSiteQ9NR33.

Polymorphism databases

DMDM116241340.

Proteomic databases

MaxQBQ9NR33.
PaxDbQ9NR33.
PRIDEQ9NR33.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000483063; ENSP00000420176; ENSG00000115350.
GeneID56655.
KEGGhsa:56655.
UCSCuc002snf.3. human.

Organism-specific databases

CTD56655.
GeneCardsGC02P075185.
H-InvDBHIX0002198.
HGNCHGNC:18755. POLE4.
HPAHPA054979.
MIM607269. gene.
neXtProtNX_Q9NR33.
PharmGKBPA38677.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5208.
HOGENOMHOG000007271.
HOVERGENHBG051399.
KOK03506.
OMAPITRIKH.
OrthoDBEOG7BGHNS.
PhylomeDBQ9NR33.
TreeFamTF103009.

Gene expression databases

BgeeQ9NR33.
CleanExHS_POLE4.
GenevestigatorQ9NR33.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR003958. CBFA_NFYB_domain.
IPR009072. Histone-fold.
[Graphical view]
PfamPF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi56655.
NextBio62121.
PROQ9NR33.
SOURCESearch...

Entry information

Entry nameDPOE4_HUMAN
AccessionPrimary (citable) accession number: Q9NR33
Secondary accession number(s): Q53TR2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 110 of the entry and version 2 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

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 2

Human chromosome 2: entries, gene names and cross-references to MIM