Q9NR33 (DPOE4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

POLE4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	117 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	DNA-directed DNA polymerase Nucleotidyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H3 acetylation Inferred from direct assay PubMed 18838386. Source: BHF-UCL
Cellular_component	Ada2/Gcn5/Ada3 transcription activator complex Inferred from direct assay PubMed 18838386. Source: BHF-UCL epsilon DNA polymerase complex Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	DNA-directed DNA polymerase activity Traceable author statement Ref.1. Source: ProtInc sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ORF	Q9Q2G4	2	EBI-867034,EBI-6248094	From a different organism.
POLE3	Q9NRF9	3	EBI-867034,EBI-744901

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 117	116	DNA polymerase epsilon subunit 4		PRO_0000191746
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.5
	Modified residue	11	1	Phosphothreonine Ref.5
	Modified residue	25	1	Phosphoserine Ref.4
Natural variations
	Natural variant	17	1	G → V. Ref.1 Ref.3 Ref.4 Corresponds to variant rs12366 [ dbSNP | Ensembl ].		VAR_028050

Sequences

	Sequence		Length	Mass (Da)
	Q9NR33 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 1F7273FFEC9D318C	FASTA	117	12,209
	10 20 30 40 50 60 MAAAAAAGSG TPREEEGPAG EAAASQPQAP TSVPGARLSR LPLARVKALV KADPDVTLAG 70 80 90 100 110 QEAIFILARA AELFVETIAK DAYCCAQQGK RKTLQRRDLD NAIEAVDEFA FLEGTLD

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[5]	"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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[6]	"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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF261688 Genomic DNA. Translation: AAF90132.1. AC007400 Genomic DNA. Translation: AAY15030.1. BC031331 mRNA. Translation: AAH31331.1.
IPI	IPI00008436.
RefSeq	NP_063949.2. NM_019896.2.
UniGene	Hs.469060.
3D structure databases
ProteinModelPortal	Q9NR33.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NR33. 4 interactions.
STRING	9606.ENSP00000420176.
PTM databases
PhosphoSite	Q9NR33.
Polymorphism databases
DMDM	116241340.
Proteomic databases
PaxDb	Q9NR33.
PRIDE	Q9NR33.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000483063; ENSP00000420176; ENSG00000115350.
GeneID	56655.
KEGG	hsa:56655.
UCSC	uc002snf.3. human.
Organism-specific databases
CTD	56655.
GeneCards	GC02P075185.
H-InvDB	HIX0002198.
HGNC	HGNC:18755. POLE4.
MIM	607269. gene.
neXtProt	NX_Q9NR33.
PharmGKB	PA38677.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5208.
HOGENOM	HOG000007271.
HOVERGEN	HBG051399.
KO	K03506.
OMA	EKSERAT.
OrthoDB	EOG4X6C9X.
PhylomeDB	Q9NR33.
Gene expression databases
Bgee	Q9NR33.
CleanEx	HS_POLE4.
Genevestigator	Q9NR33.
GermOnline	ENSG00000115350. Homo sapiens.
Family and domain databases
Gene3D	1.10.20.10. 1 hit.
InterPro	IPR003958. CBFA_NFYB_domain. IPR009072. Histone-fold. [Graphical view]
Pfam	PF00808. CBFD_NFYB_HMF. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	56655.
NextBio	62121.
SOURCE	Search...

Entry information

Entry name

DPOE4_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.