Q9NRF9 (DPOE3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA polymerase epsilon subunit 3
EC=2.7.7.7

Alternative name(s):
Arsenic-transactivated protein
Short name=AsTP
Chromatin accessibility complex 17 kDa protein
Short name=CHRAC-17
Short name=HuCHRAC17
DNA polymerase II subunit 3
DNA polymerase epsilon subunit p17

Gene names

Name:	POLE3
Synonyms:	CHRAC17

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	147 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	Forms a complex with DNA polymerase epsilon subunit CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1.
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Subunit structure	Consists of four subunits: POLE, POLE2, POLE3 and POLE4. Interacts with CHRAC1. Together with CHRAC1, ACF1 and ISWI/SNF2H proteins, it forms the ISWI chromatin-remodeling complex, CHRAC.
Subcellular location	Nucleus Potential.
Tissue specificity	Expressed in all tissues tested, including, heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Ligand	DNA-binding
Molecular function	DNA-directed DNA polymerase Nucleotidyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA replication Traceable author statement. Source: ProtInc histone H3 acetylation Inferred from direct assay. Source: BHF-UCL
Cellular component	Ada2/Gcn5/Ada3 transcription activator complex Inferred from direct assay. Source: BHF-UCL
Molecular function	DNA-directed DNA polymerase activity Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction Ref.2. Source: IntAct sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
POLE4	Q9NR33	3	EBI-744901,EBI-867034

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.8
	Chain	2 – 147	146	DNA polymerase epsilon subunit 3		PRO_0000208341
Regions
	Coiled coil	85 – 146	62	Potential
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.8 Ref.12
	Modified residue	83	1	Phosphothreonine Ref.11
	Modified residue	122	1	Phosphoserine Ref.9 Ref.10 Ref.11
Natural variations
	Natural variant	83	1	T → A. Ref.5		VAR_023464
	Natural variant	126	1	D → A. Corresponds to variant rs34852828 [ dbSNP | Ensembl ].		VAR_057527
	Natural variant	135	1	E → D. Ref.5 Corresponds to variant rs35933626 [ dbSNP | Ensembl ].		VAR_023465
Experimental info
	Sequence conflict	58	1	K → N in AAU15052. Ref.3
	Sequence conflict	58	1	K → N in BAC11206. Ref.4
	Sequence conflict	83	1	T → I in BAC11190. Ref.4
	Sequence conflict	146	1	D → Y in AAF90133. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9NRF9 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: DC0A4D2097046569	FASTA	147	16,860
	10 20 30 40 50 60 MAERPEDLNL PNAVITRIIK EALPDGVNIS KEARSAISRA ASVFVLYATS CANNFAMKGK 70 80 90 100 110 120 RKTLNASDVL SAMEEMEFQR FVTPLKEALE AYRREQKGKK EASEQKKKDK DKKTDSEEQD 130 140 KSRDEDNDED EERLEEEEQN EEEEVDN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1 and two novel histone-fold proteins." Poot R.A., Dellaire G., Huelsmann B.B., Grimaldi M.A., Corona D.F.V., Becker P.B., Bickmore W.A., Varga-Weisz P.D. EMBO J. 19:3377-3387(2000) [PubMed: 10880450] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 10801849] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 63-77 AND 81-86. Tissue: Cervix carcinoma.
[3]	"Screening and cloning of target genes differential expressed in HepG2 cells treated with arsenic trioxide by suppression subtractive hybridization technique." Wu S.-H., Cheng J., Liu Y., Zheng Y.-J., Zhang Y.-X., Xie Q., Guo J. Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	NIEHS SNPs program Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-83 AND ASP-135.
[6]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[8]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-17 AND 40-58, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83 AND SER-122, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF226077 mRNA. Translation: AAF72417.1. AF261689 Genomic DNA. Translation: AAF90133.1. AY720898 mRNA. Translation: AAU15052.1. AK074629 mRNA. Translation: BAC11099.1. AK074762 mRNA. Translation: BAC11190.1. AK074782 mRNA. Translation: BAC11206.1. DQ072116 Genomic DNA. Translation: AAY57326.1. AL137066 Genomic DNA. Translation: CAH70100.1. BC003166 mRNA. Translation: AAH03166.1. BC004170 mRNA. Translation: AAH04170.1.
IPI	IPI00010141.
RefSeq	NP_059139.3. NM_017443.4.
UniGene	Hs.108112.
3D structure databases
ProteinModelPortal	Q9NRF9.
SMR	Q9NRF9. Positions 6-140.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NRF9. 5 interactions.
MINT	MINT-1439872.
STRING	Q9NRF9.
PTM databases
PhosphoSite	Q9NRF9.
Polymorphism databases
DMDM	22653710.
Proteomic databases
PeptideAtlas	Q9NRF9.
PRIDE	Q9NRF9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374169; ENSP00000363284; ENSG00000148229. ENST00000374171; ENSP00000363286; ENSG00000148229.
GeneID	54107.
KEGG	hsa:54107.
UCSC	uc004bhn.1. human.
Organism-specific databases
CTD	54107.
GeneCards	GC09M116169.
H-InvDB	HIX0201370.
HGNC	HGNC:13546. POLE3.
MIM	607267. gene.
neXtProt	NX_Q9NRF9.
PharmGKB	PA33499.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG20899.
GeneTree	ENSGT00550000074689.
HOGENOM	HBG748799.
HOVERGEN	HBG060262.
InParanoid	Q9NRF9.
OMA	REDDNDE.
OrthoDB	EOG4TB4CS.
PhylomeDB	Q9NRF9.
Gene expression databases
ArrayExpress	Q9NRF9.
Bgee	Q9NRF9.
CleanEx	HS_POLE3.
Genevestigator	Q9NRF9.
GermOnline	ENSG00000148229. Homo sapiens.
Family and domain databases
InterPro	IPR003958. CBFA_NFYB_domain. IPR009072. Histone-fold. [Graphical view]
Gene3D	G3DSA:1.10.20.10. Histone-fold. 1 hit.
KO	K02326.
Pfam	PF00808. CBFD_NFYB_HMF. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
ProtoNet	Search...
Other
NextBio	56470.
SOURCE	Search...

Entry information

Entry name

DPOE3_HUMAN

Accession

Primary (citable) accession number: Q9NRF9
Secondary accession number(s): Q5W0U1 , Q8N758, Q8NCE5, Q9NR32

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 99 of the entry and version 1 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.