Reviewed, UniProtKB/Swiss-Prot Q15054 (DPOD3_HUMAN)

Names and origin

Protein names

Recommended name:
    DNA polymerase delta subunit 3
Alternative name(s):
    DNA polymerase delta subunit p66

Gene names

Name:	POLD3
Synonyms:	KIAA0039

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	466 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	Required for optimal DNA polymerase delta activity. Ref.5 Ref.6 Ref.8
Subunit structure	Heterotetramer composed of subunits of 125 kDa, 50 kDa, 66 kDa and 12 kDa. Interacts with POLD2. Interacts with PCNA. Ref.8
Subcellular location	Nucleus.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Molecular function	DNA-directed DNA polymerase Nucleotidyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA synthesis during DNA repair Non-traceable author statement. Source: UniProtKB mismatch repair Non-traceable author statement. Source: UniProtKB nucleotide-excision repair, DNA gap filling Inferred from Experiment. Source: Reactome
Cellular component	delta DNA polymerase complex Ref.5 Non-traceable author statement. Source: UniProtKB nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	DNA-directed DNA polymerase activity Ref.5 Non-traceable author statement. Source: UniProtKB protein binding Ref.8 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PCNA	P12004	3	EBI-864956,EBI-358311
POLD2	P49005	4	EBI-864956,EBI-372354

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 466

465

DNA polymerase delta subunit 3

PRO_0000186047

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.4

Modified residue

277

1

Phosphothreonine Ref.13

Modified residue

307

1

Phosphoserine Ref.13 Ref.7 Ref.9 Ref.10 Ref.11 Ref.15

Modified residue

407

1

Phosphoserine Ref.7 Ref.11

Modified residue

409

1

Phosphoserine Ref.7 Ref.11

Modified residue

411

1

Phosphothreonine Ref.7 Ref.11

Modified residue

413

1

Phosphoserine Ref.7 Ref.11

Modified residue

458

1

Phosphoserine Ref.11

Secondary structure

1

.

.

.

466

Helix Strand Turn

Details...

Helix

459 – 461

3

Sequences

	Sequence		Length	Mass (Da)
	Q15054-1 [UniParc]. Last modified September 26, 2001. Version 2. Checksum: E9625E0188725F45	FASTA	466	51,400
	10 20 30 40 50 60 MADQLYLENI DEFVTDQNKI VTYKWLSYTL GVHVNQAKQM LYDYVERKRK ENSGAQLHVT 70 80 90 100 110 120 YLVSGSLIQN GHSCHKVAVV REDKLEAVKS KLAVTASIHV YSIQKAMLKD SGPLFNTDYD 130 140 150 160 170 180 ILKSNLQNCS KFSAIQCAAA VPRAPAESSS SSKKFEQSHL HMSSETQANN ELTTNGHGPP 190 200 210 220 230 240 ASKQVSQQPK GIMGMFASKA AAKTQETNKE TKTEAKEVTN ASAAGNKAPG KGNMMSNFFG 250 260 270 280 290 300 KAAMNKFKVN LDSEQAVKEE KIVEQPTVSV TEPKLATPAG LKKSSKKAEP VKVLQKEKKR 310 320 330 340 350 360 GKRVALSDDE TKETENMRKK RRRIKLPESD SSEDEVFPDS PGAYEAESPS PPPPPSPPLE 370 380 390 400 410 420 PVPKTEPEPP SVKSSSGENK RKRKRVLKSK TYLDGEGCIV TEKVYESESC TDSEEELNMK 430 440 450 460 TSSVHRPPAM TVKKEPREER KGPKKGTAAL GKANRQVSIT GFFQRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1." Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S. DNA Res. 1:27-35(1994) [PubMed: 7584026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[2]	"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]. Tissue: Placenta.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-19 AND 110-123, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[5]	"Isolation and identification of the third subunit of mammalian DNA polymerase delta by PCNA-affinity chromatography of mouse FM3A cell extracts." Hughes P., Tratner I., Ducoux M., Piard K., Baldacci G. Nucleic Acids Res. 27:2108-2114(1999) [PubMed: 10219083] [Abstract] Cited for: FUNCTION.
[6]	"Evidence that DNA polymerase delta isolated by immunoaffinity chromatography exhibits high-molecular weight characteristics and is associated with the KIAA0039 protein and RPA." Mo J.-Y., Liu L., Leon A., Mazloum N., Lee M.Y.W.T. Biochemistry 39:7245-7254(2000) [PubMed: 10852724] [Abstract] Cited for: FUNCTION.
[7]	"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-307; SER-407; SER-409; THR-411 AND SER-413, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"Functional roles of p12, the fourth subunit of human DNA polymerase delta." Li H., Xie B., Zhou Y., Rahmeh A., Trusa S., Zhang S., Gao Y., Lee E.Y., Lee M.Y. J. Biol. Chem. 281:14748-14755(2006) [PubMed: 16510448] [Abstract] Cited for: FUNCTION, INTERACTION WITH PCNA.
[9]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, MASS SPECTROMETRY.
[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-307, MASS SPECTROMETRY.
[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 SER-307; SER-407; SER-409; THR-411; SER-413 AND SER-458, MASS SPECTROMETRY.
[12]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-277 AND SER-307, MASS SPECTROMETRY.
[14]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, MASS SPECTROMETRY.
[15]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, MASS SPECTROMETRY. Tissue: T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D26018 mRNA. Translation: BAA05039.1. Different initiation.
AK316301 mRNA. Translation: BAH14672.1.
CH471076 Genomic DNA. Translation: EAW74942.1.

IPI

IPI00394926.

RefSeq

NP_006582.1.

UniGene

Hs.82502

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U76	X-ray	2.60	B/D/F	452-466	[»]
3E0J	X-ray	3.00	B/D/F/H	1-144	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15054. 4 interactions.

STRING

Q15054.

PTM databases

PhosphoSite

Q15054.

Proteomic databases

PeptideAtlas

Q15054.

PRIDE

Q15054.

Genome annotation databases

Ensembl

ENST00000263681; ENSP00000263681; ENSG00000077514; Homo sapiens. [Genome view]

GeneID

10714.

KEGG

hsa:10714.

UCSC

uc001ovf.1. human.

Organism-specific databases

CTD

10714.

GeneCards

GC11P073981.

H-InvDB

HIX0009934.

HGNC

HGNC:20932. POLD3.

MIM

611415. gene.

PharmGKB

PA134868595.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG445280.

HOVERGEN

Q15054.

InParanoid

Q15054.

OMA

GIMGMFA.

OrthoDB

EOG9HHRN1.

PhylomeDB

Q15054.

Enzyme and pathway databases

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_216. DNA Repair.
REACT_383. DNA Replication.
REACT_7970. Telomere Maintenance.

Gene expression databases

ArrayExpress

Q15054.

Bgee

Q15054.

Genevestigator

Q15054.

GermOnline

ENSG00000077514. Homo sapiens.

Family and domain databases

InterPro

IPR019038. DNA_polymerase_subunit_Cdc27.
[Graphical view]

Pfam

PF09507. CDC27. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

40675.

SOURCE

Search...

Entry information

Entry name

DPOD3_HUMAN

Accession

Primary (citable) accession number: Q15054
Secondary accession number(s): B7ZAI6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	September 26, 2001
Last modified:	February 9, 2010
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.