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Q15054 (DPOD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 delta subunit 3
Alternative name(s):
DNA polymerase delta subunit p66
Gene names
Name:POLD3
Synonyms:KIAA0039
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence caution

The sequence BAA05039.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   Molecular functionDNA-directed DNA polymerase
Nucleotidyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processDNA strand elongation involved in DNA replication

Traceable author statement. Source: Reactome

DNA synthesis involved in DNA repair

Non-traceable author statement. Source: UniProtKB

S phase of mitotic cell cycle

Traceable author statement. Source: Reactome

base-excision repair

Traceable author statement. Source: Reactome

mismatch repair

Non-traceable author statement. Source: UniProtKB

nucleotide-excision repair, DNA gap filling

Inferred from mutant phenotype. Source: UniProtKB

telomere maintenance via recombination

Traceable author statement. Source: Reactome

telomere maintenance via semi-conservative replication

Traceable author statement. Source: Reactome

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

   Cellular componentdelta DNA polymerase complex

Non-traceable author statement Ref.5. Source: UniProtKB

mitochondrion

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular functionDNA-directed DNA polymerase activity

Non-traceable author statement Ref.5. Source: UniProtKB

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PCNAP120044EBI-864956,EBI-358311
POLD2P490055EBI-864956,EBI-372354

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 466465DNA polymerase delta subunit 3
PRO_0000186047

Amino acid modifications

Modified residue21N-acetylalanine Ref.4
Modified residue2771Phosphothreonine Ref.12
Modified residue3071Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Modified residue4071Phosphoserine Ref.7 Ref.11
Modified residue4091Phosphoserine Ref.7 Ref.11
Modified residue4111Phosphothreonine Ref.7 Ref.11
Modified residue4131Phosphoserine Ref.7 Ref.11
Modified residue4581Phosphoserine Ref.11

Natural variations

Natural variant1941G → V Found in a renal cell carcinoma sample; somatic mutation. Ref.15
VAR_064745
Natural variant1951M → L Found in a renal cell carcinoma sample; somatic mutation. Ref.15
VAR_064746

Secondary structure

... 466
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15054 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: E9625E0188725F45

FASTA46651,400
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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: Cervix carcinoma.
[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.
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-307, 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 SER-307; SER-407; SER-409; THR-411; SER-413 AND SER-458, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-277 AND SER-307, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[13]"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.
[14]"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: Leukemic T-cell.
[15]"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma."
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. expand/collapse author list , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 469:539-542(2011) [PubMed: 21248752] [Abstract]
Cited for: VARIANTS VAL-194 AND LEU-195.
[16]"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.

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.
IPIIPI00394926.
RefSeqNP_006582.1. NM_006591.1.
UniGeneHs.82502.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U76X-ray2.60B/D/F452-466[»]
3E0JX-ray3.00B/D/F/H1-144[»]
ProteinModelPortalQ15054.
SMRQ15054. Positions 2-144.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-35772N.
IntActQ15054. 4 interactions.
MINTMINT-2789689.
STRINGQ15054.

PTM databases

PhosphoSiteQ15054.

Polymorphism databases

DMDM17375506.

Proteomic databases

PeptideAtlasQ15054.
PRIDEQ15054.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263681; ENSP00000263681; ENSG00000077514.
GeneID10714.
KEGGhsa:10714.
UCSCuc001ovf.1. human.

Organism-specific databases

CTD10714.
GeneCardsGC11P074207.
H-InvDBHIX0009934.
HGNCHGNC:20932. POLD3.
HPAHPA039627.
MIM611415. gene.
neXtProtNX_Q15054.
PharmGKBPA134868595.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG445280.
HOVERGENHBG051397.
InParanoidQ15054.
OMAQQPKGIM.
OrthoDBEOG49KFQR.
PhylomeDBQ15054.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_216. DNA Repair.
REACT_22172. Chromosome Maintenance.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressQ15054.
BgeeQ15054.
GenevestigatorQ15054.
GermOnlineENSG00000077514. Homo sapiens.

Family and domain databases

InterProIPR019038. DNA_polymerase_subunit_Cdc27.
[Graphical view]
KOK03504.
PfamPF09507. CDC27. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio40675.
SOURCESearch...

Entry information

Entry nameDPOD3_HUMAN
AccessionPrimary (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: January 25, 2012
This is version 101 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

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Human chromosome 11: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references