DNA polymerase delta subunit 2 - Homo sapiens (Human)

Contribute

Send feedback

Read comments (?) or add your own

P49005 (DPOD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 127. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
DNA polymerase delta subunit 2
EC=2.7.7.7

Alternative name(s):
DNA polymerase delta subunit p50

Gene names

Name:

POLD2

Organism

Homo sapiens (Human) [Reference 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	469 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The function of the small subunit is not yet clear.
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Subunit structure	Heterotetramer composed of subunits of 125 kDa, 50 kDa, 66 kDa and 12 kDa. Interacts with KCTD10 By similarity. Interacts with KCTD13/POLDIP1, POLDIP2 and POLDIP3. Interacts with WRNIP1. Interacts with POLD4. Ref.5 Ref.6 Ref.7 Ref.8
Subcellular location	Nucleus.
Sequence similarities	Belongs to the DNA polymerase delta/II small subunit family.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Molecular function	DNA-directed DNA polymerase Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA strand elongation involved in DNA replication Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome base-excision repair Traceable author statement. Source: Reactome nucleotide-excision repair, DNA gap filling Traceable author statement. Source: Reactome 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_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
POLD1	P28340	9	EBI-372354,EBI-716569
POLD3	Q15054	5	EBI-372354,EBI-864956
POLD4	Q9HCU8	3	EBI-372354,EBI-864968
WRNIP1	Q96S55	2	EBI-372354,EBI-2513471

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 469

469

DNA polymerase delta subunit 2

PRO_0000096166

Amino acid modifications

Modified residue

Phosphoserine Ref.9

Natural variations

Natural variant

303

N → S. Ref.3
Corresponds to variant rs3087366 [ dbSNP | Ensembl ].

VAR_014885

Secondary structure

469

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P49005 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 389EF730999755AC
Show »

FASTA

469

51,289

        10         20         30         40         50         60 
MFSEQAAQRA HTLLSPPSAN NATFARVPVA TYTNSSQPFR LGERSFSRQY AHIYATRLIQ 

        70         80         90        100        110        120 
MRPFLENRAQ QHWGSGVGVK KLCELQPEEK CCVVGTLFKA MPLQPSILRE VSEEHNLLPQ 

       130        140        150        160        170        180 
PPRSKYIHPD DELVLEDELQ RIKLKGTIDV SKLVTGTVLA VFGSVRDDGK FLVEDYCFAD 

       190        200        210        220        230        240 
LAPQKPAPPL DTDRFVLLVS GLGLGGGGGE SLLGTQLLVD VVTGQLGDEG EQCSAAHVSR 

       250        260        270        280        290        300 
VILAGNLLSH STQSRDSINK AKYLTKKTQA ASVEAVKMLD EILLQLSASV PVDVMPGEFD 

       310        320        330        340        350        360 
PTNYTLPQQP LHPCMFPLAT AYSTLQLVTN PYQATIDGVR FLGTSGQNVS DIFRYSSMED 

       370        380        390        400        410        420 
HLEILEWTLR VRHISPTAPD TLGCYPFYKT DPFIFPECPH VYFCGNTPSF GSKIIRGPED 

       430        440        450        460 
QTVLLVTVPD FSATQTACLV NLRSLACQPI SFSGFGAEDD DLGGLGLGP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the cDNAs for the small subunits of bovine and human DNA polymerase delta and chromosomal location of the human gene (POLD2)." Zhang J., Tan C.-K., McMullen B., Downey K.M., So A.G. Genomics 29:179-186(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Characterization of the 5'-flanking region of the gene encoding the 50 kDa subunit of human DNA polymerase delta." Perez A., Leon A., Lee M.Y.W.T. Biochim. Biophys. Acta 1493:231-236(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	NIEHS SNPs program Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-303.
[4]	"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]. Tissue: Lung.
[5]	"A tumor necrosis factor alpha- and interleukin 6-inducible protein that interacts with the small subunit of DNA polymerase delta and proliferating cell nuclear antigen." He H., Tan C.-K., Downey K.M., So A.G. Proc. Natl. Acad. Sci. U.S.A. 98:11979-11984(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KCTD13/POLDIP1.
[6]	"Identification of a novel protein, PDIP38, that interacts with the p50 subunit of DNA polymerase delta and proliferating cell nuclear antigen." Liu L., Rodriguez-Belmonte E.M., Mazloum N., Xie B., Lee M.Y.W.T. J. Biol. Chem. 278:10041-10047(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH POLDIP2 AND POLDIP3.
[7]	"Human Werner helicase interacting protein 1 (WRNIP1) functions as a novel modulator for DNA polymerase delta." Tsurimoto T., Shinozaki A., Yano M., Seki M., Enomoto T. Genes Cells 10:13-22(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WRNIP1.
[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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH POLD4.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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].
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U21090 mRNA. Translation: AAC50216.1.
AF239710 Genomic DNA. Translation: AAG09763.1.
AY116646 Genomic DNA. Translation: AAM51148.1.
BC000459 mRNA. Translation: AAH00459.1.

IPI

IPI00025616.

PIR

I38950.

RefSeq

NP_001120690.1. NM_001127218.2.
NP_001243808.1. NM_001256879.1.
NP_006221.2. NM_006230.3.

UniGene

Hs.306791.
Hs.740138.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3E0J	X-ray	3.00	A/C/E/G	1-469	[»]

ProteinModelPortal

P49005.

ModBase

Search...

Protein-protein interaction databases

IntAct

P49005. 14 interactions.

STRING

9606.ENSP00000379148.

PTM databases

PhosphoSite

P49005.

Polymorphism databases

DMDM

1352307.

Proteomic databases

PaxDb

P49005.

PeptideAtlas

P49005.

PRIDE

P49005.

Protocols and materials databases

DNASU

5425.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000406581; ENSP00000386105; ENSG00000106628.
ENST00000452185; ENSP00000395231; ENSG00000106628.

GeneID

5425.

KEGG

hsa:5425.

UCSC

uc003tkf.4. human.

Organism-specific databases

CTD

5425.

GeneCards

GC07M044120.

HGNC

HGNC:9176. POLD2.

HPA

HPA026745.

MIM

600815. gene.

neXtProt

NX_P49005.

PharmGKB

PA33497.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1311.

HOGENOM

HOG000189057.

HOVERGEN

HBG051396.

InParanoid

P49005.

K02328.

OMA

HWGSGVG.

OrthoDB

EOG41NTKZ.

PhylomeDB

P49005.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.
REACT_216. DNA Repair.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpress

P49005.

Bgee

P49005.

CleanEx

HS_POLD2.

Genevestigator

P49005.

GermOnline

ENSG00000106628. Homo sapiens.

Family and domain databases

InterPro

IPR007185. DNA_pol_alpha/epsilon_bsu.
IPR024826. DNA_pol_delta/II_ssu.
[Graphical view]

PANTHER

PTHR10416. PTHR10416. 1 hit.

Pfam

PF04042. DNA_pol_E_B. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL2763.

ChiTaRS

POLD2. human.

EvolutionaryTrace

P49005.

GenomeRNAi

5425.

NextBio

20989.

SOURCE

Search...

Entry information

Entry name

DPOD2_HUMAN

Accession

Primary (citable) accession number: P49005

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 127 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.

Relevant documents

Human chromosome 7

Human chromosome 7: 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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents