Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P52431 (DPOD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA polymerase delta catalytic subunit

EC=2.7.7.7
Gene names
Name:Pold1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1105 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction. Required with its accessory proteins (proliferating cell nuclear antigen (PCNA) and replication factor C (RFC) or activator 1) for leading strand synthesis. Also involved in completing Okazaki fragments initiated by the DNA polymerase alpha/primase complex.

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactor

Binds 1 4Fe-4S cluster By similarity.

Subunit structure

Heterotetramer composed of subunits of 125 kDa, 50 kDa, 66 kDa and 12 kDa. The 125 kDa subunit contains the polymerase active site and most likely the active site for the 3'-5' exonuclease activity. Interacts with WRNIP1. Interacts with POLD4 and PCNA By similarity.

Subcellular location

Nucleus.

Domain

The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes By similarity.

Miscellaneous

In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.

Sequence similarities

Belongs to the DNA polymerase type-B family.

Contains 1 CysA-type zinc finger.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentNucleus
   DomainZinc-finger
   Ligand4Fe-4S
DNA-binding
Iron
Iron-sulfur
Metal-binding
Zinc
   Molecular functionDNA-directed DNA polymerase
Exonuclease
Hydrolase
Nuclease
Nucleotidyltransferase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication proofreading

Inferred from mutant phenotype PubMed 12429860. Source: MGI

DNA replication, removal of RNA primer

Inferred from Biological aspect of Ancestor. Source: RefGenome

DNA synthesis involved in DNA repair

Inferred from electronic annotation. Source: Ensembl

base-excision repair, gap-filling

Inferred from mutant phenotype PubMed 15177179. Source: MGI

fatty acid homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

nucleic acid phosphodiester bond hydrolysis

Inferred from mutant phenotype PubMed 12429860. Source: GOC

nucleotide-excision repair, DNA gap filling

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of mitotic cell cycle

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentdelta DNA polymerase complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleotide-excision repair complex

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_function3'-5' exonuclease activity

Inferred from mutant phenotype PubMed 12429860. Source: MGI

4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-directed DNA polymerase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

chromatin binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11051105DNA polymerase delta catalytic subunit
PRO_0000046444

Regions

Zinc finger1010 – 102718CysA-type
Motif4 – 1916Nuclear localization signal Potential
Motif1056 – 107419CysB motif

Sites

Metal binding10101Zinc By similarity
Metal binding10131Zinc By similarity
Metal binding10241Zinc By similarity
Metal binding10271Zinc By similarity
Metal binding10561Iron-sulfur (4Fe-4S) By similarity
Metal binding10591Iron-sulfur (4Fe-4S) By similarity
Metal binding10691Iron-sulfur (4Fe-4S) By similarity
Metal binding10741Iron-sulfur (4Fe-4S) By similarity

Experimental info

Sequence conflict1121G → R in CAA79895. Ref.1
Sequence conflict1141L → P in AAB99910. Ref.2
Sequence conflict5761S → G in CAA79895. Ref.1
Sequence conflict5761S → G in AAB99910. Ref.2
Sequence conflict7931E → K in AAB99910. Ref.2
Sequence conflict10001L → F in AAB99910. Ref.2
Sequence conflict10351Y → S in CAA79895. Ref.1
Sequence conflict1045 – 10528LEERFSRL → WKNGSLRF in AAB99910. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P52431 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 2AE377D42E3A6A86

FASTA1,105123,790
        10         20         30         40         50         60 
MDCKRRQGPG PGVPPKRARG HLWDEDEPSP SQFEANLALL EEIEAENRLQ EAEEELQLPP 

        70         80         90        100        110        120 
EGTVGGQFST ADIDPRWRRP TLRALDPSTE PLIFQQLEID HYVGSAPPLP EGPLPSRNSV 

       130        140        150        160        170        180 
PILRAFGVTD EGFSVCCHIQ GFAPYFYTPA PPGFGAEHLS ELQQELNAAI SRDQRGGKEL 

       190        200        210        220        230        240 
SGPAVLAIEL CSRESMFGYH GHGPSPFLRI TLALPRLMAP ARRLLEQGVR VPGLGTPSFA 

       250        260        270        280        290        300 
PYEANVDFEI RFMVDADIVG CNWLELPAGK YVRRAEKKAT LCQLEVDVLW SDVISHPPEG 

       310        320        330        340        350        360 
QWQRIAPLRV LSFDIECAGR KGIFPEPERD PVIQICSLGL RWGEPEPFLR LALTLRPCAP 

       370        380        390        400        410        420 
ILGAKVQSYE REEDLLQAWA DFILAMDPDV ITGYNIQNFD LPYLISRAQA LKVDRFPFLG 

       430        440        450        460        470        480 
RVTGLRSNIR DSSFQSRQVG RRDSKVISMV GRVQMDMLQV LLREHKLRSY TLNAVSFHFL 

       490        500        510        520        530        540 
GEQKEDVQHS IITDLQNGNE QTRRRLAVYC LKDAFLPLRL LERLMVLVNN VEMARVTGVP 

       550        560        570        580        590        600 
LGYLLTRGQQ VKVVSQLLRQ AMRQGLLMPV VKTEGSEDYT GATVIEPLKG YYDVPIATLD 

       610        620        630        640        650        660 
FSSLYPSIMM AHNLCYTTLL RPGAAQKLGL KPDEFIKTPT GDEFVKSSVR KGLLPQILEN 

       670        680        690        700        710        720 
LLSARKRAKA ELAQETDPLR RQVLDGRQLA LKVSANSVYG FTGAQVGKLP CLEISQSVTG 

       730        740        750        760        770        780 
FGRQMIEKTK QLVESKYTVE NGYDANAKVV YGDTDSVMCR FGVSSVAEAM SLGREAANWV 

       790        800        810        820        830        840 
SSHFPSPIRL EFEKVYFPYL LISKKRYAGL LFSSRSDAHD KMDCKGLEAV RRDNCPLVAN 

       850        860        870        880        890        900 
LVTSSLRRIL VDRDPDGAVA HAKDVISDLL CNRIDISQLV ITKELTRAAA DYAGKQAHVE 

       910        920        930        940        950        960 
LAERMRKRDP GSAPSLGDRV PYVIIGAAKG VAAYMKSEDP LFVLEHSLPI DTQYYLEQQL 

       970        980        990       1000       1010       1020 
AKPLLRIFEP ILGEGRAESV LLRGDHTRCK TVLTSKVGGL LAFTKRRNCC IGCRSVIDHQ 

      1030       1040       1050       1060       1070       1080 
GAVCKFCQPR ESELYQKEVS HLNALEERFS RLWTQCQRCQ GSLHEDVICT SRDCPIFYMR 

      1090       1100 
KKVRKDLEDQ ERLLQRFGPP GPEAW 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a mouse cDNA encoding DNA polymerase delta: refinement of the homology boxes."
Cullmann G., Hindges R., Berchtold M.W., Huebscher U.
Gene 134:191-200(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"Mouse DNA polymerase delta gene (Pold1) maps to chromosome 7."
Goldsby R.E., Singh M., Preston B.D.
Mamm. Genome 9:92-93(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Heart and Liver.
[4]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 408-415, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z21848 mRNA. Translation: CAA79895.1.
AF024570 Genomic DNA. Translation: AAB99910.1.
AK167569 mRNA. Translation: BAE39632.1.
AK168967 mRNA. Translation: BAE40772.1.
AK169040 mRNA. Translation: BAE40829.1.
CCDSCCDS21210.1.
PIRS40243.
RefSeqNP_035261.3. NM_011131.3.
UniGeneMm.16549.

3D structure databases

ProteinModelPortalP52431.
SMRP52431. Positions 297-969.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202290. 3 interactions.
DIPDIP-45885N.
IntActP52431. 1 interaction.
STRING10090.ENSMUSP00000039776.

PTM databases

PhosphoSiteP52431.

Proteomic databases

MaxQBP52431.
PaxDbP52431.
PRIDEP52431.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049343; ENSMUSP00000039776; ENSMUSG00000038644.
GeneID18971.
KEGGmmu:18971.
UCSCuc009gpx.2. mouse.

Organism-specific databases

CTD5424.
MGIMGI:97741. Pold1.

Phylogenomic databases

eggNOGCOG0417.
GeneTreeENSGT00560000077365.
HOGENOMHOG000036616.
HOVERGENHBG051395.
InParanoidQ3TFX6.
KOK02327.
OMAQLFRKAN.
OrthoDBEOG7992PP.
TreeFamTF352785.

Gene expression databases

BgeeP52431.
GenevestigatorP52431.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProIPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR004578. DNA-dir_DNA_pol_B_pol2.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
IPR025687. Znf-C4pol.
[Graphical view]
PfamPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF14260. zf-C4pol. 1 hit.
[Graphical view]
PRINTSPR00106. DNAPOLB.
SMARTSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMSSF53098. SSF53098. 1 hit.
TIGRFAMsTIGR00592. pol2. 1 hit.
PROSITEPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPOLD1. mouse.
NextBio295320.
PMAP-CutDBP52431.
PROP52431.
SOURCESearch...

Entry information

Entry nameDPOD1_MOUSE
AccessionPrimary (citable) accession number: P52431
Secondary accession number(s): O54883, Q3TFX6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot