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P52431

- DPOD1_MOUSE

UniProt

P52431 - DPOD1_MOUSE

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Protein
DNA polymerase delta catalytic subunit
Gene
Pold1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Binds 1 4Fe-4S cluster By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1010 – 10101Zinc By similarity
Metal bindingi1013 – 10131Zinc By similarity
Metal bindingi1024 – 10241Zinc By similarity
Metal bindingi1027 – 10271Zinc By similarity
Metal bindingi1056 – 10561Iron-sulfur (4Fe-4S) By similarity
Metal bindingi1059 – 10591Iron-sulfur (4Fe-4S) By similarity
Metal bindingi1069 – 10691Iron-sulfur (4Fe-4S) By similarity
Metal bindingi1074 – 10741Iron-sulfur (4Fe-4S) By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1010 – 102718CysA-type
Add
BLAST

GO - Molecular functioni

  1. 3'-5' exonuclease activity Source: MGI
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. DNA binding Source: UniProtKB-KW
  4. DNA-directed DNA polymerase activity Source: RefGenome
  5. chromatin binding Source: Ensembl
  6. metal ion binding Source: UniProtKB-KW
  7. nucleotide binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. DNA replication proofreading Source: MGI
  2. DNA replication, removal of RNA primer Source: RefGenome
  3. DNA synthesis involved in DNA repair Source: Ensembl
  4. base-excision repair, gap-filling Source: MGI
  5. fatty acid homeostasis Source: UniProtKB
  6. nucleic acid phosphodiester bond hydrolysis Source: GOC
  7. nucleotide-excision repair, DNA gap filling Source: RefGenome
  8. regulation of mitotic cell cycle Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

4Fe-4S, DNA-binding, Iron, Iron-sulfur, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_196637. Cytosolic iron-sulfur cluster assembly.
REACT_209299. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_216529. Removal of the Flap Intermediate from the C-strand.
REACT_219337. Removal of DNA patch containing abasic residue.
REACT_219381. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_220175. Telomere C-strand (Lagging Strand) Synthesis.
REACT_223154. Processive synthesis on the C-strand of the telomere.
REACT_225604. Polymerase switching on the C-strand of the telomere.
REACT_227394. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase delta catalytic subunit (EC:2.7.7.7)
Gene namesi
Name:Pold1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:97741. Pold1.

Subcellular locationi

GO - Cellular componenti

  1. delta DNA polymerase complex Source: RefGenome
  2. nucleotide-excision repair complex Source: Ensembl
  3. nucleus Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11051105DNA polymerase delta catalytic subunit
PRO_0000046444Add
BLAST

Proteomic databases

MaxQBiP52431.
PaxDbiP52431.
PRIDEiP52431.

PTM databases

PhosphoSiteiP52431.

Miscellaneous databases

PMAP-CutDBP52431.

Expressioni

Gene expression databases

BgeeiP52431.
GenevestigatoriP52431.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi202290. 3 interactions.
DIPiDIP-45885N.
IntActiP52431. 1 interaction.
STRINGi10090.ENSMUSP00000039776.

Structurei

3D structure databases

ProteinModelPortaliP52431.
SMRiP52431. Positions 297-969.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi4 – 1916Nuclear localization signal Reviewed prediction
Add
BLAST
Motifi1056 – 107419CysB motif
Add
BLAST

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0417.
GeneTreeiENSGT00560000077365.
HOGENOMiHOG000036616.
HOVERGENiHBG051395.
InParanoidiQ3TFX6.
KOiK02327.
OMAiQLFRKAN.
OrthoDBiEOG7992PP.
TreeFamiTF352785.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProiIPR006172. 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.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
IPR025687. Znf-C4pol.
[Graphical view]
PfamiPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF14260. zf-C4pol. 1 hit.
[Graphical view]
PRINTSiPR00106. DNAPOLB.
SMARTiSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52431-1 [UniParc]FASTAAdd to Basket

« Hide

MDCKRRQGPG PGVPPKRARG HLWDEDEPSP SQFEANLALL EEIEAENRLQ     50
EAEEELQLPP EGTVGGQFST ADIDPRWRRP TLRALDPSTE PLIFQQLEID 100
HYVGSAPPLP EGPLPSRNSV PILRAFGVTD EGFSVCCHIQ GFAPYFYTPA 150
PPGFGAEHLS ELQQELNAAI SRDQRGGKEL SGPAVLAIEL CSRESMFGYH 200
GHGPSPFLRI TLALPRLMAP ARRLLEQGVR VPGLGTPSFA PYEANVDFEI 250
RFMVDADIVG CNWLELPAGK YVRRAEKKAT LCQLEVDVLW SDVISHPPEG 300
QWQRIAPLRV LSFDIECAGR KGIFPEPERD PVIQICSLGL RWGEPEPFLR 350
LALTLRPCAP ILGAKVQSYE REEDLLQAWA DFILAMDPDV ITGYNIQNFD 400
LPYLISRAQA LKVDRFPFLG RVTGLRSNIR DSSFQSRQVG RRDSKVISMV 450
GRVQMDMLQV LLREHKLRSY TLNAVSFHFL GEQKEDVQHS IITDLQNGNE 500
QTRRRLAVYC LKDAFLPLRL LERLMVLVNN VEMARVTGVP LGYLLTRGQQ 550
VKVVSQLLRQ AMRQGLLMPV VKTEGSEDYT GATVIEPLKG YYDVPIATLD 600
FSSLYPSIMM AHNLCYTTLL RPGAAQKLGL KPDEFIKTPT GDEFVKSSVR 650
KGLLPQILEN LLSARKRAKA ELAQETDPLR RQVLDGRQLA LKVSANSVYG 700
FTGAQVGKLP CLEISQSVTG FGRQMIEKTK QLVESKYTVE NGYDANAKVV 750
YGDTDSVMCR FGVSSVAEAM SLGREAANWV SSHFPSPIRL EFEKVYFPYL 800
LISKKRYAGL LFSSRSDAHD KMDCKGLEAV RRDNCPLVAN LVTSSLRRIL 850
VDRDPDGAVA HAKDVISDLL CNRIDISQLV ITKELTRAAA DYAGKQAHVE 900
LAERMRKRDP GSAPSLGDRV PYVIIGAAKG VAAYMKSEDP LFVLEHSLPI 950
DTQYYLEQQL AKPLLRIFEP ILGEGRAESV LLRGDHTRCK TVLTSKVGGL 1000
LAFTKRRNCC IGCRSVIDHQ GAVCKFCQPR ESELYQKEVS HLNALEERFS 1050
RLWTQCQRCQ GSLHEDVICT SRDCPIFYMR KKVRKDLEDQ ERLLQRFGPP 1100
GPEAW 1105
Length:1,105
Mass (Da):123,790
Last modified:July 27, 2011 - v2
Checksum:i2AE377D42E3A6A86
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121G → R in CAA79895. 1 Publication
Sequence conflicti114 – 1141L → P in AAB99910. 1 Publication
Sequence conflicti576 – 5761S → G in CAA79895. 1 Publication
Sequence conflicti576 – 5761S → G in AAB99910. 1 Publication
Sequence conflicti793 – 7931E → K in AAB99910. 1 Publication
Sequence conflicti1000 – 10001L → F in AAB99910. 1 Publication
Sequence conflicti1035 – 10351Y → S in CAA79895. 1 Publication
Sequence conflicti1045 – 10528LEERFSRL → WKNGSLRF in AAB99910. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS21210.1.
PIRiS40243.
RefSeqiNP_035261.3. NM_011131.3.
UniGeneiMm.16549.

Genome annotation databases

EnsembliENSMUST00000049343; ENSMUSP00000039776; ENSMUSG00000038644.
GeneIDi18971.
KEGGimmu:18971.
UCSCiuc009gpx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS21210.1.
PIRi S40243.
RefSeqi NP_035261.3. NM_011131.3.
UniGenei Mm.16549.

3D structure databases

ProteinModelPortali P52431.
SMRi P52431. Positions 297-969.
ModBasei Search...

Protein-protein interaction databases

BioGridi 202290. 3 interactions.
DIPi DIP-45885N.
IntActi P52431. 1 interaction.
STRINGi 10090.ENSMUSP00000039776.

PTM databases

PhosphoSitei P52431.

Proteomic databases

MaxQBi P52431.
PaxDbi P52431.
PRIDEi P52431.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000049343 ; ENSMUSP00000039776 ; ENSMUSG00000038644 .
GeneIDi 18971.
KEGGi mmu:18971.
UCSCi uc009gpx.2. mouse.

Organism-specific databases

CTDi 5424.
MGIi MGI:97741. Pold1.

Phylogenomic databases

eggNOGi COG0417.
GeneTreei ENSGT00560000077365.
HOGENOMi HOG000036616.
HOVERGENi HBG051395.
InParanoidi Q3TFX6.
KOi K02327.
OMAi QLFRKAN.
OrthoDBi EOG7992PP.
TreeFami TF352785.

Enzyme and pathway databases

Reactomei REACT_196637. Cytosolic iron-sulfur cluster assembly.
REACT_209299. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_216529. Removal of the Flap Intermediate from the C-strand.
REACT_219337. Removal of DNA patch containing abasic residue.
REACT_219381. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_220175. Telomere C-strand (Lagging Strand) Synthesis.
REACT_223154. Processive synthesis on the C-strand of the telomere.
REACT_225604. Polymerase switching on the C-strand of the telomere.
REACT_227394. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.

Miscellaneous databases

ChiTaRSi POLD1. mouse.
NextBioi 295320.
PMAP-CutDB P52431.
PROi P52431.
SOURCEi Search...

Gene expression databases

Bgeei P52431.
Genevestigatori P52431.

Family and domain databases

Gene3Di 3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProi IPR006172. 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.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
IPR025687. Znf-C4pol.
[Graphical view ]
Pfami PF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF14260. zf-C4pol. 1 hit.
[Graphical view ]
PRINTSi PR00106. DNAPOLB.
SMARTi SM00486. POLBc. 1 hit.
[Graphical view ]
SUPFAMi SSF53098. SSF53098. 1 hit.
PROSITEi PS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiDPOD1_MOUSE
AccessioniPrimary (citable) accession number: P52431
Secondary accession number(s): O54883, Q3TFX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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