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Protein

DNA polymerase alpha subunit B

Gene

Pola2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May play an essential role at the early stage of chromosomal DNA replication by coupling the polymerase alpha/primase complex to the cellular replication machinery.By similarity

GO - Molecular functioni

  • DNA binding Source: InterPro
  • DNA-directed DNA polymerase activity Source: InterPro
  • protein heterodimerization activity Source: MGI

GO - Biological processi

  • DNA replication Source: MGI
  • DNA replication initiation Source: GO_Central
  • protein import into nucleus, translocation Source: MGI
Complete GO annotation...

Keywords - Biological processi

DNA replication

Enzyme and pathway databases

ReactomeiR-MMU-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-MMU-174411. Polymerase switching on the C-strand of the telomere.
R-MMU-174430. Telomere C-strand synthesis initiation.
R-MMU-68952. DNA replication initiation.
R-MMU-68962. Activation of the pre-replicative complex.
R-MMU-69091. Polymerase switching.
R-MMU-69109. Leading Strand Synthesis.
R-MMU-69166. Removal of the Flap Intermediate.
R-MMU-69183. Processive synthesis on the lagging strand.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase alpha subunit B
Alternative name(s):
DNA polymerase alpha 70 kDa subunit
Gene namesi
Name:Pola2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:99690. Pola2.

Subcellular locationi

GO - Cellular componenti

  • alpha DNA polymerase:primase complex Source: MGI
  • cytoplasm Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 600600DNA polymerase alpha subunit BPRO_0000194036Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei126 – 1261PhosphoserineBy similarity
Modified residuei127 – 1271PhosphothreonineCombined sources
Modified residuei130 – 1301PhosphothreonineCombined sources
Modified residuei141 – 1411PhosphoserineBy similarity
Modified residuei147 – 1471PhosphoserineBy similarity
Modified residuei152 – 1521PhosphoserineBy similarity
Modified residuei154 – 1541PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated in a cell cycle-dependent manner, in G2/M phase.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP33611.
MaxQBiP33611.
PaxDbiP33611.
PeptideAtlasiP33611.
PRIDEiP33611.

PTM databases

iPTMnetiP33611.
PhosphoSiteiP33611.

Expressioni

Gene expression databases

BgeeiP33611.
CleanExiMM_POLA2.
ExpressionAtlasiP33611. baseline and differential.
GenevisibleiP33611. MM.

Interactioni

Subunit structurei

DNA polymerase alpha:primase is a four subunit enzyme complex, which is assembled throughout the cell cycle, and consists of the two DNA polymerase subunits A and B, and the DNA primase large and small subunits. Subunit B binds to subunit A.

Binary interactionsi

WithEntry#Exp.IntActNotes
Pola1P336095EBI-848759,EBI-688051

GO - Molecular functioni

  • protein heterodimerization activity Source: MGI

Protein-protein interaction databases

IntActiP33611. 3 interactions.
STRINGi10090.ENSMUSP00000025752.

Structurei

3D structure databases

ProteinModelPortaliP33611.
SMRiP33611. Positions 1-77, 207-565.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi101 – 1077Poly-Glu
Compositional biasi115 – 15743Pro/Ser/Thr-richAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1625. Eukaryota.
COG5214. LUCA.
GeneTreeiENSGT00390000016784.
HOGENOMiHOG000007382.
HOVERGENiHBG055628.
InParanoidiP33611.
KOiK02321.
OMAiGDREHSS.
OrthoDBiEOG7GXPB7.
TreeFamiTF314249.

Family and domain databases

InterProiIPR007185. DNA_pol_alpha/epsilon_bsu.
IPR016722. DNA_pol_alpha_bsu.
IPR013627. Pol_alpha_B_N.
[Graphical view]
PfamiPF04042. DNA_pol_E_B. 1 hit.
PF08418. Pol_alpha_B_N. 1 hit.
[Graphical view]
PIRSFiPIRSF018300. DNA_pol_alph_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P33611-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSTQQLAE ELQIFGLDYE DSLLEKLAEL CVLYRQTEDG MVSELIAFCT
60 70 80 90 100
SAGKTCLTVD ILNSFEYEVL NKKLSKAWHS ASKDSGHAGT RDIVSIQELI
110 120 130 140 150
EAEEEEETLL SSYTTPSKGP LKRVSSTPET PLTKRSVAAR SPRQLLSPSS
160 170 180 190 200
FSPSATPSQK YTSRTNRGEV VTTFGSAQGL SWSGRGGSGS VSLKVVGDPE
210 220 230 240 250
PLTGSYKAMF QQLMGVREVL TSKIEELGSE LKEHHKIEAF TPLLVPAQEP
260 270 280 290 300
VILLGQIGCD SNGKLNSKSV ILEGDQEHSY GAQIPVDLSE LKEYSLFPGQ
310 320 330 340 350
VVIMEGFNTT GRRLTATKLY EGVPLPFYQP TEEEGASEQT MVVVACGPYT
360 370 380 390 400
TSDSITYDPL LDLIAIINRD QPDVCILFGP FLDAKHEQVE NCKLTSPFED
410 420 430 440 450
VFKQCLRTVI EGTRSSGSHL VFVPSLRDVH HEPVYPQPPF TFSELSREDK
460 470 480 490 500
KRVQFVSEPC SLSINGVMFG LTSTDLLFHI GAEEIFSSSG TSDRFSRVLK
510 520 530 540 550
HILTQRSYYP LYPPHEDMAI DYENFYTYAQ LPVTPDVFIV PSELRYFVKD
560 570 580 590 600
IFGCVCVNPG RLTKGQVGGT FGRLYLRRQP KAMDGGGRQG LSVAAQVVRI
Length:600
Mass (Da):66,214
Last modified:July 27, 2011 - v2
Checksum:i79F94443EF33FAA9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti346 – 3461C → R in BAA02746 (PubMed:8463324).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13546 mRNA. Translation: BAA02746.1.
AK150099 mRNA. Translation: BAE29306.1.
CH466612 Genomic DNA. Translation: EDL33190.1.
BC021424 mRNA. Translation: AAH21424.1.
BC064795 mRNA. Translation: AAH64795.1.
CCDSiCCDS29485.1.
PIRiB46642.
RefSeqiNP_032919.2. NM_008893.3.
UniGeneiMm.209931.

Genome annotation databases

EnsembliENSMUST00000025752; ENSMUSP00000025752; ENSMUSG00000024833.
GeneIDi18969.
KEGGimmu:18969.
UCSCiuc008ggb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13546 mRNA. Translation: BAA02746.1.
AK150099 mRNA. Translation: BAE29306.1.
CH466612 Genomic DNA. Translation: EDL33190.1.
BC021424 mRNA. Translation: AAH21424.1.
BC064795 mRNA. Translation: AAH64795.1.
CCDSiCCDS29485.1.
PIRiB46642.
RefSeqiNP_032919.2. NM_008893.3.
UniGeneiMm.209931.

3D structure databases

ProteinModelPortaliP33611.
SMRiP33611. Positions 1-77, 207-565.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP33611. 3 interactions.
STRINGi10090.ENSMUSP00000025752.

PTM databases

iPTMnetiP33611.
PhosphoSiteiP33611.

Proteomic databases

EPDiP33611.
MaxQBiP33611.
PaxDbiP33611.
PeptideAtlasiP33611.
PRIDEiP33611.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025752; ENSMUSP00000025752; ENSMUSG00000024833.
GeneIDi18969.
KEGGimmu:18969.
UCSCiuc008ggb.2. mouse.

Organism-specific databases

CTDi23649.
MGIiMGI:99690. Pola2.

Phylogenomic databases

eggNOGiKOG1625. Eukaryota.
COG5214. LUCA.
GeneTreeiENSGT00390000016784.
HOGENOMiHOG000007382.
HOVERGENiHBG055628.
InParanoidiP33611.
KOiK02321.
OMAiGDREHSS.
OrthoDBiEOG7GXPB7.
TreeFamiTF314249.

Enzyme and pathway databases

ReactomeiR-MMU-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-MMU-174411. Polymerase switching on the C-strand of the telomere.
R-MMU-174430. Telomere C-strand synthesis initiation.
R-MMU-68952. DNA replication initiation.
R-MMU-68962. Activation of the pre-replicative complex.
R-MMU-69091. Polymerase switching.
R-MMU-69109. Leading Strand Synthesis.
R-MMU-69166. Removal of the Flap Intermediate.
R-MMU-69183. Processive synthesis on the lagging strand.

Miscellaneous databases

PROiP33611.
SOURCEiSearch...

Gene expression databases

BgeeiP33611.
CleanExiMM_POLA2.
ExpressionAtlasiP33611. baseline and differential.
GenevisibleiP33611. MM.

Family and domain databases

InterProiIPR007185. DNA_pol_alpha/epsilon_bsu.
IPR016722. DNA_pol_alpha_bsu.
IPR013627. Pol_alpha_B_N.
[Graphical view]
PfamiPF04042. DNA_pol_E_B. 1 hit.
PF08418. Pol_alpha_B_N. 1 hit.
[Graphical view]
PIRSFiPIRSF018300. DNA_pol_alph_2. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the cDNAs for the four subunits of mouse DNA polymerase alpha-primase complex and their gene expression during cell proliferation and the cell cycle."
    Miyazawa H., Izumi M., Tada S., Takada R., Masutani M., Ui M., Hanaoka F.
    J. Biol. Chem. 268:8111-8122(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 84-102; 269-285 AND 394-403.
  2. "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: Bone marrow.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Strain: C57BL/6J and FVB/N-3.
    Tissue: Mammary tumor.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-127 AND THR-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung and Spleen.

Entry informationi

Entry nameiDPOA2_MOUSE
AccessioniPrimary (citable) accession number: P33611
Secondary accession number(s): Q8VDR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.