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Q14181

- DPOA2_HUMAN

UniProt

Q14181 - DPOA2_HUMAN

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Protein
DNA polymerase alpha subunit B
Gene
POLA2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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

  1. DNA binding Source: InterPro
  2. DNA-directed DNA polymerase activity Source: InterPro
  3. protein heterodimerization activity Source: RefGenome
Complete GO annotation...

GO - Biological processi

  1. DNA replication Source: UniProtKB
  2. DNA replication initiation Source: RefGenome
  3. DNA strand elongation involved in DNA replication Source: Reactome
  4. G1/S transition of mitotic cell cycle Source: Reactome
  5. mitotic cell cycle Source: Reactome
  6. protein import into nucleus, translocation Source: Ensembl
  7. telomere maintenance Source: Reactome
  8. telomere maintenance via recombination Source: Reactome
  9. telomere maintenance via semi-conservative replication Source: Reactome
Complete GO annotation...

Keywords - Biological processi

DNA replication

Enzyme and pathway databases

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_1385. Processive synthesis on the lagging strand.
REACT_1792. Polymerase switching.
REACT_1838. Leading Strand Synthesis.
REACT_2244. DNA replication initiation.
REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_70. Removal of the Flap Intermediate.
REACT_7987. Polymerase switching on the C-strand of the telomere.
REACT_7993. Telomere C-strand synthesis initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase alpha subunit B
Alternative name(s):
DNA polymerase alpha 70 kDa subunit
Gene namesi
Name:POLA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:30073. POLA2.

Subcellular locationi

GO - Cellular componenti

  1. alpha DNA polymerase:primase complex Source: RefGenome
  2. cytoplasm Source: HPA
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA411.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 598598DNA polymerase alpha subunit B
PRO_0000194035Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei126 – 1261Phosphoserine1 Publication
Modified residuei127 – 1271Phosphothreonine2 Publications
Modified residuei130 – 1301Phosphothreonine2 Publications
Modified residuei141 – 1411Phosphoserine4 Publications
Modified residuei147 – 1471Phosphoserine2 Publications
Modified residuei152 – 1521Phosphoserine3 Publications

Post-translational modificationi

Phosphorylated in a cell cycle-dependent manner, in G2/M phase.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14181.
PaxDbiQ14181.
PeptideAtlasiQ14181.
PRIDEiQ14181.

PTM databases

PhosphoSiteiQ14181.

Expressioni

Gene expression databases

ArrayExpressiQ14181.
BgeeiQ14181.
CleanExiHS_POLA2.
GenevestigatoriQ14181.

Organism-specific databases

HPAiHPA037570.

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.

Protein-protein interaction databases

BioGridi117176. 41 interactions.
IntActiQ14181. 31 interactions.
MINTiMINT-1382407.
STRINGi9606.ENSP00000265465.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1511
Helixi21 – 3414
Helixi38 – 5215
Helixi59 – 6810
Helixi70 – 734

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KEBNMR-A1-78[»]
4E2IX-ray5.001/2/3/4/5/6/7/8/9/U/W1-78[»]
ProteinModelPortaliQ14181.
SMRiQ14181. Positions 1-78.

Miscellaneous databases

EvolutionaryTraceiQ14181.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi101 – 1077Poly-Glu
Compositional biasi115 – 15743Pro/Ser/Thr-rich
Add
BLAST
Compositional biasi486 – 4894Poly-Ser

Domaini

The N-terminal 240 amino acids are sufficient to mediate complex formation.

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5214.
HOGENOMiHOG000007382.
HOVERGENiHBG055628.
InParanoidiQ14181.
KOiK02321.
OMAiDREHSSG.
OrthoDBiEOG7GXPB7.
PhylomeDBiQ14181.
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.

Q14181-1 [UniParc]FASTAAdd to Basket

« Hide

MSASAQQLAE ELQIFGLDCE EALIEKLVEL CVQYGQNEEG MVGELIAFCT    50
STHKVGLTSE ILNSFEHEFL SKRLSKARHS TCKDSGHAGA RDIVSIQELI 100
EVEEEEEILL NSYTTPSKGS QKRAISTPET PLTKRSVSTR SPHQLLSPSS 150
FSPSATPSQK YNSRSNRGEV VTSFGLAQGV SWSGRGGAGN ISLKVLGCPE 200
ALTGSYKSMF QKLPDIREVL TCKIEELGSE LKEHYKIEAF TPLLAPAQEP 250
VTLLGQIGCD SNGKLNNKSV ILEGDREHSS GAQIPVDLSE LKEYSLFPGQ 300
VVIMEGINTT GRKLVATKLY EGVPLPFYQP TEEDADFEQS MVLVACGPYT 350
TSDSITYDPL LDLIAVINHD RPDVCILFGP FLDAKHEQVE NCLLTSPFED 400
IFKQCLRTII EGTRSSGSHL VFVPSLRDVH HEPVYPQPPF SYSDLSREDK 450
KQVQFVSEPC SLSINGVIFG LTSTDLLFHL GAEEISSSSG TSDRFSRILK 500
HILTQRSYYP LYPPQEDMAI DYESFYVYAQ LPVTPDVLII PSELRYFVKD 550
VLGCVCVNPG RLTKGQVGGT FARLYLRRPA ADGAERQSPC IAVQVVRI 598
Length:598
Mass (Da):65,948
Last modified:February 7, 2006 - v2
Checksum:iF5CBD7E022ADDDBF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti583 – 5831G → R.
Corresponds to variant rs487989 [ dbSNP | Ensembl ].
VAR_033896
Natural varianti588 – 5881S → N.
Corresponds to variant rs7123885 [ dbSNP | Ensembl ].
VAR_033897

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti383 – 3842DA → ES in AAA16459. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L24559 mRNA. Translation: AAA16459.1.
CR456737 mRNA. Translation: CAG33018.1.
BC002990 mRNA. Translation: AAH02990.1.
BC001347 mRNA. Translation: AAH01347.1.
CCDSiCCDS8098.1.
PIRiS39621.
RefSeqiNP_002680.2. NM_002689.2.
UniGeneiHs.201897.

Genome annotation databases

EnsembliENST00000265465; ENSP00000265465; ENSG00000014138.
GeneIDi23649.
KEGGihsa:23649.
UCSCiuc001odj.3. human.

Polymorphism databases

DMDMi90110415.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L24559 mRNA. Translation: AAA16459.1 .
CR456737 mRNA. Translation: CAG33018.1 .
BC002990 mRNA. Translation: AAH02990.1 .
BC001347 mRNA. Translation: AAH01347.1 .
CCDSi CCDS8098.1.
PIRi S39621.
RefSeqi NP_002680.2. NM_002689.2.
UniGenei Hs.201897.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KEB NMR - A 1-78 [» ]
4E2I X-ray 5.00 1/2/3/4/5/6/7/8/9/U/W 1-78 [» ]
ProteinModelPortali Q14181.
SMRi Q14181. Positions 1-78.
ModBasei Search...

Protein-protein interaction databases

BioGridi 117176. 41 interactions.
IntActi Q14181. 31 interactions.
MINTi MINT-1382407.
STRINGi 9606.ENSP00000265465.

Chemistry

DrugBanki DB00851. Dacarbazine.

PTM databases

PhosphoSitei Q14181.

Polymorphism databases

DMDMi 90110415.

Proteomic databases

MaxQBi Q14181.
PaxDbi Q14181.
PeptideAtlasi Q14181.
PRIDEi Q14181.

Protocols and materials databases

DNASUi 23649.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265465 ; ENSP00000265465 ; ENSG00000014138 .
GeneIDi 23649.
KEGGi hsa:23649.
UCSCi uc001odj.3. human.

Organism-specific databases

CTDi 23649.
GeneCardsi GC11P065029.
HGNCi HGNC:30073. POLA2.
HPAi HPA037570.
neXtProti NX_Q14181.
PharmGKBi PA411.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5214.
HOGENOMi HOG000007382.
HOVERGENi HBG055628.
InParanoidi Q14181.
KOi K02321.
OMAi DREHSSG.
OrthoDBi EOG7GXPB7.
PhylomeDBi Q14181.
TreeFami TF314249.

Enzyme and pathway databases

Reactomei REACT_1095. Activation of the pre-replicative complex.
REACT_1385. Processive synthesis on the lagging strand.
REACT_1792. Polymerase switching.
REACT_1838. Leading Strand Synthesis.
REACT_2244. DNA replication initiation.
REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_70. Removal of the Flap Intermediate.
REACT_7987. Polymerase switching on the C-strand of the telomere.
REACT_7993. Telomere C-strand synthesis initiation.

Miscellaneous databases

ChiTaRSi POLA2. human.
EvolutionaryTracei Q14181.
GeneWikii POLA2.
GenomeRNAii 23649.
NextBioi 46481.
PROi Q14181.

Gene expression databases

ArrayExpressi Q14181.
Bgeei Q14181.
CleanExi HS_POLA2.
Genevestigatori Q14181.

Family and domain databases

InterProi IPR007185. DNA_pol_alpha/epsilon_bsu.
IPR016722. DNA_pol_alpha_bsu.
IPR013627. Pol_alpha_B_N.
[Graphical view ]
Pfami PF04042. DNA_pol_E_B. 1 hit.
PF08418. Pol_alpha_B_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF018300. DNA_pol_alph_2. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The role of the 70 kDa subunit of human DNA polymerase alpha in DNA replication."
    Collins K.L., Russo A.A.R., Tseng B.Y., Kelly T.J.
    EMBO J. 12:4555-4566(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Cervix epithelium.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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.
  4. "Cell cycle-dependent phosphorylation of human DNA polymerase alpha."
    Nasheuer H.-P., Moore A., Wahl A.F., Wang T.S.-F.
    J. Biol. Chem. 266:7893-7903(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; THR-127; THR-130; SER-141 AND SER-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "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 THR-127; THR-130; SER-141; SER-147 AND SER-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDPOA2_HUMAN
AccessioniPrimary (citable) accession number: Q14181
Secondary accession number(s): Q9BPV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 7, 2006
Last modified: September 3, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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