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Q14181 (DPOA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 alpha subunit B
Alternative name(s):
DNA polymerase alpha 70 kDa subunit
Gene names
Name:POLA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length598 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Nucleus.

Domain

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

Post-translational modification

Phosphorylated in a cell cycle-dependent manner, in G2/M phase. Ref.4

Sequence similarities

Belongs to the DNA polymerase alpha subunit B family.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Non-traceable author statement Ref.1. Source: UniProtKB

DNA replication initiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

DNA strand elongation involved in DNA replication

Traceable author statement. Source: Reactome

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

protein import into nucleus, translocation

Inferred from electronic annotation. Source: Ensembl

telomere maintenance

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

   Cellular_componentalpha DNA polymerase:primase complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasm

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: InterPro

protein heterodimerization activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 598598DNA polymerase alpha subunit B
PRO_0000194035

Regions

Compositional bias101 – 1077Poly-Glu
Compositional bias115 – 15743Pro/Ser/Thr-rich
Compositional bias486 – 4894Poly-Ser

Amino acid modifications

Modified residue1261Phosphoserine Ref.5
Modified residue1271Phosphothreonine Ref.5 Ref.8
Modified residue1301Phosphothreonine Ref.5 Ref.8
Modified residue1411Phosphoserine Ref.5 Ref.7 Ref.8 Ref.10
Modified residue1471Phosphoserine Ref.5 Ref.8
Modified residue1521Phosphoserine Ref.7 Ref.8 Ref.10

Natural variations

Natural variant5831G → R.
Corresponds to variant rs487989 [ dbSNP | Ensembl ].
VAR_033896
Natural variant5881S → N.
Corresponds to variant rs7123885 [ dbSNP | Ensembl ].
VAR_033897

Experimental info

Sequence conflict383 – 3842DA → ES in AAA16459. Ref.1

Secondary structure

........... 598
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14181 [UniParc].

Last modified February 7, 2006. Version 2.
Checksum: F5CBD7E022ADDDBF

FASTA59865,948
        10         20         30         40         50         60 
MSASAQQLAE ELQIFGLDCE EALIEKLVEL CVQYGQNEEG MVGELIAFCT STHKVGLTSE 

        70         80         90        100        110        120 
ILNSFEHEFL SKRLSKARHS TCKDSGHAGA RDIVSIQELI EVEEEEEILL NSYTTPSKGS 

       130        140        150        160        170        180 
QKRAISTPET PLTKRSVSTR SPHQLLSPSS FSPSATPSQK YNSRSNRGEV VTSFGLAQGV 

       190        200        210        220        230        240 
SWSGRGGAGN ISLKVLGCPE ALTGSYKSMF QKLPDIREVL TCKIEELGSE LKEHYKIEAF 

       250        260        270        280        290        300 
TPLLAPAQEP VTLLGQIGCD SNGKLNNKSV ILEGDREHSS GAQIPVDLSE LKEYSLFPGQ 

       310        320        330        340        350        360 
VVIMEGINTT GRKLVATKLY EGVPLPFYQP TEEDADFEQS MVLVACGPYT TSDSITYDPL 

       370        380        390        400        410        420 
LDLIAVINHD RPDVCILFGP FLDAKHEQVE NCLLTSPFED IFKQCLRTII EGTRSSGSHL 

       430        440        450        460        470        480 
VFVPSLRDVH HEPVYPQPPF SYSDLSREDK KQVQFVSEPC SLSINGVIFG LTSTDLLFHL 

       490        500        510        520        530        540 
GAEEISSSSG TSDRFSRILK HILTQRSYYP LYPPQEDMAI DYESFYVYAQ LPVTPDVLII 

       550        560        570        580        590 
PSELRYFVKD VLGCVCVNPG RLTKGQVGGT FARLYLRRPA ADGAERQSPC IAVQVVRI 

« Hide

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"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].
[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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L24559 mRNA. Translation: AAA16459.1.
CR456737 mRNA. Translation: CAG33018.1.
BC002990 mRNA. Translation: AAH02990.1.
BC001347 mRNA. Translation: AAH01347.1.
CCDSCCDS8098.1.
PIRS39621.
RefSeqNP_002680.2. NM_002689.2.
UniGeneHs.201897.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KEBNMR-A1-78[»]
4E2IX-ray5.001/2/3/4/5/6/7/8/9/U/W1-78[»]
ProteinModelPortalQ14181.
SMRQ14181. Positions 1-78.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117176. 41 interactions.
IntActQ14181. 31 interactions.
MINTMINT-1382407.
STRING9606.ENSP00000265465.

Chemistry

DrugBankDB00851. Dacarbazine.

PTM databases

PhosphoSiteQ14181.

Polymorphism databases

DMDM90110415.

Proteomic databases

MaxQBQ14181.
PaxDbQ14181.
PeptideAtlasQ14181.
PRIDEQ14181.

Protocols and materials databases

DNASU23649.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265465; ENSP00000265465; ENSG00000014138.
GeneID23649.
KEGGhsa:23649.
UCSCuc001odj.3. human.

Organism-specific databases

CTD23649.
GeneCardsGC11P065029.
HGNCHGNC:30073. POLA2.
HPAHPA037570.
neXtProtNX_Q14181.
PharmGKBPA411.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5214.
HOGENOMHOG000007382.
HOVERGENHBG055628.
InParanoidQ14181.
KOK02321.
OMADREHSSG.
OrthoDBEOG7GXPB7.
PhylomeDBQ14181.
TreeFamTF314249.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressQ14181.
BgeeQ14181.
CleanExHS_POLA2.
GenevestigatorQ14181.

Family and domain databases

InterProIPR007185. DNA_pol_alpha/epsilon_bsu.
IPR016722. DNA_pol_alpha_bsu.
IPR013627. Pol_alpha_B_N.
[Graphical view]
PfamPF04042. DNA_pol_E_B. 1 hit.
PF08418. Pol_alpha_B_N. 1 hit.
[Graphical view]
PIRSFPIRSF018300. DNA_pol_alph_2. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPOLA2. human.
EvolutionaryTraceQ14181.
GeneWikiPOLA2.
GenomeRNAi23649.
NextBio46481.
PROQ14181.

Entry information

Entry nameDPOA2_HUMAN
AccessionPrimary (citable) accession number: Q14181
Secondary accession number(s): Q9BPV3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 7, 2006
Last modified: July 9, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM