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Protein

DNA polymerase alpha subunit B

Gene

POLA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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: GO_Central

GO - Biological processi

  1. DNA replication Source: UniProtKB
  2. DNA replication initiation Source: GO_Central
  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 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:30073. POLA2.

Subcellular locationi

GO - Cellular componenti

  1. alpha DNA polymerase:primase complex Source: GO_Central
  2. cytoplasm Source: HPA
  3. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA411.

Chemistry

DrugBankiDB00851. Dacarbazine.

Polymorphism and mutation databases

BioMutaiPOLA2.
DMDMi90110415.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 598598DNA polymerase alpha subunit BPRO_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

BgeeiQ14181.
CleanExiHS_POLA2.
ExpressionAtlasiQ14181. baseline and differential.
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. 46 interactions.
IntActiQ14181. 31 interactions.
MINTiMINT-1382407.
STRINGi9606.ENSP00000265465.

Structurei

Secondary structure

1
598
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1511Combined sources
Helixi21 – 3414Combined sources
Helixi38 – 5215Combined sources
Helixi59 – 6810Combined sources
Helixi70 – 734Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14181.

Family & Domainsi

Compositional bias

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

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5214.
GeneTreeiENSGT00390000016784.
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.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14181-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSASAQQLAE ELQIFGLDCE EALIEKLVEL CVQYGQNEEG MVGELIAFCT
60 70 80 90 100
STHKVGLTSE ILNSFEHEFL SKRLSKARHS TCKDSGHAGA RDIVSIQELI
110 120 130 140 150
EVEEEEEILL NSYTTPSKGS QKRAISTPET PLTKRSVSTR SPHQLLSPSS
160 170 180 190 200
FSPSATPSQK YNSRSNRGEV VTSFGLAQGV SWSGRGGAGN ISLKVLGCPE
210 220 230 240 250
ALTGSYKSMF QKLPDIREVL TCKIEELGSE LKEHYKIEAF TPLLAPAQEP
260 270 280 290 300
VTLLGQIGCD SNGKLNNKSV ILEGDREHSS GAQIPVDLSE LKEYSLFPGQ
310 320 330 340 350
VVIMEGINTT GRKLVATKLY EGVPLPFYQP TEEDADFEQS MVLVACGPYT
360 370 380 390 400
TSDSITYDPL LDLIAVINHD RPDVCILFGP FLDAKHEQVE NCLLTSPFED
410 420 430 440 450
IFKQCLRTII EGTRSSGSHL VFVPSLRDVH HEPVYPQPPF SYSDLSREDK
460 470 480 490 500
KQVQFVSEPC SLSINGVIFG LTSTDLLFHL GAEEISSSSG TSDRFSRILK
510 520 530 540 550
HILTQRSYYP LYPPQEDMAI DYESFYVYAQ LPVTPDVLII PSELRYFVKD
560 570 580 590
VLGCVCVNPG RLTKGQVGGT FARLYLRRPA ADGAERQSPC IAVQVVRI
Length:598
Mass (Da):65,948
Last modified:February 7, 2006 - v2
Checksum:iF5CBD7E022ADDDBF
GO
Isoform 2 (identifier: Q14181-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-208: Missing.
     550-598: DVLGCVCVNPGRLTKGQVGGTFARLYLRRPAADGAERQSPCIAVQVVRI → VGLNSAFSQKHQNPVFDFPF

Note: No experimental confirmation available.

Show »
Length:361
Mass (Da):40,579
Checksum:i53B1AE982B92ED81
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti383 – 3842DA → ES in AAA16459 (PubMed:8223465).Curated

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 208208Missing in isoform 2. 1 PublicationVSP_056608Add
BLAST
Alternative sequencei550 – 59849DVLGC…QVVRI → VGLNSAFSQKHQNPVFDFPF in isoform 2. 1 PublicationVSP_056609Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24559 mRNA. Translation: AAA16459.1.
AK297842 mRNA. Translation: BAG60176.1.
CR456737 mRNA. Translation: CAG33018.1.
AP000944 Genomic DNA. No translation available.
BC002990 mRNA. Translation: AAH02990.1.
BC001347 mRNA. Translation: AAH01347.1.
CCDSiCCDS8098.1. [Q14181-1]
PIRiS39621.
RefSeqiNP_002680.2. NM_002689.3. [Q14181-1]
UniGeneiHs.201897.

Genome annotation databases

EnsembliENST00000265465; ENSP00000265465; ENSG00000014138. [Q14181-1]
GeneIDi23649.
KEGGihsa:23649.
UCSCiuc001odj.3. human. [Q14181-1]

Polymorphism and mutation databases

BioMutaiPOLA2.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24559 mRNA. Translation: AAA16459.1.
AK297842 mRNA. Translation: BAG60176.1.
CR456737 mRNA. Translation: CAG33018.1.
AP000944 Genomic DNA. No translation available.
BC002990 mRNA. Translation: AAH02990.1.
BC001347 mRNA. Translation: AAH01347.1.
CCDSiCCDS8098.1. [Q14181-1]
PIRiS39621.
RefSeqiNP_002680.2. NM_002689.3. [Q14181-1]
UniGeneiHs.201897.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117176. 46 interactions.
IntActiQ14181. 31 interactions.
MINTiMINT-1382407.
STRINGi9606.ENSP00000265465.

Chemistry

DrugBankiDB00851. Dacarbazine.

PTM databases

PhosphoSiteiQ14181.

Polymorphism and mutation databases

BioMutaiPOLA2.
DMDMi90110415.

Proteomic databases

MaxQBiQ14181.
PaxDbiQ14181.
PeptideAtlasiQ14181.
PRIDEiQ14181.

Protocols and materials databases

DNASUi23649.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265465; ENSP00000265465; ENSG00000014138. [Q14181-1]
GeneIDi23649.
KEGGihsa:23649.
UCSCiuc001odj.3. human. [Q14181-1]

Organism-specific databases

CTDi23649.
GeneCardsiGC11P065029.
HGNCiHGNC:30073. POLA2.
HPAiHPA037570.
neXtProtiNX_Q14181.
PharmGKBiPA411.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5214.
GeneTreeiENSGT00390000016784.
HOGENOMiHOG000007382.
HOVERGENiHBG055628.
InParanoidiQ14181.
KOiK02321.
OMAiDREHSSG.
OrthoDBiEOG7GXPB7.
PhylomeDBiQ14181.
TreeFamiTF314249.

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.

Miscellaneous databases

ChiTaRSiPOLA2. human.
EvolutionaryTraceiQ14181.
GeneWikiiPOLA2.
GenomeRNAii23649.
NextBioi35473563.
PROiQ14181.

Gene expression databases

BgeeiQ14181.
CleanExiHS_POLA2.
ExpressionAtlasiQ14181. baseline and differential.
GenevestigatoriQ14181.

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. "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] (ISOFORM 1).
    Tissue: Cervix epithelium.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Heart.
  3. "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] (ISOFORM 1).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Lung.
  6. "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.
  7. 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.
  8. "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].
  9. "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.
  10. "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.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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): B4DNB4, Q9BPV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 7, 2006
Last modified: April 29, 2015
This is version 135 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

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 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.