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Q14181

- DPOA2_HUMAN

UniProt

Q14181 - DPOA2_HUMAN

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
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (07 Feb 2006)
      Previous versions | rss
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    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

    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

    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

    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 BPRO_0000194035Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei126 – 1261Phosphoserine2 Publications
    Modified residuei127 – 1271Phosphothreonine3 Publications
    Modified residuei130 – 1301Phosphothreonine3 Publications
    Modified residuei141 – 1411Phosphoserine5 Publications
    Modified residuei147 – 1471Phosphoserine3 Publications
    Modified residuei152 – 1521Phosphoserine4 Publications

    Post-translational modificationi

    Phosphorylated in a cell cycle-dependent manner, in G2/M phase.5 Publications

    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

    1
    598
    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.
    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.
    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. Align

    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

    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
    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:
    EMBL
    GenBank
    DDBJ
    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.
    PIRiS39621.
    RefSeqiNP_002680.2. NM_002689.2.
    UniGeneiHs.201897.

    Genome annotation databases

    EnsembliENST00000265465; ENSP00000265465; ENSG00000014138.
    ENST00000541089; ENSP00000443222; ENSG00000014138.
    GeneIDi23649.
    KEGGihsa:23649.
    UCSCiuc001odj.3. human.

    Polymorphism databases

    DMDMi90110415.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    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...
    MobiDBi 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 .
    ENST00000541089 ; ENSP00000443222 ; 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

    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: October 1, 2014
    This is version 129 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