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P49005

- DPOD2_HUMAN

UniProt

P49005 - DPOD2_HUMAN

Protein

DNA polymerase delta subunit 2

Gene

POLD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    The function of the small subunit is not yet clear.

    Catalytic activityi

    Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. DNA-directed DNA polymerase activity Source: UniProtKB-KW
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. base-excision repair Source: Reactome
    2. DNA repair Source: Reactome
    3. DNA replication Source: ProtInc
    4. DNA strand elongation involved in DNA replication Source: Reactome
    5. mitotic cell cycle Source: Reactome
    6. nucleotide-excision repair Source: Reactome
    7. nucleotide-excision repair, DNA gap filling Source: Reactome
    8. telomere maintenance Source: Reactome
    9. telomere maintenance via recombination Source: Reactome
    10. telomere maintenance via semi-conservative replication Source: Reactome
    11. transcription-coupled nucleotide-excision repair Source: Reactome

    Keywords - Molecular functioni

    DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA replication

    Enzyme and pathway databases

    ReactomeiREACT_1128. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
    REACT_1385. Processive synthesis on the lagging strand.
    REACT_1792. Polymerase switching.
    REACT_1838. Leading Strand Synthesis.
    REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
    REACT_2192. Removal of DNA patch containing abasic residue.
    REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
    REACT_70. Removal of the Flap Intermediate.
    REACT_7961. Telomere C-strand (Lagging Strand) Synthesis.
    REACT_7987. Polymerase switching on the C-strand of the telomere.
    REACT_7999. Removal of the Flap Intermediate from the C-strand.
    REACT_8027. Processive synthesis on the C-strand of the telomere.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA polymerase delta subunit 2 (EC:2.7.7.7)
    Alternative name(s):
    DNA polymerase delta subunit p50
    Gene namesi
    Name:POLD2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:9176. POLD2.

    Subcellular locationi

    GO - Cellular componenti

    1. delta DNA polymerase complex Source: Ensembl
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33497.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 469469DNA polymerase delta subunit 2PRO_0000096166Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei15 – 151Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP49005.
    PaxDbiP49005.
    PeptideAtlasiP49005.
    PRIDEiP49005.

    PTM databases

    PhosphoSiteiP49005.

    Expressioni

    Gene expression databases

    ArrayExpressiP49005.
    BgeeiP49005.
    CleanExiHS_POLD2.
    GenevestigatoriP49005.

    Organism-specific databases

    HPAiHPA026745.

    Interactioni

    Subunit structurei

    Heterotetramer composed of subunits of 125 kDa, 50 kDa, 66 kDa and 12 kDa. Interacts with KCTD10 By similarity. Interacts with KCTD13/POLDIP1, POLDIP2 and POLDIP3. Interacts with WRNIP1. Interacts with POLD4.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    POLD1P283409EBI-372354,EBI-716569
    POLD3Q150545EBI-372354,EBI-864956
    POLD4Q9HCU83EBI-372354,EBI-864968
    WRNIP1Q96S552EBI-372354,EBI-2513471

    Protein-protein interaction databases

    BioGridi111421. 16 interactions.
    IntActiP49005. 14 interactions.
    STRINGi9606.ENSP00000379148.

    Structurei

    Secondary structure

    1
    469
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 76
    Beta strandi13 – 164
    Beta strandi32 – 343
    Helixi37 – 393
    Helixi55 – 7218
    Beta strandi82 – 843
    Beta strandi91 – 10010
    Beta strandi132 – 1365
    Beta strandi141 – 1477
    Turni150 – 1523
    Beta strandi158 – 1658
    Beta strandi169 – 1779
    Beta strandi195 – 1995
    Helixi209 – 22315
    Helixi229 – 2357
    Beta strandi238 – 2458
    Helixi265 – 28723
    Beta strandi292 – 2954
    Beta strandi300 – 3023
    Beta strandi304 – 3074
    Helixi317 – 3204
    Beta strandi325 – 3273
    Beta strandi330 – 3367
    Beta strandi339 – 3435
    Helixi347 – 3559
    Helixi361 – 37010
    Beta strandi400 – 40910
    Beta strandi411 – 4166
    Beta strandi422 – 4298
    Helixi431 – 4344
    Beta strandi436 – 4416
    Turni442 – 4454
    Beta strandi449 – 4546
    Turni460 – 4623

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3E0JX-ray3.00A/C/E/G1-469[»]
    ProteinModelPortaliP49005.
    SMRiP49005. Positions 1-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49005.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1311.
    HOGENOMiHOG000189057.
    HOVERGENiHBG051396.
    InParanoidiP49005.
    KOiK02328.
    OMAiATRLIQM.
    OrthoDBiEOG7RZ5PQ.
    PhylomeDBiP49005.
    TreeFamiTF101073.

    Family and domain databases

    InterProiIPR007185. DNA_pol_alpha/epsilon_bsu.
    IPR024826. DNA_pol_delta/II_ssu.
    [Graphical view]
    PANTHERiPTHR10416. PTHR10416. 1 hit.
    PfamiPF04042. DNA_pol_E_B. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P49005-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFSEQAAQRA HTLLSPPSAN NATFARVPVA TYTNSSQPFR LGERSFSRQY    50
    AHIYATRLIQ MRPFLENRAQ QHWGSGVGVK KLCELQPEEK CCVVGTLFKA 100
    MPLQPSILRE VSEEHNLLPQ PPRSKYIHPD DELVLEDELQ RIKLKGTIDV 150
    SKLVTGTVLA VFGSVRDDGK FLVEDYCFAD LAPQKPAPPL DTDRFVLLVS 200
    GLGLGGGGGE SLLGTQLLVD VVTGQLGDEG EQCSAAHVSR VILAGNLLSH 250
    STQSRDSINK AKYLTKKTQA ASVEAVKMLD EILLQLSASV PVDVMPGEFD 300
    PTNYTLPQQP LHPCMFPLAT AYSTLQLVTN PYQATIDGVR FLGTSGQNVS 350
    DIFRYSSMED HLEILEWTLR VRHISPTAPD TLGCYPFYKT DPFIFPECPH 400
    VYFCGNTPSF GSKIIRGPED QTVLLVTVPD FSATQTACLV NLRSLACQPI 450
    SFSGFGAEDD DLGGLGLGP 469
    Length:469
    Mass (Da):51,289
    Last modified:February 1, 1996 - v1
    Checksum:i389EF730999755AC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti271 – 2711A → T in BAG35221. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti303 – 3031N → S.1 Publication
    Corresponds to variant rs3087366 [ dbSNP | Ensembl ].
    VAR_014885

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U21090 mRNA. Translation: AAC50216.1.
    AF239710 Genomic DNA. Translation: AAG09763.1.
    AY116646 Genomic DNA. Translation: AAM51148.1.
    AK292347 mRNA. Translation: BAF85036.1.
    AK312294 mRNA. Translation: BAG35221.1.
    CH236960 Genomic DNA. Translation: EAL23767.1.
    CH471128 Genomic DNA. Translation: EAW61118.1.
    BC000459 mRNA. Translation: AAH00459.1.
    CCDSiCCDS5477.1.
    PIRiI38950.
    RefSeqiNP_001120690.1. NM_001127218.2.
    NP_001243808.1. NM_001256879.1.
    NP_006221.2. NM_006230.3.
    UniGeneiHs.306791.
    Hs.740138.

    Genome annotation databases

    EnsembliENST00000406581; ENSP00000386105; ENSG00000106628.
    ENST00000452185; ENSP00000395231; ENSG00000106628.
    GeneIDi5425.
    KEGGihsa:5425.
    UCSCiuc003tkf.5. human.

    Polymorphism databases

    DMDMi1352307.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U21090 mRNA. Translation: AAC50216.1 .
    AF239710 Genomic DNA. Translation: AAG09763.1 .
    AY116646 Genomic DNA. Translation: AAM51148.1 .
    AK292347 mRNA. Translation: BAF85036.1 .
    AK312294 mRNA. Translation: BAG35221.1 .
    CH236960 Genomic DNA. Translation: EAL23767.1 .
    CH471128 Genomic DNA. Translation: EAW61118.1 .
    BC000459 mRNA. Translation: AAH00459.1 .
    CCDSi CCDS5477.1.
    PIRi I38950.
    RefSeqi NP_001120690.1. NM_001127218.2.
    NP_001243808.1. NM_001256879.1.
    NP_006221.2. NM_006230.3.
    UniGenei Hs.306791.
    Hs.740138.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3E0J X-ray 3.00 A/C/E/G 1-469 [» ]
    ProteinModelPortali P49005.
    SMRi P49005. Positions 1-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111421. 16 interactions.
    IntActi P49005. 14 interactions.
    STRINGi 9606.ENSP00000379148.

    PTM databases

    PhosphoSitei P49005.

    Polymorphism databases

    DMDMi 1352307.

    Proteomic databases

    MaxQBi P49005.
    PaxDbi P49005.
    PeptideAtlasi P49005.
    PRIDEi P49005.

    Protocols and materials databases

    DNASUi 5425.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000406581 ; ENSP00000386105 ; ENSG00000106628 .
    ENST00000452185 ; ENSP00000395231 ; ENSG00000106628 .
    GeneIDi 5425.
    KEGGi hsa:5425.
    UCSCi uc003tkf.5. human.

    Organism-specific databases

    CTDi 5425.
    GeneCardsi GC07M044120.
    HGNCi HGNC:9176. POLD2.
    HPAi HPA026745.
    MIMi 600815. gene.
    neXtProti NX_P49005.
    PharmGKBi PA33497.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1311.
    HOGENOMi HOG000189057.
    HOVERGENi HBG051396.
    InParanoidi P49005.
    KOi K02328.
    OMAi ATRLIQM.
    OrthoDBi EOG7RZ5PQ.
    PhylomeDBi P49005.
    TreeFami TF101073.

    Enzyme and pathway databases

    Reactomei REACT_1128. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
    REACT_1385. Processive synthesis on the lagging strand.
    REACT_1792. Polymerase switching.
    REACT_1838. Leading Strand Synthesis.
    REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
    REACT_2192. Removal of DNA patch containing abasic residue.
    REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
    REACT_70. Removal of the Flap Intermediate.
    REACT_7961. Telomere C-strand (Lagging Strand) Synthesis.
    REACT_7987. Polymerase switching on the C-strand of the telomere.
    REACT_7999. Removal of the Flap Intermediate from the C-strand.
    REACT_8027. Processive synthesis on the C-strand of the telomere.

    Miscellaneous databases

    ChiTaRSi POLD2. human.
    EvolutionaryTracei P49005.
    GeneWikii POLD2.
    GenomeRNAii 5425.
    NextBioi 20989.
    PROi P49005.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49005.
    Bgeei P49005.
    CleanExi HS_POLD2.
    Genevestigatori P49005.

    Family and domain databases

    InterProi IPR007185. DNA_pol_alpha/epsilon_bsu.
    IPR024826. DNA_pol_delta/II_ssu.
    [Graphical view ]
    PANTHERi PTHR10416. PTHR10416. 1 hit.
    Pfami PF04042. DNA_pol_E_B. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the cDNAs for the small subunits of bovine and human DNA polymerase delta and chromosomal location of the human gene (POLD2)."
      Zhang J., Tan C.-K., McMullen B., Downey K.M., So A.G.
      Genomics 29:179-186(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Characterization of the 5'-flanking region of the gene encoding the 50 kDa subunit of human DNA polymerase delta."
      Perez A., Leon A., Lee M.Y.W.T.
      Biochim. Biophys. Acta 1493:231-236(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. NIEHS SNPs program
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-303.
    4. "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].
      Tissue: Cerebellum.
    5. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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.
    8. "A tumor necrosis factor alpha- and interleukin 6-inducible protein that interacts with the small subunit of DNA polymerase delta and proliferating cell nuclear antigen."
      He H., Tan C.-K., Downey K.M., So A.G.
      Proc. Natl. Acad. Sci. U.S.A. 98:11979-11984(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KCTD13/POLDIP1.
    9. "Identification of a novel protein, PDIP38, that interacts with the p50 subunit of DNA polymerase delta and proliferating cell nuclear antigen."
      Liu L., Rodriguez-Belmonte E.M., Mazloum N., Xie B., Lee M.Y.W.T.
      J. Biol. Chem. 278:10041-10047(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POLDIP2 AND POLDIP3.
    10. "Human Werner helicase interacting protein 1 (WRNIP1) functions as a novel modulator for DNA polymerase delta."
      Tsurimoto T., Shinozaki A., Yano M., Seki M., Enomoto T.
      Genes Cells 10:13-22(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WRNIP1.
    11. "Functional roles of p12, the fourth subunit of human DNA polymerase delta."
      Li H., Xie B., Zhou Y., Rahmeh A., Trusa S., Zhang S., Gao Y., Lee E.Y., Lee M.Y.
      J. Biol. Chem. 281:14748-14755(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POLD4.
    12. "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 SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDPOD2_HUMAN
    AccessioniPrimary (citable) accession number: P49005
    Secondary accession number(s): A4D2J4, B2R5S4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 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 7
      Human chromosome 7: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3