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Q15054

- DPOD3_HUMAN

UniProt

Q15054 - DPOD3_HUMAN

Protein

DNA polymerase delta subunit 3

Gene

POLD3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (26 Sep 2001)
      Previous versions | rss
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    Functioni

    Required for optimal DNA polymerase delta activity.3 Publications

    GO - Molecular functioni

    1. DNA-directed DNA polymerase activity Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. base-excision repair Source: Reactome
    2. DNA repair Source: Reactome
    3. DNA strand elongation involved in DNA replication Source: Reactome
    4. DNA synthesis involved in DNA repair Source: UniProtKB
    5. mismatch repair Source: UniProtKB
    6. mitotic cell cycle Source: Reactome
    7. nucleotide-excision repair Source: Reactome
    8. nucleotide-excision repair, DNA gap filling Source: UniProtKB
    9. telomere maintenance Source: Reactome
    10. telomere maintenance via recombination Source: Reactome
    11. telomere maintenance via semi-conservative replication Source: Reactome
    12. 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 3
    Alternative name(s):
    DNA polymerase delta subunit p66
    Gene namesi
    Name:POLD3
    Synonyms:KIAA0039
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:20932. POLD3.

    Subcellular locationi

    GO - Cellular componenti

    1. delta DNA polymerase complex Source: UniProtKB
    2. mitochondrion Source: HPA
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134868595.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 466465DNA polymerase delta subunit 3PRO_0000186047Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei307 – 3071Phosphoserine6 Publications
    Modified residuei407 – 4071Phosphoserine1 Publication
    Modified residuei409 – 4091Phosphoserine1 Publication
    Modified residuei411 – 4111Phosphothreonine1 Publication
    Modified residuei413 – 4131Phosphoserine1 Publication
    Modified residuei458 – 4581Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15054.
    PaxDbiQ15054.
    PeptideAtlasiQ15054.
    PRIDEiQ15054.

    PTM databases

    PhosphoSiteiQ15054.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15054.
    BgeeiQ15054.
    GenevestigatoriQ15054.

    Organism-specific databases

    HPAiHPA039627.

    Interactioni

    Subunit structurei

    Heterotetramer composed of subunits of 125 kDa, 50 kDa, 66 kDa and 12 kDa. Interacts with POLD2. Interacts with PCNA.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PCNAP120044EBI-864956,EBI-358311
    POLD2P490055EBI-864956,EBI-372354

    Protein-protein interaction databases

    BioGridi115940. 23 interactions.
    DIPiDIP-35772N.
    IntActiQ15054. 6 interactions.
    MINTiMINT-2789689.
    STRINGi9606.ENSP00000263681.

    Structurei

    Secondary structure

    1
    466
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1412
    Turni15 – 173
    Helixi23 – 308
    Helixi34 – 5219
    Beta strandi58 – 8124
    Turni82 – 843
    Helixi85 – 917
    Beta strandi93 – 10614
    Beta strandi109 – 1113
    Helixi113 – 12513
    Helixi129 – 1313
    Beta strandi134 – 1363
    Helixi459 – 4613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U76X-ray2.60B/D/F452-466[»]
    3E0JX-ray3.00B/D/F/H1-144[»]
    ProteinModelPortaliQ15054.
    SMRiQ15054. Positions 2-144.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15054.

    Family & Domainsi

    Phylogenomic databases

    eggNOGiNOG83700.
    HOGENOMiHOG000008055.
    HOVERGENiHBG051397.
    InParanoidiQ15054.
    KOiK03504.
    OMAiVMSNFFG.
    PhylomeDBiQ15054.
    TreeFamiTF103006.

    Family and domain databases

    InterProiIPR019038. DNA_polymerase_subunit_Cdc27.
    [Graphical view]
    PfamiPF09507. CDC27. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15054-1) [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

    MADQLYLENI DEFVTDQNKI VTYKWLSYTL GVHVNQAKQM LYDYVERKRK    50
    ENSGAQLHVT YLVSGSLIQN GHSCHKVAVV REDKLEAVKS KLAVTASIHV 100
    YSIQKAMLKD SGPLFNTDYD ILKSNLQNCS KFSAIQCAAA VPRAPAESSS 150
    SSKKFEQSHL HMSSETQANN ELTTNGHGPP ASKQVSQQPK GIMGMFASKA 200
    AAKTQETNKE TKTEAKEVTN ASAAGNKAPG KGNMMSNFFG KAAMNKFKVN 250
    LDSEQAVKEE KIVEQPTVSV TEPKLATPAG LKKSSKKAEP VKVLQKEKKR 300
    GKRVALSDDE TKETENMRKK RRRIKLPESD SSEDEVFPDS PGAYEAESPS 350
    PPPPPSPPLE PVPKTEPEPP SVKSSSGENK RKRKRVLKSK TYLDGEGCIV 400
    TEKVYESESC TDSEEELNMK TSSVHRPPAM TVKKEPREER KGPKKGTAAL 450
    GKANRQVSIT GFFQRK 466
    Length:466
    Mass (Da):51,400
    Last modified:September 26, 2001 - v2
    Checksum:iE9625E0188725F45
    GO
    Isoform 2 (identifier: Q15054-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-39: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:427
    Mass (Da):46,801
    Checksum:i29070FF3F00F0BCB
    GO
    Isoform 3 (identifier: Q15054-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-106: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:360
    Mass (Da):39,320
    Checksum:i70ACBAD78175C9BC
    GO

    Sequence cautioni

    The sequence BAA05039.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti194 – 1941G → V Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
    VAR_064745
    Natural varianti195 – 1951M → L Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
    VAR_064746

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 106106Missing in isoform 3. 1 PublicationVSP_054149Add
    BLAST
    Alternative sequencei1 – 3939Missing in isoform 2. 1 PublicationVSP_054150Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26018 mRNA. Translation: BAA05039.1. Different initiation.
    AK316301 mRNA. Translation: BAH14672.1.
    AP001104 Genomic DNA. No translation available.
    AP001324 Genomic DNA. No translation available.
    AP001372 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74942.1.
    BC108908 mRNA. Translation: AAI08909.1.
    BC108909 mRNA. Translation: AAI08910.1.
    CCDSiCCDS8233.1. [Q15054-1]
    RefSeqiNP_006582.1. NM_006591.2. [Q15054-1]
    UniGeneiHs.82502.

    Genome annotation databases

    EnsembliENST00000263681; ENSP00000263681; ENSG00000077514. [Q15054-1]
    ENST00000527458; ENSP00000432951; ENSG00000077514. [Q15054-2]
    ENST00000532497; ENSP00000436018; ENSG00000077514. [Q15054-3]
    GeneIDi10714.
    KEGGihsa:10714.
    UCSCiuc001ovf.2. human. [Q15054-1]

    Polymorphism databases

    DMDMi17375506.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26018 mRNA. Translation: BAA05039.1 . Different initiation.
    AK316301 mRNA. Translation: BAH14672.1 .
    AP001104 Genomic DNA. No translation available.
    AP001324 Genomic DNA. No translation available.
    AP001372 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74942.1 .
    BC108908 mRNA. Translation: AAI08909.1 .
    BC108909 mRNA. Translation: AAI08910.1 .
    CCDSi CCDS8233.1. [Q15054-1 ]
    RefSeqi NP_006582.1. NM_006591.2. [Q15054-1 ]
    UniGenei Hs.82502.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U76 X-ray 2.60 B/D/F 452-466 [» ]
    3E0J X-ray 3.00 B/D/F/H 1-144 [» ]
    ProteinModelPortali Q15054.
    SMRi Q15054. Positions 2-144.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115940. 23 interactions.
    DIPi DIP-35772N.
    IntActi Q15054. 6 interactions.
    MINTi MINT-2789689.
    STRINGi 9606.ENSP00000263681.

    PTM databases

    PhosphoSitei Q15054.

    Polymorphism databases

    DMDMi 17375506.

    Proteomic databases

    MaxQBi Q15054.
    PaxDbi Q15054.
    PeptideAtlasi Q15054.
    PRIDEi Q15054.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263681 ; ENSP00000263681 ; ENSG00000077514 . [Q15054-1 ]
    ENST00000527458 ; ENSP00000432951 ; ENSG00000077514 . [Q15054-2 ]
    ENST00000532497 ; ENSP00000436018 ; ENSG00000077514 . [Q15054-3 ]
    GeneIDi 10714.
    KEGGi hsa:10714.
    UCSCi uc001ovf.2. human. [Q15054-1 ]

    Organism-specific databases

    CTDi 10714.
    GeneCardsi GC11P074207.
    HGNCi HGNC:20932. POLD3.
    HPAi HPA039627.
    MIMi 611415. gene.
    neXtProti NX_Q15054.
    PharmGKBi PA134868595.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG83700.
    HOGENOMi HOG000008055.
    HOVERGENi HBG051397.
    InParanoidi Q15054.
    KOi K03504.
    OMAi VMSNFFG.
    PhylomeDBi Q15054.
    TreeFami TF103006.

    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

    EvolutionaryTracei Q15054.
    GeneWikii POLD3.
    GenomeRNAii 10714.
    NextBioi 40675.
    PROi Q15054.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15054.
    Bgeei Q15054.
    Genevestigatori Q15054.

    Family and domain databases

    InterProi IPR019038. DNA_polymerase_subunit_Cdc27.
    [Graphical view ]
    Pfami PF09507. CDC27. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
      Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
      DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    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 1).
      Tissue: Placenta.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 2 AND 3).
    6. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-19 AND 110-123, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    7. "Isolation and identification of the third subunit of mammalian DNA polymerase delta by PCNA-affinity chromatography of mouse FM3A cell extracts."
      Hughes P., Tratner I., Ducoux M., Piard K., Baldacci G.
      Nucleic Acids Res. 27:2108-2114(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Evidence that DNA polymerase delta isolated by immunoaffinity chromatography exhibits high-molecular weight characteristics and is associated with the KIAA0039 protein and RPA."
      Mo J.-Y., Liu L., Leon A., Mazloum N., Lee M.Y.W.T.
      Biochemistry 39:7245-7254(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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: FUNCTION, INTERACTION WITH PCNA.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-407; SER-409; THR-411; SER-413 AND SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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].
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: VARIANTS VAL-194 AND LEU-195.

    Entry informationi

    Entry nameiDPOD3_HUMAN
    AccessioniPrimary (citable) accession number: Q15054
    Secondary accession number(s): B7ZAI6, Q32MZ9, Q32N00
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 125 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, Direct protein sequencing, 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. 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

    External Data

    Dasty 3