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O75607

- NPM3_HUMAN

UniProt

O75607 - NPM3_HUMAN

Protein

Nucleoplasmin-3

Gene

NPM3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    May act as a chaperone.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. rRNA processing Source: Ensembl
    2. rRNA transcription Source: Ensembl

    Keywords - Molecular functioni

    Chaperone

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleoplasmin-3
    Gene namesi
    Name:NPM3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:7931. NPM3.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleolus Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31733.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed6 Publications
    Chaini2 – 178177Nucleoplasmin-3PRO_0000219489Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine6 Publications
    Modified residuei13 – 131Phosphoserine2 Publications
    Modified residuei16 – 161Phosphoserine1 Publication
    Modified residuei147 – 1471Phosphoserine1 Publication
    Modified residuei151 – 1511Phosphoserine1 Publication
    Modified residuei158 – 1581Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated.Curated

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO75607.
    PaxDbiO75607.
    PeptideAtlasiO75607.
    PRIDEiO75607.

    PTM databases

    PhosphoSiteiO75607.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    BgeeiO75607.
    CleanExiHS_NPM3.
    GenevestigatoriO75607.

    Organism-specific databases

    HPAiHPA036295.
    HPA036296.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    tatP046082EBI-721544,EBI-6164389From a different organism.

    Protein-protein interaction databases

    BioGridi115640. 13 interactions.
    IntActiO75607. 3 interactions.
    MINTiMINT-1426791.
    STRINGi9606.ENSP00000359128.

    Structurei

    3D structure databases

    ProteinModelPortaliO75607.
    SMRiO75607. Positions 37-137.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 109Ala-rich
    Compositional biasi145 – 16420Asp/Glu-rich (highly acidic)Add
    BLAST
    Compositional biasi148 – 1569Poly-Glu

    Sequence similaritiesi

    Belongs to the nucleoplasmin family.Curated

    Phylogenomic databases

    eggNOGiNOG87795.
    HOGENOMiHOG000030911.
    HOVERGENiHBG045601.
    InParanoidiO75607.
    KOiK11278.
    OMAiANLRLSC.
    OrthoDBiEOG79W97G.
    PhylomeDBiO75607.
    TreeFamiTF327704.

    Family and domain databases

    Gene3Di2.60.120.340. 1 hit.
    InterProiIPR004301. Nucleoplasmin.
    IPR024057. Nucleoplasmin_core_dom.
    [Graphical view]
    PANTHERiPTHR22747. PTHR22747. 1 hit.
    SUPFAMiSSF69203. SSF69203. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    O75607-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAGTAAALA FLSQESRTRA GGVGGLRVPA PVTMDSFFFG CELSGHTRSF    50
    TFKVEEEDDA EHVLALTMLC LTEGAKDECN VVEVVARNHD HQEIAVPVAN 100
    LKLSCQPMLS LDDFQLQPPV TFRLKSGSGP VRITGRHQIV TMSNDVSEEE 150
    SEEEEEDSDE EEVELCPILP AKKQGGRP 178
    Length:178
    Mass (Da):19,344
    Last modified:January 23, 2007 - v3
    Checksum:i8C899DE8C3CD61FA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 622EH → DD in AAD51496. 1 PublicationCurated
    Sequence conflicti83 – 831E → K in AAD51496. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161S → N.
    Corresponds to variant rs34376117 [ dbSNP | Ensembl ].
    VAR_050410
    Natural varianti80 – 801N → I.1 Publication
    Corresponds to variant rs2735420 [ dbSNP | Ensembl ].
    VAR_050411

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY049737 mRNA. Translation: AAL12172.1.
    AF081280 mRNA. Translation: AAC31609.1.
    AF079325 Genomic DNA. Translation: AAD51496.1.
    BC041067 mRNA. Translation: AAH41067.1.
    BC054868 mRNA. Translation: AAH54868.1.
    CCDSiCCDS7519.1.
    RefSeqiNP_008924.1. NM_006993.2.
    UniGeneiHs.90691.

    Genome annotation databases

    EnsembliENST00000370110; ENSP00000359128; ENSG00000107833.
    GeneIDi10360.
    KEGGihsa:10360.
    UCSCiuc001ktt.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY049737 mRNA. Translation: AAL12172.1 .
    AF081280 mRNA. Translation: AAC31609.1 .
    AF079325 Genomic DNA. Translation: AAD51496.1 .
    BC041067 mRNA. Translation: AAH41067.1 .
    BC054868 mRNA. Translation: AAH54868.1 .
    CCDSi CCDS7519.1.
    RefSeqi NP_008924.1. NM_006993.2.
    UniGenei Hs.90691.

    3D structure databases

    ProteinModelPortali O75607.
    SMRi O75607. Positions 37-137.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115640. 13 interactions.
    IntActi O75607. 3 interactions.
    MINTi MINT-1426791.
    STRINGi 9606.ENSP00000359128.

    PTM databases

    PhosphoSitei O75607.

    Proteomic databases

    MaxQBi O75607.
    PaxDbi O75607.
    PeptideAtlasi O75607.
    PRIDEi O75607.

    Protocols and materials databases

    DNASUi 10360.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370110 ; ENSP00000359128 ; ENSG00000107833 .
    GeneIDi 10360.
    KEGGi hsa:10360.
    UCSCi uc001ktt.3. human.

    Organism-specific databases

    CTDi 10360.
    GeneCardsi GC10M103532.
    HGNCi HGNC:7931. NPM3.
    HPAi HPA036295.
    HPA036296.
    MIMi 606456. gene.
    neXtProti NX_O75607.
    PharmGKBi PA31733.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG87795.
    HOGENOMi HOG000030911.
    HOVERGENi HBG045601.
    InParanoidi O75607.
    KOi K11278.
    OMAi ANLRLSC.
    OrthoDBi EOG79W97G.
    PhylomeDBi O75607.
    TreeFami TF327704.

    Miscellaneous databases

    GeneWikii NPM3.
    GenomeRNAii 10360.
    NextBioi 39273.
    PROi O75607.
    SOURCEi Search...

    Gene expression databases

    Bgeei O75607.
    CleanExi HS_NPM3.
    Genevestigatori O75607.

    Family and domain databases

    Gene3Di 2.60.120.340. 1 hit.
    InterProi IPR004301. Nucleoplasmin.
    IPR024057. Nucleoplasmin_core_dom.
    [Graphical view ]
    PANTHERi PTHR22747. PTHR22747. 1 hit.
    SUPFAMi SSF69203. SSF69203. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression and nuclear localization of human NPM3, a member of the nucleophosmin/nucleoplasmin family of nuclear chaperones."
      Shackleford G.M., Ganguly A., MacArthur C.A.
      BMC Genomics 2:8-8(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. Hu G.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Retinoic acid induces differential expression of FGF8 isoforms in LNCaP cells."
      Brondani V., Albrecht G., Hamy F.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-80.
    4. "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: Skin.
    5. Bienvenut W.V.
      Submitted (JUL-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-17, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147; SER-151 AND SER-158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNPM3_HUMAN
    AccessioniPrimary (citable) accession number: O75607
    Secondary accession number(s): Q9UNY6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 116 of the entry and version 3 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3