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Q3T160

- NPM_BOVIN

UniProt

Q3T160 - NPM_BOVIN

Protein

Nucleophosmin

Gene

NPM1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (11 Oct 2005)
      Previous versions | rss
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    Functioni

    Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication By similarity. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei55 – 551Interaction between pentamersBy similarity
    Sitei80 – 801Interaction between pentamersBy similarity

    GO - Molecular functioni

    1. protein kinase inhibitor activity Source: UniProtKB
    2. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. DNA repair Source: UniProtKB
    2. negative regulation of apoptotic process Source: UniProtKB
    3. negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
    4. positive regulation of translation Source: UniProtKB
    5. regulation of centriole replication Source: UniProtKB
    6. regulation of eIF2 alpha phosphorylation by dsRNA Source: UniProtKB
    7. regulation of endodeoxyribonuclease activity Source: UniProtKB
    8. regulation of endoribonuclease activity Source: UniProtKB

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleophosmin
    Short name:
    NPM
    Gene namesi
    Name:NPM1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    Nucleusnucleolus. Nucleusnucleoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
    Note: Generally nucleolar, but is translocated to the nucleoplasm in case of serum starvation or treatment with anticancer drugs. Colocalizes with the methylated form of RPS10 in the granular component (GC) region of the nucleolus. Colocalized with nucleolin and APEX1 in nucleoli. NEK2 is required for its localization to the centrosome during mitosis. Interacts with CENPW By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. microtubule organizing center Source: UniProtKB-SubCell
    3. nucleolus Source: UniProtKB-SubCell
    4. nucleoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 294294NucleophosminPRO_0000253598Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei4 – 41Phosphoserine; by PLK1 and PLK2By similarity
    Modified residuei10 – 101PhosphoserineBy similarity
    Modified residuei32 – 321N6-acetyllysineBy similarity
    Modified residuei70 – 701PhosphoserineBy similarity
    Modified residuei75 – 751PhosphothreonineBy similarity
    Modified residuei95 – 951PhosphothreonineBy similarity
    Modified residuei125 – 1251Phosphoserine; by CDK2By similarity
    Modified residuei137 – 1371PhosphoserineBy similarity
    Modified residuei139 – 1391PhosphoserineBy similarity
    Modified residuei150 – 1501N6-acetyllysineBy similarity
    Modified residuei154 – 1541N6-acetyllysineBy similarity
    Modified residuei200 – 2001Phosphothreonine; by CDK1 and CDK2By similarity
    Modified residuei213 – 2131N6-acetyllysineBy similarity
    Modified residuei219 – 2191Phosphothreonine; by CDK1By similarity
    Modified residuei227 – 2271PhosphoserineBy similarity
    Modified residuei229 – 2291N6-acetyllysineBy similarity
    Modified residuei230 – 2301N6-acetyllysine; alternateBy similarity
    Cross-linki230 – 230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
    Modified residuei234 – 2341PhosphothreonineBy similarity
    Modified residuei237 – 2371PhosphothreonineBy similarity
    Modified residuei242 – 2421PhosphoserineBy similarity
    Modified residuei243 – 2431PhosphoserineBy similarity
    Modified residuei250 – 2501N6-acetyllysineBy similarity
    Modified residuei254 – 2541PhosphoserineBy similarity
    Modified residuei257 – 2571N6-acetyllysineBy similarity
    Modified residuei260 – 2601PhosphoserineBy similarity
    Cross-linki263 – 263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei267 – 2671N6-acetyllysineBy similarity
    Modified residuei273 – 2731N6-acetyllysineBy similarity
    Modified residuei279 – 2791PhosphothreonineBy similarity
    Modified residuei292 – 2921N6-acetyllysineBy similarity

    Post-translational modificationi

    Acetylated at C-terminal lysine residues, thereby increasing affinity to histones.By similarity
    ADP-ribosylated.By similarity
    Phosphorylated at Ser-4 by PLK1 and PLK2. Phosphorylation at Ser-4 by PLK2 in S phase is required for centriole duplication and is sufficient to trigger centriole replication. Phosphorylation at Ser-4 by PLK1 takes place during mitosis. Phosphorylated by CDK2 at Ser-125 and Thr-200. Phosphorylation at Thr-200 may trigger initiation of centrosome duplication. Phosphorylated by CDK1 at Thr-200, Thr-219, Thr-234 and Thr-237 during cell mitosis. When these four sites are phosphorated, RNA-binding activity seem to be abolished. May be phosphorylated at Ser-70 by NEK2. The Thr-200 phosphorylated form has higher affinity for ROCK2 By similarity.By similarity
    Sumoylated by ARF.By similarity

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ3T160.
    PRIDEiQ3T160.

    Interactioni

    Subunit structurei

    Decamer formed by two pentameric rings associated in a head-to-head fashion. Disulfide-linked dimers under certain conditions. The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with NSUN2 and SENP3. Interacts with the methylated form of RPS10. Interacts (via N-terminal domain) with APEX1; the interaction is RNA-dependent and decreases in hydrogen peroxide-damaged cells. Interacts with NEK2. Interacts with ROCK2 and BRCA2 By similarity. Interacts with RPGR By similarity. Interacts with EIF2AK2/PKR By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000020363.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3T160.
    SMRiQ3T160. Positions 15-118, 243-294.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 187187Required for interaction with SENP3By similarityAdd
    BLAST
    Regioni1 – 117117Necessary for interaction with APEX1By similarityAdd
    BLAST
    Regioni243 – 29452Required for nucleolar localizationBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi152 – 1576Nuclear localization signalSequence Analysis
    Motifi192 – 1987Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1 – 99Met-rich
    Compositional biasi120 – 13213Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi163 – 18927Asp/Glu-rich (highly acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the nucleoplasmin family.Curated

    Phylogenomic databases

    eggNOGiNOG79897.
    HOGENOMiHOG000013061.
    HOVERGENiHBG001860.
    InParanoidiQ3T160.
    KOiK11276.

    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.

    Q3T160-1 [UniParc]FASTAAdd to Basket

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    MEDSMDMDMS PLRPQNYLFG CELKADRDYH FKVDNDENEH QLSLRTVSLG    50
    AGAKDELHVV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL 100
    RLKCGSGPVH ISGQHLVAVE EDAESEEEEE EEVKLLSISG KRSAPGSGSK 150
    VPQKKVKLAA DEDEDDDDDD DDDDDEDDDD DDFDEEVEEK APVKKSVRDT 200
    PAKNAQKSNQ NGKDSKPSTP RSKGQESFKK QEKTPKTPRG PSSVEDIKAK 250
    MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL 294
    Length:294
    Mass (Da):32,703
    Last modified:October 11, 2005 - v1
    Checksum:i644EBD839DDF160A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC102099 mRNA. Translation: AAI02100.1.
    RefSeqiNP_001030518.1. NM_001035441.2.
    UniGeneiBt.61659.

    Genome annotation databases

    GeneIDi614028.
    KEGGibta:614028.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC102099 mRNA. Translation: AAI02100.1 .
    RefSeqi NP_001030518.1. NM_001035441.2.
    UniGenei Bt.61659.

    3D structure databases

    ProteinModelPortali Q3T160.
    SMRi Q3T160. Positions 15-118, 243-294.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000020363.

    Proteomic databases

    PaxDbi Q3T160.
    PRIDEi Q3T160.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 614028.
    KEGGi bta:614028.

    Organism-specific databases

    CTDi 4869.

    Phylogenomic databases

    eggNOGi NOG79897.
    HOGENOMi HOG000013061.
    HOVERGENi HBG001860.
    InParanoidi Q3T160.
    KOi K11276.

    Miscellaneous databases

    NextBioi 20898902.

    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. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Ileum.

    Entry informationi

    Entry nameiNPM_BOVIN
    AccessioniPrimary (citable) accession number: Q3T160
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3