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Q61937

- NPM_MOUSE

UniProt

Q61937 - NPM_MOUSE

Protein

Nucleophosmin

Gene

Npm1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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. 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 By similarity. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. 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. DNA binding Source: UniProtKB-KW
    2. NF-kappaB binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein kinase inhibitor activity Source: UniProtKB
    5. ribosomal large subunit binding Source: MGI
    6. ribosomal small subunit binding Source: MGI
    7. RNA binding Source: MGI
    8. rRNA binding Source: MGI
    9. unfolded protein binding Source: UniProtKB

    GO - Biological processi

    1. cell aging Source: UniProtKB
    2. cell growth Source: MGI
    3. cell volume homeostasis Source: MGI
    4. centrosome cycle Source: UniProtKB
    5. DNA repair Source: UniProtKB
    6. negative regulation of apoptotic process Source: UniProtKB
    7. negative regulation of cell proliferation Source: UniProtKB
    8. negative regulation of mRNA splicing, via spliceosome Source: MGI
    9. negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
    10. nucleocytoplasmic transport Source: MGI
    11. positive regulation of cell proliferation Source: MGI
    12. positive regulation of cellular biosynthetic process Source: MGI
    13. positive regulation of centrosome duplication Source: MGI
    14. positive regulation of protein kinase activity Source: MGI
    15. positive regulation of translation Source: UniProtKB
    16. protein localization Source: MGI
    17. protein oligomerization Source: MGI
    18. regulation of cell cycle Source: MGI
    19. regulation of centriole replication Source: UniProtKB
    20. regulation of centrosome duplication Source: MGI
    21. regulation of DNA damage response, signal transduction by p53 class mediator Source: MGI
    22. regulation of eIF2 alpha phosphorylation by dsRNA Source: UniProtKB
    23. regulation of endodeoxyribonuclease activity Source: UniProtKB
    24. regulation of endoribonuclease activity Source: UniProtKB
    25. ribosomal large subunit biogenesis Source: MGI
    26. ribosomal large subunit export from nucleus Source: MGI
    27. ribosomal small subunit biogenesis Source: MGI
    28. ribosomal small subunit export from nucleus Source: MGI
    29. rRNA export from nucleus Source: MGI

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198597. Deposition of new CENPA-containing nucleosomes at the centromere.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleophosmin
    Short name:
    NPM
    Alternative name(s):
    Nucleolar phosphoprotein B23
    Nucleolar protein NO38
    Numatrin
    Gene namesi
    Name:Npm1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:106184. Npm1.

    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 By similarity.By similarity

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: MGI
    4. granular component Source: MGI
    5. large ribosomal subunit Source: MGI
    6. nuclear speck Source: MGI
    7. nucleolus Source: MGI
    8. nucleoplasm Source: MGI
    9. nucleus Source: UniProtKB
    10. ribonucleoprotein complex Source: MGI
    11. small ribosomal subunit Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 292292NucleophosminPRO_0000219482Add
    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 – 701Phosphoserine1 Publication
    Modified residuei75 – 751PhosphothreonineBy similarity
    Modified residuei95 – 951PhosphothreonineBy similarity
    Modified residuei125 – 1251Phosphoserine5 Publications
    Modified residuei139 – 1391PhosphoserineBy similarity
    Modified residuei150 – 1501N6-acetyllysineBy similarity
    Modified residuei154 – 1541N6-acetyllysineBy similarity
    Modified residuei198 – 1981Phosphothreonine; by CDK1 and CDK2By similarity
    Modified residuei211 – 2111N6-acetyllysineBy similarity
    Modified residuei217 – 2171Phosphothreonine; by CDK1By similarity
    Modified residuei225 – 2251PhosphoserineBy similarity
    Modified residuei227 – 2271N6-acetyllysineBy similarity
    Modified residuei228 – 2281N6-acetyllysine; alternateBy similarity
    Cross-linki228 – 228Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
    Modified residuei232 – 2321Phosphothreonine; by CDK1By similarity
    Modified residuei235 – 2351Phosphothreonine; by CDK1By similarity
    Modified residuei240 – 2401PhosphoserineBy similarity
    Modified residuei241 – 2411PhosphoserineBy similarity
    Modified residuei248 – 2481N6-acetyllysineBy similarity
    Modified residuei252 – 2521PhosphoserineBy similarity
    Modified residuei255 – 2551N6-acetyllysineBy similarity
    Modified residuei258 – 2581PhosphoserineBy similarity
    Cross-linki261 – 261Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei265 – 2651N6-acetyllysineBy similarity
    Modified residuei271 – 2711N6-acetyllysineBy similarity
    Modified residuei277 – 2771PhosphothreonineBy similarity
    Modified residuei290 – 2901N6-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-198. Phosphorylation at Thr-198 may trigger initiation of centrosome duplication. Phosphorylated by CDK1 at Thr-198, Thr-217, Thr-232 and Thr-235 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-198 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

    MaxQBiQ61937.
    PaxDbiQ61937.
    PRIDEiQ61937.

    PTM databases

    PhosphoSiteiQ61937.

    Expressioni

    Tissue specificityi

    Expressed in B-cells that have been induced to switch to various Ig isotypes.1 Publication

    Gene expression databases

    ArrayExpressiQ61937.
    BgeeiQ61937.
    CleanExiMM_NPM1.
    GenevestigatoriQ61937.

    Interactioni

    Subunit structurei

    Decamer formed by two pentameric rings associated in a head-to-head fashion. Disulfide-linked dimers under certain conditions. Interacts with NSUN2 and SENP3 By similarity. The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with the methylated form of RPS10. Interacts (via N-terminal domain) with APEX1; the interaction is RNA-dependent and decreases peroxide-damaged cells. Interacts with NEK2. Interacts with ROCK2 and BRCA2 By similarity. Interacts with RPGR. Interacts with CENPW By similarity. Interacts with EIF2AK2/PKR.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MDM2Q009872EBI-626362,EBI-389668From a different organism.

    Protein-protein interaction databases

    BioGridi201823. 47 interactions.
    IntActiQ61937. 10 interactions.
    MINTiMINT-270928.

    Structurei

    Secondary structure

    1
    292
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 2410
    Beta strandi29 – 313
    Helixi37 – 393
    Beta strandi40 – 4910
    Beta strandi58 – 658
    Beta strandi69 – 8012
    Turni81 – 833
    Beta strandi84 – 9411
    Beta strandi96 – 1049
    Beta strandi109 – 1179

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4N8MX-ray1.80A/B/C/D/E1-130[»]
    ProteinModelPortaliQ61937.
    SMRiQ61937. Positions 13-120, 223-292.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 185185Required for interaction with SENP3By similarityAdd
    BLAST
    Regioni1 – 117117Necessary for interaction with APEX1By similarityAdd
    BLAST
    Regioni241 – 29252Required for nucleolar localizationBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi152 – 1576Nuclear localization signalSequence Analysis
    Motifi190 – 1967Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1 – 99Met-rich
    Compositional biasi120 – 13213Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi158 – 18730Asp/Glu-rich (highly acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the nucleoplasmin family.Curated

    Phylogenomic databases

    eggNOGiNOG79897.
    GeneTreeiENSGT00440000034554.
    HOGENOMiHOG000013061.
    HOVERGENiHBG001860.
    InParanoidiQ61937.
    KOiK11276.
    OMAiNCFRTED.
    OrthoDBiEOG79W97G.
    PhylomeDBiQ61937.
    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.

    Q61937-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG    50
    AGAKDELHIV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL 100
    RLKCGSGPVH ISGQHLVAVE EDAESEDEDE EDVKLLGMSG KRSAPGGGNK 150
    VPQKKVKLDE DDEDDDEDDE DDEDDDDDDF DEEETEEKVP VKKSVRDTPA 200
    KNAQKSNQNG KDLKPSTPRS KGQESFKKQE KTPKTPKGPS SVEDIKAKMQ 250
    ASIEKGGSLP KVEAKFINYV KNCFRMTDQE AIQDLWQWRK SL 292
    Length:292
    Mass (Da):32,560
    Last modified:November 1, 1996 - v1
    Checksum:iE68750C549ED25E6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33212 mRNA. Translation: AAA39801.1.
    AK028253 mRNA. Translation: BAC25844.1.
    BC054755 mRNA. Translation: AAH54755.1.
    CCDSiCCDS24532.1.
    PIRiI52858.
    RefSeqiNP_032748.1. NM_008722.3.
    UniGeneiMm.485384.

    Genome annotation databases

    EnsembliENSMUST00000075641; ENSMUSP00000075067; ENSMUSG00000057113.
    GeneIDi18148.
    KEGGimmu:18148.
    UCSCiuc007ikd.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33212 mRNA. Translation: AAA39801.1 .
    AK028253 mRNA. Translation: BAC25844.1 .
    BC054755 mRNA. Translation: AAH54755.1 .
    CCDSi CCDS24532.1.
    PIRi I52858.
    RefSeqi NP_032748.1. NM_008722.3.
    UniGenei Mm.485384.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4N8M X-ray 1.80 A/B/C/D/E 1-130 [» ]
    ProteinModelPortali Q61937.
    SMRi Q61937. Positions 13-120, 223-292.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201823. 47 interactions.
    IntActi Q61937. 10 interactions.
    MINTi MINT-270928.

    Chemistry

    ChEMBLi CHEMBL5386.

    PTM databases

    PhosphoSitei Q61937.

    Proteomic databases

    MaxQBi Q61937.
    PaxDbi Q61937.
    PRIDEi Q61937.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000075641 ; ENSMUSP00000075067 ; ENSMUSG00000057113 .
    GeneIDi 18148.
    KEGGi mmu:18148.
    UCSCi uc007ikd.2. mouse.

    Organism-specific databases

    CTDi 4869.
    MGIi MGI:106184. Npm1.

    Phylogenomic databases

    eggNOGi NOG79897.
    GeneTreei ENSGT00440000034554.
    HOGENOMi HOG000013061.
    HOVERGENi HBG001860.
    InParanoidi Q61937.
    KOi K11276.
    OMAi NCFRTED.
    OrthoDBi EOG79W97G.
    PhylomeDBi Q61937.
    TreeFami TF327704.

    Enzyme and pathway databases

    Reactomei REACT_198597. Deposition of new CENPA-containing nucleosomes at the centromere.

    Miscellaneous databases

    NextBioi 293410.
    PROi Q61937.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61937.
    Bgeei Q61937.
    CleanExi MM_NPM1.
    Genevestigatori Q61937.

    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. "DNA cloning and amino acid sequence determination of a major constituent protein of mammalian nucleoli. Correspondence of the nucleoplasmin-related protein NO38 to mammalian protein B23."
      Schmidt-Zachmann M.S., Franke W.W.
      Chromosoma 96:417-426(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo.
    3. "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].
      Strain: C57BL/6.
      Tissue: Brain.
    4. Lubec G., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 33-45.
      Tissue: Brain.
    5. Cited for: PROTEIN SEQUENCE OF 46-52 AND 266-271, SUBUNIT, TISSUE SPECIFICITY.
      Strain: C57BL/6.
      Tissue: Spleen.
    6. "Nucleophosmin interacts with and inhibits the catalytic function of eukaryotic initiation factor 2 kinase PKR."
      Pang Q., Christianson T.A., Koretsky T., Carlson H., David L., Keeble W., Faulkner G.R., Speckhart A., Bagby G.C.
      J. Biol. Chem. 278:41709-41717(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF2AK2.
    7. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    12. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiNPM_MOUSE
    AccessioniPrimary (citable) accession number: Q61937
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 132 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3