NPM_MOUSE
ID NPM_MOUSE Reviewed; 292 AA.
AC Q61937;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Nucleophosmin;
DE Short=NPM;
DE AltName: Full=Nucleolar phosphoprotein B23;
DE AltName: Full=Nucleolar protein NO38;
DE AltName: Full=Numatrin;
GN Name=Npm1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3219912; DOI=10.1007/bf00303035;
RA Schmidt-Zachmann M.S., Franke W.W.;
RT "DNA cloning and amino acid sequence determination of a major constituent
RT protein of mammalian nucleoli. Correspondence of the nucleoplasmin-related
RT protein NO38 to mammalian protein B23.";
RL Chromosoma 96:417-426(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 33-45.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 46-52 AND 266-271, SUBUNIT, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=9642267; DOI=10.1074/jbc.273.27.17025;
RA Borggrefe T., Wabl M., Akhmedov A.T., Jessberger R.;
RT "A B-cell-specific DNA recombination complex.";
RL J. Biol. Chem. 273:17025-17035(1998).
RN [6]
RP INTERACTION WITH EIF2AK2.
RX PubMed=12882984; DOI=10.1074/jbc.m301392200;
RA Pang Q., Christianson T.A., Koretsky T., Carlson H., David L., Keeble W.,
RA Faulkner G.R., Speckhart A., Bagby G.C.;
RT "Nucleophosmin interacts with and inhibits the catalytic function of
RT eukaryotic initiation factor 2 kinase PKR.";
RL J. Biol. Chem. 278:41709-41717(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-125, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67; SER-70; THR-75 AND
RP SER-125, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION, AND INTERACTION WITH TTF1.
RX PubMed=20513429; DOI=10.1016/j.molcel.2010.03.015;
RA Lessard F., Morin F., Ivanchuk S., Langlois F., Stefanovsky V., Rutka J.,
RA Moss T.;
RT "The ARF tumor suppressor controls ribosome biogenesis by regulating the
RT RNA polymerase I transcription factor TTF-I.";
RL Mol. Cell 38:539-550(2010).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-255; LYS-265 AND LYS-271,
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-265, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [15]
RP INTERACTION WITH LRRC34.
RX PubMed=24991885; DOI=10.1089/scd.2013.0470;
RA Luehrig S., Siamishi I., Tesmer-Wolf M., Zechner U., Engel W., Nolte J.;
RT "Lrrc34, a novel nucleolar protein, interacts with npm1 and ncl and has an
RT impact on pluripotent stem cells.";
RL Stem Cells Dev. 23:2862-2874(2014).
CC -!- FUNCTION: Involved in diverse cellular processes such as ribosome
CC biogenesis, centrosome duplication, protein chaperoning, histone
CC assembly, cell proliferation, and regulation of tumor suppressors
CC p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear
CC export. Associated with nucleolar ribonucleoprotein structures and bind
CC single-stranded nucleic acids. Acts as a chaperonin for the core
CC histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on
CC apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1
CC endonuclease activity on AP single-stranded RNA. May exert a control of
CC APEX1 endonuclease activity within nucleoli devoted to repair AP on
CC rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2,
CC regulates centrosome duplication. Regulates centriole duplication:
CC phosphorylation by PLK2 is able to trigger centriole replication.
CC Negatively regulates the activation of EIF2AK2/PKR and suppresses
CC apoptosis through inhibition of EIF2AK2/PKR autophosphorylation.
CC Antagonizes the inhibitory effect of ATF5 on cell proliferation and
CC relieves ATF5-induced G2/M blockade. In complex with MYC enhances the
CC transcription of MYC target genes. May act as chaperonin or
CC cotransporter in the nucleolar localization of transcription
CC termination factor TTF1 (PubMed:20513429).
CC {ECO:0000250|UniProtKB:P06748}.
CC -!- SUBUNIT: Decamer formed by two pentameric rings associated in a head-
CC to-head fashion. Disulfide-linked dimers under certain conditions.
CC Interacts with NSUN2 and SENP3 (By similarity). The SWAP complex
CC consists of NPM1, NCL, PARP1 and SWAP70. Interacts with the methylated
CC form of RPS10. Interacts (via N-terminal domain) with APEX1; the
CC interaction is RNA-dependent and decreases peroxide-damaged cells.
CC Interacts with NEK2. Interacts with ROCK2 and BRCA2 (By similarity).
CC Interacts with RPGR. Interacts with CENPW (By similarity). Interacts
CC with EIF2AK2/PKR. Interacts with DDX31; this interaction prevents
CC interaction between NPM1 and HDM2 (By similarity). Interacts with MYC;
CC competitive with NOP53. Interacts with NOP53; the interaction is direct
CC and competitive with MYC (By similarity). Interacts with LRRC34
CC (PubMed:24991885). Interacts with RRP1B (By similarity). Interacts with
CC NPM3 (By similarity). Interacts with ALKBH2. Interacts with TTF1 (via
CC C-terminal region) (PubMed:20513429). {ECO:0000250|UniProtKB:P06748,
CC ECO:0000269|PubMed:12882984, ECO:0000269|PubMed:24991885,
CC ECO:0000269|PubMed:9642267}.
CC -!- INTERACTION:
CC Q61937; Q00987: MDM2; Xeno; NbExp=2; IntAct=EBI-626362, EBI-389668;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P06748}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P06748}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P06748}.
CC Note=Generally nucleolar, but is translocated to the nucleoplasm in
CC case of serum starvation or treatment with anticancer drugs.
CC Colocalizes with the methylated form of RPS10 in the granular component
CC (GC) region of the nucleolus. Colocalized with nucleolin and APEX1 in
CC nucleoli. NEK2 is required for its localization to the centrosome
CC during mitosis (By similarity). {ECO:0000250|UniProtKB:P06748}.
CC -!- TISSUE SPECIFICITY: Expressed in B-cells that have been induced to
CC switch to various Ig isotypes. {ECO:0000269|PubMed:9642267}.
CC -!- PTM: Acetylated at C-terminal lysine residues, thereby increasing
CC affinity to histones. {ECO:0000250|UniProtKB:P06748}.
CC -!- PTM: ADP-ribosylated. {ECO:0000250|UniProtKB:P06748}.
CC -!- PTM: Phosphorylated at Ser-4 by PLK1 and PLK2. Phosphorylation at Ser-4
CC by PLK2 in S phase is required for centriole duplication and is
CC sufficient to trigger centriole replication. Phosphorylation at Ser-4
CC by PLK1 takes place during mitosis. Phosphorylated by CDK2 at Ser-125
CC and Thr-198. Phosphorylation at Thr-198 may trigger initiation of
CC centrosome duplication. Phosphorylated by CDK1 at Thr-198, Thr-217,
CC Thr-232 and Thr-235 during cell mitosis. When these four sites are
CC phosphorated, RNA-binding activity seem to be abolished. May be
CC phosphorylated at Ser-70 by NEK2. The Thr-198 phosphorylated form has
CC higher affinity for ROCK2 (By similarity).
CC {ECO:0000250|UniProtKB:P06748}.
CC -!- PTM: Sumoylated by ARF. {ECO:0000250|UniProtKB:P06748}.
CC -!- PTM: Ubiquitinated. Ubiquitination leads to proteasomal degradation.
CC Deubiquitinated by USP36. {ECO:0000250|UniProtKB:P06748}.
CC -!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
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DR EMBL; M33212; AAA39801.1; -; mRNA.
DR EMBL; AK028253; BAC25844.1; -; mRNA.
DR EMBL; BC054755; AAH54755.1; -; mRNA.
DR CCDS; CCDS24532.1; -.
DR PIR; I52858; I52858.
DR RefSeq; NP_032748.1; NM_008722.3.
DR PDB; 4N8M; X-ray; 1.80 A; A/B/C/D/E=1-130.
DR PDBsum; 4N8M; -.
DR AlphaFoldDB; Q61937; -.
DR BMRB; Q61937; -.
DR SMR; Q61937; -.
DR BioGRID; 201823; 96.
DR CORUM; Q61937; -.
DR IntAct; Q61937; 11.
DR MINT; Q61937; -.
DR STRING; 10090.ENSMUSP00000075067; -.
DR ChEMBL; CHEMBL5386; -.
DR iPTMnet; Q61937; -.
DR PhosphoSitePlus; Q61937; -.
DR SwissPalm; Q61937; -.
DR EPD; Q61937; -.
DR jPOST; Q61937; -.
DR MaxQB; Q61937; -.
DR PaxDb; Q61937; -.
DR PRIDE; Q61937; -.
DR ProteomicsDB; 295514; -.
DR DNASU; 18148; -.
DR Ensembl; ENSMUST00000075641; ENSMUSP00000075067; ENSMUSG00000057113.
DR GeneID; 18148; -.
DR KEGG; mmu:18148; -.
DR UCSC; uc007ikd.2; mouse.
DR CTD; 4869; -.
DR MGI; MGI:106184; Npm1.
DR VEuPathDB; HostDB:ENSMUSG00000057113; -.
DR eggNOG; KOG0488; Eukaryota.
DR GeneTree; ENSGT00940000153052; -.
DR InParanoid; Q61937; -.
DR OMA; MSVQPTX; -.
DR OrthoDB; 1485080at2759; -.
DR PhylomeDB; Q61937; -.
DR TreeFam; TF327704; -.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-MMU-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR Reactome; R-MMU-8869496; TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation.
DR BioGRID-ORCS; 18148; 25 hits in 112 CRISPR screens.
DR ChiTaRS; Npm1; mouse.
DR PRO; PR:Q61937; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q61937; protein.
DR Bgee; ENSMUSG00000057113; Expressed in embryonic post-anal tail and 65 other tissues.
DR ExpressionAtlas; Q61937; baseline and differential.
DR Genevisible; Q61937; MM.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0001652; C:granular component; IDA:MGI.
DR GO; GO:0015934; C:large ribosomal subunit; IDA:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0015935; C:small ribosomal subunit; IDA:MGI.
DR GO; GO:0031616; C:spindle pole centrosome; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0051059; F:NF-kappaB binding; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0043422; F:protein kinase B binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:MGI.
DR GO; GO:0043023; F:ribosomal large subunit binding; ISO:MGI.
DR GO; GO:0043024; F:ribosomal small subunit binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0019843; F:rRNA binding; IDA:MGI.
DR GO; GO:0030957; F:Tat protein binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
DR GO; GO:0006884; P:cell volume homeostasis; IDA:MGI.
DR GO; GO:0034644; P:cellular response to UV; ISO:MGI.
DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISO:MGI.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; ISO:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IGI:MGI.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IDA:MGI.
DR GO; GO:0006334; P:nucleosome assembly; ISO:MGI.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO:MGI.
DR GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0031328; P:positive regulation of cellular biosynthetic process; IDA:MGI.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; IGI:MGI.
DR GO; GO:0051054; P:positive regulation of DNA metabolic process; ISO:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:MGI.
DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; IMP:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:CAFA.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0050821; P:protein stabilization; IMP:CAFA.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
DR GO; GO:0001558; P:regulation of cell growth; IDA:MGI.
DR GO; GO:0046599; P:regulation of centriole replication; ISS:UniProtKB.
DR GO; GO:0010824; P:regulation of centrosome duplication; IMP:MGI.
DR GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IGI:MGI.
DR GO; GO:0060735; P:regulation of eIF2 alpha phosphorylation by dsRNA; ISS:UniProtKB.
DR GO; GO:0032071; P:regulation of endodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0060699; P:regulation of endoribonuclease activity; ISS:UniProtKB.
DR GO; GO:1902629; P:regulation of mRNA stability involved in cellular response to UV; ISO:MGI.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IDA:MGI.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:MGI.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:MGI.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IDA:MGI.
DR GO; GO:0006407; P:rRNA export from nucleus; IDA:MGI.
DR GO; GO:0009303; P:rRNA transcription; ISO:MGI.
DR InterPro; IPR032569; NPM1_C.
DR InterPro; IPR004301; Nucleoplasmin.
DR InterPro; IPR024057; Nucleoplasmin_core_dom.
DR InterPro; IPR036824; Nucleoplasmin_core_dom_sf.
DR PANTHER; PTHR22747; PTHR22747; 1.
DR Pfam; PF16276; NPM1-C; 1.
DR Pfam; PF03066; Nucleoplasmin; 1.
DR SUPFAM; SSF69203; SSF69203; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Chaperone; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Disulfide bond; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..292
FT /note="Nucleophosmin"
FT /id="PRO_0000219482"
FT REGION 1..185
FT /note="Required for interaction with SENP3"
FT /evidence="ECO:0000250"
FT REGION 1..117
FT /note="Necessary for interaction with APEX1"
FT /evidence="ECO:0000250"
FT REGION 138..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..292
FT /note="Required for nucleolar localization"
FT /evidence="ECO:0000250"
FT MOTIF 152..157
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 190..196
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 160..185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 55
FT /note="Interaction between pentamers"
FT /evidence="ECO:0000250"
FT SITE 80
FT /note="Interaction between pentamers"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 4
FT /note="Phosphoserine; by PLK1 and PLK2"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 32
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 67
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 95
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 150
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 154
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 198
FT /note="Phosphothreonine; by CDK1 and CDK2"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 206
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 211
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 217
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 227
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 228
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 232
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 235
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 248
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 255
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 265
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 265
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 271
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 290
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 150
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 228
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 261
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 261
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 265
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 265
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:4N8M"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:4N8M"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:4N8M"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:4N8M"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:4N8M"
FT STRAND 69..80
FT /evidence="ECO:0007829|PDB:4N8M"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:4N8M"
FT STRAND 84..94
FT /evidence="ECO:0007829|PDB:4N8M"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:4N8M"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:4N8M"
SQ SEQUENCE 292 AA; 32560 MW; E68750C549ED25E6 CRC64;
MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV
EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE
EDAESEDEDE EDVKLLGMSG KRSAPGGGNK VPQKKVKLDE DDEDDDEDDE DDEDDDDDDF
DEEETEEKVP VKKSVRDTPA KNAQKSNQNG KDLKPSTPRS KGQESFKKQE KTPKTPKGPS
SVEDIKAKMQ ASIEKGGSLP KVEAKFINYV KNCFRMTDQE AIQDLWQWRK SL
