ID Q5SQB7_MOUSE Unreviewed; 292 AA. AC Q5SQB7; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 161. DE RecName: Full=Nucleophosmin {ECO:0000256|ARBA:ARBA00020749}; GN Name=Npm1 {ECO:0000313|EMBL:AAH89546.1, ECO:0000313|MGI:MGI:106184}; 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 {ECO:0000313|EMBL:BAE26667.1}; RN [1] {ECO:0000313|EMBL:BAE26667.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26667.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAE38420.1}, Mammary gland RC {ECO:0000313|EMBL:BAE26248.1}, and Mullerian duct includes surrounding RC region {ECO:0000313|EMBL:BAE22562.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAE26667.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26667.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAE38420.1}, Mammary gland RC {ECO:0000313|EMBL:BAE26248.1}, and Mullerian duct includes surrounding RC region {ECO:0000313|EMBL:BAE22562.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare RT full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAE26667.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26667.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAE38420.1}, Mammary gland RC {ECO:0000313|EMBL:BAE26248.1}, and Mullerian duct includes surrounding RC region {ECO:0000313|EMBL:BAE22562.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R., RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing RT pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAE26667.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26667.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAE38420.1}, Mammary gland RC {ECO:0000313|EMBL:BAE26248.1}, and Mullerian duct includes surrounding RC region {ECO:0000313|EMBL:BAE22562.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAE26667.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26667.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAE38420.1}, Mammary gland RC {ECO:0000313|EMBL:BAE26248.1}, and Mullerian duct includes surrounding RC region {ECO:0000313|EMBL:BAE22562.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [6] {ECO:0000313|EMBL:AAH89546.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6 {ECO:0000313|EMBL:AAH92378.1}; RC TISSUE=Brain {ECO:0000313|EMBL:AAH92378.1}, and Molar RC {ECO:0000313|EMBL:AAH89546.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; 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 [7] {ECO:0000313|EMBL:BAE26667.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26667.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAE38420.1}, Mammary gland RC {ECO:0000313|EMBL:BAE26248.1}, and Mullerian duct includes surrounding RC region {ECO:0000313|EMBL:BAE22562.1}; RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F., RA Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M., RA Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K., RA Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T., RA Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:BAE26667.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26667.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAE38420.1}, Mammary gland RC {ECO:0000313|EMBL:BAE26248.1}, and Mullerian duct includes surrounding RC region {ECO:0000313|EMBL:BAE22562.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [9] {ECO:0000313|EMBL:BAE26667.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26667.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAE38420.1}, Mammary gland RC {ECO:0000313|EMBL:BAE26248.1}, and Mullerian duct includes surrounding RC region {ECO:0000313|EMBL:BAE22562.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). RN [10] {ECO:0007829|PubMed:16452087} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [11] {ECO:0007829|PubMed:17242355} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [12] {ECO:0007829|PubMed:18630941} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [13] {ECO:0007829|PubMed:19144319} 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 [14] {ECO:0007829|PubMed:19131326} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [15] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [16] {ECO:0000313|EMBL:ADA57701.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6 {ECO:0000313|EMBL:ADA57701.1}; RX PubMed=20802533; DOI=10.1038/onc.2010.404; RA Olanich M.E., Moss B.L., Piwnica-Worms D., Townsend R.R., Weber J.D.; RT "Identification of FUSE-binding protein 1 as a regulatory mRNA-binding RT protein that represses nucleophosmin translation."; RL Oncogene 30:77-86(2011). RN [17] {ECO:0007829|PubMed:23806337} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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). CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus CC {ECO:0000256|ARBA:ARBA00004604}. Nucleus, nucleoplasm CC {ECO:0000256|ARBA:ARBA00004642}. CC -!- SIMILARITY: Belongs to the nucleoplasmin family. CC {ECO:0000256|ARBA:ARBA00010744}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC089546; AAH89546.1; -; mRNA. DR EMBL; BC092378; AAH92378.1; -; mRNA. DR EMBL; GU214027; ADA57701.1; -; mRNA. DR EMBL; AK135517; BAE22562.1; -; mRNA. DR EMBL; AK145124; BAE26248.1; -; mRNA. DR EMBL; AK145813; BAE26667.1; -; mRNA. DR EMBL; AK165860; BAE38420.1; -; mRNA. DR RefSeq; NP_001239189.1; NM_001252260.1. DR RefSeq; NP_032748.1; NM_008722.3. DR AlphaFoldDB; Q5SQB7; -. DR SMR; Q5SQB7; -. DR PeptideAtlas; Q5SQB7; -. DR TopDownProteomics; Q5SQB7; -. DR DNASU; 18148; -. DR GeneID; 18148; -. DR KEGG; mmu:18148; -. DR AGR; MGI:106184; -. DR CTD; 4869; -. DR MGI; MGI:106184; Npm1. DR VEuPathDB; HostDB:ENSMUSG00000057113; -. DR OMA; XAVEEDA; -. DR OrthoDB; 5360624at2759; -. DR BioGRID-ORCS; 18148; 27 hits in 117 CRISPR screens. DR ChiTaRS; Npm1; mouse. DR ExpressionAtlas; Q5SQB7; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl. DR GO; GO:0031616; C:spindle pole centrosome; IEA:Ensembl. DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0042393; F:histone binding; IEA:Ensembl. DR GO; GO:0140693; F:molecular condensate scaffold activity; IEA:Ensembl. DR GO; GO:0051059; F:NF-kappaB binding; IEA:Ensembl. DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl. DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl. DR GO; GO:0004860; F:protein kinase inhibitor activity; IEA:Ensembl. DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:Ensembl. DR GO; GO:0043024; F:ribosomal small subunit binding; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0030957; F:Tat protein binding; IEA:Ensembl. DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl. DR GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl. DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl. DR GO; GO:0007098; P:centrosome cycle; IEA:Ensembl. DR GO; GO:0006281; P:DNA repair; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0010826; P:negative regulation of centrosome duplication; IEA:Ensembl. DR GO; GO:0006913; P:nucleocytoplasmic transport; IEA:Ensembl. DR GO; GO:0006334; P:nucleosome assembly; IEA:Ensembl. DR GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl. DR GO; GO:0008104; P:protein localization; IEA:Ensembl. DR GO; GO:0046599; P:regulation of centriole replication; IEA:Ensembl. DR GO; GO:0060735; P:regulation of eIF2 alpha phosphorylation by dsRNA; IEA:Ensembl. DR GO; GO:1902629; P:regulation of mRNA stability involved in cellular response to UV; IEA:Ensembl. DR Gene3D; 1.10.10.2100; -; 1. DR Gene3D; 2.60.120.340; Nucleoplasmin core domain; 1. 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:SF28; NUCLEOPHOSMIN; 1. DR PANTHER; PTHR22747; NUCLEOPLASMIN; 1. DR Pfam; PF16276; NPM1-C; 1. DR Pfam; PF03066; Nucleoplasmin; 1. DR SUPFAM; SSF69203; Nucleoplasmin-like core domain; 1. PE 1: Evidence at protein level; KW Chaperone {ECO:0000256|ARBA:ARBA00023186}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}. FT DOMAIN 18..117 FT /note="Nucleoplasmin core" FT /evidence="ECO:0000259|Pfam:PF03066" FT DOMAIN 243..291 FT /note="Nucleophosmin C-terminal" FT /evidence="ECO:0000259|Pfam:PF16276" FT REGION 138..248 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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" 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 //