ID Q5SQB0_MOUSE Unreviewed; 264 AA. AC Q5SQB0; DT 21-DEC-2004, integrated into UniProtKB/TrEMBL. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 123. DE RecName: Full=Nucleophosmin {ECO:0000256|ARBA:ARBA00020749}; GN Name=Npm1 {ECO:0000313|Ensembl:ENSMUSP00000090891.7, GN 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|Ensembl:ENSMUSP00000090891.7, ECO:0000313|Proteomes:UP000000589}; RN [1] {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 [2] {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 [3] {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 [4] {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 [5] {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 [6] {ECO:0000313|Ensembl:ENSMUSP00000090891.7, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000090891.7, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [7] {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 [8] {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). RN [9] {ECO:0000313|Ensembl:ENSMUSP00000090891.7} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000090891.7}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. 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 AlphaFoldDB; Q5SQB0; -. DR SMR; Q5SQB0; -. DR jPOST; Q5SQB0; -. DR MaxQB; Q5SQB0; -. DR PeptideAtlas; Q5SQB0; -. DR ProteomicsDB; 365742; -. DR TopDownProteomics; Q5SQB0; -. DR Ensembl; ENSMUST00000093201.13; ENSMUSP00000090891.7; ENSMUSG00000057113.14. DR AGR; MGI:106184; -. DR MGI; MGI:106184; Npm1. DR VEuPathDB; HostDB:ENSMUSG00000057113; -. DR GeneTree; ENSGT00940000153052; -. DR HOGENOM; CLU_058838_0_0_1; -. DR ChiTaRS; Npm1; mouse. DR Proteomes; UP000000589; Chromosome 11. DR Bgee; ENSMUSG00000057113; Expressed in embryonic post-anal tail and 68 other cell types or tissues. DR ExpressionAtlas; Q5SQB0; 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:0003723; F:RNA binding; IEA:UniProtKB-KW. 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 Proteomics identification {ECO:0007829|EPD:Q5SQB0, KW ECO:0007829|MaxQB:Q5SQB0}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}. FT DOMAIN 18..117 FT /note="Nucleoplasmin core" FT /evidence="ECO:0000259|Pfam:PF03066" FT DOMAIN 215..263 FT /note="Nucleophosmin C-terminal" FT /evidence="ECO:0000259|Pfam:PF16276" FT REGION 138..219 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 186..206 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 264 AA; 29525 MW; 87C12DB1C92DAF58 CRC64; MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE EDAESEDEDE EDVKLLGMSG KRSAPGGGNK VPQKKVKLDE DDEDDDEDDE DDEDDDDDDF DEEETEEKVP VKKGQESFKK QEKTPKTPKG PSSVEDIKAK MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL //