NPM3_HUMAN
ID NPM3_HUMAN Reviewed; 178 AA.
AC O75607; Q9UNY6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Nucleoplasmin-3;
GN Name=NPM3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11722795; DOI=10.1186/1471-2164-2-8;
RA Shackleford G.M., Ganguly A., MacArthur C.A.;
RT "Cloning, expression and nuclear localization of human NPM3, a member of
RT the nucleophosmin/nucleoplasmin family of nuclear chaperones.";
RL BMC Genomics 2:8-8(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hu G.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-80.
RA Brondani V., Albrecht G., Hamy F.;
RT "Retinoic acid induces differential expression of FGF8 isoforms in LNCaP
RT cells.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [5]
RP PROTEIN SEQUENCE OF 2-17, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUL-2005) to UniProtKB.
RN [6]
RP FUNCTION, INTERACTION WITH NPM, AND SUBCELLULAR LOCATION.
RX PubMed=15596447; DOI=10.1074/jbc.m407856200;
RA Huang N., Negi S., Szebeni A., Olson M.O.;
RT "Protein NPM3 interacts with the multifunctional nucleolar protein
RT B23/nucleophosmin and inhibits ribosome biogenesis.";
RL J. Biol. Chem. 280:5496-5502(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147; SER-151 AND SER-158, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION.
RX PubMed=20073534; DOI=10.1021/bi9021632;
RA Gadad S.S., Shandilya J., Kishore A.H., Kundu T.K.;
RT "NPM3, a member of the nucleophosmin/nucleoplasmin family, enhances
RT activator-dependent transcription.";
RL Biochemistry 49:1355-1357(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-13 AND SER-16, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-13, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NPM.
RX PubMed=22362753; DOI=10.1093/nar/gks162;
RA Okuwaki M., Sumi A., Hisaoka M., Saotome-Nakamura A., Akashi S.,
RA Nishimura Y., Nagata K.;
RT "Function of homo- and hetero-oligomers of human
RT nucleoplasmin/nucleophosmin family proteins NPM1, NPM2 and NPM3 during
RT sperm chromatin remodeling.";
RL Nucleic Acids Res. 40:4861-4878(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-16, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-27, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Plays a role in the regulation of diverse cellular processes
CC such as ribosome biogenesis, chromatin remodeling or protein
CC chaperoning (PubMed:22362753, PubMed:20073534). Modulates the histone
CC chaperone function and the RNA-binding activity of nucleolar
CC phosphoprotein B23/NPM (PubMed:22362753). Efficiently mediates
CC chromatin remodeling when included in a pentamer containing NPM3 and
CC NPM (PubMed:15596447). {ECO:0000269|PubMed:15596447,
CC ECO:0000269|PubMed:20073534, ECO:0000269|PubMed:22362753}.
CC -!- SUBUNIT: Interacts with NPM (via N-terminus) (PubMed:15596447). Forms a
CC pentamer with NPM at a ratio 4:1 (NPM3/NPM). Two pentamers form a
CC decamer (PubMed:22362753). {ECO:0000269|PubMed:15596447,
CC ECO:0000269|PubMed:22362753}.
CC -!- INTERACTION:
CC O75607; Q86SE8: NPM2; NbExp=5; IntAct=EBI-721544, EBI-6658150;
CC O75607; Q96BW1: UPRT; NbExp=3; IntAct=EBI-721544, EBI-742943;
CC O75607; P04608: tat; Xeno; NbExp=2; IntAct=EBI-721544, EBI-6164389;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11722795}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:15596447, ECO:0000269|PubMed:22362753}.
CC Note=Mainly found in the granular component of the nucleolus.
CC {ECO:0000269|PubMed:22362753}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11722795}.
CC -!- PTM: Phosphorylated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
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DR EMBL; AY049737; AAL12172.1; -; mRNA.
DR EMBL; AF081280; AAC31609.1; -; mRNA.
DR EMBL; AF079325; AAD51496.1; -; Genomic_DNA.
DR EMBL; BC041067; AAH41067.1; -; mRNA.
DR EMBL; BC054868; AAH54868.1; -; mRNA.
DR CCDS; CCDS7519.1; -.
DR RefSeq; NP_008924.1; NM_006993.2.
DR AlphaFoldDB; O75607; -.
DR SMR; O75607; -.
DR BioGRID; 115640; 236.
DR IntAct; O75607; 43.
DR MINT; O75607; -.
DR STRING; 9606.ENSP00000359128; -.
DR GlyGen; O75607; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75607; -.
DR PhosphoSitePlus; O75607; -.
DR BioMuta; NPM3; -.
DR EPD; O75607; -.
DR jPOST; O75607; -.
DR MassIVE; O75607; -.
DR MaxQB; O75607; -.
DR PaxDb; O75607; -.
DR PeptideAtlas; O75607; -.
DR PRIDE; O75607; -.
DR ProteomicsDB; 50116; -.
DR TopDownProteomics; O75607; -.
DR Antibodypedia; 31335; 122 antibodies from 20 providers.
DR DNASU; 10360; -.
DR Ensembl; ENST00000370110.5; ENSP00000359128.5; ENSG00000107833.10.
DR GeneID; 10360; -.
DR KEGG; hsa:10360; -.
DR MANE-Select; ENST00000370110.6; ENSP00000359128.5; NM_006993.3; NP_008924.1.
DR UCSC; uc001ktt.3; human.
DR CTD; 10360; -.
DR DisGeNET; 10360; -.
DR GeneCards; NPM3; -.
DR HGNC; HGNC:7931; NPM3.
DR HPA; ENSG00000107833; Low tissue specificity.
DR MIM; 606456; gene.
DR neXtProt; NX_O75607; -.
DR OpenTargets; ENSG00000107833; -.
DR PharmGKB; PA31733; -.
DR VEuPathDB; HostDB:ENSG00000107833; -.
DR eggNOG; ENOG502S1E6; Eukaryota.
DR GeneTree; ENSGT00940000158796; -.
DR HOGENOM; CLU_058838_1_0_1; -.
DR InParanoid; O75607; -.
DR OMA; TEDYFWG; -.
DR OrthoDB; 1485080at2759; -.
DR PhylomeDB; O75607; -.
DR TreeFam; TF327704; -.
DR PathwayCommons; O75607; -.
DR SignaLink; O75607; -.
DR BioGRID-ORCS; 10360; 68 hits in 1081 CRISPR screens.
DR ChiTaRS; NPM3; human.
DR GeneWiki; NPM3; -.
DR GenomeRNAi; 10360; -.
DR Pharos; O75607; Tbio.
DR PRO; PR:O75607; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O75607; protein.
DR Bgee; ENSG00000107833; Expressed in oocyte and 126 other tissues.
DR Genevisible; O75607; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:Ensembl.
DR GO; GO:0009303; P:rRNA transcription; IEA:Ensembl.
DR InterPro; IPR004301; Nucleoplasmin.
DR InterPro; IPR024057; Nucleoplasmin_core_dom.
DR InterPro; IPR036824; Nucleoplasmin_core_dom_sf.
DR PANTHER; PTHR22747; PTHR22747; 1.
DR Pfam; PF03066; Nucleoplasmin; 1.
DR SUPFAM; SSF69203; SSF69203; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Direct protein sequencing; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..178
FT /note="Nucleoplasmin-3"
FT /id="PRO_0000219489"
FT REGION 141..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..164
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 27
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 16
FT /note="S -> N (in dbSNP:rs34376117)"
FT /id="VAR_050410"
FT VARIANT 80
FT /note="N -> I (in dbSNP:rs2735420)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_050411"
FT CONFLICT 61..62
FT /note="EH -> DD (in Ref. 3; AAD51496)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="E -> K (in Ref. 3; AAD51496)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 178 AA; 19344 MW; 8C899DE8C3CD61FA CRC64;
MAAGTAAALA FLSQESRTRA GGVGGLRVPA PVTMDSFFFG CELSGHTRSF TFKVEEEDDA
EHVLALTMLC LTEGAKDECN VVEVVARNHD HQEIAVPVAN LKLSCQPMLS LDDFQLQPPV
TFRLKSGSGP VRITGRHQIV TMSNDVSEEE SEEEEEDSDE EEVELCPILP AKKQGGRP
