NPM3_MOUSE
ID NPM3_MOUSE Reviewed; 175 AA.
AC Q9CPP0; Q3UJ58;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Nucleoplasmin-3;
GN Name=Npm3;
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=9177783; DOI=10.1006/geno.1997.4353;
RA MacArthur C.A., Shackleford G.M.;
RT "Npm3: a novel, widely expressed gene encoding a protein related to the
RT molecular chaperones nucleoplasmin and nucleophosmin.";
RL Genomics 42:137-140(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
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 TISSUE=Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen, and
RC 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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=28366643; DOI=10.1016/j.molcel.2017.02.025;
RA Barral S., Morozumi Y., Tanaka H., Montellier E., Govin J.,
RA de Dieuleveult M., Charbonnier G., Coute Y., Puthier D., Buchou T.,
RA Boussouar F., Urahama T., Fenaille F., Curtet S., Hery P.,
RA Fernandez-Nunez N., Shiota H., Gerard M., Rousseaux S., Kurumizaka H.,
RA Khochbin S.;
RT "Histone variant H2A.L.2 guides transition protein-dependent protamine
RT assembly in male germ cells.";
RL Mol. Cell 66:89-101(2017).
CC -!- FUNCTION: Plays a role in the regulation of diverse cellular processes
CC such as ribosome biogenesis, chromatin remodeling or protein
CC chaperoning. Modulates the histone chaperone function and the RNA-
CC binding activity of nucleolar phosphoprotein B23/NPM. Efficiently
CC mediates chromatin remodeling when included in a pentamer containing
CC NPM3 and NPM. {ECO:0000250|UniProtKB:O75607}.
CC -!- SUBUNIT: Interacts with NPM (via N-terminus). Forms a pentamer with NPM
CC at a ratio 4:1 (NPM3/NPM). Two pentamers form a decamer.
CC {ECO:0000250|UniProtKB:O75607}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75607}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:O75607}. Note=Mainly found in the
CC granular component of the nucleolus. {ECO:0000250|UniProtKB:O75607}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis.
CC {ECO:0000269|PubMed:28366643}.
CC -!- PTM: Phosphorylated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
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DR EMBL; U64450; AAC53205.1; -; mRNA.
DR EMBL; AK011749; BAB27818.1; -; mRNA.
DR EMBL; AK146603; BAE27297.1; -; mRNA.
DR EMBL; BC048491; AAH48491.1; -; mRNA.
DR CCDS; CCDS29865.1; -.
DR RefSeq; NP_032749.1; NM_008723.1.
DR AlphaFoldDB; Q9CPP0; -.
DR SMR; Q9CPP0; -.
DR BioGRID; 201824; 8.
DR CORUM; Q9CPP0; -.
DR IntAct; Q9CPP0; 1.
DR MINT; Q9CPP0; -.
DR STRING; 10090.ENSMUSP00000069578; -.
DR iPTMnet; Q9CPP0; -.
DR PhosphoSitePlus; Q9CPP0; -.
DR SwissPalm; Q9CPP0; -.
DR EPD; Q9CPP0; -.
DR jPOST; Q9CPP0; -.
DR MaxQB; Q9CPP0; -.
DR PaxDb; Q9CPP0; -.
DR PeptideAtlas; Q9CPP0; -.
DR PRIDE; Q9CPP0; -.
DR ProteomicsDB; 253004; -.
DR Antibodypedia; 31335; 122 antibodies from 20 providers.
DR DNASU; 18150; -.
DR Ensembl; ENSMUST00000070215; ENSMUSP00000069578; ENSMUSG00000056209.
DR GeneID; 18150; -.
DR KEGG; mmu:18150; -.
DR UCSC; uc008hrk.1; mouse.
DR CTD; 10360; -.
DR MGI; MGI:894653; Npm3.
DR VEuPathDB; HostDB:ENSMUSG00000056209; -.
DR eggNOG; ENOG502S1E6; Eukaryota.
DR GeneTree; ENSGT00940000158796; -.
DR HOGENOM; CLU_058838_1_0_1; -.
DR InParanoid; Q9CPP0; -.
DR OMA; TEDYFWG; -.
DR OrthoDB; 1485080at2759; -.
DR PhylomeDB; Q9CPP0; -.
DR TreeFam; TF327704; -.
DR BioGRID-ORCS; 18150; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Npm3; mouse.
DR PRO; PR:Q9CPP0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9CPP0; protein.
DR Bgee; ENSMUSG00000056209; Expressed in epiblast (generic) and 63 other tissues.
DR Genevisible; Q9CPP0; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
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; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IDA:MGI.
DR GO; GO:0009303; P:rRNA transcription; IDA:MGI.
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; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75607"
FT CHAIN 2..175
FT /note="Nucleoplasmin-3"
FT /id="PRO_0000219490"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O75607"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75607"
FT MOD_RES 27
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O75607"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75607"
SQ SEQUENCE 175 AA; 19023 MW; 27E9F37CA22838EA CRC64;
MAAGAAAALA FLNQESRARA GGVGGLRVPA PVTMDSFFFG CELSGHTRSF TFKVEEEDDT
EHVLALNMLC LTEGATDECN VVEVVARDHD NQEIAVPVAN LRLSCQPMLS VDDFQLQPPV
TFRLKSGSGP VRITGRHQIV CINNDLSEEE SDDESEEDEI KLCGILPAKK HRGRP
