NPM2_MOUSE
ID NPM2_MOUSE Reviewed; 207 AA.
AC Q80W85; Q8BW23;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Nucleoplasmin-2;
GN Name=Npm2;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=129S6/SvEv;
RX PubMed=12714744; DOI=10.1126/science.1081813;
RA Burns K.H., Viveiros M.M., Ren Y., Wang P., DeMayo F.J., Frail D.E.,
RA Eppig J.J., Matzuk M.M.;
RT "Roles of NPM2 in chromatin and nucleolar organization in oocytes and
RT embryos.";
RL Science 300:633-636(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary;
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).
CC -!- FUNCTION: Core histones chaperone involved in chromatin reprogramming,
CC specially during fertilization and early embryonic development.
CC Probably involved in sperm DNA decondensation during fertilization.
CC -!- SUBUNIT: Homopentamer, when bound to H2A-H2B dimers only. Homodecamer
CC of two stacked pentamers, when bound to H2A-H2B dimers and H3-H4
CC tetramers simultaneously (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12714744}. Note=Found
CC in the oocyte nucleus before nuclear membrane breakdown, after which it
CC is redistributed to the cytoplasm.
CC -!- TISSUE SPECIFICITY: Ovary specific. {ECO:0000269|PubMed:12714744}.
CC -!- DOMAIN: The acidic tract A2 mediates histone binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
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DR EMBL; AY262112; AAP33133.1; -; mRNA.
DR EMBL; AK054533; BAC35815.1; -; mRNA.
DR CCDS; CCDS27261.1; -.
DR RefSeq; NP_851990.2; NM_181345.3.
DR RefSeq; XP_006519206.1; XM_006519143.2.
DR RefSeq; XP_006519208.1; XM_006519145.3.
DR RefSeq; XP_006519209.1; XM_006519146.3.
DR RefSeq; XP_006519210.1; XM_006519147.2.
DR RefSeq; XP_011243393.1; XM_011245091.2.
DR RefSeq; XP_017171550.1; XM_017316061.1.
DR AlphaFoldDB; Q80W85; -.
DR SMR; Q80W85; -.
DR BioGRID; 236605; 1.
DR STRING; 10090.ENSMUSP00000057365; -.
DR iPTMnet; Q80W85; -.
DR PhosphoSitePlus; Q80W85; -.
DR REPRODUCTION-2DPAGE; Q80W85; -.
DR PaxDb; Q80W85; -.
DR PRIDE; Q80W85; -.
DR ProteomicsDB; 293713; -.
DR Antibodypedia; 22452; 98 antibodies from 23 providers.
DR DNASU; 328440; -.
DR Ensembl; ENSMUST00000062629; ENSMUSP00000057365; ENSMUSG00000047911.
DR GeneID; 328440; -.
DR KEGG; mmu:328440; -.
DR UCSC; uc007uot.2; mouse.
DR CTD; 10361; -.
DR MGI; MGI:1890811; Npm2.
DR VEuPathDB; HostDB:ENSMUSG00000047911; -.
DR eggNOG; ENOG502S0N8; Eukaryota.
DR GeneTree; ENSGT00940000161418; -.
DR HOGENOM; CLU_058838_2_0_1; -.
DR InParanoid; Q80W85; -.
DR OMA; GQECYES; -.
DR OrthoDB; 1485080at2759; -.
DR PhylomeDB; Q80W85; -.
DR TreeFam; TF327704; -.
DR BioGRID-ORCS; 328440; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Npm2; mouse.
DR PRO; PR:Q80W85; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q80W85; protein.
DR Bgee; ENSMUSG00000047911; Expressed in primary oocyte and 70 other tissues.
DR ExpressionAtlas; Q80W85; baseline and differential.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0001824; P:blastocyst development; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IMP:MGI.
DR GO; GO:0009994; P:oocyte differentiation; ISS:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO: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:0045836; P:positive regulation of meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0007096; P:regulation of exit from mitosis; ISS:UniProtKB.
DR GO; GO:0007338; P:single fertilization; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Chaperone; Chromatin regulator; Developmental protein; Fertilization;
KW Nucleus; Reference proteome.
FT CHAIN 1..207
FT /note="Nucleoplasmin-2"
FT /id="PRO_0000219488"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..152
FT /note="Acidic tract A2"
FT /evidence="ECO:0000250"
FT MOTIF 165..180
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 121..146
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 57
FT /note="Interaction between pentamers"
FT /evidence="ECO:0000250"
FT SITE 84
FT /note="Interaction between pentamers"
FT /evidence="ECO:0000250"
FT CONFLICT 196
FT /note="S -> F (in Ref. 2; BAC35815)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 207 AA; 23309 MW; 8B8A8931F85032EE CRC64;
MSRHSTSSVT ETTAKNMLWG SELNQEKQTC TFRGQGEKKD SCKLLLSTIC LGEKAKEEVN
RVEVLSQEGR KPPITIATLK ASVLPMVTVS GIELSPPVTF RLRTGSGPVF LSGLECYETS
DLTWEDDEEE EEEEEEEDED EDADISLEEI PVKQVKRVAP QKQMSIAKKK KVEKEEDETV
VRPSPQDKSP WKKEKSTPRA KKPVTKK
