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 08-JUN-2016, entry version 96. DE RecName: Full=Nucleoplasmin-2; GN Name=Npm2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE RP 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: Core histones chaperone involved in chromatin CC reprogramming, specially during fertilization and early embryonic CC development. Probably involved in sperm DNA decondensation during CC fertilization. CC -!- SUBUNIT: Homopentamer, when bound to H2A-H2B dimers only. CC Homodecamer of two stacked pentamers, when bound to H2A-H2B dimers CC and H3-H4 tetramers simultaneously (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12714744}. CC Note=Found in the oocyte nucleus before nuclear membrane CC breakdown, after which it is redistributed to the cytoplasm. CC -!- TISSUE SPECIFICITY: Ovary specific. {ECO:0000269|PubMed:12714744}. CC -!- DOMAIN: The acidic tract A2 mediates histone binding. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}. 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; 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_006519145.2. DR RefSeq; XP_006519209.1; XM_006519146.2. DR RefSeq; XP_006519210.1; XM_006519147.2. DR RefSeq; XP_011243392.1; XM_011245090.1. DR RefSeq; XP_011243393.1; XM_011245091.1. DR UniGene; Mm.347749; -. DR ProteinModelPortal; Q80W85; -. DR SMR; Q80W85; 17-117. DR BioGrid; 236605; 1. DR STRING; 10090.ENSMUSP00000057365; -. DR iPTMnet; Q80W85; -. DR PhosphoSite; Q80W85; -. DR REPRODUCTION-2DPAGE; Q80W85; -. DR PaxDb; Q80W85; -. DR PRIDE; Q80W85; -. 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 eggNOG; ENOG410IYZ7; Eukaryota. DR eggNOG; ENOG410XY21; LUCA. DR GeneTree; ENSGT00440000034554; -. DR HOGENOM; HOG000056457; -. DR HOVERGEN; HBG045601; -. DR InParanoid; Q80W85; -. DR KO; K11277; -. DR OMA; EKRTWTF; -. DR OrthoDB; EOG7ZWD4F; -. DR PhylomeDB; Q80W85; -. DR TreeFam; TF327704; -. DR PRO; PR:Q80W85; -. DR Proteomes; UP000000589; Chromosome 14. DR Bgee; Q80W85; -. DR CleanEx; MM_NPM2; -. DR GO; GO:0000789; C:cytoplasmic chromatin; ISS:UniProtKB. DR GO; GO:0000790; C:nuclear chromatin; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB. DR GO; GO:0009790; P:embryo development; ISS:UniProtKB. DR GO; GO:0009994; P:oocyte differentiation; ISS:UniProtKB. DR GO; GO:0043085; P:positive regulation of catalytic activity; IEA:Ensembl. DR GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl. DR GO; GO:0045836; P:positive regulation of meiotic nuclear division; ISS:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl. DR GO; GO:0007096; P:regulation of exit from mitosis; ISS:UniProtKB. DR GO; GO:0007338; P:single fertilization; ISS:UniProtKB. DR Gene3D; 2.60.120.340; -; 1. DR InterPro; IPR004301; Nucleoplasmin. DR InterPro; IPR024057; Nucleoplasmin_core_dom. DR PANTHER; PTHR22747; PTHR22747; 1. DR SUPFAM; SSF69203; SSF69203; 1. PE 2: Evidence at transcript level; KW Chaperone; Chromatin regulator; Complete proteome; KW Developmental protein; Fertilization; Nucleus; Reference proteome. FT CHAIN 1 207 Nucleoplasmin-2. FT /FTId=PRO_0000219488. FT REGION 129 152 Acidic tract A2. {ECO:0000250}. FT MOTIF 165 180 Bipartite nuclear localization signal. FT {ECO:0000250}. FT COMPBIAS 128 141 Poly-Glu. FT COMPBIAS 168 171 Poly-Lys. FT SITE 57 57 Interaction between pentamers. FT {ECO:0000250}. FT SITE 84 84 Interaction between pentamers. FT {ECO:0000250}. FT CONFLICT 196 196 S -> F (in Ref. 2; BAC35815). FT {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 //