ID NPM2_HUMAN Reviewed; 214 AA. AC Q86SE8; B3KSU0; D3DSQ8; Q6NVH6; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 154. DE RecName: Full=Nucleoplasmin-2; GN Name=NPM2; 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] (ISOFORM 1). 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] (ISOFORM 1). RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [6] RP REVIEW ON FUNCTION. RX PubMed=17187372; DOI=10.1002/bies.20512; RA Frehlick L.J., Eirin-Lopez J.M., Ausio J.; RT "New insights into the nucleophosmin/nucleoplasmin family of nuclear RT chaperones."; RL Bioessays 29:49-59(2007). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 14-122, FUNCTION, DOMAIN, AND RP SUBUNIT. RX PubMed=21863821; DOI=10.1021/bi2006652; RA Platonova O., Akey I.V., Head J.F., Akey C.W.; RT "Crystal structure and function of human nucleoplasmin (npm2): a histone RT chaperone in oocytes and embryos."; RL Biochemistry 50:8078-8089(2011). 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 {ECO:0000269|PubMed:21863821}. 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. {ECO:0000269|PubMed:21863821}. CC -!- INTERACTION: CC Q86SE8; P06748: NPM1; NbExp=6; IntAct=EBI-6658150, EBI-78579; CC Q86SE8; O75607: NPM3; NbExp=5; IntAct=EBI-6658150, EBI-721544; CC Q86SE8; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-6658150, EBI-742388; CC Q86SE8; Q9H190: SDCBP2; NbExp=4; IntAct=EBI-6658150, EBI-742426; CC Q86SE8-2; P06748: NPM1; NbExp=5; IntAct=EBI-12193061, EBI-78579; CC Q86SE8-2; P06748-2: NPM1; NbExp=4; IntAct=EBI-12193061, EBI-354154; CC Q86SE8-2; Q96S99: PLEKHF1; NbExp=3; IntAct=EBI-12193061, EBI-745767; CC Q86SE8-2; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-12193061, EBI-742388; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Found in the oocyte CC nucleus before nuclear membrane breakdown, after which it is CC redistributed to the cytoplasm. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q86SE8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q86SE8-2; Sequence=VSP_054261; CC -!- DOMAIN: The acidic tract A2 mediates histone binding. CC {ECO:0000269|PubMed:21863821}. 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; AY262113; AAP33134.1; -; mRNA. DR EMBL; AY262114; AAP33135.1; -; mRNA. DR EMBL; AK094267; BAG52852.1; -; mRNA. DR EMBL; AC091171; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471080; EAW63731.1; -; Genomic_DNA. DR EMBL; CH471080; EAW63732.1; -; Genomic_DNA. DR EMBL; BC068078; AAH68078.1; -; mRNA. DR CCDS; CCDS6018.1; -. [Q86SE8-1] DR CCDS; CCDS75703.1; -. [Q86SE8-2] DR RefSeq; NP_001273609.1; NM_001286680.1. [Q86SE8-1] DR RefSeq; NP_001273610.1; NM_001286681.1. [Q86SE8-2] DR RefSeq; NP_877724.1; NM_182795.1. [Q86SE8-1] DR RefSeq; XP_011542664.1; XM_011544362.2. DR RefSeq; XP_011542665.1; XM_011544363.2. DR RefSeq; XP_016868437.1; XM_017012948.1. DR RefSeq; XP_016868438.1; XM_017012949.1. DR PDB; 3T30; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J=14-122. DR PDBsum; 3T30; -. DR AlphaFoldDB; Q86SE8; -. DR SMR; Q86SE8; -. DR BioGRID; 115641; 12. DR IntAct; Q86SE8; 11. DR STRING; 9606.ENSP00000381032; -. DR GlyGen; Q86SE8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q86SE8; -. DR PhosphoSitePlus; Q86SE8; -. DR BioMuta; NPM2; -. DR DMDM; 37537936; -. DR MassIVE; Q86SE8; -. DR MaxQB; Q86SE8; -. DR PaxDb; 9606-ENSP00000381032; -. DR PeptideAtlas; Q86SE8; -. DR ProteomicsDB; 66718; -. DR ProteomicsDB; 69576; -. [Q86SE8-1] DR Antibodypedia; 22452; 123 antibodies from 23 providers. DR DNASU; 10361; -. DR Ensembl; ENST00000289820.10; ENSP00000289820.6; ENSG00000158806.14. [Q86SE8-1] DR Ensembl; ENST00000381530.9; ENSP00000370941.5; ENSG00000158806.14. [Q86SE8-2] DR Ensembl; ENST00000397940.5; ENSP00000381032.1; ENSG00000158806.14. [Q86SE8-1] DR Ensembl; ENST00000518119.6; ENSP00000427741.1; ENSG00000158806.14. [Q86SE8-1] DR Ensembl; ENST00000521157.5; ENSP00000429413.1; ENSG00000158806.14. [Q86SE8-1] DR Ensembl; ENST00000615914.1; ENSP00000481018.1; ENSG00000158806.14. [Q86SE8-2] DR Ensembl; ENST00000621538.4; ENSP00000481077.1; ENSG00000158806.14. [Q86SE8-1] DR GeneID; 10361; -. DR KEGG; hsa:10361; -. DR MANE-Select; ENST00000518119.6; ENSP00000427741.1; NM_001286680.2; NP_001273609.1. DR UCSC; uc003xac.5; human. [Q86SE8-1] DR AGR; HGNC:7930; -. DR CTD; 10361; -. DR DisGeNET; 10361; -. DR GeneCards; NPM2; -. DR HGNC; HGNC:7930; NPM2. DR HPA; ENSG00000158806; Tissue enhanced (brain, parathyroid gland). DR MIM; 608073; gene. DR neXtProt; NX_Q86SE8; -. DR OpenTargets; ENSG00000158806; -. DR PharmGKB; PA31732; -. DR VEuPathDB; HostDB:ENSG00000158806; -. DR eggNOG; ENOG502S0N8; Eukaryota. DR GeneTree; ENSGT00940000161418; -. DR HOGENOM; CLU_058838_2_0_1; -. DR InParanoid; Q86SE8; -. DR OMA; GQECYES; -. DR OrthoDB; 4640673at2759; -. DR PhylomeDB; Q86SE8; -. DR TreeFam; TF327704; -. DR PathwayCommons; Q86SE8; -. DR Reactome; R-HSA-9821993; Replacement of protamines by nucleosomes in the male pronucleus. DR SignaLink; Q86SE8; -. DR BioGRID-ORCS; 10361; 10 hits in 1148 CRISPR screens. DR ChiTaRS; NPM2; human. DR GenomeRNAi; 10361; -. DR Pharos; Q86SE8; Tbio. DR PRO; PR:Q86SE8; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q86SE8; Protein. DR Bgee; ENSG00000158806; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 176 other cell types or tissues. DR ExpressionAtlas; Q86SE8; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA: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:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central. DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl. DR GO; GO:0042393; F:histone binding; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0001824; P:blastocyst development; IMP:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB. DR GO; GO:0009994; P:oocyte differentiation; IEP:UniProtKB. DR GO; GO:0045740; P:positive regulation of DNA replication; IBA:GO_Central. DR GO; GO:0045836; P:positive regulation of meiotic nuclear division; IMP:UniProtKB. DR GO; GO:0007096; P:regulation of exit from mitosis; IMP:UniProtKB. DR GO; GO:0007338; P:single fertilization; IMP:UniProtKB. DR Gene3D; 2.60.120.340; Nucleoplasmin core domain; 1. DR InterPro; IPR004301; Nucleoplasmin. DR InterPro; IPR024057; Nucleoplasmin_core_dom. DR InterPro; IPR036824; Nucleoplasmin_core_dom_sf. DR PANTHER; PTHR22747; NUCLEOPLASMIN; 1. DR PANTHER; PTHR22747:SF14; NUCLEOPLASMIN-2; 1. DR Pfam; PF03066; Nucleoplasmin; 1. DR SUPFAM; SSF69203; Nucleoplasmin-like core domain; 1. DR Genevisible; Q86SE8; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chaperone; Chromatin regulator; KW Developmental protein; Fertilization; Nucleus; Reference proteome. FT CHAIN 1..214 FT /note="Nucleoplasmin-2" FT /id="PRO_0000219487" FT REGION 119..214 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 129..152 FT /note="Acidic tract A2" FT MOTIF 165..180 FT /note="Bipartite nuclear localization signal" FT /evidence="ECO:0000250" FT COMPBIAS 125..154 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 175..201 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 57 FT /note="Interaction between pentamers" FT SITE 84 FT /note="Interaction between pentamers" FT VAR_SEQ 123..214 FT /note="ASDLTWEEEEEEEGEEEEEEEEDDEDEDADISLEEQSPVKQVKRLVPQKQAS FT VAKKKKLEKEEEEIRASVRDKSPVKKAKATARAKKPGFKK -> KKAGKRRRGNKSQR FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054261" FT STRAND 16..23 FT /evidence="ECO:0007829|PDB:3T30" FT STRAND 29..32 FT /evidence="ECO:0007829|PDB:3T30" FT STRAND 43..51 FT /evidence="ECO:0007829|PDB:3T30" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:3T30" FT STRAND 78..84 FT /evidence="ECO:0007829|PDB:3T30" FT TURN 85..87 FT /evidence="ECO:0007829|PDB:3T30" FT STRAND 90..98 FT /evidence="ECO:0007829|PDB:3T30" FT STRAND 100..109 FT /evidence="ECO:0007829|PDB:3T30" FT STRAND 113..120 FT /evidence="ECO:0007829|PDB:3T30" SQ SEQUENCE 214 AA; 24152 MW; EAE3BEF1DC8E1CC1 CRC64; MNLSSASSTE EKAVTTVLWG CELSQERRTW TFRPQLEGKQ SCRLLLHTIC LGEKAKEEMH RVEILPPANQ EDKKMQPVTI ASLQASVLPM VSMVGVQLSP PVTFQLRAGS GPVFLSGQER YEASDLTWEE EEEEEGEEEE EEEEDDEDED ADISLEEQSP VKQVKRLVPQ KQASVAKKKK LEKEEEEIRA SVRDKSPVKK AKATARAKKP GFKK //