NPM2_HUMAN
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 03-AUG-2022, entry version 146.
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}.
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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. [Q86SE8-1]
DR RefSeq; XP_011542665.1; XM_011544363.2. [Q86SE8-1]
DR RefSeq; XP_016868437.1; XM_017012948.1. [Q86SE8-1]
DR RefSeq; XP_016868438.1; XM_017012949.1. [Q86SE8-1]
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 iPTMnet; Q86SE8; -.
DR PhosphoSitePlus; Q86SE8; -.
DR BioMuta; NPM2; -.
DR DMDM; 37537936; -.
DR MassIVE; Q86SE8; -.
DR MaxQB; Q86SE8; -.
DR PaxDb; Q86SE8; -.
DR PeptideAtlas; Q86SE8; -.
DR PRIDE; Q86SE8; -.
DR ProteomicsDB; 66718; -.
DR ProteomicsDB; 69576; -. [Q86SE8-1]
DR Antibodypedia; 22452; 98 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 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; 1485080at2759; -.
DR PhylomeDB; Q86SE8; -.
DR TreeFam; TF327704; -.
DR PathwayCommons; Q86SE8; -.
DR SignaLink; Q86SE8; -.
DR BioGRID-ORCS; 10361; 9 hits in 1071 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 right frontal lobe and 174 other tissues.
DR ExpressionAtlas; Q86SE8; baseline and differential.
DR Genevisible; Q86SE8; HS.
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:0042393; F:histone binding; IBA:GO_Central.
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 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 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
