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Nucleophosmin (NPM) (Nucleolar phosphoprotein B23) (Nucleolar protein NO38) (Numatrin)

 NPM_MOUSE               Reviewed;         292 AA.
Q61937;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 173.
RecName: Full=Nucleophosmin;
Short=NPM;
AltName: Full=Nucleolar phosphoprotein B23;
AltName: Full=Nucleolar protein NO38;
AltName: Full=Numatrin;
Name=Npm1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3219912; DOI=10.1007/BF00303035;
Schmidt-Zachmann M.S., Franke W.W.;
"DNA cloning and amino acid sequence determination of a major
constituent protein of mammalian nucleoli. Correspondence of the
nucleoplasmin-related protein NO38 to mammalian protein B23.";
Chromosoma 96:417-426(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 33-45.
TISSUE=Brain;
Lubec G., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 46-52 AND 266-271, SUBUNIT, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Spleen;
PubMed=9642267; DOI=10.1074/jbc.273.27.17025;
Borggrefe T., Wabl M., Akhmedov A.T., Jessberger R.;
"A B-cell-specific DNA recombination complex.";
J. Biol. Chem. 273:17025-17035(1998).
[6]
INTERACTION WITH EIF2AK2.
PubMed=12882984; DOI=10.1074/jbc.M301392200;
Pang Q., Christianson T.A., Koretsky T., Carlson H., David L.,
Keeble W., Faulkner G.R., Speckhart A., Bagby G.C.;
"Nucleophosmin interacts with and inhibits the catalytic function of
eukaryotic initiation factor 2 kinase PKR.";
J. Biol. Chem. 278:41709-41717(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-125, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67; SER-70; THR-75 AND
SER-125, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-255; LYS-265 AND LYS-271,
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-265, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[14]
INTERACTION WITH LRRC34.
PubMed=24991885; DOI=10.1089/scd.2013.0470;
Luehrig S., Siamishi I., Tesmer-Wolf M., Zechner U., Engel W.,
Nolte J.;
"Lrrc34, a novel nucleolar protein, interacts with npm1 and ncl and
has an impact on pluripotent stem cells.";
Stem Cells Dev. 23:2862-2874(2014).
-!- FUNCTION: Involved in diverse cellular processes such as ribosome
biogenesis, centrosome duplication, protein chaperoning, histone
assembly, cell proliferation, and regulation of tumor suppressors
p53/TP53 and ARF. Binds ribosome presumably to drive ribosome
nuclear export. Associated with nucleolar ribonucleoprotein
structures and bind single-stranded nucleic acids. Acts as a
chaperonin for the core histones H3, H2B and H4. Stimulates APEX1
endonuclease activity on apurinic/apyrimidinic (AP) double-
stranded DNA but inhibits APEX1 endonuclease activity on AP
single-stranded RNA. May exert a control of APEX1 endonuclease
activity within nucleoli devoted to repair AP on rDNA and the
removal of oxidized rRNA molecules. In concert with BRCA2,
regulates centrosome duplication. Regulates centriole duplication:
phosphorylation by PLK2 is able to trigger centriole replication.
Negatively regulates the activation of EIF2AK2/PKR and suppresses
apoptosis through inhibition of EIF2AK2/PKR autophosphorylation.
Antagonizes the inhibitory effect of ATF5 on cell proliferation
and relieves ATF5-induced G2/M blockade. In complex with MYC
enhances the transcription of MYC target genes.
{ECO:0000250|UniProtKB:P06748}.
-!- SUBUNIT: Decamer formed by two pentameric rings associated in a
head-to-head fashion. Disulfide-linked dimers under certain
conditions. Interacts with NSUN2 and SENP3 (By similarity). The
SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts
with the methylated form of RPS10. Interacts (via N-terminal
domain) with APEX1; the interaction is RNA-dependent and decreases
peroxide-damaged cells. Interacts with NEK2. Interacts with ROCK2
and BRCA2 (By similarity). Interacts with RPGR. Interacts with
CENPW (By similarity). Interacts with EIF2AK2/PKR. Interacts with
CEBPA (isoform 4) (By similarity). Interacts with DDX31; this
interaction prevents interaction between NPM1 and HDM2 (By
similarity). Interacts with MYC; competitive with NOP53. Interacts
with NOP53; the interaction is direct and competitive with MYC (By
similarity). Interacts with LRRC34 (PubMed:24991885). Interacts
with RRP1B (By similarity). {ECO:0000250|UniProtKB:P06748,
ECO:0000269|PubMed:12882984, ECO:0000269|PubMed:24991885,
ECO:0000269|PubMed:9642267}.
-!- INTERACTION:
Q00987:MDM2 (xeno); NbExp=2; IntAct=EBI-626362, EBI-389668;
Q9CPP0:Npm3; NbExp=2; IntAct=EBI-626362, EBI-7422336;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000250|UniProtKB:P06748}. Nucleus, nucleoplasm
{ECO:0000250|UniProtKB:P06748}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:P06748}. Note=Generally nucleolar, but is
translocated to the nucleoplasm in case of serum starvation or
treatment with anticancer drugs. Colocalizes with the methylated
form of RPS10 in the granular component (GC) region of the
nucleolus. Colocalized with nucleolin and APEX1 in nucleoli. NEK2
is required for its localization to the centrosome during mitosis
(By similarity). {ECO:0000250|UniProtKB:P06748}.
-!- TISSUE SPECIFICITY: Expressed in B-cells that have been induced to
switch to various Ig isotypes. {ECO:0000269|PubMed:9642267}.
-!- PTM: Acetylated at C-terminal lysine residues, thereby increasing
affinity to histones. {ECO:0000250|UniProtKB:P06748}.
-!- PTM: ADP-ribosylated. {ECO:0000250|UniProtKB:P06748}.
-!- PTM: Phosphorylated at Ser-4 by PLK1 and PLK2. Phosphorylation at
Ser-4 by PLK2 in S phase is required for centriole duplication and
is sufficient to trigger centriole replication. Phosphorylation at
Ser-4 by PLK1 takes place during mitosis. Phosphorylated by CDK2
at Ser-125 and Thr-198. Phosphorylation at Thr-198 may trigger
initiation of centrosome duplication. Phosphorylated by CDK1 at
Thr-198, Thr-217, Thr-232 and Thr-235 during cell mitosis. When
these four sites are phosphorated, RNA-binding activity seem to be
abolished. May be phosphorylated at Ser-70 by NEK2. The Thr-198
phosphorylated form has higher affinity for ROCK2 (By similarity).
{ECO:0000250|UniProtKB:P06748}.
-!- PTM: Sumoylated by ARF. {ECO:0000250|UniProtKB:P06748}.
-!- PTM: Ubiquitinated. Ubiquitination leads to proteasomal
degradation. Deubiquitinated by USP36.
{ECO:0000250|UniProtKB:P06748}.
-!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
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EMBL; M33212; AAA39801.1; -; mRNA.
EMBL; AK028253; BAC25844.1; -; mRNA.
EMBL; BC054755; AAH54755.1; -; mRNA.
CCDS; CCDS24532.1; -.
PIR; I52858; I52858.
RefSeq; NP_032748.1; NM_008722.3.
UniGene; Mm.485384; -.
PDB; 4N8M; X-ray; 1.80 A; A/B/C/D/E=1-130.
PDBsum; 4N8M; -.
ProteinModelPortal; Q61937; -.
SMR; Q61937; -.
BioGrid; 201823; 44.
CORUM; Q61937; -.
IntAct; Q61937; 12.
MINT; Q61937; -.
STRING; 10090.ENSMUSP00000075067; -.
ChEMBL; CHEMBL5386; -.
iPTMnet; Q61937; -.
PhosphoSitePlus; Q61937; -.
SwissPalm; Q61937; -.
EPD; Q61937; -.
MaxQB; Q61937; -.
PaxDb; Q61937; -.
PRIDE; Q61937; -.
Ensembl; ENSMUST00000075641; ENSMUSP00000075067; ENSMUSG00000057113.
GeneID; 18148; -.
KEGG; mmu:18148; -.
UCSC; uc007ikd.2; mouse.
CTD; 4869; -.
MGI; MGI:106184; Npm1.
eggNOG; ENOG410IHZM; Eukaryota.
eggNOG; ENOG4111IKX; LUCA.
GeneTree; ENSGT00440000034554; -.
HOGENOM; HOG000013061; -.
HOVERGEN; HBG001860; -.
InParanoid; Q61937; -.
KO; K11276; -.
OMA; KMQASVD; -.
OrthoDB; EOG091G0NLY; -.
PhylomeDB; Q61937; -.
TreeFam; TF327704; -.
ChiTaRS; Gja1; mouse.
PRO; PR:Q61937; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000057113; -.
CleanEx; MM_NPM1; -.
ExpressionAtlas; Q61937; baseline and differential.
Genevisible; Q61937; MM.
GO; GO:0005813; C:centrosome; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0001652; C:granular component; IDA:MGI.
GO; GO:0015934; C:large ribosomal subunit; IDA:MGI.
GO; GO:0016363; C:nuclear matrix; ISO:MGI.
GO; GO:0016607; C:nuclear speck; IDA:MGI.
GO; GO:0005730; C:nucleolus; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
GO; GO:0015935; C:small ribosomal subunit; IDA:MGI.
GO; GO:0031616; C:spindle pole centrosome; ISO:MGI.
GO; GO:0033613; F:activating transcription factor binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0001047; F:core promoter binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0042393; F:histone binding; ISO:MGI.
GO; GO:0051059; F:NF-kappaB binding; ISS:UniProtKB.
GO; GO:0002039; F:p53 binding; ISO:MGI.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0043422; F:protein kinase B binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:MGI.
GO; GO:0043023; F:ribosomal large subunit binding; ISO:MGI.
GO; GO:0043024; F:ribosomal small subunit binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; IDA:MGI.
GO; GO:0019843; F:rRNA binding; IDA:MGI.
GO; GO:0030957; F:Tat protein binding; ISO:MGI.
GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
GO; GO:0003300; P:cardiac muscle hypertrophy; IEA:Ensembl.
GO; GO:0007569; P:cell aging; ISS:UniProtKB.
GO; GO:0006884; P:cell volume homeostasis; IDA:MGI.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071394; P:cellular response to testosterone stimulus; IEA:Ensembl.
GO; GO:0034644; P:cellular response to UV; ISO:MGI.
GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISO:MGI.
GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0010826; P:negative regulation of centrosome duplication; ISO:MGI.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IGI:MGI.
GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0006913; P:nucleocytoplasmic transport; IDA:MGI.
GO; GO:0006334; P:nucleosome assembly; ISO:MGI.
GO; GO:0043085; P:positive regulation of catalytic activity; ISO:MGI.
GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:0031328; P:positive regulation of cellular biosynthetic process; IDA:MGI.
GO; GO:0010825; P:positive regulation of centrosome duplication; IGI:MGI.
GO; GO:0051054; P:positive regulation of DNA metabolic process; ISO:MGI.
GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; ISO:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:MGI.
GO; GO:1904751; P:positive regulation of protein localization to nucleolus; IMP:MGI.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:CAFA.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
GO; GO:0010608; P:posttranscriptional regulation of gene expression; IMP:MGI.
GO; GO:0051259; P:protein complex oligomerization; ISO:MGI.
GO; GO:0051260; P:protein homooligomerization; IDA:MGI.
GO; GO:0008104; P:protein localization; IMP:MGI.
GO; GO:0050821; P:protein stabilization; IMP:CAFA.
GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
GO; GO:0001558; P:regulation of cell growth; IDA:MGI.
GO; GO:0046599; P:regulation of centriole replication; ISS:UniProtKB.
GO; GO:0010824; P:regulation of centrosome duplication; IMP:MGI.
GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IGI:MGI.
GO; GO:0060735; P:regulation of eIF2 alpha phosphorylation by dsRNA; ISS:UniProtKB.
GO; GO:0032071; P:regulation of endodeoxyribonuclease activity; ISS:UniProtKB.
GO; GO:0060699; P:regulation of endoribonuclease activity; ISS:UniProtKB.
GO; GO:1902629; P:regulation of mRNA stability involved in cellular response to UV; ISO:MGI.
GO; GO:0043523; P:regulation of neuron apoptotic process; ISO:MGI.
GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
GO; GO:0042273; P:ribosomal large subunit biogenesis; IDA:MGI.
GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:MGI.
GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:MGI.
GO; GO:0000056; P:ribosomal small subunit export from nucleus; IDA:MGI.
GO; GO:0006407; P:rRNA export from nucleus; IDA:MGI.
GO; GO:0009303; P:rRNA transcription; ISO:MGI.
Gene3D; 1.10.10.2100; -; 1.
InterPro; IPR032569; NPM1_C.
InterPro; IPR038101; NPM1_C_sf.
InterPro; IPR004301; Nucleoplasmin.
InterPro; IPR024057; Nucleoplasmin_core_dom.
InterPro; IPR036824; Nucleoplasmin_core_dom_sf.
PANTHER; PTHR22747; PTHR22747; 1.
Pfam; PF16276; NPM1-C; 1.
Pfam; PF03066; Nucleoplasmin; 1.
SUPFAM; SSF69203; SSF69203; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Chaperone;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Disulfide bond; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; Ubl conjugation.
CHAIN 1 292 Nucleophosmin.
/FTId=PRO_0000219482.
REGION 1 185 Required for interaction with SENP3.
{ECO:0000250}.
REGION 1 117 Necessary for interaction with APEX1.
{ECO:0000250}.
REGION 241 292 Required for nucleolar localization.
{ECO:0000250}.
MOTIF 152 157 Nuclear localization signal.
{ECO:0000255}.
MOTIF 190 196 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 1 9 Met-rich.
COMPBIAS 120 132 Asp/Glu-rich (acidic).
COMPBIAS 158 187 Asp/Glu-rich (highly acidic).
SITE 55 55 Interaction between pentamers.
{ECO:0000250}.
SITE 80 80 Interaction between pentamers.
{ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 4 4 Phosphoserine; by PLK1 and PLK2.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 32 32 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 67 67 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 70 70 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 75 75 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 95 95 Phosphothreonine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 150 150 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 154 154 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 198 198 Phosphothreonine; by CDK1 and CDK2.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 206 206 ADP-ribosylserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 211 211 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 217 217 Phosphothreonine; by CDK1. {ECO:0000250}.
MOD_RES 225 225 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 227 227 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 228 228 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 232 232 Phosphothreonine; by CDK1.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 235 235 Phosphothreonine; by CDK1.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 248 248 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 255 255 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 265 265 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 265 265 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 271 271 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 277 277 Phosphothreonine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 290 290 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 141 141 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 150 150 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 214 214 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 228 228 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 246 246 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 246 246 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 248 248 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 255 255 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 255 255 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 261 261 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 261 261 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 265 265 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 265 265 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 271 271 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
STRAND 15 24 {ECO:0000244|PDB:4N8M}.
STRAND 29 31 {ECO:0000244|PDB:4N8M}.
HELIX 37 39 {ECO:0000244|PDB:4N8M}.
STRAND 40 49 {ECO:0000244|PDB:4N8M}.
STRAND 58 65 {ECO:0000244|PDB:4N8M}.
STRAND 69 80 {ECO:0000244|PDB:4N8M}.
TURN 81 83 {ECO:0000244|PDB:4N8M}.
STRAND 84 94 {ECO:0000244|PDB:4N8M}.
STRAND 96 104 {ECO:0000244|PDB:4N8M}.
STRAND 109 117 {ECO:0000244|PDB:4N8M}.
SEQUENCE 292 AA; 32560 MW; E68750C549ED25E6 CRC64;
MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV
EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE
EDAESEDEDE EDVKLLGMSG KRSAPGGGNK VPQKKVKLDE DDEDDDEDDE DDEDDDDDDF
DEEETEEKVP VKKSVRDTPA KNAQKSNQNG KDLKPSTPRS KGQESFKKQE KTPKTPKGPS
SVEDIKAKMQ ASIEKGGSLP KVEAKFINYV KNCFRMTDQE AIQDLWQWRK SL


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