NPM1

NPM1
Estruturas disponíveis
PDB	Pesquisa Human UniProt: PDBe RCSB
Lista de códigos id do PDB
	2LLH, 2P1B, 2VXD
Identificadores
Nomes alternativos	NPM1
IDs externos	OMIM: 164040 HomoloGene: 81697 GeneCards: NPM1
Targeted by Drug
	ceritinib
Ontologia genética
Função molecular	• ribosomal large subunit binding; • protein homodimerization activity; • ribosomal small subunit binding; • unfolded protein binding; • GO:0001105 transcription coactivator activity; • protein kinase inhibitor activity; • GO:0031493 histone binding; • Tat protein binding; • NF-kappaB binding; • GO:0001948, GO:0016582 ligação a proteínas plasmáticas; • RNA binding; • protein heterodimerization activity; • nucleic acid binding; • protein kinase binding; • transcription factor binding; • rRNA binding; • protein N-terminus binding; • chromatin binding;
Componente celular	• citoplasma; • membrane; • focal adhesion; • spindle pole centrosome; • cariolinfa; • centro organizador dos microtúbulos; • nucléolo; • citoesqueleto; • núcleo celular; • protein-DNA complex; • granular component; • centrossoma; • citosol; • large ribosomal subunit; • small ribosomal subunit; • nuclear speck; • GO:0009327 complexo macromolecular; • partículas de ribonucleoproteínas heterogéneas;
Processo biológico	• centrosome cycle; • regulation of eIF2 alpha phosphorylation by dsRNA; • positive regulation of cell cycle G2/M phase transition; • negative regulation of centrosome duplication; • regulation of centriole replication; • response to stress; • positive regulation of translation; • GO:0061641 CENP-A containing chromatin assembly; • GO:0060469, GO:0009371 positive regulation of transcription, DNA-templated; • positive regulation of NF-kappaB transcription factor activity; • protein complex oligomerization; • negative regulation of protein kinase activity by regulation of protein phosphorylation; • regulation of endodeoxyribonuclease activity; • regulation of endoribonuclease activity; • ribosome assembly; • intracellular protein transport; • GO:0100026 reparo de ADN; • GO:0072468 transdução de sinal; • negative regulation of cell population proliferation; • nucleosome assembly; • GO:0022415 viral process; • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; • GO:0044324, GO:0003256, GO:1901213, GO:0046019, GO:0046020, GO:1900094, GO:0061216, GO:0060994, GO:1902064, GO:0003258, GO:0072212 regulation of transcription by RNA polymerase II; • cellular response to UV; • ribosomal large subunit export from nucleus; • ribosomal small subunit export from nucleus; • rRNA export from nucleus; • cell volume homeostasis; • nucleocytoplasmic transport; • GO:0034613 protein localization; • positive regulation of cell population proliferation; • posttranscriptional regulation of gene expression; • negative regulation of gene expression; • regulation of centrosome duplication; • positive regulation of centrosome duplication; • Crescimento celular; • positive regulation of cellular biosynthetic process; • positive regulation of protein ubiquitination; • regulation of protein stability; • ribosomal large subunit biogenesis; • ribosomal small subunit biogenesis; • negative regulation of apoptotic process; • regulation of DNA damage response, signal transduction by p53 class mediator; • positive regulation of protein kinase activity; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II; • negative regulation of mRNA splicing, via spliceosome; • protein stabilization; • protein homooligomerization; • regulation of cell cycle; • positive regulation of protein localization to nucleolus; • chromatin remodeling; • regulation of mRNA stability involved in cellular response to UV;
	Sources:Amigo / QuickGO
Padrão de expressão RNA
	Mais dados de referência de expressão
Ortólogos
	4869
	n/a
	ENSG00000181163
	n/a
	P06748
	n/a
NM_001037738; NM_002520; NM_199185; NM_001355006; NM_001355009;
	NM_001355007; NM_001355010
	n/a
NP_001032827; NP_002511; NP_954654; NP_001341935; NP_001341938;
	NP_001341936; NP_001341939
	n/a
	Wikidata
Ver/Editar Humano

A nucleofosfomina (fosfoproteína nucleolar B23, numatrina ou NPM1) é uma proteína nucleolar ubiquamente expressada que transloca-se entre o núcleo celular e o citoplasma. Está implicada em múltiplas funções celulares, incluindo codificação proteica ribossomal e transporte, controle da duplicação do centrossomo e regulação do gene supressor de tumor ARF.

Mutações que relocam a NPM1 do núcleo para o citoplasma estão associadas com o desenvolvimento da leucemia mielóide aguda.

Referências

↑ «Drogas que interagem fisicamente com Nucleophosmin 1 ver/editar referências no wikidata»
↑ «Human PubMed Reference:»
↑ Schneider F; et al. (maio de 2009). «NPM1 but not FLT3-ITD mutations predict early blast cell clearance and CR rate in patients with normal karyotype AML (NK-AML) or high-risk myelodysplastic syndrome (MDS)». Blood. 113 (21). pp. 5250–3

Leitura de apoio

Yun C, Wang Y, Mukhopadhyay D; et al. (2008). «Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases.». J Cell Biol. 183 (4): 589–95. PMC 2582899. PMID 19015314. doi:10.1083/jcb.200807185
Haindl M, Harasim T, Eick D; et al. (2008). «The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of nucleophosmin and is required for rRNA processing.». EMBO reports. 9 (3): 273–279. doi:10.1038/embor.2008.3
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Chan PK, Chan WY, Yung BY; et al. (1986). «Amino acid sequence of a specific antigenic peptide of protein B23.». J. Biol. Chem. 261 (30): 14335–41. PMID 2429957
Zhang XX, Thomis DC, Samuel CE (1989). «Isolation and characterization of a molecular cDNA clone of a human mRNA from interferon-treated cells encoding nucleolar protein B23, numatrin.». Biochem. Biophys. Res. Commun. 164 (1): 176–84. PMID 2478125. doi:10.1016/0006-291X(89)91699-9
Hale TK, Mansfield BC (1990). «Nucleotide sequence of a cDNA clone representing a third allele of human protein B23.». Nucleic Acids Res. 17 (23). 10112 páginas. PMC 335249. PMID 2602120
Chan WY, Liu QR, Borjigin J; et al. (1989). «Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth.». Biochemistry. 28 (3): 1033–9. PMID 2713355. doi:10.1021/bi00429a017
Li XZ, McNeilage LJ, Whittingham S (1989). «The nucleotide sequence of a human cDNA encoding the highly conserved nucleolar phosphoprotein B23.». Biochem. Biophys. Res. Commun. 163 (1): 72–8. PMID 2775293. doi:10.1016/0006-291X(89)92100-1
Chan PK, Aldrich M, Cook RG, Busch H (1986). «Amino acid sequence of protein B23 phosphorylation site.». J. Biol. Chem. 261 (4): 1868–72. PMID 3944116
Bocker T, Bittinger A, Wieland W; et al. (1995). «In vitro and ex vivo expression of nucleolar proteins B23 and p120 in benign and malignant epithelial lesions of the prostate.». Mod. Pathol. 8 (3): 226–31. PMID 7542384
Dundr M, Leno GH, Hammarskjöld ML; et al. (1995). «The roles of nucleolar structure and function in the subcellular location of the HIV-1 Rev protein.». J. Cell. Sci. 108 ( Pt 8): 2811–23. PMID 7593322
Miyazaki Y, Takamatsu T, Nosaka T; et al. (1995). «The cytotoxicity of human immunodeficiency virus type 1 Rev: implications for its interaction with the nucleolar protein B23.». Exp. Cell Res. 219 (1): 93–101. PMID 7628555. doi:10.1006/excr.1995.1209
Szebeni A, Herrera JE, Olson MO (1995). «Interaction of nucleolar protein B23 with peptides related to nuclear localization signals.». Biochemistry. 34 (25): 8037–42. PMID 7794916. doi:10.1021/bi00025a009
Kato S, Sekine S, Oh SW; et al. (1995). «Construction of a human full-length cDNA bank.». Gene. 150 (2): 243–50. PMID 7821789. doi:10.1016/0378-1119(94)90433-2
Marasco WA, Szilvay AM, Kalland KH; et al. (1995). «Spatial association of HIV-1 tat protein and the nucleolar transport protein B23 in stably transfected Jurkat T-cells.». Arch. Virol. 139 (1-2): 133–54. PMID 7826206. doi:10.1007/BF01309460
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[1] «Drogas que interagem fisicamente com Nucleophosmin 1 ver/editar referências no wikidata»

[2] «Human PubMed Reference:»

[3] Schneider F; et al. (maio de 2009). «NPM1 but not FLT3-ITD mutations predict early blast cell clearance and CR rate in patients with normal karyotype AML (NK-AML) or high-risk myelodysplastic syndrome (MDS)». Blood. 113 (21). pp. 5250–3