HSF1 |
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Estruturas disponíveis |
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PDB | Pesquisa Human UniProt: PDBe RCSB |
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Identificadores |
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Nomes alternativos | HSF1, Fator de choque térmico 1 |
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IDs externos | OMIM: 140580 HomoloGene: 74556 GeneCards: HSF1 |
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Ontologia genética |
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Função molecular | • GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity • chromatin binding • GO:0001078, GO:0001214, GO:0001206 DNA-binding transcription repressor activity, RNA polymerase II-specific • GO:0001948, GO:0016582 ligação a proteínas plasmáticas • RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding • sequence-specific single stranded DNA binding • DNA binding • protein kinase binding • heat shock protein binding • chromatin DNA binding • identical protein binding • sequence-specific DNA binding • protein self-association • protein heterodimerization activity • Hsp90 protein binding • translation elongation factor binding • promoter-specific chromatin binding • GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding • GO:0001200, GO:0001133, GO:0001201 DNA-binding transcription factor activity, RNA polymerase II-specific • STAT family protein binding
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Componente celular | • citoplasma • pronúcleo • GO:0035327 eucromatina • GO:0035328 heterocromatina • núcleo celular • centrossoma • citosol • PML body • nuclear stress granule • mitotic spindle pole • Partículas de ribonucleoproteínas heterogéneas • centrómero • cinetócoro • spindle pole • cariolinfa • cromossoma • centro organizador dos microtúbulos • citoesqueleto • perinuclear region of cytoplasm • GO:0009327 complexo macromolecular
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Processo biológico | • defense response • GO:0009373 regulation of transcription, DNA-templated • embryonic placenta development • mRNA transcription • in utero embryonic development • GO:1901227 negative regulation of transcription by RNA polymerase II • response to heat • female meiotic nuclear division • transcription, DNA-templated • embryonic process involved in female pregnancy • protein phosphorylation • response to lipopolysaccharide • espermatogênese • positive regulation of multicellular organism growth • negative regulation of tumor necrosis factor production • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II • negative regulation of cell population proliferation • response to organonitrogen compound • cellular response to lipopolysaccharide • negative regulation of gene expression • cellular response to amino acid stimulus • cellular response to hydrogen peroxide • positive regulation of microtubule binding • response to peptide • cellular response to nitroglycerin • negative regulation of cardiac muscle cell apoptotic process • response to estradiol • GO:1904579 cellular response to organic cyclic compound • GO:1901313 positive regulation of gene expression • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process • cellular response to potassium ion • response to amino acid • negative regulation of inclusion body assembly • positive regulation of apoptotic DNA fragmentation • cellular response to L-glutamine • response to psychosocial stress • GO:1904578 response to organic cyclic compound • negative regulation of neuron death • response to nutrient • cellular response to angiotensin • response to testosterone • response to hypobaric hypoxia • response to activity • cellular response to radiation • cellular response to estradiol stimulus • positive regulation of inclusion body assembly • MAPK cascade • positive regulation of cell population proliferation • cellular response to heat • Unfolded Protein Response • regulation of protein heterodimerization activity • positive regulation of mitotic cell cycle • protein homooligomerization • positive regulation of transcription from RNA polymerase II promoter in response to heat stress • protein homotrimerization • cellular response to cadmium ion • cellular response to copper ion • cellular response to gamma radiation • cellular response to diamide • regulation of cellular response to heat • positive regulation of mRNA polyadenylation • cellular response to sodium arsenite • negative regulation of double-strand break repair via nonhomologous end joining • GO:0100026 reparo de ADN • mRNA processing • cellular response to DNA damage stimulus • mRNA transport • positive regulation of tyrosine phosphorylation of STAT protein • positive regulation of cold-induced thermogenesis
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Sources:Amigo / QuickGO |
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Wikidata |
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Fator de choque térmico 1 é uma proteína que em humanos é codificada pelo gene HSF1.[2]
O HSF1, assim como o gene relacionado HSF2, codifica uma proteína que se liga especificamente ao elemento de choque térmico[3] e é altamente conservado em eucariotos e é o mediador primário das respostas transcricionais ao estresse proteotóxico, com papéis importantes na regulação não relacionada ao estresse, como o desenvolvimento e o metabolismo.[4]
Referências
- Voellmy R (1996). Sensing stress and responding to stress. Exs. 77. [S.l.: s.n.] pp. 121–37. ISBN 978-3-0348-9901-7. PMID 8856972. doi:10.1007/978-3-0348-9088-5_9
- Abravaya K, Myers MP, Murphy SP, Morimoto RI (julho de 1992). «The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression». Genes & Development. 6 (7): 1153–64. PMID 1628823. doi:10.1101/gad.6.7.1153
- Schuetz TJ, Gallo GJ, Sheldon L, Tempst P, Kingston RE (agosto de 1991). «Isolation of a cDNA for HSF2: evidence for two heat shock factor genes in humans». Proceedings of the National Academy of Sciences of the United States of America. 88 (16): 6911–5. PMC 52203
. PMID 1871106. doi:10.1073/pnas.88.16.6911
- Nunes SL, Calderwood SK (agosto de 1995). «Heat shock factor-1 and the heat shock cognate 70 protein associate in high molecular weight complexes in the cytoplasm of NIH-3T3 cells». Biochemical and Biophysical Research Communications. 213 (1): 1–6. PMID 7639722. doi:10.1006/bbrc.1995.2090
- Maruyama K, Sugano S (janeiro de 1994). «Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides». Gene. 138 (1–2): 171–4. PMID 8125298. doi:10.1016/0378-1119(94)90802-8
- Chu B, Soncin F, Price BD, Stevenson MA, Calderwood SK (novembro de 1996). «Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor-1». The Journal of Biological Chemistry. 271 (48): 30847–57. PMID 8940068. doi:10.1074/jbc.271.48.30847
- Fukunaga R, Hunter T (abril de 1997). «MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates». The EMBO Journal. 16 (8): 1921–33. PMC 1169795
. PMID 9155018. doi:10.1093/emboj/16.8.1921
- Nair SC, Toran EJ, Rimerman RA, Hjermstad S, Smithgall TE, Smith DF (dezembro de 1996). «A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor». Cell Stress & Chaperones. 1 (4): 237–50. PMC 376461
. PMID 9222609. doi:10.1379/1466-1268(1996)001<0237:APOMCI>2.3.CO;2
- Huang J, Nueda A, Yoo S, Dynan WS (outubro de 1997). «Heat shock transcription factor 1 binds selectively in vitro to Ku protein and the catalytic subunit of the DNA-dependent protein kinase». The Journal of Biological Chemistry. 272 (41): 26009–16. PMID 9325337. doi:10.1074/jbc.272.41.26009
- Cotto J, Fox S, Morimoto R (dezembro de 1997). «HSF1 granules: a novel stress-induced nuclear compartment of human cells». Journal of Cell Science. 110 ( Pt 23) (23): 2925–34. PMID 9359875
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (outubro de 1997). «Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library». Gene. 200 (1–2): 149–56. PMID 9373149. doi:10.1016/S0378-1119(97)00411-3
- Shi Y, Mosser DD, Morimoto RI (março de 1998). «Molecular chaperones as HSF1-specific transcriptional repressors». Genes & Development. 12 (5): 654–66. PMC 316571
. PMID 9499401. doi:10.1101/gad.12.5.654
- Satyal SH, Chen D, Fox SG, Kramer JM, Morimoto RI (julho de 1998). «Negative regulation of the heat shock transcriptional response by HSBP1». Genes & Development. 12 (13): 1962–74. PMC 316975
. PMID 9649501. doi:10.1101/gad.12.13.1962
- Zhou X, Tron VA, Li G, Trotter MJ (agosto de 1998). «Heat shock transcription factor-1 regulates heat shock protein-72 expression in human keratinocytes exposed to ultraviolet B light». The Journal of Investigative Dermatology. 111 (2): 194–8. PMID 9699716. doi:10.1046/j.1523-1747.1998.00266.x
- Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R (agosto de 1998). «Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1». Cell. 94 (4): 471–80. PMID 9727490. doi:10.1016/S0092-8674(00)81588-3
- Stephanou A, Isenberg DA, Nakajima K, Latchman DS (janeiro de 1999). «Signal transducer and activator of transcription-1 and heat shock factor-1 interact and activate the transcription of the Hsp-70 and Hsp-90beta gene promoters». The Journal of Biological Chemistry. 274 (3): 1723–8. PMID 9880553. doi:10.1074/jbc.274.3.1723
- Dai R, Frejtag W, He B, Zhang Y, Mivechi NF (junho de 2000). «c-Jun NH2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity». The Journal of Biological Chemistry. 275 (24): 18210–8. PMID 10747973. doi:10.1074/jbc.M000958200
- Choi Y, Asada S, Uesugi M (maio de 2000). «Divergent hTAFII31-binding motifs hidden in activation domains». The Journal of Biological Chemistry. 275 (21): 15912–6. PMID 10821850. doi:10.1074/jbc.275.21.15912