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HSF1 англ Heat shock transcription factor 1 білок який кодується однойменним геном розташованим у людей на короткому пле

HSF1

HSF1

HSF1 (англ. Heat shock transcription factor 1) – білок, який кодується однойменним геном, розташованим у людей на короткому плечі 8-ї хромосоми. Довжина поліпептидного ланцюга білка становить 529 амінокислот, а молекулярна маса — 57 260.

HSF1
Наявні структури
PDBПошук ортологів: PDBe RCSB
Ідентифікатори
Символи HSF1, HSTF1, heat shock transcription factor 1
Зовнішні ІД OMIM: 140580 MGI: 96238 HomoloGene: 74556 GeneCards: HSF1
Ортологи
Види Людина Миша
Entrez
3297
15499
Ensembl
ENSG00000185122
ENSG00000284774
ENSMUSG00000022556
UniProt
Q00613
P38532
RefSeq (мРНК)
NM_005526
NM_008296
RefSeq (білок)
NP_005517
NP_001318081
NP_001318082
NP_001318083
NP_001318143
NP_032322
Локус (UCSC) Хр. 8: 144.29 – 144.31 Mb н/д
PubMed search
Вікідані
Див./Ред. для людейДив./Ред. для мишей
Послідовність амінокислот
1020304050
MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQG
QFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQ
HPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTKLLTDVQLMKGK
QECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSN
RILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPYSAPSPAYSSS
SLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEE
PPSPPQSPRVEEASPGRPSSVDTLLSPTALIDSILRESEPAPASVTALTD
ARGHTDTEGRPPSPPPTSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQT
MLSSHGFSVDTSALLDLFSPSVTVPDMSLPDLDSSLASIQELLSPQEPPR
PPEAENSSPDSGKQLVHYTAQPLFLLDPGSVDTGSNDLPVLFELGEGSYF
SEGDGFAEDPTISLLTGSEPPKAKDPTVS

Кодований геном білок за функціями належить до активаторів, фосфопротеїнів. Задіяний у таких біологічних процесах, як процесинг мРНК, відповідь на стрес, транскрипція, регуляція транскрипції, транспорт, пошкодження ДНК, репарація ДНК, транспорт мРНК, ацетилювання, альтернативний сплайсинг. Білок має сайт для зв'язування з ДНК. Локалізований у цитоплазмі, цитоскелеті, ядрі, хромосомах, центромерах, кінетохорі.

Література

  • Rabindran S.K., Giorgi G., Clos J., Wu C. (1991). Molecular cloning and expression of a human heat shock factor, HSF1. Proc. Natl. Acad. Sci. U.S.A. 88: 6906—6910. PMID 1871105 DOI:10.1073/pnas.88.16.6906
  • The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 14: 2121—2127. 2004. PMID 15489334 DOI:10.1101/gr.2596504
  • Schuetz T.J., Gallo G.J., Sheldon L., Tempst P., Kingston R.E. (1991). Isolation of a cDNA for HSF2: evidence for two heat shock factor genes in humans. Proc. Natl. Acad. Sci. U.S.A. 88: 6911—6915. PMID 1871106 DOI:10.1073/pnas.88.16.6911
  • Abravaya K., Phillips B., Morimoto R.I. (1991). Heat shock-induced interactions of heat shock transcription factor and the human hsp70 promoter examined by in vivo footprinting. Mol. Cell. Biol. 11: 586—592. PMID 1986252 DOI:10.1128/MCB.11.1.586
  • Baler R., Dahl G., Voellmy R. (1993). Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1. Mol. Cell. Biol. 13: 2486—2496. PMID 8455624 DOI:10.1128/MCB.13.4.2486
  • Rabindran S.K., Wisniewski J., Li L., Li G.C., Wu C. (1994). Interaction between heat shock factor and hsp70 is insufficient to suppress induction of DNA-binding activity in vivo. Mol. Cell. Biol. 14: 6552—6560. PMID 7935376 DOI:10.1128/MCB.14.10.6552

Примітки

  1. Human PubMed Reference:.
  2. Mouse PubMed Reference:.
  3. HUGO Gene Nomenclature Commitee, HGNC:5224 (англ.) . Процитовано 7 вересня 2017.
  4. (англ.) . Архів оригіналу за 29 серпня 2017. Процитовано 7 вересня 2017.

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HSF1 angl Heat shock transcription factor 1 bilok yakij koduyetsya odnojmennim genom roztashovanim u lyudej na korotkomu plechi 8 yi hromosomi Dovzhina polipeptidnogo lancyuga bilka stanovit 529 aminokislot a molekulyarna masa 57 260 HSF1Nayavni strukturiPDBPoshuk ortologiv PDBe RCSB Spisok kodiv PDB2LDU 5D5U 5D5VIdentifikatoriSimvoliHSF1 HSTF1 heat shock transcription factor 1Zovnishni ID OMIM 140580 MGI 96238 HomoloGene 74556 GeneCards HSF1Ontologiya genaMolekulyarna funkciya 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 protein binding 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 bindingKlitinna komponenta citoplazma Pronukleus GO 0035327 Euhromatin GO 0035328 Geterohromatin klitinne yadro centrosoma gialoplazma PML body nuclear stress granule mitotic spindle pole Ribonukleoproteyini centromera kinetohor spindle pole nukleoplazma hromosoma centr organizaciyi mikrotrubochok citoskelet perinuclear region of cytoplasm GO 0009327 protein containing complexBiologichnij proces 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 Spermatogenez 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 Reparaciya DNK mRNA processing cellular response to DNA damage stimulus mRNA transport positive regulation of tyrosine phosphorylation of STAT protein positive regulation of cold induced thermogenesisDzherela Amigo QuickGOOrtologiVidi Lyudina MishaEntrez3297 15499Ensembl ENSG00000185122 ENSG00000284774 ENSMUSG00000022556UniProt Q00613 P38532RefSeq mRNK NM 005526NM 008296RefSeq bilok NP 005517NP 001318081 NP 001318082 NP 001318083 NP 001318143 NP 032322Lokus UCSC Hr 8 144 29 144 31 Mbn dPubMed searchVikidaniDiv Red dlya lyudejDiv Red dlya mishej Poslidovnist aminokislot1020304050 MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQG QFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQ HPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTKLLTDVQLMKGK QECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSN RILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPYSAPSPAYSSS SLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEE PPSPPQSPRVEEASPGRPSSVDTLLSPTALIDSILRESEPAPASVTALTD ARGHTDTEGRPPSPPPTSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQT MLSSHGFSVDTSALLDLFSPSVTVPDMSLPDLDSSLASIQELLSPQEPPR PPEAENSSPDSGKQLVHYTAQPLFLLDPGSVDTGSNDLPVLFELGEGSYF SEGDGFAEDPTISLLTGSEPPKAKDPTVS A Alanin C Cisteyin D Asparaginova kislota E Glutaminova kislota F Fenilalanin G Glicin H Gistidin I Izolejcin K Lizin L Lejcin M Metionin N Asparagin P Prolin Q Glutamin R Arginin S Serin T Treonin V Valin W Triptofan Y Tirozin Kodovanij genom bilok za funkciyami nalezhit do aktivatoriv fosfoproteyiniv Zadiyanij u takih biologichnih procesah yak procesing mRNK vidpovid na stres transkripciya regulyaciya transkripciyi transport poshkodzhennya DNK reparaciya DNK transport mRNK acetilyuvannya alternativnij splajsing Bilok maye sajt dlya zv yazuvannya z DNK Lokalizovanij u citoplazmi citoskeleti yadri hromosomah centromerah kinetohori LiteraturaRabindran S K Giorgi G Clos J Wu C 1991 Molecular cloning and expression of a human heat shock factor HSF1 Proc Natl Acad Sci U S A 88 6906 6910 PMID 1871105 DOI 10 1073 pnas 88 16 6906 The status quality and expansion of the NIH full length cDNA project the Mammalian Gene Collection MGC Genome Res 14 2121 2127 2004 PMID 15489334 DOI 10 1101 gr 2596504 Schuetz T J Gallo G J Sheldon L Tempst P Kingston R E 1991 Isolation of a cDNA for HSF2 evidence for two heat shock factor genes in humans Proc Natl Acad Sci U S A 88 6911 6915 PMID 1871106 DOI 10 1073 pnas 88 16 6911 Abravaya K Phillips B Morimoto R I 1991 Heat shock induced interactions of heat shock transcription factor and the human hsp70 promoter examined by in vivo footprinting Mol Cell Biol 11 586 592 PMID 1986252 DOI 10 1128 MCB 11 1 586 Baler R Dahl G Voellmy R 1993 Activation of human heat shock genes is accompanied by oligomerization modification and rapid translocation of heat shock transcription factor HSF1 Mol Cell Biol 13 2486 2496 PMID 8455624 DOI 10 1128 MCB 13 4 2486 Rabindran S K Wisniewski J Li L Li G C Wu C 1994 Interaction between heat shock factor and hsp70 is insufficient to suppress induction of DNA binding activity in vivo Mol Cell Biol 14 6552 6560 PMID 7935376 DOI 10 1128 MCB 14 10 6552PrimitkiHuman PubMed Reference Mouse PubMed Reference HUGO Gene Nomenclature Commitee HGNC 5224 angl Procitovano 7 veresnya 2017 angl Arhiv originalu za 29 serpnya 2017 Procitovano 7 veresnya 2017 Div takozhHromosoma 8 Ce nezavershena stattya pro bilki Vi mozhete dopomogti proyektu vipravivshi abo dopisavshi yiyi

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