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HSPA1A англ Heat shock 70 kDa protein 1A білок який кодується однойменним геном розташованим у людей на короткому плечі

HSPA1A

HSPA1A

HSPA1A (англ. Heat shock 70 kDa protein 1A) – білок, який кодується однойменним геном, розташованим у людей на короткому плечі 6-ї хромосоми. Довжина поліпептидного ланцюга білка становить 641 амінокислот, а молекулярна маса — 70 052.

HSPA1A
image
Наявні структури
PDBПошук ортологів: PDBe RCSB
Ідентифікатори
Символи HSPA1A, HEL-S-103, HSP70-1, HSP70-1A, HSP70I, HSP72, HSPA1, HSP70.1, heat shock protein family A (Hsp70) member 1A, HSP70.2, HSP70-2, HSP70
Зовнішні ІД OMIM: 140550 MGI: 96244 HomoloGene: 74294 GeneCards: HSPA1A
Ортологи
Види Людина Миша
Entrez
3303
193740
Ensembl
ENSMUSG00000091971
UniProt
P0DMV8
P0DMV9
Q61696
RefSeq (мРНК)
NM_005345
NM_010479
RefSeq (білок)
NP_005337
NP_005336
NP_005336
NP_005336.3
NP_005337.2
NP_034609
Локус (UCSC) Хр. 6: 31.82 – 31.82 Mb Хр. 17: 35.19 – 35.19 Mb
PubMed search
Вікідані
Див./Ред. для людейДив./Ред. для мишей
Послідовність амінокислот
1020304050
MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERL
IGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDK
PKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYF
NDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDL
GGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHK
KDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRA
RFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLL
QDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLS
LGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMT
KDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANK
ITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMK
SAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELE
QVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD

Кодований геном білок за функціями належить до шаперонів, рецепторів клітини-хазяїна для входу вірусу, рецепторів, фосфопротеїнів. Задіяний у таких біологічних процесах, як відповідь на стрес, ацетилювання, альтернативний сплайсинг. Білок має сайт для зв'язування з АТФ, нуклеотидами. Локалізований у цитоплазмі, цитоскелеті, ядрі.

Література

  • Hunt C., Morimoto R.I. (1985). Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. Proc. Natl. Acad. Sci. U.S.A. 82: 6455—6459. PMID 3931075 DOI:10.1073/pnas.82.19.6455
  • Milner C.M., Campbell R.D. (1990). Structure and expression of the three MHC-linked HSP70 genes. Immunogenetics. 32: 242—251. PMID 1700760 DOI:10.1007/BF00187095
  • 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
  • Sargent C.A., Dunham I., Trowsdale J., Campbell R.D. (1989). Human major histocompatibility complex contains genes for the major heat shock protein HSP70. Proc. Natl. Acad. Sci. U.S.A. 86: 1968—1972. PMID 2538825 DOI:10.1073/pnas.86.6.1968
  • Drabent B., Genthe A., Benecke B.-J. (1986). In vitro transcription of a human hsp 70 heat shock gene by extracts prepared from heat-shocked and non-heat-shocked human cells. Nucleic Acids Res. 14: 8933—8948. PMID 3786141 DOI:10.1093/nar/14.22.8933
  • Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B. (2013). A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity. PLoS Genet. 9: E1003210—E1003210. PMID 23349634 DOI:10.1371/journal.pgen.1003210

Примітки

  1. Human PubMed Reference:.
  2. Mouse PubMed Reference:.
  3. HUGO Gene Nomenclature Commitee, HGNC:5232 (англ.) . Процитовано 6 вересня 2017.
  4. (англ.) . Архів оригіналу за 4 вересня 2017. Процитовано 6 вересня 2017.

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HSPA1A angl Heat shock 70 kDa protein 1A bilok yakij koduyetsya odnojmennim genom roztashovanim u lyudej na korotkomu plechi 6 yi hromosomi Dovzhina polipeptidnogo lancyuga bilka stanovit 641 aminokislot a molekulyarna masa 70 052 HSPA1ANayavni strukturiPDBPoshuk ortologiv PDBe RCSB Spisok kodiv PDB1HJO 1S3X 1XQS 2E88 2E8A 2LMG 3A8Y 3ATU 3ATV 3AY9 3D2E 3D2F 3JXU 3LOF 4IO8 4J8F 4PO2 4WV5 4WV7 5AR0 5AQZ 3Q49 s3D2EIdentifikatoriSimvoliHSPA1A HEL S 103 HSP70 1 HSP70 1A HSP70I HSP72 HSPA1 HSP70 1 heat shock protein family A Hsp70 member 1A HSP70 2 HSP70 2 HSP70Zovnishni ID OMIM 140550 MGI 96244 HomoloGene 74294 GeneCards HSPA1AOntologiya genaMolekulyarna funkciya nucleotide binding heat shock protein binding signaling receptor binding C3HC4 type RING finger domain binding ATPase activity virus receptor activity histone deacetylase binding protein folding chaperone activity G protein coupled receptor binding ATP binding enzyme binding ubiquitin protein ligase binding GO 0001948 GO 0016582 protein binding GO 0001106 transcription corepressor activity cadherin binding RNA binding denatured protein binding protein N terminus binding unfolded protein binding disordered domain specific binding misfolded protein bindingKlitinna komponenta blood microparticle Centriol nukleoplazma inclusion body focal adhesion perinuclear region of cytoplasm ubiquitin ligase complex gialoplazma extracellular region ficolin 1 rich granule lumen centrosoma centr organizaciyi mikrotrubochok citoskelet klitinne yadro citoplazma mitohondriya endoplazmatichnij retikulum aggresome nuclear speck vezikula ekzosoma COP9 signalosome GO 0009327 protein containing complex RibonukleoproteyiniBiologichnij proces cellular response to oxidative stress regulation of mRNA stability negative regulation of endoplasmic reticulum stress induced intrinsic apoptotic signaling pathway positive regulation of NF kappaB transcription factor activity negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway cellular heat acclimation negative regulation of inclusion body assembly positive regulation of tumor necrosis factor mediated signaling pathway negative regulation of cell death GO 1901313 positive regulation of gene expression viral entry into host cell regulation of cell death ATP metabolic process negative regulation of protein ubiquitination negative regulation of extrinsic apoptotic signaling pathway in absence of ligand positive regulation of endoribonuclease activity positive regulation of nucleotide binding oligomerization domain containing 2 signaling pathway regulation of protein ubiquitination positive regulation of interleukin 8 production regulation of cellular response to heat cellular response to heat negative regulation of transforming growth factor beta receptor signaling pathway positive regulation of proteasomal ubiquitin dependent protein catabolic process neutrophil degranulation negative regulation of transcription from RNA polymerase II promoter in response to stress protein refolding positive regulation of microtubule nucleation regulation of mitotic spindle assembly mRNA catabolic process response to unfolded protein negative regulation of cell population proliferation negative regulation of cell growth negative regulation of apoptotic process protein stabilization chaperone mediated protein complex assembly positive regulation of RNA splicing Unfolded Protein Response positive regulation of erythrocyte differentiation chaperone cofactor dependent protein refolding lysosomal transport response to heat telomere maintenance GO 0100026 Reparaciya DNKDzherela Amigo QuickGOOrtologiVidi Lyudina MishaEntrez3303 193740Ensembl ENSG00000234475 ENSG00000204389 ENSG00000237724 ENSG00000235941 ENSG00000215328n d ENSMUSG00000091971UniProt P0DMV8 P0DMV9 Q61696RefSeq mRNK NM 005345NM 010479RefSeq bilok NP 005337 NP 005336 NP 005336 NP 005336 3 NP 005337 2NP 034609Lokus UCSC Hr 6 31 82 31 82 MbHr 17 35 19 35 19 MbPubMed searchVikidaniDiv Red dlya lyudejDiv Red dlya mishej Poslidovnist aminokislot1020304050 MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERL IGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDK PKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYF NDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDL GGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHK KDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRA RFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLL QDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLS LGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMT KDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANK ITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMK SAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELE QVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD 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 shaperoniv receptoriv klitini hazyayina dlya vhodu virusu receptoriv fosfoproteyiniv Zadiyanij u takih biologichnih procesah yak vidpovid na stres acetilyuvannya alternativnij splajsing Bilok maye sajt dlya zv yazuvannya z ATF nukleotidami Lokalizovanij u citoplazmi citoskeleti yadri LiteraturaHunt C Morimoto R I 1985 Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70 Proc Natl Acad Sci U S A 82 6455 6459 PMID 3931075 DOI 10 1073 pnas 82 19 6455 Milner C M Campbell R D 1990 Structure and expression of the three MHC linked HSP70 genes Immunogenetics 32 242 251 PMID 1700760 DOI 10 1007 BF00187095 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 Sargent C A Dunham I Trowsdale J Campbell R D 1989 Human major histocompatibility complex contains genes for the major heat shock protein HSP70 Proc Natl Acad Sci U S A 86 1968 1972 PMID 2538825 DOI 10 1073 pnas 86 6 1968 Drabent B Genthe A Benecke B J 1986 In vitro transcription of a human hsp 70 heat shock gene by extracts prepared from heat shocked and non heat shocked human cells Nucleic Acids Res 14 8933 8948 PMID 3786141 DOI 10 1093 nar 14 22 8933 Cloutier P Lavallee Adam M Faubert D Blanchette M Coulombe B 2013 A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity PLoS Genet 9 E1003210 E1003210 PMID 23349634 DOI 10 1371 journal pgen 1003210PrimitkiHuman PubMed Reference Mouse PubMed Reference HUGO Gene Nomenclature Commitee HGNC 5232 angl Procitovano 6 veresnya 2017 angl Arhiv originalu za 4 veresnya 2017 Procitovano 6 veresnya 2017 Div takozhHromosoma 6 Ce nezavershena stattya pro bilki Vi mozhete dopomogti proyektu vipravivshi abo dopisavshi yiyi

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