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HSPA5 англ Heat shock protein family A Hsp70 member 5 білок який кодується однойменним геном розташованим у людей на кор

HSPA5

HSPA5

HSPA5 (англ. Heat shock protein family A (Hsp70) member 5) – білок, який кодується однойменним геном, розташованим у людей на короткому плечі 9-ї хромосоми. Довжина поліпептидного ланцюга білка становить 654 амінокислот, а молекулярна маса — 72 333.

HSPA5
Наявні структури
PDBПошук ортологів: PDBe RCSB
Ідентифікатори
Символи HSPA5, BIP, GRP78, HEL-S-89n, MIF2, Binding immunoglobulin protein, heat shock protein family A (Hsp70) member 5, GRP78/Bip
Зовнішні ІД OMIM: 138120 MGI: 95835 HomoloGene: 3908 GeneCards: HSPA5
Шаблон експресії
image
Більше даних
Ортологи
Види Людина Миша
Entrez
3309
14828
Ensembl
ENSG00000044574
ENSMUSG00000026864
UniProt
P11021
P20029
RefSeq (мРНК)
NM_005347
NM_001163434
NM_022310
RefSeq (білок)
NP_005338
NP_001156906
NP_071705
Локус (UCSC) Хр. 9: 125.23 – 125.24 Mb Хр. 2: 34.66 – 34.67 Mb
PubMed search
Вікідані
Див./Ред. для людейДив./Ред. для мишей
Послідовність амінокислот
1020304050
MKLSLVAAMLLLLSAARAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRV
EIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIG
RTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVL
TKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIIN
EPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGD
THLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALS
SQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSD
LKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAV
QAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQI
FSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVT
FEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAE
EDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEE
KIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTAE
KDEL

Білок має сайт для зв'язування з АТФ, нуклеотидами. Локалізований у цитоплазмі, ендоплазматичному ретикулумі.

Література

  • Ting J., Lee A.S. (1988). Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation. DNA. 7: 275—286. PMID 2840249 DOI:10.1089/dna.1988.7.275
  • 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
  • Chao C.C.K., Lin-Chao S. (1992). A direct-repeat sequence of the human BiP gene is required for A23187-mediated inducibility and an inducible nuclear factor binding. Nucleic Acids Res. 20: 6481—6485. PMID 1480470 DOI:10.1093/nar/20.24.6481
  • Dana R.C., Welch W.J., Deftos L.J. (1990). Heat shock proteins bind calcitonin. Endocrinology. 126: 672—674. PMID 2294010 DOI:10.1210/endo-126-1-672
  • 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
  • Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M. (2002). A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol. Biol. Cell. 13: 4456—4469. PMID 12475965 DOI:10.1091/mbc.E02-05-0311

Примітки

  1. Human PubMed Reference:.
  2. Mouse PubMed Reference:.
  3. (англ.) . Архів оригіналу за 7 лютого 2017. Процитовано 6 лютого 2017.
  4. (англ.) . Архів оригіналу за 7 лютого 2017. Процитовано 6 лютого 2017.

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HSPA5 angl Heat shock protein family A Hsp70 member 5 bilok yakij koduyetsya odnojmennim genom roztashovanim u lyudej na korotkomu plechi 9 yi hromosomi Dovzhina polipeptidnogo lancyuga bilka stanovit 654 aminokislot a molekulyarna masa 72 333 HSPA5Nayavni strukturiPDBPoshuk ortologiv PDBe RCSB Spisok kodiv PDB3IUC 3LDL 3LDN 3LDO 3LDP 5E84 5E86 5E85 5F1X 5EX5 5EVZ 5F2R 5F0X 5EY4 5EXWIdentifikatoriSimvoliHSPA5 BIP GRP78 HEL S 89n MIF2 Binding immunoglobulin protein heat shock protein family A Hsp70 member 5 GRP78 BipZovnishni ID OMIM 138120 MGI 95835 HomoloGene 3908 GeneCards HSPA5Ontologiya genaMolekulyarna funkciya nucleotide binding calcium ion binding chaperone binding protein domain specific binding ribosome binding misfolded protein binding ATPase activity GO 0001948 GO 0016582 protein binding enzyme binding ATP binding ubiquitin protein ligase binding unfolded protein binding cadherin binding hydrolase activity heat shock protein binding protein folding chaperone activityKlitinna komponenta citoplazma endoplasmic reticulum lumen endoplasmic reticulum membrane membrana focal adhesion Melanosoma myelin sheath klitinna membrana smooth endoplasmic reticulum endoplasmic reticulum chaperone complex cell surface integral component of endoplasmic reticulum membrane midbody endoplazmatichnij retikulum mitohondriya COP9 signalosome ekzosoma klitinne yadro endoplasmic reticulum Golgi intermediate compartment GO 0005578 Pozaklitinna matricya gialoplazma GO 0009327 protein containing complex vnutrishnoklitinna membranna organelaBiologichnij proces cellular response to interleukin 4 regulation of ATF6 mediated unfolded protein response cellular response to glucose starvation regulation of protein folding in endoplasmic reticulum substantia nigra development positive regulation of cell migration positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress maintenance of protein localization in endoplasmic reticulum negative regulation of apoptotic process protein folding in endoplasmic reticulum negative regulation of transforming growth factor beta receptor signaling pathway toxin transport response to endoplasmic reticulum stress PERK mediated unfolded protein response cerebellum structural organization ER overload response Vidpovid na nezgornuti bilki ATF6 mediated unfolded protein response IRE1 mediated unfolded protein response cerebellar Purkinje cell layer development regulation of PERK mediated unfolded protein response ubiquitin dependent ERAD pathway GO 1904577 cellular response to antibiotic negative regulation of protein homodimerization activity proteolysis involved in cellular protein catabolic process cellular response to manganese ion positive regulation of protein ubiquitination regulation of IRE1 mediated unfolded protein response response to radiation positive regulation of neuron projection development neuron differentiation response to cocaine neuron apoptotic process cellular response to calcium ion cellular response to cAMP stress response to metal ion response to methamphetamine hydrochloride cellular response to nerve growth factor stimulus cellular response to gamma radiation luteolysis response to unfolded protein cellular response to heat Unfolded Protein Response protein refolding chaperone cofactor dependent protein refolding negative regulation of IRE1 mediated unfolded protein response posttranslational protein targeting to membrane translocationDzherela Amigo QuickGOShablon ekspresiyiBilshe danihOrtologiVidi Lyudina MishaEntrez3309 14828Ensembl ENSG00000044574 ENSMUSG00000026864UniProt P11021 P20029RefSeq mRNK NM 005347NM 001163434 NM 022310RefSeq bilok NP 005338NP 001156906 NP 071705Lokus UCSC Hr 9 125 23 125 24 MbHr 2 34 66 34 67 MbPubMed searchVikidaniDiv Red dlya lyudejDiv Red dlya mishej Poslidovnist aminokislot1020304050 MKLSLVAAMLLLLSAARAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRV EIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIG RTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVL TKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIIN EPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGD THLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALS SQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSD LKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAV QAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQI FSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVT FEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAE EDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEE KIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTAE KDEL 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 Bilok maye sajt dlya zv yazuvannya z ATF nukleotidami Lokalizovanij u citoplazmi endoplazmatichnomu retikulumi LiteraturaTing J Lee A S 1988 Human gene encoding the 78 000 dalton glucose regulated protein and its pseudogene structure conservation and regulation DNA 7 275 286 PMID 2840249 DOI 10 1089 dna 1988 7 275 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 Chao C C K Lin Chao S 1992 A direct repeat sequence of the human BiP gene is required for A23187 mediated inducibility and an inducible nuclear factor binding Nucleic Acids Res 20 6481 6485 PMID 1480470 DOI 10 1093 nar 20 24 6481 Dana R C Welch W J Deftos L J 1990 Heat shock proteins bind calcitonin Endocrinology 126 672 674 PMID 2294010 DOI 10 1210 endo 126 1 672 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 Meunier L Usherwood Y K Chung K T Hendershot L M 2002 A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins Mol Biol Cell 13 4456 4469 PMID 12475965 DOI 10 1091 mbc E02 05 0311PrimitkiHuman PubMed Reference Mouse PubMed Reference angl Arhiv originalu za 7 lyutogo 2017 Procitovano 6 lyutogo 2017 angl Arhiv originalu za 7 lyutogo 2017 Procitovano 6 lyutogo 2017 Div takozhHromosoma 9 Ce nezavershena stattya pro bilki Vi mozhete dopomogti proyektu vipravivshi abo dopisavshi yiyi Cya stattya nedostatno chi zovsim ne kategorizovana abo kategoriyi do yakih vona nalezhit ne isnuyut Bud laska dopomozhit dodati nalezhni kategoriyi abi cyu stattyu mozhna bulo kategorizuvati iz sumizhnimi storinkami sichen 2024

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