HSPA1A

Protein toplotnog šoka 70 kDa 1A
PDB prikaz baziran na 1hjo​.
Dostupne strukture
1hjo​, 1s3x​, 1xqs​
Identifikatori
Simboli HSPA1A; HSP70-1; HSP72; HSPA1; HSPA1B; HSPA1A; HSP70-2
Vanjski ID OMIM: 140550 MGI: 99517 HomoloGene: 74294 GeneCards: HSPA1A Gene
Ontologija gena
Molekularna funkcija • vezivanje nukleotida
• ATP vezivanje
• vezivanje nesavijenog proteina
Celularna komponenta • jedro
• citoplazma
• mitohondrija
• endoplazmatični retikulum
Biološki proces • proteinsko savijanje
• respons na nesavijeni protein
• iRNK katabolički proces
• anti-apoptoza
Ortolozi
Vrsta Čovek Miš
Entrez 3303 15511
Ensembl ENSG00000204389 ENSMUSG00000067284
UniProt P08107 O88687
RefSeq (mRNA) NM_005345 XM_001002795
RefSeq (protein) NP_005336 XP_001002795
Lokacija (UCSC) Chr 6:
31.78 - 31.79 Mb		 Chr 17:
34.57 - 34.57 Mb
PubMed pretraga [1] [2]

HSPA1A, protein toplotnog šoka 70 kDa 1, je protein koji je kod čoveka kodiran HSPA1A genom.

Ovaj gen ne sadrži introne. On je član familije proteina toplotnog šoka 70. Zajedno s drugim proteinima toplotnog šoka, ovaj protein sprečava agregaciju postojećih proteina i posreduje savijanje novo transliranih proteina u citosolu i organelama. On takođe učestvuje u ubikvitin-proteasom putu tako što ostvaruje interakcije sa AU-bogatim elementom RNK-vezujućeg proteina 1. Ovaj gen je lociran u regionu klase III glavnog histokompatibilnostnog kompleksa, u klasteru sa dva blisko srodna gena koji kodiraju slične proteine.[1]

Interakcije

Za HSPA1A je bilo pokazano da interaguje sa ASK1,[2] STUB1,[3][4] MSR1,[5] BAG3,[6][7] Parkinovom ligazom,[4] Fankonijeva anemija, komplementaciona grupa C,[8][9] GPR37,[4] HSF1[10][11] i AIFM1.[12][13]

Reference

  1. ^ „Entrez Gene: HSPA1A heat shock 70kDa protein 1A”. 
  2. ^ Park, Hee-Sae; Cho Ssang-Goo; et al. (2002). „Heat shock protein hsp72 is a negative regulator of apoptosis signal-regulating kinase 1”. Mol. Cell. Biol. United States. 22 (22): 7721—30. ISSN 0270-7306. PMC 134722 Слободан приступ. PMID 12391142. doi:10.1128/MCB.22.22.7721-7730.2002. 
  3. ^ Ballinger, C A; Connell P; et al. (1999). „Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions”. Mol. Cell. Biol. UNITED STATES. 19 (6): 4535—45. ISSN 0270-7306. PMC 104411 Слободан приступ. PMID 10330192. 
  4. ^ а б в Imai, Yuzuru; Soda Mariko; et al. (2002). „CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity”. Mol. Cell. United States. 10 (1): 55—67. ISSN 1097-2765. PMID 12150907. doi:10.1016/S1097-2765(02)00583-X. 
  5. ^ Nakamura, Toshinobu; Hinagata Jun-ichi; et al. (2002). „HSP90, HSP70, and GAPDH directly interact with the cytoplasmic domain of macrophage scavenger receptors”. Biochem. Biophys. Res. Commun. United States. 290 (2): 858—64. ISSN 0006-291X. PMID 11785981. doi:10.1006/bbrc.2001.6271. 
  6. ^ Doong, H; Price J; et al. (2000). „CAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-gamma and Hsp70/Hsc70”. Oncogene. ENGLAND. 19 (38): 4385—95. ISSN 0950-9232. PMID 10980614. doi:10.1038/sj.onc.1203797. 
  7. ^ Antoku, K; Maser R S; et al. (2001). „Isolation of Bcl-2 binding proteins that exhibit homology with BAG-1 and suppressor of death domains protein”. Biochem. Biophys. Res. Commun. United States. 286 (5): 1003—10. ISSN 0006-291X. PMID 11527400. doi:10.1006/bbrc.2001.5512. 
  8. ^ Pang, Qishen; Christianson Tracy A; et al. (2002). „The anti-apoptotic function of Hsp70 in the interferon-inducible double-stranded RNA-dependent protein kinase-mediated death signaling pathway requires the Fanconi anemia protein, FANCC”. J. Biol. Chem. United States. 277 (51): 49638—43. ISSN 0021-9258. PMID 12397061. doi:10.1074/jbc.M209386200. 
  9. ^ Reuter, Tanja Y; Medhurst Annette L; et al. (2003). „Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport”. Exp. Cell Res. United States. 289 (2): 211—21. ISSN 0014-4827. PMID 14499622. doi:10.1016/S0014-4827(03)00261-1. 
  10. ^ Shi, Y; Mosser D D; Morimoto R I (1998). „Molecular chaperones as HSF1-specific transcriptional repressors”. Genes Dev. UNITED STATES. 12 (5): 654—66. ISSN 0890-9369. PMC 316571 Слободан приступ. PMID 9499401. 
  11. ^ Zhou, X; Tron V A; et al. (1998). „Heat shock transcription factor-1 regulates heat shock protein-72 expression in human keratinocytes exposed to ultraviolet B light”. J. Invest. Dermatol. UNITED STATES. 111 (2): 194—8. ISSN 0022-202X. PMID 9699716. doi:10.1046/j.1523-1747.1998.00266.x. 
  12. ^ Ruchalski, Kathleen; Mao Haiping; et al. (2003). „HSP72 inhibits apoptosis-inducing factor release in ATP-depleted renal epithelial cells”. Am. J. Physiol., Cell Physiol. United States. 285 (6): C1483—93. ISSN 0363-6143. PMID 12930708. doi:10.1152/ajpcell.00049.2003. 
  13. ^ Ravagnan, L; Gurbuxani S; et al. (2001). „Heat-shock protein 70 antagonizes apoptosis-inducing factor”. Nat. Cell Biol. England. 3 (9): 839—43. ISSN 1465-7392. PMID 11533664. doi:10.1038/ncb0901-839. 

Literatura

  • Andersen JL, Planelles V (2005). „The role of Vpr in HIV-1 pathogenesis.”. Curr. HIV Res. 3 (1): 43—51. PMID 15638722. doi:10.2174/1570162052772988. 
  • Zhao RY, Elder RT (2005). „Viral infections and cell cycle G2/M regulation.”. Cell Res. 15 (3): 143—9. PMID 15780175. doi:10.1038/sj.cr.7290279. 
  • Zhao RY, Bukrinsky M, Elder RT (2005). „HIV-1 viral protein R (Vpr) & host cellular responses.”. Indian J. Med. Res. 121 (4): 270—86. PMID 15817944. 
  • Muthumani K; Choo AY; Premkumar A; et al. (2006). „Human immunodeficiency virus type 1 (HIV-1) Vpr-regulated cell death: insights into mechanism.”. Cell Death Differ. 12. Suppl 1: 962—70. PMID 15832179. doi:10.1038/sj.cdd.4401583. 
  • Grosz MD, Womack JE, Skow LC (1993). „Syntenic conservation of HSP70 genes in cattle and humans.”. Genomics. 14 (4): 863—8. PMID 1478667. doi:10.1016/S0888-7543(05)80106-5. 
  • Veldscholte J; Berrevoets CA; Brinkmann AO; et al. (1992). „Anti-androgens and the mutated androgen receptor of LNCaP cells: differential effects on binding affinity, heat-shock protein interaction, and transcription activation.”. Biochemistry. 31 (8): 2393—9. PMID 1540595. doi:10.1021/bi00123a026. 
  • Abravaya K, Myers MP, Murphy SP, Morimoto RI (1992). „The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression.”. Genes Dev. 6 (7): 1153—64. PMID 1628823. doi:10.1101/gad.6.7.1153. 
  • Milner CM, Campbell RD (1990). „Structure and expression of the three MHC-linked HSP70 genes.”. Immunogenetics. 32 (4): 242—51. PMID 1700760. doi:10.1007/BF00187095. 
  • Sargent CA, Dunham I, Trowsdale J, Campbell RD (1989). „Human major histocompatibility complex contains genes for the major heat shock protein HSP70.”. Proc. Natl. Acad. Sci. U.S.A. 86 (6): 1968—72. PMC 286826 Слободан приступ. PMID 2538825. doi:10.1073/pnas.86.6.1968. 
  • Wu B, Hunt C, Morimoto R (1985). „Structure and expression of the human gene encoding major heat shock protein HSP70.”. Mol. Cell. Biol. 5 (2): 330—41. PMC 366716 Слободан приступ. PMID 2858050. 
  • Goate AM; Cooper DN; Hall C; et al. (1987). „Localization of a human heat-shock HSP 70 gene sequence to chromosome 6 and detection of two other loci by somatic-cell hybrid and restriction fragment length polymorphism analysis.”. Hum. Genet. 75 (2): 123—8. PMID 2880793. doi:10.1007/BF00591072. 
  • Hickey E; Brandon SE; Sadis S; et al. (1986). „Molecular cloning of sequences encoding the human heat-shock proteins and their expression during hyperthermia.”. Gene. 43 (1-2): 147—54. PMID 3019832. doi:10.1016/0378-1119(86)90018-1. 
  • Harrison GS; Drabkin HA; Kao FT; et al. (1987). „Chromosomal location of human genes encoding major heat-shock protein HSP70.”. Somat. Cell Mol. Genet. 13 (2): 119—30. PMID 3470951. doi:10.1007/BF01534692. 
  • Drabent B, Genthe A, Benecke BJ (1987). „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 (22): 8933—48. PMC 311921 Слободан приступ. PMID 3786141. doi:10.1093/nar/14.22.8933. 
  • Hunt C, Morimoto RI (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 (19): 6455—9. PMC 390735 Слободан приступ. PMID 3931075. doi:10.1073/pnas.82.19.6455. 
  • Liao J, Lowthert LA, Ghori N, Omary MB (1995). „The 70-kDa heat shock proteins associate with glandular intermediate filaments in an ATP-dependent manner.”. J. Biol. Chem. 270 (2): 915—22. PMID 7529764. doi:10.1074/jbc.270.2.915. 
  • Selkirk JK, Merrick BA, Stackhouse BL, He C (1995). „Multiple p53 protein isoforms and formation of oligomeric complexes with heat shock proteins Hsp70 and Hsp90 in the human mammary tumor, T47D, cell line.”. Appl. Theor. Electrophor. 4 (1): 11—8. PMID 7811761. 
  • Furlini G; Vignoli M; Re MC; et al. (1994). „Human immunodeficiency virus type 1 interaction with the membrane of CD4+ cells induces the synthesis and nuclear translocation of 70K heat shock protein.”. J. Gen. Virol. 75. (Pt 1) (1): 193—9. PMID 7906708. doi:10.1099/0022-1317-75-1-193. 
  • Maruyama K, Sugano S (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. 
  • Prapapanich V; Chen S; Toran EJ; et al. (1996). „Mutational analysis of the hsp70-interacting protein Hip.”. Mol. Cell. Biol. 16 (11): 6200—7. PMC 231623 Слободан приступ. PMID 8887650. 

Vidi još

Spoljašnje veze

  • HSPA1A+protein,+human на US National Library of Medicine Medical Subject Headings (MeSH)
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Šaperoni/
proteinsko savijanje
Proteini toplotnog šoka/
Šaperonini
Hsp10/GroES (Faktor rane trudnoće) · Hsp27 · Hsp47 · HSP60/GroEL

Hsp40/DnaJ (A1, A2, A3, B1, B2, B11, B4, B6, B9, C1, C3, C5, C6, C7, C10, C11, C13, C14, C19)

Hsp70 (1A, 1B, 1L, 2, 4, 4L, 5, 6, 7, 8, 9, 12A, 14)

Hsp90 (α1, α2, β, ER, TRAP1)
Drugi
Alfa kristalin · Klusterin · Opstanak motornog neurona (SMN1, SMN2)
Sortiranje proteinaUbikvitin
E1 Enzim ubikvitinske aktivacije (UBA1, UBA2, UBA3, UBA5, UBA6, UBA7, ATG7, NAE1, SAE1)

E2 Ubikvitin-konjugujući enzim (A • B • C • D1, D2, D3 • E1, E2, E3 • G1, G2 • H • I • J1, J2 • K • L1, L2, L3, L4, L6 • M • N • O • Q1, Q2 • R1 (CDC34), R2 • S • V1, V2 • Z)

E3 Ubikvitin ligaza (VHL, Kalin, CBL, MDM2, FANCL, UBR1)

Deubikvitinirajući enzim: Ataksin 3 • USP6 • CYLD

ATG3 • BIRC6 • UFC1
Drugi
vidi još Poremećaji posttranslacionih modifikacija
B bsyn: dnk (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)
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PDB Galerija
  • 1hjo​: Protein toplotnog šoka 70 kD, 42 kD ATPaza N-terminalni domen
    1hjo​: Protein toplotnog šoka 70 kD, 42 kD ATPaza N-terminalni domen
  • 1s3x​: Kristalna struktura ljudskog Hsp70 ATPaznog domena
    1s3x​: Kristalna struktura ljudskog Hsp70 ATPaznog domena
  • 1xqs​: Kristalna struktura HspBP1 sržnog domena u kompleksu sa fragmentom Hsp70 ATPaznog domena
    1xqs​: Kristalna struktura HspBP1 sržnog domena u kompleksu sa fragmentom Hsp70 ATPaznog domena