HSPA4

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HSPA4
Identifiers
Aliases HSPA4, APG-2, HEL-S-5a, HS24/P52, HSPH2, RY, hsp70, hsp70RY, heat shock protein family A (Hsp70) member 4
External IDs MGI: 1342292 HomoloGene: 1624 GeneCards: 3308
RNA expression pattern
PBB GE HSPA4 208814 at tn.png

PBB GE HSPA4 208815 x at tn.png

PBB GE HSPA4 211015 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_198431
NM_002154

NM_008300

RefSeq (protein)

NP_002145.3

n/a

Location (UCSC) Chr 5: 133.05 – 133.11 Mb Chr 11: 53.26 – 53.3 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Heat shock 70 kDa protein 4 is a protein that in humans is encoded by the HSPA4 gene.[1][2]

The protein encoded by this gene was originally suggested to be a member of the heat shock protein 70 family.[1] However it is now known that human HSPA4 is an equivalent to mouse the Apg-2 protein and is a member of the Hsp110 family.[3]

Interactions[edit]

HSPA4 has been shown to interact with:

References[edit]

  1. ^ a b Fathallah DM, Cherif D, Dellagi K, Arnaout MA (Jul 1993). "Molecular cloning of a novel human hsp70 from a B cell line and its assignment to chromosome 5". Journal of Immunology 151 (2): 810–3. PMID 8335910. 
  2. ^ "Entrez Gene: HSPA4 heat shock 70kDa protein 4". 
  3. ^ Kaneko Y, Kimura T, Kishishita M, Noda Y, Fujita J (Apr 1997). "Cloning of apg-2 encoding a novel member of heat shock protein 110 family". Gene 189 (1): 19–24. doi:10.1016/S0378-1119(96)00807-4. PMID 9161406. 
  4. ^ Saleh A, Srinivasula SM, Balkir L, Robbins PD, Alnemri ES (Aug 2000). "Negative regulation of the Apaf-1 apoptosome by Hsp70". Nature Cell Biology 2 (8): 476–83. doi:10.1038/35019510. PMID 10934467. 
  5. ^ a b c Oh WK, Song J (Aug 2003). "Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation". Molecules and Cells 16 (1): 84–91. PMID 14503850. 
  6. ^ a b Johnson CA, White DA, Lavender JS, O'Neill LP, Turner BM (Mar 2002). "Human class I histone deacetylase complexes show enhanced catalytic activity in the presence of ATP and co-immunoprecipitate with the ATP-dependent chaperone protein Hsp70". The Journal of Biological Chemistry 277 (11): 9590–7. doi:10.1074/jbc.M107942200. PMID 11777905. 
  7. ^ Nair SC, Toran EJ, Rimerman RA, Hjermstad S, Smithgall TE, Smith DF (Dec 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. doi:10.1379/1466-1268(1996)001<0237:apomci>2.3.co;2. PMC 376461. PMID 9222609. 
  8. ^ Abravaya K, Myers MP, Murphy SP, Morimoto RI (Jul 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. doi:10.1101/gad.6.7.1153. PMID 1628823. 
  9. ^ Anwar A, Siegel D, Kepa JK, Ross D (Apr 2002). "Interaction of the molecular chaperone Hsp70 with human NAD(P)H:quinone oxidoreductase 1". The Journal of Biological Chemistry 277 (16): 14060–7. doi:10.1074/jbc.M111576200. PMID 11821413. 
  10. ^ Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY, Patterson C (Jun 1999). "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions". Molecular and Cellular Biology 19 (6): 4535–45. doi:10.1128/mcb.19.6.4535. PMC 104411. PMID 10330192. 

Further reading[edit]

External links[edit]