HSPA4

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Heat shock 70kDa protein 4
Identifiers
Symbols HSPA4 ; APG-2; HS24/P52; HSPH2; RY; hsp70; hsp70RY
External IDs OMIM601113 MGI1342292 HomoloGene1624 GeneCards: HSPA4 Gene
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 3308 15525
Ensembl ENSG00000170606 ENSMUSG00000020361
UniProt P34932 Q61316
RefSeq (mRNA) NM_002154 NM_008300
RefSeq (protein) NP_002145 NP_032326
Location (UCSC) Chr 5:
132.39 – 132.44 Mb
Chr 11:
53.26 – 53.3 Mb
PubMed search [1] [2]

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 HDAC1,[4] STUB1,[5] Histone deacetylase 2,[4] TTC1,[6] NAD(P)H dehydrogenase (quinone 1),[7] HSF1,[8][9] HSPBP1,[6] APAF1[10] and DNAJB1.[6]

References[edit]

  1. ^ a b Fathallah DM, Cherif D, Dellagi K, Arnaout MA (Aug 1993). "Molecular cloning of a novel human hsp70 from a B cell line and its assignment to chromosome 5". J Immunol 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 (April 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. ^ a b Johnson, Colin A; White Darren A, Lavender Jayne S, O'Neill Laura P, Turner Bryan M (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". J. Biol. Chem. (United States) 277 (11): 9590–7. doi:10.1074/jbc.M107942200. ISSN 0021-9258. PMID 11777905. 
  5. ^ Ballinger, C A; Connell P; Wu Y; Hu Z; Thompson L J; Yin L Y; Patterson C (Jun 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. PMID 10330192. 
  6. ^ a b c Oh, Won-Kyung; Song Jaewhan (Aug 2003). "Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation". Mol. Cells (Korea (South)) 16 (1): 84–91. ISSN 1016-8478. PMID 14503850. 
  7. ^ Anwar, Adil; Siegel David; Kepa Jadwiga K; Ross David (Apr 2002). "Interaction of the molecular chaperone Hsp70 with human NAD(P)H:quinone oxidoreductase 1". J. Biol. Chem. (United States) 277 (16): 14060–7. doi:10.1074/jbc.M111576200. ISSN 0021-9258. PMID 11821413. 
  8. ^ Nair, S C; Toran E J; Rimerman R A; Hjermstad S; Smithgall T E; Smith D F (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 (UNITED STATES) 1 (4): 237–50. doi:10.1379/1466-1268(1996)001<0237:APOMCI>2.3.CO;2. ISSN 1355-8145. PMC 376461. PMID 9222609. 
  9. ^ Abravaya, K; Myers M P; Murphy S P; Morimoto R I (Jul 1992). "The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression". Genes Dev. (UNITED STATES) 6 (7): 1153–64. doi:10.1101/gad.6.7.1153. ISSN 0890-9369. PMID 1628823. 
  10. ^ Saleh, A; Srinivasula S M; Balkir L; Robbins P D; Alnemri E S (Aug 2000). "Negative regulation of the Apaf-1 apoptosome by Hsp70". Nat. Cell Biol. (ENGLAND) 2 (8): 476–83. doi:10.1038/35019510. ISSN 1465-7392. PMID 10934467. 

Further reading[edit]

External links[edit]