Heat shock 70 kDa protein 4 is a protein that in humans is encoded by the HSPA4 gene.[5][6]

HSPA4
Identifiers
AliasesHSPA4, APG-2, HEL-S-5a, HS24/P52, HSPH2, RY, hsp70, hsp70RY, heat shock protein family A (Hsp70) member 4
External IDsOMIM: 601113; MGI: 1342292; HomoloGene: 1624; GeneCards: HSPA4; OMA:HSPA4 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_198431
NM_002154

NM_008300

RefSeq (protein)

NP_002145

NP_032326

Location (UCSC)Chr 5: 133.05 – 133.11 MbChr 11: 53.15 – 53.19 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

The protein encoded by this gene was originally suggested to be a member of the heat shock protein 70 family.[5] 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.[7]

Interactions

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HSPA4 has been shown to interact with:

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000170606Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020361Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. doi:10.4049/jimmunol.151.2.810. PMID 8335910.
  6. ^ "Entrez Gene: HSPA4 heat shock 70kDa protein 4".
  7. ^ 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.
  8. ^ 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. S2CID 20374981.
  9. ^ 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. doi:10.1016/S1016-8478(23)13770-8. PMID 14503850.
  10. ^ 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.
  11. ^ 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 (inactive 2024-11-02). PMC 376461. PMID 9222609.{{cite journal}}: CS1 maint: DOI inactive as of November 2024 (link)
  12. ^ 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.
  13. ^ 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.
  14. ^ 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

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