HSPA4

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
Gene location (Human)
Chr.Chromosome 5 (human)[1]
Band5q31.1Start133,052,013 bp[1]
End133,106,449 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

3308

15525

Ensembl

ENSG00000170606

ENSMUSG00000020361

UniProt

P34932

Q61316
Q3U2G2

RefSeq (mRNA)

NM_198431
NM_002154

NM_008300

RefSeq (protein)

NP_002145

NP_032326

Location (UCSC)Chr 5: 133.05 – 133.11 MbChr 11: 53.26 – 53.3 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

HSPA4 has been shown to interact with:

References

  1. GRCh38: Ensembl release 89: ENSG00000170606 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000020361 - Ensembl, 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. 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.
  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. 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.
  10. 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. PMC 376461. PMID 9222609.
  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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