HSPA4

Heat shock 70kDa protein 4
Identifiers
SymbolsHSPA4 ; APG-2; HEL-S-5a; HS24/P52; HSPH2; RY; hsp70; hsp70RY
External IDsOMIM: 601113 MGI: 1342292 HomoloGene: 1624 GeneCards: HSPA4 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez330815525
EnsemblENSG00000170606ENSMUSG00000020361
UniProtP34932Q61316
RefSeq (mRNA)NM_002154NM_008300
RefSeq (protein)NP_002145NP_032326
Location (UCSC)Chr 5:
132.39 – 132.44 Mb		Chr 11:
53.26 – 53.3 Mb
PubMed search

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

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

  1. ↑ 1.0 1.1 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. ↑ 4.0 4.1 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. ↑ 6.0 6.1 6.2 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

  • 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. doi:10.1101/gad.6.7.1153. PMID 1628823.
  • 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. doi:10.1074/jbc.270.2.915. PMID 7529764.
  • 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 (1): 193–9. doi:10.1099/0022-1317-75-1-193. PMID 7906708.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Schulte AM; Fischer S; Sachse GE et al. (1997). "Identification and characterization of a novel hsc70-like gene in the human lung tumor cell line HS24". DNA Cell Biol. 16 (3): 257–68. doi:10.1089/dna.1997.16.257. PMID 9115634.
  • Kaneko Y; Kimura T; Kishishita M et al. (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.
  • Bruner KL; Derfoul A; Robertson NM et al. (1998). "The unliganded mineralocorticoid receptor is associated with heat shock proteins 70 and 90 and the immunophilin FKBP-52". Receptors & signal transduction 7 (2): 85–98. PMID 9392437.
  • Satyal SH; Chen D; Fox SG et al. (1998). "Negative regulation of the heat shock transcriptional response by HSBP1". Genes Dev. 12 (13): 1962–74. doi:10.1101/gad.12.13.1962. PMC 316975. PMID 9649501.
  • Naylor DJ, Stines AP, Hoogenraad NJ, Høj PB (1998). "Evidence for the existence of distinct mammalian cytosolic, microsomal, and two mitochondrial GrpE-like proteins, the Co-chaperones of specific Hsp70 members". J. Biol. Chem. 273 (33): 21169–77. doi:10.1074/jbc.273.33.21169. PMID 9694873.
  • Melville MW; Tan SL; Wambach M et al. (1999). "The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity". J. Biol. Chem. 274 (6): 3797–803. doi:10.1074/jbc.274.6.3797. PMID 9920933.
  • Ballinger CA; Connell P; Wu Y 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. 19 (6): 4535–45. PMC 104411. PMID 10330192.
  • Liu H; Vuyyuru VB; Pham CD et al. (1999). "Evidence of an interaction between Mos and Hsp70: a role of the Mos residue serine 3 in mediating Hsp70 association". Oncogene 18 (23): 3461–70. doi:10.1038/sj.onc.1202699. PMID 10376524.
  • Nonoguchi K; Itoh K; Xue JH et al. (1999). "Cloning of human cDNAs for Apg-1 and Apg-2, members of the Hsp110 family, and chromosomal assignment of their genes". Gene 237 (1): 21–8. doi:10.1016/S0378-1119(99)00325-X. PMID 10524232.
  • O'Keeffe B; Fong Y; Chen D et al. (2000). "Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription". J. Biol. Chem. 275 (1): 279–87. doi:10.1074/jbc.275.1.279. PMID 10617616.
  • Agostini I; Popov S; Li J et al. (2000). "Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex". Exp. Cell Res. 259 (2): 398–403. doi:10.1006/excr.2000.4992. PMID 10964507.
  • Kim M; Jiang LH; Wilson HL et al. (2002). "Proteomic and functional evidence for a P2X7 receptor signalling complex". EMBO J. 20 (22): 6347–58. doi:10.1093/emboj/20.22.6347. PMC 125721. PMID 11707406.
  • Johnson CA; White DA; Lavender JS et al. (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. 277 (11): 9590–7. doi:10.1074/jbc.M107942200. PMID 11777905.
  • Gurer C, Cimarelli A, Luban J (2002). "Specific Incorporation of Heat Shock Protein 70 Family Members into Primate Lentiviral Virions". J. Virol. 76 (9): 4666–70. doi:10.1128/JVI.76.9.4666-4670.2002. PMC 155079. PMID 11932435.
  • Freeman BC, Yamamoto KR (2002). "Disassembly of transcriptional regulatory complexes by molecular chaperones". Science 296 (5576): 2232–5. doi:10.1126/science.1073051. PMID 12077419.

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