From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
Heat shock 70 kDa protein 4 is a protein that in humans is encoded by the HSPA4 gene .[ 5] [ 6]
The protein encoded by this gene was originally suggested to be a member of the heat shock protein 70 family.[ 5] [ 7]
HSPA4 has been shown to interact with:
^ a b c GRCh38: Ensembl release 89: ENSG00000170606 – Ensembl , May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020361 – Ensembl , May 2017^ "Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ "Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ 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 . ^ "Entrez Gene: HSPA4 heat shock 70kDa protein 4" .^ 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 . ^ 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 . ^ 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 . ^ 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 . ^ 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 )^ 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 . ^ 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 . ^ 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 .
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"Specific incorporation of heat shock protein 70 family members into primate lentiviral virions" . Journal of Virology . 76 (9): 4666–70. doi :10.1128/JVI.76.9.4666-4670.2002 . PMC 155079 PMID 11932435 . Freeman BC, Yamamoto KR (Jun 2002). "Disassembly of transcriptional regulatory complexes by molecular chaperones". Science . 296 (5576): 2232–5. doi :10.1126/science.1073051 . PMID 12077419 . S2CID 8844179 .
