// Workers AI · dad joke modeWhat did HSPA4 say to its friend? "Cell" you later.

HSPA4
Identifiers
Aliases	HSPA4, APG-2, HEL-S-5a, HS24/P52, HSPH2, RY, hsp70, hsp70RY, heat shock protein family A (Hsp70) member 4
External IDs	OMIM: 601113; MGI: 1342292; HomoloGene: 1624; GeneCards: HSPA4; OMA:HSPA4 - orthologs
Gene location (Human)
Chr.	Chromosome 5 (human)
End	133,106,449 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	53,191,284 bp
RNA expression pattern
	Top expressed in
	gonad; ; gingival epithelium; ; islet of Langerhans; ; right testis; ; left testis; ; mucosa of pharynx; ; stromal cell of endometrium; ; amniotic fluid; ; tendon of biceps brachii; ; tonsil;
	Top expressed in
	otic placode; ; saccule; ; tail of embryo; ; genital tubercle; ; otic vesicle; ; primitive streak; ; epiblast; ; Ileal epithelium; ; trigeminal ganglion; ; endothelial cell of lymphatic vessel;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	nucleotide binding; protein binding; ATP binding;
Cellular component	cytoplasm; cytosol; extracellular exosome; nucleus;
Biological process	response to unfolded protein; protein insertion into mitochondrial outer membrane; chaperone-mediated protein complex assembly;
	Sources:Amigo / QuickGO
Orthologs
	3308
	15525
	ENSG00000170606
	ENSMUSG00000020361
	P34932
	Q61316; Q3U2G2
	NM_198431; NM_002154
	NM_008300
	NP_002145
	NP_032326
	Wikidata
View/Edit Human	View/Edit Mouse

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] 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 2 3 GRCh38: Ensembl release 89: ENSG00000170606 – Ensembl, May 2017
1 2 3 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.
1 2 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.
1 2 3 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.
1 2 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 12 July 2025). PMC 376461. PMID 9222609.{{cite journal}}: CS1 maint: DOI inactive as of July 2025 (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.

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.
Liao J, Lowthert LA, Ghori N, Omary MB (Jan 1995). "The 70-kDa heat shock proteins associate with glandular intermediate filaments in an ATP-dependent manner". The Journal of Biological Chemistry. 270 (2): 915–22. doi:10.1074/jbc.270.2.915. PMID 7529764.
Furlini G, Vignoli M, Re MC, Gibellini D, Ramazzotti E, Zauli G, La Placa M (Jan 1994). "Human immunodeficiency virus type 1 interaction with the membrane of CD4+ cells induces the synthesis and nuclear translocation of 70K heat shock protein". The Journal of General Virology. 75 (1): 193–9. doi:10.1099/0022-1317-75-1-193. PMID 7906708.
Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Schulte AM, Fischer S, Sachse GE, Häfner S, Stelck S, Gassen HG (Mar 1997). "Identification and characterization of a novel hsc70-like gene in the human lung tumor cell line HS24". DNA and Cell Biology. 16 (3): 257–68. doi:10.1089/dna.1997.16.257. PMID 9115634.
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.
Bruner KL, Derfoul A, Robertson NM, Guerriero G, Fernandes-Alnemri T, Alnemri ES, Litwack G (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, Kramer JM, Morimoto RI (Jul 1998). "Negative regulation of the heat shock transcriptional response by HSBP1". Genes & Development. 12 (13): 1962–74. doi:10.1101/gad.12.13.1962. PMC 316975. PMID 9649501.
Naylor DJ, Stines AP, Hoogenraad NJ, Høj PB (Aug 1998). "Evidence for the existence of distinct mammalian cytosolic, microsomal, and two mitochondrial GrpE-like proteins, the Co-chaperones of specific Hsp70 members". The Journal of Biological Chemistry. 273 (33): 21169–77. doi:10.1074/jbc.273.33.21169. PMID 9694873.
Melville MW, Tan SL, Wambach M, Song J, Morimoto RI, Katze MG (Feb 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". The Journal of Biological Chemistry. 274 (6): 3797–803. doi:10.1074/jbc.274.6.3797. PMID 9920933.
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.
Liu H, Vuyyuru VB, Pham CD, Yang Y, Singh B (Jun 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, Tokuchi H, Nishiyama H, Kaneko Y, Tatsumi K, Okuno H, Tomiwa K, Fujita J (Sep 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, Zhou S, Zhou Q (Jan 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". The Journal of Biological Chemistry. 275 (1): 279–87. doi:10.1074/jbc.275.1.279. PMID 10617616.
Agostini I, Popov S, Li J, Dubrovsky L, Hao T, Bukrinsky M (Sep 2000). "Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex". Experimental Cell Research. 259 (2): 398–403. doi:10.1006/excr.2000.4992. PMID 10964507.
Kim M, Jiang LH, Wilson HL, North RA, Surprenant A (Nov 2001). "Proteomic and functional evidence for a P2X7 receptor signalling complex". The EMBO Journal. 20 (22): 6347–58. doi:10.1093/emboj/20.22.6347. PMC 125721. PMID 11707406.
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.
Gurer C, Cimarelli A, Luban J (May 2002). "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.

External links

HSPA4+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000170606 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid8335910-5] 1 2 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-6] "Entrez Gene: HSPA4 heat shock 70kDa protein 4".

[pmid9161406-7] 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.

[pmid10934467-8] 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.

[pmid14503850-9] 1 2 3 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.

[pmid11777905-10] 1 2 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.

[pmid9222609-11] 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 12 July 2025). PMC 376461. PMID 9222609.{{cite journal}}: CS1 maint: DOI inactive as of July 2025 (link)

[pmid1628823-12] 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.

[pmid11821413-13] 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.

[pmid10330192-14] 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.

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// Workers AI · dad joke modeWhat did HSPA4 say to its friend? "Cell" you later.

Interactions

References

Further reading

External links