HSPA4

Proteína de choque térmico 4
Estructuras disponibles
PDB	Buscar ortólogos: PDBe, RCSB
Identificadores
Símbolos	HSPA4 (HGNC: 5237) APG-2; HS24/P52; MGC131852; RY; hsp70; hsp70RY
Identificadores; externos	OMIM: 601113 ; EBI: HSPA4; GeneCards: Gen HSPA4; UniProt: HSPA4;
Locus	Cr. 5 q31.1
	Referencias: AmiGO / QuickGO
Ortólogos
Humano	Ratón
3308
P34932	n/a
NP_002145	n/a
	v; t; e;
	[editar datos en Wikidata]

La proteína de choque térmico 4 (HSPA4) es una proteína codificada en humanos por el gen HSPA4.^[1]^[2]

La proteína codificada por este gen fue originalmente propuesta como un miembro de la familia de proteínas de choque térmico Hsp70.^[1] Sin embargo, ahora se sabe que la proteína humana HSPA4 es un ortólogo de la proteína de ratón Apg-2 y es miembro de la familia Hsp110.^[3]

Interacciones editar

La proteína HSPA4 ha demostrado ser capaz de interaccionar con:

Referencias editar

↑ ^a ^b Fathallah DM, Cherif D, Dellagi K, Arnaout MA (julio de 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.
↑ «Entrez Gene: HSPA4 heat shock 70kDa protein 4».
↑ Kaneko Y, Kimura T, Kishishita M, Noda Y, Fujita J (abril de 1997). «Cloning of apg-2 encoding a novel member of heat shock protein 110 family». Gene 189 (1): 19-24. PMID 9161406. doi:10.1016/S0378-1119(96)00807-4.
↑ ^a ^b Johnson, Colin A; White Darren A, Lavender Jayne S, O'Neill Laura P, Turner Bryan M (Mar. de 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. (EE. UU.) 277 (11): 9590-7. ISSN 0021-9258. PMID 11777905. doi:10.1074/jbc.M107942200.
↑ Ballinger, C A; Connell P, Wu Y, Hu Z, Thompson L J, Yin L Y, Patterson C (Jun. de 1999). «Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions». Mol. Cell. Biol. (EE. UU.) 19 (6): 4535-45. ISSN 0270-7306. PMID 10330192.
↑ ^a ^b ^c Oh, Won-Kyung; Song Jaewhan (Aug. de 2003). «Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation». Mol. Cells (Corea del Sur) 16 (1): 84-91. ISSN 1016-8478. PMID 14503850.
↑ Anwar, Adil; Siegel David, Kepa Jadwiga K, Ross David (Apr. de 2002). «Interaction of the molecular chaperone Hsp70 with human NAD(P)H:quinone oxidoreductase 1». J. Biol. Chem. (EE. UU.) 277 (16): 14060-7. ISSN 0021-9258. PMID 11821413. doi:10.1074/jbc.M111576200.
↑ Nair, S C; Toran E J, Rimerman R A, Hjermstad S, Smithgall T E, Smith D F (Dec. de 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 (EE. UU.) 1 (4): 237-50. ISSN 1355-8145. PMID 9222609.
↑ Abravaya, K; Myers M P, Murphy S P, Morimoto R I (Jul. de 1992). «The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression». Genes Dev. (EE. UU.) 6 (7): 1153-64. ISSN 0890-9369. PMID 1628823.
↑ Saleh, A; Srinivasula S M, Balkir L, Robbins P D, Alnemri E S (Aug. de 2000). «Negative regulation of the Apaf-1 apoptosome by Hsp70». Nat. Cell Biol. (Inglaterra) 2 (8): 476-83. ISSN 1465-7392. PMID 10934467. doi:10.1038/35019510.

Enlaces externos editar

MeSH: HSPA4+protein,+human (en inglés)

Datos: Q18027348

[pmid8335910-1] Fathallah DM, Cherif D, Dellagi K, Arnaout MA (julio de 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.

[entrez-2] «Entrez Gene: HSPA4 heat shock 70kDa protein 4».

[pmid9161406-3] Kaneko Y, Kimura T, Kishishita M, Noda Y, Fujita J (abril de 1997). «Cloning of apg-2 encoding a novel member of heat shock protein 110 family». Gene 189 (1): 19-24. PMID 9161406. doi:10.1016/S0378-1119(96)00807-4.

[pmid11777905-4] Johnson, Colin A; White Darren A, Lavender Jayne S, O'Neill Laura P, Turner Bryan M (Mar. de 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. (EE. UU.) 277 (11): 9590-7. ISSN 0021-9258. PMID 11777905. doi:10.1074/jbc.M107942200.

[pmid10330192-5] Ballinger, C A; Connell P, Wu Y, Hu Z, Thompson L J, Yin L Y, Patterson C (Jun. de 1999). «Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions». Mol. Cell. Biol. (EE. UU.) 19 (6): 4535-45. ISSN 0270-7306. PMID 10330192.

[pmid14503850-6] Oh, Won-Kyung; Song Jaewhan (Aug. de 2003). «Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation». Mol. Cells (Corea del Sur) 16 (1): 84-91. ISSN 1016-8478. PMID 14503850.

[pmid11821413-7] Anwar, Adil; Siegel David, Kepa Jadwiga K, Ross David (Apr. de 2002). «Interaction of the molecular chaperone Hsp70 with human NAD(P)H:quinone oxidoreductase 1». J. Biol. Chem. (EE. UU.) 277 (16): 14060-7. ISSN 0021-9258. PMID 11821413. doi:10.1074/jbc.M111576200.

[pmid9222609-8] Nair, S C; Toran E J, Rimerman R A, Hjermstad S, Smithgall T E, Smith D F (Dec. de 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 (EE. UU.) 1 (4): 237-50. ISSN 1355-8145. PMID 9222609.

[pmid1628823-9] Abravaya, K; Myers M P, Murphy S P, Morimoto R I (Jul. de 1992). «The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression». Genes Dev. (EE. UU.) 6 (7): 1153-64. ISSN 0890-9369. PMID 1628823.

[pmid10934467-10] Saleh, A; Srinivasula S M, Balkir L, Robbins P D, Alnemri E S (Aug. de 2000). «Negative regulation of the Apaf-1 apoptosome by Hsp70». Nat. Cell Biol. (Inglaterra) 2 (8): 476-83. ISSN 1465-7392. PMID 10934467. doi:10.1038/35019510.

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