CHICK:HS90A

Species (Taxon ID)	Gallus gallus (Chicken). (9031)
Gene Name(s)	HSP90AA1 (synonyms: HSPCA)
Protein Name(s)	Heat shock protein HSP 90-alpha
External Links
UniProt	P11501
EMBL	X07265 X15028
PIR	A32298
RefSeq	NP_001103255.1
UniGene	Gga.6482
ProteinModelPortal	P11501
SMR	P11501
BioGrid	683988
IntAct	P11501
STRING	9031.ENSGALP00000018498
PaxDb	P11501
PRIDE	P11501
GeneID	423463
KEGG	gga:423463
CTD	3320
eggNOG	COG0326
HOVERGEN	HBG007374
InParanoid	P11501
KO	K04079
PhylomeDB	P11501
NextBio	20825936
PRO	PR:P11501
Proteomes	UP000000539
GO	GO:0005737 GO:0005576 GO:0042470 GO:0005524 GO:0030235 GO:0042803 GO:0030911 GO:0045429 GO:0006457 GO:0050790 GO:0006950
Gene3D	3.30.565.10
HAMAP	MF_00505
InterPro	IPR003594 IPR019805 IPR001404 IPR020575 IPR020568
PANTHER	PTHR11528
Pfam	PF00183
PIRSF	PIRSF002583
PRINTS	PR00775
SMART	SM00387
SUPFAM	SSF54211 SSF55874
PROSITE	PS00298

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0051219	phosphoprotein binding	PMID:8423808^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:A0A1D5P4K6 UniProtKB:Q9PSQ5	F	occurs_in:(UBERON:0000955)\|occurs_in:(UBERON:0002107)\|occurs_in:(UBERON:0000993) occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:8423808^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:A0A1D5PFJ6 UniProtKB:F1NWP3 UniProtKB:O73885	F	occurs_in:(UBERON:0000955)\|occurs_in:(UBERON:0002107)\|occurs_in:(UBERON:0000993) occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:8423808^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:A0A1D5PFJ6	F	occurs_in:(UBERON:0000955)\|occurs_in:(UBERON:0002107)\|occurs_in:(UBERON:0000993) occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P07900	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P07900	F		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:11387221^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902751	positive regulation of cell cycle G2/M phase transition	PMID:11387221^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:11387221^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0046790	virion binding	PMID:17522206^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q9WR38:PRO_5000055429)	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:17522206^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:17522206^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0046677	response to antibiotic	PMID:25239533^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(UBERON:0002381)	Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:25239533^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(UBERON:0002381)	Seeded From UniProt	complete
part_of	GO:0043204	perikaryon	PMID:9786217^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000740)	Seeded From UniProt	complete
part_of	GO:0030424	axon	PMID:9786217^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000740)	Seeded From UniProt	complete
involved_in	GO:0032570	response to progesterone	PMID:2779568^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(UBERON:0000993)	Seeded From UniProt	complete
enables	GO:0033142	progesterone receptor binding	PMID:2779568^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07812	F	occurs_in:(UBERON:0000993) occurs_in:(GO:0005829)	Seeded From UniProt	complete
part_of	GO:0043235	receptor complex	PMID:2779568^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	occurs_in:(UBERON:0000993) occurs_in:(GO:0005829)	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:2779568^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0000993)	Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:9716376^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010243	response to organonitrogen compound	PMID:9716376^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(CHEBI:75142)	Seeded From UniProt	complete
involved_in	GO:0014070	response to organic cyclic compound	PMID:9716376^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(CHEBI:75142)	Seeded From UniProt	complete
part_of	GO:0005623	cell	PMID:10504401^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0000970)\|part_of:(UBERON:0000955)\|part_of:(CL:0000232)\|part_of:(UBERON:0002048)\|part_of:(UBERON:0000948)\|part_of:(UBERON:0002107)\|part_of:(UBERON:0002113)\|part_of:(UBERON:0005052)\|part_of:(UBERON:0000160)\|part_of:(UBERON:0003903)	Seeded From UniProt	complete
involved_in	GO:0009409	response to cold	PMID:23636703^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(UBERON:0000948)	Seeded From UniProt	complete
enables	GO:0033142	progesterone receptor binding	PMID:8114727^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07812	F		Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:19735020^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(UBERON:0002113) occurs_in:(UBERON:0002107) occurs_in:(UBERON:0000948)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:19735020^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000182) part_of:(CL:0002543) part_of:(UBERON:0001281) part_of:(UBERON:0006966) part_of:(UBERON:0003517)	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:19735020^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000182) part_of:(CL:0002543) part_of:(UBERON:0001281) part_of:(UBERON:0006966) part_of:(UBERON:0003517)	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:11599567^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0000993)	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:8832390^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:8832390^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion	UniProtKB:P11501	F		Seeded From UniProt	complete
enables	GO:0051879	Hsp90 protein binding	PMID:8832390^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	PMID:8832390^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion	UniProtKB:P11501	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:8832390^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:8832390^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:15135047^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0045429	positive regulation of nitric oxide biosynthetic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P07901	P		Seeded From UniProt	complete
enables	GO:0030911	TPR domain binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P07900	F		Seeded From UniProt	complete
enables	GO:0030235	nitric-oxide synthase regulator activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P07901	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:8423808^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0000993)	Seeded From UniProt	complete
enables	GO:0030331	estrogen receptor binding	PMID:8832390^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P06212	F		Seeded From UniProt	complete
enables	GO:0030331	estrogen receptor binding	PMID:8832390^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:E5L8C9	F		Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000163632 UniProtKB:P07900 UniProtKB:Q76LV2	F		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0001233 PANTHER:PTN000163629 PomBase:SPAC926.04c SGD:S000004798 SGD:S000006161	F		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000163629 UniProtKB:P07900 UniProtKB:P11501	P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0001233 MGI:MGI:96250 PANTHER:PTN000163629 RGD:631409 WB:WBGene00000915	C		Seeded From UniProt	complete
part_of	GO:0043209	myelin sheath	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96250 PANTHER:PTN002609464 RGD:631409	C		Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96250 PANTHER:PTN002609464 RGD:631409 UniProtKB:P11501	C		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96250 PANTHER:PTN000163632 UniProtKB:P07900 UniProtKB:P11501	F		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000201062 PANTHER:PTN000163629 SGD:S000004798	P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000163629 RGD:631409 UniProtKB:P07900 UniProtKB:P11501 WB:WBGene00000915	C		Seeded From UniProt	complete
enables	GO:0030235	nitric-oxide synthase regulator activity	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96250 PANTHER:PTN000163675 UniProtKB:P07900	F		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000201062 PANTHER:PTN000163629 RGD:631409 UniProtKB:P11501	C		Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000201062 FB:FBgn0001233 PANTHER:PTN000163629 RGD:631409 SGD:S000004798 UniProtKB:P11501	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000201062 MGI:MGI:96250 PANTHER:PTN000163629 RGD:631409 TAIR:locus:2161775 TAIR:locus:2161790 UniProtKB:P11501	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96250 PANTHER:PTN000163629 RGD:631409 TAIR:locus:2161775 UniProtKB:P11501 UniProtKB:P40292 dictyBase:DDB_G0267400	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000201062 FB:FBgn0001233 MGI:MGI:96250 PANTHER:PTN000163629 RGD:631409 SGD:S000006161 TAIR:locus:2161775 TAIR:locus:2161790 UniProtKB:P07900 UniProtKB:P11501 UniProtKB:P40292 UniProtKB:Q76LV2 UniProtKB:Q8I0V4 WB:WBGene00000915 ZFIN:ZDB-GENE-990415-94 dictyBase:DDB_G0267400	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96250 PANTHER:PTN002609464 UniProtKB:P11501	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000163632 RGD:631409 UniProtKB:P07900	F		Seeded From UniProt	complete
involved_in	GO:0050790	regulation of catalytic activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0030235	P		Seeded From UniProt	complete
involved_in	GO:0050790	regulation of catalytic activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0030235	P		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001404 InterPro:IPR019805	F		Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001404 InterPro:IPR019805	P		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001404 InterPro:IPR019805	F		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
part_of	GO:0042470	melanosome	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0161	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Smith, DF et al. (1993) Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70. Mol. Cell. Biol. 13 869-76 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Nakai, A & Ishikawa, T (2001) Cell cycle transition under stress conditions controlled by vertebrate heat shock factors. EMBO J. 20 2885-95 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Lin, TW et al. (2007) Chicken heat shock protein 90 is a component of the putative cellular receptor complex of infectious bursal disease virus. J. Virol. 81 8730-41 PubMed GONUTS page
↑ ^4.0 ^4.1 Hao, Y & Gu, XH (2014) Effects of heat shock protein 90 expression on pectoralis major oxidation in broilers exposed to acute heat stress. Poult. Sci. 93 2709-17 PubMed GONUTS page
↑ ^5.0 ^5.1 Morales, AV et al. (1998) Heat shock proteins in retinal neurogenesis: identification of the PM1 antigen as the chick Hsc70 and its expression in comparison to that of other chaperones. Eur. J. Neurosci. 10 3237-45 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 Kost, SL et al. (1989) Binding of heat shock proteins to the avian progesterone receptor. Mol. Cell. Biol. 9 3829-38 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Kawazoe, Y et al. (1998) Proteasome inhibition leads to the activation of all members of the heat-shock-factor family. Eur. J. Biochem. 255 356-62 PubMed GONUTS page
↑ Kawazoe, Y et al. (1999) HSF3 is a major heat shock responsive factor duringchicken embryonic development. Eur. J. Biochem. 265 688-97 PubMed GONUTS page
↑ Zhao, FQ et al. (2013) The role of heat shock proteins in inflammatory injury induced by cold stress in chicken hearts. Cell Stress Chaperones 18 773-83 PubMed GONUTS page
↑ Johnson, JL et al. (1994) Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes. Mol. Cell. Biol. 14 1956-63 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Lei, L et al. (2009) Expression of heat shock protein 90 (Hsp90) and transcription of its corresponding mRNA in broilers exposed to high temperature. Br. Poult. Sci. 50 504-11 PubMed GONUTS page
↑ Haverinen, M et al. (2001) Heat shock protein 90 and the nuclear transport of progesterone receptor. Cell Stress Chaperones 6 256-62 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 ^13.6 ^13.7 Meng, X et al. (1996) Mutational analysis of Hsp90 alpha dimerization and subcellular localization: dimer disruption does not impede "in vivo' interaction with estrogen receptor. J. Cell. Sci. 109 ( Pt 7) 1677-87 PubMed GONUTS page
↑ Katoh, Y et al. (2004) Hsp25, a member of the Hsp30 family, promotes inclusion formation in response to stress. FEBS Lett. 565 28-32 PubMed GONUTS page
↑ ^15.00 ^15.01 ^15.02 ^15.03 ^15.04 ^15.05 ^15.06 ^15.07 ^15.08 ^15.09 ^15.10 ^15.11 ^15.12 ^15.13 ^15.14 ^15.15 ^15.16 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:8423808-1] 1.0 ^1.1 ^1.2 ^1.3 Smith, DF et al. (1993) Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70. Mol. Cell. Biol. 13 869-76 PubMed GONUTS page

[PMID:11387221-2] 2.0 ^2.1 ^2.2 Nakai, A & Ishikawa, T (2001) Cell cycle transition under stress conditions controlled by vertebrate heat shock factors. EMBO J. 20 2885-95 PubMed GONUTS page

[PMID:17522206-3] 3.0 ^3.1 ^3.2 Lin, TW et al. (2007) Chicken heat shock protein 90 is a component of the putative cellular receptor complex of infectious bursal disease virus. J. Virol. 81 8730-41 PubMed GONUTS page

[PMID:25239533-4] 4.0 ^4.1 Hao, Y & Gu, XH (2014) Effects of heat shock protein 90 expression on pectoralis major oxidation in broilers exposed to acute heat stress. Poult. Sci. 93 2709-17 PubMed GONUTS page

[PMID:9786217-5] 5.0 ^5.1 Morales, AV et al. (1998) Heat shock proteins in retinal neurogenesis: identification of the PM1 antigen as the chick Hsc70 and its expression in comparison to that of other chaperones. Eur. J. Neurosci. 10 3237-45 PubMed GONUTS page

[PMID:2779568-6] 6.0 ^6.1 ^6.2 ^6.3 Kost, SL et al. (1989) Binding of heat shock proteins to the avian progesterone receptor. Mol. Cell. Biol. 9 3829-38 PubMed GONUTS page

[PMID:9716376-7] 7.0 ^7.1 ^7.2 Kawazoe, Y et al. (1998) Proteasome inhibition leads to the activation of all members of the heat-shock-factor family. Eur. J. Biochem. 255 356-62 PubMed GONUTS page

[PMID:10504401-8] Kawazoe, Y et al. (1999) HSF3 is a major heat shock responsive factor duringchicken embryonic development. Eur. J. Biochem. 265 688-97 PubMed GONUTS page

[PMID:23636703-9] Zhao, FQ et al. (2013) The role of heat shock proteins in inflammatory injury induced by cold stress in chicken hearts. Cell Stress Chaperones 18 773-83 PubMed GONUTS page

[PMID:8114727-10] Johnson, JL et al. (1994) Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes. Mol. Cell. Biol. 14 1956-63 PubMed GONUTS page

[PMID:19735020-11] 11.0 ^11.1 ^11.2 Lei, L et al. (2009) Expression of heat shock protein 90 (Hsp90) and transcription of its corresponding mRNA in broilers exposed to high temperature. Br. Poult. Sci. 50 504-11 PubMed GONUTS page

[PMID:11599567-12] Haverinen, M et al. (2001) Heat shock protein 90 and the nuclear transport of progesterone receptor. Cell Stress Chaperones 6 256-62 PubMed GONUTS page

[PMID:8832390-13] 13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 ^13.6 ^13.7 Meng, X et al. (1996) Mutational analysis of Hsp90 alpha dimerization and subcellular localization: dimer disruption does not impede "in vivo' interaction with estrogen receptor. J. Cell. Sci. 109 ( Pt 7) 1677-87 PubMed GONUTS page

[PMID:15135047-14] Katoh, Y et al. (2004) Hsp25, a member of the Hsp30 family, promotes inclusion formation in response to stress. FEBS Lett. 565 28-32 PubMed GONUTS page

[PMID:21873635-15] 15.00 ^15.01 ^15.02 ^15.03 ^15.04 ^15.05 ^15.06 ^15.07 ^15.08 ^15.09 ^15.10 ^15.11 ^15.12 ^15.13 ^15.14 ^15.15 ^15.16 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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CHICK:HS90A

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