HUMAN:HS90B

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	HSP90AB1 (synonyms: HSP90B, HSPC2, HSPCB)
Protein Name(s)	Heat shock protein HSP 90-beta HSP 90 Heat shock 84 kDa HSP 84 HSP84
External Links
UniProt	P08238
EMBL	M16660 J04988 AY359878 AL136543 AK312255 DQ314872 AL139392 CH471081 BC004928 BC009206 BC012807 BC014485 BC016753 BC068474 AH007358 AF275719
CCDS	CCDS4909.1
PIR	A29461 T46243
RefSeq	NP_001258898.1 NP_001258899.1 NP_001258900.1 NP_031381.2 XP_005249132.1
UniGene	Hs.509736
PDB	1QZ2 1UYM 2L6J 3NMQ 3PRY 3UQ3
PDBsum	1QZ2 1UYM 2L6J 3NMQ 3PRY 3UQ3
ProteinModelPortal	P08238
SMR	P08238
BioGrid	109558
DIP	DIP-413N
IntAct	P08238
MINT	MINT-99712
STRING	9606.ENSP00000325875
BindingDB	P08238
ChEMBL	CHEMBL4303
PhosphoSite	P08238
DMDM	17865718
OGP	P08238
MaxQB	P08238
PaxDb	P08238
PeptideAtlas	P08238
PRIDE	P08238
DNASU	3326
Ensembl	ENST00000353801 ENST00000371554 ENST00000371646 ENST00000620073
GeneID	3326
KEGG	hsa:3326
UCSC	uc003oxa.2
CTD	3326
GeneCards	GC06P044214
H-InvDB	HIX0031498 HIX0057380
HGNC	HGNC:5258
HPA	CAB005230 HPA055729
MIM	140572
neXtProt	NX_P08238
PharmGKB	PA29524
eggNOG	COG0326
GeneTree	ENSGT00760000119253
HOGENOM	HOG000031988
HOVERGEN	HBG007374
InParanoid	P08238
KO	K04079
OMA	EIPSRVT
OrthoDB	EOG780RM0
PhylomeDB	P08238
TreeFam	TF300686
Reactome	REACT_160086 REACT_19236 REACT_200624 REACT_200744 REACT_200775 REACT_75808
ChiTaRS	HSP90AB1
EvolutionaryTrace	P08238
GeneWiki	HSP90AB1
GenomeRNAi	3326
NextBio	13182
PRO	PR:P08238
Proteomes	UP000005640
Bgee	P08238
CleanEx	HS_HSP90AB1
ExpressionAtlas	P08238
Genevestigator	P08238
GO	GO:0016324 GO:0016323 GO:0031526 GO:0009986 GO:0005737 GO:0005829 GO:0070062 GO:0016234 GO:0042470 GO:0016020 GO:0005739 GO:0005524 GO:0002135 GO:0032564 GO:0003725 GO:0005525 GO:0023026 GO:0030235 GO:0044822 GO:0030911 GO:0002134 GO:0007411 GO:0071353 GO:0071407 GO:0038096 GO:0045087 GO:0043524 GO:0032435 GO:0035872 GO:0001890 GO:0045793 GO:0045429 GO:0032092 GO:0033160 GO:0071902 GO:0006457 GO:0060334 GO:0060338 GO:0009651 GO:0006986
Gene3D	3.30.565.10
HAMAP	MF_00505
InterPro	IPR003594 IPR019805 IPR001404 IPR020575 IPR020568
PANTHER	PTHR11528
Pfam	PF02518 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
	GO:0016032	viral process	PMID:24098578^[1]	ECO:0000314			P		Figure 3: RD cells transfected with Hsp90-alpha and Hsp90-beta specific siRNA. Only Hsp90-beta siRNA prevented EV71 capsid protein expression showing Hsp90-beta is involved in EV71 infection	complete CACAO 8833
	GO:0019062	virion attachment to host cell	PMID:24098578^[1]	ECO:0000315			P		Figure 5B	complete CACAO 8850
	GO:0043206	extracellular fibril organization	PMID:24466266^[2]	ECO:0000315			P		Fig 7	complete
	GO:0097435	fibril organization	PMID:24466266^[2]	ECO:0000315			P		An Interaction observed in vitro and colocalization of Hsp90 and FN in both normal and cancer cell lines were investigated using confocal microscopy and the DOC assay. These methods helped to determine the effect of exogenous Hsp90β on FN matrix formation and morphology in Hs578T cells. Treatment of the Hs578T cell line with exogenous soluble Hsp90β led to an increase in insoluble FN relative to soluble FN, suggesting a role for extracellular Hsp90 in fibril formation. Other methods used include co-immunoprecipitation, solid phase binding assay, immunoblot analysis, SPR spectroscopy and mass spectrometry.	complete CACAO 9330
involved_in	GO:1902949	positive regulation of tau-protein kinase activity	GO_REF:0000111	ECO:0000305	curator inference used in manual assertion	GO:1904031	P	has_regulation_target:(UniProtKB:Q00535)	Seeded From UniProt	complete
involved_in	GO:1904031	positive regulation of cyclin-dependent protein kinase activity	PMID:17517623^[3]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P34058	P	has_regulation_target:(UniProtKB:Q00535) regulates_o_occurs_in:(CL:0002609) occurs_in:(CL:0002609)	Seeded From UniProt	complete
involved_in	GO:1901799	negative regulation of proteasomal protein catabolic process	PMID:17517623^[3]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P34058	P	has_regulation_target:(UniProtKB:Q15078:PRO_0000004794) regulates_o_occurs_in:(CL:0002609) occurs_in:(CL:0002609) regulates:(GO:0097472)\|has_regulation_target(UniProtKB:P10636) regulates_o_occurs_in:(CL:0002609) occurs_in:(CL:0002609)	Seeded From UniProt	complete
involved_in	GO:0051248	negative regulation of protein metabolic process	PMID:17517623^[3]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P34058	P	regulates_o_occurs_in:(CL:0002609) occurs_in:(CL:0002609)	Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:16207813^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9UNE7	F		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11499	C	part_of:(CL:0002608) part_of:(GO:0043025)	Seeded From UniProt	complete
part_of	GO:0044295	axonal growth cone	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11499	C	part_of:(CL:0002608) exists_during:(GO:0031175) exists_during:(GO:0030010)	Seeded From UniProt	complete
part_of	GO:0044294	dendritic growth cone	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11499	C	part_of:(CL:0002608) exists_during:(GO:0031175) exists_during:(GO:0030010)	Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11499	C	part_of:(CL:0002608)	Seeded From UniProt	complete
involved_in	GO:1903827	regulation of cellular protein localization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11499	P	occurs_in:(CL:0002608) has_regulation_target:(UniProtKB:O60282) regulates_o_occurs_in:(CL:0002608) causally_upstream_of:(GO:0030010)	Seeded From UniProt	complete
involved_in	GO:0051897	positive regulation of protein kinase B signaling	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11499	P	occurs_in:(CL:0002608) regulates_o_occurs_in:(CL:0002608)	Seeded From UniProt	complete
involved_in	GO:0048675	axon extension	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11499	P	occurs_in:(CL:0002608)	Seeded From UniProt	complete
involved_in	GO:0033138	positive regulation of peptidyl-serine phosphorylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11499	P	occurs_in:(CL:0002608) regulates_o_occurs_in:(CL:0002608) part_of:(GO:0051897)	Seeded From UniProt	complete
involved_in	GO:0030010	establishment of cell polarity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11499	P	occurs_in:(CL:0002608)	Seeded From UniProt	complete
involved_in	GO:0021955	central nervous system neuron axonogenesis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11499	P	occurs_in:(CL:0002608)	Seeded From UniProt	complete
part_of	GO:1990565	HSP90-CDC37 chaperone complex	PMID:21855797^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0048156	tau protein binding	PMID:28386764^[6]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	PMID:15713458^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P53041	F		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:10811660^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0051131	chaperone-mediated protein complex assembly	PMID:10811660^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:10811660^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:10811660^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0043008	ATP-dependent protein binding	PMID:10811660^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q15185	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:10543959^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:10543959^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0043008	ATP-dependent protein binding	PMID:10543959^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q15185	F		Seeded From UniProt	complete
involved_in	GO:0007004	telomere maintenance via telomerase	PMID:10197982^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051973	positive regulation of telomerase activity	PMID:10197982^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0034751	aryl hydrocarbon receptor complex	PMID:15581363^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:11785981^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	PMID:11785981^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P21758	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:24880080^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:1990226	histone methyltransferase binding	PMID:24880080^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9NRG4	F		Seeded From UniProt	complete
enables	GO:0045296	cadherin binding	PMID:25468996^[14]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:23349634^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0032516	positive regulation of phosphoprotein phosphatase activity	PMID:26593036^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:10791971^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030511	positive regulation of transforming growth factor beta receptor signaling pathway	PMID:24613385^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032435	negative regulation of proteasomal ubiquitin-dependent protein catabolic process	PMID:24613385^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000010	positive regulation of protein localization to cell surface	PMID:23431407^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:20353823^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07900	F		Seeded From UniProt	complete
enables	GO:0019900	kinase binding	PMID:20353823^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q02156	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:18239673^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:18239673^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0070182	DNA polymerase binding	PMID:19751963^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O14746	F		Seeded From UniProt	complete
involved_in	GO:1905323	telomerase holoenzyme complex assembly	PMID:10197982^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0070182	DNA polymerase binding	PMID:10197982^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O14746	F		Seeded From UniProt	complete
involved_in	GO:0045597	positive regulation of cell differentiation	PMID:18239673^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0046983	protein dimerization activity	PMID:7588731^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0031396	regulation of protein ubiquitination	PMID:16809764^[24]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q9UPR3)	Seeded From UniProt	complete
enables	GO:0042826	histone deacetylase binding	PMID:16809764^[24]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9BY41	F		Seeded From UniProt	complete
involved_in	GO:1901389	negative regulation of transforming growth factor beta activation	PMID:20599762^[25]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042277	peptide binding	PMID:20599762^[25]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P01137:PRO_0000033762	F		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:20599762^[25]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0019062	virion attachment to host cell	PMID:24098578^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097435	supramolecular fiber organization	PMID:24466266^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019900	kinase binding	PMID:21855797^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O70405	F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[26]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[27]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[28]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[28]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
enables	GO:0023026	MHC class II protein complex binding	PMID:20458337^[28]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:20833797^[29]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001134)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16580629^[30]	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:0003723	RNA binding	PMID:22681889^[31]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[32]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		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
colocalizes_with	GO:0008180	COP9 signalosome	PMID:18850735^[33]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006986	response to unfolded protein	PMID:2768249^[34]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071157	negative regulation of cell cycle arrest	PMID:22843495^[35]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903827	regulation of cellular protein localization	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96247 PANTHER:PTN002609442 UniProtKB:P08238	P		Seeded From UniProt	complete
involved_in	GO:1901799	negative regulation of proteasomal protein catabolic process	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96247 PANTHER:PTN002609442 RGD:1303075 UniProtKB:P08238	P		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0001233 PANTHER:PTN000163527 PomBase:SPAC926.04c SGD:S000004798 SGD:S000006161	F		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96247 PANTHER:PTN002609442	F		Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000201062 EcoGene:EG10461 PANTHER:PTN000163527 PomBase:SPAC926.04c SGD:S000004798 SGD:S000006161 WB:WBGene00000915	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002609442 RGD:1303075 UniProtKB:P08238	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96247 PANTHER:PTN002609442 RGD:1303075 UniProtKB:P08238	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002609442 RGD:1303075 UniProtKB:P08238	F		Seeded From UniProt	complete
involved_in	GO:0060338	regulation of type I interferon-mediated signaling pathway	PMID:16280321^[37]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060334	regulation of interferon-gamma-mediated signaling pathway	PMID:16280321^[37]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032435	negative regulation of proteasomal ubiquitin-dependent protein catabolic process	PMID:16280321^[37]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003725	double-stranded RNA binding	PMID:21266579^[38]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22939624^[39]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P08238	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21183720^[40]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P08238	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1990565	HSP90-CDC37 chaperone complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	C		Seeded From UniProt	complete
involved_in	GO:1904031	positive regulation of cyclin-dependent protein kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	P		Seeded From UniProt	complete
involved_in	GO:1903827	regulation of cellular protein localization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	P		Seeded From UniProt	complete
involved_in	GO:1901799	negative regulation of proteasomal protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	P		Seeded From UniProt	complete
involved_in	GO:0071353	cellular response to interleukin-4	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	P		Seeded From UniProt	complete
involved_in	GO:0051897	positive regulation of protein kinase B signaling	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	P		Seeded From UniProt	complete
involved_in	GO:0048675	axon extension	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	C		Seeded From UniProt	complete
enables	GO:0048156	tau protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	F		Seeded From UniProt	complete
part_of	GO:0044295	axonal growth cone	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	C		Seeded From UniProt	complete
part_of	GO:0044294	dendritic growth cone	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	C		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	P		Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	C		Seeded From UniProt	complete
involved_in	GO:0033138	positive regulation of peptidyl-serine phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	P		Seeded From UniProt	complete
involved_in	GO:0030010	establishment of cell polarity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	P		Seeded From UniProt	complete
involved_in	GO:0021955	central nervous system neuron axonogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	P		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	F		Seeded From UniProt	complete
enables	GO:0019900	kinase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	F		Seeded From UniProt	complete
enables	GO:0019887	protein kinase regulator activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	F		Seeded From UniProt	complete
involved_in	GO:0010033	response to organic substance	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	C		Seeded From UniProt	complete
involved_in	GO:0001890	placenta development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11499 ensembl:ENSMUSP00000024739	P		Seeded From UniProt	complete
part_of	GO:1990917	ooplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	C		Seeded From UniProt	complete
part_of	GO:1990913	sperm head plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	C		Seeded From UniProt	complete
involved_in	GO:1904031	positive regulation of cyclin-dependent protein kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	P		Seeded From UniProt	complete
involved_in	GO:1903660	negative regulation of complement-dependent cytotoxicity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	P		Seeded From UniProt	complete
involved_in	GO:1901799	negative regulation of proteasomal protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	P		Seeded From UniProt	complete
involved_in	GO:0071902	positive regulation of protein serine/threonine kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	P		Seeded From UniProt	complete
involved_in	GO:0071407	cellular response to organic cyclic compound	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	P		Seeded From UniProt	complete
involved_in	GO:0051248	negative regulation of protein metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	P		Seeded From UniProt	complete
involved_in	GO:0045793	positive regulation of cell size	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	P		Seeded From UniProt	complete
enables	GO:0044325	ion channel binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	F		Seeded From UniProt	complete
involved_in	GO:0043524	negative regulation of neuron apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	P		Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	P		Seeded From UniProt	complete
involved_in	GO:0042220	response to cocaine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	P		Seeded From UniProt	complete
involved_in	GO:0035690	cellular response to drug	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	P		Seeded From UniProt	complete
enables	GO:0032564	dATP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	F		Seeded From UniProt	complete
involved_in	GO:0032092	positive regulation of protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	P		Seeded From UniProt	complete
part_of	GO:0031526	brush border membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	C		Seeded From UniProt	complete
enables	GO:0017098	sulfonylurea receptor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	F		Seeded From UniProt	complete
part_of	GO:0016324	apical plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	C		Seeded From UniProt	complete
part_of	GO:0016323	basolateral plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	C		Seeded From UniProt	complete
part_of	GO:0016234	inclusion body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	C		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	C		Seeded From UniProt	complete
involved_in	GO:0009651	response to salt stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	P		Seeded From UniProt	complete
enables	GO:0008144	drug binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	C		Seeded From UniProt	complete
part_of	GO:0005765	lysosomal membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	C		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	F		Seeded From UniProt	complete
enables	GO:0002135	CTP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	F		Seeded From UniProt	complete
enables	GO:0002134	UTP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P34058 ensembl:ENSRNOP00000026920	F		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
part_of	GO:1904813	ficolin-1-rich granule lumen	Reactome:R-HSA-6800434	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1900034	regulation of cellular response to heat	Reactome:R-HSA-3371571	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	Reactome:R-HSA-8852362	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042623	ATPase activity, coupled	Reactome:R-HSA-8939203	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0038096	Fc-gamma receptor signaling pathway involved in phagocytosis	Reactome:R-HSA-2029480	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0034774	secretory granule lumen	Reactome:R-HSA-6798748	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006805	xenobiotic metabolic process	Reactome:R-HSA-211945	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-8937169 Reactome:R-HSA-8936849 Reactome:R-HSA-8852362 Reactome:R-HSA-874087 Reactome:R-HSA-873951 Reactome:R-HSA-844612 Reactome:R-HSA-844610 Reactome:R-HSA-844440 Reactome:R-HSA-5618110 Reactome:R-HSA-5618107 Reactome:R-HSA-5618105 Reactome:R-HSA-5618099 Reactome:R-HSA-5618098 Reactome:R-HSA-5618085 Reactome:R-HSA-5618080 Reactome:R-HSA-5618073 Reactome:R-HSA-5324632 Reactome:R-HSA-419645 Reactome:R-HSA-419644 Reactome:R-HSA-3371586 Reactome:R-HSA-3371503 Reactome:R-HSA-1306876 Reactome:R-HSA-1296421	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-9038161 Reactome:R-HSA-9032751 Reactome:R-HSA-8939204 Reactome:R-HSA-8939203 Reactome:R-HSA-8937191 Reactome:R-HSA-8937169 Reactome:R-HSA-5618093 Reactome:R-HSA-5618080 Reactome:R-HSA-5324617 Reactome:R-HSA-5082409 Reactome:R-HSA-5082356	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-6800434 Reactome:R-HSA-6798748	ECO:0000304	author statement supported by traceable reference used in manual assertion		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:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		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
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		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:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		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
edit table

Notes

References

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

↑ ^1.0 ^1.1 ^1.2 Tsou, YL et al. (2013) Heat shock protein 90: role in enterovirus 71 entry and assembly and potential target for therapy. PLoS ONE 8 e77133 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Hunter, MC et al. (2014) Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells. PLoS ONE 9 e86842 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Luo, W et al. (2007) Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies. Proc. Natl. Acad. Sci. U.S.A. 104 9511-6 PubMed GONUTS page
↑ Arndt, V et al. (2005) BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. Mol. Biol. Cell 16 5891-900 PubMed GONUTS page
↑ ^5.0 ^5.1 Joo, JH et al. (2011) Hsp90-Cdc37 chaperone complex regulates Ulk1- and Atg13-mediated mitophagy. Mol. Cell 43 572-85 PubMed GONUTS page
↑ Guo, T et al. (2017) Roles of tau protein in health and disease. Acta Neuropathol. 133 665-704 PubMed GONUTS page
↑ Cliff, MJ et al. (2005) Molecular recognition via coupled folding and binding in a TPR domain. J. Mol. Biol. 346 717-32 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 Weaver, AJ et al. (2000) Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone. J. Biol. Chem. 275 23045-52 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Weikl, T et al. (1999) An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function. J. Mol. Biol. 293 685-91 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 Holt, SE et al. (1999) Functional requirement of p23 and Hsp90 in telomerase complexes. Genes Dev. 13 817-26 PubMed GONUTS page
↑ Ogiso, H et al. (2004) Phosphorylation analysis of 90 kDa heat shock protein within the cytosolic arylhydrocarbon receptor complex. Biochemistry 43 15510-9 PubMed GONUTS page
↑ ^12.0 ^12.1 Nakamura, T et al. (2002) HSP90, HSP70, and GAPDH directly interact with the cytoplasmic domain of macrophage scavenger receptors. Biochem. Biophys. Res. Commun. 290 858-64 PubMed GONUTS page
↑ ^13.0 ^13.1 Hamamoto, R et al. (2014) SMYD2-dependent HSP90 methylation promotes cancer cell proliferation by regulating the chaperone complex formation. Cancer Lett. 351 126-33 PubMed GONUTS page
↑ Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page
↑ Cloutier, P et al. (2013) A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity. PLoS Genet. 9 e1003210 PubMed GONUTS page
↑ Haslbeck, V et al. (2015) The activity of protein phosphatase 5 towards native clients is modulated by the middle- and C-terminal domains of Hsp90. Sci Rep 5 17058 PubMed GONUTS page
↑ Ko, YG et al. (2000) Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesis. J. Cell Biol. 149 567-74 PubMed GONUTS page
↑ ^18.0 ^18.1 Shang, Y et al. (2014) Hsp70 and Hsp90 oppositely regulate TGF-β signaling through CHIP/Stub1. Biochem. Biophys. Res. Commun. 446 387-92 PubMed GONUTS page
↑ Gao, Y et al. (2013) Distinct roles of molecular chaperones HSP90α and HSP90β in the biogenesis of KCNQ4 channels. PLoS ONE 8 e57282 PubMed GONUTS page
↑ ^20.0 ^20.1 Cheng, MB et al. (2010) Stat1 mediates an auto-regulation of hsp90beta gene in heat shock response. Cell. Signal. 22 1206-13 PubMed GONUTS page
↑ ^21.0 ^21.1 ^21.2 Didelot, C et al. (2008) Interaction of heat-shock protein 90 beta isoform (HSP90 beta) with cellular inhibitor of apoptosis 1 (c-IAP1) is required for cell differentiation. Cell Death Differ. 15 859-66 PubMed GONUTS page
↑ Lee, JH & Chung, IK (2010) Curcumin inhibits nuclear localization of telomerase by dissociating the Hsp90 co-chaperone p23 from hTERT. Cancer Lett. 290 76-86 PubMed GONUTS page
↑ Nemoto, T et al. (1995) Mechanism of dimer formation of the 90-kDa heat-shock protein. Eur. J. Biochem. 233 1-8 PubMed GONUTS page
↑ ^24.0 ^24.1 Lee, H et al. (2006) Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradation. Mol. Cell. Biol. 26 5259-69 PubMed GONUTS page
↑ ^25.0 ^25.1 ^25.2 Suzuki, S & Kulkarni, AB (2010) Extracellular heat shock protein HSP90beta secreted by MG63 osteosarcoma cells inhibits activation of latent TGF-beta1. Biochem. Biophys. Res. Commun. 398 525-31 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ ^28.0 ^28.1 ^28.2 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ Zhao, X et al. (2011) Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes. Mol. Cell Proteomics 10 M110.000299 PubMed GONUTS page
↑ Yin, H et al. (2006) SGT, a Hsp90beta binding partner, is accumulated in the nucleus during cell apoptosis. Biochem. Biophys. Res. Commun. 343 1153-8 PubMed GONUTS page
↑ Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
↑ Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
↑ Fang, L et al. (2008) Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry. J. Proteome Res. 7 4914-25 PubMed GONUTS page
↑ Rebbe, NF et al. (1989) Nucleotide sequence and regulation of a human 90-kDa heat shock protein gene. J. Biol. Chem. 264 15006-11 PubMed GONUTS page
↑ Giessrigl, B et al. (2012) Hsp90 stabilizes Cdc25A and counteracts heat shock-mediated Cdc25A degradation and cell-cycle attenuation in pancreatic carcinoma cells. Hum. Mol. Genet. 21 4615-27 PubMed GONUTS page
↑ ^36.0 ^36.1 ^36.2 ^36.3 ^36.4 ^36.5 ^36.6 ^36.7 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^37.0 ^37.1 ^37.2 Shang, L & Tomasi, TB (2006) The heat shock protein 90-CDC37 chaperone complex is required for signaling by types I and II interferons. J. Biol. Chem. 281 1876-84 PubMed GONUTS page
↑ Watanabe, A et al. (2011) Raftlin is involved in the nucleocapture complex to induce poly(I:C)-mediated TLR3 activation. J. Biol. Chem. 286 10702-11 PubMed GONUTS page
↑ Taipale, M et al. (2012) Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition. Cell 150 987-1001 PubMed GONUTS page
↑ Karagöz, GE et al. (2011) N-terminal domain of human Hsp90 triggers binding to the cochaperone p23. Proc. Natl. Acad. Sci. U.S.A. 108 580-5 PubMed GONUTS page

[PMID:24098578-1] 1.0 ^1.1 ^1.2 Tsou, YL et al. (2013) Heat shock protein 90: role in enterovirus 71 entry and assembly and potential target for therapy. PLoS ONE 8 e77133 PubMed GONUTS page

[PMID:24466266-2] 2.0 ^2.1 ^2.2 Hunter, MC et al. (2014) Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells. PLoS ONE 9 e86842 PubMed GONUTS page

[PMID:17517623-3] 3.0 ^3.1 ^3.2 Luo, W et al. (2007) Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies. Proc. Natl. Acad. Sci. U.S.A. 104 9511-6 PubMed GONUTS page

[PMID:16207813-4] Arndt, V et al. (2005) BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. Mol. Biol. Cell 16 5891-900 PubMed GONUTS page

[PMID:21855797-5] 5.0 ^5.1 Joo, JH et al. (2011) Hsp90-Cdc37 chaperone complex regulates Ulk1- and Atg13-mediated mitophagy. Mol. Cell 43 572-85 PubMed GONUTS page

[PMID:28386764-6] Guo, T et al. (2017) Roles of tau protein in health and disease. Acta Neuropathol. 133 665-704 PubMed GONUTS page

[PMID:15713458-7] Cliff, MJ et al. (2005) Molecular recognition via coupled folding and binding in a TPR domain. J. Mol. Biol. 346 717-32 PubMed GONUTS page

[PMID:10811660-8] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 Weaver, AJ et al. (2000) Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone. J. Biol. Chem. 275 23045-52 PubMed GONUTS page

[PMID:10543959-9] 9.0 ^9.1 ^9.2 Weikl, T et al. (1999) An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function. J. Mol. Biol. 293 685-91 PubMed GONUTS page

[PMID:10197982-10] 10.0 ^10.1 ^10.2 ^10.3 Holt, SE et al. (1999) Functional requirement of p23 and Hsp90 in telomerase complexes. Genes Dev. 13 817-26 PubMed GONUTS page

[PMID:15581363-11] Ogiso, H et al. (2004) Phosphorylation analysis of 90 kDa heat shock protein within the cytosolic arylhydrocarbon receptor complex. Biochemistry 43 15510-9 PubMed GONUTS page

[PMID:11785981-12] 12.0 ^12.1 Nakamura, T et al. (2002) HSP90, HSP70, and GAPDH directly interact with the cytoplasmic domain of macrophage scavenger receptors. Biochem. Biophys. Res. Commun. 290 858-64 PubMed GONUTS page

[PMID:24880080-13] 13.0 ^13.1 Hamamoto, R et al. (2014) SMYD2-dependent HSP90 methylation promotes cancer cell proliferation by regulating the chaperone complex formation. Cancer Lett. 351 126-33 PubMed GONUTS page

[PMID:25468996-14] Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page

[PMID:23349634-15] Cloutier, P et al. (2013) A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity. PLoS Genet. 9 e1003210 PubMed GONUTS page

[PMID:26593036-16] Haslbeck, V et al. (2015) The activity of protein phosphatase 5 towards native clients is modulated by the middle- and C-terminal domains of Hsp90. Sci Rep 5 17058 PubMed GONUTS page

[PMID:10791971-17] Ko, YG et al. (2000) Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesis. J. Cell Biol. 149 567-74 PubMed GONUTS page

[PMID:24613385-18] 18.0 ^18.1 Shang, Y et al. (2014) Hsp70 and Hsp90 oppositely regulate TGF-β signaling through CHIP/Stub1. Biochem. Biophys. Res. Commun. 446 387-92 PubMed GONUTS page

[PMID:23431407-19] Gao, Y et al. (2013) Distinct roles of molecular chaperones HSP90α and HSP90β in the biogenesis of KCNQ4 channels. PLoS ONE 8 e57282 PubMed GONUTS page

[PMID:20353823-20] 20.0 ^20.1 Cheng, MB et al. (2010) Stat1 mediates an auto-regulation of hsp90beta gene in heat shock response. Cell. Signal. 22 1206-13 PubMed GONUTS page

[PMID:18239673-21] 21.0 ^21.1 ^21.2 Didelot, C et al. (2008) Interaction of heat-shock protein 90 beta isoform (HSP90 beta) with cellular inhibitor of apoptosis 1 (c-IAP1) is required for cell differentiation. Cell Death Differ. 15 859-66 PubMed GONUTS page

[PMID:19751963-22] Lee, JH & Chung, IK (2010) Curcumin inhibits nuclear localization of telomerase by dissociating the Hsp90 co-chaperone p23 from hTERT. Cancer Lett. 290 76-86 PubMed GONUTS page

[PMID:7588731-23] Nemoto, T et al. (1995) Mechanism of dimer formation of the 90-kDa heat-shock protein. Eur. J. Biochem. 233 1-8 PubMed GONUTS page

[PMID:16809764-24] 24.0 ^24.1 Lee, H et al. (2006) Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradation. Mol. Cell. Biol. 26 5259-69 PubMed GONUTS page

[PMID:20599762-25] 25.0 ^25.1 ^25.2 Suzuki, S & Kulkarni, AB (2010) Extracellular heat shock protein HSP90beta secreted by MG63 osteosarcoma cells inhibits activation of latent TGF-beta1. Biochem. Biophys. Res. Commun. 398 525-31 PubMed GONUTS page

[PMID:23533145-26] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19946888-27] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:20458337-28] 28.0 ^28.1 ^28.2 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:20833797-29] Zhao, X et al. (2011) Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes. Mol. Cell Proteomics 10 M110.000299 PubMed GONUTS page

[PMID:16580629-30] Yin, H et al. (2006) SGT, a Hsp90beta binding partner, is accumulated in the nucleus during cell apoptosis. Biochem. Biophys. Res. Commun. 343 1153-8 PubMed GONUTS page

[PMID:22681889-31] Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page

[PMID:22658674-32] Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page

[PMID:18850735-33] Fang, L et al. (2008) Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry. J. Proteome Res. 7 4914-25 PubMed GONUTS page

[PMID:2768249-34] Rebbe, NF et al. (1989) Nucleotide sequence and regulation of a human 90-kDa heat shock protein gene. J. Biol. Chem. 264 15006-11 PubMed GONUTS page

[PMID:22843495-35] Giessrigl, B et al. (2012) Hsp90 stabilizes Cdc25A and counteracts heat shock-mediated Cdc25A degradation and cell-cycle attenuation in pancreatic carcinoma cells. Hum. Mol. Genet. 21 4615-27 PubMed GONUTS page

[PMID:21873635-36] 36.0 ^36.1 ^36.2 ^36.3 ^36.4 ^36.5 ^36.6 ^36.7 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:16280321-37] 37.0 ^37.1 ^37.2 Shang, L & Tomasi, TB (2006) The heat shock protein 90-CDC37 chaperone complex is required for signaling by types I and II interferons. J. Biol. Chem. 281 1876-84 PubMed GONUTS page

[PMID:21266579-38] Watanabe, A et al. (2011) Raftlin is involved in the nucleocapture complex to induce poly(I:C)-mediated TLR3 activation. J. Biol. Chem. 286 10702-11 PubMed GONUTS page

[PMID:22939624-39] Taipale, M et al. (2012) Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition. Cell 150 987-1001 PubMed GONUTS page

[PMID:21183720-40] Karagöz, GE et al. (2011) N-terminal domain of human Hsp90 triggers binding to the cochaperone p23. Proc. Natl. Acad. Sci. U.S.A. 108 580-5 PubMed GONUTS page

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HUMAN:HS90B

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