HUMAN:HS90A

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	HSP90AA1 (synonyms: HSP90A, HSPC1, HSPCA)
Protein Name(s)	Heat shock protein HSP 90-alpha Heat shock 86 kDa HSP 86 HSP86 Lipopolysaccharide-associated protein 2 LAP-2 LPS-associated protein 2 Renal carcinoma antigen NY-REN-38
External Links
UniProt	P07900
EMBL	X15183 M27024 AJ890082 AJ890083 DQ314871 AK056446 AK291115 AK291607 AL133223 CH471061 X07270 M30626 BC000987 BC121062 D87666 D87666
CCDS	CCDS32160.1 CCDS9967.1
PIR	A32319
RefSeq	NP_001017963.2 NP_005339.3
UniGene	Hs.525600
PDB	1BYQ 1OSF 1UY6 1UY7 1UY8 1UY9 1UYC 1UYD 1UYE 1UYF 1UYG 1UYH 1UYI 1UYK 1UYL 1YC1 1YC3 1YC4 1YER 1YES 1YET 2BSM 2BT0 2BUG 2BYH 2BYI 2BZ5 2C2L 2CCS 2CCT 2CCU 2CDD 2FWY 2FWZ 2H55 2JJC 2K5B 2QF6 2QFO 2QG0 2QG2 2UWD 2VCI 2VCJ 2WI1 2WI2 2WI3 2WI4 2WI5 2WI6 2WI7 2XAB 2XDK 2XDL 2XDS 2XDU 2XDX 2XHR 2XHT 2XHX 2XJG 2XJJ 2XJX 2XK2 2YE2 2YE3 2YE4 2YE5 2YE6 2YE7 2YE8 2YE9 2YEA 2YEB 2YEC 2YED 2YEE 2YEF 2YEG 2YEH 2YEI 2YEJ 2YI0 2YI5 2YI6 2YI7 2YJW 2YJX 2YK2 2YK9 2YKB 2YKC 2YKE 2YKI 2YKJ 3B24 3B25 3B26 3B27 3B28 3BM9 3BMY 3D0B 3EKO 3EKR 3FT5 3FT8 3HEK 3HHU 3HYY 3HYZ 3HZ1 3HZ5 3INW 3INX 3K97 3K98 3K99 3MNR 3O0I 3OW6 3OWB 3OWD 3Q6M 3Q6N 3QDD 3QTF 3R4M 3R4N 3R4O 3R4P 3R91 3R92 3RKZ 3RLP 3RLQ 3RLR 3T0H 3T0Z 3T10 3T1K 3T2S 3TUH 3VHA 3VHC 3VHD 3WHA 4AIF 4AWO 4AWP 4AWQ 4B7P 4BQJ 4CGU 4CGV 4CGW 4CWF 4CWN 4CWO 4CWP 4CWQ 4CWR 4CWS 4CWT 4EEH 4EFT 4EFU 4EGH 4EGI 4EGK 4FCP 4FCQ 4FCR 4HY6 4JQL 4L8Z 4L90 4L91 4L93 4L94 4LWE 4LWF 4LWG 4LWH 4LWI 4NH7 4NH8 4O05 4O07 4O09 4O0B 4R3M
PDBsum	1BYQ 1OSF 1UY6 1UY7 1UY8 1UY9 1UYC 1UYD 1UYE 1UYF 1UYG 1UYH 1UYI 1UYK 1UYL 1YC1 1YC3 1YC4 1YER 1YES 1YET 2BSM 2BT0 2BUG 2BYH 2BYI 2BZ5 2C2L 2CCS 2CCT 2CCU 2CDD 2FWY 2FWZ 2H55 2JJC 2K5B 2QF6 2QFO 2QG0 2QG2 2UWD 2VCI 2VCJ 2WI1 2WI2 2WI3 2WI4 2WI5 2WI6 2WI7 2XAB 2XDK 2XDL 2XDS 2XDU 2XDX 2XHR 2XHT 2XHX 2XJG 2XJJ 2XJX 2XK2 2YE2 2YE3 2YE4 2YE5 2YE6 2YE7 2YE8 2YE9 2YEA 2YEB 2YEC 2YED 2YEE 2YEF 2YEG 2YEH 2YEI 2YEJ 2YI0 2YI5 2YI6 2YI7 2YJW 2YJX 2YK2 2YK9 2YKB 2YKC 2YKE 2YKI 2YKJ 3B24 3B25 3B26 3B27 3B28 3BM9 3BMY 3D0B 3EKO 3EKR 3FT5 3FT8 3HEK 3HHU 3HYY 3HYZ 3HZ1 3HZ5 3INW 3INX 3K97 3K98 3K99 3MNR 3O0I 3OW6 3OWB 3OWD 3Q6M 3Q6N 3QDD 3QTF 3R4M 3R4N 3R4O 3R4P 3R91 3R92 3RKZ 3RLP 3RLQ 3RLR 3T0H 3T0Z 3T10 3T1K 3T2S 3TUH 3VHA 3VHC 3VHD 3WHA 4AIF 4AWO 4AWP 4AWQ 4B7P 4BQJ 4CGU 4CGV 4CGW 4CWF 4CWN 4CWO 4CWP 4CWQ 4CWR 4CWS 4CWT 4EEH 4EFT 4EFU 4EGH 4EGI 4EGK 4FCP 4FCQ 4FCR 4HY6 4JQL 4L8Z 4L90 4L91 4L93 4L94 4LWE 4LWF 4LWG 4LWH 4LWI 4NH7 4NH8 4O05 4O07 4O09 4O0B 4R3M
ProteinModelPortal	P07900
SMR	P07900
BioGrid	109552
DIP	DIP-27595N
IntAct	P07900
MINT	MINT-132070
STRING	9606.ENSP00000335153
BindingDB	P07900
ChEMBL	CHEMBL2095165
DrugBank	DB00716 DB00615
PhosphoSite	P07900
DMDM	92090606
OGP	P07900
REPRODUCTION-2DPAGE	IPI00784295
MaxQB	P07900
PRIDE	P07900
Ensembl	ENST00000216281 ENST00000334701
GeneID	3320
KEGG	hsa:3320
UCSC	uc001yku.4 uc001ykv.4
CTD	3320
GeneCards	GC14M102547
HGNC	HGNC:5253
HPA	CAB002058 HPA047290
MIM	140571
neXtProt	NX_P07900
PharmGKB	PA29519
GeneTree	ENSGT00760000119253
HOVERGEN	HBG007374
InParanoid	P07900
KO	K04079
OMA	AIYYITA
OrthoDB	EOG780RM0
PhylomeDB	P07900
TreeFam	TF300686
Reactome	REACT_111176 REACT_115755 REACT_115852 REACT_12477 REACT_15296 REACT_15364 REACT_15451 REACT_160086 REACT_160315 REACT_163813 REACT_19236 REACT_200624 REACT_200744 REACT_200775 REACT_228016 REACT_228063 REACT_228166 REACT_9434
ChiTaRS	HSP90AA1
EvolutionaryTrace	P07900
GenomeRNAi	3320
NextBio	13162
PMAP-CutDB	P07900
PRO	PR:P07900
Proteomes	UP000005640
Bgee	P07900
CleanEx	HS_HSP90AA1
ExpressionAtlas	P07900
Genevestigator	P07900
GO	GO:0005737 GO:0005829 GO:0071682 GO:0005576 GO:0070062 GO:0042470 GO:0016020 GO:0005739 GO:0005634 GO:0005886 GO:0005524 GO:0016887 GO:0042802 GO:0023026 GO:0030235 GO:0000166 GO:0044822 GO:0042803 GO:0030911 GO:0006200 GO:0007411 GO:0051131 GO:0038096 GO:0000086 GO:0045087 GO:0006839 GO:0000278 GO:0046209 GO:0045429 GO:0045040 GO:0042026 GO:0050999 GO:0006986 GO:0007165 GO:0044281
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
involved_in	GO:0032273	positive regulation of protein polymerization	PMID:19363271^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P10636)	Seeded From UniProt	complete
involved_in	GO:0001934	positive regulation of protein phosphorylation	PMID:19363271^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P10636)	Seeded From UniProt	complete
involved_in	GO:1902949	positive regulation of tau-protein kinase activity	PMID:19363271^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P49841)	Seeded From UniProt	complete
enables	GO:0048156	tau protein binding	PMID:19363271^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P19332	F	occurs_in:(UBERON:0000955)	Seeded From UniProt	complete
involved_in	GO:1903364	positive regulation of cellular protein catabolic process	PMID:18292230^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q9UNE7	P	has_regulation_target:(UniProtKB:P31749)	Seeded From UniProt	complete
enables	GO:0097110	scaffold protein binding	PMID:10409742^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q61097	F		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:P07901	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:P07901	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:P07901	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:P07901	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:P07901	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:P07901	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:P07901	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:P07901	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:P07901	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:P07901	P	occurs_in:(CL:0002608)	Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:29127155^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:29127155^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:29127155^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	PMID:15713458^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P53041	F		Seeded From UniProt	complete
involved_in	GO:0007004	telomere maintenance via telomerase	PMID:10197982^[7]	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^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:23349634^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:10791971^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:1990782	protein tyrosine kinase binding	PMID:20353823^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60674	F		Seeded From UniProt	complete
enables	GO:0070182	DNA polymerase binding	PMID:19751963^[11]	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^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0070182	DNA polymerase binding	PMID:10197982^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O14746	F		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:27353360^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:27353360^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:27353360^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0031396	regulation of protein ubiquitination	PMID:16809764^[13]	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^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9BY41	F		Seeded From UniProt	complete
involved_in	GO:0043254	regulation of protein complex assembly	PMID:20176123^[14]	ECO:0000303	author statement without traceable support used in manual assertion		P	occurs_in:(GO:0043202) part_of:(GO:0061684)	Seeded From UniProt	complete
involved_in	GO:0043335	protein unfolding	PMID:20176123^[14]	ECO:0000303	author statement without traceable support used in manual assertion		P	occurs_at:(GO:0005765) part_of:(GO:0061684)	Seeded From UniProt	complete
involved_in	GO:0009409	response to cold	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11501	P		Seeded From UniProt	complete
involved_in	GO:0046677	response to antibiotic	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11501	P		Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11501	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11501	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11501	C		Seeded From UniProt	complete
enables	GO:0051020	GTPase binding	PMID:24337748^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P32455	F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[16]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[17]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[18]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001831)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:11487543^[19]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	produced_by:(CL:0002563)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:12519789^[20]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	produced_by:(CL:0000236)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[21]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[21]	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^[21]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21630459^[22]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000019)	Seeded From UniProt	complete
involved_in	GO:0051131	chaperone-mediated protein complex assembly	PMID:15644312^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045040	protein insertion into mitochondrial outer membrane	PMID:15644312^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		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^[24]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[25]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0030911	TPR domain binding	PMID:9660753^[26]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0030235	nitric-oxide synthase regulator activity	PMID:15937123^[27]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:15937123^[27]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0007165	signal transduction	PMID:11470816^[28]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006986	response to unfolded protein	PMID:2527334^[29]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:12526792^[30]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	PMID:21873635^[31]	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^[31]	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
involved_in	GO:0050821	protein stabilization	PMID:21873635^[31]	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^[31]	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^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002609464 RGD:631409	C		Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	PMID:21873635^[31]	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
involved_in	GO:0034605	cellular response to heat	PMID:21873635^[31]	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^[31]	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
part_of	GO:0009986	cell surface	PMID:21873635^[31]	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^[31]	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
involved_in	GO:0006457	protein folding	PMID:21873635^[31]	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:0005886	plasma membrane	PMID:21873635^[31]	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^[31]	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^[31]	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^[31]	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^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000163632 RGD:631409 UniProtKB:P07900	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:8289821^[32]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07900	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25036637^[33]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07900	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21460846^[34]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07900	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21360678^[35]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07900	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16169070^[36]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07900	F		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:P07901 ensembl:ENSMUSP00000091921	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:P07901 ensembl:ENSMUSP00000091921	P		Seeded From UniProt	complete
involved_in	GO:0048675	axon extension	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07901 ensembl:ENSMUSP00000091921	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:P07901 ensembl:ENSMUSP00000091921	C		Seeded From UniProt	complete
involved_in	GO:0045429	positive regulation of nitric oxide biosynthetic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07901 ensembl:ENSMUSP00000091921	P		Seeded From UniProt	complete
part_of	GO:0044295	axonal growth cone	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07901 ensembl:ENSMUSP00000091921	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:P07901 ensembl:ENSMUSP00000091921	C		Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07901 ensembl:ENSMUSP00000091921	C		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07901 ensembl:ENSMUSP00000091921	F		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:P07901 ensembl:ENSMUSP00000091921	P		Seeded From UniProt	complete
enables	GO:0030235	nitric-oxide synthase regulator activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07901 ensembl:ENSMUSP00000091921	F		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:P07901 ensembl:ENSMUSP00000091921	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:P07901 ensembl:ENSMUSP00000091921	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07901 ensembl:ENSMUSP00000091921	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07901 ensembl:ENSMUSP00000091921	C		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
involved_in	GO:0061684	chaperone-mediated autophagy	PMID:25719862^[37]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0043202	lysosomal lumen	PMID:25719862^[37]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:11470816^[28]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0042026	protein refolding	PMID:9660753^[26]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0030911	TPR domain binding	PMID:12526792^[30]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006839	mitochondrial transport	PMID:12526792^[30]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:11470816^[28]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	PMID:11470816^[28]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-419645 Reactome:R-HSA-419644 Reactome:R-HSA-380508 Reactome:R-HSA-380455 Reactome:R-HSA-380316 Reactome:R-HSA-380311 Reactome:R-HSA-380303 Reactome:R-HSA-380294 Reactome:R-HSA-380283 Reactome:R-HSA-380272 Reactome:R-HSA-3371586 Reactome:R-HSA-3371503 Reactome:R-HSA-3000319 Reactome:R-HSA-3000310 Reactome:R-HSA-2574845 Reactome:R-HSA-2574840 Reactome:R-HSA-202129 Reactome:R-HSA-202127 Reactome:R-HSA-202111 Reactome:R-HSA-1963589 Reactome:R-HSA-1918095 Reactome:R-HSA-1918092 Reactome:R-HSA-1497810 Reactome:R-HSA-1497796 Reactome:R-HSA-1497784 Reactome:R-HSA-1248655 Reactome:R-HSA-1248002 Reactome:R-HSA-1247999 Reactome:R-HSA-1247844 Reactome:R-HSA-1247842 Reactome:R-HSA-1247841 Reactome:R-HSA-1226016 Reactome:R-HSA-1226014 Reactome:R-HSA-1226012 Reactome:R-HSA-1225961 Reactome:R-HSA-1225960 Reactome:R-HSA-1225957 Reactome:R-HSA-1225956 Reactome:R-HSA-1225952 Reactome:R-HSA-1225951 Reactome:R-HSA-1225950 Reactome:R-HSA-1225949 Reactome:R-HSA-1225947 Reactome:R-HSA-1220614 Reactome:R-HSA-1220613 Reactome:R-HSA-1220612 Reactome:R-HSA-1220611 Reactome:R-HSA-1220610 Reactome:R-HSA-1218833 Reactome:R-HSA-1218824 Reactome:R-HSA-1169421 Reactome:R-HSA-8853419 Reactome:R-HSA-8853405 Reactome:R-HSA-8852362 Reactome:R-HSA-6790041 Reactome:R-HSA-5638137 Reactome:R-HSA-5638009 Reactome:R-HSA-5637808 Reactome:R-HSA-5637806 Reactome:R-HSA-5637801 Reactome:R-HSA-5637800 Reactome:R-HSA-5637798 Reactome:R-HSA-5637796 Reactome:R-HSA-5637795 Reactome:R-HSA-5637794 Reactome:R-HSA-5637792 Reactome:R-HSA-5637770 Reactome:R-HSA-5637766 Reactome:R-HSA-5637765 Reactome:R-HSA-5637764 Reactome:R-HSA-5626699 Reactome:R-HSA-5626681 Reactome:R-HSA-5626228 Reactome:R-HSA-5626227 Reactome:R-HSA-5626223 Reactome:R-HSA-5626220 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-5617816 Reactome:R-HSA-5324632 Reactome:R-HSA-5218851 Reactome:R-HSA-5218839 Reactome:R-HSA-5218838 Reactome:R-HSA-5218826 Reactome:R-HSA-5218822 Reactome:R-HSA-5218811 Reactome:R-HSA-5218809 Reactome:R-HSA-5218643	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-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 Reactome:R-HSA-2247514	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000086	G2/M transition of mitotic cell cycle	Reactome:R-HSA-69275	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		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:0097711	ciliary basal body-plasma membrane docking	Reactome:R-HSA-5620912	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0071682	endocytic vesicle lumen	Reactome:R-HSA-2247514	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0051186	cofactor metabolic process	Reactome:R-HSA-8978934	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050999	regulation of nitric-oxide synthase activity	Reactome:R-HSA-203615	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:0048010	vascular endothelial growth factor receptor signaling pathway	Reactome:R-HSA-194138	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:0038128	ERBB2 signaling pathway	Reactome:R-HSA-1227986	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		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:0019221	cytokine-mediated signaling pathway	Reactome:R-HSA-6785807	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010389	regulation of G2/M transition of mitotic cell cycle	Reactome:R-HSA-8854518	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006898	receptor-mediated endocytosis	Reactome:R-HSA-3000484	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-HSA-202144 Reactome:R-HSA-202137 Reactome:R-HSA-202129 Reactome:R-HSA-202111	ECO:0000304	author statement supported by traceable reference used in manual assertion		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
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: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
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: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: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: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 ^1.3 Tortosa, E et al. (2009) Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein. J. Alzheimers Dis. 17 319-25 PubMed GONUTS page
↑ Dickey, CA et al. (2008) Akt and CHIP coregulate tau degradation through coordinated interactions. Proc. Natl. Acad. Sci. U.S.A. 105 3622-7 PubMed GONUTS page
↑ Stewart, S et al. (1999) Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization. Mol. Cell. Biol. 19 5523-34 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 ^5.2 Woodford, MR et al. (2017) Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients. EMBO J. 36 3650-3665 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
↑ ^7.0 ^7.1 ^7.2 ^7.3 Holt, SE et al. (1999) Functional requirement of p23 and Hsp90 in telomerase complexes. Genes Dev. 13 817-26 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
↑ 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
↑ 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
↑ 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
↑ ^12.0 ^12.1 ^12.2 Woodford, MR et al. (2016) The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding. Nat Commun 7 12037 PubMed GONUTS page
↑ ^13.0 ^13.1 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
↑ ^14.0 ^14.1 Orenstein, SJ & Cuervo, AM (2010) Chaperone-mediated autophagy: molecular mechanisms and physiological relevance. Semin. Cell Dev. Biol. 21 719-26 PubMed GONUTS page
↑ Forster, F et al. (2014) Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton. J. Immunol. 192 771-81 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
↑ Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
↑ van Niel, G et al. (2001) Intestinal epithelial cells secrete exosome-like vesicles. Gastroenterology 121 337-49 PubMed GONUTS page
↑ Wubbolts, R et al. (2003) Proteomic and biochemical analyses of human B cell-derived exosomes. Potential implications for their function and multivesicular body formation. J. Biol. Chem. 278 10963-72 PubMed GONUTS page
↑ ^21.0 ^21.1 ^21.2 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
↑ de Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page
↑ ^23.0 ^23.1 Humphries, AD et al. (2005) Dissection of the mitochondrial import and assembly pathway for human Tom40. J. Biol. Chem. 280 11535-43 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
↑ ^26.0 ^26.1 Young, JC et al. (1998) Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90. J. Biol. Chem. 273 18007-10 PubMed GONUTS page
↑ ^27.0 ^27.1 Martínez-Ruiz, A et al. (2005) S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc. Natl. Acad. Sci. U.S.A. 102 8525-30 PubMed GONUTS page
↑ ^28.0 ^28.1 ^28.2 ^28.3 Young, JC et al. (2001) Hsp90: a specialized but essential protein-folding tool. J. Cell Biol. 154 267-73 PubMed GONUTS page
↑ Hickey, E et al. (1989) Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein. Mol. Cell. Biol. 9 2615-26 PubMed GONUTS page
↑ ^30.0 ^30.1 ^30.2 Young, JC et al. (2003) Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112 41-50 PubMed GONUTS page
↑ ^31.00 ^31.01 ^31.02 ^31.03 ^31.04 ^31.05 ^31.06 ^31.07 ^31.08 ^31.09 ^31.10 ^31.11 ^31.12 ^31.13 ^31.14 ^31.15 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Minami, Y et al. (1994) The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. Mol. Cell. Biol. 14 1459-64 PubMed GONUTS page
↑ Taipale, M et al. (2014) A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. Cell 158 434-48 PubMed GONUTS page
↑ Park, SJ et al. (2011) The client protein p53 adopts a molten globule-like state in the presence of Hsp90. Nat. Struct. Mol. Biol. 18 537-41 PubMed GONUTS page
↑ Skarra, DV et al. (2011) Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5. Proteomics 11 1508-16 PubMed GONUTS page
↑ Stelzl, U et al. (2005) A human protein-protein interaction network: a resource for annotating the proteome. Cell 122 957-68 PubMed GONUTS page
↑ ^37.0 ^37.1 Macri, C et al. (2015) Modulation of deregulated chaperone-mediated autophagy by a phosphopeptide. Autophagy 11 472-86 PubMed GONUTS page

[PMID:19363271-1] 1.0 ^1.1 ^1.2 ^1.3 Tortosa, E et al. (2009) Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein. J. Alzheimers Dis. 17 319-25 PubMed GONUTS page

[PMID:18292230-2] Dickey, CA et al. (2008) Akt and CHIP coregulate tau degradation through coordinated interactions. Proc. Natl. Acad. Sci. U.S.A. 105 3622-7 PubMed GONUTS page

[PMID:10409742-3] Stewart, S et al. (1999) Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization. Mol. Cell. Biol. 19 5523-34 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:29127155-5] 5.0 ^5.1 ^5.2 Woodford, MR et al. (2017) Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients. EMBO J. 36 3650-3665 PubMed GONUTS page

[PMID:15713458-6] 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:10197982-7] 7.0 ^7.1 ^7.2 ^7.3 Holt, SE et al. (1999) Functional requirement of p23 and Hsp90 in telomerase complexes. Genes Dev. 13 817-26 PubMed GONUTS page

[PMID:23349634-8] 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:10791971-9] 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:20353823-10] 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:19751963-11] 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:27353360-12] 12.0 ^12.1 ^12.2 Woodford, MR et al. (2016) The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding. Nat Commun 7 12037 PubMed GONUTS page

[PMID:16809764-13] 13.0 ^13.1 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:20176123-14] 14.0 ^14.1 Orenstein, SJ & Cuervo, AM (2010) Chaperone-mediated autophagy: molecular mechanisms and physiological relevance. Semin. Cell Dev. Biol. 21 719-26 PubMed GONUTS page

[PMID:24337748-15] Forster, F et al. (2014) Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton. J. Immunol. 192 771-81 PubMed GONUTS page

[PMID:23533145-16] 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:19946888-17] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:19199708-18] Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page

[PMID:11487543-19] van Niel, G et al. (2001) Intestinal epithelial cells secrete exosome-like vesicles. Gastroenterology 121 337-49 PubMed GONUTS page

[PMID:12519789-20] Wubbolts, R et al. (2003) Proteomic and biochemical analyses of human B cell-derived exosomes. Potential implications for their function and multivesicular body formation. J. Biol. Chem. 278 10963-72 PubMed GONUTS page

[PMID:20458337-21] 21.0 ^21.1 ^21.2 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:21630459-22] Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page

[PMID:15644312-23] 23.0 ^23.1 Humphries, AD et al. (2005) Dissection of the mitochondrial import and assembly pathway for human Tom40. J. Biol. Chem. 280 11535-43 PubMed GONUTS page

[PMID:22681889-24] 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:22658674-25] 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:9660753-26] 26.0 ^26.1 Young, JC et al. (1998) Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90. J. Biol. Chem. 273 18007-10 PubMed GONUTS page

[PMID:15937123-27] 27.0 ^27.1 Martínez-Ruiz, A et al. (2005) S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc. Natl. Acad. Sci. U.S.A. 102 8525-30 PubMed GONUTS page

[PMID:11470816-28] 28.0 ^28.1 ^28.2 ^28.3 Young, JC et al. (2001) Hsp90: a specialized but essential protein-folding tool. J. Cell Biol. 154 267-73 PubMed GONUTS page

[PMID:2527334-29] Hickey, E et al. (1989) Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein. Mol. Cell. Biol. 9 2615-26 PubMed GONUTS page

[PMID:12526792-30] 30.0 ^30.1 ^30.2 Young, JC et al. (2003) Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112 41-50 PubMed GONUTS page

[PMID:21873635-31] 31.00 ^31.01 ^31.02 ^31.03 ^31.04 ^31.05 ^31.06 ^31.07 ^31.08 ^31.09 ^31.10 ^31.11 ^31.12 ^31.13 ^31.14 ^31.15 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:8289821-32] Minami, Y et al. (1994) The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. Mol. Cell. Biol. 14 1459-64 PubMed GONUTS page

[PMID:25036637-33] Taipale, M et al. (2014) A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. Cell 158 434-48 PubMed GONUTS page

[PMID:21460846-34] Park, SJ et al. (2011) The client protein p53 adopts a molten globule-like state in the presence of Hsp90. Nat. Struct. Mol. Biol. 18 537-41 PubMed GONUTS page

[PMID:21360678-35] Skarra, DV et al. (2011) Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5. Proteomics 11 1508-16 PubMed GONUTS page

[PMID:16169070-36] Stelzl, U et al. (2005) A human protein-protein interaction network: a resource for annotating the proteome. Cell 122 957-68 PubMed GONUTS page

[PMID:25719862-37] 37.0 ^37.1 Macri, C et al. (2015) Modulation of deregulated chaperone-mediated autophagy by a phosphopeptide. Autophagy 11 472-86 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

[17]

[18]

[19]

[20]

[21]

[22]

[23]

[24]

[25]

[26]

[27]

[28]

[29]

[30]

[31]

[32]

[33]

[34]

[35]

[36]

[37]

HUMAN:HS90A

Contents

Annotations

Notes

References

a

c

d

e

f

g

h

i

l

m

n

o

p

r

s

t

u

v

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools