HUMAN:CH60

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	HSPD1 (synonyms: HSP60)
Protein Name(s)	60 kDa heat shock protein, mitochondrial 60 kDa chaperonin Chaperonin 60 CPN60 Heat shock protein 60 HSP-60 Hsp60 HuCHA60 Mitochondrial matrix protein P1 P60 lymphocyte protein
External Links
UniProt	P10809
EMBL	M22382 M34664 AJ250915 DQ217936 AK301276 AK312240 AC010746 AC020550 AC114809 BC002676 BC003030 BC067082 BC073746
CCDS	CCDS33357.1
PIR	A32800
RefSeq	NP_002147.2 NP_955472.1 XP_005246575.1
UniGene	Hs.595053 Hs.727543
PDB	4PJ1
PDBsum	4PJ1
ProteinModelPortal	P10809
SMR	P10809
BioGrid	109561
DIP	DIP-58N
IntAct	P10809
MINT	MINT-1162735
STRING	9606.ENSP00000340019
ChEMBL	CHEMBL4721
PhosphoSite	P10809
BioMuta	HSPD1
DMDM	129379
DOSAC-COBS-2DPAGE	P10809
OGP	P10809
REPRODUCTION-2DPAGE	IPI00784154 P10809
SWISS-2DPAGE	P10809
UCD-2DPAGE	P10809
MaxQB	P10809
PaxDb	P10809
PRIDE	P10809
DNASU	3329
Ensembl	ENST00000345042 ENST00000388968
GeneID	3329
KEGG	hsa:3329
UCSC	uc002uui.3
CTD	3329
GeneCards	GC02M198315
HGNC	HGNC:5261
HPA	CAB002775 HPA001523 HPA050025
MIM	118190 605280 612233
neXtProt	NX_P10809
Orphanet	100994 280288
PharmGKB	PA29527
eggNOG	COG0459
GeneTree	ENSGT00390000005727
HOGENOM	HOG000076290
HOVERGEN	HBG001982
InParanoid	P10809
KO	K04077
OMA	CELDNPL
OrthoDB	EOG7HTHGJ
PhylomeDB	P10809
TreeFam	TF300475
Reactome	REACT_118595
ChiTaRS	HSPD1
GeneWiki	GroEL
GenomeRNAi	3329
NextBio	13188
PRO	PR:P10809
Proteomes	UP000005640
Bgee	P10809
CleanEx	HS_HSPD1
ExpressionAtlas	P10809
Genevisible	P10809
GO	GO:0009986 GO:0005905 GO:0030135 GO:0005737 GO:0005829 GO:0005769 GO:0070062 GO:0005615 GO:0005794 GO:0046696 GO:0016020 GO:0045121 GO:0030061 GO:0005743 GO:0005759 GO:0005739 GO:0043209 GO:0005886 GO:0043234 GO:0005791 GO:0030141 GO:0042588 GO:0005524 GO:0016887 GO:0051087 GO:0003688 GO:0003725 GO:0001530 GO:0002039 GO:0044822 GO:0003697 GO:0031625 GO:0051082 GO:0006458 GO:0006919 GO:0042113 GO:0002368 GO:0042100 GO:0051085 GO:0051131 GO:0002236 GO:0048291 GO:0002755 GO:0043066 GO:0043524 GO:0043065 GO:0050729 GO:0032727 GO:0032729 GO:0032733 GO:0032735 GO:0032755 GO:0043032 GO:0050870 GO:0002842 GO:0051604 GO:0042026 GO:0050821 GO:0033198 GO:0042220 GO:0042493 GO:0043627 GO:0009408 GO:0042542 GO:0001666 GO:0032496 GO:0006986 GO:0042110 GO:0016032
Gene3D	1.10.560.10 3.50.7.10
HAMAP	MF_00600
InterPro	IPR018370 IPR001844 IPR002423 IPR027409 IPR027413
PANTHER	PTHR11353
Pfam	PF00118
PRINTS	PR00298
SUPFAM	SSF52029
TIGRFAMs	TIGR02348
PROSITE	PS00296

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0006457	protein folding	PMID:2528694^[1]	ECO:0000314			P		As seen in figure 4a, addition of ATP is required for proper release and folding into protease resistant conformation of protein from hsp60	complete CACAO 8868
	GO:0046789	host cell surface receptor binding	PMID:12496435^[2]	ECO:0000314			F		2D gel electrophoresis, flow cytometric analysis and other methods were used and analyzed to determine and identify the ligand(s) on the surface of Hc yeasts that binds to human macrophage CD11/CD18.	complete CACAO 9339
enables	GO:0019899	enzyme binding	PMID:20507888^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q6Q3I2	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:20507888^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q6Q3I0	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:20507888^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q6Q3H8	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:20507888^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q6Q3I1	F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:23349634^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	PMID:19393246^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	PMID:24746669^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
NOT\|involved_in	GO:0044406	adhesion of symbiont to host	PMID:20633027^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051702	interaction with symbiont	PMID:20507888^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:Q6Q3I2)	Seeded From UniProt	complete
enables	GO:0034185	apolipoprotein binding	PMID:11027668^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02652	F		Seeded From UniProt	complete
enables	GO:0008035	high-density lipoprotein particle binding	PMID:11027668^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0034186	apolipoprotein A-I binding	PMID:11027668^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02647	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:11027668^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000066)	Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:19725078^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60260	F		Seeded From UniProt	complete
involved_in	GO:0009409	response to cold	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5ZL72	P		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:21753002^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60260	F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:21276792^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000351)	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[12]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[13]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[14]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
involved_in	GO:0051604	protein maturation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19882	P		Seeded From UniProt	complete
involved_in	GO:0051131	chaperone-mediated protein complex assembly	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19882	P		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19882	F		Seeded From UniProt	complete
involved_in	GO:0050870	positive regulation of T cell activation	PMID:17164250^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050870	positive regulation of T cell activation	PMID:16148103^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050870	positive regulation of T cell activation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P63038	P		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19882	P		Seeded From UniProt	complete
involved_in	GO:0048291	isotype switching to IgG isotypes	PMID:16148103^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0046696	lipopolysaccharide receptor complex	PMID:17164250^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:17823127^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:17823127^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043032	positive regulation of macrophage activation	PMID:17164250^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042113	B cell activation	PMID:16148103^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042100	B cell proliferation	PMID:16148103^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032755	positive regulation of interleukin-6 production	PMID:16148103^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032735	positive regulation of interleukin-12 production	PMID:17164250^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032733	positive regulation of interleukin-10 production	PMID:16148103^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032729	positive regulation of interferon-gamma production	PMID:17164250^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032729	positive regulation of interferon-gamma production	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P63038	P		Seeded From UniProt	complete
involved_in	GO:0032727	positive regulation of interferon-alpha production	PMID:17164250^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030141	secretory granule	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P63038	C		Seeded From UniProt	complete
part_of	GO:0030135	coated vesicle	PMID:11807771^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19882	F		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:10663613^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:11807771^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006986	response to unfolded protein	PMID:11050098^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	PMID:17823127^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006458	'de novo' protein folding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19882	P		Seeded From UniProt	complete
part_of	GO:0005905	clathrin-coated pit	PMID:11807771^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:17823127^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005769	early endosome	PMID:11807771^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P63038	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:17823127^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:18229457^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19882	F		Seeded From UniProt	complete
enables	GO:0003688	DNA replication origin binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19882	F		Seeded From UniProt	complete
involved_in	GO:0002842	positive regulation of T cell mediated immune response to tumor cell	PMID:10663613^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0002755	MyD88-dependent toll-like receptor signaling pathway	PMID:16148103^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0002368	B cell cytokine production	PMID:16148103^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0001530	lipopolysaccharide binding	PMID:17164250^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:21245038^[22]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:10205158^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P61604	F		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:11050098^[20]	ECO:0000305	curator inference used in manual assertion	GO:0042026	F		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:18086682^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		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
part_of	GO:0032991	protein-containing complex	PMID:21328542^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:18086682^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042026	protein refolding	PMID:11050098^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:9243807^[27]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18086682^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:18086682^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21328542^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0002039	p53 binding	PMID:18086682^[24]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04637	F		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10599 PANTHER:PTN000143677 SGD:S000004249	F		Seeded From UniProt	complete
involved_in	GO:0045041	protein import into mitochondrial intermembrane space	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000143508 SGD:S000004249	P		Seeded From UniProt	complete
involved_in	GO:0042110	T cell activation	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96242 PANTHER:PTN000143515 UniProtKB:P10809	P		Seeded From UniProt	complete
involved_in	GO:0008637	apoptotic mitochondrial changes	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000143510 RGD:621314	P		Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015245 PANTHER:PTN000888029 WB:WBGene00002025	P		Seeded From UniProt	complete
involved_in	GO:0006458	'de novo' protein folding	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000143677 SGD:S000004249	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000143507 RGD:621314 TAIR:locus:2076081 TAIR:locus:2161048 UniProtKB:P10809	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015245 MGI:MGI:96242 PANTHER:PTN000888029 RGD:621314 SGD:S000004249 TAIR:locus:2057841 TAIR:locus:2076081 TAIR:locus:2087959 TAIR:locus:2092825 TAIR:locus:2161048 UniProtKB:P10809 UniProtKB:Q8IJN9 UniProtKB:Q8L7B5 WB:WBGene00002025 dictyBase:DDB_G0288181	C		Seeded From UniProt	complete
involved_in	GO:0042110	T cell activation	PMID:18256040^[29]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042110	T cell activation	PMID:17164250^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042110	T cell activation	PMID:15371451^[30]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032729	positive regulation of interferon-gamma production	PMID:17164250^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003725	double-stranded RNA binding	PMID:21266579^[31]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		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:IPR002423 InterPro:IPR018370	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001844 InterPro:IPR018370	C		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:IPR018370	P		Seeded From UniProt	complete
involved_in	GO:0042026	protein refolding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001844	P		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	PMID:17823127^[17] Reactome:R-HSA-8869558	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006357	regulation of transcription by RNA polymerase II	Reactome:R-HSA-8864260	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		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
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		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:0005739	mitochondrion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496	C		Seeded From UniProt	complete
enables	GO:0016853	isomerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0413	F		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0170	C		Seeded From UniProt	complete
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Notes

References

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

↑ Ostermann, J et al. (1989) Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature 341 125-30 PubMed GONUTS page
↑ Long, KH et al. (2003) Identification of heat shock protein 60 as the ligand on Histoplasma capsulatum that mediates binding to CD18 receptors on human macrophages. J. Immunol. 170 487-94 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Jagadeesan, B et al. (2010) LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeria, promotes bacterial adhesion to enterocyte-like Caco-2 cells only in pathogenic species. Microbiology (Reading, Engl.) 156 2782-95 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
↑ Oswald, C et al. (2009) Knockdown of human COX17 affects assembly and supramolecular organization of cytochrome c oxidase. J. Mol. Biol. 389 470-9 PubMed GONUTS page
↑ Wang, Z et al. (2014) Cyclin B1/Cdk1 coordinates mitochondrial respiration for cell-cycle G2/M progression. Dev. Cell 29 217-32 PubMed GONUTS page
↑ Hickey, TB et al. (2010) Mycobacterium tuberculosis employs Cpn60.2 as an adhesin that binds CD43 on the macrophage surface. Cell. Microbiol. 12 1634-47 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Bocharov, AV et al. (2000) Heat shock protein 60 is a high-affinity high-density lipoprotein binding protein. Biochem. Biophys. Res. Commun. 277 228-35 PubMed GONUTS page
↑ Davison, EJ et al. (2009) Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function. Proteomics 9 4284-97 PubMed GONUTS page
↑ Van Humbeeck, C et al. (2011) Parkin interacts with Ambra1 to induce mitophagy. J. Neurosci. 31 10249-61 PubMed GONUTS page
↑ Atay, S et al. (2011) Morphologic and proteomic characterization of exosomes released by cultured extravillous trophoblast cells. Exp. Cell Res. 317 1192-202 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ 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
↑ ^15.0 ^15.1 ^15.2 ^15.3 ^15.4 ^15.5 ^15.6 ^15.7 ^15.8 Osterloh, A et al. (2007) Synergistic and differential modulation of immune responses by Hsp60 and lipopolysaccharide. J. Biol. Chem. 282 4669-80 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 ^16.4 ^16.5 ^16.6 ^16.7 Cohen-Sfady, M et al. (2005) Heat shock protein 60 activates B cells via the TLR4-MyD88 pathway. J. Immunol. 175 3594-602 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 ^17.4 ^17.5 Chandra, D et al. (2007) Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3. J. Biol. Chem. 282 31289-301 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 ^18.3 Lipsker, D et al. (2002) Heat shock proteins 70 and 60 share common receptors which are expressed on human monocyte-derived but not epidermal dendritic cells. Eur. J. Immunol. 32 322-32 PubMed GONUTS page
↑ ^19.0 ^19.1 Thomas, ML et al. (2000) gammadelta T cells lyse autologous and allogenic oesophageal tumours: involvement of heat-shock proteins in the tumour cell lysis. Cancer Immunol. Immunother. 48 653-9 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 Richardson, A et al. (2001) The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli. J. Biol. Chem. 276 4981-7 PubMed GONUTS page
↑ Shamaei-Tousi, A et al. (2007) Plasma heat shock protein 60 and cardiovascular disease risk: the role of psychosocial, genetic, and biological factors. Cell Stress Chaperones 12 384-92 PubMed GONUTS page
↑ Poulsen, JB et al. (2011) Human 2'-phosphodiesterase localizes to the mitochondrial matrix with a putative function in mitochondrial RNA turnover. Nucleic Acids Res. 39 3754-70 PubMed GONUTS page
↑ Samali, A et al. (1999) Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells. EMBO J. 18 2040-8 PubMed GONUTS page
↑ ^24.0 ^24.1 ^24.2 ^24.3 ^24.4 Ghosh, JC et al. (2008) Hsp60 regulation of tumor cell apoptosis. J. Biol. Chem. 283 5188-94 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 Sircoulomb, F et al. (2011) ZNF703 gene amplification at 8p12 specifies luminal B breast cancer. EMBO Mol Med 3 153-66 PubMed GONUTS page
↑ Soltys, BJ & Gupta, RS (1997) Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells. Cell Biol. Int. 21 315-20 PubMed GONUTS page
↑ ^28.0 ^28.1 ^28.2 ^28.3 ^28.4 ^28.5 ^28.6 ^28.7 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Osterloh, A et al. (2008) Hsp60-mediated T cell stimulation is independent of TLR4 and IL-12. Int. Immunol. 20 433-43 PubMed GONUTS page
↑ Osterloh, A et al. (2004) Lipopolysaccharide-free heat shock protein 60 activates T cells. J. Biol. Chem. 279 47906-11 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

[PMID:2528694-1] Ostermann, J et al. (1989) Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature 341 125-30 PubMed GONUTS page

[PMID:12496435-2] Long, KH et al. (2003) Identification of heat shock protein 60 as the ligand on Histoplasma capsulatum that mediates binding to CD18 receptors on human macrophages. J. Immunol. 170 487-94 PubMed GONUTS page

[PMID:20507888-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 Jagadeesan, B et al. (2010) LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeria, promotes bacterial adhesion to enterocyte-like Caco-2 cells only in pathogenic species. Microbiology (Reading, Engl.) 156 2782-95 PubMed GONUTS page

[PMID:23349634-4] 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:19393246-5] Oswald, C et al. (2009) Knockdown of human COX17 affects assembly and supramolecular organization of cytochrome c oxidase. J. Mol. Biol. 389 470-9 PubMed GONUTS page

[PMID:24746669-6] Wang, Z et al. (2014) Cyclin B1/Cdk1 coordinates mitochondrial respiration for cell-cycle G2/M progression. Dev. Cell 29 217-32 PubMed GONUTS page

[PMID:20633027-7] Hickey, TB et al. (2010) Mycobacterium tuberculosis employs Cpn60.2 as an adhesin that binds CD43 on the macrophage surface. Cell. Microbiol. 12 1634-47 PubMed GONUTS page

[PMID:11027668-8] 8.0 ^8.1 ^8.2 ^8.3 Bocharov, AV et al. (2000) Heat shock protein 60 is a high-affinity high-density lipoprotein binding protein. Biochem. Biophys. Res. Commun. 277 228-35 PubMed GONUTS page

[PMID:19725078-9] Davison, EJ et al. (2009) Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function. Proteomics 9 4284-97 PubMed GONUTS page

[PMID:21753002-10] Van Humbeeck, C et al. (2011) Parkin interacts with Ambra1 to induce mitophagy. J. Neurosci. 31 10249-61 PubMed GONUTS page

[PMID:21276792-11] Atay, S et al. (2011) Morphologic and proteomic characterization of exosomes released by cultured extravillous trophoblast cells. Exp. Cell Res. 317 1192-202 PubMed GONUTS page

[PMID:19946888-12] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:19056867-13] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:20458337-14] 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:17164250-15] 15.0 ^15.1 ^15.2 ^15.3 ^15.4 ^15.5 ^15.6 ^15.7 ^15.8 Osterloh, A et al. (2007) Synergistic and differential modulation of immune responses by Hsp60 and lipopolysaccharide. J. Biol. Chem. 282 4669-80 PubMed GONUTS page

[PMID:16148103-16] 16.0 ^16.1 ^16.2 ^16.3 ^16.4 ^16.5 ^16.6 ^16.7 Cohen-Sfady, M et al. (2005) Heat shock protein 60 activates B cells via the TLR4-MyD88 pathway. J. Immunol. 175 3594-602 PubMed GONUTS page

[PMID:17823127-17] 17.0 ^17.1 ^17.2 ^17.3 ^17.4 ^17.5 Chandra, D et al. (2007) Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3. J. Biol. Chem. 282 31289-301 PubMed GONUTS page

[PMID:11807771-18] 18.0 ^18.1 ^18.2 ^18.3 Lipsker, D et al. (2002) Heat shock proteins 70 and 60 share common receptors which are expressed on human monocyte-derived but not epidermal dendritic cells. Eur. J. Immunol. 32 322-32 PubMed GONUTS page

[PMID:10663613-19] 19.0 ^19.1 Thomas, ML et al. (2000) gammadelta T cells lyse autologous and allogenic oesophageal tumours: involvement of heat-shock proteins in the tumour cell lysis. Cancer Immunol. Immunother. 48 653-9 PubMed GONUTS page

[PMID:11050098-20] 20.0 ^20.1 ^20.2 Richardson, A et al. (2001) The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli. J. Biol. Chem. 276 4981-7 PubMed GONUTS page

[PMID:18229457-21] Shamaei-Tousi, A et al. (2007) Plasma heat shock protein 60 and cardiovascular disease risk: the role of psychosocial, genetic, and biological factors. Cell Stress Chaperones 12 384-92 PubMed GONUTS page

[PMID:21245038-22] Poulsen, JB et al. (2011) Human 2'-phosphodiesterase localizes to the mitochondrial matrix with a putative function in mitochondrial RNA turnover. Nucleic Acids Res. 39 3754-70 PubMed GONUTS page

[PMID:10205158-23] Samali, A et al. (1999) Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells. EMBO J. 18 2040-8 PubMed GONUTS page

[PMID:18086682-24] 24.0 ^24.1 ^24.2 ^24.3 ^24.4 Ghosh, JC et al. (2008) Hsp60 regulation of tumor cell apoptosis. J. Biol. Chem. 283 5188-94 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:21328542-26] 26.0 ^26.1 Sircoulomb, F et al. (2011) ZNF703 gene amplification at 8p12 specifies luminal B breast cancer. EMBO Mol Med 3 153-66 PubMed GONUTS page

[PMID:9243807-27] Soltys, BJ & Gupta, RS (1997) Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells. Cell Biol. Int. 21 315-20 PubMed GONUTS page

[PMID:21873635-28] 28.0 ^28.1 ^28.2 ^28.3 ^28.4 ^28.5 ^28.6 ^28.7 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:18256040-29] Osterloh, A et al. (2008) Hsp60-mediated T cell stimulation is independent of TLR4 and IL-12. Int. Immunol. 20 433-43 PubMed GONUTS page

[PMID:15371451-30] Osterloh, A et al. (2004) Lipopolysaccharide-free heat shock protein 60 activates T cells. J. Biol. Chem. 279 47906-11 PubMed GONUTS page

[PMID:21266579-31] 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

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HUMAN:CH60

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