HUMAN:HS71A

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	HSPA1A (synonyms: HSPA1, HSX70)
Protein Name(s)	Heat shock 70 kDa protein 1A (ECO:0000312 with HGNC:HGNC:5232) Heat shock 70 kDa protein 1 HSP70-1 (ECO:0000303 with PMID:14656967^[1], ECO:0000303 with PMID:2538825^[2]) HSP70.1
External Links
UniProt	P0DMV8
EMBL	M11717 M59828 BA000025 AF134726 AK304652 DQ451402 AL671762 BC002453 M24743 X04676 X04677
CCDS	CCDS34414.1
PIR	A29160 A45871 I59139 I79540
RefSeq	NP_005336.3 NP_005337.2
UniGene	Hs.274402 Hs.702139 Hs.719966 Hs.743411
PDB	1HJO 1S3X 1XQS 2E88 2E8A 2LMG 3A8Y 3ATU 3ATV 3AY9 3D2E 3D2F 3JXU 3LOF 4IO8 4J8F 4PO2 4WV5 4WV7
PDBsum	1HJO 1S3X 1XQS 2E88 2E8A 2LMG 3A8Y 3ATU 3ATV 3AY9 3D2E 3D2F 3JXU 3LOF 4IO8 4J8F 4PO2 4WV5 4WV7
ProteinModelPortal	P0DMV8
SMR	P0DMV8
IntAct	P0DMV8
MINT	MINT-96699
BindingDB	P0DMV8
ChEMBL	CHEMBL5460
SwissPalm	P0DMV8
DMDM	147744565
REPRODUCTION-2DPAGE	IPI00304925
DNASU	3303
Ensembl	ENST00000375651 ENST00000400040 ENST00000430065 ENST00000433487 ENST00000441618
GeneID	3303 3304
KEGG	hsa:3303 hsa:3304
CTD	3303 3304
H-InvDB	HIX0058169 HIX0058187 HIX0166160
HGNC	HGNC:5232
HPA	CAB008640 CAB017451 CAB032815 HPA052504
MIM	140550 603012
neXtProt	NX_P0DMV8
HOGENOM	HOG000228135
HOVERGEN	HBG051845
KO	K03283
OrthoDB	EOG7PCJGF
TreeFam	TF105042
Reactome	R-HSA-168330 R-HSA-3371453 R-HSA-3371568 R-HSA-3371571 R-HSA-450408
ChiTaRS	HSPA1A HSPA1B
GeneWiki	HSPA1A
NextBio	13103
PRO	PR:P0DMV8
Proteomes	UP000005640
CleanEx	HS_HSPA1A
ExpressionAtlas	P0DMV8
GO	GO:0072562 GO:0005814 GO:0005737 GO:0005829 GO:0005925 GO:0016234 GO:0005739 GO:0005654 GO:0048471 GO:0005524 GO:0016887 GO:0042623 GO:0055131 GO:0019899 GO:0001664 GO:0031072 GO:0042826 GO:0044183 GO:0005102 GO:0031625 GO:0051082 GO:0001618 GO:0046034 GO:0070370 GO:0034605 GO:0034599 GO:0010467 GO:0060548 GO:1902236 GO:2001240 GO:0090084 GO:1901029 GO:0031397 GO:1902380 GO:0010628 GO:0032757 GO:1904722 GO:0051092 GO:0070434 GO:1903265 GO:0042026 GO:0050821 GO:1900034 GO:0043488 GO:0031396
Gene3D	1.20.1270.10 2.60.34.10
InterPro	IPR018181 IPR029048 IPR029047 IPR013126
Pfam	PF00012
PRINTS	PR00301
SUPFAM	SSF100920 SSF100934
PROSITE	PS00297 PS00329 PS01036

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:0007041	lysosomal transport	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q61696	P		Seeded From UniProt	complete
involved_in	GO:0034620	cellular response to unfolded protein	PMID:20625543^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051131	chaperone-mediated protein complex assembly	PMID:10811660^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:11785981^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	PMID:11785981^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P21758	F		Seeded From UniProt	complete
enables	GO:0045296	cadherin binding	PMID:25468996^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0031249	denatured protein binding	PMID:21909508^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P42858	F		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
involved_in	GO:0030512	negative regulation of transforming growth factor beta receptor signaling pathway	PMID:24613385^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process	PMID:24613385^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:21909508^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031396	regulation of protein ubiquitination	PMID:16809764^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q9UPR3) part_of:(GO:0031647)	Seeded From UniProt	complete
enables	GO:0042826	histone deacetylase binding	PMID:16809764^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9BY41	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:24790089^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0042026	protein refolding	PMID:27708256^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090063	positive regulation of microtubule nucleation	PMID:27137183^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1901673	regulation of mitotic spindle assembly	PMID:27137183^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005813	centrosome	PMID:27137183^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:15603737^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60260	F		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:23921388^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P25685	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:23921388^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8WXB1	F		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:15603737^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016234	inclusion body	PMID:15603737^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0044183	protein folding chaperone	PMID:15603737^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:23921388^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:23921388^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:2001240	negative regulation of extrinsic apoptotic signaling pathway in absence of ligand	PMID:17167422^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090084	negative regulation of inclusion body assembly	PMID:15603737^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046034	ATP metabolic process	PMID:23921388^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042026	protein refolding	PMID:15603737^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:25281747^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q12809)	Seeded From UniProt	complete
enables	GO:0055131	C3HC4-type RING finger domain binding	PMID:25281747^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q6ZRF8	F		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:17182002^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8WXX5	F		Seeded From UniProt	complete
enables	GO:0005102	signaling receptor binding	PMID:24790089^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9HC29	F	occurs_in:(CL:0011108)	Seeded From UniProt	complete
involved_in	GO:0051092	positive regulation of NF-kappaB transcription factor activity	PMID:24790089^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion	UniProtKB:Q9HC29	P	happens_during:(GO:0032495) occurs_in:(CL:0011108)\|happens_during(GO:0071356)	Seeded From UniProt	complete
involved_in	GO:0070434	positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway	PMID:24790089^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion	UniProtKB:Q9HC29	P	causally_upstream_of:(GO:0051092) causally_upstream_of:(GO:0032757)	Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:24790089^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q9HC29)	Seeded From UniProt	complete
involved_in	GO:1903265	positive regulation of tumor necrosis factor-mediated signaling pathway	PMID:24790089^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion	UniProtKB:Q9HC29	P		Seeded From UniProt	complete
involved_in	GO:0033120	positive regulation of RNA splicing	PMID:20625543^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P17861)	Seeded From UniProt	complete
involved_in	GO:1902380	positive regulation of endoribonuclease activity	PMID:20625543^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O75460)	Seeded From UniProt	complete
involved_in	GO:1901029	negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway	PMID:20625543^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902236	negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway	PMID:20625543^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0001664	G protein-coupled receptor binding	PMID:12150907^[19]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:O15354)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[20]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:12150907^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60260	F		Seeded From UniProt	complete
part_of	GO:0031982	vesicle	PMID:19190083^[21]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002202)	Seeded From UniProt	complete
involved_in	GO:1902236	negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway	PMID:12150907^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:12150907^[19]	ECO:0000303	author statement without traceable support used in manual assertion		F	has_input:(UniProtKB:O15354)	Seeded From UniProt	complete
involved_in	GO:0031397	negative regulation of protein ubiquitination	PMID:12150907^[19]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O15354)	Seeded From UniProt	complete
colocalizes_with	GO:0000151	ubiquitin ligase complex	PMID:12150907^[19]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0000955)	Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:21423176^[22]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
involved_in	GO:0090084	negative regulation of inclusion body assembly	PMID:21231916^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0072562	blood microparticle	PMID:22516433^[24]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0070370	cellular heat acclimation	PMID:21231916^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[25]	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:20458337^[26]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[26]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
involved_in	GO:0060548	negative regulation of cell death	PMID:21231916^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0034605)	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:21231916^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042623	ATPase activity, coupled	PMID:21231916^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0042026	protein refolding	PMID:21231916^[23]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:P04637)	Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:24061851^[27]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:21231916^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8NHS0	F		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:21231916^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q7Z6W7	F		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:21231916^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O75190	F		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:21231916^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O75953	F		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:21231916^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9UDY4	F		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:21231916^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P25686	F		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:21231916^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P25685	F		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:21231916^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8WW22	F		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:21231916^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60884	F		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:21231916^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P31689	F		Seeded From UniProt	complete
NOT\|involved_in	GO:0010941	regulation of cell death	PMID:21231916^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21231916^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005814	centriole	PMID:24061851^[27]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:24061851^[27]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0032757	positive regulation of interleukin-8 production	PMID:24790089^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion	UniProtKB:Q9HC29	P	happens_during:(GO:0032495) occurs_in:(CL:0011108)\|causally_upstream_of(GO:0071356)	Seeded From UniProt	complete
enables	GO:0003714	transcription corepressor activity	PMID:9499401^[28]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0097201	negative regulation of transcription from RNA polymerase II promoter in response to stress	PMID:9499401^[28]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:10205060^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0047485	protein N-terminus binding	PMID:9553041^[30]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P19544	F		Seeded From UniProt	complete
involved_in	GO:0045648	positive regulation of erythrocyte differentiation	PMID:17167422^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P15976) occurs_in:(GO:0005634)	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
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:17167422^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0045648) has_regulation_target:(UniProtKB:P15976) occurs_in:(GO:0005634)	Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	PMID:17289661^[33]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030308	negative regulation of cell growth	PMID:9553041^[30]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016607	nuclear speck	PMID:9553041^[30]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000653)	Seeded From UniProt	complete
part_of	GO:0016235	aggresome	PMID:15885686^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0008285	negative regulation of cell population proliferation	PMID:9553041^[30]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0008180	COP9 signalosome	PMID:18850735^[35]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006986	response to unfolded protein	PMID:10859165^[36]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006402	mRNA catabolic process	PMID:10205060^[29]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9553041^[30]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:10859165^[36]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:17167422^[16]	ECO:0000314	direct assay evidence used in manual assertion		C	exists_during:(GO:0030218)	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:10205060^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1901673	regulation of mitotic spindle assembly	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000453125 UniProtKB:P0DMV8 UniProtKB:P0DMV9	P		Seeded From UniProt	complete
enables	GO:0051787	misfolded protein binding	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95835 PANTHER:PTN002321897 RGD:2843 UniProtKB:P11021	F		Seeded From UniProt	complete
involved_in	GO:0051085	chaperone cofactor-dependent protein refolding	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10241 MGI:MGI:105384 PANTHER:PTN002321897	P		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10241 MGI:MGI:105384 PANTHER:PTN002321897 RGD:2843 RGD:621725 SGD:S000000004 SGD:S000000171 SGD:S000000905 SGD:S000001106 SGD:S000001556 SGD:S000002388 SGD:S000003571 SGD:S000003947 SGD:S000005153 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P11142 UniProtKB:P17066 UniProtKB:P34931 UniProtKB:P54652	F		Seeded From UniProt	complete
enables	GO:0044183	protein folding chaperone	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10241 PANTHER:PTN002321897 UniProtKB:P0DMV8 UniProtKB:P0DMV9	F		Seeded From UniProt	complete
enables	GO:0042623	ATPase activity, coupled	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:105384 PANTHER:PTN002321897 RGD:621725 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P17066	F		Seeded From UniProt	complete
involved_in	GO:0042026	protein refolding	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002321897 SGD:S000000004 SGD:S000000756 SGD:S000003806 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P11142 UniProtKB:P17066 UniProtKB:P34931 UniProtKB:P54652	P		Seeded From UniProt	complete
involved_in	GO:0034620	cellular response to unfolded protein	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10241 PANTHER:PTN002321897 UniProtKB:P0DMV8	P		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000184706 PANTHER:PTN002321897 RGD:621725 SGD:S000000905 UniProtKB:A5I640 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P17066	P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000453103 RGD:2840 UniProtKB:P0DMV8 UniProtKB:P0DMV9	C		Seeded From UniProt	complete
involved_in	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000453125 UniProtKB:P0DMV8	P		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000453103 UniProtKB:P0DMV8 UniProtKB:P0DMV9	F		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002321897 RGD:1311806 UniProtKB:K7NTP5 UniProtKB:O73885 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P11142 UniProtKB:P17066 UniProtKB:P34931 UniProtKB:Q8IB24	F		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10241 EcoGene:EG12130 EcoGene:EG13653 PANTHER:PTN002321897 PomBase:SPAC664.11 RGD:621725 SGD:S000000004 SGD:S000000171 SGD:S000002388 SGD:S000003571 SGD:S000003806 SGD:S000005153 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P11021 UniProtKB:P11142 WB:WBGene00002005	F		Seeded From UniProt	complete
colocalizes_with	GO:0008180	COP9 signalosome	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000453103 UniProtKB:P0DMV8 UniProtKB:P17066 UniProtKB:P48741	C		Seeded From UniProt	complete
involved_in	GO:0006986	response to unfolded protein	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002321897 RGD:1593284 RGD:2840 SGD:S000001556 SGD:S000003571 UniProtKB:P0DMV8	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002321762 PomBase:SPBC1709.05 RGD:2840 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P17066 UniProtKB:P34931 UniProtKB:Q0VDF9	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10241 FB:FBgn0266599 MGI:MGI:105384 MGI:MGI:96244 PANTHER:PTN002321897 PomBase:SPCC1739.13 RGD:1311806 RGD:2843 RGD:621725 SGD:S000000004 SGD:S000000905 SGD:S000001106 SGD:S000002388 SGD:S000003947 UniProtKB:O73885 UniProtKB:P08106 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P17066 UniProtKB:P22953 UniProtKB:Q27975 UniProtKB:Q8IB24 WB:WBGene00002005	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000453103 RGD:2840 UniProtKB:P0DMV8 UniProtKB:P0DMV9	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:21873635^[37]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10241 EcoGene:EG12130 PANTHER:PTN002321897 RGD:621725 SGD:S000001556 SGD:S000003947 TAIR:locus:2101222 TAIR:locus:2121022 TAIR:locus:2135897 TAIR:locus:2144801 UniProtKB:P08106 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P11142 UniProtKB:Q7SX63	F		Seeded From UniProt	complete
involved_in	GO:0046718	viral entry into host cell	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0001618	P		Seeded From UniProt	complete
involved_in	GO:0034599	cellular response to oxidative stress	PMID:24252804^[38]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:24252804^[38]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_input:(UniProtKB:P37840)	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:16130169^[39]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:16130169^[39]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:16130169^[39]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:16130169^[39]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16130169^[39]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		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 Reactome:R-HSA-3371453	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043488	regulation of mRNA stability	Reactome:R-HSA-450408	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-3371422	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-5618110 Reactome:R-HSA-5618107 Reactome:R-HSA-5618105 Reactome:R-HSA-5618098 Reactome:R-HSA-5618085 Reactome:R-HSA-5252079 Reactome:R-HSA-5252041 Reactome:R-HSA-5251959 Reactome:R-HSA-5251942 Reactome:R-HSA-450580 Reactome:R-HSA-450551 Reactome:R-HSA-3371590 Reactome:R-HSA-3371503 Reactome:R-HSA-3371422	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-5252041 Reactome:R-HSA-5251955 Reactome:R-HSA-5082384 Reactome:R-HSA-5082369 Reactome:R-HSA-5082356 Reactome:R-HSA-3371554 Reactome:R-HSA-3371518 Reactome:R-HSA-3371467	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	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
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: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
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:0005856	cytoskeleton	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206	C		Seeded From UniProt	complete
enables	GO:0001618	virus receptor activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1183	F		Seeded From UniProt	complete
part_of	GO:0005815	microtubule organizing center	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0048	C		Seeded From UniProt	complete
edit table

Notes

References

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

↑ Xie, T et al. (2003) Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse. Genome Res. 13 2621-36 PubMed GONUTS page
↑ Sargent, CA et al. (1989) Human major histocompatibility complex contains genes for the major heat shock protein HSP70. Proc. Natl. Acad. Sci. U.S.A. 86 1968-72 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Gupta, S et al. (2010) HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1alpha-XBP1 signaling through a physical interaction. PLoS Biol. 8 e1000410 PubMed GONUTS page
↑ 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
↑ ^5.0 ^5.1 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
↑ Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page
↑ ^7.0 ^7.1 Chakrabortee, S et al. (2012) Intrinsically disordered proteins as molecular shields. Mol Biosyst 8 210-9 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
↑ ^9.0 ^9.1 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
↑ ^10.0 ^10.1 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
↑ ^11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 ^11.6 Mohanan, V & Grimes, CL (2014) The molecular chaperone HSP70 binds to and stabilizes NOD2, an important protein involved in Crohn disease. J. Biol. Chem. 289 18987-98 PubMed GONUTS page
↑ Seo, JH et al. (2016) ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation. Nat Commun 7 12882 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 Fang, CT et al. (2016) HSP70 regulates the function of mitotic centrosomes. Cell. Mol. Life Sci. 73 3949-60 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 Kalia, SK et al. (2004) BAG5 inhibits parkin and enhances dopaminergic neuron degeneration. Neuron 44 931-45 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 ^15.4 Jakobsson, ME et al. (2013) Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylation. J. Biol. Chem. 288 27752-63 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 Ribeil, JA et al. (2007) Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1. Nature 445 102-5 PubMed GONUTS page
↑ ^17.0 ^17.1 Roder, K et al. (2014) RING finger protein RNF207, a novel regulator of cardiac excitation. J. Biol. Chem. 289 33730-40 PubMed GONUTS page
↑ Han, C et al. (2007) HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain. Biochem. Biophys. Res. Commun. 353 280-5 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 ^19.3 ^19.4 ^19.5 Imai, Y et al. (2002) CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol. Cell 10 55-67 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
↑ Kesimer, M et al. (2009) Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J. 23 1858-68 PubMed GONUTS page
↑ Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page
↑ ^23.00 ^23.01 ^23.02 ^23.03 ^23.04 ^23.05 ^23.06 ^23.07 ^23.08 ^23.09 ^23.10 ^23.11 ^23.12 ^23.13 ^23.14 ^23.15 ^23.16 ^23.17 Hageman, J et al. (2011) The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities. Biochem. J. 435 127-42 PubMed GONUTS page
↑ Bastos-Amador, P et al. (2012) Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. J Proteomics 75 3574-84 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
↑ ^26.0 ^26.1 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
↑ ^27.0 ^27.1 ^27.2 Khalouei, S et al. (2014) Stress-induced localization of HSPA6 (HSP70B') and HSPA1A (HSP70-1) proteins to centrioles in human neuronal cells. Cell Stress Chaperones 19 321-7 PubMed GONUTS page
↑ ^28.0 ^28.1 Shi, Y et al. (1998) Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev. 12 654-66 PubMed GONUTS page
↑ ^29.0 ^29.1 ^29.2 Laroia, G et al. (1999) Control of mRNA decay by heat shock-ubiquitin-proteasome pathway. Science 284 499-502 PubMed GONUTS page
↑ ^30.0 ^30.1 ^30.2 ^30.3 ^30.4 Maheswaran, S et al. (1998) Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70. Genes Dev. 12 1108-20 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
↑ Jønson, L et al. (2007) Molecular composition of IMP1 ribonucleoprotein granules. Mol. Cell Proteomics 6 798-811 PubMed GONUTS page
↑ Kallijärvi, J et al. (2005) TRIM37 defective in mulibrey nanism is a novel RING finger ubiquitin E3 ligase. Exp. Cell Res. 308 146-55 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
↑ ^36.0 ^36.1 Cuesta, R et al. (2000) Chaperone hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes. Genes Dev. 14 1460-70 PubMed GONUTS page
↑ ^37.00 ^37.01 ^37.02 ^37.03 ^37.04 ^37.05 ^37.06 ^37.07 ^37.08 ^37.09 ^37.10 ^37.11 ^37.12 ^37.13 ^37.14 ^37.15 ^37.16 ^37.17 ^37.18 ^37.19 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^38.0 ^38.1 Dias, V et al. (2013) The role of oxidative stress in Parkinson's disease. J Parkinsons Dis 3 461-91 PubMed GONUTS page
↑ ^39.0 ^39.1 ^39.2 ^39.3 ^39.4 Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

[PMID:14656967-1] Xie, T et al. (2003) Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse. Genome Res. 13 2621-36 PubMed GONUTS page

[PMID:2538825-2] Sargent, CA et al. (1989) Human major histocompatibility complex contains genes for the major heat shock protein HSP70. Proc. Natl. Acad. Sci. U.S.A. 86 1968-72 PubMed GONUTS page

[PMID:20625543-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 Gupta, S et al. (2010) HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1alpha-XBP1 signaling through a physical interaction. PLoS Biol. 8 e1000410 PubMed GONUTS page

[PMID:10811660-4] 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:11785981-5] 5.0 ^5.1 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:25468996-6] Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page

[PMID:21909508-7] 7.0 ^7.1 Chakrabortee, S et al. (2012) Intrinsically disordered proteins as molecular shields. Mol Biosyst 8 210-9 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:24613385-9] 9.0 ^9.1 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:16809764-10] 10.0 ^10.1 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:24790089-11] 11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 ^11.6 Mohanan, V & Grimes, CL (2014) The molecular chaperone HSP70 binds to and stabilizes NOD2, an important protein involved in Crohn disease. J. Biol. Chem. 289 18987-98 PubMed GONUTS page

[PMID:27708256-12] Seo, JH et al. (2016) ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation. Nat Commun 7 12882 PubMed GONUTS page

[PMID:27137183-13] 13.0 ^13.1 ^13.2 Fang, CT et al. (2016) HSP70 regulates the function of mitotic centrosomes. Cell. Mol. Life Sci. 73 3949-60 PubMed GONUTS page

[PMID:15603737-14] 14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 Kalia, SK et al. (2004) BAG5 inhibits parkin and enhances dopaminergic neuron degeneration. Neuron 44 931-45 PubMed GONUTS page

[PMID:23921388-15] 15.0 ^15.1 ^15.2 ^15.3 ^15.4 Jakobsson, ME et al. (2013) Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylation. J. Biol. Chem. 288 27752-63 PubMed GONUTS page

[PMID:17167422-16] 16.0 ^16.1 ^16.2 ^16.3 Ribeil, JA et al. (2007) Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1. Nature 445 102-5 PubMed GONUTS page

[PMID:25281747-17] 17.0 ^17.1 Roder, K et al. (2014) RING finger protein RNF207, a novel regulator of cardiac excitation. J. Biol. Chem. 289 33730-40 PubMed GONUTS page

[PMID:17182002-18] Han, C et al. (2007) HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain. Biochem. Biophys. Res. Commun. 353 280-5 PubMed GONUTS page

[PMID:12150907-19] 19.0 ^19.1 ^19.2 ^19.3 ^19.4 ^19.5 Imai, Y et al. (2002) CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol. Cell 10 55-67 PubMed GONUTS page

[PMID:23533145-20] 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:19190083-21] Kesimer, M et al. (2009) Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J. 23 1858-68 PubMed GONUTS page

[PMID:21423176-22] Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page

[PMID:21231916-23] 23.00 ^23.01 ^23.02 ^23.03 ^23.04 ^23.05 ^23.06 ^23.07 ^23.08 ^23.09 ^23.10 ^23.11 ^23.12 ^23.13 ^23.14 ^23.15 ^23.16 ^23.17 Hageman, J et al. (2011) The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities. Biochem. J. 435 127-42 PubMed GONUTS page

[PMID:22516433-24] Bastos-Amador, P et al. (2012) Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. J Proteomics 75 3574-84 PubMed GONUTS page

[PMID:19199708-25] 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:20458337-26] 26.0 ^26.1 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:24061851-27] 27.0 ^27.1 ^27.2 Khalouei, S et al. (2014) Stress-induced localization of HSPA6 (HSP70B') and HSPA1A (HSP70-1) proteins to centrioles in human neuronal cells. Cell Stress Chaperones 19 321-7 PubMed GONUTS page

[PMID:9499401-28] 28.0 ^28.1 Shi, Y et al. (1998) Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev. 12 654-66 PubMed GONUTS page

[PMID:10205060-29] 29.0 ^29.1 ^29.2 Laroia, G et al. (1999) Control of mRNA decay by heat shock-ubiquitin-proteasome pathway. Science 284 499-502 PubMed GONUTS page

[PMID:9553041-30] 30.0 ^30.1 ^30.2 ^30.3 ^30.4 Maheswaran, S et al. (1998) Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70. Genes Dev. 12 1108-20 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:17289661-33] Jønson, L et al. (2007) Molecular composition of IMP1 ribonucleoprotein granules. Mol. Cell Proteomics 6 798-811 PubMed GONUTS page

[PMID:15885686-34] Kallijärvi, J et al. (2005) TRIM37 defective in mulibrey nanism is a novel RING finger ubiquitin E3 ligase. Exp. Cell Res. 308 146-55 PubMed GONUTS page

[PMID:18850735-35] 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:10859165-36] 36.0 ^36.1 Cuesta, R et al. (2000) Chaperone hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes. Genes Dev. 14 1460-70 PubMed GONUTS page

[PMID:21873635-37] 37.00 ^37.01 ^37.02 ^37.03 ^37.04 ^37.05 ^37.06 ^37.07 ^37.08 ^37.09 ^37.10 ^37.11 ^37.12 ^37.13 ^37.14 ^37.15 ^37.16 ^37.17 ^37.18 ^37.19 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:24252804-38] 38.0 ^38.1 Dias, V et al. (2013) The role of oxidative stress in Parkinson's disease. J Parkinsons Dis 3 461-91 PubMed GONUTS page

[PMID:16130169-39] 39.0 ^39.1 ^39.2 ^39.3 ^39.4 Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

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HUMAN:HS71A

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