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HSP70 (human)

Overview HSP70 a critical chaperone protein that has a high affinity for unfolded polypeptide chains. It binds extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In cooperation with other chaperones, hsp70 stabilizes preexistent proteins against aggregation and mediates the folding of newly translated polypeptides in the cytosol as well as within organelles. Mitochondrial HSP70 is crucial to the import process: mutant forms of HSP70 fail to import precursor proteins. Is anti-apoptotic in sympathetic neurones and mediates this effect primarily by suppressing c-Jun transcriptional signalling. Interacts with tau protein and mediates proper folding of tau. Can promote the degradation of tau protein. Triptolide, a potential therapeutic agent for progression/metastasis of pancreatic cancer, causes pancreatic cancer cell death by induction of apoptosis, an effect mediated by the inhibition of HSP70. Note: This description may include information from UniProtKB. Protein type: Chaperone; Motility/polarity/chemotaxis Reference #:  P08107 (UniProtKB) Alt. Names/Synonyms: dnaK-type molecular chaperone HSP70-1; Heat shock 70 kDa protein 1/2; Heat shock 70 kDa protein 1A/1B; heat shock 70kD protein 1A; heat shock 70kDa protein 1A; heat shock-induced protein; HSP70-1; HSP70-1/HSP70-2; HSP70-1A; HSP70.1/HSP70.2; HSP70I; HSP71; HSP72; HSPA1; HSPA1A; HSPA1B Gene Symbols: HSPA1A Molecular weight: 70,052 Da Basal Isoelectric point: 5.48  Predict pI for various phosphorylation states CST Pathways:  Inhibition of Apoptosis Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below HSP70 1HJO - A=3-382 (human) 1S3X - A=1-382 (human) 1XQS - C/D=182-371 (human) 2E88 - A=1-388 (human) 2E8A - A=1-388 (human) 2LMG - A=537-610 (human) 3A8Y - A/B=1-388 (human) 3ATU - A=1-388 (human) 3ATV - A=1-388 (human) 3AY9 - A=1-388 (human) 3D2E - D/B=1-382 (human) 3D2F - D/B=1-382 (human) 3JXU - A=1-387 (human) 3LOF - F/A/D/C/E/B=534-641 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1HJO 1S3X 1XQS 2E88 2E8A 2LMG 3A8Y 3ATU 3ATV 3AY9 3D2E 3D2F 3JXU 3LOF  |  Phospho3D  |  DISEASE 140550 603012  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Sites Implicated In
intracellular localization: Y525‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	2		K3-a	_____MAkAAAIGID
0	2		K3-u	_____MAkAAAIGID
0	47		Y15-p	GIDLGTTySCVGVFQ
0	5		S40-p	QGNRTTPsyVAFTDT
0	417		Y41-p	GNRTTPsyVAFTDTE
0	1		R49-m1	VAFTDTErLIGDAAk
0	34		K56-u	rLIGDAAkNQVALNP
0	105		K71-a	QNTVFDAkRLIGRkF
0	15		K71-u	QNTVFDAkRLIGRkF
0	4		K77-u	AkRLIGRkFGDPVVQ
0	6		K88-a	PVVQSDMkHWPFQVI
0	24		Y107-p	KPKVQVSykGETkAF
0	2		K108-a	PKVQVSykGETkAFY
0	16		K108-u	PKVQVSykGETkAFY
0	1		K112-a	VSykGETkAFYPEEI
0	4		K112-u	VSykGETkAFYPEEI
0	6		K126-u	ISSMVLTkMKEIAEA
0	2		S153-p	VPAYFNDsQRQATkD
0	23		K159-u	DsQRQATkDAGVIAG
0	1		K220-u	DDGIFEVkATAGDTH
0	67		K246-a	NHFVEEFkRKHKKDI
0	7		K246-u	NHFVEEFkRKHKKDI
0	2		S254-p	RKHKKDIsQNkRAVR
0	3		K257-u	KKDIsQNkRAVRRLR
0	103		T265-p	RAVRRLRtACERAKR
0	14		K319-u	STLEPVEkALRDAkL
1	7		K325-u	EkALRDAkLDkAQIH
0	1		K328-a	LRDAkLDkAQIHDLV
0	4		K328-u	LRDAkLDkAQIHDLV
0	1		K345-u	GGSTRIPkVQkLLQD
0	20		K348-u	TRIPkVQkLLQDFFN
0	2		K415-u	GVMTALIkRNsTIPT
0	2		S418-p	TALIkRNsTIPTkQT
0	3		K423-u	RNsTIPTkQTQIFTT
1	26		K451-u	EGERAMTkDNNLLGR
0	18		R469-m1	SGIPPAPrGVPQIEV
0	11		K500-u	KSTGKANkItITNDk
0	1		T502-p	TGKANkItITNDkGR
0	123		K507-u	kItITNDkGRLSkEE
0	50		K512-u	NDkGRLSkEEIERMV
0	2		K524-a	RMVQEAEkykAEDEV
1	84		K524-u	RMVQEAEkykAEDEV
1	23		Y525-p	MVQEAEkykAEDEVQ
0	1		K526-a	VQEAEkykAEDEVQR
1	19		K526-u	VQEAEkykAEDEVQR
0	22		K539-u	QRERVSAkNALESYA
0	5		K550-u	ESYAFNMkSAVEDEG
1	15		K559-u	AVEDEGLkGkISEAD
0	1		K561-m1	EDEGLkGkISEADKK
1	2		K561-m2	EDEGLkGkISEADKK
1	1		K561-m3	EDEGLkGkISEADKK
0	7		K561-u	EDEGLkGkISEADKK
0	1		K567	GkISEADKKKVLDkC
0	2		K573-u	DKKKVLDkCQEVISW
0	1		K589-u	DANTLAEkDEFEHkR
0	3		K595-a	EkDEFEHkRkELEQV
0	3		K595-u	EkDEFEHkRkELEQV
0	36		K597-u	DEFEHkRkELEQVCN
0	2		N604	kELEQVCNPIISGLy
0	55		Y611-p	NPIISGLyQGAGGPG
0	14		K628-u	GFGAQGPkGGsGSGP
0	6		S631-p	AQGPkGGsGSGPTIE

	mouse
K3	_____MAKNTAIGID
K3-u	_____MAkNTAIGID
Y15-p	GIDLGTTySCVGVFQ
S40	QGNRTTPSyVAFTDT
Y41-p	GNRTTPSyVAFTDTE
R49	VAFTDTERLIGDAAk
K56-u	RLIGDAAkNQVALNP
K71-a	QNTVFDAkRLIGRKF
K71-u	QNTVFDAkRLIGRKF
K77	AkRLIGRKFGDAVVQ
K88	AVVQSDMKHWPFQVV
Y107	KPKVQVNYkGESRSF
K108	PKVQVNYKGESRSFF
K108-u	PKVQVNYkGESRSFF
R112	VNYkGESRSFFPEEI
R112	VNYkGESRSFFPEEI
K126-u	ISSMVLTkMKEIAEA
S153	VPAYFNDSQRQATkD
K159-u	DSQRQATkDAGVIAG
K220	DDGIFEVKATAGDTH
K246	SHFVEEFKRKHKKDI
K246	SHFVEEFKRKHKKDI
S254-p	RKHKKDIsQNkRAVR
K257-u	KKDIsQNkRAVRRLR
T265-p	RAVRRLRtACERAKR
K319	GTLEPVEKALRDAKM
K325	EKALRDAKMDKAQIH
K328	LRDAKMDKAQIHDLV
K328	LRDAKMDKAQIHDLV
K345	GGSTRIPKVQkLLQD
K348-u	TRIPKVQkLLQDFFN
K415	GVMTALIKRNSTIPT
S418	TALIKRNSTIPTKQT
K423	RNSTIPTKQTQTFTT
R451	EGERAMTRDNNLLGR
R469-m1	SGIPPAPrGVPQIEV
K500-u	KSTGKANkITITNDk
T502	TGKANkITITNDkGR
K507-u	kITITNDkGRLSkEE
K512-u	NDkGRLSkEEIERMV
R524	RMVQEAERYKAEDEV
R524	RMVQEAERYKAEDEV
Y525	MVQEAERYKAEDEVQ
K526	VQEAERYKAEDEVQR
K526	VQEAERYKAEDEVQR
K539-u	QRDRVAAkNALESYA
K550	ESYAFNMKSAVEDEG
K559	AVEDEGLKGKLSEAD
K561	EDEGLKGKLSEADkK
K561	EDEGLKGKLSEADkK
K561	EDEGLKGKLSEADkK
K561	EDEGLKGKLSEADkK
K567-a	GKLSEADkKKVLDKC
K573	DkKKVLDKCQEVISW
K589	DSNTLADKEEFVHKR
K595	DKEEFVHKREELERV
K595	DKEEFVHKREELERV
E597	EEFVHKREELERVCs
S604-p	EELERVCsPIISGLY
Y611	sPIISGLYQGAGAPG
K628-u	GFGAQAPkGASGSGP
S631	AQAPkGASGSGPTIE

	rat
K3	_____MAKKTAIGID
K3	_____MAKKTAIGID
Y15	GIDLGTTYSCVGVFQ
S40	QGNRTTPSyVAFTDT
Y41-p	GNRTTPSyVAFTDTE
R49	VAFTDTERLIGDAAK
K56	RLIGDAAKNQVALNP
K71	QNTVFDAKRLIGRKF
K71-u	QNTVFDAkRLIGRKF
K77	AkRLIGRKFGDPVVQ
K88	PVVQSDMKHWPFQVV
Y107	KPKVQVNYkGENRSF
K108	PKVQVNYKGENRSFY
K108-u	PKVQVNYkGENRSFY
R112	VNYkGENRSFYPEEI
R112	VNYkGENRSFYPEEI
K126	ISSMVLTKMKEIAEA
S153	VPAYFNDSQRQATkD
K159-u	DSQRQATkDAGVIAG
K220	DDGIFEVKATAGDTH
K246	SHFVEEFKRKHKKDI
K246-u	SHFVEEFkRKHKKDI
S254	RKHKKDISQNKRAVR
K257	KKDISQNKRAVRRLR
T265	RAVRRLRTACERAKR
K319	GTLEPVEKALRDAKL
K325	EKALRDAKLDkAQIH
K328	LRDAKLDKAQIHDLV
K328-u	LRDAKLDkAQIHDLV
K345	GGSTRIPKVQkLLQD
K348-u	TRIPKVQkLLQDFFN
K415	GVMTALIKRNSTIPT
S418	TALIKRNSTIPTKQT
K423	RNSTIPTKQTQTFTT
R451	EGERAMTRDNNLLGR
R469-m1	SGIPPAPrGVPQIEV
K500	KSTGKANKITITNDk
T502	TGKANKITITNDkGR
K507-u	KITITNDkGRLSKEE
K512	NDkGRLSKEEIERMV
R524	RMVQEAERYKAEDEV
R524	RMVQEAERYKAEDEV
Y525	MVQEAERYKAEDEVQ
K526	VQEAERYKAEDEVQR
K526	VQEAERYKAEDEVQR
K539	QRERVAAKNALESYA
K550	ESYAFNMKSAVEDEG
K559	AVEDEGLKGKISEAD
K561	EDEGLKGKISEADKK
K561	EDEGLKGKISEADKK
K561	EDEGLKGKISEADKK
K561	EDEGLKGKISEADKK
K567	GKISEADKKKVLDKC
K573	DKKKVLDKCQEVISW
K589	DSNTLAEKEEFVHKR
K595	EKEEFVHKREELERV
K595	EKEEFVHKREELERV
E597	EEFVHKREELERVCN
N604	EELERVCNPIISGLY
Y611	NPIISGLYQGAGAPG
K628	GFGAQAPKGGsGSGP
S631-p	AQAPKGGsGSGPTIE

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