Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
HSP70 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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; Heat shock protein
Chromosomal Location of Human Ortholog: 6p21.3
Cellular Component: signalosome; focal adhesion; mitochondrion; endoplasmic reticulum; inclusion body; ribonucleoprotein complex; cytosol; centriole; nucleoplasm; perinuclear region of cytoplasm; cytoplasm; nuclear speck; nucleus; ubiquitin ligase complex; vesicle
Molecular Function: viral receptor activity; protein binding; enzyme binding; G-protein-coupled receptor binding; ubiquitin protein ligase binding; heat shock protein binding; unfolded protein binding; double-stranded RNA binding; ATPase activity; protein N-terminus binding; ATPase activity, coupled; ATP binding
Biological Process: negative regulation of cell proliferation; entry of virus into host cell; protein stabilization; positive regulation of erythrocyte differentiation; mRNA catabolic process; negative regulation of protein ubiquitination; protein refolding; gene expression; negative regulation of cell growth; response to unfolded protein; negative regulation of apoptosis
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/1B; heat shock 70kDa protein 1A/1B; 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, HSPA1B
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® Total Proteins
Select Structure to View Below

HSP70

Protein Structure Not Found.


STRING  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  Ensembl Protein


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
 

Show Multiple Sequence Alignment


 LTP 

LTP: 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.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 7 S106-p DkPKVQVsykGETkA
0 2 K3-ac _____MAkAAAIGID
0 2 K3-ub _____MAkAAAIGID
0 1 T13-p AIGIDLGtTysCVGV
0 50 Y15-p GIDLGtTysCVGVFQ
0 8 S16-p IDLGtTysCVGVFQH
0 6 S40-p QGNRTTPsyVAFTDT
0 417 Y41-p GNRTTPsyVAFTDTE
0 1 R49-m1 VAFTDTErLIGDAAk
0 2 K56-ac rLIGDAAkNQVALNP
0 33 K56-ub rLIGDAAkNQVALNP
0 1 T66-p VALNPQNtVFDAkRL
0 105 K71-ac QNtVFDAkRLIGRkF
0 15 K71-ub QNtVFDAkRLIGRkF
0 1 K71-sc QNtVFDAkRLIGRkF
0 4 K77-ub AkRLIGRkFGDPVVQ
0 2 S85-p FGDPVVQsDMkhWPF
0 6 K88-ac PVVQsDMkhWPFQVI
0 3 K88-ub PVVQsDMkhWPFQVI
1 0 H89-p VVQsDMkhWPFQVIN
0 1 K100-ub QVINDGDkPKVQVsy
0 26 Y107-p kPKVQVsykGETkAF
0 3 K108-ac PKVQVsykGETkAFY
0 16 K108-ub PKVQVsykGETkAFY
0 1 K108-sc PKVQVsykGETkAFY
0 1 K112-ac VsykGETkAFYPEEI
0 4 K112-ub VsykGETkAFYPEEI
1 0 K126-ac ISSMVLTkMkEIAEA
0 6 K126-ub ISSMVLTkMkEIAEA
0 1 K128-ub SMVLTkMkEIAEAYL
0 3 S153-p VPAYFNDsQRQATkD
1 0 K159-ac DsQRQATkDAGVIAG
0 23 K159-ub DsQRQATkDAGVIAG
0 1 K190 YGLDRTGKGERNVLI
0 1 K220-ub DDGIFEVkATAGDtH
0 1 T226-p VkATAGDtHLGGEDF
0 69 K246-ac NHFVEEFkRKHKKDI
0 7 K246-ub NHFVEEFkRKHKKDI
0 1 K246-sc NHFVEEFkRKHKKDI
0 4 S254-p RKHKKDIsQNkRAVR
0 3 K257-ub KKDIsQNkRAVRRLR
0 103 T265-p RAVRRLRtACERAKR
0 2 K319-ac STLEPVEkALRDAkL
0 14 K319-ub STLEPVEkALRDAkL
1 7 K325-ub EkALRDAkLDkAQIH
0 1 K328-ac LRDAkLDkAQIHDLV
0 4 K328-ub LRDAkLDkAQIHDLV
0 1 K345-ub GGSTRIPkVQkLLQD
0 3 K348-ac TRIPkVQkLLQDFFN
0 20 K348-ub TRIPkVQkLLQDFFN
0 5 S362-p NGRDLNKsINPDEAV
0 2 K415-ub GVMTALIkRNsTIPT
1 2 S418-p TALIkRNsTIPTkQT
0 3 K423-ub RNsTIPTkQTQIFTT
1 26 K451-ub EGERAMTkDNNLLGR
0 19 R469-m1 SGIPPAPrGVPQIEV
0 3 K500-ac KSTGKANkItITNDk
0 11 K500-ub KSTGKANkItITNDk
0 2 T502-p TGKANkItITNDkGR
0 123 K507-ub kItITNDkGRLSkEE
0 50 K512-ub NDkGRLSkEEIERMV
0 2 K524-ac RMVQEAEkykAEDEV
1 84 K524-ub RMVQEAEkykAEDEV
1 24 Y525-p MVQEAEkykAEDEVQ
0 1 K526-ac VQEAEkykAEDEVQR
1 19 K526-ub VQEAEkykAEDEVQR
0 1 S537-p EVQRERVsAkNALES
0 22 K539-ub QRERVsAkNALESYA
0 1 K539-sc QRERVsAkNALESYA
0 5 K550-ub ESYAFNMksAVEDEG
0 2 S551-p SYAFNMksAVEDEGL
1 15 K559-ub AVEDEGLkGkISEAD
0 2 K561-m1 EDEGLkGkISEADKK
1 3 K561-m2 EDEGLkGkISEADKK
1 2 K561-m3 EDEGLkGkISEADKK
0 7 K561-ub EDEGLkGkISEADKK
0 1 K567 GkISEADKKKVLDkC
0 2 K573-ub DKKKVLDkCQEVISW
0 1 K589-ub DANTLAEkDEFEHkR
0 3 K595-ac EkDEFEHkRkELEQV
0 3 K595-ub EkDEFEHkRkELEQV
0 36 K597-ub DEFEHkRkELEQVCN
0 2 N604 kELEQVCNPIIsGLy
0 1 S608-p QVCNPIIsGLyQGAG
0 59 Y611-p NPIIsGLyQGAGGPG
0 14 K628-ub GFGAQGPkGGsGsGP
1 6 S631-p AQGPkGGsGsGPtIE
1 5 S633-p GPkGGsGsGPtIEEV
1 4 T636-p GGsGsGPtIEEVD__
  HSP70 iso2  
- gap
K3 _____MAKAAAIGID
K3 _____MAKAAAIGID
T13 AIGIDLGTTYSCVGV
Y15 GIDLGTTYSCVGVFQ
S16 IDLGTTYSCVGVFQH
S40 QGNRTTPSYVAFTDT
Y41 GNRTTPSYVAFTDTE
R49 VAFTDTERLIGDAAK
K56 RLIGDAAKNQVALNP
K56 RLIGDAAKNQVALNP
T66 VALNPQNTVFDAKRL
K71 QNTVFDAKRLIGRKF
K71 QNTVFDAKRLIGRKF
K71 QNTVFDAKRLIGRKF
K77 AKRLIGRKFGDPVVQ
S85 FGDPVVQSDMKHWPF
K88 PVVQSDMKHWPFQVI
K88 PVVQSDMKHWPFQVI
H89 VVQSDMKHWPFQVIN
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
S98 PFQVINDSQRQATKD
K104 DSQRQATKDAGVIAG
K104 DSQRQATKDAGVIAG
K135 YGLDRTGKGERNVLI
K165 DDGIFEVKATAGDTH
T171 VKATAGDTHLGGEDF
K191 NHFVEEFKRKHKKDI
K191 NHFVEEFKRKHKKDI
K191 NHFVEEFKRKHKKDI
S199 RKHKKDISQNKRAVR
K202 KKDISQNKRAVRRLR
T210 RAVRRLRTACERAKR
K264 STLEPVEKALRDAKL
K264 STLEPVEKALRDAKL
K270 EKALRDAKLDKAQIH
K273 LRDAKLDKAQIHDLV
K273 LRDAKLDKAQIHDLV
K290 GGSTRIPKVQKLLQD
K293 TRIPKVQKLLQDFFN
K293 TRIPKVQKLLQDFFN
S307 NGRDLNKSINPDEAV
K360 GVMTALIKRNSTIPT
S363 TALIKRNSTIPTKQT
K368 RNSTIPTKQTQIFTT
K396 EGERAMTKDNNLLGR
R414 SGIPPAPRGVPQIEV
K445 KSTGKANKITITNDK
K445 KSTGKANKITITNDK
T447 TGKANKITITNDKGR
K452 KITITNDKGRLSKEE
K457 NDKGRLSKEEIERMV
K469 RMVQEAEKYKAEDEV
K469 RMVQEAEKYKAEDEV
Y470 MVQEAEKYKAEDEVQ
K471 VQEAEKYKAEDEVQR
K471 VQEAEKYKAEDEVQR
S482 EVQRERVSAKNALES
K484 QRERVSAKNALESYA
K484 QRERVSAKNALESYA
K495 ESYAFNMKSAVEDEG
S496 SYAFNMKSAVEDEGL
K504 AVEDEGLKGKISEAD
K506 EDEGLKGKISEADKK
K506 EDEGLKGKISEADKK
K506 EDEGLKGKISEADKK
K506 EDEGLKGKISEADKK
K512 GKISEADKKKVLDKC
K518 DKKKVLDKCQEVISW
K534 DANTLAEKDEFEHKR
K540 EKDEFEHKRKELEQV
K540 EKDEFEHKRKELEQV
K542 DEFEHKRKELEQVCN
N549 KELEQVCNPIISGLY
S553 QVCNPIISGLYQGAG
Y556 NPIISGLYQGAGGPG
K573 GFGAQGPKGGSGSGP
S576 AQGPKGGSGSGPTIE
S578 GPKGGSGSGPTIEEV
T581 GGSGSGPTIEEVD__
  mouse

 
N106 DKPKVQVNYkGESRS
K3 _____MAKNTAIGID
K3-ub _____MAkNTAIGID
T13 AIGIDLGTTySCVGV
Y15-p GIDLGTTySCVGVFQ
S16 IDLGTTySCVGVFQH
S40-p QGNRTTPsyVAFTDT
Y41-p GNRTTPsyVAFTDTE
R49 VAFTDTERLIGDAAk
K56 RLIGDAAKNQVALNP
K56-ub RLIGDAAkNQVALNP
T66 VALNPQNTVFDAkRL
K71-ac QNTVFDAkRLIGRKF
K71-ub QNTVFDAkRLIGRKF
K71 QNTVFDAKRLIGRKF
K77 AkRLIGRKFGDAVVQ
S85 FGDAVVQSDMKHWPF
K88 AVVQSDMKHWPFQVV
K88 AVVQSDMKHWPFQVV
H89 VVQSDMKHWPFQVVN
K100 QVVNDGDKPKVQVNY
Y107 KPKVQVNYkGESRSF
K108 PKVQVNYKGESRSFF
K108-ub PKVQVNYkGESRSFF
K108 PKVQVNYKGESRSFF
R112 VNYkGESRSFFPEEI
R112 VNYkGESRSFFPEEI
K126 ISSMVLTKMKEIAEA
K126-ub ISSMVLTkMKEIAEA
K128 SMVLTkMKEIAEAYL
S153 VPAYFNDSQRQATkD
K159 DSQRQATKDAGVIAG
K159-ub DSQRQATkDAGVIAG
K190-ub YGLDRTGkGERNVLI
K220 DDGIFEVKATAGDtH
T226-p VKATAGDtHLGGEDF
K246-ac SHFVEEFkRKHKKDI
K246 SHFVEEFKRKHKKDI
K246 SHFVEEFKRKHKKDI
S254-p RKHKKDIsQNkRAVR
K257-ub KKDIsQNkRAVRRLR
T265-p RAVRRLRtACERAKR
K319 GTLEPVEKALRDAKM
K319 GTLEPVEKALRDAKM
K325 EKALRDAKMDKAQIH
K328 LRDAKMDKAQIHDLV
K328 LRDAKMDKAQIHDLV
K345 GGSTRIPKVQkLLQD
K348 TRIPKVQKLLQDFFN
K348-ub TRIPKVQkLLQDFFN
S362 NGRDLNKSINPDEAV
K415 GVMTALIKRNSTIPT
S418 TALIKRNSTIPTKQT
K423 RNSTIPTKQTQTFTT
R451 EGERAMTRDNNLLGR
R469-m1 SGIPPAPrGVPQIEV
K500 KSTGKANKITITNDk
K500-ub KSTGKANkITITNDk
T502 TGKANkITITNDkGR
K507-ub kITITNDkGRLSkEE
K512-ub NDkGRLSkEEIERMV
R524 RMVQEAERYKAEDEV
R524 RMVQEAERYKAEDEV
Y525 MVQEAERYKAEDEVQ
K526 VQEAERYKAEDEVQR
K526 VQEAERYKAEDEVQR
A537 EVQRDRVAAkNALES
K539-ub QRDRVAAkNALESYA
K539 QRDRVAAKNALESYA
K550 ESYAFNMKSAVEDEG
S551 SYAFNMKSAVEDEGL
K559 AVEDEGLKGKLSEAD
K561 EDEGLKGKLSEADkK
K561 EDEGLKGKLSEADkK
K561 EDEGLKGKLSEADkK
K561 EDEGLKGKLSEADkK
K567-ac GKLSEADkKKVLDKC
K573 DkKKVLDKCQEVISW
K589 DSNTLADKEEFVHKR
K595 DKEEFVHKREELERV
K595 DKEEFVHKREELERV
E597 EEFVHKREELERVCs
S604-p EELERVCsPIISGLY
S608 RVCsPIISGLYQGAG
Y611 sPIISGLYQGAGAPG
K628-ub GFGAQAPkGASGSGP
S631 AQAPkGASGSGPTIE
S633 APkGASGSGPTIEEV
T636 GASGSGPTIEEVD__
  rat

 
N106 DKPKVQVNYkGENRS
K3 _____MAKKTAIGID
K3 _____MAKKTAIGID
T13 AIGIDLGTTYSCVGV
Y15 GIDLGTTYSCVGVFQ
S16 IDLGTTYSCVGVFQH
S40 QGNRTTPSyVAFTDT
Y41-p GNRTTPSyVAFTDTE
R49 VAFTDTERLIGDAAk
K56-ac RLIGDAAkNQVALNP
K56 RLIGDAAKNQVALNP
T66 VALNPQNTVFDAkRL
K71 QNTVFDAKRLIGRKF
K71-ub QNTVFDAkRLIGRKF
K71 QNTVFDAKRLIGRKF
K77 AkRLIGRKFGDPVVQ
S85 FGDPVVQSDMKHWPF
K88 PVVQSDMKHWPFQVV
K88 PVVQSDMKHWPFQVV
H89 VVQSDMKHWPFQVVN
K100 QVVNDGDKPKVQVNY
Y107 KPKVQVNYkGENRSF
K108-ac PKVQVNYkGENRSFY
K108-ub PKVQVNYkGENRSFY
K108 PKVQVNYKGENRSFY
R112 VNYkGENRSFYPEEI
R112 VNYkGENRSFYPEEI
K126 ISSMVLTKMKEIAEA
K126 ISSMVLTKMKEIAEA
K128 SMVLTKMKEIAEAYL
S153 VPAYFNDSQRQATkD
K159 DSQRQATKDAGVIAG
K159-ub DSQRQATkDAGVIAG
K190 YGLDRTGKGERNVLI
K220 DDGIFEVKATAGDTH
T226 VKATAGDTHLGGEDF
K246-ac SHFVEEFkRKHKKDI
K246-ub SHFVEEFkRKHKKDI
K246 SHFVEEFKRKHKKDI
S254 RKHKKDISQNKRAVR
K257 KKDISQNKRAVRRLR
T265 RAVRRLRTACERAKR
K319-ac GTLEPVEkALRDAKL
K319 GTLEPVEKALRDAKL
K325 EkALRDAKLDkAQIH
K328 LRDAKLDKAQIHDLV
K328-ub LRDAKLDkAQIHDLV
K345 GGSTRIPKVQkLLQD
K348-ac TRIPKVQkLLQDFFN
K348-ub TRIPKVQkLLQDFFN
S362 NGRDLNKSINPDEAV
K415 GVMTALIKRNSTIPT
S418 TALIKRNSTIPTKQT
K423 RNSTIPTKQTQTFTT
R451 EGERAMTRDNNLLGR
R469-m1 SGIPPAPrGVPQIEV
K500-ac KSTGKANkITITNDk
K500 KSTGKANKITITNDk
T502 TGKANkITITNDkGR
K507-ub kITITNDkGRLSKEE
K512 NDkGRLSKEEIERMV
R524 RMVQEAERYKAEDEV
R524 RMVQEAERYKAEDEV
Y525 MVQEAERYKAEDEVQ
K526 VQEAERYKAEDEVQR
K526 VQEAERYKAEDEVQR
A537 EVQRERVAAKNALES
K539 QRERVAAKNALESYA
K539 QRERVAAKNALESYA
K550 ESYAFNMKSAVEDEG
S551 SYAFNMKSAVEDEGL
K559 AVEDEGLKGKISEAD
K561 EDEGLKGKISEADKK
K561 EDEGLKGKISEADKK
K561 EDEGLKGKISEADKK
K561 EDEGLKGKISEADKK
K567 GKISEADKKKVLDKC
K573 DKKKVLDKCQEVISW
K589 DSNTLAEKEEFVHKR
K595 EKEEFVHKREELERV
K595 EKEEFVHKREELERV
E597 EEFVHKREELERVCN
N604 EELERVCNPIISGLY
S608 RVCNPIISGLYQGAG
Y611 NPIISGLYQGAGAPG
K628 GFGAQAPKGGsGSGP
S631-p AQAPKGGsGSGPTIE
S633 APKGGsGSGPTIEEV
T636 GGsGSGPTIEEVD__
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.