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Protein Page:
HSP40 (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
HSP40 a chaperone protein that translocates rapidly from the cytoplasm to the nucleus, and especially to the nucleoli, upon heat shock.Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Interacts with DNAJC3. Interacts with SRPK1. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Nucleolus
Cellular Component: nucleolus; nucleus; cytosol
Molecular Function: ATPase activator activity; protein binding; chaperone binding; unfolded protein binding; Hsp70 protein binding; ATPase binding
Biological Process: chaperone cofactor-dependent protein folding; positive regulation of ATPase activity; response to unfolded protein
Reference #:  P25685 (UniProtKB)
Alt. Names/Synonyms: DnaJ (Hsp40) homolog, subfamily B, member 1; DnaJ (Hsp40) homolog, subfmaily B, member 1; DnaJ homolog subfamily B member 1; DnaJ protein homolog 1; DNAJ1; DNAJB1; DNJB1; hDj-1; HDJ1; Heat shock 40 kDa protein 1; heat shock 40kD protein 1; Heat shock protein 40; HSP40; HSPF1; Human DnaJ protein 1; radial spoke 16 homolog B; RSPH16B; Sis1
Gene Symbols: DNAJB1
Molecular weight: 38,044 Da
Basal Isoelectric point: 8.74  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

HSP40

Protein Structure Not Found.


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Sites Implicated In
transcription, inhibited: S149‑p, S151‑p, S171‑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


 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 4 Y5-p ___MGKDyYQTLGLA
0 2 K21-ub GASDEEIkRAYRRQA
0 1 K21-sc GASDEEIkRAYRRQA
0 3 K35-ub ALRYHPDkNKEPGAE
0 1 K44-ac KEPGAEEkFKEIAEA
0 1 K44 KEPGAEEKFKEIAEA
0 1 K46 PGAEEkFKEIAEAYD
0 1 T88-p SGGGANGtsFSYTFH
0 1 S89-p GGGANGtsFSYTFHG
1 0 S149-p TNVNFGRsRsAQEPA
1 1 S151-p VNFGRsRsAQEPARK
1 0 S171-p VTHDLRVsLEEIysG
0 501 Y176-p RVsLEEIysGCtkKM
0 3 S177-p VsLEEIysGCtkKMK
0 1 T180-p EEIysGCtkKMKIsH
0 6 K181-ac EIysGCtkKMKIsHK
0 4 S186-p CtkKMKIsHKRLNPD
0 2 K195-ac KRLNPDGksIRNEDK
0 9 K195-ub KRLNPDGksIRNEDK
0 1 S196-p RLNPDGksIRNEDKI
0 1 T205-p RNEDKILtIEVKKGW
0 1 T227-p FPKEGDQtsNNIPAD
0 1 S228-p PKEGDQtsNNIPADI
0 2 S252-p NIFKRDGsDVIYPAR
0 1 S261-p VIYPARIsLREALCG
0 2 K286-ub RTIPVVFkDVIRPGM
0 1 K296-ub IRPGMRRkVPGEGLP
0 1 K306-ub GEGLPLPktPEKRGD
0 5 T307-p EGLPLPktPEKRGDL
  mouse

 
Y5 ___MGKDYYQTLGLA
K21 GASDDEIKRAYRRQA
K21 GASDDEIKRAYRRQA
K35-ub ALRYHPDkNKEPGAE
K44 KEPGAEEKFkEIAEA
K44-ub KEPGAEEkFkEIAEA
K46-ub PGAEEkFkEIAEAYD
T88 SSGGANGTSFSYTFH
S89 SGGANGTSFSYTFHG
S149 TNMNFGRSRPSQEPT
P151 MNFGRSRPSQEPTRK
S171 VTHDLRVSLEEIySG
Y176-p RVSLEEIySGCTKKM
S177 VSLEEIySGCTKKMK
T180 EEIySGCTKKMKISH
K181 EIySGCTKKMKISHK
S186 CTKKMKISHKRLNPD
K195 KRLNPDGKSIRNEDK
K195-ub KRLNPDGkSIRNEDK
S196 RLNPDGkSIRNEDKI
T205 RNEDKILTIEVKRGW
T227 FPKEGDQTSNNIPAD
S228 PKEGDQTSNNIPADI
S252 NIFKRDGSDVIYPAR
S261 VIYPARISLREALCG
K286-ub RTIPVVFkDVIRPGM
K296 IRPGMRRKVPGEGLP
K306 GEGLPLPKTPEKRGD
T307 EGLPLPKTPEKRGDL
  rat

 
Y5 ___MGKDYYQTLGLA
K21 GASDDEIKRAYRRQA
K21 GASDDEIKRAYRRQA
K35 ALRYHPDKNKEPGAE
K44 KEPGAEEKFKEIAEA
K44 KEPGAEEKFKEIAEA
K46 PGAEEKFKEIAEAYD
T88 SSGGANGTSFSYTFH
S89 SGGANGTSFSYTFHG
S149 TNMNFGRSRPTQEPT
P151 MNFGRSRPTQEPTRK
S171 VTHDLRVSLEEIySG
Y176-p RVSLEEIySGCTKKM
S177 VSLEEIySGCTKKMK
T180 EEIySGCTKKMKISH
K181 EIySGCTKKMKISHK
S186 CTKKMKISHKRLNPD
K195 KRLNPDGKSIRNEDK
K195 KRLNPDGKSIRNEDK
S196 RLNPDGKSIRNEDKI
T205 RNEDKILTIEVKRGW
T227 FPKEGDQTSNNIPAD
S228 PKEGDQTSNNIPADI
S252 NIFKRDGSDVIYPAR
S261 VIYPARISLREALCG
- gap
- gap
- gap
- gap
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