HSPB1_MOUSE - dbPTM
HSPB1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSPB1_MOUSE
UniProt AC P14602
Protein Name Heat shock protein beta-1
Gene Name Hspb1
Organism Mus musculus (Mouse).
Sequence Length 209
Subcellular Localization Cytoplasm . Nucleus . Cytoplasm, cytoskeleton, spindle . Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles o
Protein Description Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization. [PubMed: 17661394 Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (By similarity]
Protein Sequence MTERRVPFSLLRSPSWEPFRDWYPAHSRLFDQAFGVPRLPDEWSQWFSAAGWPGYVRPLPAATAEGPAAVTLAAPAFSRALNRQLSSGVSEIRQTADRWRVSLDVNHFAPEELTVKTKEGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTLVSSSLSPEGTLTVEAPLPKAVTQSAEITIPVTFEARAQIGGPEAGKSEQSGAK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
9PhosphorylationTERRVPFSLLRSPSW
CCCCCCHHHCCCCCC
22.0324719451
12MethylationRVPFSLLRSPSWEPF
CCCHHHCCCCCCCCC
52.3824129315
13PhosphorylationVPFSLLRSPSWEPFR
CCHHHCCCCCCCCCC
24.2126824392
15PhosphorylationFSLLRSPSWEPFRDW
HHHCCCCCCCCCCCC
45.371860870
27PhosphorylationRDWYPAHSRLFDQAF
CCCCHHHHHHHHHHH
32.55-
71PhosphorylationAEGPAAVTLAAPAFS
CCCCEEEEEHHHHHH
13.12-
78PhosphorylationTLAAPAFSRALNRQL
EEHHHHHHHHHHHHH
20.81-
86PhosphorylationRALNRQLSSGVSEIR
HHHHHHHHHCHHHHH
19.391860870
87PhosphorylationALNRQLSSGVSEIRQ
HHHHHHHHCHHHHHH
52.3724925903
90PhosphorylationRQLSSGVSEIRQTAD
HHHHHCHHHHHHHHH
30.7224925903
102PhosphorylationTADRWRVSLDVNHFA
HHHHEEEEEECCCCC
15.4126824392
116UbiquitinationAPEELTVKTKEGVVE
CCHHCEEEEECCEEE
48.9522790023
118UbiquitinationEELTVKTKEGVVEIT
HHCEEEEECCEEEEC
46.9122790023
127AcetylationGVVEITGKHEERQDE
CEEEECCCCCCCCCC
38.91-
137PhosphorylationERQDEHGYISRCFTR
CCCCCCCCEEEEEEC
9.5328464351
139PhosphorylationQDEHGYISRCFTRKY
CCCCCCEEEEEECCC
17.95-
144 (in isoform 3)O-linked_Glycosylation-15.1030016717
145UbiquitinationISRCFTRKYTLPPGV
EEEEEECCCCCCCCC
39.2622790023
146PhosphorylationSRCFTRKYTLPPGVD
EEEEECCCCCCCCCC
15.3725293948
147PhosphorylationRCFTRKYTLPPGVDP
EEEECCCCCCCCCCC
35.5022006019
155PhosphorylationLPPGVDPTLVSSSLS
CCCCCCCCEECCCCC
35.0225293948
158PhosphorylationGVDPTLVSSSLSPEG
CCCCCEECCCCCCCC
19.8125293948
159PhosphorylationVDPTLVSSSLSPEGT
CCCCEECCCCCCCCC
28.0225293948
160PhosphorylationDPTLVSSSLSPEGTL
CCCEECCCCCCCCCE
25.9225293948
162PhosphorylationTLVSSSLSPEGTLTV
CEECCCCCCCCCEEE
23.8926824392
178PhosphorylationAPLPKAVTQSAEITI
ECCCCCCCCCEEEEE
22.9726824392
180PhosphorylationLPKAVTQSAEITIPV
CCCCCCCCEEEEEEE
20.6426824392
188O-linked_GlycosylationAEITIPVTFEARAQI
EEEEEEEEEEEEEEC
15.4830016717
202UbiquitinationIGGPEAGKSEQSGAK
CCCCCCCCCCCCCCC
58.8422790023
203PhosphorylationGGPEAGKSEQSGAK-
CCCCCCCCCCCCCC-
39.6926824392
206PhosphorylationEAGKSEQSGAK----
CCCCCCCCCCC----
36.34-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
15SPhosphorylationKinaseMAPKAPK2P49138
Uniprot
15SPhosphorylationKinasePKC-FAMILY-GPS
15SPhosphorylationKinasePKA-Uniprot
15SPhosphorylationKinasePKA-FAMILY-GPS
15SPhosphorylationKinasePKC-Uniprot
15SPhosphorylationKinasePRKACAP05132
GPS
15SPhosphorylationKinaseMAPKAPK3Q3UMW7
Uniprot
15SPhosphorylationKinaseMAPKAPK2P49137
PSP
15SPhosphorylationKinasePRKCDP28867
GPS
15SPhosphorylationKinasePRKCAP20444
GPS
15SPhosphorylationKinasePKA_GROUP-PhosphoELM
15SPhosphorylationKinasePKC_GROUP-PhosphoELM
86SPhosphorylationKinaseMAPKAPK5O54992
Uniprot
86SPhosphorylationKinasePKC-Uniprot
86SPhosphorylationKinasePKA_GROUP-PhosphoELM
86SPhosphorylationKinasePKA-Uniprot
86SPhosphorylationKinasePKC_GROUP-PhosphoELM
86SPhosphorylationKinasePKC-FAMILY-GPS
86SPhosphorylationKinasePKA-FAMILY-GPS
86SPhosphorylationKinaseMAPKAPK3Q3UMW7
Uniprot
86SPhosphorylationKinaseMAPKAPK2P49138
Uniprot
86SPhosphorylationKinaseMAPKAPK2P49137
PSP
86SPhosphorylationKinasePRKCDP28867
GPS
86SPhosphorylationKinasePRKCAP20444
GPS
86SPhosphorylationKinasePRKACAP05132
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSPB1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of HSPB1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KPCD_MOUSEPrkcdphysical
15731106
HSPB1_MOUSEHspb1physical
10383393
CISY_HUMANCSphysical
10383393
INS_HUMANINSphysical
10383393
CISY_PIGCSphysical
8093612
AMYG_YEASTSGA1physical
8093612

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSPB1_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASSSPECTROMETRY.
"Identification of MAPKAP kinase 2 as a major enzyme responsible forthe phosphorylation of the small mammalian heat shock proteins.";
Stokoe D., Engel K., Campbell D.G., Cohen P., Gaestel M.;
FEBS Lett. 313:307-313(1992).
Cited for: PHOSPHORYLATION AT SER-15 AND SER-86 BY MAPKAPK2.
"Identification of the phosphorylation sites of the murine small heatshock protein hsp25.";
Gaestel M., Schroeder W., Benndorf R., Lippmann C., Buchner K.,Hucho F., Erdmann V.A., Bielka H.;
J. Biol. Chem. 266:14721-14724(1991).
Cited for: PHOSPHORYLATION AT SER-15 AND SER-86.

TOP