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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
9 | Phosphorylation | TERRVPFSLLRSPSW CCCCCCHHHCCCCCC | 22.03 | 24719451 | |
12 | Methylation | RVPFSLLRSPSWEPF CCCHHHCCCCCCCCC | 52.38 | 24129315 | |
13 | Phosphorylation | VPFSLLRSPSWEPFR CCHHHCCCCCCCCCC | 24.21 | 26824392 | |
15 | Phosphorylation | FSLLRSPSWEPFRDW HHHCCCCCCCCCCCC | 45.37 | 1860870 | |
27 | Phosphorylation | RDWYPAHSRLFDQAF CCCCHHHHHHHHHHH | 32.55 | - | |
71 | Phosphorylation | AEGPAAVTLAAPAFS CCCCEEEEEHHHHHH | 13.12 | - | |
78 | Phosphorylation | TLAAPAFSRALNRQL EEHHHHHHHHHHHHH | 20.81 | - | |
86 | Phosphorylation | RALNRQLSSGVSEIR HHHHHHHHHCHHHHH | 19.39 | 1860870 | |
87 | Phosphorylation | ALNRQLSSGVSEIRQ HHHHHHHHCHHHHHH | 52.37 | 24925903 | |
90 | Phosphorylation | RQLSSGVSEIRQTAD HHHHHCHHHHHHHHH | 30.72 | 24925903 | |
102 | Phosphorylation | TADRWRVSLDVNHFA HHHHEEEEEECCCCC | 15.41 | 26824392 | |
116 | Ubiquitination | APEELTVKTKEGVVE CCHHCEEEEECCEEE | 48.95 | 22790023 | |
118 | Ubiquitination | EELTVKTKEGVVEIT HHCEEEEECCEEEEC | 46.91 | 22790023 | |
127 | Acetylation | GVVEITGKHEERQDE CEEEECCCCCCCCCC | 38.91 | - | |
137 | Phosphorylation | ERQDEHGYISRCFTR CCCCCCCCEEEEEEC | 9.53 | 28464351 | |
139 | Phosphorylation | QDEHGYISRCFTRKY CCCCCCEEEEEECCC | 17.95 | - | |
144 (in isoform 3) | O-linked_Glycosylation | - | 15.10 | 30016717 | |
145 | Ubiquitination | ISRCFTRKYTLPPGV EEEEEECCCCCCCCC | 39.26 | 22790023 | |
146 | Phosphorylation | SRCFTRKYTLPPGVD EEEEECCCCCCCCCC | 15.37 | 25293948 | |
147 | Phosphorylation | RCFTRKYTLPPGVDP EEEECCCCCCCCCCC | 35.50 | 22006019 | |
155 | Phosphorylation | LPPGVDPTLVSSSLS CCCCCCCCEECCCCC | 35.02 | 25293948 | |
158 | Phosphorylation | GVDPTLVSSSLSPEG CCCCCEECCCCCCCC | 19.81 | 25293948 | |
159 | Phosphorylation | VDPTLVSSSLSPEGT CCCCEECCCCCCCCC | 28.02 | 25293948 | |
160 | Phosphorylation | DPTLVSSSLSPEGTL CCCEECCCCCCCCCE | 25.92 | 25293948 | |
162 | Phosphorylation | TLVSSSLSPEGTLTV CEECCCCCCCCCEEE | 23.89 | 26824392 | |
178 | Phosphorylation | APLPKAVTQSAEITI ECCCCCCCCCEEEEE | 22.97 | 26824392 | |
180 | Phosphorylation | LPKAVTQSAEITIPV CCCCCCCCEEEEEEE | 20.64 | 26824392 | |
188 | O-linked_Glycosylation | AEITIPVTFEARAQI EEEEEEEEEEEEEEC | 15.48 | 30016717 | |
202 | Ubiquitination | IGGPEAGKSEQSGAK CCCCCCCCCCCCCCC | 58.84 | 22790023 | |
203 | Phosphorylation | GGPEAGKSEQSGAK- CCCCCCCCCCCCCC- | 39.69 | 26824392 | |
206 | Phosphorylation | EAGKSEQSGAK---- CCCCCCCCCCC---- | 36.34 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
15 | S | Phosphorylation | Kinase | MAPKAPK2 | P49138 | Uniprot |
15 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
15 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
15 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
15 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
15 | S | Phosphorylation | Kinase | PRKACA | P05132 | GPS |
15 | S | Phosphorylation | Kinase | MAPKAPK3 | Q3UMW7 | Uniprot |
15 | S | Phosphorylation | Kinase | MAPKAPK2 | P49137 | PSP |
15 | S | Phosphorylation | Kinase | PRKCD | P28867 | GPS |
15 | S | Phosphorylation | Kinase | PRKCA | P20444 | GPS |
15 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
15 | S | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
86 | S | Phosphorylation | Kinase | MAPKAPK5 | O54992 | Uniprot |
86 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
86 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
86 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
86 | S | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
86 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
86 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
86 | S | Phosphorylation | Kinase | MAPKAPK3 | Q3UMW7 | Uniprot |
86 | S | Phosphorylation | Kinase | MAPKAPK2 | P49138 | Uniprot |
86 | S | Phosphorylation | Kinase | MAPKAPK2 | P49137 | PSP |
86 | S | Phosphorylation | Kinase | PRKCD | P28867 | GPS |
86 | S | Phosphorylation | Kinase | PRKCA | P20444 | GPS |
86 | S | Phosphorylation | Kinase | PRKACA | P05132 | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HSPB1_MOUSE !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
KPCD_MOUSE | Prkcd | physical | 15731106 | |
HSPB1_MOUSE | Hspb1 | physical | 10383393 | |
CISY_HUMAN | CS | physical | 10383393 | |
INS_HUMAN | INS | physical | 10383393 | |
CISY_PIG | CS | physical | 8093612 | |
AMYG_YEAST | SGA1 | physical | 8093612 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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. |