| UniProt ID | CHIP_MOUSE | |
|---|---|---|
| UniProt AC | Q9WUD1 | |
| Protein Name | STIP1 homology and U box-containing protein 1 {ECO:0000305} | |
| Gene Name | Stub1 {ECO:0000312|MGI:MGI:1891731} | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 304 | |
| Subcellular Localization | Cytoplasm . Nucleus . Translocates to the nucleus in response to inflammatory signals in regulatory T-cells (Treg). | |
| Protein Description | E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner. [PubMed: 23973223 Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation. Likely mediates polyubiquitination and downregulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation (By similarity] | |
| Protein Sequence | MKGKEEKEGGARLGTGGGGSPDKSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQPEQALADCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRIAKKKRWNSIEERRIHQESELHSYLTRLIAAERERELEECQRNHEGHEDDGHIRAQQACIEAKHDKYMADMDELFSQVDEKRKKRDIPDYLCGKISFELMREPCITPSGITYDRKDIEEHLQRVGHFDPVTRSPLTQEQLIPNLAMKEVIDAFISENGWVEDY | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Ubiquitination | ------MKGKEEKEG ------CCCCCCCCC | 77.89 | 21855799 | |
| 15 | Phosphorylation | EGGARLGTGGGGSPD CCCCCCCCCCCCCCC | 36.93 | 24925903 | |
| 20 | Phosphorylation | LGTGGGGSPDKSPSA CCCCCCCCCCCCCCH | 32.95 | 27087446 | |
| 23 | Ubiquitination | GGGGSPDKSPSAQEL CCCCCCCCCCCHHHH | 68.59 | - | |
| 24 | Phosphorylation | GGGSPDKSPSAQELK CCCCCCCCCCHHHHH | 31.31 | 24925903 | |
| 26 | Phosphorylation | GSPDKSPSAQELKEQ CCCCCCCCHHHHHHH | 50.07 | 24925903 | |
| 42 | Acetylation | NRLFVGRKYPEAAAC CCEECCCCCHHHHHH | 60.26 | 22826441 | |
| 126 | Ubiquitination | QRAYSLAKEQRLNFG HHHHHHHHHHHCCCC | 60.72 | 27667366 | |
| 150 | Phosphorylation | AKKKRWNSIEERRIH HHHHCCCCHHHHHHC | 25.15 | 26643407 | |
| 272 | Phosphorylation | VGHFDPVTRSPLTQE HCCCCCCCCCCCCHH | 30.71 | 25521595 | |
| 274 | Phosphorylation | HFDPVTRSPLTQEQL CCCCCCCCCCCHHHH | 18.20 | 21082442 | |
| 277 | Phosphorylation | PVTRSPLTQEQLIPN CCCCCCCCHHHHCHH | 33.18 | 25521595 |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 2 | K | ubiquitylation |
| 21855799 |
* 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 CHIP_MOUSE !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-26, AND MASSSPECTROMETRY. | |
| "The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY. | |
| "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-20, AND MASSSPECTROMETRY. | |
| "Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP."; Scaglione K.M., Zavodszky E., Todi S.V., Patury S., Xu P.,Rodriguez-Lebron E., Fischer S., Konen J., Djarmati A., Peng J.,Gestwicki J.E., Paulson H.L.; Mol. Cell 43:599-612(2011). Cited for: FUNCTION, INTERACTION WITH UBE2W AND ATXN3, UBIQUITINATION AT LYS-2,AND MUTAGENESIS OF LYS-2; LYS-4 AND LYS-7. | |
