UniProt ID | SGTA_RAT | |
---|---|---|
UniProt AC | O70593 | |
Protein Name | Small glutamine-rich tetratricopeptide repeat-containing protein alpha | |
Gene Name | Sgta | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 314 | |
Subcellular Localization | Cytoplasm . Nucleus . Co-localizes with HSP90AB1 in the cytoplasm. Increased nuclear accumulation seen during cell apoptosis. | |
Protein Description | Co-chaperone that binds misfolded and hydrophobic patches-containing client proteins in the cytosol. Mediates their targeting to the endoplasmic reticulum but also regulates their sorting to the proteasome when targeting fails. Functions in tail-anchored/type II transmembrane proteins membrane insertion constituting with ASNA1 and the BAG6 complex a targeting module. Functions upstream of the BAG6 complex and ASNA1, binding more rapidly the transmembrane domain of newly synthesized proteins. It is also involved in the regulation of the endoplasmic reticulum-associated misfolded protein catabolic process via its interaction with BAG6: collaborates with the BAG6 complex to maintain hydrophobic substrates in non-ubiquitinated states. Competes with RNF126 for interaction with BAG6, preventing the ubiquitination of client proteins associated with the BAG6 complex (By similarity). Binds directly to HSC70 and HSP70 and regulates their ATPase activity. [PubMed: 12878599] | |
Protein Sequence | MDNRKRLAYAIIQFLHGQLRHGGLSSDAQESLEVAIQCLETAFGVTLEDSDLALPQTLPEIFEAATASKEMPQDPRGPDRTPPSEEDSAEAERLKTEGNEQMKLENFEAAVHLYGKAIELNPANAVYFCNRAAAYSKLGNYVGAVQDCERAIGIDPGYSKAYGRMGLALSSLNKHAEAVAYYKKALELDPDNDTYKSNLKIAELKLREAPSPTGGVGSLDIAGLLNNPHFITMASSLMNSPQLQQLMSGMISGGHNPLGTPGSSPQHSDLASLIQAGQQFAQQMQQQNPEFVEQIRSQVVRSRTPSASHEEQQE | |
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 |
---|---|---|---|---|---|
81 | Phosphorylation | DPRGPDRTPPSEEDS CCCCCCCCCCCHHHH | 47.10 | 19700791 | |
84 | Phosphorylation | GPDRTPPSEEDSAEA CCCCCCCCHHHHHHH | 55.62 | 25403869 | |
88 | Phosphorylation | TPPSEEDSAEAERLK CCCCHHHHHHHHHHH | 31.15 | 25403869 | |
95 | Acetylation | SAEAERLKTEGNEQM HHHHHHHHCCCCHHH | 51.23 | 22902405 | |
137 | Acetylation | NRAAAYSKLGNYVGA HHHHHHHHHHCHHHH | 47.97 | - | |
137 | Ubiquitination | NRAAAYSKLGNYVGA HHHHHHHHHHCHHHH | 47.97 | - | |
160 | Acetylation | GIDPGYSKAYGRMGL CCCCCCHHHHHHHHH | 36.82 | 22902405 | |
160 | Ubiquitination | GIDPGYSKAYGRMGL CCCCCCHHHHHHHHH | 36.82 | - | |
200 | Ubiquitination | DTYKSNLKIAELKLR CHHHHHHHHHEEEEC | 44.09 | - | |
211 | Phosphorylation | LKLREAPSPTGGVGS EEECCCCCCCCCCCC | 41.99 | 30240740 | |
297 | Phosphorylation | EFVEQIRSQVVRSRT HHHHHHHHHHHHHCC | 29.02 | 25575281 | |
302 | Phosphorylation | IRSQVVRSRTPSASH HHHHHHHHCCCCCCH | 28.97 | 29779826 | |
304 | Phosphorylation | SQVVRSRTPSASHEE HHHHHHCCCCCCHHH | 23.88 | 21738781 | |
306 | Phosphorylation | VVRSRTPSASHEEQQ HHHHCCCCCCHHHHC | 41.62 | 23712012 | |
308 | Phosphorylation | RSRTPSASHEEQQE- HHCCCCCCHHHHCC- | 35.45 | 27097102 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of SGTA_RAT !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SGTA_RAT !! |
* 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 SGTA_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites."; Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-81, AND MASSSPECTROMETRY. |