| UniProt ID | SGT2_YEAST | |
|---|---|---|
| UniProt AC | Q12118 | |
| Protein Name | Small glutamine-rich tetratricopeptide repeat-containing protein 2 | |
| Gene Name | SGT2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 346 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Co-chaperone that binds to the molecular chaperone Hsp70 (SSA1 and SSA2). Regulates Hsp70 ATPase activity (By similarity). Required for recovery from heat shock.. | |
| Protein Sequence | MSASKEEIAALIVNYFSSIVEKKEISEDGADSLNVAMDCISEAFGFEREAVSGILGKSEFKGQHLADILNSASRVPESNKKDDAENVEINIPEDDAETKAKAEDLKMQGNKAMANKDYELAINKYTEAIKVLPTNAIYYANRAAAHSSLKEYDQAVKDAESAISIDPSYFRGYSRLGFAKYAQGKPEEALEAYKKVLDIEGDNATEAMKRDYESAKKKVEQSLNLEKTVPEQSRDADVDASQGASAGGLPDLGSLLGGGLGGLMNNPQLMQAAQKMMSNPGAMQNIQKMMQDPSIRQMAEGFASGGGTPNLSDLMNNPALRNMAGNLFGGAGAQSTDETPDNENKQ | |
| 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 | Phosphorylation | ------MSASKEEIA ------CCCCHHHHH | 41.05 | 22369663 | |
| 4 | Phosphorylation | ----MSASKEEIAAL ----CCCCHHHHHHH | 33.04 | 22369663 | |
| 15 | Phosphorylation | IAALIVNYFSSIVEK HHHHHHHHHHHHHHC | 8.24 | 22369663 | |
| 17 | Phosphorylation | ALIVNYFSSIVEKKE HHHHHHHHHHHHCCC | 14.59 | 22369663 | |
| 18 | Phosphorylation | LIVNYFSSIVEKKEI HHHHHHHHHHHCCCC | 22.28 | 22369663 | |
| 52 | Phosphorylation | GFEREAVSGILGKSE CCCHHHHHHHCCCCC | 27.45 | 22369663 | |
| 57 | Acetylation | AVSGILGKSEFKGQH HHHHHCCCCCCCCHH | 43.28 | 24489116 | |
| 61 | Acetylation | ILGKSEFKGQHLADI HCCCCCCCCHHHHHH | 54.32 | 24489116 | |
| 80 | Succinylation | SRVPESNKKDDAENV HCCCCCCCCCCHHCC | 67.85 | 23954790 | |
| 80 | Acetylation | SRVPESNKKDDAENV HCCCCCCCCCCHHCC | 67.85 | 24489116 | |
| 81 | Acetylation | RVPESNKKDDAENVE CCCCCCCCCCHHCCE | 66.16 | 24489116 | |
| 106 | Acetylation | KAKAEDLKMQGNKAM HHHHHHHHHHCCHHH | 41.31 | 24489116 | |
| 116 | Succinylation | GNKAMANKDYELAIN CCHHHHCCCHHHHHH | 52.75 | 23954790 | |
| 116 | Ubiquitination | GNKAMANKDYELAIN CCHHHHCCCHHHHHH | 52.75 | 23749301 | |
| 116 | Acetylation | GNKAMANKDYELAIN CCHHHHCCCHHHHHH | 52.75 | 24489116 | |
| 124 | Acetylation | DYELAINKYTEAIKV CHHHHHHHHHHHHHH | 47.65 | 24489116 | |
| 130 | Ubiquitination | NKYTEAIKVLPTNAI HHHHHHHHHCCCCHH | 44.78 | 24961812 | |
| 130 | Acetylation | NKYTEAIKVLPTNAI HHHHHHHHHCCCCHH | 44.78 | 24489116 | |
| 147 | Phosphorylation | ANRAAAHSSLKEYDQ HHHHHHHHHHHHHHH | 32.41 | 28889911 | |
| 148 | Phosphorylation | NRAAAHSSLKEYDQA HHHHHHHHHHHHHHH | 33.33 | 28889911 | |
| 150 | Succinylation | AAAHSSLKEYDQAVK HHHHHHHHHHHHHHH | 57.06 | 23954790 | |
| 150 | Acetylation | AAAHSSLKEYDQAVK HHHHHHHHHHHHHHH | 57.06 | 22865919 | |
| 157 | Acetylation | KEYDQAVKDAESAIS HHHHHHHHHHHHHHC | 54.99 | 24489116 | |
| 161 | Phosphorylation | QAVKDAESAISIDPS HHHHHHHHHHCCCHH | 32.40 | 28889911 | |
| 168 | Phosphorylation | SAISIDPSYFRGYSR HHHCCCHHHHCCCCH | 32.91 | 19823750 | |
| 169 | Phosphorylation | AISIDPSYFRGYSRL HHCCCHHHHCCCCHH | 11.59 | 19823750 | |
| 173 | Phosphorylation | DPSYFRGYSRLGFAK CHHHHCCCCHHCHHH | 6.07 | 19823750 | |
| 174 | Phosphorylation | PSYFRGYSRLGFAKY HHHHCCCCHHCHHHH | 24.69 | 19823750 | |
| 181 | Phosphorylation | SRLGFAKYAQGKPEE CHHCHHHHHCCCHHH | 10.75 | 21082442 | |
| 185 | Acetylation | FAKYAQGKPEEALEA HHHHHCCCHHHHHHH | 36.86 | 24489116 | |
| 194 | Acetylation | EEALEAYKKVLDIEG HHHHHHHHHHHCCCC | 43.37 | 24489116 | |
| 195 | Ubiquitination | EALEAYKKVLDIEGD HHHHHHHHHHCCCCC | 35.04 | 23749301 | |
| 209 | Ubiquitination | DNATEAMKRDYESAK CCHHHHHHHHHHHHH | 49.52 | 23749301 | |
| 209 | Acetylation | DNATEAMKRDYESAK CCHHHHHHHHHHHHH | 49.52 | 22865919 | |
| 209 | Succinylation | DNATEAMKRDYESAK CCHHHHHHHHHHHHH | 49.52 | 23954790 | |
| 216 | Succinylation | KRDYESAKKKVEQSL HHHHHHHHHHHHHHH | 63.51 | 23954790 | |
| 216 | Ubiquitination | KRDYESAKKKVEQSL HHHHHHHHHHHHHHH | 63.51 | 17644757 | |
| 217 | Ubiquitination | RDYESAKKKVEQSLN HHHHHHHHHHHHHHC | 62.86 | 17644757 | |
| 218 | Ubiquitination | DYESAKKKVEQSLNL HHHHHHHHHHHHHCH | 50.74 | 23749301 | |
| 227 | Ubiquitination | EQSLNLEKTVPEQSR HHHHCHHHCCCCHHH | 58.97 | 23749301 | |
| 227 | Acetylation | EQSLNLEKTVPEQSR HHHHCHHHCCCCHHH | 58.97 | 24489116 | |
| 228 | Phosphorylation | QSLNLEKTVPEQSRD HHHCHHHCCCCHHHC | 31.73 | 28889911 | |
| 233 | Phosphorylation | EKTVPEQSRDADVDA HHCCCCHHHCCCCCH | 30.39 | 28889911 | |
| 278 | Phosphorylation | QAAQKMMSNPGAMQN HHHHHHHCCHHHHHH | 36.05 | 28152593 | |
| 288 | Ubiquitination | GAMQNIQKMMQDPSI HHHHHHHHHHCCHHH | 32.32 | 23749301 | |
| 294 | Phosphorylation | QKMMQDPSIRQMAEG HHHHCCHHHHHHHHH | 38.40 | 30377154 | |
| 304 | Phosphorylation | QMAEGFASGGGTPNL HHHHHHHCCCCCCCH | 35.39 | 22369663 | |
| 308 | Phosphorylation | GFASGGGTPNLSDLM HHHCCCCCCCHHHHH | 16.57 | 24909858 | |
| 312 | Phosphorylation | GGGTPNLSDLMNNPA CCCCCCHHHHHCCHH | 35.03 | 22369663 | |
| 335 | Phosphorylation | FGGAGAQSTDETPDN CCCCCCCCCCCCCCC | 36.97 | 23749301 | |
| 336 | Phosphorylation | GGAGAQSTDETPDNE CCCCCCCCCCCCCCC | 26.27 | 28132839 | |
| 339 | Phosphorylation | GAQSTDETPDNENKQ CCCCCCCCCCCCCCC | 38.46 | 28132839 | |
| 345 | Ubiquitination | ETPDNENKQ------ CCCCCCCCC------ | 51.73 | 23749301 |
| 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 SGT2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SGT2_YEAST !! | ||||||
* 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 SGT2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; THR-308 AND SER-312,AND MASS SPECTROMETRY. | |
