| UniProt ID | SGT1_YEAST | |
|---|---|---|
| UniProt AC | Q08446 | |
| Protein Name | Protein SGT1 {ECO:0000303|PubMed:10445024, ECO:0000303|PubMed:12456005} | |
| Gene Name | SGT1 {ECO:0000312|SGD:S000005583} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 395 | |
| Subcellular Localization | ||
| Protein Description | Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Required for both entry into S phase and kinetochore function. Also involved in cyclic AMP (cAMP) pathway, possibly by participating in the assembly or the conformational activation of specific multiprotein complexes.. | |
| Protein Sequence | MPVEKDLKTAYKALYDEKEPLKALHLYDEILKGSPTNLTALIFKAACLEKLYFGFSDWHSDATMENAKELLDKALMTAEGRGDRSKIGLVNFRYFVHFFNIKDYELAQSYFKKAKNLGYVDDTLPLWEDRLETKLNKKNKKQKDSTNKHTIKPVESIENRGDNNSSHSPISPLKIETAPQESPKFKIDWYQSSTSVTISLFTVNLPESKEQVNIYISPNDRRTLSISYQVPKSGSEFQYNAKLSHEVDPKAVSLKIFPKKLEITLSKIDSTQWKKLEEDILTESSRLSDEGKNSDSATRLLSAETASKERLSYPSSSKKKIDWSKLDIDEEADEEAGSADSFFQKLYAGADPDTKRAMMKSFIESNGTALSTDWEDVSKGTVKTSPPEGMEPKHW | |
| 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 |
|---|---|---|---|---|---|
| 32 | Ubiquitination | HLYDEILKGSPTNLT HHHHHHHCCCCCCHH | 64.10 | 23749301 | |
| 73 | Ubiquitination | NAKELLDKALMTAEG HHHHHHHHHHHHHCC | 43.31 | 17644757 | |
| 86 | Ubiquitination | EGRGDRSKIGLVNFR CCCCCHHHEEEEECE | 41.51 | 17644757 | |
| 150 | Phosphorylation | KDSTNKHTIKPVESI CCCCCCCCCCCHHHH | 32.10 | 29136822 | |
| 156 | Phosphorylation | HTIKPVESIENRGDN CCCCCHHHHCCCCCC | 35.12 | 29136822 | |
| 165 | Phosphorylation | ENRGDNNSSHSPISP CCCCCCCCCCCCCCC | 35.36 | 22369663 | |
| 166 | Phosphorylation | NRGDNNSSHSPISPL CCCCCCCCCCCCCCC | 30.06 | 22369663 | |
| 168 | Phosphorylation | GDNNSSHSPISPLKI CCCCCCCCCCCCCEE | 26.36 | 22369663 | |
| 171 | Phosphorylation | NSSHSPISPLKIETA CCCCCCCCCCEEEEC | 27.80 | 22369663 | |
| 177 | Phosphorylation | ISPLKIETAPQESPK CCCCEEEECCCCCCC | 47.30 | 28889911 | |
| 182 | Phosphorylation | IETAPQESPKFKIDW EEECCCCCCCCEEEE | 28.30 | 29688323 | |
| 225 | Phosphorylation | PNDRRTLSISYQVPK CCCCCEEEEEEECCC | 14.63 | 25752575 | |
| 282 | Phosphorylation | KLEEDILTESSRLSD HHHHHHHHHHHCCCC | 33.87 | 22369663 | |
| 284 | Phosphorylation | EEDILTESSRLSDEG HHHHHHHHHCCCCCC | 18.61 | 22369663 | |
| 285 | Phosphorylation | EDILTESSRLSDEGK HHHHHHHHCCCCCCC | 30.89 | 22369663 | |
| 288 | Phosphorylation | LTESSRLSDEGKNSD HHHHHCCCCCCCCCH | 32.29 | 22369663 | |
| 292 | Ubiquitination | SRLSDEGKNSDSATR HCCCCCCCCCHHHHH | 51.75 | 23749301 | |
| 294 | Phosphorylation | LSDEGKNSDSATRLL CCCCCCCCHHHHHHH | 36.11 | 21440633 | |
| 296 | Phosphorylation | DEGKNSDSATRLLSA CCCCCCHHHHHHHCH | 31.21 | 21440633 | |
| 302 | Phosphorylation | DSATRLLSAETASKE HHHHHHHCHHHHCCH | 28.75 | 22369663 | |
| 305 | Phosphorylation | TRLLSAETASKERLS HHHHCHHHHCCHHHC | 35.63 | 24909858 | |
| 307 | Phosphorylation | LLSAETASKERLSYP HHCHHHHCCHHHCCC | 42.33 | 22369663 | |
| 312 | Phosphorylation | TASKERLSYPSSSKK HHCCHHHCCCCCCCC | 41.02 | 28889911 | |
| 313 | Phosphorylation | ASKERLSYPSSSKKK HCCHHHCCCCCCCCC | 16.24 | 28889911 | |
| 341 | Phosphorylation | EEAGSADSFFQKLYA HHCCCHHHHHHHHHC | 27.90 | 30377154 | |
| 355 | Ubiquitination | AGADPDTKRAMMKSF CCCCHHHHHHHHHHH | 45.61 | 23749301 | |
| 361 | Phosphorylation | TKRAMMKSFIESNGT HHHHHHHHHHHHCCC | 17.35 | 25521595 | |
| 365 | Phosphorylation | MMKSFIESNGTALST HHHHHHHHCCCEECC | 35.43 | 25521595 | |
| 384 | Phosphorylation | VSKGTVKTSPPEGME HCCCCCCCCCCCCCC | 41.97 | 28889911 | |
| 385 | Phosphorylation | SKGTVKTSPPEGMEP CCCCCCCCCCCCCCC | 32.51 | 28889911 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SGT1_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 SGT1_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-165; SER-166; SER-168;SER-171; SER-225 AND THR-305, AND MASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-168 ANDSER-171, AND MASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-171, ANDMASS SPECTROMETRY. | |
