| UniProt ID | GCS1_YEAST | |
|---|---|---|
| UniProt AC | P35197 | |
| Protein Name | ADP-ribosylation factor GTPase-activating protein GCS1 | |
| Gene Name | GCS1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 352 | |
| Subcellular Localization | Cytoplasm . Mitochondrion . Cytoplasm, perinuclear region . Golgi apparatus . Found also in the mitochondria and in the perinuclear region. | |
| Protein Description | GTPase-activating protein (GAP) for ARF1 and ARF2. Involved in intracellular vesicular transport. Required for transport from the trans-Golgi network. Implicated in the regulation of retrograde transport from the Golgi to the ER and in actin cytoskeletal organization. May be involved in the maintenance of mitochondrial morphology, possibly through organizing the actin cytoskeleton in Saccharomyces.. | |
| Protein Sequence | MSDWKVDPDTRRRLLQLQKIGANKKCMDCGAPNPQWATPKFGAFICLECAGIHRGLGVHISFVRSITMDQFKPEELLRMEKGGNEPLTEWFKSHNIDLSLPQKVKYDNPVAEDYKEKLTCLCEDRVFEEREHLDFDASKLSATSQTAASATPGVAQSREGTPLENRRSATPANSSNGANFQKEKNEAYFAELGKKNQSRPDHLPPSQGGKYQGFGSTPAKPPQERSAGSSNTLSLENFQADPLGTLSRGWGLFSSAVTKSFEDVNETVIKPHVQQWQSGELSEETKRAAAQFGQKFQETSSYGFQAFSNFTKNFNGNAEDSSTAGNTTHTEYQKIDNNDKKNEQDEDKWDDF | |
| 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 | ------MSDWKVDPD ------CCCCCCCHH | 52.78 | 24961812 | |
| 19 | Acetylation | RRLLQLQKIGANKKC HHHHHHHHHCCCCCC | 52.26 | 22865919 | |
| 40 | Ubiquitination | NPQWATPKFGAFICL CCCCCCCCCCEEEEH | 52.67 | 23749301 | |
| 65 | Phosphorylation | VHISFVRSITMDQFK CCCEEEEECCHHHCC | 19.67 | 27017623 | |
| 67 | Phosphorylation | ISFVRSITMDQFKPE CEEEEECCHHHCCHH | 18.88 | 25752575 | |
| 72 | Acetylation | SITMDQFKPEELLRM ECCHHHCCHHHHHHH | 45.98 | 24489116 | |
| 92 | Ubiquitination | EPLTEWFKSHNIDLS CCHHHHHHHCCCCCC | 52.45 | 17644757 | |
| 103 | Ubiquitination | IDLSLPQKVKYDNPV CCCCCCCCCCCCCCC | 38.46 | 17644757 | |
| 138 | Phosphorylation | EHLDFDASKLSATSQ HHCCCCHHHCCCCCH | 35.65 | 19779198 | |
| 139 | Acetylation | HLDFDASKLSATSQT HCCCCHHHCCCCCHH | 48.45 | 24489116 | |
| 141 | Phosphorylation | DFDASKLSATSQTAA CCCHHHCCCCCHHHH | 32.98 | 22890988 | |
| 143 | Phosphorylation | DASKLSATSQTAASA CHHHCCCCCHHHHHC | 20.28 | 22890988 | |
| 144 | Phosphorylation | ASKLSATSQTAASAT HHHCCCCCHHHHHCC | 25.83 | 22890988 | |
| 146 | Phosphorylation | KLSATSQTAASATPG HCCCCCHHHHHCCCC | 24.77 | 22890988 | |
| 149 | Phosphorylation | ATSQTAASATPGVAQ CCCHHHHHCCCCCCC | 30.16 | 22369663 | |
| 151 | Phosphorylation | SQTAASATPGVAQSR CHHHHHCCCCCCCCC | 20.34 | 22369663 | |
| 157 | Phosphorylation | ATPGVAQSREGTPLE CCCCCCCCCCCCCCC | 23.67 | 22369663 | |
| 161 | Phosphorylation | VAQSREGTPLENRRS CCCCCCCCCCCCCCC | 21.68 | 22369663 | |
| 168 | Phosphorylation | TPLENRRSATPANSS CCCCCCCCCCCCCCC | 33.00 | 22369663 | |
| 170 | Phosphorylation | LENRRSATPANSSNG CCCCCCCCCCCCCCC | 24.95 | 22369663 | |
| 174 | Phosphorylation | RSATPANSSNGANFQ CCCCCCCCCCCCCCC | 27.56 | 22369663 | |
| 175 | Phosphorylation | SATPANSSNGANFQK CCCCCCCCCCCCCCH | 38.81 | 22369663 | |
| 182 | Ubiquitination | SNGANFQKEKNEAYF CCCCCCCHHHHHHHH | 67.53 | 23749301 | |
| 184 | Acetylation | GANFQKEKNEAYFAE CCCCCHHHHHHHHHH | 68.10 | 24489116 | |
| 210 | Ubiquitination | LPPSQGGKYQGFGST CCCCCCCCCCCCCCC | 41.02 | 23749301 | |
| 216 | Phosphorylation | GKYQGFGSTPAKPPQ CCCCCCCCCCCCCCC | 29.02 | 22369663 | |
| 217 | Phosphorylation | KYQGFGSTPAKPPQE CCCCCCCCCCCCCCC | 27.87 | 22369663 | |
| 220 | Ubiquitination | GFGSTPAKPPQERSA CCCCCCCCCCCCCCC | 59.44 | 23749301 | |
| 226 | Phosphorylation | AKPPQERSAGSSNTL CCCCCCCCCCCCCCC | 35.91 | 22369663 | |
| 229 | Phosphorylation | PQERSAGSSNTLSLE CCCCCCCCCCCCCCC | 21.82 | 22369663 | |
| 230 | Phosphorylation | QERSAGSSNTLSLEN CCCCCCCCCCCCCCC | 32.68 | 22369663 | |
| 232 | Phosphorylation | RSAGSSNTLSLENFQ CCCCCCCCCCCCCCC | 21.48 | 22369663 | |
| 234 | Phosphorylation | AGSSNTLSLENFQAD CCCCCCCCCCCCCCC | 31.44 | 22369663 | |
| 255 | Phosphorylation | RGWGLFSSAVTKSFE CCCCCCCHHHHHCHH | 21.30 | 22369663 | |
| 258 | Phosphorylation | GLFSSAVTKSFEDVN CCCCHHHHHCHHHHH | 22.23 | 22369663 | |
| 260 | Phosphorylation | FSSAVTKSFEDVNET CCHHHHHCHHHHHHH | 25.22 | 22369663 | |
| 267 | Phosphorylation | SFEDVNETVIKPHVQ CHHHHHHHCCCHHHH | 23.48 | 22369663 | |
| 278 | Phosphorylation | PHVQQWQSGELSEET HHHHHHHCCCCCHHH | 31.13 | 22369663 | |
| 282 | Phosphorylation | QWQSGELSEETKRAA HHHCCCCCHHHHHHH | 29.14 | 22369663 | |
| 285 | Phosphorylation | SGELSEETKRAAAQF CCCCCHHHHHHHHHH | 23.06 | 22369663 | |
| 286 | Ubiquitination | GELSEETKRAAAQFG CCCCHHHHHHHHHHH | 43.23 | 23749301 | |
| 295 | Acetylation | AAAQFGQKFQETSSY HHHHHHHHHHHHHHC | 49.77 | 25381059 | |
| 295 | Ubiquitination | AAAQFGQKFQETSSY HHHHHHHHHHHHHHC | 49.77 | 22817900 | |
| 300 | Phosphorylation | GQKFQETSSYGFQAF HHHHHHHHHCHHHHH | 22.32 | 27017623 | |
| 301 | Phosphorylation | QKFQETSSYGFQAFS HHHHHHHHCHHHHHH | 36.37 | 30377154 | |
| 302 | Phosphorylation | KFQETSSYGFQAFSN HHHHHHHCHHHHHHC | 23.02 | 30377154 | |
| 312 | Ubiquitination | QAFSNFTKNFNGNAE HHHHCCCCCCCCCCC | 56.24 | 22817900 | |
| 321 | Phosphorylation | FNGNAEDSSTAGNTT CCCCCCCCCCCCCCC | 22.54 | 22369663 | |
| 322 | Phosphorylation | NGNAEDSSTAGNTTH CCCCCCCCCCCCCCC | 34.30 | 22369663 | |
| 323 | Phosphorylation | GNAEDSSTAGNTTHT CCCCCCCCCCCCCCC | 42.40 | 22369663 | |
| 327 | Phosphorylation | DSSTAGNTTHTEYQK CCCCCCCCCCCEEEE | 21.02 | 22369663 | |
| 328 | Phosphorylation | SSTAGNTTHTEYQKI CCCCCCCCCCEEEEC | 30.69 | 23749301 | |
| 330 | Phosphorylation | TAGNTTHTEYQKIDN CCCCCCCCEEEECCC | 34.00 | 22369663 | |
| 332 | Phosphorylation | GNTTHTEYQKIDNND CCCCCCEEEECCCCC | 19.09 | 22369663 | |
| 334 | Acetylation | TTHTEYQKIDNNDKK CCCCEEEECCCCCCC | 51.64 | 24489116 | |
| 334 | Ubiquitination | TTHTEYQKIDNNDKK CCCCEEEECCCCCCC | 51.64 | 23749301 | |
| 340 | Acetylation | QKIDNNDKKNEQDED EECCCCCCCCCCCCC | 60.67 | 25381059 | |
| 348 | Ubiquitination | KNEQDEDKWDDF--- CCCCCCCCCCCC--- | 50.94 | 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 GCS1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GCS1_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 GCS1_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 THR-67; SER-144; SER-157;THR-161; SER-168; THR-170; SER-216; THR-217; SER-229; SER-230; THR-232AND SER-260, 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-157; THR-161; THR-170;SER-174 AND SER-175, 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-157 AND THR-161, ANDMASS SPECTROMETRY. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170 AND SER-175, ANDMASS SPECTROMETRY. | |
