| UniProt ID | GGA1_YEAST | |
|---|---|---|
| UniProt AC | Q06336 | |
| Protein Name | ADP-ribosylation factor-binding protein GGA1 | |
| Gene Name | GGA1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 557 | |
| Subcellular Localization | Golgi apparatus, trans-Golgi network. | |
| Protein Description | May play a role in the regulation of membrane traffic through the trans-Golgi network.. | |
| Protein Sequence | MPQRIELTSEPVRKPRSTESSLLRKIQRACRSTLPEPDLGLNLDVADYINSKQGATPREAVLAIEKLVNNGDTQAAVFALSLLDVLVKNCGYSIHLQISRKEFLNDLVKRFPEQPPLRYSKVQQMILEAIEEWYQTICKHASYKDDLQYINDMHKLLKYKGYTFPKVGSENLAVLRPNDQLRTPSELQEEQERAQAAKLEELLRSGKPDDLKEANKLMKIMAGFKDDTKVAVKQAINNELNKLKRKADLFNEMLTSADEPDLENEAIQELYGDLKSAQPKFKKLIEEERDDDALVSNLSKFNDLVIQLLKRYKSIKGMKEEELNVPDTNEPAKELNLIDFDDDTTANTPSVTSPSKSLQPFDDLLGDFNKVSLSSPKSPQENDTVVDILGDAHSKSSGIDLLDFDSQPGESKTALSAYSNSIVLPNGLLNSSSNSKEITAQSQRHILNQSDHLRIDYELTRESMTKLRLVIFYSNISSDPITNFALLVASPKGTTLSLQPQSGNMLQSNSRDGIKQIASVEGISVNLGKPIKLKWKANYCTKGDSKEESGTTSLPTI | |
| 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 |
|---|---|---|---|---|---|
| 183 | Phosphorylation | RPNDQLRTPSELQEE CCCCCCCCHHHHHHH | 39.50 | 21126336 | |
| 185 | Phosphorylation | NDQLRTPSELQEEQE CCCCCCHHHHHHHHH | 50.77 | 25752575 | |
| 225 | Ubiquitination | MKIMAGFKDDTKVAV HHHHCCCCCCHHHHH | 54.50 | 23749301 | |
| 242 | Ubiquitination | AINNELNKLKRKADL HHHHHHHHHHHHHHH | 68.93 | 23749301 | |
| 246 | Ubiquitination | ELNKLKRKADLFNEM HHHHHHHHHHHHHHH | 44.67 | 24961812 | |
| 310 | Acetylation | DLVIQLLKRYKSIKG HHHHHHHHHHHHCCC | 63.37 | 24489116 | |
| 344 | Phosphorylation | LIDFDDDTTANTPSV CEECCCCCCCCCCCC | 34.50 | 22369663 | |
| 345 | Phosphorylation | IDFDDDTTANTPSVT EECCCCCCCCCCCCC | 25.55 | 22369663 | |
| 348 | Phosphorylation | DDDTTANTPSVTSPS CCCCCCCCCCCCCCC | 17.93 | 22369663 | |
| 350 | Phosphorylation | DTTANTPSVTSPSKS CCCCCCCCCCCCCCC | 35.67 | 22369663 | |
| 352 | Phosphorylation | TANTPSVTSPSKSLQ CCCCCCCCCCCCCCC | 38.98 | 25521595 | |
| 353 | Phosphorylation | ANTPSVTSPSKSLQP CCCCCCCCCCCCCCC | 25.64 | 22369663 | |
| 355 | Phosphorylation | TPSVTSPSKSLQPFD CCCCCCCCCCCCCHH | 34.34 | 20377248 | |
| 357 | Phosphorylation | SVTSPSKSLQPFDDL CCCCCCCCCCCHHHH | 36.25 | 22369663 | |
| 372 | Phosphorylation | LGDFNKVSLSSPKSP HCCCCCCCCCCCCCC | 24.92 | 22369663 | |
| 374 | Phosphorylation | DFNKVSLSSPKSPQE CCCCCCCCCCCCCCC | 36.77 | 25521595 | |
| 375 | Phosphorylation | FNKVSLSSPKSPQEN CCCCCCCCCCCCCCC | 41.46 | 25521595 | |
| 378 | Phosphorylation | VSLSSPKSPQENDTV CCCCCCCCCCCCCCE | 34.89 | 22369663 | |
| 384 | Phosphorylation | KSPQENDTVVDILGD CCCCCCCCEEEHHCC | 33.73 | 22369663 | |
| 394 | Phosphorylation | DILGDAHSKSSGIDL EHHCCCCCCCCCCCE | 35.63 | 22369663 | |
| 396 | Phosphorylation | LGDAHSKSSGIDLLD HCCCCCCCCCCCEEE | 36.49 | 22369663 | |
| 397 | Phosphorylation | GDAHSKSSGIDLLDF CCCCCCCCCCCEEEC | 43.43 | 22369663 | |
| 406 | Phosphorylation | IDLLDFDSQPGESKT CCEEECCCCCCCCHH | 37.96 | 29136822 | |
| 411 | Phosphorylation | FDSQPGESKTALSAY CCCCCCCCHHHHHHH | 41.02 | 22369663 | |
| 413 | Phosphorylation | SQPGESKTALSAYSN CCCCCCHHHHHHHCC | 41.95 | 30377154 | |
| 416 | Phosphorylation | GESKTALSAYSNSIV CCCHHHHHHHCCCEE | 23.77 | 30377154 | |
| 431 | Phosphorylation | LPNGLLNSSSNSKEI CCCCCCCCCCCCCCC | 34.80 | 30377154 | |
| 432 | Phosphorylation | PNGLLNSSSNSKEIT CCCCCCCCCCCCCCH | 32.25 | 30377154 | |
| 435 | Phosphorylation | LLNSSSNSKEITAQS CCCCCCCCCCCHHHH | 33.35 | 30377154 |
| 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 GGA1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GGA1_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 GGA1_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-185; SER-350; SER-355;SER-372; SER-374; SER-375; SER-378; THR-384; SER-394; SER-396 ANDSER-397, 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-375 AND SER-378, ANDMASS 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 THR-348; SER-357 ANDSER-378, AND MASS SPECTROMETRY. | |