UniProt ID | GFA1_YEAST | |
---|---|---|
UniProt AC | P14742 | |
Protein Name | Glutamine--fructose-6-phosphate aminotransferase [isomerizing] | |
Gene Name | GFA1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 717 | |
Subcellular Localization | ||
Protein Description | Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins).. | |
Protein Sequence | MCGIFGYCNYLVERSRGEIIDTLVDGLQRLEYRGYDSTGIAIDGDEADSTFIYKQIGKVSALKEEITKQNPNRDVTFVSHCGIAHTRWATHGRPEQVNCHPQRSDPEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLYLHLYNTNLQNGHDLDFHELTKLVLLELEGSYGLLCKSCHYPNEVIATRKGSPLLIGVKSEKKLKVDFVDVEFPEENAGQPEIPLKSNNKSFGLGPKKAREFEAGSQNANLLPIAANEFNLRHSQSRAFLSEDGSPTPVEFFVSSDAASVVKHTKKVLFLEDDDLAHIYDGELHIHRSRREVGASMTRSIQTLEMELAQIMKGPYDHFMQKEIYEQPESTFNTMRGRIDYENNKVILGGLKAWLPVVRRARRLIMIACGTSYHSCLATRAIFEELSDIPVSVELASDFLDRKCPVFRDDVCVFVSQSGETADTMLALNYCLERGALTVGIVNSVGSSISRVTHCGVHINAGPEIGVASTKAYTSQYIALVMFALSLSDDRVSKIDRRIEIIQGLKLIPGQIKQVLKLEPRIKKLCATELKDQKSLLLLGRGYQFAAALEGALKIKEISYMHSEGVLAGELKHGVLALVDENLPIIAFGTRDSLFPKVVSSIEQVTARKGHPIIICNENDEVWAQKSKSIDLQTLEVPQTVDCLQGLINIIPLQLMSYWLAVNKGIDVDFPRNLAKSVTVE | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
7 | Phosphorylation | -MCGIFGYCNYLVER -CCCCCHHHHHHHHH | 2.69 | 30377154 | |
10 | Phosphorylation | GIFGYCNYLVERSRG CCCHHHHHHHHHCCC | 14.46 | 30377154 | |
15 | Phosphorylation | CNYLVERSRGEIIDT HHHHHHHCCCCHHHH | 31.00 | 30377154 | |
49 | Phosphorylation | IDGDEADSTFIYKQI ECCCCCCCEEEHHHH | 32.06 | 27214570 | |
54 | Ubiquitination | ADSTFIYKQIGKVSA CCCEEEHHHHCCHHH | 30.53 | 17644757 | |
58 | Ubiquitination | FIYKQIGKVSALKEE EEHHHHCCHHHHHHH | 34.35 | 17644757 | |
63 | Ubiquitination | IGKVSALKEEITKQN HCCHHHHHHHHHHHC | 53.68 | 17644757 | |
63 | Acetylation | IGKVSALKEEITKQN HCCHHHHHHHHHHHC | 53.68 | 22865919 | |
63 | Succinylation | IGKVSALKEEITKQN HCCHHHHHHHHHHHC | 53.68 | 23954790 | |
68 | Ubiquitination | ALKEEITKQNPNRDV HHHHHHHHHCCCCCE | 54.46 | 17644757 | |
125 | 2-Hydroxyisobutyrylation | ITNFRELKTLLINKG ECCHHHHHHHHHCCC | 32.16 | - | |
131 | Acetylation | LKTLLINKGYKFESD HHHHHHCCCCCCCCC | 57.53 | 22865919 | |
134 | Ubiquitination | LLINKGYKFESDTDT HHHCCCCCCCCCCCH | 51.85 | 23749301 | |
134 | Acetylation | LLINKGYKFESDTDT HHHCCCCCCCCCCCH | 51.85 | 24489116 | |
146 | Ubiquitination | TDTECIAKLYLHLYN CCHHHHHHHHHHHHH | 20.11 | 17644757 | |
169 | Ubiquitination | LDFHELTKLVLLELE CCHHHHHHHHHHCCC | 49.58 | 17644757 | |
184 | Ubiquitination | GSYGLLCKSCHYPNE CCCEEEEHHCCCCCC | 56.96 | 17644757 | |
197 | Ubiquitination | NEVIATRKGSPLLIG CCEEEECCCCCEEEE | 60.43 | 17644757 | |
199 | Phosphorylation | VIATRKGSPLLIGVK EEEECCCCCEEEEEC | 18.53 | 22369663 | |
206 | Ubiquitination | SPLLIGVKSEKKLKV CCEEEEECCCCCEEE | 47.92 | 17644757 | |
206 | Acetylation | SPLLIGVKSEKKLKV CCEEEEECCCCCEEE | 47.92 | 22865919 | |
209 | Ubiquitination | LIGVKSEKKLKVDFV EEEECCCCCEEECEE | 71.18 | 17644757 | |
210 | Ubiquitination | IGVKSEKKLKVDFVD EEECCCCCEEECEEE | 49.87 | 17644757 | |
212 | Ubiquitination | VKSEKKLKVDFVDVE ECCCCCEEECEEECC | 48.95 | 17644757 | |
233 | Ubiquitination | GQPEIPLKSNNKSFG CCCCCCCCCCCCCCC | 45.87 | 17644757 | |
237 | Ubiquitination | IPLKSNNKSFGLGPK CCCCCCCCCCCCCHH | 51.95 | 23749301 | |
237 | Acetylation | IPLKSNNKSFGLGPK CCCCCCCCCCCCCHH | 51.95 | 25381059 | |
238 | Phosphorylation | PLKSNNKSFGLGPKK CCCCCCCCCCCCHHH | 27.03 | 22369663 | |
245 | Ubiquitination | SFGLGPKKAREFEAG CCCCCHHHHHCCCCC | 56.67 | 17644757 | |
253 | Phosphorylation | AREFEAGSQNANLLP HHCCCCCCCCCCCCC | 27.58 | 22369663 | |
271 | Phosphorylation | NEFNLRHSQSRAFLS CCHHCCCCCCCEEEC | 24.34 | 22369663 | |
273 | Phosphorylation | FNLRHSQSRAFLSED HHCCCCCCCEEECCC | 28.70 | 21440633 | |
278 | Phosphorylation | SQSRAFLSEDGSPTP CCCCEEECCCCCCCC | 27.47 | 22369663 | |
282 | Phosphorylation | AFLSEDGSPTPVEFF EEECCCCCCCCEEEE | 37.61 | 22369663 | |
284 | Phosphorylation | LSEDGSPTPVEFFVS ECCCCCCCCEEEEEC | 41.48 | 22369663 | |
291 | Phosphorylation | TPVEFFVSSDAASVV CCEEEEECCCHHHHH | 19.83 | 22369663 | |
292 | Phosphorylation | PVEFFVSSDAASVVK CEEEEECCCHHHHHH | 26.43 | 22369663 | |
296 | Phosphorylation | FVSSDAASVVKHTKK EECCCHHHHHHHCCE | 29.21 | 22369663 | |
299 | Ubiquitination | SDAASVVKHTKKVLF CCHHHHHHHCCEEEE | 43.32 | 17644757 | |
302 | Ubiquitination | ASVVKHTKKVLFLED HHHHHHCCEEEEECC | 40.37 | 17644757 | |
303 | Ubiquitination | SVVKHTKKVLFLEDD HHHHHCCEEEEECCC | 45.38 | 17644757 | |
332 | Phosphorylation | SRREVGASMTRSIQT CHHHHHCHHHHHHHH | 18.11 | 22369663 | |
334 | Phosphorylation | REVGASMTRSIQTLE HHHHCHHHHHHHHHH | 20.83 | 22369663 | |
336 | Phosphorylation | VGASMTRSIQTLEME HHCHHHHHHHHHHHH | 15.19 | 22369663 | |
339 | Phosphorylation | SMTRSIQTLEMELAQ HHHHHHHHHHHHHHH | 24.02 | 22369663 | |
358 | Ubiquitination | PYDHFMQKEIYEQPE CCHHHHHHHHHHCCH | 34.00 | 17644757 | |
358 | Acetylation | PYDHFMQKEIYEQPE CCHHHHHHHHHHCCH | 34.00 | 24489116 | |
381 | Ubiquitination | RIDYENNKVILGGLK EEECCCCEEEECHHH | 42.08 | 23749301 | |
381 | Acetylation | RIDYENNKVILGGLK EEECCCCEEEECHHH | 42.08 | 24489116 | |
507 | Ubiquitination | EIGVASTKAYTSQYI CCCCCCCHHHHHHHH | 36.58 | 17644757 | |
542 | Acetylation | IEIIQGLKLIPGQIK HHHHHHCCCCCCHHH | 51.71 | 24489116 | |
542 | Ubiquitination | IEIIQGLKLIPGQIK HHHHHHCCCCCCHHH | 51.71 | 15699485 | |
549 | Acetylation | KLIPGQIKQVLKLEP CCCCCHHHHHHHCCH | 26.85 | 24489116 | |
553 | Acetylation | GQIKQVLKLEPRIKK CHHHHHHHCCHHHHH | 52.53 | 22865919 | |
559 | Ubiquitination | LKLEPRIKKLCATEL HHCCHHHHHHHHHHH | 40.76 | 17644757 | |
560 | Ubiquitination | KLEPRIKKLCATELK HCCHHHHHHHHHHHC | 46.56 | 23749301 | |
567 | Ubiquitination | KLCATELKDQKSLLL HHHHHHHCCCHHHHH | 52.46 | 17644757 | |
567 | Acetylation | KLCATELKDQKSLLL HHHHHHHCCCHHHHH | 52.46 | 25381059 | |
570 | Ubiquitination | ATELKDQKSLLLLGR HHHHCCCHHHHHHHC | 53.88 | 17644757 | |
570 | Acetylation | ATELKDQKSLLLLGR HHHHCCCHHHHHHHC | 53.88 | 24489116 | |
608 | Ubiquitination | GVLAGELKHGVLALV CCCCHHCCCCEEEEE | 33.73 | 17644757 | |
633 | Acetylation | TRDSLFPKVVSSIEQ CCHHHCHHHHHCHHH | 48.19 | 24489116 | |
645 | Ubiquitination | IEQVTARKGHPIIIC HHHHHCCCCCCEEEE | 60.14 | 17644757 | |
662 | Ubiquitination | NDEVWAQKSKSIDLQ CCCHHHHCCCCCCCC | 52.70 | 17644757 | |
700 | Ubiquitination | SYWLAVNKGIDVDFP HHHHHHHCCCCCCCC | 51.12 | 15699485 | |
712 | Ubiquitination | DFPRNLAKSVTVE-- CCCCCHHCCCCCC-- | 48.93 | 23749301 | |
713 | Phosphorylation | FPRNLAKSVTVE--- CCCCHHCCCCCC--- | 19.88 | 21440633 |
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 GFA1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GFA1_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 GFA1_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-199; SER-238; SER-253;SER-332 AND THR-334, 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-199, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND MASSSPECTROMETRY. |