UniProt ID | KGUA_YEAST | |
---|---|---|
UniProt AC | P15454 | |
Protein Name | Guanylate kinase | |
Gene Name | GUK1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 187 | |
Subcellular Localization | ||
Protein Description | Essential for recycling GMP and indirectly, cGMP.. | |
Protein Sequence | MSRPIVISGPSGTGKSTLLKKLFAEYPDSFGFSVSSTTRTPRAGEVNGKDYNFVSVDEFKSMIKNNEFIEWAQFSGNYYGSTVASVKQVSKSGKTCILDIDMQGVKSVKAIPELNARFLFIAPPSVEDLKKRLEGRGTETEESINKRLSAAQAELAYAETGAHDKVIVNDDLDKAYKELKDFIFAEK | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MSRPIVISG ------CCCCEEEEC | 46.92 | 1314905 | |
2 | Phosphorylation | ------MSRPIVISG ------CCCCEEEEC | 46.92 | 27717283 | |
8 | Phosphorylation | MSRPIVISGPSGTGK CCCCEEEECCCCCCH | 33.48 | 27717283 | |
11 | Phosphorylation | PIVISGPSGTGKSTL CEEEECCCCCCHHHH | 53.14 | 27717283 | |
13 | Phosphorylation | VISGPSGTGKSTLLK EEECCCCCCHHHHHH | 45.86 | 27717283 | |
15 | Acetylation | SGPSGTGKSTLLKKL ECCCCCCHHHHHHHH | 39.85 | 24489116 | |
21 | Ubiquitination | GKSTLLKKLFAEYPD CHHHHHHHHHHHCCC | 49.13 | 23749301 | |
29 | Phosphorylation | LFAEYPDSFGFSVSS HHHHCCCCCCEECCC | 23.82 | 22369663 | |
33 | Phosphorylation | YPDSFGFSVSSTTRT CCCCCCEECCCCCCC | 22.82 | 22369663 | |
35 | Phosphorylation | DSFGFSVSSTTRTPR CCCCEECCCCCCCCC | 22.29 | 22369663 | |
36 | Phosphorylation | SFGFSVSSTTRTPRA CCCEECCCCCCCCCC | 31.48 | 22369663 | |
37 | Phosphorylation | FGFSVSSTTRTPRAG CCEECCCCCCCCCCE | 16.88 | 22369663 | |
38 | Phosphorylation | GFSVSSTTRTPRAGE CEECCCCCCCCCCEE | 34.20 | 22369663 | |
40 | Phosphorylation | SVSSTTRTPRAGEVN ECCCCCCCCCCEEEC | 18.29 | 22369663 | |
49 | Succinylation | RAGEVNGKDYNFVSV CCEEECCCCCCEEEH | 52.41 | 23954790 | |
49 | Acetylation | RAGEVNGKDYNFVSV CCEEECCCCCCEEEH | 52.41 | 24489116 | |
60 | Acetylation | FVSVDEFKSMIKNNE EEEHHHHHHHHHCCC | 36.75 | 24489116 | |
92 | Phosphorylation | SVKQVSKSGKTCILD EEEEECCCCCEEEEE | 37.71 | 19823750 | |
95 | Phosphorylation | QVSKSGKTCILDIDM EECCCCCEEEEEEEC | 14.33 | 19823750 | |
106 | Ubiquitination | DIDMQGVKSVKAIPE EEECCCCCEEEECHH | 57.25 | 22817900 | |
107 | Phosphorylation | IDMQGVKSVKAIPEL EECCCCCEEEECHHH | 26.83 | 19823750 | |
109 | Ubiquitination | MQGVKSVKAIPELNA CCCCCEEEECHHHCE | 47.92 | 22817900 | |
125 | Phosphorylation | FLFIAPPSVEDLKKR EEEECCCCHHHHHHH | 36.76 | 22369663 | |
130 | Succinylation | PPSVEDLKKRLEGRG CCCHHHHHHHHCCCC | 48.44 | 23954790 | |
130 | Acetylation | PPSVEDLKKRLEGRG CCCHHHHHHHHCCCC | 48.44 | 24489116 | |
146 | Ubiquitination | ETEESINKRLSAAQA CCHHHHHHHHHHHHH | 53.71 | 23749301 | |
146 | Acetylation | ETEESINKRLSAAQA CCHHHHHHHHHHHHH | 53.71 | 22865919 | |
149 | Phosphorylation | ESINKRLSAAQAELA HHHHHHHHHHHHHHH | 26.12 | 22369663 | |
157 | Phosphorylation | AAQAELAYAETGAHD HHHHHHHHHHHCCCC | 20.00 | 22890988 | |
160 | Phosphorylation | AELAYAETGAHDKVI HHHHHHHHCCCCEEE | 31.34 | 22890988 | |
165 | Acetylation | AETGAHDKVIVNDDL HHHCCCCEEEECCCH | 24.80 | 24489116 | |
174 | 2-Hydroxyisobutyrylation | IVNDDLDKAYKELKD EECCCHHHHHHHHHH | 62.00 | - | |
174 | Acetylation | IVNDDLDKAYKELKD EECCCHHHHHHHHHH | 62.00 | 24489116 | |
174 | Succinylation | IVNDDLDKAYKELKD EECCCHHHHHHHHHH | 62.00 | 23954790 | |
176 | Phosphorylation | NDDLDKAYKELKDFI CCCHHHHHHHHHHHH | 15.67 | 25005228 | |
177 | Acetylation | DDLDKAYKELKDFIF CCHHHHHHHHHHHHH | 62.52 | 24489116 | |
180 | Acetylation | DKAYKELKDFIFAEK HHHHHHHHHHHHCCC | 52.24 | 24489116 | |
180 | Succinylation | DKAYKELKDFIFAEK HHHHHHHHHHHHCCC | 52.24 | 23954790 |
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 KGUA_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KGUA_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 KGUA_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Refined structure of the complex between guanylate kinase and itssubstrate GMP at 2.0-A resolution."; Stehle T., Schulz G.E.; J. Mol. Biol. 224:1127-1141(1992). Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). | |
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-149, AND MASSSPECTROMETRY. | |
"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-149, AND MASSSPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASSSPECTROMETRY. | |
"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-149, AND MASSSPECTROMETRY. |