UniProt ID | RGA1_YEAST | |
---|---|---|
UniProt AC | P39083 | |
Protein Name | Rho-type GTPase-activating protein 1 | |
Gene Name | RGA1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1007 | |
Subcellular Localization | ||
Protein Description | GTPase-activating protein (GAP) for CDC42 and/or RHO1. Negative regulator of the pheromone-response pathway through the STE20 protein kinase; acts at a step between the G-protein and the MAP kinase module. Dominant suppressor of bud emergence defect caused by deletion of IPL2/BEM2. Involved in the control of polarized cell growth and proper bud site selection.. | |
Protein Sequence | MASTAPNEQFPSCVRCKEFITTGHAYELGCDRWHTHCFACYKCEKPLSCESDFLVLGTGALICFDCSDSCKNCGKKIDDLAIILSSSNEAYCSDCFKCCKCGENIADLRYAKTKRGLFCLSCHEKLLAKRKYYEEKKRRLKKNLPSLPTPVIDNGHTDEVSASAVLPEKTFSRPASLVNEIPSGSEPSKDIETNSSDIVPHFITGYNDSDDNSGSSKFGSNVSIDVIGPEENSTEHVNDDVKEEAEAPSANMSLNVATDPTLSCKEPPSHSRNLLNKTPLRNSSGQYLAKSPSSYRQGIIVNDSLEESDQIDPPNNSSRNASELLTSVLHSPVSVNMKNPKGSNTDIFNTGEISQMDPSLSRKVLNNIVEETNALQRPVVEVVKEDRSVPDLAGVQQEQAEKYSYSNNSGKGRKISRSLSRRSKDLMINLKSRATGKQDSNVKLSPASKVTSRRSQDLMRDNDSHTGLDTPNSNSTSLDILVNNQKSLNYKRFTDNGTLRVTSGKETALEEQKNHSFKSPSPIDHLLQSPATPSNVSMYRTPPLDSSLTFDRRNGSSYSNQNYSIPSWQKTPKTQLENSDNFEEQKETLYENSESRNDPSLDKEIVTAEHYLKQLKINLKELESQREELMKEITEMKSMKEALRRHIESYNSEKNKLYLDSNELSNNPPMINEISLGESPPVKHVATASSVARSSVKPKFWKFFSSAKPQTEQSIQGVSTNNTNSIVKSAPVLLSAPSSGSNSGRLEISPPVLQNPNEFSDVRLVPIENDANMGQSKDGEEYLDGSNLYGSSLVARCNYENNEIPMILSVCIDFIESDEENMRSEGIYRKSGSQLVIEEIEKQFSAWKVQQNTETPNILTEQDLNVVTGVLKRYLRKLPNPIFTFQIYEPLMRLVKSKKMMENLPFVGGKLSLEAKNSDTYMSSKSALKNILEDLPREHYRVLRVLSEHIEKVTRYSHWNRMTLYNLALVFAPGLIRDFSGEKDIIDMKERNYIVAFIFGNYKDILT | |
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 |
---|---|---|---|---|---|
3 | Phosphorylation | -----MASTAPNEQF -----CCCCCCCCCC | 36.64 | 30377154 | |
12 | Phosphorylation | APNEQFPSCVRCKEF CCCCCCCCCCCCCCE | 26.91 | 30377154 | |
146 | Phosphorylation | RLKKNLPSLPTPVID HHHHHCCCCCCCCCC | 50.58 | 24961812 | |
149 | Phosphorylation | KNLPSLPTPVIDNGH HHCCCCCCCCCCCCC | 35.17 | 21440633 | |
161 | Phosphorylation | NGHTDEVSASAVLPE CCCCCCCCHHHCCCC | 17.92 | 21440633 | |
170 | Phosphorylation | SAVLPEKTFSRPASL HHCCCCCCCCCCHHH | 25.77 | 22890988 | |
172 | Phosphorylation | VLPEKTFSRPASLVN CCCCCCCCCCHHHHC | 42.45 | 22369663 | |
176 | Phosphorylation | KTFSRPASLVNEIPS CCCCCCHHHHCCCCC | 35.22 | 22369663 | |
183 | Phosphorylation | SLVNEIPSGSEPSKD HHHCCCCCCCCCCCC | 61.69 | 22890988 | |
185 | Phosphorylation | VNEIPSGSEPSKDIE HCCCCCCCCCCCCCC | 51.15 | 22890988 | |
188 | Phosphorylation | IPSGSEPSKDIETNS CCCCCCCCCCCCCCC | 38.62 | 22890988 | |
209 | Phosphorylation | FITGYNDSDDNSGSS HHCCCCCCCCCCCCC | 43.13 | 20377248 | |
213 | Phosphorylation | YNDSDDNSGSSKFGS CCCCCCCCCCCCCCC | 47.23 | 21551504 | |
216 | Phosphorylation | SDDNSGSSKFGSNVS CCCCCCCCCCCCCEE | 35.21 | 21551504 | |
220 | Phosphorylation | SGSSKFGSNVSIDVI CCCCCCCCCEEEEEE | 36.87 | 28889911 | |
223 | Phosphorylation | SKFGSNVSIDVIGPE CCCCCCEEEEEECCC | 19.81 | 27717283 | |
234 | Phosphorylation | IGPEENSTEHVNDDV ECCCCCCCCCCCHHH | 41.51 | 28889911 | |
278 | Phosphorylation | SRNLLNKTPLRNSSG CCCCCCCCCCCCCCC | 26.87 | 17330950 | |
283 | Phosphorylation | NKTPLRNSSGQYLAK CCCCCCCCCCCEECC | 29.43 | 21440633 | |
284 | Phosphorylation | KTPLRNSSGQYLAKS CCCCCCCCCCEECCC | 33.20 | 21440633 | |
287 | Phosphorylation | LRNSSGQYLAKSPSS CCCCCCCEECCCCCC | 16.50 | 21440633 | |
291 | Phosphorylation | SGQYLAKSPSSYRQG CCCEECCCCCCCCCC | 25.14 | 25752575 | |
322 | Phosphorylation | NNSSRNASELLTSVL CCCCCCHHHHHHHHH | 32.12 | 15665377 | |
326 | Phosphorylation | RNASELLTSVLHSPV CCHHHHHHHHHCCCC | 29.43 | 22369663 | |
327 | Phosphorylation | NASELLTSVLHSPVS CHHHHHHHHHCCCCE | 23.74 | 22369663 | |
331 | Phosphorylation | LLTSVLHSPVSVNMK HHHHHHCCCCEECCC | 23.88 | 22369663 | |
334 | Phosphorylation | SVLHSPVSVNMKNPK HHHCCCCEECCCCCC | 15.91 | 22369663 | |
337 | Oxidation | HSPVSVNMKNPKGSN CCCCEECCCCCCCCC | 4.09 | 15665377 | |
343 | Phosphorylation | NMKNPKGSNTDIFNT CCCCCCCCCCCCCCC | 42.56 | 21440633 | |
345 | Phosphorylation | KNPKGSNTDIFNTGE CCCCCCCCCCCCCCH | 31.97 | 21551504 | |
350 | Phosphorylation | SNTDIFNTGEISQMD CCCCCCCCCHHHHCC | 25.99 | 27017623 | |
359 | Phosphorylation | EISQMDPSLSRKVLN HHHHCCHHHCHHHHH | 34.41 | 21551504 | |
361 | Phosphorylation | SQMDPSLSRKVLNNI HHCCHHHCHHHHHHH | 34.10 | 27017623 | |
372 | Phosphorylation | LNNIVEETNALQRPV HHHHHHHHCCCCCCE | 16.58 | 24961812 | |
388 | Phosphorylation | EVVKEDRSVPDLAGV EHHCCCCCCCCCCCC | 50.77 | 22369663 | |
406 | Phosphorylation | QAEKYSYSNNSGKGR HHHHHCCCCCCCCCH | 24.48 | 28889911 | |
423 | Phosphorylation | SRSLSRRSKDLMINL HHHHHHHCHHEEHEE | 29.43 | 25704821 | |
440 | Phosphorylation | RATGKQDSNVKLSPA CCCCCCCCCCCCCCH | 40.82 | 22369663 | |
445 | Phosphorylation | QDSNVKLSPASKVTS CCCCCCCCCHHHHCC | 16.83 | 22369663 | |
448 | Phosphorylation | NVKLSPASKVTSRRS CCCCCCHHHHCCHHH | 30.92 | 22369663 | |
455 | Phosphorylation | SKVTSRRSQDLMRDN HHHCCHHHHHHCCCC | 27.25 | 25704821 | |
464 | Phosphorylation | DLMRDNDSHTGLDTP HHCCCCCCCCCCCCC | 29.24 | 21551504 | |
470 | Phosphorylation | DSHTGLDTPNSNSTS CCCCCCCCCCCCCCC | 29.43 | 23749301 | |
473 | Phosphorylation | TGLDTPNSNSTSLDI CCCCCCCCCCCCEEE | 33.10 | 21440633 | |
476 | Phosphorylation | DTPNSNSTSLDILVN CCCCCCCCCEEEEEC | 37.24 | 28889911 | |
494 | Phosphorylation | SLNYKRFTDNGTLRV CCCCEEECCCCEEEE | 32.37 | 25704821 | |
503 | Phosphorylation | NGTLRVTSGKETALE CCEEEECCCCHHHHH | 45.04 | 28889911 | |
519 | Phosphorylation | QKNHSFKSPSPIDHL HHCCCCCCCCHHHHH | 28.71 | 22369663 | |
521 | Phosphorylation | NHSFKSPSPIDHLLQ CCCCCCCCHHHHHHC | 41.39 | 22369663 | |
529 | Phosphorylation | PIDHLLQSPATPSNV HHHHHHCCCCCCCCC | 19.24 | 23749301 | |
532 | Phosphorylation | HLLQSPATPSNVSMY HHHCCCCCCCCCEEC | 30.54 | 23749301 | |
537 | Phosphorylation | PATPSNVSMYRTPPL CCCCCCCEECCCCCC | 17.85 | 19779198 | |
541 | Phosphorylation | SNVSMYRTPPLDSSL CCCEECCCCCCCCCC | 16.27 | 28889911 | |
558 | Phosphorylation | DRRNGSSYSNQNYSI ECCCCCCCCCCCCCC | 17.21 | 23749301 | |
564 | Phosphorylation | SYSNQNYSIPSWQKT CCCCCCCCCCCCCCC | 35.26 | 21440633 | |
567 | Phosphorylation | NQNYSIPSWQKTPKT CCCCCCCCCCCCCCH | 40.23 | 21440633 | |
571 | Phosphorylation | SIPSWQKTPKTQLEN CCCCCCCCCCHHHCC | 18.21 | 23749301 | |
574 | Phosphorylation | SWQKTPKTQLENSDN CCCCCCCHHHCCCCC | 39.32 | 21551504 | |
579 | Phosphorylation | PKTQLENSDNFEEQK CCHHHCCCCCHHHHH | 25.26 | 23749301 | |
593 | Phosphorylation | KETLYENSESRNDPS HHHHHHCCCCCCCCC | 25.63 | 20377248 | |
595 | Phosphorylation | TLYENSESRNDPSLD HHHHCCCCCCCCCCC | 35.88 | 21440633 | |
600 | Phosphorylation | SESRNDPSLDKEIVT CCCCCCCCCCHHHHH | 52.65 | 24961812 | |
679 | Phosphorylation | NEISLGESPPVKHVA CEEECCCCCCCCCEE | 32.48 | 28152593 | |
738 | Phosphorylation | PVLLSAPSSGSNSGR CEEEECCCCCCCCCC | 47.23 | 27017623 | |
741 | Phosphorylation | LSAPSSGSNSGRLEI EECCCCCCCCCCCEE | 29.75 | 27214570 | |
743 | Phosphorylation | APSSGSNSGRLEISP CCCCCCCCCCCEECC | 27.30 | 23749301 | |
749 | Phosphorylation | NSGRLEISPPVLQNP CCCCCEECCCCCCCC | 17.49 | 25752575 | |
912 | Phosphorylation | PFVGGKLSLEAKNSD CCCCCEEEEEECCCC | 27.87 | 28889911 | |
921 | Phosphorylation | EAKNSDTYMSSKSAL EECCCCCCCCCHHHH | 10.45 | 28889911 |
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 RGA1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RGA1_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 RGA1_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-278; SER-388; SER-519;SER-521 AND SER-741, AND MASS SPECTROMETRY. | |
"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-322, 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 THR-278, AND MASSSPECTROMETRY. |