UniProt ID | TUS1_YEAST | |
---|---|---|
UniProt AC | Q06412 | |
Protein Name | Rho1 guanine nucleotide exchange factor TUS1 | |
Gene Name | TUS1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1307 | |
Subcellular Localization | ||
Protein Description | Guanine nucleotide-exchange factor (GEF) for RHO1 that stimulates the exchange of RHO1 GDP-bound form into GTP-bound form. Required for signaling of cell wall defects to RHO1.. | |
Protein Sequence | MYRYNRSSPFERTPEKRVSRQESQRKSIELPKLPPLNTRNSFLDDSDNGTDNISIGWTPISDTQQFQSPVPQAFTFTSKHSARGNGTSSSESTPKSTKYVKERRPPPPPPLLYSTESIRIDSPMVSPSSQSRERSPNKLSFIGNSEERHHMEYISNHSRILKSPFANGFSPNSPKSPRDSSKQQAHFSDESDLRCHEREKALPPIPFTTTLLLSPFDDEDSEFFTKPPPPLSTSRNVSGNSRVSEALESVYSDSDYTFNNSNARQSSFNSLLGAKPLELAPSITAPTQPFSIQSIDEHKLYQCDNVYKLSAIYEWILKVYFEWFNECVFTKIDLFQIVQLLLEFQMPTNFDQDTIDSNVDNIMASFISQKAVRFDIINDEEVAVVVGGLDITGVFTELLPCYSFIDNTYGSTNSLICYSNVCTHGQSSGFRKEIKLSEIINKSVGLWTEYWHLTPDDLAEINPREVQRQSFIFDLIILEERSLNMATAAVEIYGKRFDKSLLPDEPEFKALAFDIFEPLIQLHTEFLLTPIFWKLKTRGKFIDGVGKIYSKWCGEAKNIYLNYAKAMATVHEIIMWEKKNKTKFVTWLKEIDNSVEITRSKMYHDVIFFGGFFKSLQNMPVTLRSILKNTDPSMEDYEYLKIVIKEVEKLNFEVNQVHGLAIDHRKLVRFSKQLVLSTNSSNATSYVNVGGSTNANDDDAIQDKLALGLTYPERKLVLSGTVYKKRDLWLDPTPVYIALLDNCLLITEEISKGETQKYKLIERPIPIDYLSLEKRKIPGTSKQPLRNYSQKEHKSPMHNFSTPINSMRPLLKSSGNHMSTAYGDRKTSNTEISNANPNTDEFSFKIRNTATGESFKFFTESAEVLNQWIDAIMESFKRNAENHDLNAFEFTVLSSEFAYFDKDAPVNLPVAPEGSEIDVALKAYAQKANKDSCSWSKTTRILCCEDVKFEGRIYLFVATTDGIYVKYRDDYGSGFVKILELNDVKRMEANVKLGLLFVLDNRKLCYFNISTVVSRYLAQGNTLDENCIVGTVIRDKVRFFKIADDFGNSKHLFFERKGKIVILTPEFDQLTNQVKYFKFYKEYKLPSSSNNILNNEIEDIAIFRKSFAVCTKKTVILYQDSFEDNGIVLPSFLNDKDMMAHLRHPHLNSLPFKSATDSKKRPSIESLTEEAKKDIATCKAIPVNFFQISQSSFFALVYDEAVVKINCYGEMSDWRKDILLLDFCCTGASFHGNHLILVGDNLIQIYDLKNVEQNLGELVPVQIIKGKKIKLASSERREKTILVLSHPNILNRQLLVACNPVAMADHQ | |
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 | -MYRYNRSSPFERTP -CCCCCCCCCCCCCH | 38.43 | 22369663 | |
8 | Phosphorylation | MYRYNRSSPFERTPE CCCCCCCCCCCCCHH | 30.30 | 22369663 | |
13 | Phosphorylation | RSSPFERTPEKRVSR CCCCCCCCHHHCCCH | 28.71 | 22369663 | |
23 | Phosphorylation | KRVSRQESQRKSIEL HCCCHHHHHHCCCCC | 27.26 | 28889911 | |
27 | Phosphorylation | RQESQRKSIELPKLP HHHHHHCCCCCCCCC | 24.39 | 22369663 | |
88 | Phosphorylation | SARGNGTSSSESTPK CCCCCCCCCCCCCCC | 33.01 | 28889911 | |
122 | Phosphorylation | TESIRIDSPMVSPSS CCEEEECCCCCCCCC | 16.72 | 28889911 | |
126 | Phosphorylation | RIDSPMVSPSSQSRE EECCCCCCCCCCCCC | 16.89 | 25752575 | |
128 | Phosphorylation | DSPMVSPSSQSRERS CCCCCCCCCCCCCCC | 33.24 | 23749301 | |
129 | Phosphorylation | SPMVSPSSQSRERSP CCCCCCCCCCCCCCC | 35.24 | 17563356 | |
131 | Phosphorylation | MVSPSSQSRERSPNK CCCCCCCCCCCCCCC | 37.75 | 28889911 | |
135 | Phosphorylation | SSQSRERSPNKLSFI CCCCCCCCCCCCCCC | 28.24 | 28889911 | |
163 | Phosphorylation | NHSRILKSPFANGFS HHHHHHCCCCCCCCC | 23.08 | 22369663 | |
170 | Phosphorylation | SPFANGFSPNSPKSP CCCCCCCCCCCCCCC | 25.27 | 22369663 | |
173 | Phosphorylation | ANGFSPNSPKSPRDS CCCCCCCCCCCCCCC | 36.77 | 22369663 | |
176 | Phosphorylation | FSPNSPKSPRDSSKQ CCCCCCCCCCCCCHH | 28.66 | 22369663 | |
180 | Phosphorylation | SPKSPRDSSKQQAHF CCCCCCCCCHHHHCC | 40.49 | 24961812 | |
181 | Phosphorylation | PKSPRDSSKQQAHFS CCCCCCCCHHHHCCC | 38.48 | 21440633 | |
267 | Phosphorylation | NSNARQSSFNSLLGA CCCCCHHHHHHHHCC | 21.80 | 30377154 | |
270 | Phosphorylation | ARQSSFNSLLGAKPL CCHHHHHHHHCCCCC | 23.98 | 30377154 | |
282 | Phosphorylation | KPLELAPSITAPTQP CCCCCCCCCCCCCCC | 27.28 | 21551504 | |
284 | Phosphorylation | LELAPSITAPTQPFS CCCCCCCCCCCCCCC | 30.81 | 21551504 | |
569 | Phosphorylation | NYAKAMATVHEIIMW HHHHHHHHHHHHHHH | 14.87 | 30377154 | |
774 | Acetylation | IDYLSLEKRKIPGTS CCEEECCCCCCCCCC | 65.37 | 24489116 | |
795 | Phosphorylation | YSQKEHKSPMHNFST CCHHCCCCCCCCCCC | 29.39 | 19823750 | |
801 | Phosphorylation | KSPMHNFSTPINSMR CCCCCCCCCCHHHHH | 38.29 | 19823750 | |
802 | Phosphorylation | SPMHNFSTPINSMRP CCCCCCCCCHHHHHH | 24.85 | 21440633 | |
806 | Phosphorylation | NFSTPINSMRPLLKS CCCCCHHHHHHHHHC | 19.52 | 19823750 | |
813 | Phosphorylation | SMRPLLKSSGNHMST HHHHHHHCCCCCCHH | 43.37 | 19823750 | |
814 | Phosphorylation | MRPLLKSSGNHMSTA HHHHHHCCCCCCHHH | 41.86 | 19823750 | |
819 | Phosphorylation | KSSGNHMSTAYGDRK HCCCCCCHHHCCCCC | 11.44 | 19823750 | |
820 | Phosphorylation | SSGNHMSTAYGDRKT CCCCCCHHHCCCCCC | 19.14 | 19823750 | |
822 | Phosphorylation | GNHMSTAYGDRKTSN CCCCHHHCCCCCCCC | 21.46 | 19823750 | |
828 | Phosphorylation | AYGDRKTSNTEISNA HCCCCCCCCCCCCCC | 44.80 | 28889911 | |
967 | Phosphorylation | TDGIYVKYRDDYGSG CCCEEEEEECCCCCC | 14.83 | 19779198 | |
971 | Phosphorylation | YVKYRDDYGSGFVKI EEEEECCCCCCEEEE | 19.92 | 19779198 | |
1149 | Phosphorylation | LRHPHLNSLPFKSAT HCCCCHHCCCCCCCC | 43.72 | 28889911 | |
1156 | Phosphorylation | SLPFKSATDSKKRPS CCCCCCCCCCCCCCC | 48.15 | 28889911 | |
1163 | Phosphorylation | TDSKKRPSIESLTEE CCCCCCCCHHHHCHH | 42.92 | 27017623 | |
1168 | Phosphorylation | RPSIESLTEEAKKDI CCCHHHHCHHHHHHH | 40.85 | 27017623 |
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 TUS1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TUS1_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 TUS1_YEAST !! |
Kegg Drug | ||||||
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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-170; SER-173 ANDSER-176, 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-129, AND MASSSPECTROMETRY. |