| UniProt ID | MOT1_YEAST | |
|---|---|---|
| UniProt AC | P32333 | |
| Protein Name | TATA-binding protein-associated factor MOT1 | |
| Gene Name | MOT1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1867 | |
| Subcellular Localization | Mitochondrion. Nucleus. Localized on chromatin. Specifically localized to the promoters of the genes it regulates. | |
| Protein Description | Regulates transcription in association with TATA binding protein (TBP). Removes TBP from the TATA box via its C-terminal ATPase activity. Both transcription activation and repression require its ATPase activity.. | |
| Protein Sequence | MTSRVSRLDRQVILIETGSTQVVRNMAADQMGDLAKQHPEDILSLLSRVYPFLLVKKWETRVTAARAVGGIVAHAPSWDPNESDLVGGTNEGSPLDNAQVKLEHEMKIKLEEATQNNQLNLLQEDHHLSSLSDWKLNEILKSGKVLLASSMNDYNVLGKADDNIRKQAKTDDIKQETSMLNASDKANENKSNANKKSARMLAMARRKKKMSAKNTPKHPVDITESSVSKTLLNGKNMTNSAASLATSPTSNQLNPKLEITEQADESKLMIESTVRPLLEQHEIVAGLVWQFQGIYELLLDNLMSENWEIRHGAALGLRELVKKHAYGVSRVKGNTREENNLRNSRSLEDLASRLLTVFALDRFGDYVYDTVVAPVRESVAQTLAALLIHLDSTLSIKIFNCLEQLVLQDPLQTGLPNKIWEATHGGLLGIRYFVSIKTNFLFAHGLLENVVRIVLYGLNQSDDDVQSVAASILTPITSEFVKLNNSTIEILVTTIWSLLARLDDDISSSVGSIMDLLAKLCDHQEVLDILKNKALEHPSEWSFKSLVPKLYPFLRHSISSVRRAVLNLLIAFLSIKDDSTKNWLNGKVFRLVFQNILLEQNPELLQLSFDVYVALLEHYKVKHTEKTLDHVFSKHLQPILHLLNTPVGEKGKNYAMESQYILKPSQHYQLHPEKKRSISETTTDSDIPIPKNNEHINIDAPMIAGDITLLGLDVILNTRIMGAKAFALTLSMFQDSTLQSFFTNVLVRCLELPFSTPRMLAGIIVSQFCSSWLQKHPEGEKLPSFVSEIFSPVMNKQLLNRDEFPVFRELVPSLKALRTQCQSLLATFVDVGMLPQYKLPNVAIVVQGETEAGPHAFGVETAEKVYGEYYDKMFKSMNNSYKLLAKKPLEDSKHRVLMAINSAKESAKLRTGSILANYASSILLFDGLPLKLNPIIRSLMDSVKEERNEKLQTMAGESVVHLIQQLLENNKVNVSGKIVKNLCGFLCVDTSEVPDFSVNAEYKEKILTLIKESNSIAAQDDINLAKMSEEAQLKRKGGLITLKILFEVLGPSILQKLPQLRSILFDSLSDHENEEASKVDNEQGQKIVDSFGVLRALFPFMSDSLRSSEVFTRFPVLLTFLRSNLSVFRYSAARTFADLAKISSVEVMAYTIREILPLMNSAGSLSDRQGSTELIYHLSLSMETDVLPYVIFLIVPLLGRMSDSNEDVRNLATTTFASIIKLVPLEAGIADPKGLPEELVASRERERDFIQQMMDPSKAKPFKLPIAIKATLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASDQYLRKEDYEKTRSVESRALPSLIICPPSLTGHWENEFDQYAPFLKVVVYAGGPTVRLTLRPQLSDADIIVTSYDVARNDLAVLNKTEYNYCVLDEGHIIKNSQSKLAKAVKEITANHRLILTGTPIQNNVLELWSLFDFLMPGFLGTEKMFQERFAKPIAASRNSKTSSKEQEAGVLALEALHKQVLPFMLRRLKEDVLSDLPPKIIQDYYCELGDLQKQLYMDFTKKQKNVVEKDIENSEIADGKQHIFQALQYMRKLCNHPALVLSPNHPQLAQVQDYLKQTGLDLHDIINAPKLSALRTLLFECGIGEEDIDKKASQDQNFPIQNVISQHRALIFCQLKDMLDMVENDLFKKYMPSVTYMRLDGSIDPRDRQKVVRKFNEDPSIDCLLLTTKVGGLGLNLTGADTVIFVEHDWNPMNDLQAMDRAHRIGQKKVVNVYRIITKGTLEEKIMGLQKFKMNIASTVVNQQNSGLASMDTHQLLDLFDPDNVTSQDNEEKNNGDSQAAKGMEDIANETGLTGKAKEALGELKELWDPSQYEEEYNLDTFIKTLR | |
| 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 |
|---|---|---|---|---|---|
| 6 | Phosphorylation | --MTSRVSRLDRQVI --CCCCHHHHCCEEE | 26.47 | 25533186 | |
| 89 | Phosphorylation | ESDLVGGTNEGSPLD CCCCCCCCCCCCCCC | 24.94 | 28889911 | |
| 93 | Phosphorylation | VGGTNEGSPLDNAQV CCCCCCCCCCCCHHH | 18.99 | 23749301 | |
| 101 | Sumoylation | PLDNAQVKLEHEMKI CCCCHHHHHHHHHHH | 35.76 | - | |
| 109 | Sumoylation | LEHEMKIKLEEATQN HHHHHHHCHHHHHHH | 44.31 | - | |
| 141 | Ubiquitination | WKLNEILKSGKVLLA HHHHHHHHHCCEEEE | 63.92 | 23749301 | |
| 159 | Acetylation | NDYNVLGKADDNIRK CCCCCCCCCCHHHHH | 44.47 | 22865919 | |
| 177 | Phosphorylation | TDDIKQETSMLNASD HCCHHHHHHHCCHHH | 19.55 | 24961812 | |
| 178 | Phosphorylation | DDIKQETSMLNASDK CCHHHHHHHCCHHHH | 22.11 | 24961812 | |
| 183 | Phosphorylation | ETSMLNASDKANENK HHHHCCHHHHHHHCC | 38.27 | 24961812 | |
| 213 | Acetylation | RKKKMSAKNTPKHPV HHHHCCCCCCCCCCC | 54.79 | 25381059 | |
| 223 | Phosphorylation | PKHPVDITESSVSKT CCCCCCCCCCHHHHH | 25.92 | 29688323 | |
| 225 | Phosphorylation | HPVDITESSVSKTLL CCCCCCCCHHHHHHH | 27.65 | 29688323 | |
| 226 | Phosphorylation | PVDITESSVSKTLLN CCCCCCCHHHHHHHC | 24.95 | 21440633 | |
| 228 | Phosphorylation | DITESSVSKTLLNGK CCCCCHHHHHHHCCC | 23.13 | 29688323 | |
| 229 | Acetylation | ITESSVSKTLLNGKN CCCCHHHHHHHCCCC | 40.82 | 24489116 | |
| 238 | Phosphorylation | LLNGKNMTNSAASLA HHCCCCCCCCHHHHH | 35.10 | 19823750 | |
| 240 | Phosphorylation | NGKNMTNSAASLATS CCCCCCCCHHHHHCC | 18.95 | 19823750 | |
| 243 | Phosphorylation | NMTNSAASLATSPTS CCCCCHHHHHCCCCC | 20.46 | 23749301 | |
| 246 | Phosphorylation | NSAASLATSPTSNQL CCHHHHHCCCCCCCC | 40.30 | 21440633 | |
| 247 | Phosphorylation | SAASLATSPTSNQLN CHHHHHCCCCCCCCC | 22.15 | 25521595 | |
| 249 | Phosphorylation | ASLATSPTSNQLNPK HHHHCCCCCCCCCCC | 39.82 | 23749301 | |
| 250 | Phosphorylation | SLATSPTSNQLNPKL HHHCCCCCCCCCCCE | 26.43 | 28889911 | |
| 346 | Phosphorylation | NNLRNSRSLEDLASR HCCCCCCCHHHHHHH | 35.61 | 30377154 | |
| 509 | Phosphorylation | LDDDISSSVGSIMDL CCCHHHHHHHHHHHH | 24.57 | 23749301 | |
| 512 | Phosphorylation | DISSSVGSIMDLLAK HHHHHHHHHHHHHHH | 16.75 | 23749301 | |
| 519 | Ubiquitination | SIMDLLAKLCDHQEV HHHHHHHHHCCHHHH | 50.01 | 23749301 | |
| 677 | Phosphorylation | LHPEKKRSISETTTD CCHHHCCCCCCCCCC | 39.07 | 17330950 | |
| 679 | Phosphorylation | PEKKRSISETTTDSD HHHCCCCCCCCCCCC | 30.09 | 19823750 | |
| 681 | Phosphorylation | KKRSISETTTDSDIP HCCCCCCCCCCCCCC | 28.36 | 27214570 | |
| 682 | Phosphorylation | KRSISETTTDSDIPI CCCCCCCCCCCCCCC | 25.26 | 27214570 | |
| 683 | Phosphorylation | RSISETTTDSDIPIP CCCCCCCCCCCCCCC | 40.71 | 28152593 | |
| 685 | Phosphorylation | ISETTTDSDIPIPKN CCCCCCCCCCCCCCC | 35.03 | 27214570 | |
| 784 | Phosphorylation | PEGEKLPSFVSEIFS CCCCCCCHHHHHHHH | 49.03 | 28889911 | |
| 787 | Phosphorylation | EKLPSFVSEIFSPVM CCCCHHHHHHHHHHH | 23.98 | 28889911 | |
| 791 | Phosphorylation | SFVSEIFSPVMNKQL HHHHHHHHHHHCHHH | 23.42 | 28889911 | |
| 876 | Phosphorylation | YYDKMFKSMNNSYKL HHHHHHHHCCHHHHH | 18.58 | 26447709 | |
| 880 | Phosphorylation | MFKSMNNSYKLLAKK HHHHCCHHHHHHHCC | 20.74 | 26447709 | |
| 881 | Phosphorylation | FKSMNNSYKLLAKKP HHHCCHHHHHHHCCC | 14.05 | 26447709 | |
| 1150 | Phosphorylation | SSVEVMAYTIREILP CCHHHHHHHHHHHHH | 5.65 | 28889911 | |
| 1151 | Phosphorylation | SVEVMAYTIREILPL CHHHHHHHHHHHHHH | 12.20 | 28889911 | |
| 1161 | Phosphorylation | EILPLMNSAGSLSDR HHHHHHHCCCCCCCC | 21.75 | 27214570 | |
| 1616 | Phosphorylation | PKLSALRTLLFECGI HHHHHHHHHHHHCCC | 28.76 | 28152593 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MOT1_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 MOT1_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-247; SER-250; SER-677;SER-679 AND THR-683, AND MASS SPECTROMETRY. | |
| "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-677, 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-677, AND MASSSPECTROMETRY. | |
