UniProt ID | TOR2_YEAST | |
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UniProt AC | P32600 | |
Protein Name | Serine/threonine-protein kinase TOR2 | |
Gene Name | TOR2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 2474 | |
Subcellular Localization |
Cell membrane Peripheral membrane protein Cytoplasmic side . Vacuole membrane Peripheral membrane protein Cytoplasmic side . Also localizes to membranous structures both proximal to, yet distinct from, the plasma membrane as well as within th |
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Protein Description | Phosphatidylinositol 3-kinase homolog, component of both TORC1 and TORC2. TORC1 regulates multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls ribosome biogenesis via control of rRNA, ribosomal protein and tRNA gene expression, and rRNA processing. TORC1 positively controls protein biosynthesis by regulation of mRNA stability, translation initiation factor activity, and high-affinity amino acid permeases that serve to provide amino acids for use by the translation machinery. TORC1 also promotes growth by sequestering a number of nutrient and general stress-responsive transcription factors in the cytoplasm. TORC1 negatively controls macroautophagy, a process to recycle surplus cytoplasmic mass under nutrient starvation conditions. TORC1 controls many of these processes via TIP41-TAP42-mediated inhibition of the type 2A-related phosphatases PP2A and SIT4. [PubMed: 10198052] | |
Protein Sequence | MNKYINKYTTPPNLLSLRQRAEGKHRTRKKLTHKSHSHDDEMSTTSNTDSNHNGPNDSGRVITGSAGHIGKISFVDSELDTTFSTLNLIFDKLKSDVPQERASGANELSTTLTSLAREVSAEQFQRFSNSLNNKIFELIHGFTSSEKIGGILAVDTLISFYLSTEELPNQTSRLANYLRVLIPSSDIEVMRLAANTLGRLTVPGGTLTSDFVEFEVRTCIDWLTLTADNNSSSSKLEYRRHAALLIIKALADNSPYLLYPYVNSILDNIWVPLRDAKLIIRLDAAVALGKCLTIIQDRDPALGKQWFQRLFQGCTHGLSLNTNDSVHATLLVFRELLSLKAPYLRDKYDDIYKSTMKYKEYKFDVIRREVYAILPLLAAFDPAIFTKKYLDRIMVHYLRYLKNIDMNAANNSDKPFILVSIGDIAFEVGSSISPYMTLILDNIREGLRTKFKVRKQFEKDLFYCIGKLACALGPAFAKHLNKDLLNLMLNCPMSDHMQETLMILNEKIPSLESTVNSRILNLLSISLSGEKFIQSNQYDFNNQFSIEKARKSRNQSFMKKTGESNDDITDAQILIQCFKMLQLIHHQYSLTEFVRLITISYIEHEDSSVRKLAALTSCDLFIKDDICKQTSVHALHSVSEVLSKLLMIAITDPVAEIRLEILQHLGSNFDPQLAQPDNLRLLFMALNDEIFGIQLEAIKIIGRLSSVNPAYVVPSLRKTLLELLTQLKFSNMPKKKEESATLLCTLINSSDEVAKPYIDPILDVILPKCQDASSAVASTALKVLGELSVVGGKEMTRYLKELMPLIINTFQDQSNSFKRDAALTTLGQLAASSGYVVGPLLDYPELLGILINILKTENNPHIRRGTVRLIGILGALDPYKHREIEVTSNSKSSVEQNAPSIDIALLMQGVSPSNDEYYPTVVIHNLMKILNDPSLSIHHTAAIQAIMHIFQNLGLRCVSFLDQIIPGIILVMRSCPPSQLDFYFQQLGSLISIVKQHIRPHVEKIYGVIREFFPIIKLQITIISVIESISKALEGEFKRFVPETLTFFLDILENDQSNKRIVPIRILKSLVTFGPNLEDYSHLIMPIVVRMTEYSAGSLKKISIITLGRLAKNINLSEMSSRIVQALVRILNNGDRELTKATMNTLSLLLLQLGTDFVVFVPVINKALLRNRIQHSVYDQLVNKLLNNECLPTNIIFDKENEVPERKNYEDEMQVTKLPVNQNILKNAWYCSQQKTKEDWQEWIRRLSIQLLKESPSACLRSCSSLVSVYYPLARELFNASFSSCWVELQTSYQEDLIQALCKALSSSENPPEIYQMLLNLVEFMEHDDKPLPIPIHTLGKYAQKCHAFAKALHYKEVEFLEEPKNSTIEALISINNQLHQTDSAIGILKHAQQHNELQLKETWYEKLQRWEDALAAYNEKEAAGEDSVEVMMGKLRSLYALGEWEELSKLASEKWGTAKPEVKKAMAPLAAGAAWGLEQWDEIAQYTSVMKSQSPDKEFYDAILCLHRNNFKKAEVHIFNARDLLVTELSALVNESYNRAYNVVVRAQIIAELEEIIKYKKLPQNSDKRLTMRETWNTRLLGCQKNIDVWQRILRVRSLVIKPKEDAQVRIKFANLCRKSGRMALAKKVLNTLLEETDDPDHPNTAKASPPVVYAQLKYLWATGLQDEALKQLINFTSRMAHDLGLDPNNMIAQSVPQQSKRVPRHVEDYTKLLARCFLKQGEWRVCLQPKWRLSNPDSILGSYLLATHFDNTWYKAWHNWALANFEVISMLTSVSKKKQEGSDASSVTDINEFDNGMIGVNTFDAKEVHYSSNLIHRHVIPAIKGFFHSISLSESSSLQDALRLLTLWFTFGGIPEATQAMHEGFNLIQIGTWLEVLPQLISRIHQPNQIVSRSLLSLLSDLGKAHPQALVYPLMVAIKSESLSRQKAALSIIEKMRIHSPVLVDQAELVSHELIRMAVLWHEQWYEGLDDASRQFFGEHNTEKMFAALEPLYEMLKRGPETLREISFQNSFGRDLNDAYEWLMNYKKSKDVSNLNQAWDIYYNVFRKIGKQLPQLQTLELQHVSPKLLSAHDLELAVPGTRASGGKPIVKISKFEPVFSVISSKQRPRKFCIKGSDGKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLQNDAECFRRHLDIQQYPAIPLSPKSGLLGWVPNSDTFHVLIREHREAKKIPLNIEHWVMLQMAPDYDNLTLLQKVEVFTYALNNTEGQDLYKVLWLKSRSSETWLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRITGKVIHIDFGDCFEAAILREKFPEKVPFRLTRMLTYAMEVSGIEGSFRITCENVMKVLRDNKGSLMAILEAFAFDPLINWGFDLPTKKIEEETGIQLPVMNANELLSNGAITEEEVQRVENEHKNAIRNARAMLVLKRITDKLTGNDIRRFNDLDVPEQVDKLIQQATSVENLCQHYIGWCPFW | |
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 |
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9 | Phosphorylation | NKYINKYTTPPNLLS CCCCCCCCCCCCHHH | 34.14 | 24961812 | |
10 | Phosphorylation | KYINKYTTPPNLLSL CCCCCCCCCCCHHHH | 33.39 | 16055732 | |
16 | Phosphorylation | TTPPNLLSLRQRAEG CCCCCHHHHHHHHHC | 25.36 | 24961812 | |
35 | Phosphorylation | RKKLTHKSHSHDDEM CCCCCCCCCCCCCCC | 23.71 | 19779198 | |
37 | Phosphorylation | KLTHKSHSHDDEMST CCCCCCCCCCCCCCC | 35.38 | 28889911 | |
43 | Phosphorylation | HSHDDEMSTTSNTDS CCCCCCCCCCCCCCC | 26.87 | 24961812 | |
44 | Phosphorylation | SHDDEMSTTSNTDSN CCCCCCCCCCCCCCC | 32.69 | 24961812 | |
45 | Phosphorylation | HDDEMSTTSNTDSNH CCCCCCCCCCCCCCC | 16.81 | 19779198 | |
46 | Phosphorylation | DDEMSTTSNTDSNHN CCCCCCCCCCCCCCC | 37.51 | 29136822 | |
48 | Phosphorylation | EMSTTSNTDSNHNGP CCCCCCCCCCCCCCC | 40.34 | 19779198 | |
50 | Phosphorylation | STTSNTDSNHNGPND CCCCCCCCCCCCCCC | 37.64 | 29136822 | |
63 | Phosphorylation | NDSGRVITGSAGHIG CCCCCEEECCCCEEE | 23.40 | 28889911 | |
65 | Phosphorylation | SGRVITGSAGHIGKI CCCEEECCCCEEEEE | 23.56 | 27214570 | |
103 | Phosphorylation | DVPQERASGANELST CCCHHHHCCHHHHHH | 44.66 | 21126336 | |
348 | Phosphorylation | APYLRDKYDDIYKST CHHHHHCCHHHHHHH | 24.12 | 27017623 | |
352 | Phosphorylation | RDKYDDIYKSTMKYK HHCCHHHHHHHCCCC | 13.09 | 27017623 | |
355 | Phosphorylation | YDDIYKSTMKYKEYK CHHHHHHHCCCCCCC | 17.33 | 27017623 | |
773 | Phosphorylation | LPKCQDASSAVASTA CHHCCCHHHHHHHHH | 27.41 | 30377154 | |
774 | Phosphorylation | PKCQDASSAVASTAL HHCCCHHHHHHHHHH | 28.60 | 30377154 | |
887 | Phosphorylation | KHREIEVTSNSKSSV CCCEEEEECCCCCCH | 14.92 | 28889911 | |
1106 | Phosphorylation | LKKISIITLGRLAKN CCEEEEEEHHHHHHH | 22.84 | 19779198 | |
1142 | Phosphorylation | DRELTKATMNTLSLL CHHHHHHHHHHHHHH | 16.71 | 30377154 | |
1145 | Phosphorylation | LTKATMNTLSLLLLQ HHHHHHHHHHHHHHH | 13.60 | 30377154 | |
1147 | Phosphorylation | KATMNTLSLLLLQLG HHHHHHHHHHHHHHC | 18.22 | 30377154 | |
1237 | Ubiquitination | YCSQQKTKEDWQEWI HCCCCCCHHHHHHHH | 61.79 | 22106047 | |
1291 | Phosphorylation | SCWVELQTSYQEDLI HCEEEHHHCHHHHHH | 41.86 | 28889911 | |
1306 | Phosphorylation | QALCKALSSSENPPE HHHHHHHHCCCCCHH | 36.36 | 30377154 | |
1315 | Phosphorylation | SENPPEIYQMLLNLV CCCCHHHHHHHHHHH | 6.04 | 30377154 | |
1975 | Phosphorylation | YEGLDDASRQFFGEH HCCCCHHHHHHHCCC | 33.34 | 28889911 | |
2009 | Phosphorylation | PETLREISFQNSFGR HHHHHHHHCCCCCCC | 18.94 | 22369663 | |
2013 | Phosphorylation | REISFQNSFGRDLND HHHHCCCCCCCCHHH | 20.49 | 22369663 | |
2174 | Ubiquitination | PAIPLSPKSGLLGWV CCCCCCCCCCCCEEC | 54.50 | 17644757 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of TOR2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of TOR2_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of TOR2_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 THR-10 AND SER-2013, ANDMASS SPECTROMETRY. |