UniProt ID | RICTR_SCHPO | |
---|---|---|
UniProt AC | Q09743 | |
Protein Name | Target of rapamycin complex 2 subunit ste20 {ECO:0000305|PubMed:18076573} | |
Gene Name | ste20 {ECO:0000303|PubMed:10467002} | |
Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
Sequence Length | 1309 | |
Subcellular Localization |
Membrane Multi-pass membrane protein . |
|
Protein Description | Component of TORC2, which regulates multiple cellular processes to control cell growth in response to environmental signals. TORC2 is required for cell survival under various stress conditions. TORC2 positively controls G1 cell-cycle arrest, sexual development and amino acid uptake. Positively regulates amino acid uptake through the control of expression of amino acid permeases.. | |
Protein Sequence | MKPVRRGQTDTALDISSHAKTNGDFIKKMNTTDSKRLKLLEDLKGKLEVECKIRDGAETLLQVFDTNFKKETKERKEMLKKKCTDELESSKKKIEELVSSIESFQGENGEAKTGSTSLTRSASATVSRKSSLQEKYSTRFSYKAGCSDSCSVTVSGTGELIGPTRNAHSNLTPTVIQRIDFENVNEKNNSSSEDTQPNGKRPSSLQSNFSQFPLNPWLDNIYKACLEGSMKDVIDSSNNLCEYLHEHSDPAYAKNFSLITPTILSMLELNVSEVTASVYRLLRHLFLDATAFSCCQMLNLPWILSKSLLSGTDAYQIEREQAFRLIRTLYFLSSTEGHEDYLSGITRTIISICEHVSDVSRGIAVETLIELMIIRPKILFKANGLRVLMISLIDGSISENLAASAALALVYLLDDPESACYVNLPYDIGILLSPFTSSSSRDTFNSSEEQSEQAAKAMKSSAKVASVLLNSWSGLLALSTNDFQALRSIVDTLRVPSFAPRSDVIDLFFLIFQVEYSSWSESFLAGKRLTVVKNQAVSNDDNINMVNIPDGSNKKYMSLRQHFTAVLLFIFLELGLVESIVCMIRASDDPSASRKATYLLGEVLRLSDELLPIHLGAKIQSLPSLFNMASQFTAEDRFVATSVLQSIESLNRVKFHSATQPFSQTTSLLFKEQKTDGSFRGQRQVEHVKLKMGMQIDDSHFRSMLAETNVLATKNYQKWRWDTLVQIMEGPLLSPKRIDETLRTTKFMRRLLAFYKPFSNRFSSIQNTKPNQKFIKVGCLVFRTLLANPEGVKYLSESKVIKQIAESLSQIDGYSEQVSEPIFSNSRLQKTLTHGYFPMLKVLSSQKEGHAIMERWRIFTTLYHLTELRNRDDLIIIFLTNLDYRLEGHTRIIFSKALNTGQQAVRLTATKHLAALINSESANDNLNHWAISLLIFQLYDPCLEVCKTAVKVLNEVCARNENLLAQVVQLQPSLAHLGEIGSPLLLRFLATTVGFHYLSEINFIEHELDNWYHHRNIDYVDLLEQNFFLSFVSNLKIIDKKNNEPDENILPLHFYGELVKSPQGCEVLESSGHFESFMGTLVEFYDKPLGNEAIRQLKSALWAIGNIGKTDQGITFLINHDTIPLIVKYAENSLIPTVRGTAYFVLGLISRTSKGVEILESLHWYSLMSLMGTSQGICIPRHAGQVLSTPRRNVEFVNERVPTPEFSSLLSSLTNSEREVIRLVSNLSNHVLTNESARQLTKIRSKNAKVFSSKRLVKACMTILGKFHYRVQIQQFVFELFPYSVLLSSSTSQDLNESPSRPNNLSISA | |
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 |
---|---|---|---|---|---|
100 | Phosphorylation | KIEELVSSIESFQGE HHHHHHHHHHHHCCC | 21712547 | ||
103 | Phosphorylation | ELVSSIESFQGENGE HHHHHHHHHCCCCCC | 21712547 | ||
121 | Phosphorylation | GSTSLTRSASATVSR CCCCCCCCCCEEECC | 25720772 | ||
123 | Phosphorylation | TSLTRSASATVSRKS CCCCCCCCEEECCCH | 25720772 | ||
125 | Phosphorylation | LTRSASATVSRKSSL CCCCCCEEECCCHHH | 25720772 | ||
127 | Phosphorylation | RSASATVSRKSSLQE CCCCEEECCCHHHHH | 25720772 | ||
130 | Phosphorylation | SATVSRKSSLQEKYS CEEECCCHHHHHHHC | 25720772 | ||
131 | Phosphorylation | ATVSRKSSLQEKYST EEECCCHHHHHHHCC | 25720772 | ||
151 | Phosphorylation | AGCSDSCSVTVSGTG CCCCCCCEEEECCCC | 18076573 | ||
203 | Phosphorylation | QPNGKRPSSLQSNFS CCCCCCCCHHHCCCC | 21712547 | ||
204 | Phosphorylation | PNGKRPSSLQSNFSQ CCCCCCCHHHCCCCC | 21712547 | ||
207 | Phosphorylation | KRPSSLQSNFSQFPL CCCCHHHCCCCCCCC | 21712547 | ||
1203 | Phosphorylation | FVNERVPTPEFSSLL CCCCCCCCHHHHHHH | 18076573 |
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 RICTR_SCHPO !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RICTR_SCHPO !! |
* 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 RICTR_SCHPO !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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