CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006415
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase TOR1 
Protein Synonyms/Alias
 Dominant rapamycin resistance protein 1; Phosphatidylinositol kinase homolog TOR1; Target of rapamycin kinase 1 
Gene Name
 TOR1 
Gene Synonyms/Alias
 DRR1; YJR066W; J1803 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
1186NNDVLPTKILEANTTubiquitination[1]
1196EANTTDYKPAEQMEAubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 Phosphatidylinositol 3-kinase homolog, component of TORC1, which 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. 
Sequence Annotation
 REPEAT 114 151 HEAT 1.
 REPEAT 249 286 HEAT 2.
 REPEAT 627 663 HEAT 3.
 REPEAT 664 701 HEAT 4.
 REPEAT 747 784 HEAT 5.
 REPEAT 788 826 HEAT 6.
 REPEAT 832 870 HEAT 7.
 REPEAT 908 946 HEAT 8.
 REPEAT 950 987 HEAT 9.
 REPEAT 1069 1107 HEAT 10.
 REPEAT 1109 1147 HEAT 11.
 DOMAIN 1331 1919 FAT.
 DOMAIN 2125 2437 PI3K/PI4K.
 DOMAIN 2438 2470 FATC.
 REGION 1775 2157 Interaction with FKBP-rapamycin.  
Keyword
 3D-structure; ATP-binding; Cell cycle; Cell membrane; Complete proteome; Kinase; Membrane; Nucleotide-binding; Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase; Vacuole. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2470 AA 
Protein Sequence
MEPHEEQIWK SKLLKAANND MDMDRNVPLA PNLNVNMNMK MNASRNGDEF GLTSSRFDGV 60
VIGSNGDVNF KPILEKIFRE LTSDYKEERK LASISLFDLL VSLEHELSIE EFQAVSNDIN 120
NKILELVHTK KTSTRVGAVL SIDTLISFYA YTERLPNETS RLAGYLRGLI PSNDVEVMRL 180
AAKTLGKLAV PGGTYTSDFV EFEIKSCLEW LTASTEKNSF SSSKPDHAKH AALLIITALA 240
ENCPYLLYQY LNSILDNIWR ALRDPHLVIR IDASITLAKC LSTLRNRDPQ LTSQWVQRLA 300
TSCEYGFQVN TLECIHASLL VYKEILFLKD PFLNQVFDQM CLNCIAYENH KAKMIREKIY 360
QIVPLLASFN PQLFAGKYLH QIMDNYLEIL TNAPANKIPH LKDDKPQILI SIGDIAYEVG 420
PDIAPYVKQI LDYIEHDLQT KFKFRKKFEN EIFYCIGRLA VPLGPVLGKL LNRNILDLMF 480
KCPLSDYMQE TFQILTERIP SLGPKINDEL LNLVCSTLSG TPFIQPGSPM EIPSFSRERA 540
REWRNKNILQ KTGESNDDNN DIKIIIQAFR MLKNIKSRFS LVEFVRIVAL SYIEHTDPRV 600
RKLAALTSCE IYVKDNICKQ TSLHSLNTVS EVLSKLLAIT IADPLQDIRL EVLKNLNPCF 660
DPQLAQPDNL RLLFTALHDE SFNIQSVAME LVGRLSSVNP AYVIPSIRKI LLELLTKLKF 720
STSSREKEET ASLLCTLIRS SKDVAKPYIE PLLNVLLPKF QDTSSTVAST ALRTIGELSV 780
VGGEDMKIYL KDLFPLIIKT FQDQSNSFKR EAALKALGQL AASSGYVIDP LLDYPELLGI 840
LVNILKTENS QNIRRQTVTL IGILGAIDPY RQKEREVTST TDISTEQNAP PIDIALLMQG 900
MSPSNDEYYT TVVIHCLLKI LKDPSLSSYH TAVIQAIMHI FQTLGLKCVS FLDQIIPTIL 960
DVMRTCSQSL LEFYFQQLCS LIIIVRQHIR PHVDSIFQAI KDFSSVAKLQ ITLVSVIEAI 1020
SKALEGEFKR LVPLTLTLFL VILENDKSSD KVLSRRVLRL LESFGPNLEG YSHLITPKIV 1080
QMAEFTSGNL QRSAIITIGK LAKDVDLFEM SSRIVHSLLR VLSSTTSDEL SKVIMNTLSL 1140
LLIQMGTSFA IFIPVINEVL MKKHIQHTIY DDLTNRILNN DVLPTKILEA NTTDYKPAEQ 1200
MEAADAGVAK LPINQSVLKS AWNSSQQRTK EDWQEWSKRL SIQLLKESPS HALRACSNLA 1260
SMYYPLAKEL FNTAFACVWT ELYSQYQEDL IGSLCIALSS PLNPPEIHQT LLNLVEFMEH 1320
DDKALPIPTQ SLGEYAERCH AYAKALHYKE IKFIKEPENS TIESLISINN QLNQTDAAIG 1380
ILKHAQQHHS LQLKETWFEK LERWEDALHA YNEREKAGDT SVSVTLGKMR SLHALGEWEQ 1440
LSQLAARKWK VSKLQTKKLI APLAAGAAWG LGEWDMLEQY ISVMKPKSPD KEFFDAILYL 1500
HKNDYDNASK HILNARDLLV TEISALINES YNRAYSVIVR TQIITEFEEI IKYKQLPPNS 1560
EKKLHYQNLW TKRLLGCQKN VDLWQRVLRV RSLVIKPKQD LQIWIKFANL CRKSGRMRLA 1620
NKALNMLLEG GNDPSLPNTF KAPPPVVYAQ LKYIWATGAY KEALNHLIGF TSRLAHDLGL 1680
DPNNMIAQSV KLSSASTAPY VEEYTKLLAR CFLKQGEWRI ATQPNWRNTN PDAILGSYLL 1740
ATHFDKNWYK AWHNWALANF EVISMVQEET KLNGGKNDDD DDTAVNNDNV RIDGSILGSG 1800
SLTINGNRYP LELIQRHVVP AIKGFFHSIS LLETSCLQDT LRLLTLLFNF GGIKEVSQAM 1860
YEGFNLMKIE NWLEVLPQLI SRIHQPDPTV SNSLLSLLSD LGKAHPQALV YPLTVAIKSE 1920
SVSRQKAALS IIEKIRIHSP VLVNQAELVS HELIRVAVLW HELWYEGLED ASRQFFVEHN 1980
IEKMFSTLEP LHKHLGNEPQ TLSEVSFQKS FGRDLNDAYE WLNNYKKSKD INNLNQAWDI 2040
YYNVFRKITR QIPQLQTLDL QHVSPQLLAT HDLELAVPGT YFPGKPTIRI AKFEPLFSVI 2100
SSKQRPRKFS IKGSDGKDYK YVLKGHEDIR QDSLVMQLFG LVNTLLKNDS ECFKRHLDIQ 2160
QYPAIPLSPK SGLLGWVPNS DTFHVLIREH RDAKKIPLNI EHWVMLQMAP DYENLTLLQK 2220
IEVFTYALDN TKGQDLYKIL WLKSRSSETW LERRTTYTRS LAVMSMTGYI LGLGDRHPSN 2280
LMLDRITGKV IHIDFGDCFE AAILREKYPE KVPFRLTRML TYAMEVSGIE GSFRITCENV 2340
MRVLRDNKES LMAILEAFAL DPLIHWGFDL PPQKLTEQTG IPLPLINPSE LLRKGAITVE 2400
EAANMEAEQQ NETKNARAML VLRRITDKLT GNDIKRFNEL DVPEQVDKLI QQATSIERLC 2460
QHYIGWCPFW 2470 
Gene Ontology
 GO:0010008; C:endosome membrane; IDA:SGD.
 GO:0031234; C:extrinsic to internal side of plasma membrane; IDA:SGD.
 GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
 GO:0000139; C:Golgi membrane; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0031931; C:TORC1 complex; IPI:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008144; F:drug binding; IEA:InterPro.
 GO:0004672; F:protein kinase activity; IMP:SGD.
 GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
 GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
 GO:0007126; P:meiosis; IMP:SGD.
 GO:0031930; P:mitochondria-nucleus signaling pathway; IMP:SGD.
 GO:0010507; P:negative regulation of autophagy; IGI:SGD.
 GO:0051726; P:regulation of cell cycle; IMP:SGD.
 GO:0001558; P:regulation of cell growth; IMP:SGD.
 GO:0006974; P:response to DNA damage stimulus; IMP:SGD.
 GO:0042254; P:ribosome biogenesis; IMP:SGD.
 GO:0031929; P:TOR signaling cascade; IMP:SGD.
 GO:0042790; P:transcription of nuclear large rRNA transcript from RNA polymerase I promoter; IMP:SGD. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR024585; DUF3385_TOR.
 IPR003152; FATC.
 IPR011009; Kinase-like_dom.
 IPR000403; PI3/4_kinase_cat_dom.
 IPR018936; PI3/4_kinase_CS.
 IPR003151; PIK-rel_kinase_FAT.
 IPR014009; PIK_FAT.
 IPR009076; Rapamycin-bd_dom.
 IPR026683; TOR/Smg1. 
Pfam
 PF11865; DUF3385
 PF02259; FAT
 PF02260; FATC
 PF00454; PI3_PI4_kinase
 PF08771; Rapamycin_bind 
SMART
 SM00146; PI3Kc 
PROSITE
 PS51189; FAT
 PS51190; FATC
 PS50077; HEAT_REPEAT
 PS00915; PI3_4_KINASE_1
 PS00916; PI3_4_KINASE_2
 PS50290; PI3_4_KINASE_3 
PRINTS