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P32600

- TOR2_YEAST

UniProt

P32600 - TOR2_YEAST

Protein

Serine/threonine-protein kinase TOR2

Gene

TOR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 3 (09 Jan 2007)
      Previous versions | rss
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    Functioni

    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. TORC2 regulates cell cycle-dependent polarization of the actin-cytoskeleton, cell wall integrity, and receptor endocytosis. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway by activating the RHO1 guanine nucleotide exchange factor ROM2. TORC2 phosphorylates the AGC kinase YPK2, an upstream effector of the cell integrity pathway. TORC2 negatively regulates calcineurin-dependent stress signaling via phosphorylation of its effector SLM1-SLM2.15 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication
    ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate.1 Publication

    GO - Molecular functioni

    1. 1-phosphatidylinositol 4-kinase activity Source: UniProtKB-EC
    2. ATP binding Source: UniProtKB-KW
    3. drug binding Source: InterPro
    4. protein binding Source: IntAct
    5. protein serine/threonine kinase activity Source: SGD

    GO - Biological processi

    1. actin filament reorganization involved in cell cycle Source: SGD
    2. cytoskeleton organization Source: SGD
    3. establishment or maintenance of actin cytoskeleton polarity Source: SGD
    4. negative regulation of autophagy Source: SGD
    5. positive regulation of endocytosis Source: SGD
    6. positive regulation of Rho guanyl-nucleotide exchange factor activity Source: SGD
    7. positive regulation of Rho protein signal transduction Source: SGD
    8. protein phosphorylation Source: GOC
    9. regulation of cell cycle Source: SGD
    10. regulation of cell growth Source: SGD
    11. ribosome biogenesis Source: SGD
    12. signal transduction Source: SGD
    13. TOR signaling Source: SGD

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31962-MONOMER.
    BRENDAi2.7.1.137. 984.
    ReactomeiREACT_188481. S6K1-mediated signalling.
    REACT_188925. CD28 dependent PI3K/Akt signaling.
    REACT_188931. PIP3 activates AKT signaling.
    REACT_219346. HSF1-dependent transactivation.
    REACT_223756. Constitutive PI3K/AKT Signaling in Cancer.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase TOR2 (EC:2.7.1.67, EC:2.7.11.1)
    Alternative name(s):
    Dominant rapamycin resistance protein 2
    Phosphatidylinositol 4-kinase TOR2
    Short name:
    PI4-kinase TOR2
    Short name:
    PI4K TOR2
    Short name:
    PtdIns-4-kinase TOR2
    Target of rapamycin kinase 2
    Temperature-sensitive CSG2 suppressor protein 14
    Gene namesi
    Name:TOR2
    Synonyms:DRR2, TSC14
    Ordered Locus Names:YKL203C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    CYGDiYKL203c.
    SGDiS000001686. TOR2.

    Subcellular locationi

    Cell membrane; Peripheral membrane protein; Cytoplasmic side. Vacuole membrane; Peripheral membrane protein; Cytoplasmic side
    Note: Also localizes to membranous structures both proximal to, yet distinct from, the plasma membrane as well as within the cell interior, probably endosomal or Golgi membranes.

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. extrinsic component of cytoplasmic side of plasma membrane Source: SGD
    3. fungal-type vacuole membrane Source: SGD
    4. plasma membrane Source: SGD
    5. TORC1 complex Source: SGD
    6. TORC2 complex Source: SGD

    Keywords - Cellular componenti

    Cell membrane, Membrane, Vacuole

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1975 – 19751S → I in TOR2-1; confers resistance to rapamycin. 1 Publication
    Mutagenesisi2129 – 21291G → R: Causes defect in receptor endocytosis. 1 Publication
    Mutagenesisi2279 – 22791D → A: Loss of function. 1 Publication
    Mutagenesisi2298 – 22981D → E: Loss of kinase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 24742474Serine/threonine-protein kinase TOR2PRO_0000088815Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei10 – 101Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32600.
    PaxDbiP32600.
    PeptideAtlasiP32600.

    Expressioni

    Gene expression databases

    GenevestigatoriP32600.

    Interactioni

    Subunit structurei

    The target of rapamycin complex 1 (TORC1) is composed of at least KOG1, LST8, TCO89 and either TOR1 (TORC1-A) or TOR2 (TORC1-B). TORC1 binds to and is inhibited by FKBP-rapamycin. The target of rapamycin complex 2 (TORC2) is composed of at least AVO1, AVO2, BIT61, LST8, TOR2 and TSC11. TORC2 likely forms a homodimer. Contrary to TORC1, TORC2 does not bind to and is not sensitive to FKBP-rapamycin. Interacts with SLM1 and SLM2.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AVO1Q082364EBI-19385,EBI-29284
    AVO2Q047494EBI-19385,EBI-28131
    BIT61P470412EBI-19385,EBI-25889
    LST8P413187EBI-19385,EBI-28598
    TAP42Q043724EBI-19385,EBI-18926
    TSC11P400615EBI-19385,EBI-22621

    Protein-protein interaction databases

    BioGridi33920. 250 interactions.
    DIPiDIP-2332N.
    IntActiP32600. 24 interactions.
    MINTiMINT-2843476.
    STRINGi4932.YKL203C.

    Structurei

    3D structure databases

    ProteinModelPortaliP32600.
    SMRiP32600. Positions 1405-1447, 1955-2420, 2442-2474.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati588 – 62639HEAT 1Add
    BLAST
    Repeati636 – 67439HEAT 2Add
    BLAST
    Repeati676 – 71035HEAT 3Add
    BLAST
    Repeati756 – 79338HEAT 4Add
    BLAST
    Repeati797 – 83539HEAT 5Add
    BLAST
    Repeati841 – 87939HEAT 6Add
    BLAST
    Repeati917 – 95539HEAT 7Add
    BLAST
    Repeati1039 – 107638HEAT 8Add
    BLAST
    Repeati1079 – 111638HEAT 9Add
    BLAST
    Repeati1118 – 115538HEAT 10Add
    BLAST
    Repeati1292 – 133140HEAT 11Add
    BLAST
    Domaini1338 – 1922585FATPROSITE-ProRule annotationAdd
    BLAST
    Domaini2123 – 2441319PI3K/PI4KPROSITE-ProRule annotationAdd
    BLAST
    Domaini2442 – 247433FATCPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PI3/PI4-kinase family.Curated
    Contains 1 FAT domain.PROSITE-ProRule annotation
    Contains 1 FATC domain.PROSITE-ProRule annotation
    Contains 11 HEAT repeats.Curated
    Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5032.
    GeneTreeiENSGT00720000108744.
    HOGENOMiHOG000163215.
    KOiK07203.
    OMAiTYKQNIG.
    OrthoDBiEOG7Z3FCR.

    Family and domain databases

    Gene3Di1.10.1070.11. 3 hits.
    1.25.10.10. 6 hits.
    InterProiIPR011989. 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.
    [Graphical view]
    PfamiPF11865. DUF3385. 1 hit.
    PF02259. FAT. 1 hit.
    PF02260. FATC. 1 hit.
    PF00454. PI3_PI4_kinase. 1 hit.
    PF08771. Rapamycin_bind. 1 hit.
    [Graphical view]
    SMARTiSM00146. PI3Kc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47212. SSF47212. 1 hit.
    SSF48371. SSF48371. 9 hits.
    SSF56112. SSF56112. 3 hits.
    PROSITEiPS51189. FAT. 1 hit.
    PS51190. FATC. 1 hit.
    PS00915. PI3_4_KINASE_1. 1 hit.
    PS00916. PI3_4_KINASE_2. 1 hit.
    PS50290. PI3_4_KINASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32600-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKYINKYTT PPNLLSLRQR AEGKHRTRKK LTHKSHSHDD EMSTTSNTDS     50
    NHNGPNDSGR VITGSAGHIG KISFVDSELD TTFSTLNLIF DKLKSDVPQE 100
    RASGANELST TLTSLAREVS AEQFQRFSNS LNNKIFELIH GFTSSEKIGG 150
    ILAVDTLISF YLSTEELPNQ TSRLANYLRV LIPSSDIEVM RLAANTLGRL 200
    TVPGGTLTSD FVEFEVRTCI DWLTLTADNN SSSSKLEYRR HAALLIIKAL 250
    ADNSPYLLYP YVNSILDNIW VPLRDAKLII RLDAAVALGK CLTIIQDRDP 300
    ALGKQWFQRL FQGCTHGLSL NTNDSVHATL LVFRELLSLK APYLRDKYDD 350
    IYKSTMKYKE YKFDVIRREV YAILPLLAAF DPAIFTKKYL DRIMVHYLRY 400
    LKNIDMNAAN NSDKPFILVS IGDIAFEVGS SISPYMTLIL DNIREGLRTK 450
    FKVRKQFEKD LFYCIGKLAC ALGPAFAKHL NKDLLNLMLN CPMSDHMQET 500
    LMILNEKIPS LESTVNSRIL NLLSISLSGE KFIQSNQYDF NNQFSIEKAR 550
    KSRNQSFMKK TGESNDDITD AQILIQCFKM LQLIHHQYSL TEFVRLITIS 600
    YIEHEDSSVR KLAALTSCDL FIKDDICKQT SVHALHSVSE VLSKLLMIAI 650
    TDPVAEIRLE ILQHLGSNFD PQLAQPDNLR LLFMALNDEI FGIQLEAIKI 700
    IGRLSSVNPA YVVPSLRKTL LELLTQLKFS NMPKKKEESA TLLCTLINSS 750
    DEVAKPYIDP ILDVILPKCQ DASSAVASTA LKVLGELSVV GGKEMTRYLK 800
    ELMPLIINTF QDQSNSFKRD AALTTLGQLA ASSGYVVGPL LDYPELLGIL 850
    INILKTENNP HIRRGTVRLI GILGALDPYK HREIEVTSNS KSSVEQNAPS 900
    IDIALLMQGV SPSNDEYYPT VVIHNLMKIL NDPSLSIHHT AAIQAIMHIF 950
    QNLGLRCVSF LDQIIPGIIL VMRSCPPSQL DFYFQQLGSL ISIVKQHIRP 1000
    HVEKIYGVIR EFFPIIKLQI TIISVIESIS KALEGEFKRF VPETLTFFLD 1050
    ILENDQSNKR IVPIRILKSL VTFGPNLEDY SHLIMPIVVR MTEYSAGSLK 1100
    KISIITLGRL AKNINLSEMS SRIVQALVRI LNNGDRELTK ATMNTLSLLL 1150
    LQLGTDFVVF VPVINKALLR NRIQHSVYDQ LVNKLLNNEC LPTNIIFDKE 1200
    NEVPERKNYE DEMQVTKLPV NQNILKNAWY CSQQKTKEDW QEWIRRLSIQ 1250
    LLKESPSACL RSCSSLVSVY YPLARELFNA SFSSCWVELQ TSYQEDLIQA 1300
    LCKALSSSEN PPEIYQMLLN LVEFMEHDDK PLPIPIHTLG KYAQKCHAFA 1350
    KALHYKEVEF LEEPKNSTIE ALISINNQLH QTDSAIGILK HAQQHNELQL 1400
    KETWYEKLQR WEDALAAYNE KEAAGEDSVE VMMGKLRSLY ALGEWEELSK 1450
    LASEKWGTAK PEVKKAMAPL AAGAAWGLEQ WDEIAQYTSV MKSQSPDKEF 1500
    YDAILCLHRN NFKKAEVHIF NARDLLVTEL SALVNESYNR AYNVVVRAQI 1550
    IAELEEIIKY KKLPQNSDKR LTMRETWNTR LLGCQKNIDV WQRILRVRSL 1600
    VIKPKEDAQV RIKFANLCRK SGRMALAKKV LNTLLEETDD PDHPNTAKAS 1650
    PPVVYAQLKY LWATGLQDEA LKQLINFTSR MAHDLGLDPN NMIAQSVPQQ 1700
    SKRVPRHVED YTKLLARCFL KQGEWRVCLQ PKWRLSNPDS ILGSYLLATH 1750
    FDNTWYKAWH NWALANFEVI SMLTSVSKKK QEGSDASSVT DINEFDNGMI 1800
    GVNTFDAKEV HYSSNLIHRH VIPAIKGFFH SISLSESSSL QDALRLLTLW 1850
    FTFGGIPEAT QAMHEGFNLI QIGTWLEVLP QLISRIHQPN QIVSRSLLSL 1900
    LSDLGKAHPQ ALVYPLMVAI KSESLSRQKA ALSIIEKMRI HSPVLVDQAE 1950
    LVSHELIRMA VLWHEQWYEG LDDASRQFFG EHNTEKMFAA LEPLYEMLKR 2000
    GPETLREISF QNSFGRDLND AYEWLMNYKK SKDVSNLNQA WDIYYNVFRK 2050
    IGKQLPQLQT LELQHVSPKL LSAHDLELAV PGTRASGGKP IVKISKFEPV 2100
    FSVISSKQRP RKFCIKGSDG KDYKYVLKGH EDIRQDSLVM QLFGLVNTLL 2150
    QNDAECFRRH LDIQQYPAIP LSPKSGLLGW VPNSDTFHVL IREHREAKKI 2200
    PLNIEHWVML QMAPDYDNLT LLQKVEVFTY ALNNTEGQDL YKVLWLKSRS 2250
    SETWLERRTT YTRSLAVMSM TGYILGLGDR HPSNLMLDRI TGKVIHIDFG 2300
    DCFEAAILRE KFPEKVPFRL TRMLTYAMEV SGIEGSFRIT CENVMKVLRD 2350
    NKGSLMAILE AFAFDPLINW GFDLPTKKIE EETGIQLPVM NANELLSNGA 2400
    ITEEEVQRVE NEHKNAIRNA RAMLVLKRIT DKLTGNDIRR FNDLDVPEQV 2450
    DKLIQQATSV ENLCQHYIGW CPFW 2474
    Length:2,474
    Mass (Da):281,568
    Last modified:January 9, 2007 - v3
    Checksum:iF2349690146058CF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1473 – 14731Missing in CAA82048. (PubMed:8196765)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71416 Genomic DNA. Translation: CAA50548.1.
    Z28203 Genomic DNA. Translation: CAA82048.1.
    BK006944 Genomic DNA. Translation: DAA08966.1.
    PIRiS38040.
    RefSeqiNP_012719.2. NM_001179768.1.

    Genome annotation databases

    EnsemblFungiiYKL203C; YKL203C; YKL203C.
    GeneIDi853632.
    KEGGisce:YKL203C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71416 Genomic DNA. Translation: CAA50548.1 .
    Z28203 Genomic DNA. Translation: CAA82048.1 .
    BK006944 Genomic DNA. Translation: DAA08966.1 .
    PIRi S38040.
    RefSeqi NP_012719.2. NM_001179768.1.

    3D structure databases

    ProteinModelPortali P32600.
    SMRi P32600. Positions 1405-1447, 1955-2420, 2442-2474.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33920. 250 interactions.
    DIPi DIP-2332N.
    IntActi P32600. 24 interactions.
    MINTi MINT-2843476.
    STRINGi 4932.YKL203C.

    Proteomic databases

    MaxQBi P32600.
    PaxDbi P32600.
    PeptideAtlasi P32600.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKL203C ; YKL203C ; YKL203C .
    GeneIDi 853632.
    KEGGi sce:YKL203C.

    Organism-specific databases

    CYGDi YKL203c.
    SGDi S000001686. TOR2.

    Phylogenomic databases

    eggNOGi COG5032.
    GeneTreei ENSGT00720000108744.
    HOGENOMi HOG000163215.
    KOi K07203.
    OMAi TYKQNIG.
    OrthoDBi EOG7Z3FCR.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31962-MONOMER.
    BRENDAi 2.7.1.137. 984.
    Reactomei REACT_188481. S6K1-mediated signalling.
    REACT_188925. CD28 dependent PI3K/Akt signaling.
    REACT_188931. PIP3 activates AKT signaling.
    REACT_219346. HSF1-dependent transactivation.
    REACT_223756. Constitutive PI3K/AKT Signaling in Cancer.

    Miscellaneous databases

    NextBioi 974511.
    PROi P32600.

    Gene expression databases

    Genevestigatori P32600.

    Family and domain databases

    Gene3Di 1.10.1070.11. 3 hits.
    1.25.10.10. 6 hits.
    InterProi 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.
    [Graphical view ]
    Pfami PF11865. DUF3385. 1 hit.
    PF02259. FAT. 1 hit.
    PF02260. FATC. 1 hit.
    PF00454. PI3_PI4_kinase. 1 hit.
    PF08771. Rapamycin_bind. 1 hit.
    [Graphical view ]
    SMARTi SM00146. PI3Kc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47212. SSF47212. 1 hit.
    SSF48371. SSF48371. 9 hits.
    SSF56112. SSF56112. 3 hits.
    PROSITEi PS51189. FAT. 1 hit.
    PS51190. FATC. 1 hit.
    PS00915. PI3_4_KINASE_1. 1 hit.
    PS00916. PI3_4_KINASE_2. 1 hit.
    PS50290. PI3_4_KINASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression."
      Kunz J., Henriquez R., Schneider U., Deuter-Reinhard M., Movva N., Hall M.N.
      Cell 73:585-596(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: JK9-3D.
    2. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "TOR kinase domains are required for two distinct functions, only one of which is inhibited by rapamycin."
      Zheng X.-F., Florentino D., Chen J., Crabtree G.R., Schreiber S.L.
      Cell 82:121-130(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "FKBP12-rapamycin target TOR2 is a vacuolar protein with an associated phosphatidylinositol-4 kinase activity."
      Cardenas M.E., Heitman J.
      EMBO J. 14:5892-5907(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-1975 AND ASP-2279, CATALYTIC ACTIVITY.
    6. "TOR controls translation initiation and early G1 progression in yeast."
      Barbet N.C., Schneider U., Helliwell S.B., Stansfield I., Tuite M.F., Hall M.N.
      Mol. Biol. Cell 7:25-42(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "TOR2 is required for organization of the actin cytoskeleton in yeast."
      Schmidt A., Kunz J., Hall M.N.
      Proc. Natl. Acad. Sci. U.S.A. 93:13780-13785(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease."
      Schmidt A., Beck T., Koller A., Kunz J., Hall M.N.
      EMBO J. 17:6924-6931(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "The TOR (target of rapamycin) signal transduction pathway regulates the stability of translation initiation factor eIF4G in the yeast Saccharomyces cerevisiae."
      Berset C., Trachsel H., Altmann M.
      Proc. Natl. Acad. Sci. U.S.A. 95:4264-4269(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Tor proteins and protein phosphatase 2A reciprocally regulate Tap42 in controlling cell growth in yeast."
      Jiang Y., Broach J.R.
      EMBO J. 18:2782-2792(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Regulation of ribosome biogenesis by the rapamycin-sensitive TOR-signaling pathway in Saccharomyces cerevisiae."
      Powers T., Walter P.
      Mol. Biol. Cell 10:987-1000(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors."
      Beck T., Hall M.N.
      Nature 402:689-692(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "HEAT repeats mediate plasma membrane localization of Tor2p in yeast."
      Kunz J., Schneider U., Howald I., Schmidt A., Hall M.N.
      J. Biol. Chem. 275:37011-37020(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "TIP41 interacts with TAP42 and negatively regulates the TOR signaling pathway."
      Jacinto E., Guo B., Arndt K.T., Schmelzle T., Hall M.N.
      Mol. Cell 8:1017-1026(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control."
      Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L., Bonenfant D., Oppliger W., Jenoe P., Hall M.N.
      Mol. Cell 10:457-468(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    16. "Tor kinases are in distinct membrane-associated protein complexes in Saccharomyces cerevisiae."
      Wedaman K.P., Reinke A., Anderson S., Yates J.R. III, McCaffery J.M., Powers T.
      Mol. Biol. Cell 14:1204-1220(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH LST8.
    17. "Receptor internalization in yeast requires the Tor2-Rho1 signaling pathway."
      deHart A.K.A., Schnell J.D., Allen D.A., Tsai J.-Y., Hicke L.
      Mol. Biol. Cell 14:4676-4684(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RECEPTOR ENDOCYTOSIS, MUTAGENESIS OF GLY-2129.
    18. "TOR regulates ribosomal protein gene expression via PKA and the forkhead transcription factor FHL1."
      Martin D.E., Soulard A., Hall M.N.
      Cell 119:969-979(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Genome-wide lethality screen identifies new PI4,5P2 effectors that regulate the actin cytoskeleton."
      Audhya A., Loewith R., Parsons A.B., Gao L., Tabuchi M., Zhou H., Boone C., Hall M.N., Emr S.D.
      EMBO J. 23:3747-3757(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION OF SLM1-SLM2.
    20. "Molecular organization of target of rapamycin complex 2."
      Wullschleger S., Loewith R., Oppliger W., Hall M.N.
      J. Biol. Chem. 280:30697-30704(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH LST8 AND TSC11.
    21. "The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-bisphosphate and TORC2."
      Fadri M., Daquinag A., Wang S., Xue T., Kunz J.
      Mol. Biol. Cell 16:1883-1900(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLM1 AND SLM2.
    22. "Tor2 directly phosphorylates the AGC kinase Ypk2 to regulate actin polarization."
      Kamada Y., Fujioka Y., Suzuki N.N., Inagaki F., Wullschleger S., Loewith R., Hall M.N., Ohsumi Y.
      Mol. Cell. Biol. 25:7239-7248(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION OF YPK2, MUTAGENESIS OF ASP-2298.
    23. "Mutual antagonism of TOR and calcineurin signaling."
      Mulet J.M., Martin D.E., Loewith R., Hall M.N.
      J. Biol. Chem. 281:33000-33007(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SLM1.
    24. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTOR2_YEAST
    AccessioniPrimary (citable) accession number: P32600
    Secondary accession number(s): D6VX00
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 134 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3