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P32600 (TOR2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TOR2
Synonyms:DRR2, TSC14
Ordered Locus Names:YKL203C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length2474 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.17 Ref.18 Ref.19 Ref.22 Ref.23

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.5

ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate. Ref.5

Subunit structure

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. Ref.15 Ref.16 Ref.20 Ref.21 Ref.23

Subcellular location

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. Ref.5 Ref.13 Ref.16

Sequence similarities

Belongs to the PI3/PI4-kinase family.

Contains 1 FAT domain.

Contains 1 FATC domain.

Contains 11 HEAT repeats.

Contains 1 PI3K/PI4K domain.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCell membrane
Membrane
Vacuole
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processTOR signaling

Inferred from mutant phenotype PubMed 12719473PubMed 8186460. Source: SGD

actin filament reorganization involved in cell cycle

Traceable author statement PubMed 9038344. Source: SGD

establishment or maintenance of actin cytoskeleton polarity

Inferred from mutant phenotype Ref.15. Source: SGD

negative regulation of autophagy

Inferred from genetic interaction PubMed 9461583. Source: SGD

phosphatidylinositol phosphorylation

Inferred from electronic annotation. Source: GOC

positive regulation of Rho guanyl-nucleotide exchange factor activity

Inferred from mutant phenotype PubMed 9038344. Source: SGD

positive regulation of Rho protein signal transduction

Inferred from mutant phenotype PubMed 9038344. Source: SGD

positive regulation of endocytosis

Inferred from mutant phenotype Ref.17. Source: SGD

regulation of cell cycle

Traceable author statement PubMed 9475724. Source: SGD

regulation of cell growth

Traceable author statement PubMed 11057898. Source: SGD

ribosome biogenesis

Inferred from mutant phenotype Ref.11. Source: SGD

   Cellular_componentTORC1 complex

Inferred from physical interaction Ref.15. Source: SGD

TORC2 complex

Inferred from physical interaction Ref.15. Source: SGD

extrinsic component of cytoplasmic side of plasma membrane

Inferred from direct assay Ref.16. Source: SGD

fungal-type vacuole membrane

Inferred from direct assay Ref.5. Source: SGD

   Molecular_function1-phosphatidylinositol 4-kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

drug binding

Inferred from electronic annotation. Source: InterPro

protein serine/threonine kinase activity

Inferred from direct assay Ref.22. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24742474Serine/threonine-protein kinase TOR2
PRO_0000088815

Regions

Repeat588 – 62639HEAT 1
Repeat636 – 67439HEAT 2
Repeat676 – 71035HEAT 3
Repeat756 – 79338HEAT 4
Repeat797 – 83539HEAT 5
Repeat841 – 87939HEAT 6
Repeat917 – 95539HEAT 7
Repeat1039 – 107638HEAT 8
Repeat1079 – 111638HEAT 9
Repeat1118 – 115538HEAT 10
Repeat1292 – 133140HEAT 11
Domain1338 – 1922585FAT
Domain2123 – 2441319PI3K/PI4K
Domain2442 – 247433FATC

Amino acid modifications

Modified residue101Phosphothreonine Ref.25

Experimental info

Mutagenesis19751S → I in TOR2-1; confers resistance to rapamycin. Ref.5
Mutagenesis21291G → R: Causes defect in receptor endocytosis. Ref.17
Mutagenesis22791D → A: Loss of function. Ref.5
Mutagenesis22981D → E: Loss of kinase activity. Ref.22
Sequence conflict14731Missing in CAA82048. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P32600 [UniParc].

Last modified January 9, 2007. Version 3.
Checksum: F2349690146058CF

FASTA2,474281,568
        10         20         30         40         50         60 
MNKYINKYTT PPNLLSLRQR AEGKHRTRKK LTHKSHSHDD EMSTTSNTDS NHNGPNDSGR 

        70         80         90        100        110        120 
VITGSAGHIG KISFVDSELD TTFSTLNLIF DKLKSDVPQE RASGANELST TLTSLAREVS 

       130        140        150        160        170        180 
AEQFQRFSNS LNNKIFELIH GFTSSEKIGG ILAVDTLISF YLSTEELPNQ TSRLANYLRV 

       190        200        210        220        230        240 
LIPSSDIEVM RLAANTLGRL TVPGGTLTSD FVEFEVRTCI DWLTLTADNN SSSSKLEYRR 

       250        260        270        280        290        300 
HAALLIIKAL ADNSPYLLYP YVNSILDNIW VPLRDAKLII RLDAAVALGK CLTIIQDRDP 

       310        320        330        340        350        360 
ALGKQWFQRL FQGCTHGLSL NTNDSVHATL LVFRELLSLK APYLRDKYDD IYKSTMKYKE 

       370        380        390        400        410        420 
YKFDVIRREV YAILPLLAAF DPAIFTKKYL DRIMVHYLRY LKNIDMNAAN NSDKPFILVS 

       430        440        450        460        470        480 
IGDIAFEVGS SISPYMTLIL DNIREGLRTK FKVRKQFEKD LFYCIGKLAC ALGPAFAKHL 

       490        500        510        520        530        540 
NKDLLNLMLN CPMSDHMQET LMILNEKIPS LESTVNSRIL NLLSISLSGE KFIQSNQYDF 

       550        560        570        580        590        600 
NNQFSIEKAR KSRNQSFMKK TGESNDDITD AQILIQCFKM LQLIHHQYSL TEFVRLITIS 

       610        620        630        640        650        660 
YIEHEDSSVR KLAALTSCDL FIKDDICKQT SVHALHSVSE VLSKLLMIAI TDPVAEIRLE 

       670        680        690        700        710        720 
ILQHLGSNFD PQLAQPDNLR LLFMALNDEI FGIQLEAIKI IGRLSSVNPA YVVPSLRKTL 

       730        740        750        760        770        780 
LELLTQLKFS NMPKKKEESA TLLCTLINSS DEVAKPYIDP ILDVILPKCQ DASSAVASTA 

       790        800        810        820        830        840 
LKVLGELSVV GGKEMTRYLK ELMPLIINTF QDQSNSFKRD AALTTLGQLA ASSGYVVGPL 

       850        860        870        880        890        900 
LDYPELLGIL INILKTENNP HIRRGTVRLI GILGALDPYK HREIEVTSNS KSSVEQNAPS 

       910        920        930        940        950        960 
IDIALLMQGV SPSNDEYYPT VVIHNLMKIL NDPSLSIHHT AAIQAIMHIF QNLGLRCVSF 

       970        980        990       1000       1010       1020 
LDQIIPGIIL VMRSCPPSQL DFYFQQLGSL ISIVKQHIRP HVEKIYGVIR EFFPIIKLQI 

      1030       1040       1050       1060       1070       1080 
TIISVIESIS KALEGEFKRF VPETLTFFLD ILENDQSNKR IVPIRILKSL VTFGPNLEDY 

      1090       1100       1110       1120       1130       1140 
SHLIMPIVVR MTEYSAGSLK KISIITLGRL AKNINLSEMS SRIVQALVRI LNNGDRELTK 

      1150       1160       1170       1180       1190       1200 
ATMNTLSLLL LQLGTDFVVF VPVINKALLR NRIQHSVYDQ LVNKLLNNEC LPTNIIFDKE 

      1210       1220       1230       1240       1250       1260 
NEVPERKNYE DEMQVTKLPV NQNILKNAWY CSQQKTKEDW QEWIRRLSIQ LLKESPSACL 

      1270       1280       1290       1300       1310       1320 
RSCSSLVSVY YPLARELFNA SFSSCWVELQ TSYQEDLIQA LCKALSSSEN PPEIYQMLLN 

      1330       1340       1350       1360       1370       1380 
LVEFMEHDDK PLPIPIHTLG KYAQKCHAFA KALHYKEVEF LEEPKNSTIE ALISINNQLH 

      1390       1400       1410       1420       1430       1440 
QTDSAIGILK HAQQHNELQL KETWYEKLQR WEDALAAYNE KEAAGEDSVE VMMGKLRSLY 

      1450       1460       1470       1480       1490       1500 
ALGEWEELSK LASEKWGTAK PEVKKAMAPL AAGAAWGLEQ WDEIAQYTSV MKSQSPDKEF 

      1510       1520       1530       1540       1550       1560 
YDAILCLHRN NFKKAEVHIF NARDLLVTEL SALVNESYNR AYNVVVRAQI IAELEEIIKY 

      1570       1580       1590       1600       1610       1620 
KKLPQNSDKR LTMRETWNTR LLGCQKNIDV WQRILRVRSL VIKPKEDAQV RIKFANLCRK 

      1630       1640       1650       1660       1670       1680 
SGRMALAKKV LNTLLEETDD PDHPNTAKAS PPVVYAQLKY LWATGLQDEA LKQLINFTSR 

      1690       1700       1710       1720       1730       1740 
MAHDLGLDPN NMIAQSVPQQ SKRVPRHVED YTKLLARCFL KQGEWRVCLQ PKWRLSNPDS 

      1750       1760       1770       1780       1790       1800 
ILGSYLLATH FDNTWYKAWH NWALANFEVI SMLTSVSKKK QEGSDASSVT DINEFDNGMI 

      1810       1820       1830       1840       1850       1860 
GVNTFDAKEV HYSSNLIHRH VIPAIKGFFH SISLSESSSL QDALRLLTLW FTFGGIPEAT 

      1870       1880       1890       1900       1910       1920 
QAMHEGFNLI QIGTWLEVLP QLISRIHQPN QIVSRSLLSL LSDLGKAHPQ ALVYPLMVAI 

      1930       1940       1950       1960       1970       1980 
KSESLSRQKA ALSIIEKMRI HSPVLVDQAE LVSHELIRMA VLWHEQWYEG LDDASRQFFG 

      1990       2000       2010       2020       2030       2040 
EHNTEKMFAA LEPLYEMLKR GPETLREISF QNSFGRDLND AYEWLMNYKK SKDVSNLNQA 

      2050       2060       2070       2080       2090       2100 
WDIYYNVFRK IGKQLPQLQT LELQHVSPKL LSAHDLELAV PGTRASGGKP IVKISKFEPV 

      2110       2120       2130       2140       2150       2160 
FSVISSKQRP RKFCIKGSDG KDYKYVLKGH EDIRQDSLVM QLFGLVNTLL QNDAECFRRH 

      2170       2180       2190       2200       2210       2220 
LDIQQYPAIP LSPKSGLLGW VPNSDTFHVL IREHREAKKI PLNIEHWVML QMAPDYDNLT 

      2230       2240       2250       2260       2270       2280 
LLQKVEVFTY ALNNTEGQDL YKVLWLKSRS SETWLERRTT YTRSLAVMSM TGYILGLGDR 

      2290       2300       2310       2320       2330       2340 
HPSNLMLDRI TGKVIHIDFG DCFEAAILRE KFPEKVPFRL TRMLTYAMEV SGIEGSFRIT 

      2350       2360       2370       2380       2390       2400 
CENVMKVLRD NKGSLMAILE AFAFDPLINW GFDLPTKKIE EETGIQLPVM NANELLSNGA 

      2410       2420       2430       2440       2450       2460 
ITEEEVQRVE NEHKNAIRNA RAMLVLKRIT DKLTGNDIRR FNDLDVPEQV DKLIQQATSV 

      2470 
ENLCQHYIGW CPFW 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X71416 Genomic DNA. Translation: CAA50548.1.
Z28203 Genomic DNA. Translation: CAA82048.1.
BK006944 Genomic DNA. Translation: DAA08966.1.
PIRS38040.
RefSeqNP_012719.2. NM_001179768.1.

3D structure databases

ProteinModelPortalP32600.
SMRP32600. Positions 754-871, 1955-2411, 2442-2474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33920. 249 interactions.
DIPDIP-2332N.
IntActP32600. 24 interactions.
MINTMINT-2843476.
STRING4932.YKL203C.

Proteomic databases

PaxDbP32600.
PeptideAtlasP32600.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL203C; YKL203C; YKL203C.
GeneID853632.
KEGGsce:YKL203C.

Organism-specific databases

CYGDYKL203c.
SGDS000001686. TOR2.

Phylogenomic databases

eggNOGCOG5032.
GeneTreeENSGT00720000108744.
HOGENOMHOG000163215.
KOK07203.
OMADPYKHKM.
OrthoDBEOG7Z3FCR.

Enzyme and pathway databases

BioCycYEAST:G3O-31962-MONOMER.
BRENDA2.7.1.137. 984.

Gene expression databases

GenevestigatorP32600.

Family and domain databases

Gene3D1.10.1070.11. 3 hits.
1.25.10.10. 6 hits.
InterProIPR011989. 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.
[Graphical view]
PANTHERPTHR11139:SF9. PTHR11139:SF9. 1 hit.
PfamPF11865. DUF3385. 1 hit.
PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08771. Rapamycin_bind. 1 hit.
[Graphical view]
SMARTSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF47212. SSF47212. 1 hit.
SSF48371. SSF48371. 9 hits.
SSF56112. SSF56112. 3 hits.
PROSITEPS51189. 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]
ProtoNetSearch...

Other

NextBio974511.
PROP32600.

Entry information

Entry nameTOR2_YEAST
AccessionPrimary (citable) accession number: P32600
Secondary accession number(s): D6VX00
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 9, 2007
Last modified: March 19, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families