Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P32600

- TOR2_YEAST

UniProt

P32600 - TOR2_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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 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
Complete GO annotation...

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_219346. HSF1-dependent transactivation.
REACT_252465. mTOR signalling.

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
Complete GO annotation...

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 265-291, 590-623, 678-709, 758-832, 1086-1111, 1408-1446, 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.
GeneTreeiENSGT00770000120840.
HOGENOMiHOG000163215.
InParanoidiP32600.
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

        10         20         30         40         50
MNKYINKYTT PPNLLSLRQR AEGKHRTRKK LTHKSHSHDD EMSTTSNTDS
60 70 80 90 100
NHNGPNDSGR VITGSAGHIG KISFVDSELD TTFSTLNLIF DKLKSDVPQE
110 120 130 140 150
RASGANELST TLTSLAREVS AEQFQRFSNS LNNKIFELIH GFTSSEKIGG
160 170 180 190 200
ILAVDTLISF YLSTEELPNQ TSRLANYLRV LIPSSDIEVM RLAANTLGRL
210 220 230 240 250
TVPGGTLTSD FVEFEVRTCI DWLTLTADNN SSSSKLEYRR HAALLIIKAL
260 270 280 290 300
ADNSPYLLYP YVNSILDNIW VPLRDAKLII RLDAAVALGK CLTIIQDRDP
310 320 330 340 350
ALGKQWFQRL FQGCTHGLSL NTNDSVHATL LVFRELLSLK APYLRDKYDD
360 370 380 390 400
IYKSTMKYKE YKFDVIRREV YAILPLLAAF DPAIFTKKYL DRIMVHYLRY
410 420 430 440 450
LKNIDMNAAN NSDKPFILVS IGDIAFEVGS SISPYMTLIL DNIREGLRTK
460 470 480 490 500
FKVRKQFEKD LFYCIGKLAC ALGPAFAKHL NKDLLNLMLN CPMSDHMQET
510 520 530 540 550
LMILNEKIPS LESTVNSRIL NLLSISLSGE KFIQSNQYDF NNQFSIEKAR
560 570 580 590 600
KSRNQSFMKK TGESNDDITD AQILIQCFKM LQLIHHQYSL TEFVRLITIS
610 620 630 640 650
YIEHEDSSVR KLAALTSCDL FIKDDICKQT SVHALHSVSE VLSKLLMIAI
660 670 680 690 700
TDPVAEIRLE ILQHLGSNFD PQLAQPDNLR LLFMALNDEI FGIQLEAIKI
710 720 730 740 750
IGRLSSVNPA YVVPSLRKTL LELLTQLKFS NMPKKKEESA TLLCTLINSS
760 770 780 790 800
DEVAKPYIDP ILDVILPKCQ DASSAVASTA LKVLGELSVV GGKEMTRYLK
810 820 830 840 850
ELMPLIINTF QDQSNSFKRD AALTTLGQLA ASSGYVVGPL LDYPELLGIL
860 870 880 890 900
INILKTENNP HIRRGTVRLI GILGALDPYK HREIEVTSNS KSSVEQNAPS
910 920 930 940 950
IDIALLMQGV SPSNDEYYPT VVIHNLMKIL NDPSLSIHHT AAIQAIMHIF
960 970 980 990 1000
QNLGLRCVSF LDQIIPGIIL VMRSCPPSQL DFYFQQLGSL ISIVKQHIRP
1010 1020 1030 1040 1050
HVEKIYGVIR EFFPIIKLQI TIISVIESIS KALEGEFKRF VPETLTFFLD
1060 1070 1080 1090 1100
ILENDQSNKR IVPIRILKSL VTFGPNLEDY SHLIMPIVVR MTEYSAGSLK
1110 1120 1130 1140 1150
KISIITLGRL AKNINLSEMS SRIVQALVRI LNNGDRELTK ATMNTLSLLL
1160 1170 1180 1190 1200
LQLGTDFVVF VPVINKALLR NRIQHSVYDQ LVNKLLNNEC LPTNIIFDKE
1210 1220 1230 1240 1250
NEVPERKNYE DEMQVTKLPV NQNILKNAWY CSQQKTKEDW QEWIRRLSIQ
1260 1270 1280 1290 1300
LLKESPSACL RSCSSLVSVY YPLARELFNA SFSSCWVELQ TSYQEDLIQA
1310 1320 1330 1340 1350
LCKALSSSEN PPEIYQMLLN LVEFMEHDDK PLPIPIHTLG KYAQKCHAFA
1360 1370 1380 1390 1400
KALHYKEVEF LEEPKNSTIE ALISINNQLH QTDSAIGILK HAQQHNELQL
1410 1420 1430 1440 1450
KETWYEKLQR WEDALAAYNE KEAAGEDSVE VMMGKLRSLY ALGEWEELSK
1460 1470 1480 1490 1500
LASEKWGTAK PEVKKAMAPL AAGAAWGLEQ WDEIAQYTSV MKSQSPDKEF
1510 1520 1530 1540 1550
YDAILCLHRN NFKKAEVHIF NARDLLVTEL SALVNESYNR AYNVVVRAQI
1560 1570 1580 1590 1600
IAELEEIIKY KKLPQNSDKR LTMRETWNTR LLGCQKNIDV WQRILRVRSL
1610 1620 1630 1640 1650
VIKPKEDAQV RIKFANLCRK SGRMALAKKV LNTLLEETDD PDHPNTAKAS
1660 1670 1680 1690 1700
PPVVYAQLKY LWATGLQDEA LKQLINFTSR MAHDLGLDPN NMIAQSVPQQ
1710 1720 1730 1740 1750
SKRVPRHVED YTKLLARCFL KQGEWRVCLQ PKWRLSNPDS ILGSYLLATH
1760 1770 1780 1790 1800
FDNTWYKAWH NWALANFEVI SMLTSVSKKK QEGSDASSVT DINEFDNGMI
1810 1820 1830 1840 1850
GVNTFDAKEV HYSSNLIHRH VIPAIKGFFH SISLSESSSL QDALRLLTLW
1860 1870 1880 1890 1900
FTFGGIPEAT QAMHEGFNLI QIGTWLEVLP QLISRIHQPN QIVSRSLLSL
1910 1920 1930 1940 1950
LSDLGKAHPQ ALVYPLMVAI KSESLSRQKA ALSIIEKMRI HSPVLVDQAE
1960 1970 1980 1990 2000
LVSHELIRMA VLWHEQWYEG LDDASRQFFG EHNTEKMFAA LEPLYEMLKR
2010 2020 2030 2040 2050
GPETLREISF QNSFGRDLND AYEWLMNYKK SKDVSNLNQA WDIYYNVFRK
2060 2070 2080 2090 2100
IGKQLPQLQT LELQHVSPKL LSAHDLELAV PGTRASGGKP IVKISKFEPV
2110 2120 2130 2140 2150
FSVISSKQRP RKFCIKGSDG KDYKYVLKGH EDIRQDSLVM QLFGLVNTLL
2160 2170 2180 2190 2200
QNDAECFRRH LDIQQYPAIP LSPKSGLLGW VPNSDTFHVL IREHREAKKI
2210 2220 2230 2240 2250
PLNIEHWVML QMAPDYDNLT LLQKVEVFTY ALNNTEGQDL YKVLWLKSRS
2260 2270 2280 2290 2300
SETWLERRTT YTRSLAVMSM TGYILGLGDR HPSNLMLDRI TGKVIHIDFG
2310 2320 2330 2340 2350
DCFEAAILRE KFPEKVPFRL TRMLTYAMEV SGIEGSFRIT CENVMKVLRD
2360 2370 2380 2390 2400
NKGSLMAILE AFAFDPLINW GFDLPTKKIE EETGIQLPVM NANELLSNGA
2410 2420 2430 2440 2450
ITEEEVQRVE NEHKNAIRNA RAMLVLKRIT DKLTGNDIRR FNDLDVPEQV
2460 2470
DKLIQQATSV ENLCQHYIGW CPFW
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 265-291, 590-623, 678-709, 758-832, 1086-1111, 1408-1446, 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 ENSGT00770000120840.
HOGENOMi HOG000163215.
InParanoidi P32600.
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_219346. HSF1-dependent transactivation.
REACT_252465. mTOR signalling.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 136 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