Reviewed, UniProtKB/Swiss-Prot P32600 (TOR2_YEAST)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase TOR2
    EC=2.7.11.1
    EC=2.7.1.67
Alternative name(s):
    Phosphatidylinositol 4-kinase TOR2
      Short name=PtdIns-4-kinase TOR2
      Short name=PI4-kinase TOR2
      Short name=PI4K TOR2
    Target of rapamycin kinase 2
    Dominant rapamycin resistance protein 2
    Temperature-sensitive CSG2 suppressor protein 14

Gene names

Name:	TOR2
Synonyms:	DRR2, TSC14
Ordered Locus Names:	YKL203C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	2474 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.16 Ref.17 Ref.18 Ref.21 Ref.22
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.4 ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate. Ref.4
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.22 Ref.14 Ref.15 Ref.19 Ref.20
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 membanes. Ref.4 Ref.15 Ref.12
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 process	Cell cycle
Cellular component	Cell membrane Membrane Vacuole
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	G1 phase of mitotic cell cycle Traceable author statement. Source: SGD Rho protein signal transduction Inferred from mutant phenotype. Source: SGD TOR signaling pathway Ref.14 Inferred from mutant phenotype. Source: SGD actin filament reorganization during cell cycle Traceable author statement. Source: SGD endocytosis Ref.16 Inferred from mutant phenotype. Source: SGD establishment or maintenance of actin cytoskeleton polarity Ref.14 Inferred from mutant phenotype. Source: SGD regulation of cell cycle Traceable author statement. Source: SGD regulation of cell growth Traceable author statement. Source: SGD ribosome biogenesis Ref.10 Inferred from mutant phenotype. Source: SGD
Cellular component	TORC1 complex Ref.14 Inferred from physical interaction. Source: SGD TORC2 complex Ref.14 Inferred from physical interaction. Source: SGD extrinsic to internal side of plasma membrane Ref.15 Inferred from direct assay. Source: SGD membrane fraction Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD vacuolar membrane Ref.4 Inferred from direct assay. Source: SGD
Molecular function	1-phosphatidylinositol 4-kinase activity Inferred from electronic annotation. Source: EC ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.9 Ref.15 Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Ref.21 Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AVO1	Q08236	1	EBI-19385,EBI-29284
AVO2	Q04749	1	EBI-19385,EBI-28131
BIT61	P47041	1	EBI-19385,EBI-25889
KOG1	P38873	1	EBI-19385,EBI-24864
LST8	P41318	1	EBI-19385,EBI-28598
TAP42	Q04372	1	EBI-19385,EBI-18926
TSC11	P40061	1	EBI-19385,EBI-22621

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2474	2474	Serine/threonine-protein kinase TOR2		PRO_0000088815
Regions
	Repeat	588 – 626	39	HEAT 1
	Repeat	636 – 674	39	HEAT 2
	Repeat	676 – 710	35	HEAT 3
	Repeat	756 – 793	38	HEAT 4
	Repeat	797 – 835	39	HEAT 5
	Repeat	841 – 879	39	HEAT 6
	Repeat	917 – 955	39	HEAT 7
	Repeat	1039 – 1076	38	HEAT 8
	Repeat	1079 – 1116	38	HEAT 9
	Repeat	1118 – 1155	38	HEAT 10
	Repeat	1292 – 1331	40	HEAT 11
	Domain	1338 – 1922	585	FAT
	Domain	2123 – 2441	319	PI3K/PI4K
	Domain	2442 – 2474	33	FATC
Amino acid modifications
	Modified residue	10	1	Phosphothreonine Ref.23
	Modified residue	2013	1	Phosphoserine Ref.23
Experimental info
	Mutagenesis	1975	1	S → I in TOR2-1; confers resistance to rapamycin. Ref.4
	Mutagenesis	2129	1	G → R: Causes defect in receptor endocytosis. Ref.16
	Mutagenesis	2279	1	D → A: Loss of function. Ref.4
	Mutagenesis	2298	1	D → E: Loss of kinase activity. Ref.21
	Sequence conflict	1473	1	Missing in CAA82048. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P32600-1 [UniParc]. Last modified January 9, 2007. Version 3. Checksum: F2349690146058CF	FASTA	2,474	281,568
	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

References

	« Hide 'large scale' referencesShow '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: 8387896] [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: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"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: 7606777] [Abstract] Cited for: FUNCTION.
[4]	"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: 8846782] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-1975 AND ASP-2279, CATALYTIC ACTIVITY.
[5]	"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: 8741837] [Abstract] Cited for: FUNCTION.
[6]	"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: 8943012] [Abstract] Cited for: FUNCTION.
[7]	"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: 9843498] [Abstract] Cited for: FUNCTION.
[8]	"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: 9539725] [Abstract] Cited for: FUNCTION.
[9]	"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: 10329624] [Abstract] Cited for: FUNCTION.
[10]	"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: 10198052] [Abstract] Cited for: FUNCTION.
[11]	"The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors." Beck T., Hall M.N. Nature 402:689-692(1999) [PubMed: 10604478] [Abstract] Cited for: FUNCTION.
[12]	"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: 10973982] [Abstract] Cited for: SUBCELLULAR LOCATION.
[13]	"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: 11741537] [Abstract] Cited for: FUNCTION.
[14]	"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: 12408816] [Abstract] Cited for: SUBUNIT.
[15]	"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: 12631735] [Abstract] Cited for: SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH LST8.
[16]	"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: 14593073] [Abstract] Cited for: FUNCTION IN RECEPTER ENDOCYTOSIS, MUTAGENESIS OF GLY-2129.
[17]	"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: 15620355] [Abstract] Cited for: FUNCTION.
[18]	"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: 15372071] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION OF SLM1-SLM2.
[19]	"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: 16002396] [Abstract] Cited for: SUBUNIT, INTERACTION WITH LST8 AND TSC11.
[20]	"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: 15689497] [Abstract] Cited for: INTERACTION WITH SLM1 AND SLM2.
[21]	"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: 16055732] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION OF YPK2, MUTAGENESIS OF ASP-2298.
[22]	"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: 16959779] [Abstract] Cited for: FUNCTION, INTERACTION WITH SLM1.
[23]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10 AND SER-2013, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X71416 Genomic DNA. Translation: CAA50548.1. Z28203 Genomic DNA. Translation: CAA82048.1.
PIR	S38040.
RefSeq	NP_012719.2.
3D structure databases
HSSP	HSSP built from PDB template 1AUE based on UniProtKB P42345.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2332N.
IntAct	P32600. 13 interactions.
STRING	P32600.
Proteomic databases
PeptideAtlas	P32600.
PRIDE	P32600.
Genome annotation databases
Ensembl	YKL203C; YKL203C; YKL203C; Saccharomyces cerevisiae. [Genome view]
GeneID	853632.
GenomeReviews	Gene locus YKL203C in contig Y13137_GR.
KEGG	sce:YKL203C.
NMPDR	fig|4932.3.peg.3697.
Organism-specific databases
CYGD	YKL203c.
SGD	S000001686. TOR2.
Phylogenomic databases
HOGENOM	P32600.
OMA	WRDESED.
Enzyme and pathway databases
BRENDA	2.7.1.137. 250. 2.7.1.67. 250. 2.7.11.1. 250.
Gene expression databases
ArrayExpress	P32600.
Genevestigator	P32600.
GermOnline	YKL203C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011989. ARM-like. IPR003152. FATC. IPR009076. FKBP_rapamycin-assoc_FKBP12-bd. IPR000357. HEAT. IPR000403. PI3/4_kinase_cat. IPR018936. PI3/4_kinase_CS. IPR003151. PIK-rel_kinase_FAT. IPR014009. PIK_FAT. [Graphical view]
Gene3D	G3DSA:1.25.10.10. ARM-like. 1 hit. G3DSA:1.20.120.150. FRAP_FKBP12_bd. 1 hit. G3DSA:1.10.1070.11. PI3/4_kinase_cat. 1 hit.
Pfam	PF02259. FAT. 1 hit. PF02260. FATC. 1 hit. PF02985. HEAT. 2 hits. PF00454. PI3_PI4_kinase. 1 hit. PF08771. Rapamycin_bind. 1 hit. [Graphical view]
SMART	SM00146. PI3Kc. 1 hit. [Graphical view]
PROSITE	PS51189. FAT. 1 hit. PS51190. FATC. 1 hit. PS50077. HEAT_REPEAT. False negative. PS00915. PI3_4_KINASE_1. 1 hit. PS00916. PI3_4_KINASE_2. 1 hit. PS50290. PI3_4_KINASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	974511.

Entry information

Entry name

TOR2_YEAST

Accession

Primary (citable) accession number: P32600

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	January 9, 2007
Last modified:	November 3, 2009
This is version 85 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)