P35169 (TOR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase TOR1
EC=2.7.11.1

Alternative name(s):
Dominant rapamycin resistance protein 1
Phosphatidylinositol kinase homolog TOR1
Target of rapamycin kinase 1

Gene names

Name:	TOR1
Synonyms:	DRR1
Ordered Locus Names:	YJR066W
ORF Names:	J1803

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	2470 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Phosphatidylinositol 3-kinase homolog, component of TORC1, which regulates multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls ribosome biogenesis via control of rRNA, ribosomal protein and tRNA gene expression, and rRNA processing. TORC1 positively controls protein biosynthesis by regulation of mRNA stability, translation initiation factor activity, and high-affinity amino acid permeases that serve to provide amino acids for use by the translation machinery. TORC1 also promotes growth by sequestering a number of nutrient and general stress-responsive transcription factors in the cytoplasm. TORC1 negatively controls macroautophagy, a process to recycle surplus cytoplasmic mass under nutrient starvation conditions. TORC1 controls many of these processes via TIP41-TAP42-mediated inhibition of the type 2A-related phosphatases PP2A and SIT4. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15 Ref.16 Ref.20
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.12
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. Ref.17 Ref.18
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.14 Ref.18
Miscellaneous	It may act on another substrate or phosphorylate a different position in the phosphatidylinositol ring. Present with 589 molecules/cell in log phase SD medium.
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.
Caution	It is uncertain whether Met-1 is the initiator.

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
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1 phase of mitotic cell cycle Inferred from mutant phenotype Ref.7. Source: SGD TOR signaling cascade Inferred from mutant phenotype PubMed 12719473Ref.2. Source: SGD fungal-type cell wall organization Inferred from mutant phenotype PubMed 14736892. Source: SGD meiosis Inferred from mutant phenotype PubMed 9096347. Source: SGD mitochondria-nucleus signaling pathway Inferred from mutant phenotype PubMed 11997479. Source: SGD negative regulation of autophagy Inferred from genetic interaction PubMed 9461583. Source: SGD regulation of cell cycle Inferred from mutant phenotype Ref.7. Source: SGD regulation of cell growth Inferred from mutant phenotype PubMed 12171921. Source: SGD response to DNA damage stimulus Inferred from mutant phenotype PubMed 17698581. Source: SGD ribosome biogenesis Inferred from mutant phenotype Ref.11. Source: SGD transcription of nuclear large rRNA transcript from RNA polymerase I promoter Inferred from mutant phenotype PubMed 16900101. Source: SGD
Cellular_component	Golgi membrane Inferred from direct assay PubMed 12719473. Source: SGD TORC1 complex Inferred from physical interaction Ref.17. Source: SGD endosome membrane Inferred from direct assay PubMed 12719473. Source: SGD extrinsic to internal side of plasma membrane Inferred from direct assay Ref.18. Source: SGD fungal-type vacuole membrane Inferred from direct assay PubMed 12719473. Source: SGD nucleus Inferred from direct assay PubMed 16900101. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW drug binding Inferred from electronic annotation. Source: InterPro protein kinase activity Inferred from mutant phenotype Ref.10. Source: SGD protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FMP48	P53233	3	EBI-19374,EBI-9664
KOG1	P38873	7	EBI-19374,EBI-24864
KSP1	P38691	2	EBI-19374,EBI-9937
LST8	P41318	5	EBI-19374,EBI-28598
MKS1	P34072	3	EBI-19374,EBI-10978
NNK1	P36003	3	EBI-19374,EBI-9796
NPR1	P22211	2	EBI-19374,EBI-12207
SKY1	Q03656	2	EBI-19374,EBI-9800
TCO89	Q08921	4	EBI-19374,EBI-37395

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2470

2470

Serine/threonine-protein kinase TOR1

PRO_0000088813

Regions

Repeat

114 – 151

38

HEAT 1

Repeat

249 – 286

38

HEAT 2

Repeat

627 – 663

37

HEAT 3

Repeat

664 – 701

38

HEAT 4

Repeat

747 – 784

38

HEAT 5

Repeat

788 – 826

39

HEAT 6

Repeat

832 – 870

39

HEAT 7

Repeat

908 – 946

39

HEAT 8

Repeat

950 – 987

38

HEAT 9

Repeat

1069 – 1107

39

HEAT 10

Repeat

1109 – 1147

39

HEAT 11

Domain

1331 – 1919

589

FAT

Domain

2125 – 2437

313

PI3K/PI4K

Domain

2438 – 2470

33

FATC

Region

1775 – 2157

383

Interaction with FKBP-rapamycin

Compositional bias

441 – 447

7

Arg/Lys-rich (basic)

Experimental info

Mutagenesis

1972

1

S → A: No effect. Ref.1 Ref.6

Mutagenesis

1972

1

S → E or I: Confers resistance to rapamycin. Abolishes interaction with FKBP-rapamycin. Ref.1 Ref.6

Mutagenesis

1972

1

S → N in DRR1-27; confers resistance to rapamycin. Ref.1 Ref.6

Mutagenesis

1972

1

S → R in DRR1-1; confers resistance to rapamycin. Abolishes interaction with FKBP-rapamycin. Ref.1 Ref.6

Mutagenesis

2275

1

D → A: Abolishes protein kinase activity. Ref.12

Mutagenesis

2276

1

R → P: Abolishes rapamycin-resistance of mutants E-1972; I-1972 and R-1972. Ref.6

Mutagenesis

2294

1

D → E: Abolishes rapamycin-resistance of mutants E-1972; I-1972 and R-1972. Ref.6

Sequence conflict

58

1

D → G in AAB66881. Ref.1

Sequence conflict

115

1

V → I in AAB66881. Ref.1

Sequence conflict

133

1

S → N in AAB66881. Ref.1

Sequence conflict

231

1

A → R in CAA52849. Ref.2

Sequence conflict

396

1

N → K in AAB66881. Ref.1

Sequence conflict

396

1

N → K in CAA52849. Ref.2

Sequence conflict

547

1

N → S in AAB66881. Ref.1

Sequence conflict

547

1

N → S in CAA52849. Ref.2

Sequence conflict

675

1

T → I in CAA52849. Ref.2

Sequence conflict

1292

1

G → E in CAA52849. Ref.2

Sequence conflict

1436

1

G → A in CAA52849. Ref.2

Sequence conflict

1468

1

A → R in AAB66881. Ref.1

Sequence conflict

1468

1

A → R in CAA52849. Ref.2

Sequence conflict

1469 – 1471

3

WGL → GGS in CAA52849. Ref.2

Sequence conflict

1478 – 1479

2

EQ → DE in CAA52849. Ref.2

Sequence conflict

1590

1

V → I in CAA52849. Ref.2

Sequence conflict

1632 – 1642

11

NDPSLPNTFKA → TILVYQIRSKP in CAA52849. Ref.2

Sequence conflict

1640

1

F → V in AAB66881. Ref.1

Sequence conflict

1844

1

L → S in CAA52849. Ref.2

Sequence conflict

2202

1

H → Q in AAB66881. Ref.1

Sequence conflict

2414

1

K → R in AAB66881. Ref.1

Sequence conflict

2414

1

K → R in CAA52849. Ref.2

Secondary structure

1

.

.

.

2470

Helix Strand Turn

Details...

Helix

2444 – 2460

17

Sequences

	Sequence		Length	Mass (Da)
	P35169 [UniParc]. Last modified November 1, 1995. Version 3. Checksum: ACB1781B9963BB1E	FASTA	2,470	281,140
	10 20 30 40 50 60 MEPHEEQIWK SKLLKAANND MDMDRNVPLA PNLNVNMNMK MNASRNGDEF GLTSSRFDGV 70 80 90 100 110 120 VIGSNGDVNF KPILEKIFRE LTSDYKEERK LASISLFDLL VSLEHELSIE EFQAVSNDIN 130 140 150 160 170 180 NKILELVHTK KTSTRVGAVL SIDTLISFYA YTERLPNETS RLAGYLRGLI PSNDVEVMRL 190 200 210 220 230 240 AAKTLGKLAV PGGTYTSDFV EFEIKSCLEW LTASTEKNSF SSSKPDHAKH AALLIITALA 250 260 270 280 290 300 ENCPYLLYQY LNSILDNIWR ALRDPHLVIR IDASITLAKC LSTLRNRDPQ LTSQWVQRLA 310 320 330 340 350 360 TSCEYGFQVN TLECIHASLL VYKEILFLKD PFLNQVFDQM CLNCIAYENH KAKMIREKIY 370 380 390 400 410 420 QIVPLLASFN PQLFAGKYLH QIMDNYLEIL TNAPANKIPH LKDDKPQILI SIGDIAYEVG 430 440 450 460 470 480 PDIAPYVKQI LDYIEHDLQT KFKFRKKFEN EIFYCIGRLA VPLGPVLGKL LNRNILDLMF 490 500 510 520 530 540 KCPLSDYMQE TFQILTERIP SLGPKINDEL LNLVCSTLSG TPFIQPGSPM EIPSFSRERA 550 560 570 580 590 600 REWRNKNILQ KTGESNDDNN DIKIIIQAFR MLKNIKSRFS LVEFVRIVAL SYIEHTDPRV 610 620 630 640 650 660 RKLAALTSCE IYVKDNICKQ TSLHSLNTVS EVLSKLLAIT IADPLQDIRL EVLKNLNPCF 670 680 690 700 710 720 DPQLAQPDNL RLLFTALHDE SFNIQSVAME LVGRLSSVNP AYVIPSIRKI LLELLTKLKF 730 740 750 760 770 780 STSSREKEET ASLLCTLIRS SKDVAKPYIE PLLNVLLPKF QDTSSTVAST ALRTIGELSV 790 800 810 820 830 840 VGGEDMKIYL KDLFPLIIKT FQDQSNSFKR EAALKALGQL AASSGYVIDP LLDYPELLGI 850 860 870 880 890 900 LVNILKTENS QNIRRQTVTL IGILGAIDPY RQKEREVTST TDISTEQNAP PIDIALLMQG 910 920 930 940 950 960 MSPSNDEYYT TVVIHCLLKI LKDPSLSSYH TAVIQAIMHI FQTLGLKCVS FLDQIIPTIL 970 980 990 1000 1010 1020 DVMRTCSQSL LEFYFQQLCS LIIIVRQHIR PHVDSIFQAI KDFSSVAKLQ ITLVSVIEAI 1030 1040 1050 1060 1070 1080 SKALEGEFKR LVPLTLTLFL VILENDKSSD KVLSRRVLRL LESFGPNLEG YSHLITPKIV 1090 1100 1110 1120 1130 1140 QMAEFTSGNL QRSAIITIGK LAKDVDLFEM SSRIVHSLLR VLSSTTSDEL SKVIMNTLSL 1150 1160 1170 1180 1190 1200 LLIQMGTSFA IFIPVINEVL MKKHIQHTIY DDLTNRILNN DVLPTKILEA NTTDYKPAEQ 1210 1220 1230 1240 1250 1260 MEAADAGVAK LPINQSVLKS AWNSSQQRTK EDWQEWSKRL SIQLLKESPS HALRACSNLA 1270 1280 1290 1300 1310 1320 SMYYPLAKEL FNTAFACVWT ELYSQYQEDL IGSLCIALSS PLNPPEIHQT LLNLVEFMEH 1330 1340 1350 1360 1370 1380 DDKALPIPTQ SLGEYAERCH AYAKALHYKE IKFIKEPENS TIESLISINN QLNQTDAAIG 1390 1400 1410 1420 1430 1440 ILKHAQQHHS LQLKETWFEK LERWEDALHA YNEREKAGDT SVSVTLGKMR SLHALGEWEQ 1450 1460 1470 1480 1490 1500 LSQLAARKWK VSKLQTKKLI APLAAGAAWG LGEWDMLEQY ISVMKPKSPD KEFFDAILYL 1510 1520 1530 1540 1550 1560 HKNDYDNASK HILNARDLLV TEISALINES YNRAYSVIVR TQIITEFEEI IKYKQLPPNS 1570 1580 1590 1600 1610 1620 EKKLHYQNLW TKRLLGCQKN VDLWQRVLRV RSLVIKPKQD LQIWIKFANL CRKSGRMRLA 1630 1640 1650 1660 1670 1680 NKALNMLLEG GNDPSLPNTF KAPPPVVYAQ LKYIWATGAY KEALNHLIGF TSRLAHDLGL 1690 1700 1710 1720 1730 1740 DPNNMIAQSV KLSSASTAPY VEEYTKLLAR CFLKQGEWRI ATQPNWRNTN PDAILGSYLL 1750 1760 1770 1780 1790 1800 ATHFDKNWYK AWHNWALANF EVISMVQEET KLNGGKNDDD DDTAVNNDNV RIDGSILGSG 1810 1820 1830 1840 1850 1860 SLTINGNRYP LELIQRHVVP AIKGFFHSIS LLETSCLQDT LRLLTLLFNF GGIKEVSQAM 1870 1880 1890 1900 1910 1920 YEGFNLMKIE NWLEVLPQLI SRIHQPDPTV SNSLLSLLSD LGKAHPQALV YPLTVAIKSE 1930 1940 1950 1960 1970 1980 SVSRQKAALS IIEKIRIHSP VLVNQAELVS HELIRVAVLW HELWYEGLED ASRQFFVEHN 1990 2000 2010 2020 2030 2040 IEKMFSTLEP LHKHLGNEPQ TLSEVSFQKS FGRDLNDAYE WLNNYKKSKD INNLNQAWDI 2050 2060 2070 2080 2090 2100 YYNVFRKITR QIPQLQTLDL QHVSPQLLAT HDLELAVPGT YFPGKPTIRI AKFEPLFSVI 2110 2120 2130 2140 2150 2160 SSKQRPRKFS IKGSDGKDYK YVLKGHEDIR QDSLVMQLFG LVNTLLKNDS ECFKRHLDIQ 2170 2180 2190 2200 2210 2220 QYPAIPLSPK SGLLGWVPNS DTFHVLIREH RDAKKIPLNI EHWVMLQMAP DYENLTLLQK 2230 2240 2250 2260 2270 2280 IEVFTYALDN TKGQDLYKIL WLKSRSSETW LERRTTYTRS LAVMSMTGYI LGLGDRHPSN 2290 2300 2310 2320 2330 2340 LMLDRITGKV IHIDFGDCFE AAILREKYPE KVPFRLTRML TYAMEVSGIE GSFRITCENV 2350 2360 2370 2380 2390 2400 MRVLRDNKES LMAILEAFAL DPLIHWGFDL PPQKLTEQTG IPLPLINPSE LLRKGAITVE 2410 2420 2430 2440 2450 2460 EAANMEAEQQ NETKNARAML VLRRITDKLT GNDIKRFNEL DVPEQVDKLI QQATSIERLC 2470 QHYIGWCPFW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Dominant missense mutations in a novel yeast protein related to mammalian phosphatidylinositol 3-kinase and VPS34 abrogate rapamycin cytotoxicity." Cafferkey R., Young P.R., McLaughlin M.M., Bergsma D.J., Koltin Y., Sathe G.M., Faucette L., Eng W.-K., Johnson R.K., Livi G.P. Mol. Cell. Biol. 13:6012-6023(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF SER-1972. Strain: RC11-8D.
[2]	"TOR1 and TOR2 are structurally and functionally similar but not identical phosphatidylinositol kinase homologues in yeast." Helliwell S.B., Wagner P., Kunz J., Deuter-Reinhard M., Henriquez R., Hall M.N. Mol. Biol. Cell 5:105-118(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: JK9-3D.
[3]	"Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading frames and a gene cluster with a counterpart on chromosome XI." Huang M.-E., Manus V., Chuat J.-C., Galibert F. Yeast 12:869-875(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"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, MUTAGENESIS OF SER-1972; ARG-2276 AND ASP-2294, INTERACTION WITH FPR1.
[7]	"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.
[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]	"Protein kinase activity and identification of a toxic effector domain of the target of rapamycin TOR proteins in yeast." Alarcon C.M., Heitman J., Cardenas M.E. Mol. Biol. Cell 10:2531-2546(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-2275.
[13]	"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.
[14]	"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.
[15]	"Tor-mediated induction of autophagy via an Apg1 protein kinase complex." Kamada Y., Funakoshi T., Shintani T., Nagano K., Ohsumi M., Ohsumi Y. J. Cell Biol. 150:1507-1513(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN AUTOPHAGY.
[16]	"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.
[17]	"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.
[18]	"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 KOG1 AND LST8.
[19]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[20]	"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.
[21]	"The solution structure of the FATC domain of the protein kinase target of rapamycin suggests a role for redox-dependent structural and cellular stability." Dames S.A., Mulet J.M., Rathgeb-Szabo K., Hall M.N., Grzesiek S. J. Biol. Chem. 280:20558-20564(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 2438-2470.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L19540 Genomic DNA. Translation: AAB66881.1.
X74857 Genomic DNA. Translation: CAA52849.1.
Z49566 Genomic DNA. Translation: CAA89594.1.
L47993 Genomic DNA. Translation: AAB39292.1.
BK006943 Genomic DNA. Translation: DAA08853.1.

PIR

S57085.

RefSeq

NP_012600.1. NM_001181724.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W1N	NMR	-	A	2438-2470	[»]
2KIO	NMR	-	A	2438-2470	[»]
2KIT	NMR	-	A	2438-2470	[»]

ProteinModelPortal

P35169.

SMR

P35169. Positions 673-699, 766-821, 1603-1628, 1952-2051, 2091-2345, 2438-2470.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-917N.

IntAct

P35169. 33 interactions.

MINT

MINT-2782002.

STRING

4932.YJR066W.

Proteomic databases

PaxDb

P35169.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YJR066W; YJR066W; YJR066W.

GeneID

853529.

KEGG

sce:YJR066W.

Organism-specific databases

CYGD

YJR066w.

SGD

S000003827. TOR1.

Phylogenomic databases

eggNOG

COG5032.

GeneTree

ENSGT00700000104444.

HOGENOM

HOG000163215.

KO

K07203.

OMA

MEANIRE.

OrthoDB

EOG4ZCXCJ.

Enzyme and pathway databases

BRENDA

2.7.1.137. 984.

Gene expression databases

Genevestigator

P35169.

GermOnline

YJR066W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.10.1070.11. 3 hits.
1.25.10.10. 5 hits.

InterPro

IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024585. DUF3385_TOR.
IPR003152. FATC.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR009076. Rapamycin-bd_dom.
IPR026683. TOR/Smg1.
[Graphical view]

PANTHER

PTHR11139:SF9. PTHR11139:SF9. 1 hit.

Pfam

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]

SMART

SM00146. PI3Kc. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.
SSF47212. FRAP_FKBP12_bind. 1 hit.
SSF56112. Kinase_like. 1 hit.

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

EvolutionaryTrace

P35169.

NextBio

974224.

Entry information

Entry name

TOR1_YEAST

Accession

Primary (citable) accession number: P35169
Secondary accession number(s): D6VWN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 129 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program