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Protein

Serine/threonine-protein kinase TOR2

Gene

TOR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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 (PubMed:10198052, PubMed:10329624, PubMed:10604478, PubMed:11741537, PubMed:15620355, PubMed:7606777, PubMed:8741837, PubMed:9539725, PubMed:9843498). In nutrient rich conditions, responsible for the phosphorylation of AGC S6 kinase (S6K) YPK3, activating YPK3 kinase activity and promoting phosphorylation of ribosomal protein S6 (PubMed:25767889). Phosphorylates kinase SCH9 at 6 amino acids in the C-terminus, activating SCH9 kinase activity to properly regulate ribosome biogenesis, translation initiation, and entry into stationary phase (PubMed:17560372). 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 (PubMed:14593073, PubMed:15372071, PubMed:16055732, PubMed:16959779, PubMed:8846782, PubMed:8943012).17 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

GO - Biological processi

  • actin filament reorganization involved in cell cycle Source: SGD
  • cytoskeleton organization Source: SGD
  • DNA repair Source: GO_Central
  • establishment or maintenance of actin cytoskeleton polarity Source: SGD
  • negative regulation of autophagy Source: SGD
  • positive regulation of endocytosis Source: SGD
  • positive regulation of Rho guanyl-nucleotide exchange factor activity Source: SGD
  • positive regulation of Rho protein signal transduction Source: SGD
  • protein phosphorylation Source: SGD
  • regulation of cell cycle Source: SGD
  • regulation of cell growth Source: SGD
  • regulation of snRNA pseudouridine synthesis Source: SGD
  • ribosome biogenesis Source: SGD
  • signal transduction Source: SGD
  • 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.
ReactomeiR-SCE-3371571. HSF1-dependent transactivation.
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

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
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL203C.
SGDiS000001686. TOR2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • extrinsic component of cytoplasmic side of plasma membrane Source: SGD
  • fungal-type vacuole membrane Source: SGD
  • nucleus Source: GO_Central
  • plasma membrane Source: SGD
  • TORC1 complex Source: SGD
  • TORC2 complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1975S → I in TOR2-1; confers resistance to rapamycin. 1 Publication1
Mutagenesisi2129G → R: Causes defect in receptor endocytosis. 1 Publication1
Mutagenesisi2279D → A: Loss of function. 1 Publication1
Mutagenesisi2298D → E: Loss of kinase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000888151 – 2474Serine/threonine-protein kinase TOR2Add BLAST2474

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei10PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32600.
PRIDEiP32600.

PTM databases

iPTMnetiP32600.

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. 252 interactors.
DIPiDIP-2332N.
IntActiP32600. 24 interactors.
MINTiMINT-2843476.

Structurei

3D structure databases

ProteinModelPortaliP32600.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati588 – 626HEAT 1Add BLAST39
Repeati636 – 674HEAT 2Add BLAST39
Repeati676 – 710HEAT 3Add BLAST35
Repeati756 – 793HEAT 4Add BLAST38
Repeati797 – 835HEAT 5Add BLAST39
Repeati841 – 879HEAT 6Add BLAST39
Repeati917 – 955HEAT 7Add BLAST39
Repeati1039 – 1076HEAT 8Add BLAST38
Repeati1079 – 1116HEAT 9Add BLAST38
Repeati1118 – 1155HEAT 10Add BLAST38
Repeati1292 – 1331HEAT 11Add BLAST40
Domaini1338 – 1922FATPROSITE-ProRule annotationAdd BLAST585
Domaini2123 – 2441PI3K/PI4KPROSITE-ProRule annotationAdd BLAST319
Domaini2442 – 2474FATCPROSITE-ProRule annotationAdd BLAST33

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

GeneTreeiENSGT00860000133856.
HOGENOMiHOG000163215.
InParanoidiP32600.
KOiK07203.
OMAiVRCIPVD.
OrthoDBiEOG092C00HJ.

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_dom.
IPR009076. FRB_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR026683. TOR.
[Graphical view]
PANTHERiPTHR11139:SF9. PTHR11139:SF9. 2 hits.
PfamiPF11865. DUF3385. 1 hit.
PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF08771. FRB_dom. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTiSM01346. DUF3385. 1 hit.
SM01343. FATC. 1 hit.
SM00146. 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)DescriptionActionsGraphical viewLength
Sequence conflicti1473Missing in CAA82048 (PubMed:8196765).Curated1

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.
PIRiS38040.
RefSeqiNP_012719.2. NM_001179768.1.

3D structure databases

ProteinModelPortaliP32600.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33920. 252 interactors.
DIPiDIP-2332N.
IntActiP32600. 24 interactors.
MINTiMINT-2843476.

PTM databases

iPTMnetiP32600.

Proteomic databases

MaxQBiP32600.
PRIDEiP32600.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YKL203C.
SGDiS000001686. TOR2.

Phylogenomic databases

GeneTreeiENSGT00860000133856.
HOGENOMiHOG000163215.
InParanoidiP32600.
KOiK07203.
OMAiVRCIPVD.
OrthoDBiEOG092C00HJ.

Enzyme and pathway databases

BioCyciYEAST:G3O-31962-MONOMER.
BRENDAi2.7.1.137. 984.
ReactomeiR-SCE-3371571. HSF1-dependent transactivation.
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiP32600.

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_dom.
IPR009076. FRB_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR026683. TOR.
[Graphical view]
PANTHERiPTHR11139:SF9. PTHR11139:SF9. 2 hits.
PfamiPF11865. DUF3385. 1 hit.
PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF08771. FRB_dom. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTiSM01346. DUF3385. 1 hit.
SM01343. FATC. 1 hit.
SM00146. 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]
ProtoNetiSearch...

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 30, 2016
This is version 157 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.