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Protein

Target of rapamycin

Gene

Tor

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Promotes cell and tissue growth, maintains tissue homeostatis and controls responses to environmental stress and aging. Regulates growth during animal development by coupling growth factor signaling to nutrient availability. Central regulators of autophagy. May be involved in atg1 phosphorylation. May also be involved, directly or indirectly, in the control of neuronal function. Phosphorylates S6K/p70S6K, in vitro. May regulate the activity of S6K. Overexpression inhibits growth and reduces cell size. Affects the timing of neuronal cell differentiation. Hyperactivation of the signaling leads to accelerated differentiation, whereas inhibition of the signaling retards differentiation. Thus, in addition to controlling growth of the cell in which it resides, it can also influence growth of distant cells and organs during development via a humoral mechanism. In short, during development, it primarily controls growth, whereas in the adult, where there is relatively little growth, it controls aging and other aspects of nutrient-related physiology. Rag GTPases act as activators of TORC1 in response to amino acid signals.9 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: GO_Central
  • macromolecular complex binding Source: InterPro
  • protein kinase activity Source: FlyBase
  • protein self-association Source: FlyBase
  • protein serine/threonine kinase activity Source: FlyBase

GO - Biological processi

  • apical protein localization Source: FlyBase
  • axon guidance Source: FlyBase
  • cell cycle Source: UniProtKB-KW
  • cellular response to DNA damage stimulus Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • detection of nutrient Source: FlyBase
  • determination of adult lifespan Source: FlyBase
  • DNA repair Source: GO_Central
  • endocytic recycling Source: FlyBase
  • germarium-derived cystoblast division Source: FlyBase
  • gonad development Source: FlyBase
  • growth Source: FlyBase
  • multicellular organism growth Source: FlyBase
  • myoblast fusion Source: FlyBase
  • negative regulation of macroautophagy Source: FlyBase
  • phosphorylation Source: FlyBase
  • phototaxis Source: FlyBase
  • positive regulation of cell growth Source: FlyBase
  • positive regulation of cell size Source: FlyBase
  • positive regulation of multicellular organism growth Source: FlyBase
  • positive regulation of organ growth Source: FlyBase
  • positive regulation of protein phosphorylation Source: FlyBase
  • positive regulation of ribosome biogenesis Source: FlyBase
  • protein phosphorylation Source: FlyBase
  • regulation of cell growth Source: FlyBase
  • regulation of reactive oxygen species metabolic process Source: FlyBase
  • regulation of response to drug Source: FlyBase
  • regulation of terminal button organization Source: FlyBase
  • response to nutrient Source: FlyBase
  • somatic muscle development Source: FlyBase
  • synaptic growth at neuromuscular junction Source: FlyBase
  • terminal branching, open tracheal system Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-1257604. PIP3 activates AKT signaling.
R-DME-1632852. Macroautophagy.
R-DME-165159. mTOR signalling.
R-DME-166208. mTORC1-mediated signalling.
R-DME-3371571. HSF1-dependent transactivation.
R-DME-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-DME-389357. CD28 dependent PI3K/Akt signaling.
R-DME-5218920. VEGFR2 mediated vascular permeability.
R-DME-5628897. TP53 Regulates Metabolic Genes.
SignaLinkiQ9VK45.

Names & Taxonomyi

Protein namesi
Recommended name:
Target of rapamycin (EC:2.7.1.-)
Gene namesi
Name:Tor
ORF Names:CG5092
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0021796. Tor.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Not lethal. Displays phenotypes characteristic of amino acid deprivation, including reduced nucleolar size, lipid vesicle aggregation in the larval fat body, and a cell type-specific pattern of cell cycle arrest that can be bypassed by overexpression of the S-phase regulator cyclin E. Reach only the size of second instar larvae, at which point they undergo cell cycle arrest.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1956 – 19561S → T: Rapamycin resistance and loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24702470Target of rapamycinPRO_0000377458Add
BLAST

Proteomic databases

PaxDbiQ9VK45.
PRIDEiQ9VK45.

Expressioni

Inductioni

By PI3K/Akt signaling, or by nutrients such as amino acids, and by high cellular energy levels.1 Publication

Gene expression databases

BgeeiQ9VK45.
ExpressionAtlasiQ9VK45. differential.
GenevisibleiQ9VK45. DM.

Interactioni

Subunit structurei

May be part of a minimal complex, TORC1, consisting of tor, raptor and lst8. May be part of a minimal complex, TORC2, consisting of tor, rictor and lst8 (By similarity). Self-associates; assembles into homomultimeric complexes. Component of a multiprotein complex.By similarity1 Publication

GO - Molecular functioni

  • protein self-association Source: FlyBase

Protein-protein interaction databases

BioGridi70789. 10 interactions.
IntActiQ9VK45. 16 interactions.
STRINGi7227.FBpp0080003.

Structurei

3D structure databases

ProteinModelPortaliQ9VK45.
SMRiQ9VK45. Positions 1939-2033.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati172 – 20938HEAT 1Add
BLAST
Repeati746 – 78540HEAT 2Add
BLAST
Repeati791 – 82939HEAT 3Add
BLAST
Repeati835 – 87339HEAT 4Add
BLAST
Repeati962 – 99938HEAT 5Add
BLAST
Repeati1043 – 108038HEAT 6Add
BLAST
Repeati1083 – 112240HEAT 7Add
BLAST
Repeati1124 – 116037HEAT 8Add
BLAST
Domaini1349 – 1903555FATPROSITE-ProRule annotationAdd
BLAST
Repeati1407 – 144034TPR 1Add
BLAST
Repeati1712 – 175140TPR 2Add
BLAST
Repeati1854 – 189138HEAT 9Add
BLAST
Domaini2103 – 2470368PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST
Domaini2438 – 247033FATCPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi293 – 2975Poly-Ser

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 9 HEAT repeats.Curated
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
Contains 2 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG0891. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00830000128322.
InParanoidiQ9VK45.
KOiK07203.
OMAiVRCIPVD.
OrthoDBiEOG7CCBQ4.
PhylomeDBiQ9VK45.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.25.10.10. 6 hits.
1.25.40.10. 2 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.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR11139:SF9. PTHR11139:SF9. 2 hits.
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]
SMARTiSM01346. DUF3385. 1 hit.
SM01343. FATC. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF47212. SSF47212. 1 hit.
SSF48371. SSF48371. 4 hits.
SSF56112. SSF56112. 2 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.
PS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VK45-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTTSVVQQF VNGLKSRNRN VQNKATQDLL FYVKTELREM SQEELAQFFD
60 70 80 90 100
EFDHHIFTMV NATDINEKKG GALAMKCLIN CEGSLTARKG ISPYLNRLRD
110 120 130 140 150
LLLINDVSVM EIAARSLVKL ANMPTSKGAD SFDFDIKKAF EVLRGERQEY
160 170 180 190 200
RRHSAVFILR ELAIALPTYF YQHILTFFEV IFNAIFDPKP AIRESAGEAL
210 220 230 240 250
RAALIVTAQR ESTKQSSEPQ WYRICYDEAN GSFNADLGSS KDQKGVTRDD
260 270 280 290 300
RIHGGLVVFN ELFRCANATW ERRYTSLKTL FPKTQHNKFL EASSSSSMGS
310 320 330 340 350
QLNTLVPRLK VPFIDKLGST QTHLGEGEHH KGVAKFASHN VLESAYAQEI
360 370 380 390 400
LQEHYTSICD NVLEQRTSKS PYVQQALLQI LPRLAAFNRA VFVEKYLQTC
410 420 430 440 450
VSHLMQILRG KEKDRTVAYI TIGYMAVAVQ SAIEVHLSSI MTSVKVALPS
460 470 480 490 500
KDLTSKRKVP VDPAVFACIT LLAHAVKSEI ADDVKDILEQ MFYTGLSPAL
510 520 530 540 550
TVCLRELSEN VPQLKSAITE GLIGILSQVL MNKAAILPYT ALPTIAIDGS
560 570 580 590 600
LMQNGDGATT VLALKTLGTF NFEEQNMLDF VQRCADYFIV HEQQEIRLEA
610 620 630 640 650
VQTCTRLLKL AVQSSESMEN SKTLSDTVSH VIERLLMVAI TDMDCNVRIR
660 670 680 690 700
ILRSLDETFD GKLAQPESLN SLFITLHDEI FEIRELAMVT IGRLSSINPA
710 720 730 740 750
YVMPKLRTTM IELITDLKYS GMSRNKEQSA KMLDHLVIST PRLISSYMNP
760 770 780 790 800
ILKALVPKLH EPESNPGVIL NVLRTIGDLA EVNGGSDEME LWADDLLSIL
810 820 830 840 850
LEMLGDAGSP DKRGVALWTL GQLISATGRV VTPYHKYPVL IDILINFLKT
860 870 880 890 900
EQRRSIRRET IRVLGLLGAM DPYKHKMNKG LIDSQKDNVL IAYSDGKVDE
910 920 930 940 950
SQDISTAELL VNMGNALDEY YPAVAIAALM RILRDPTLST RHTSVVQAVT
960 970 980 990 1000
FIFQSLGIKC VPYLAQVLPN LLDNVRTADN NLREFLFQQL AILVAFVKLH
1010 1020 1030 1040 1050
IISYMGDIFK LIKEFWTINT PLQNTLINLI EQIAVALGCE FRDYLAELIP
1060 1070 1080 1090 1100
QILRVLQHDN SKDRMVTRRL LQALQKFGST LGYYLPLILP PIVKLFDSPY
1110 1120 1130 1140 1150
VPQQVSMVAL ETINNLACQL DFTDFSSRII HPLVRVLDAE PELRDQAMTT
1160 1170 1180 1190 1200
LRSLAKQLGK KYLVFVPMVQ RTLNKHRIVD PEYEELLSKI KSCSTLADSY
1210 1220 1230 1240 1250
GAGESELRPS RFKNNEPFVT DRNSNNKNLQ VTTNELRTAW QVTRRVSKDD
1260 1270 1280 1290 1300
WVEWLKRLSI GLLKESPSHA LRACRSLAQE YDTLLRDLFN AAFISCWTEL
1310 1320 1330 1340 1350
SPDLKNELTQ SLIQALQVTD MPEITQTILN LAEFMEHCDR DPIPIETKLL
1360 1370 1380 1390 1400
GTRAMACRAY AKALRYKEEE FLLREDSQVF ESLILINNKL QQREAAEGLL
1410 1420 1430 1440 1450
TRYRNAANEL NVQGRWYEKL HNWDEALEHY ERNLKTDSSD LEARLGHMRC
1460 1470 1480 1490 1500
LEALGDWSEL SNVTKHEWEN FGTEAKSRAG PLAAVAAWGL QDWEAMREYV
1510 1520 1530 1540 1550
RCIPEDTQDG SYYRAVLAVH HDDFETAQRL IDETRDLLDT ELTSMAGESY
1560 1570 1580 1590 1600
ERAYGAMVCV QMLAELEEVI QYKLIPERRE PLKTMWWKRL QGGQRLVEDW
1610 1620 1630 1640 1650
RRIIQVHSLV VKPHEDIHTW LKYASLCRKS GSLHLSHKTL VMLLGTDPKL
1660 1670 1680 1690 1700
NPNQPLPCNQ PQVTYAYTKY MAANNQLQEA YEQLTHFVST YSQELSCLPP
1710 1720 1730 1740 1750
EALKQQDQRL MARCYLRMAT WQNKLQDSIR PDAIQGALEC FEKATSYDPN
1760 1770 1780 1790 1800
WYKAWHLWAY MNFKVVQAQK SALDKQQPPG ASMGMTMGSG LDSDLMIIQR
1810 1820 1830 1840 1850
YAVPAVQGFF RSISLIKGNS LQDTLRLLTL WFDYGNHAEV YEALLSGMKL
1860 1870 1880 1890 1900
IEINTWLQVI PQLIARIDTH RQLVGQLIHQ LLMDIGKNHP QALVYPLTVA
1910 1920 1930 1940 1950
SKSASLARRN AAFKILDSMR KHSPTLVEQA VMCSEELIRV AILWHEQWHE
1960 1970 1980 1990 2000
GLEEASRLYF GDRNVKGMFE ILEPLHAMLE RGPQTLKETS FSQAYGRELT
2010 2020 2030 2040 2050
EAYEWSQRYK TSAVVMDLDR AWDIYYHVFQ KISRQLPQLT SLELPYVSPK
2060 2070 2080 2090 2100
LMTCKDLELA VPGSYNPGQE LIRISIIKTN LQVITSKQRP RKLCIRGSNG
2110 2120 2130 2140 2150
KDYMYLLKGH EDLRQDERVM QLFSLVNTLL LDDPDTFRRN LAIQRYAVIP
2160 2170 2180 2190 2200
LSTNSGLIGW VPHCDTLHTL IRDYRDKKKV PLNQEHRTML NFAPDYDHLT
2210 2220 2230 2240 2250
LMQKVEVFEH ALGQTQGDDL AKLLWLKSPS SELWFERRNN YTRSLAVMSM
2260 2270 2280 2290 2300
VGYILGLGDR HPSNLMLDRM SGKILHIDFG DCFEVAMTRE KFPEKIPFRL
2310 2320 2330 2340 2350
TRMLIKAMEV TGIEGTYRRT CESVMLVLRR NKDSLMAVLE AFVYDPLLNW
2360 2370 2380 2390 2400
RLLDVDKKGN DAVAGAGAPG GRGGSGMQDS LSNSVEDSLP MAKSKPYDPT
2410 2420 2430 2440 2450
LQQGGLHNNV ADETNSKASQ VIKRVKCKLT GTDFQTEKSV NEQSQVELLI
2460 2470
QQATNNENLC QCYIGWCPFW
Length:2,470
Mass (Da):281,033
Last modified:May 1, 2000 - v1
Checksum:i5D78D2ECC07C7FF9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF53237.1.
RefSeqiNP_524891.1. NM_080152.3.
UniGeneiDm.1502.

Genome annotation databases

EnsemblMetazoaiFBtr0080422; FBpp0080003; FBgn0021796.
GeneIDi47396.
KEGGidme:Dmel_CG5092.
UCSCiCG5092-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF53237.1.
RefSeqiNP_524891.1. NM_080152.3.
UniGeneiDm.1502.

3D structure databases

ProteinModelPortaliQ9VK45.
SMRiQ9VK45. Positions 1939-2033.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi70789. 10 interactions.
IntActiQ9VK45. 16 interactions.
STRINGi7227.FBpp0080003.

Proteomic databases

PaxDbiQ9VK45.
PRIDEiQ9VK45.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080422; FBpp0080003; FBgn0021796.
GeneIDi47396.
KEGGidme:Dmel_CG5092.
UCSCiCG5092-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0021796. Tor.

Phylogenomic databases

eggNOGiKOG0891. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00830000128322.
InParanoidiQ9VK45.
KOiK07203.
OMAiVRCIPVD.
OrthoDBiEOG7CCBQ4.
PhylomeDBiQ9VK45.

Enzyme and pathway databases

ReactomeiR-DME-1257604. PIP3 activates AKT signaling.
R-DME-1632852. Macroautophagy.
R-DME-165159. mTOR signalling.
R-DME-166208. mTORC1-mediated signalling.
R-DME-3371571. HSF1-dependent transactivation.
R-DME-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-DME-389357. CD28 dependent PI3K/Akt signaling.
R-DME-5218920. VEGFR2 mediated vascular permeability.
R-DME-5628897. TP53 Regulates Metabolic Genes.
SignaLinkiQ9VK45.

Miscellaneous databases

GenomeRNAii47396.
PROiQ9VK45.

Gene expression databases

BgeeiQ9VK45.
ExpressionAtlasiQ9VK45. differential.
GenevisibleiQ9VK45. DM.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.25.10.10. 6 hits.
1.25.40.10. 2 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.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR11139:SF9. PTHR11139:SF9. 2 hits.
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]
SMARTiSM01346. DUF3385. 1 hit.
SM01343. FATC. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF47212. SSF47212. 1 hit.
SSF48371. SSF48371. 4 hits.
SSF56112. SSF56112. 2 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.
PS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. "Genetic and biochemical characterization of dTOR, the Drosophila homolog of the target of rapamycin."
    Oldham S., Montagne J., Radimerski T., Thomas G., Hafen E.
    Genes Dev. 14:2689-2694(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-1956.
  4. "Regulation of cellular growth by the Drosophila target of rapamycin dTOR."
    Zhang H., Stallock J.P., Ng J.C., Reinhard C., Neufeld T.P.
    Genes Dev. 14:2712-2724(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  5. "A nutrient sensor mechanism controls Drosophila growth."
    Colombani J., Raisin S., Pantalacci S., Radimerski T., Montagne J., Leopold P.
    Cell 114:739-749(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Insulin/IGF and target of rapamycin signaling: a TOR de force in growth control."
    Oldham S., Hafen E.
    Trends Cell Biol. 13:79-85(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Temporal control of differentiation by the insulin receptor/tor pathway in Drosophila."
    Bateman J.M., McNeill H.
    Cell 119:87-96(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "TOR signaling in growth and metabolism."
    Wullschleger S., Loewith R., Hall M.N.
    Cell 124:471-484(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Drosophila target of rapamycin kinase functions as a multimer."
    Zhang Y., Billington C.J. Jr., Pan D., Neufeld T.P.
    Genetics 172:355-362(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  10. "Regulation of TORC1 by Rag GTPases in nutrient response."
    Kim E., Goraksha-Hicks P., Li L., Neufeld T.P., Guan K.L.
    Nat. Cell Biol. 10:935-945(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Integration of Insulin receptor/Foxo signaling and dMyc activity during muscle growth regulates body size in Drosophila."
    Demontis F., Perrimon N.
    Development 136:983-993(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  12. "Insulin/TOR signaling in growth and homeostasis: a view from the fly world."
    Grewal S.S.
    Int. J. Biochem. Cell Biol. 41:1006-1010(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  13. "An Atg1/Atg13 complex with multiple roles in TOR-mediated autophagy regulation."
    Chang Y.Y., Neufeld T.P.
    Mol. Biol. Cell 20:2004-2014(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiTOR_DROME
AccessioniPrimary (citable) accession number: Q9VK45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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.