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Protein

Serine/threonine-protein kinase TOR1

Gene

TOR1

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 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 (PubMed:10198052, PubMed:10329624, PubMed:10604478, PubMed:10995454, 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).12 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • macromolecular complex binding Source: InterPro
  • protein kinase activity Source: SGD
  • protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  • cellular response to DNA damage stimulus Source: SGD
  • DNA repair Source: GO_Central
  • fungal-type cell wall organization Source: SGD
  • meiotic nuclear division Source: SGD
  • mitochondria-nucleus signaling pathway Source: SGD
  • negative regulation of autophagy Source: SGD
  • peptidyl-serine phosphorylation Source: SGD
  • regulation of cell cycle Source: SGD
  • regulation of cell growth Source: SGD
  • regulation of snRNA pseudouridine synthesis Source: SGD
  • regulation of sphingolipid biosynthetic process Source: SGD
  • ribosome biogenesis Source: SGD
  • TOR signaling Source: SGD
  • transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: SGD
  • translational initiation 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-31699-MONOMER.
BRENDAi2.7.1.137. 984.

Names & Taxonomyi

Protein namesi
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 namesi
Name:TOR1
Synonyms:DRR1
Ordered Locus Names:YJR066W
ORF Names:J1803
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR066W.
SGDiS000003827. TOR1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1972S → A: No effect. 2 Publications1
Mutagenesisi1972S → E or I: Confers resistance to rapamycin. Abolishes interaction with FKBP-rapamycin. 2 Publications1
Mutagenesisi1972S → N in DRR1-27; confers resistance to rapamycin. 2 Publications1
Mutagenesisi1972S → R in DRR1-1; confers resistance to rapamycin. Abolishes interaction with FKBP-rapamycin. 2 Publications1
Mutagenesisi2275D → A: Abolishes protein kinase activity. 1 Publication1
Mutagenesisi2276R → P: Abolishes rapamycin-resistance of mutants E-1972; I-1972 and R-1972. 1 Publication1
Mutagenesisi2294D → E: Abolishes rapamycin-resistance of mutants E-1972; I-1972 and R-1972. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000888131 – 2470Serine/threonine-protein kinase TOR1Add BLAST2470

Proteomic databases

MaxQBiP35169.
PRIDEiP35169.

PTM databases

iPTMnetiP35169.

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FMP48P532333EBI-19374,EBI-9664
KOG1P388737EBI-19374,EBI-24864
KSP1P386912EBI-19374,EBI-9937
LST8P413185EBI-19374,EBI-28598
MKS1P340723EBI-19374,EBI-10978
NNK1P360033EBI-19374,EBI-9796
NPR1P222112EBI-19374,EBI-12207
SKY1Q036562EBI-19374,EBI-9800
TCO89Q089214EBI-19374,EBI-37395

Protein-protein interaction databases

BioGridi33823. 377 interactors.
DIPiDIP-917N.
IntActiP35169. 37 interactors.
MINTiMINT-2782002.

Structurei

Secondary structure

12470
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2444 – 2460Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W1NNMR-A2438-2470[»]
2KIONMR-A2438-2470[»]
2KITNMR-A2438-2470[»]
ProteinModelPortaliP35169.
SMRiP35169.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35169.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati114 – 151HEAT 1Add BLAST38
Repeati249 – 286HEAT 2Add BLAST38
Repeati627 – 663HEAT 3Add BLAST37
Repeati664 – 701HEAT 4Add BLAST38
Repeati747 – 784HEAT 5Add BLAST38
Repeati788 – 826HEAT 6Add BLAST39
Repeati832 – 870HEAT 7Add BLAST39
Repeati908 – 946HEAT 8Add BLAST39
Repeati950 – 987HEAT 9Add BLAST38
Repeati1069 – 1107HEAT 10Add BLAST39
Repeati1109 – 1147HEAT 11Add BLAST39
Domaini1331 – 1919FATPROSITE-ProRule annotationAdd BLAST589
Domaini2125 – 2437PI3K/PI4KPROSITE-ProRule annotationAdd BLAST313
Domaini2438 – 2470FATCPROSITE-ProRule annotationAdd BLAST33

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1775 – 2157Interaction with FKBP-rapamycinAdd BLAST383

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi441 – 447Arg/Lys-rich (basic)7

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

GeneTreeiENSGT00860000133827.
HOGENOMiHOG000163215.
InParanoidiP35169.
KOiK07203.
OMAiIRIDASI.
OrthoDBiEOG092C00HJ.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.25.10.10. 5 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. 6 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35169-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPHEEQIWK SKLLKAANND MDMDRNVPLA PNLNVNMNMK MNASRNGDEF
60 70 80 90 100
GLTSSRFDGV VIGSNGDVNF KPILEKIFRE LTSDYKEERK LASISLFDLL
110 120 130 140 150
VSLEHELSIE EFQAVSNDIN NKILELVHTK KTSTRVGAVL SIDTLISFYA
160 170 180 190 200
YTERLPNETS RLAGYLRGLI PSNDVEVMRL AAKTLGKLAV PGGTYTSDFV
210 220 230 240 250
EFEIKSCLEW LTASTEKNSF SSSKPDHAKH AALLIITALA ENCPYLLYQY
260 270 280 290 300
LNSILDNIWR ALRDPHLVIR IDASITLAKC LSTLRNRDPQ LTSQWVQRLA
310 320 330 340 350
TSCEYGFQVN TLECIHASLL VYKEILFLKD PFLNQVFDQM CLNCIAYENH
360 370 380 390 400
KAKMIREKIY QIVPLLASFN PQLFAGKYLH QIMDNYLEIL TNAPANKIPH
410 420 430 440 450
LKDDKPQILI SIGDIAYEVG PDIAPYVKQI LDYIEHDLQT KFKFRKKFEN
460 470 480 490 500
EIFYCIGRLA VPLGPVLGKL LNRNILDLMF KCPLSDYMQE TFQILTERIP
510 520 530 540 550
SLGPKINDEL LNLVCSTLSG TPFIQPGSPM EIPSFSRERA REWRNKNILQ
560 570 580 590 600
KTGESNDDNN DIKIIIQAFR MLKNIKSRFS LVEFVRIVAL SYIEHTDPRV
610 620 630 640 650
RKLAALTSCE IYVKDNICKQ TSLHSLNTVS EVLSKLLAIT IADPLQDIRL
660 670 680 690 700
EVLKNLNPCF DPQLAQPDNL RLLFTALHDE SFNIQSVAME LVGRLSSVNP
710 720 730 740 750
AYVIPSIRKI LLELLTKLKF STSSREKEET ASLLCTLIRS SKDVAKPYIE
760 770 780 790 800
PLLNVLLPKF QDTSSTVAST ALRTIGELSV VGGEDMKIYL KDLFPLIIKT
810 820 830 840 850
FQDQSNSFKR EAALKALGQL AASSGYVIDP LLDYPELLGI LVNILKTENS
860 870 880 890 900
QNIRRQTVTL IGILGAIDPY RQKEREVTST TDISTEQNAP PIDIALLMQG
910 920 930 940 950
MSPSNDEYYT TVVIHCLLKI LKDPSLSSYH TAVIQAIMHI FQTLGLKCVS
960 970 980 990 1000
FLDQIIPTIL DVMRTCSQSL LEFYFQQLCS LIIIVRQHIR PHVDSIFQAI
1010 1020 1030 1040 1050
KDFSSVAKLQ ITLVSVIEAI SKALEGEFKR LVPLTLTLFL VILENDKSSD
1060 1070 1080 1090 1100
KVLSRRVLRL LESFGPNLEG YSHLITPKIV QMAEFTSGNL QRSAIITIGK
1110 1120 1130 1140 1150
LAKDVDLFEM SSRIVHSLLR VLSSTTSDEL SKVIMNTLSL LLIQMGTSFA
1160 1170 1180 1190 1200
IFIPVINEVL MKKHIQHTIY DDLTNRILNN DVLPTKILEA NTTDYKPAEQ
1210 1220 1230 1240 1250
MEAADAGVAK LPINQSVLKS AWNSSQQRTK EDWQEWSKRL SIQLLKESPS
1260 1270 1280 1290 1300
HALRACSNLA SMYYPLAKEL FNTAFACVWT ELYSQYQEDL IGSLCIALSS
1310 1320 1330 1340 1350
PLNPPEIHQT LLNLVEFMEH DDKALPIPTQ SLGEYAERCH AYAKALHYKE
1360 1370 1380 1390 1400
IKFIKEPENS TIESLISINN QLNQTDAAIG ILKHAQQHHS LQLKETWFEK
1410 1420 1430 1440 1450
LERWEDALHA YNEREKAGDT SVSVTLGKMR SLHALGEWEQ LSQLAARKWK
1460 1470 1480 1490 1500
VSKLQTKKLI APLAAGAAWG LGEWDMLEQY ISVMKPKSPD KEFFDAILYL
1510 1520 1530 1540 1550
HKNDYDNASK HILNARDLLV TEISALINES YNRAYSVIVR TQIITEFEEI
1560 1570 1580 1590 1600
IKYKQLPPNS EKKLHYQNLW TKRLLGCQKN VDLWQRVLRV RSLVIKPKQD
1610 1620 1630 1640 1650
LQIWIKFANL CRKSGRMRLA NKALNMLLEG GNDPSLPNTF KAPPPVVYAQ
1660 1670 1680 1690 1700
LKYIWATGAY KEALNHLIGF TSRLAHDLGL DPNNMIAQSV KLSSASTAPY
1710 1720 1730 1740 1750
VEEYTKLLAR CFLKQGEWRI ATQPNWRNTN PDAILGSYLL ATHFDKNWYK
1760 1770 1780 1790 1800
AWHNWALANF EVISMVQEET KLNGGKNDDD DDTAVNNDNV RIDGSILGSG
1810 1820 1830 1840 1850
SLTINGNRYP LELIQRHVVP AIKGFFHSIS LLETSCLQDT LRLLTLLFNF
1860 1870 1880 1890 1900
GGIKEVSQAM YEGFNLMKIE NWLEVLPQLI SRIHQPDPTV SNSLLSLLSD
1910 1920 1930 1940 1950
LGKAHPQALV YPLTVAIKSE SVSRQKAALS IIEKIRIHSP VLVNQAELVS
1960 1970 1980 1990 2000
HELIRVAVLW HELWYEGLED ASRQFFVEHN IEKMFSTLEP LHKHLGNEPQ
2010 2020 2030 2040 2050
TLSEVSFQKS FGRDLNDAYE WLNNYKKSKD INNLNQAWDI YYNVFRKITR
2060 2070 2080 2090 2100
QIPQLQTLDL QHVSPQLLAT HDLELAVPGT YFPGKPTIRI AKFEPLFSVI
2110 2120 2130 2140 2150
SSKQRPRKFS IKGSDGKDYK YVLKGHEDIR QDSLVMQLFG LVNTLLKNDS
2160 2170 2180 2190 2200
ECFKRHLDIQ QYPAIPLSPK SGLLGWVPNS DTFHVLIREH RDAKKIPLNI
2210 2220 2230 2240 2250
EHWVMLQMAP DYENLTLLQK IEVFTYALDN TKGQDLYKIL WLKSRSSETW
2260 2270 2280 2290 2300
LERRTTYTRS LAVMSMTGYI LGLGDRHPSN LMLDRITGKV IHIDFGDCFE
2310 2320 2330 2340 2350
AAILREKYPE KVPFRLTRML TYAMEVSGIE GSFRITCENV MRVLRDNKES
2360 2370 2380 2390 2400
LMAILEAFAL DPLIHWGFDL PPQKLTEQTG IPLPLINPSE LLRKGAITVE
2410 2420 2430 2440 2450
EAANMEAEQQ NETKNARAML VLRRITDKLT GNDIKRFNEL DVPEQVDKLI
2460 2470
QQATSIERLC QHYIGWCPFW
Length:2,470
Mass (Da):281,140
Last modified:November 1, 1995 - v3
Checksum:iACB1781B9963BB1E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti58D → G in AAB66881 (PubMed:8413204).Curated1
Sequence conflicti115V → I in AAB66881 (PubMed:8413204).Curated1
Sequence conflicti133S → N in AAB66881 (PubMed:8413204).Curated1
Sequence conflicti231A → R in CAA52849 (PubMed:8186460).Curated1
Sequence conflicti396N → K in AAB66881 (PubMed:8413204).Curated1
Sequence conflicti396N → K in CAA52849 (PubMed:8186460).Curated1
Sequence conflicti547N → S in AAB66881 (PubMed:8413204).Curated1
Sequence conflicti547N → S in CAA52849 (PubMed:8186460).Curated1
Sequence conflicti675T → I in CAA52849 (PubMed:8186460).Curated1
Sequence conflicti1292G → E in CAA52849 (PubMed:8186460).Curated1
Sequence conflicti1436G → A in CAA52849 (PubMed:8186460).Curated1
Sequence conflicti1468A → R in AAB66881 (PubMed:8413204).Curated1
Sequence conflicti1468A → R in CAA52849 (PubMed:8186460).Curated1
Sequence conflicti1469 – 1471WGL → GGS in CAA52849 (PubMed:8186460).Curated3
Sequence conflicti1478 – 1479EQ → DE in CAA52849 (PubMed:8186460).Curated2
Sequence conflicti1590V → I in CAA52849 (PubMed:8186460).Curated1
Sequence conflicti1632 – 1642NDPSLPNTFKA → TILVYQIRSKP in CAA52849 (PubMed:8186460).CuratedAdd BLAST11
Sequence conflicti1640F → V in AAB66881 (PubMed:8413204).Curated1
Sequence conflicti1844L → S in CAA52849 (PubMed:8186460).Curated1
Sequence conflicti2202H → Q in AAB66881 (PubMed:8413204).Curated1
Sequence conflicti2414K → R in AAB66881 (PubMed:8413204).Curated1
Sequence conflicti2414K → R in CAA52849 (PubMed:8186460).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS57085.
RefSeqiNP_012600.1. NM_001181724.1.

Genome annotation databases

EnsemblFungiiYJR066W; YJR066W; YJR066W.
GeneIDi853529.
KEGGisce:YJR066W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS57085.
RefSeqiNP_012600.1. NM_001181724.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W1NNMR-A2438-2470[»]
2KIONMR-A2438-2470[»]
2KITNMR-A2438-2470[»]
ProteinModelPortaliP35169.
SMRiP35169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33823. 377 interactors.
DIPiDIP-917N.
IntActiP35169. 37 interactors.
MINTiMINT-2782002.

PTM databases

iPTMnetiP35169.

Proteomic databases

MaxQBiP35169.
PRIDEiP35169.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR066W; YJR066W; YJR066W.
GeneIDi853529.
KEGGisce:YJR066W.

Organism-specific databases

EuPathDBiFungiDB:YJR066W.
SGDiS000003827. TOR1.

Phylogenomic databases

GeneTreeiENSGT00860000133827.
HOGENOMiHOG000163215.
InParanoidiP35169.
KOiK07203.
OMAiIRIDASI.
OrthoDBiEOG092C00HJ.

Enzyme and pathway databases

BioCyciYEAST:G3O-31699-MONOMER.
BRENDAi2.7.1.137. 984.

Miscellaneous databases

EvolutionaryTraceiP35169.
PROiP35169.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.25.10.10. 5 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. 6 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTOR1_YEAST
AccessioniPrimary (citable) accession number: P35169
Secondary accession number(s): D6VWN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 169 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.1 Publication

Caution

It is uncertain whether Met-1 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.