UniProtKB - P35169 (TOR1_YEAST)
Protein
Serine/threonine-protein kinase TOR1
Gene
TOR1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
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
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
Catalytic activityi
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- protein-containing 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
- cellular response to heat Source: SGD
- cellular response to oxidative stress Source: SGD
- fungal-type cell wall organization Source: SGD
- meiotic cell cycle Source: SGD
- mitochondria-nucleus signaling pathway Source: SGD
- negative regulation of autophagy Source: SGD
- negative regulation of macroautophagy Source: GO_Central
- negative regulation of protein kinase activity by regulation of protein phosphorylation Source: SGD
- nucleolar large rRNA transcription by RNA polymerase I Source: SGD
- peptidyl-serine phosphorylation Source: SGD
- protein phosphorylation Source: CACAO
- 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
- response to endoplasmic reticulum stress Source: SGD
- ribosome biogenesis Source: SGD
- TORC1 signaling Source: GO_Central
- TOR signaling Source: SGD
- translational initiation Source: SGD
Keywordsi
Molecular function | Kinase, Serine/threonine-protein kinase, Transferase |
Biological process | Cell cycle |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 2.7.1.137, 984 |
Reactomei | R-SCE-975957, Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) |
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 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
EuPathDBi | FungiDB:YJR066W |
SGDi | S000003827, TOR1 |
Subcellular locationi
Plasma membrane
- Cell membrane 2 Publications; Peripheral membrane protein 2 Publications; Cytoplasmic side 2 Publications
Vacuole
- Vacuole membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
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.1 Publication
Endosome
- endosome membrane Source: SGD
Golgi apparatus
- Golgi membrane Source: SGD
Nucleus
- nucleus Source: SGD
Plasma Membrane
- extrinsic component of cytoplasmic side of plasma membrane Source: SGD
- plasma membrane Source: SGD
Vacuole
- fungal-type vacuole membrane Source: SGD
Other locations
- cytoplasm Source: SGD
- TORC1 complex Source: SGD
- TORC2 complex Source: GO_Central
Keywords - Cellular componenti
Cell membrane, Membrane, VacuolePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 1972 | S → A: No effect. 2 Publications | 1 | |
Mutagenesisi | 1972 | S → E or I: Confers resistance to rapamycin. Abolishes interaction with FKBP-rapamycin. 2 Publications | 1 | |
Mutagenesisi | 1972 | S → N in DRR1-27; confers resistance to rapamycin. 2 Publications | 1 | |
Mutagenesisi | 1972 | S → R in DRR1-1; confers resistance to rapamycin. Abolishes interaction with FKBP-rapamycin. 2 Publications | 1 | |
Mutagenesisi | 2275 | D → A: Abolishes protein kinase activity. 1 Publication | 1 | |
Mutagenesisi | 2276 | R → P: Abolishes rapamycin-resistance of mutants E-1972; I-1972 and R-1972. 1 Publication | 1 | |
Mutagenesisi | 2294 | D → E: Abolishes rapamycin-resistance of mutants E-1972; I-1972 and R-1972. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000088813 | 1 – 2470 | Serine/threonine-protein kinase TOR1Add BLAST | 2470 |
Proteomic databases
MaxQBi | P35169 |
PaxDbi | P35169 |
PRIDEi | P35169 |
PTM databases
iPTMneti | P35169 |
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 PublicationsBinary interactionsi
Hide detailsP35169
Protein-protein interaction databases
BioGRIDi | 33823, 455 interactors |
ComplexPortali | CPX-1715, TORC1 serine/threonine-protein kinase complex, TOR1 variant |
DIPi | DIP-917N |
IntActi | P35169, 37 interactors |
MINTi | P35169 |
STRINGi | 4932.YJR066W |
Miscellaneous databases
RNActi | P35169, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
BMRBi | P35169 |
PCDDBi | P35169 |
SMRi | P35169 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P35169 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 114 – 151 | HEAT 1Add BLAST | 38 | |
Repeati | 249 – 286 | HEAT 2Add BLAST | 38 | |
Repeati | 627 – 663 | HEAT 3Add BLAST | 37 | |
Repeati | 664 – 701 | HEAT 4Add BLAST | 38 | |
Repeati | 747 – 784 | HEAT 5Add BLAST | 38 | |
Repeati | 788 – 826 | HEAT 6Add BLAST | 39 | |
Repeati | 832 – 870 | HEAT 7Add BLAST | 39 | |
Repeati | 908 – 946 | HEAT 8Add BLAST | 39 | |
Repeati | 950 – 987 | HEAT 9Add BLAST | 38 | |
Repeati | 1069 – 1107 | HEAT 10Add BLAST | 39 | |
Repeati | 1109 – 1147 | HEAT 11Add BLAST | 39 | |
Domaini | 1331 – 1919 | FATPROSITE-ProRule annotationAdd BLAST | 589 | |
Domaini | 2125 – 2437 | PI3K/PI4KPROSITE-ProRule annotationAdd BLAST | 313 | |
Domaini | 2438 – 2470 | FATCPROSITE-ProRule annotationAdd BLAST | 33 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1775 – 2157 | Interaction with FKBP-rapamycinAdd BLAST | 383 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 441 – 447 | Arg/Lys-rich (basic) | 7 |
Sequence similaritiesi
Belongs to the PI3/PI4-kinase family.Curated
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG0891, Eukaryota |
GeneTreei | ENSGT00940000174195 |
HOGENOMi | CLU_000178_7_1_1 |
InParanoidi | P35169 |
OMAi | VCSLCIC |
Family and domain databases
Gene3Di | 1.10.1070.11, 1 hit 1.20.120.150, 1 hit 1.25.10.10, 3 hits |
IDEALi | IID50246 |
InterProi | View protein in InterPro IPR011989, ARM-like IPR016024, ARM-type_fold IPR024585, DUF3385_TOR IPR003152, FATC_dom IPR009076, FRB_dom IPR036738, FRB_sf IPR011009, Kinase-like_dom_sf IPR000403, PI3/4_kinase_cat_dom IPR036940, PI3/4_kinase_cat_sf IPR018936, PI3/4_kinase_CS IPR003151, PIK-rel_kinase_FAT IPR014009, PIK_FAT IPR026683, TOR |
PANTHERi | PTHR11139:SF9, PTHR11139:SF9, 1 hit |
Pfami | View protein in Pfam PF11865, DUF3385, 1 hit PF02259, FAT, 1 hit PF02260, FATC, 1 hit PF08771, FRB_dom, 1 hit PF00454, PI3_PI4_kinase, 1 hit |
SMARTi | View protein in SMART SM01346, DUF3385, 1 hit SM01343, FATC, 1 hit SM00146, PI3Kc, 1 hit |
SUPFAMi | SSF47212, SSF47212, 1 hit SSF48371, SSF48371, 2 hits SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS51189, 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 |
i Sequence
Sequence statusi: Complete.
P35169-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 58 | D → G in AAB66881 (PubMed:8413204).Curated | 1 | |
Sequence conflicti | 115 | V → I in AAB66881 (PubMed:8413204).Curated | 1 | |
Sequence conflicti | 133 | S → N in AAB66881 (PubMed:8413204).Curated | 1 | |
Sequence conflicti | 231 | A → R in CAA52849 (PubMed:8186460).Curated | 1 | |
Sequence conflicti | 396 | N → K in AAB66881 (PubMed:8413204).Curated | 1 | |
Sequence conflicti | 396 | N → K in CAA52849 (PubMed:8186460).Curated | 1 | |
Sequence conflicti | 547 | N → S in AAB66881 (PubMed:8413204).Curated | 1 | |
Sequence conflicti | 547 | N → S in CAA52849 (PubMed:8186460).Curated | 1 | |
Sequence conflicti | 675 | T → I in CAA52849 (PubMed:8186460).Curated | 1 | |
Sequence conflicti | 1292 | G → E in CAA52849 (PubMed:8186460).Curated | 1 | |
Sequence conflicti | 1436 | G → A in CAA52849 (PubMed:8186460).Curated | 1 | |
Sequence conflicti | 1468 | A → R in AAB66881 (PubMed:8413204).Curated | 1 | |
Sequence conflicti | 1468 | A → R in CAA52849 (PubMed:8186460).Curated | 1 | |
Sequence conflicti | 1469 – 1471 | WGL → GGS in CAA52849 (PubMed:8186460).Curated | 3 | |
Sequence conflicti | 1478 – 1479 | EQ → DE in CAA52849 (PubMed:8186460).Curated | 2 | |
Sequence conflicti | 1590 | V → I in CAA52849 (PubMed:8186460).Curated | 1 | |
Sequence conflicti | 1632 – 1642 | NDPSLPNTFKA → TILVYQIRSKP in CAA52849 (PubMed:8186460).CuratedAdd BLAST | 11 | |
Sequence conflicti | 1640 | F → V in AAB66881 (PubMed:8413204).Curated | 1 | |
Sequence conflicti | 1844 | L → S in CAA52849 (PubMed:8186460).Curated | 1 | |
Sequence conflicti | 2202 | H → Q in AAB66881 (PubMed:8413204).Curated | 1 | |
Sequence conflicti | 2414 | K → R in AAB66881 (PubMed:8413204).Curated | 1 | |
Sequence conflicti | 2414 | K → R in CAA52849 (PubMed:8186460).Curated | 1 |
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 |
PIRi | S57085 |
RefSeqi | NP_012600.1, NM_001181724.1 |
Genome annotation databases
EnsemblFungii | YJR066W_mRNA; YJR066W; YJR066W |
GeneIDi | 853529 |
KEGGi | sce:YJR066W |
Similar proteinsi
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 |
PIRi | S57085 |
RefSeqi | NP_012600.1, NM_001181724.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1W1N | NMR | - | A | 2438-2470 | [»] | |
2KIO | NMR | - | A | 2438-2470 | [»] | |
2KIT | NMR | - | A | 2438-2470 | [»] | |
BMRBi | P35169 | |||||
PCDDBi | P35169 | |||||
SMRi | P35169 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 33823, 455 interactors |
ComplexPortali | CPX-1715, TORC1 serine/threonine-protein kinase complex, TOR1 variant |
DIPi | DIP-917N |
IntActi | P35169, 37 interactors |
MINTi | P35169 |
STRINGi | 4932.YJR066W |
PTM databases
iPTMneti | P35169 |
Proteomic databases
MaxQBi | P35169 |
PaxDbi | P35169 |
PRIDEi | P35169 |
Genome annotation databases
EnsemblFungii | YJR066W_mRNA; YJR066W; YJR066W |
GeneIDi | 853529 |
KEGGi | sce:YJR066W |
Organism-specific databases
EuPathDBi | FungiDB:YJR066W |
SGDi | S000003827, TOR1 |
Phylogenomic databases
eggNOGi | KOG0891, Eukaryota |
GeneTreei | ENSGT00940000174195 |
HOGENOMi | CLU_000178_7_1_1 |
InParanoidi | P35169 |
OMAi | VCSLCIC |
Enzyme and pathway databases
BRENDAi | 2.7.1.137, 984 |
Reactomei | R-SCE-975957, Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) |
Miscellaneous databases
EvolutionaryTracei | P35169 |
PROi | PR:P35169 |
RNActi | P35169, protein |
Family and domain databases
Gene3Di | 1.10.1070.11, 1 hit 1.20.120.150, 1 hit 1.25.10.10, 3 hits |
IDEALi | IID50246 |
InterProi | View protein in InterPro IPR011989, ARM-like IPR016024, ARM-type_fold IPR024585, DUF3385_TOR IPR003152, FATC_dom IPR009076, FRB_dom IPR036738, FRB_sf IPR011009, Kinase-like_dom_sf IPR000403, PI3/4_kinase_cat_dom IPR036940, PI3/4_kinase_cat_sf IPR018936, PI3/4_kinase_CS IPR003151, PIK-rel_kinase_FAT IPR014009, PIK_FAT IPR026683, TOR |
PANTHERi | PTHR11139:SF9, PTHR11139:SF9, 1 hit |
Pfami | View protein in Pfam PF11865, DUF3385, 1 hit PF02259, FAT, 1 hit PF02260, FATC, 1 hit PF08771, FRB_dom, 1 hit PF00454, PI3_PI4_kinase, 1 hit |
SMARTi | View protein in SMART SM01346, DUF3385, 1 hit SM01343, FATC, 1 hit SM00146, PI3Kc, 1 hit |
SUPFAMi | SSF47212, SSF47212, 1 hit SSF48371, SSF48371, 2 hits SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS51189, 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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TOR1_YEAST | |
Accessioni | P35169Primary (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: | December 2, 2020 | |
This is version 203 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome X
Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names