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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>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

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-31699-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.1.137 984

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TOR1
Synonyms:DRR1
Ordered Locus Names:YJR066W
ORF Names:J1803
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000003827 TOR1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane, Vacuole

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000888131 – 2470Serine/threonine-protein kinase TOR1Add BLAST2470

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P35169

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P35169

PRoteomics IDEntifications database

More...
PRIDEi
P35169

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P35169

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33823, 449 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1715 TORC1 complex variant 1

Database of interacting proteins

More...
DIPi
DIP-917N

Protein interaction database and analysis system

More...
IntActi
P35169, 37 interactors

Molecular INTeraction database

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MINTi
P35169

STRING: functional protein association networks

More...
STRINGi
4932.YJR066W

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

12470
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P35169

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P35169

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P35169

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1331 – 1919FATPROSITE-ProRule annotationAdd BLAST589
Domaini2125 – 2437PI3K/PI4KPROSITE-ProRule annotationAdd BLAST313
Domaini2438 – 2470FATCPROSITE-ProRule annotationAdd BLAST33

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1775 – 2157Interaction with FKBP-rapamycinAdd BLAST383

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi441 – 447Arg/Lys-rich (basic)7

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000174195

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000163215

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P35169

KEGG Orthology (KO)

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KOi
K07203

Identification of Orthologs from Complete Genome Data

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OMAi
VCSLCIC

Database of Orthologous Groups

More...
OrthoDBi
EOG092C00HJ

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1070.11, 1 hit
1.20.120.150, 1 hit
1.25.10.10, 3 hits

Integrated resource of protein families, domains and functional sites

More...
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

The PANTHER Classification System

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PANTHERi
PTHR11139:SF9 PTHR11139:SF9, 1 hit

Pfam protein domain database

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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

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01346 DUF3385, 1 hit
SM01343 FATC, 1 hit
SM00146 PI3Kc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47212 SSF47212, 1 hit
SSF48371 SSF48371, 2 hits
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iACB1781B9963BB1E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

Protein sequence database of the Protein Information Resource

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PIRi
S57085

NCBI Reference Sequences

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RefSeqi
NP_012600.1, NM_001181724.1

Genome annotation databases

Ensembl fungal genome annotation project

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EnsemblFungii
YJR066W_mRNA; YJR066W_mRNA; YJR066W

Database of genes from NCBI RefSeq genomes

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GeneIDi
853529

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
sce:YJR066W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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, 449 interactors
ComplexPortaliCPX-1715 TORC1 complex variant 1
DIPiDIP-917N
IntActiP35169, 37 interactors
MINTiP35169
STRINGi4932.YJR066W

PTM databases

iPTMnetiP35169

Proteomic databases

MaxQBiP35169
PaxDbiP35169
PRIDEiP35169

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR066W_mRNA; YJR066W_mRNA; YJR066W
GeneIDi853529
KEGGisce:YJR066W

Organism-specific databases

SGDiS000003827 TOR1

Phylogenomic databases

GeneTreeiENSGT00940000174195
HOGENOMiHOG000163215
InParanoidiP35169
KOiK07203
OMAiVCSLCIC
OrthoDBiEOG092C00HJ

Enzyme and pathway databases

BioCyciYEAST:G3O-31699-MONOMER
BRENDAi2.7.1.137 984

Miscellaneous databases

EvolutionaryTraceiP35169

Protein Ontology

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PROi
PR:P35169

Family and domain databases

Gene3Di1.10.1070.11, 1 hit
1.20.120.150, 1 hit
1.25.10.10, 3 hits
InterProiView 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
PANTHERiPTHR11139:SF9 PTHR11139:SF9, 1 hit
PfamiView 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
SMARTiView protein in SMART
SM01346 DUF3385, 1 hit
SM01343 FATC, 1 hit
SM00146 PI3Kc, 1 hit
SUPFAMiSSF47212 SSF47212, 1 hit
SSF48371 SSF48371, 2 hits
SSF56112 SSF56112, 1 hit
PROSITEiView 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTOR1_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P35169
Secondary accession number(s): D6VWN7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 1, 1995
Last modified: December 5, 2018
This is version 189 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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