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UniProtKB - P35169 (TOR1_YEAST)

Entry version 207 (29 Sep 2021)
Sequence version 3 (01 Nov 1995)
Previous versions | rss
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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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.1.137, 984

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-1257604, PIP3 activates AKT signaling
R-SCE-3371571, HSF1-dependent transactivation
R-SCE-389357, CD28 dependent PI3K/Akt signaling
R-SCE-5218920, VEGFR2 mediated vascular permeability
R-SCE-6804757, Regulation of TP53 Degradation
R-SCE-9639288, Amino acids regulate mTORC1

<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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YJR066W

<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

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 or proteolytic cleavage.<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">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		33823, 458 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1715, TORC1 serine/threonine-protein kinase complex, TOR1 variant

Database of interacting proteins

More...DIPi		DIP-917N

Protein interaction database and analysis system

More...IntActi		P35169, 37 interactors

Molecular INTeraction database

More...MINTi		P35169

STRING: functional protein association networks

More...STRINGi		4932.YJR066W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P35169, protein

<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

Biological Magnetic Resonance Data Bank

More...BMRBi		P35169

The Protein Circular Dichroism Data Bank

More...PCDDBi		P35169

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

More...SMRi		P35169

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0891, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000174195

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000178_7_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P35169

Identification of Orthologs from Complete Genome Data

More...OMAi		VCSLCIC

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, 4 hits

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID50246

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

More...PANTHERi		PTHR11139:SF9, PTHR11139:SF9, 1 hit

Pfam protein domain database

More...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>. The information is filed in different subsections. The current subsections and their content are listed below:<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

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

More...PIRi		S57085

NCBI Reference Sequences

More...RefSeqi		NP_012600.1, NM_001181724.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YJR066W_mRNA; YJR066W; YJR066W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		853529

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...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

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W1NNMR-A2438-2470[»]
2KIONMR-A2438-2470[»]
2KITNMR-A2438-2470[»]
BMRBiP35169
PCDDBiP35169
SMRiP35169
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi33823, 458 interactors
ComplexPortaliCPX-1715, TORC1 serine/threonine-protein kinase complex, TOR1 variant
DIPiDIP-917N
IntActiP35169, 37 interactors
MINTiP35169
STRINGi4932.YJR066W

PTM databases

iPTMnetiP35169

Proteomic databases

MaxQBiP35169
PaxDbiP35169
PRIDEiP35169

Genome annotation databases

EnsemblFungiiYJR066W_mRNA; YJR066W; YJR066W
GeneIDi853529
KEGGisce:YJR066W

Organism-specific databases

SGDiS000003827, TOR1
VEuPathDBiFungiDB:YJR066W

Phylogenomic databases

eggNOGiKOG0891, Eukaryota
GeneTreeiENSGT00940000174195
HOGENOMiCLU_000178_7_1_1
InParanoidiP35169
OMAiVCSLCIC

Enzyme and pathway databases

BRENDAi2.7.1.137, 984
ReactomeiR-SCE-1257604, PIP3 activates AKT signaling
R-SCE-3371571, HSF1-dependent transactivation
R-SCE-389357, CD28 dependent PI3K/Akt signaling
R-SCE-5218920, VEGFR2 mediated vascular permeability
R-SCE-6804757, Regulation of TP53 Degradation
R-SCE-9639288, Amino acids regulate mTORC1

Miscellaneous databases

EvolutionaryTraceiP35169

Protein Ontology

More...PROi		PR:P35169
RNActiP35169, protein

Family and domain databases

Gene3Di1.10.1070.11, 1 hit
1.20.120.150, 1 hit
1.25.10.10, 4 hits
IDEALiIID50246
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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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: September 29, 2021
This is version 207 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, Reference proteome

Documents

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