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Entry version 184 (26 Feb 2020)
Sequence version 3 (09 Jan 2007)
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Protein

Serine/threonine-protein kinase TOR2

Gene

TOR2

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 both TORC1 and TORC2. TORC1 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: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). TORC2 regulates cell cycle-dependent polarization of the actin-cytoskeleton, cell wall integrity, and receptor endocytosis. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway by activating the RHO1 guanine nucleotide exchange factor ROM2. TORC2 phosphorylates the AGC kinase YPK2, an upstream effector of the cell integrity pathway. TORC2 negatively regulates calcineurin-dependent stress signaling via phosphorylation of its effector SLM1-SLM2 (PubMed:14593073, PubMed:15372071, PubMed:16055732, PubMed:16959779, PubMed:8846782, PubMed:8943012).17 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

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

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BioCyci
YEAST:G3O-31962-MONOMER

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%5Fand%5Ftaxonomy%5Fsection">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 TOR2 (EC:2.7.1.67, EC:2.7.11.1)
Alternative name(s):
Dominant rapamycin resistance protein 2
Phosphatidylinositol 4-kinase TOR2
Short name:
PI4-kinase TOR2
Short name:
PI4K TOR2
Short name:
PtdIns-4-kinase TOR2
Target of rapamycin kinase 2
Temperature-sensitive CSG2 suppressor protein 14
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:TOR2
Synonyms:DRR2, TSC14
Ordered Locus Names:YKL203C
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 XI

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
FungiDB:YKL203C

Saccharomyces Genome Database

More...
SGDi
S000001686 TOR2

<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 & Seán O’Donoghue; 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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi1975S → I in TOR2-1; confers resistance to rapamycin. 1 Publication1
Mutagenesisi2129G → R: Causes defect in receptor endocytosis. 1 Publication1
Mutagenesisi2279D → A: Loss of function. 1 Publication1
Mutagenesisi2298D → E: Loss of kinase activity. 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_00000888151 – 2474Serine/threonine-protein kinase TOR2Add BLAST2474

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei10PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P32600

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

More...
PaxDbi
P32600

PRoteomics IDEntifications database

More...
PRIDEi
P32600

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P32600

<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%5Fsection">'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%5Fsection">'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. The target of rapamycin complex 2 (TORC2) is composed of at least AVO1, AVO2, BIT61, LST8, TOR2 and TSC11. TORC2 likely forms a homodimer. Contrary to TORC1, TORC2 does not bind to and is not sensitive to FKBP-rapamycin.

Interacts with SLM1 and SLM2.

5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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

Show more details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
33920, 465 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1716 TORC1 complex variant 2
CPX-1717 TORC2 complex

Database of interacting proteins

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DIPi
DIP-2332N

Protein interaction database and analysis system

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IntActi
P32600, 24 interactors

Molecular INTeraction database

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MINTi
P32600

STRING: functional protein association networks

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STRINGi
4932.YKL203C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P32600 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

3D structure databases

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

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SMRi
P32600

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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>Repeati588 – 626HEAT 1Add BLAST39
Repeati636 – 674HEAT 2Add BLAST39
Repeati676 – 710HEAT 3Add BLAST35
Repeati756 – 793HEAT 4Add BLAST38
Repeati797 – 835HEAT 5Add BLAST39
Repeati841 – 879HEAT 6Add BLAST39
Repeati917 – 955HEAT 7Add BLAST39
Repeati1039 – 1076HEAT 8Add BLAST38
Repeati1079 – 1116HEAT 9Add BLAST38
Repeati1118 – 1155HEAT 10Add BLAST38
Repeati1292 – 1331HEAT 11Add BLAST40
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">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>Domaini1338 – 1922FATPROSITE-ProRule annotationAdd BLAST585
Domaini2123 – 2441PI3K/PI4KPROSITE-ProRule annotationAdd BLAST319
Domaini2442 – 2474FATCPROSITE-ProRule annotationAdd BLAST33

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_000178_7_1_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P32600

KEGG Orthology (KO)

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KOi
K07203

Identification of Orthologs from Complete Genome Data

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OMAi
LNIQRYP

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
1.25.40.10, 1 hit

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
IPR011990 TPR-like_helical_dom_sf

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, 3 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P32600-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNKYINKYTT PPNLLSLRQR AEGKHRTRKK LTHKSHSHDD EMSTTSNTDS
60 70 80 90 100
NHNGPNDSGR VITGSAGHIG KISFVDSELD TTFSTLNLIF DKLKSDVPQE
110 120 130 140 150
RASGANELST TLTSLAREVS AEQFQRFSNS LNNKIFELIH GFTSSEKIGG
160 170 180 190 200
ILAVDTLISF YLSTEELPNQ TSRLANYLRV LIPSSDIEVM RLAANTLGRL
210 220 230 240 250
TVPGGTLTSD FVEFEVRTCI DWLTLTADNN SSSSKLEYRR HAALLIIKAL
260 270 280 290 300
ADNSPYLLYP YVNSILDNIW VPLRDAKLII RLDAAVALGK CLTIIQDRDP
310 320 330 340 350
ALGKQWFQRL FQGCTHGLSL NTNDSVHATL LVFRELLSLK APYLRDKYDD
360 370 380 390 400
IYKSTMKYKE YKFDVIRREV YAILPLLAAF DPAIFTKKYL DRIMVHYLRY
410 420 430 440 450
LKNIDMNAAN NSDKPFILVS IGDIAFEVGS SISPYMTLIL DNIREGLRTK
460 470 480 490 500
FKVRKQFEKD LFYCIGKLAC ALGPAFAKHL NKDLLNLMLN CPMSDHMQET
510 520 530 540 550
LMILNEKIPS LESTVNSRIL NLLSISLSGE KFIQSNQYDF NNQFSIEKAR
560 570 580 590 600
KSRNQSFMKK TGESNDDITD AQILIQCFKM LQLIHHQYSL TEFVRLITIS
610 620 630 640 650
YIEHEDSSVR KLAALTSCDL FIKDDICKQT SVHALHSVSE VLSKLLMIAI
660 670 680 690 700
TDPVAEIRLE ILQHLGSNFD PQLAQPDNLR LLFMALNDEI FGIQLEAIKI
710 720 730 740 750
IGRLSSVNPA YVVPSLRKTL LELLTQLKFS NMPKKKEESA TLLCTLINSS
760 770 780 790 800
DEVAKPYIDP ILDVILPKCQ DASSAVASTA LKVLGELSVV GGKEMTRYLK
810 820 830 840 850
ELMPLIINTF QDQSNSFKRD AALTTLGQLA ASSGYVVGPL LDYPELLGIL
860 870 880 890 900
INILKTENNP HIRRGTVRLI GILGALDPYK HREIEVTSNS KSSVEQNAPS
910 920 930 940 950
IDIALLMQGV SPSNDEYYPT VVIHNLMKIL NDPSLSIHHT AAIQAIMHIF
960 970 980 990 1000
QNLGLRCVSF LDQIIPGIIL VMRSCPPSQL DFYFQQLGSL ISIVKQHIRP
1010 1020 1030 1040 1050
HVEKIYGVIR EFFPIIKLQI TIISVIESIS KALEGEFKRF VPETLTFFLD
1060 1070 1080 1090 1100
ILENDQSNKR IVPIRILKSL VTFGPNLEDY SHLIMPIVVR MTEYSAGSLK
1110 1120 1130 1140 1150
KISIITLGRL AKNINLSEMS SRIVQALVRI LNNGDRELTK ATMNTLSLLL
1160 1170 1180 1190 1200
LQLGTDFVVF VPVINKALLR NRIQHSVYDQ LVNKLLNNEC LPTNIIFDKE
1210 1220 1230 1240 1250
NEVPERKNYE DEMQVTKLPV NQNILKNAWY CSQQKTKEDW QEWIRRLSIQ
1260 1270 1280 1290 1300
LLKESPSACL RSCSSLVSVY YPLARELFNA SFSSCWVELQ TSYQEDLIQA
1310 1320 1330 1340 1350
LCKALSSSEN PPEIYQMLLN LVEFMEHDDK PLPIPIHTLG KYAQKCHAFA
1360 1370 1380 1390 1400
KALHYKEVEF LEEPKNSTIE ALISINNQLH QTDSAIGILK HAQQHNELQL
1410 1420 1430 1440 1450
KETWYEKLQR WEDALAAYNE KEAAGEDSVE VMMGKLRSLY ALGEWEELSK
1460 1470 1480 1490 1500
LASEKWGTAK PEVKKAMAPL AAGAAWGLEQ WDEIAQYTSV MKSQSPDKEF
1510 1520 1530 1540 1550
YDAILCLHRN NFKKAEVHIF NARDLLVTEL SALVNESYNR AYNVVVRAQI
1560 1570 1580 1590 1600
IAELEEIIKY KKLPQNSDKR LTMRETWNTR LLGCQKNIDV WQRILRVRSL
1610 1620 1630 1640 1650
VIKPKEDAQV RIKFANLCRK SGRMALAKKV LNTLLEETDD PDHPNTAKAS
1660 1670 1680 1690 1700
PPVVYAQLKY LWATGLQDEA LKQLINFTSR MAHDLGLDPN NMIAQSVPQQ
1710 1720 1730 1740 1750
SKRVPRHVED YTKLLARCFL KQGEWRVCLQ PKWRLSNPDS ILGSYLLATH
1760 1770 1780 1790 1800
FDNTWYKAWH NWALANFEVI SMLTSVSKKK QEGSDASSVT DINEFDNGMI
1810 1820 1830 1840 1850
GVNTFDAKEV HYSSNLIHRH VIPAIKGFFH SISLSESSSL QDALRLLTLW
1860 1870 1880 1890 1900
FTFGGIPEAT QAMHEGFNLI QIGTWLEVLP QLISRIHQPN QIVSRSLLSL
1910 1920 1930 1940 1950
LSDLGKAHPQ ALVYPLMVAI KSESLSRQKA ALSIIEKMRI HSPVLVDQAE
1960 1970 1980 1990 2000
LVSHELIRMA VLWHEQWYEG LDDASRQFFG EHNTEKMFAA LEPLYEMLKR
2010 2020 2030 2040 2050
GPETLREISF QNSFGRDLND AYEWLMNYKK SKDVSNLNQA WDIYYNVFRK
2060 2070 2080 2090 2100
IGKQLPQLQT LELQHVSPKL LSAHDLELAV PGTRASGGKP IVKISKFEPV
2110 2120 2130 2140 2150
FSVISSKQRP RKFCIKGSDG KDYKYVLKGH EDIRQDSLVM QLFGLVNTLL
2160 2170 2180 2190 2200
QNDAECFRRH LDIQQYPAIP LSPKSGLLGW VPNSDTFHVL IREHREAKKI
2210 2220 2230 2240 2250
PLNIEHWVML QMAPDYDNLT LLQKVEVFTY ALNNTEGQDL YKVLWLKSRS
2260 2270 2280 2290 2300
SETWLERRTT YTRSLAVMSM TGYILGLGDR HPSNLMLDRI TGKVIHIDFG
2310 2320 2330 2340 2350
DCFEAAILRE KFPEKVPFRL TRMLTYAMEV SGIEGSFRIT CENVMKVLRD
2360 2370 2380 2390 2400
NKGSLMAILE AFAFDPLINW GFDLPTKKIE EETGIQLPVM NANELLSNGA
2410 2420 2430 2440 2450
ITEEEVQRVE NEHKNAIRNA RAMLVLKRIT DKLTGNDIRR FNDLDVPEQV
2460 2470
DKLIQQATSV ENLCQHYIGW CPFW
Length:2,474
Mass (Da):281,568
Last modified:January 9, 2007 - 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:iF2349690146058CF
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 conflicti1473Missing in CAA82048 (PubMed:8196765).Curated1

Sequence databases

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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
X71416 Genomic DNA Translation: CAA50548.1
Z28203 Genomic DNA Translation: CAA82048.1
BK006944 Genomic DNA Translation: DAA08966.1

Protein sequence database of the Protein Information Resource

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PIRi
S38040

NCBI Reference Sequences

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RefSeqi
NP_012719.2, NM_001179768.1

Genome annotation databases

Ensembl fungal genome annotation project

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EnsemblFungii
YKL203C_mRNA; YKL203C; YKL203C

Database of genes from NCBI RefSeq genomes

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GeneIDi
853632

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
sce:YKL203C

<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
X71416 Genomic DNA Translation: CAA50548.1
Z28203 Genomic DNA Translation: CAA82048.1
BK006944 Genomic DNA Translation: DAA08966.1
PIRiS38040
RefSeqiNP_012719.2, NM_001179768.1

3D structure databases

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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
6EMKelectron microscopy8.00A/C1-2474[»]
SMRiP32600
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi33920, 465 interactors
ComplexPortaliCPX-1716 TORC1 complex variant 2
CPX-1717 TORC2 complex
DIPiDIP-2332N
IntActiP32600, 24 interactors
MINTiP32600
STRINGi4932.YKL203C

PTM databases

iPTMnetiP32600

Proteomic databases

MaxQBiP32600
PaxDbiP32600
PRIDEiP32600

Genome annotation databases

EnsemblFungiiYKL203C_mRNA; YKL203C; YKL203C
GeneIDi853632
KEGGisce:YKL203C

Organism-specific databases

EuPathDBiFungiDB:YKL203C
SGDiS000001686 TOR2

Phylogenomic databases

HOGENOMiCLU_000178_7_1_1
InParanoidiP32600
KOiK07203
OMAiLNIQRYP

Enzyme and pathway databases

BioCyciYEAST:G3O-31962-MONOMER
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

Protein Ontology

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PROi
PR:P32600
RNActiP32600 protein

Family and domain databases

Gene3Di1.10.1070.11, 1 hit
1.20.120.150, 1 hit
1.25.10.10, 3 hits
1.25.40.10, 1 hit
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
IPR011990 TPR-like_helical_dom_sf
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, 3 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...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiTOR2_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: P32600
Secondary accession number(s): D6VX00
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 9, 2007
Last modified: February 26, 2020
This is version 184 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. 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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names
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