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UniProtKB - P42345 (MTOR_HUMAN)

Entry version 207 (05 Jun 2019)
Sequence version 1 (01 Nov 1995)
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Protein

Serine/threonine-protein kinase mTOR

Gene

MTOR

Organism
Homo sapiens (Human)
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

Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals (PubMed:12087098, PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876, PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625, PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875, PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703, PubMed:23429704, PubMed:25799227, PubMed:26018084). MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins. Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2) (PubMed:15268862, PubMed:15467718, PubMed:18925875, PubMed:18497260, PubMed:20516213, PubMed:21576368, PubMed:21659604, PubMed:23429704). Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis (PubMed:12087098, PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876, PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625, PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875, PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703, PubMed:23429704, PubMed:25799227, PubMed:26018084). This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E) (By similarity). Moreover, phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein synthesis by modulating the activity of their downstream targets including ribosomal protein S6, eukaryotic translation initiation factor EIF4B, and the inhibitor of translation initiation PDCD4 (PubMed:12150925, PubMed:12087098, PubMed:18925875). Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex (PubMed:23429704, PubMed:23429703). Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor (PubMed:20516213). In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1 (By similarity). To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A (By similarity). mTORC1 also negatively regulates autophagy through phosphorylation of ULK1 (By similarity). Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1 (By similarity). Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP (PubMed:20537536). Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions (PubMed:30704899). mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor (PubMed:21659604). Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules (PubMed:12231510). As part of the mTORC2 complex MTOR may regulate other cellular processes including survival and organization of the cytoskeleton (PubMed:15268862, PubMed:15467718). Plays a critical role in the phosphorylation at 'Ser-473' of AKT1, a pro-survival effector of phosphoinositide 3-kinase, facilitating its activation by PDK1 (PubMed:15718470). mTORC2 may regulate the actin cytoskeleton, through phosphorylation of PRKCA, PXN and activation of the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or RAC1B (PubMed:15268862). mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422' (PubMed:18925875). Regulates osteoclastogenesis by adjusting the expression of CEBPB isoforms (By similarity). Plays an important regulatory role in the circadian clock function; regulates period length and rhythm amplitude of the suprachiasmatic nucleus (SCN) and liver clocks (By similarity).By similarity22 Publications

<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>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activation of mTORC1 by growth factors such as insulin involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase a potent activator of the protein kinase activity of mTORC1. Insulin-stimulated and amino acid-dependent phosphorylation at Ser-1261 promotes autophosphorylation and the activation of mTORC1. Activation by amino acids requires relocalization of the mTORC1 complex to lysosomes that is mediated by the Ragulator complex, SLC38A9, and the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD (PubMed:18497260, PubMed:20381137, PubMed:25561175, PubMed:25567906). On the other hand, low cellular energy levels can inhibit mTORC1 through activation of PRKAA1 while hypoxia inhibits mTORC1 through a REDD1-dependent mechanism which may also require PRKAA1. The kinase activity of MTOR within the mTORC1 complex is positively regulated by MLST8 and negatively regulated by DEPTOR and AKT1S1. MTOR phosphorylates RPTOR which in turn inhibits mTORC1. MTOR is the target of the immunosuppressive and anti-cancer drug rapamycin which acts in complex with FKBP1A/FKBP12, and specifically inhibits its kinase activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. It may be regulated by RHEB but in an indirect manner through the PI3K signaling pathway.8 Publications

<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 processBiological rhythms
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1257604 PIP3 activates AKT signaling
R-HSA-1632852 Macroautophagy
R-HSA-165159 mTOR signalling
R-HSA-166208 mTORC1-mediated signalling
R-HSA-3371571 HSF1-dependent transactivation
R-HSA-380972 Energy dependent regulation of mTOR by LKB1-AMPK
R-HSA-389357 CD28 dependent PI3K/Akt signaling
R-HSA-5218920 VEGFR2 mediated vascular permeability
R-HSA-5628897 TP53 Regulates Metabolic Genes
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
R-HSA-6804757 Regulation of TP53 Degradation
R-HSA-8943724 Regulation of PTEN gene transcription

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P42345

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P42345

SIGNOR Signaling Network Open Resource

More...SIGNORi		P42345

<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 mTOR (EC:2.7.11.17 Publications)
Alternative name(s):
FK506-binding protein 12-rapamycin complex-associated protein 1
FKBP12-rapamycin complex-associated protein
Mammalian target of rapamycin
Short name:
mTOR
Mechanistic target of rapamycin
Rapamycin and FKBP12 target 1
Rapamycin target protein 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:MTOR
Synonyms:FRAP, FRAP1, FRAP2, RAFT1, RAPT1
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 1

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:3942 MTOR

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601231 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P42345

<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 Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Lysosome, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane, Nucleus

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Smith-Kingsmore syndrome (SKS)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant syndrome characterized by intellectual disability, macrocephaly, seizures, umbilical hernia, and facial dysmorphic features.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0788321490W → R in SKS. 1 Publication1
Natural variantiVAR_0788331595M → I in SKS. 1 PublicationCorresponds to variant dbSNP:rs869312671EnsemblClinVar.1
Natural variantiVAR_0750721799E → K in SKS; results in increased mTOR signaling. 2 PublicationsCorresponds to variant dbSNP:rs863225264EnsemblClinVar.1
Natural variantiVAR_0788351832A → T in SKS. 1 PublicationCorresponds to variant dbSNP:rs369088781EnsemblClinVar.1
Natural variantiVAR_0788361888F → C in SKS. 1 PublicationCorresponds to variant dbSNP:rs869312666EnsemblClinVar.1
Natural variantiVAR_0788402327M → I in SKS. 1 PublicationCorresponds to variant dbSNP:rs878855328EnsemblClinVar.1
Focal cortical dysplasia 2 (FCORD2)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of focal cortical dysplasia, a malformation of cortical development that results in medically refractory epilepsy in the pediatric population and in adults. FCORD2 is a severe form, with onset usually in childhood, characterized by disrupted cortical lamination and specific cytological abnormalities. It is classified in 2 subtypes: type IIA characterized by dysmorphic neurons and lack of balloon cells; type IIB with dysmorphic neurons and balloon cells.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078824624R → H in FCORD2; somatic mutation; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs913197212Ensembl.1
Natural variantiVAR_0788261450Y → D in FCORD2; somatic mutation. 1 Publication1
Natural variantiVAR_0788271456W → G in FCORD2; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1085307114EnsemblClinVar.1
Natural variantiVAR_0788281459A → D in FCORD2; somatic mutation; increased TOR signaling. 1 Publication1
Natural variantiVAR_0788291459A → S in FCORD2; somatic mutation. 1 Publication1
Natural variantiVAR_0788301460L → P in FCORD2; somatic mutation; increased TOR signaling. 2 PublicationsCorresponds to variant dbSNP:rs1057519779EnsemblClinVar.1
Natural variantiVAR_0788311483C → R in FCORD2; somatic mutation; increased TOR signaling; increased kinase activity. 1 PublicationCorresponds to variant dbSNP:rs1057519914EnsemblClinVar.1
Natural variantiVAR_0788341709R → H in FCORD2; somatic mutation; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs587777895EnsemblClinVar.1
Natural variantiVAR_0788371977T → K in FCORD2; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs587777893EnsemblClinVar.1
Natural variantiVAR_0788382193R → C in FCORD2; somatic mutation. 1 Publication1
Natural variantiVAR_0788392215S → F in FCORD2; somatic mutation; increased TOR signaling. 3 PublicationsCorresponds to variant dbSNP:rs587777894EnsemblClinVar.1
Natural variantiVAR_0415432215S → Y in FCORD2; also found in a colorectal adenocarcinoma sample; somatic mutation; increased TOR signaling. 3 PublicationsCorresponds to variant dbSNP:rs587777894EnsemblClinVar.1
Natural variantiVAR_0788412427L → P in FCORD2; somatic mutation; increased TOR signaling; increased kinase activity. 1 PublicationCorresponds to variant dbSNP:rs1085307113EnsemblClinVar.1
Natural variantiVAR_0788422427L → Q in FCORD2; somatic mutation; increased TOR signaling; increased kinase activity. 1 PublicationCorresponds to variant dbSNP:rs1085307113EnsemblClinVar.1

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>Mutagenesisi2159S → A: Reduces mTORC1-associated S-2481 autophosphorylation; when associated with A-2164. 1 Publication1
Mutagenesisi2159S → D: Stronger phosphorylation of RPS6KB1; when associated with E-2164. 1 Publication1
Mutagenesisi2164T → A: Reduces mTORC1-associated S-2481 autophosphorylation; when associated with A-2159. 1 Publication1
Mutagenesisi2164T → E: Stronger phosphorylation of RPS6KB1; when associated with D-2159. 1 Publication1
Mutagenesisi2173T → A: Increased mTOR kinase activity. 1 Publication1
Mutagenesisi2340H → A: Barely detectable kinase activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Epilepsy, Mental retardation

Organism-specific databases

DisGeNET

More...DisGeNETi		2475

MalaCards human disease database

More...MalaCardsi		MTOR
MIMi607341 phenotype
616638 phenotype

Open Targets

More...OpenTargetsi		ENSG00000198793

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		269001 Isolated focal cortical dysplasia type IIa
269008 Isolated focal cortical dysplasia type IIb
457485 Macrocephaly-intellectual disability-neurodevelopmental disorder-small thorax syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28360

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2842

Drug and drug target database

More...DrugBanki		DB04974 AP1903
DB01590 Everolimus
DB00337 Pimecrolimus
DB05210 SF1126
DB00877 Sirolimus
DB06287 Temsirolimus
DB05241 XL765

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2109

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		MTOR

Domain mapping of disease mutations (DMDM)

More...DMDMi		1169735

<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_00000888081 – 2549Serine/threonine-protein kinase mTORAdd BLAST2549

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 residuei1N-acetylmethionineCombined sources1
Modified residuei567PhosphoserineCombined sources1
Modified residuei1162PhosphothreonineCombined sources1
Modified residuei1218N6-acetyllysineCombined sources1
Modified residuei1261PhosphoserineCombined sources1 Publication1
Modified residuei2159Phosphoserine1 Publication1
Modified residuei2164Phosphothreonine1 Publication1
Modified residuei2173Phosphothreonine; by PKB/AKT11 Publication1
Modified residuei2446Phosphothreonine; by RPS6KB11 Publication1
Modified residuei2448Phosphoserine; by RPS6KB1Combined sources2 Publications1
Modified residuei2478PhosphoserineCombined sources1
Modified residuei2481Phosphoserine; by autocatalysisCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylates when part of mTORC1 or mTORC2. Phosphorylation at Ser-1261, Ser-2159 and Thr-2164 promotes autophosphorylation. Phosphorylation in the kinase domain modulates the interactions of MTOR with RPTOR and PRAS40 and leads to increased intrinsic mTORC1 kinase activity. Phosphorylation at Thr-2173 in the ATP-binding region by AKT1 strongly reduces kinase activity.7 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P42345

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P42345

MaxQB - The MaxQuant DataBase

More...MaxQBi		P42345

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

More...PaxDbi		P42345

PeptideAtlas

More...PeptideAtlasi		P42345

PRoteomics IDEntifications database

More...PRIDEi		P42345

ProteomicsDB human proteome resource

More...ProteomicsDBi		55511

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P42345

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P42345

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in numerous tissues, with highest levels in testis.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000198793 Expressed in 167 organ(s), highest expression level in testis

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P42345 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P42345 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB069425
HPA071227

<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

Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. The mTORC1 complex is a 1 Md obligate dimer of two stoichiometric heterotetramers with overall dimensions of 290 A x 210 A x 135 A. It has a rhomboid shape and a central cavity, the dimeric interfaces are formed by interlocking interactions between the two MTOR and the two RPTOR subunits. The MLST8 subunit forms distal foot-like protuberances, and contacts only one MTOR within the complex, while the small PRAS40 localizes to the midsection of the central core, in close proximity to RPTOR. Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Interacts with PLPP7 and PML. Interacts with PRR5 and RICTOR; the interaction is direct within the mTORC2 complex. Interacts with WAC; WAC positively regulates MTOR activity by promoting the assembly of the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex which leads to the dimerization of the mTORC1 complex and its subsequent activation (PubMed:26812014). Interacts with UBQLN1. Interacts with TTI1 and TELO2. Interacts with CLIP1; phosphorylates and regulates CLIP1. Interacts with NBN. Interacts with HTR6 (PubMed:23027611). Interacts with BRAT1. Interacts with MEAK7 (via C-terminal domain); the interaction increases upon nutrient stimulation (PubMed:29750193).24 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

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108757, 216 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P42345

Database of interacting proteins

More...DIPi		DIP-790N

Protein interaction database and analysis system

More...IntActi		P42345, 84 interactors

Molecular INTeraction database

More...MINTi		P42345

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000354558

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P42345

<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

12549
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P42345

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P42345

<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>Repeati16 – 53HEAT 1Add BLAST38
Repeati55 – 99HEAT 2Add BLAST45
Repeati100 – 137HEAT 3Add BLAST38
Repeati138 – 179HEAT 4Add BLAST42
Repeati180 – 220HEAT 5Add BLAST41
Repeati222 – 276HEAT 6Add BLAST55
Repeati277 – 313HEAT 7Add BLAST37
Repeati314 – 364HEAT 8Add BLAST51
Repeati365 – 409HEAT 9Add BLAST45
Repeati410 – 445HEAT 10Add BLAST36
Repeati446 – 494HEAT 11Add BLAST49
Repeati495 – 529HEAT 12Add BLAST35
Repeati530 – 563HEAT 13Add BLAST34
Repeati564 – 596HEAT 14Add BLAST33
Repeati597 – 636HEAT 15Add BLAST40
Repeati637 – 683HEAT 16Add BLAST47
Repeati686 – 724HEAT 17Add BLAST39
Repeati727 – 766HEAT 18Add BLAST40
Repeati769 – 811HEAT 19Add BLAST43
Repeati814 – 853HEAT 20Add BLAST40
Repeati857 – 893HEAT 21Add BLAST37
Repeati894 – 942HEAT 22Add BLAST49
Repeati943 – 988HEAT 23Add BLAST46
Repeati989 – 1027HEAT 24Add BLAST39
Repeati1029 – 1068HEAT 25Add BLAST40
Repeati1069 – 1105HEAT 26Add BLAST37
Repeati1106 – 1144HEAT 27Add BLAST39
Repeati1145 – 1188HEAT 28Add BLAST44
Repeati1189 – 1225HEAT 29Add BLAST37
Repeati1226 – 1273HEAT 30Add BLAST48
Repeati1274 – 1311HEAT 31Add BLAST38
Repeati1312 – 1345HEAT 32Add BLAST34
Repeati1346 – 1382TPR 1Add BLAST37
<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>Domaini1382 – 1982FATPROSITE-ProRule annotationAdd BLAST601
Repeati1383 – 1408TPR 2Add BLAST26
Repeati1409 – 1442TPR 3Add BLAST34
Repeati1443 – 1473TPR 4Add BLAST31
Repeati1474 – 1507TPR 5Add BLAST34
Repeati1508 – 1541TPR 6Add BLAST34
Repeati1542 – 1574TPR 7Add BLAST33
Repeati1575 – 1614TPR 8Add BLAST40
Repeati1615 – 1649TPR 9Add BLAST35
Repeati1650 – 1693TPR 10Add BLAST44
Repeati1694 – 1731TPR 11Add BLAST38
Repeati1732 – 1786TPR 12Add BLAST55
Repeati1787 – 1846TPR 13Add BLAST60
Repeati1898 – 1930TPR 14Add BLAST33
Repeati1931 – 1970TPR 15Add BLAST40
Repeati1971 – 2005TPR 16Add BLAST35
Domaini2182 – 2516PI3K/PI4KPROSITE-ProRule annotationAdd BLAST335
Domaini2517 – 2549FATCPROSITE-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>Regioni1 – 651Interaction with NBN1 PublicationAdd BLAST651
Regioni2012 – 2144Sufficient for interaction with the FKBP1A/rapamycin complexBy similarityAdd BLAST133
Regioni2258 – 2296Interaction with MLST8Add BLAST39

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The kinase domain (PI3K/PI4K) is intrinsically active but has a highly restricted catalytic center.1 Publication
The FAT domain forms three discontinuous subdomains of alpha-helical TPR repeats plus a single subdomain of HEAT repeats. The four domains pack sequentially to form a C-shaped a-solenoid that clamps onto the kinase domain (PubMed:23636326).1 Publication

<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, TPR repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0891 Eukaryota
COG5032 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00930000151037

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000163215

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P42345

KEGG Orthology (KO)

More...KOi		K07203

Identification of Orthologs from Complete Genome Data

More...OMAi		LNIQRYP

Database of Orthologous Groups

More...OrthoDBi		26975at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P42345

TreeFam database of animal gene trees

More...TreeFami		TF105134

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
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

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>Sequence (1+)i

<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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P42345-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLGTGPAAAT TAATTSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM 
        60         70         80         90        100
ELREMSQEES TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN 
       110        120        130        140        150
ATRIGRFANY LRNLLPSNDP VVMEMASKAI GRLAMAGDTF TAEYVEFEVK 
       160        170        180        190        200
RALEWLGADR NEGRRHAAVL VLRELAISVP TFFFQQVQPF FDNIFVAVWD 
       210        220        230        240        250
PKQAIREGAV AALRACLILT TQREPKEMQK PQWYRHTFEE AEKGFDETLA 
       260        270        280        290        300
KEKGMNRDDR IHGALLILNE LVRISSMEGE RLREEMEEIT QQQLVHDKYC 
       310        320        330        340        350
KDLMGFGTKP RHITPFTSFQ AVQPQQSNAL VGLLGYSSHQ GLMGFGTSPS 
       360        370        380        390        400
PAKSTLVESR CCRDLMEEKF DQVCQWVLKC RNSKNSLIQM TILNLLPRLA 
       410        420        430        440        450
AFRPSAFTDT QYLQDTMNHV LSCVKKEKER TAAFQALGLL SVAVRSEFKV 
       460        470        480        490        500
YLPRVLDIIR AALPPKDFAH KRQKAMQVDA TVFTCISMLA RAMGPGIQQD 
       510        520        530        540        550
IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL KMLSLVLMHK 
       560        570        580        590        600
PLRHPGMPKG LAHQLASPGL TTLPEASDVG SITLALRTLG SFEFEGHSLT 
       610        620        630        640        650
QFVRHCADHF LNSEHKEIRM EAARTCSRLL TPSIHLISGH AHVVSQTAVQ 
       660        670        680        690        700
VVADVLSKLL VVGITDPDPD IRYCVLASLD ERFDAHLAQA ENLQALFVAL 
       710        720        730        740        750
NDQVFEIREL AICTVGRLSS MNPAFVMPFL RKMLIQILTE LEHSGIGRIK 
       760        770        780        790        800
EQSARMLGHL VSNAPRLIRP YMEPILKALI LKLKDPDPDP NPGVINNVLA 
       810        820        830        840        850
TIGELAQVSG LEMRKWVDEL FIIIMDMLQD SSLLAKRQVA LWTLGQLVAS 
       860        870        880        890        900
TGYVVEPYRK YPTLLEVLLN FLKTEQNQGT RREAIRVLGL LGALDPYKHK 
       910        920        930        940        950
VNIGMIDQSR DASAVSLSES KSSQDSSDYS TSEMLVNMGN LPLDEFYPAV 
       960        970        980        990       1000
SMVALMRIFR DQSLSHHHTM VVQAITFIFK SLGLKCVQFL PQVMPTFLNV 
      1010       1020       1030       1040       1050
IRVCDGAIRE FLFQQLGMLV SFVKSHIRPY MDEIVTLMRE FWVMNTSIQS 
      1060       1070       1080       1090       1100
TIILLIEQIV VALGGEFKLY LPQLIPHMLR VFMHDNSPGR IVSIKLLAAI 
      1110       1120       1130       1140       1150
QLFGANLDDY LHLLLPPIVK LFDAPEAPLP SRKAALETVD RLTESLDFTD 
      1160       1170       1180       1190       1200
YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV 
      1210       1220       1230       1240       1250
RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSG QGDALASGPV 
      1260       1270       1280       1290       1300
ETGPMKKLHV STINLQKAWG AARRVSKDDW LEWLRRLSLE LLKDSSSPSL 
      1310       1320       1330       1340       1350
RSCWALAQAY NPMARDLFNA AFVSCWSELN EDQQDELIRS IELALTSQDI 
      1360       1370       1380       1390       1400
AEVTQTLLNL AEFMEHSDKG PLPLRDDNGI VLLGERAAKC RAYAKALHYK 
      1410       1420       1430       1440       1450
ELEFQKGPTP AILESLISIN NKLQQPEAAA GVLEYAMKHF GELEIQATWY 
      1460       1470       1480       1490       1500
EKLHEWEDAL VAYDKKMDTN KDDPELMLGR MRCLEALGEW GQLHQQCCEK 
      1510       1520       1530       1540       1550
WTLVNDETQA KMARMAAAAA WGLGQWDSME EYTCMIPRDT HDGAFYRAVL 
      1560       1570       1580       1590       1600
ALHQDLFSLA QQCIDKARDL LDAELTAMAG ESYSRAYGAM VSCHMLSELE 
      1610       1620       1630       1640       1650
EVIQYKLVPE RREIIRQIWW ERLQGCQRIV EDWQKILMVR SLVVSPHEDM 
      1660       1670       1680       1690       1700
RTWLKYASLC GKSGRLALAH KTLVLLLGVD PSRQLDHPLP TVHPQVTYAY 
      1710       1720       1730       1740       1750
MKNMWKSARK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK QELHKLMARC 
      1760       1770       1780       1790       1800
FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA 
      1810       1820       1830       1840       1850
VLHYKHQNQA RDEKKKLRHA SGANITNATT AATTAATATT TASTEGSNSE 
      1860       1870       1880       1890       1900
SEAESTENSP TPSPLQKKVT EDLSKTLLMY TVPAVQGFFR SISLSRGNNL 
      1910       1920       1930       1940       1950
QDTLRVLTLW FDYGHWPDVN EALVEGVKAI QIDTWLQVIP QLIARIDTPR 
      1960       1970       1980       1990       2000
PLVGRLIHQL LTDIGRYHPQ ALIYPLTVAS KSTTTARHNA ANKILKNMCE 
      2010       2020       2030       2040       2050
HSNTLVQQAM MVSEELIRVA ILWHEMWHEG LEEASRLYFG ERNVKGMFEV 
      2060       2070       2080       2090       2100
LEPLHAMMER GPQTLKETSF NQAYGRDLME AQEWCRKYMK SGNVKDLTQA 
      2110       2120       2130       2140       2150
WDLYYHVFRR ISKQLPQLTS LELQYVSPKL LMCRDLELAV PGTYDPNQPI 
      2160       2170       2180       2190       2200
IRIQSIAPSL QVITSKQRPR KLTLMGSNGH EFVFLLKGHE DLRQDERVMQ 
      2210       2220       2230       2240       2250
LFGLVNTLLA NDPTSLRKNL SIQRYAVIPL STNSGLIGWV PHCDTLHALI 
      2260       2270       2280       2290       2300
RDYREKKKIL LNIEHRIMLR MAPDYDHLTL MQKVEVFEHA VNNTAGDDLA 
      2310       2320       2330       2340       2350
KLLWLKSPSS EVWFDRRTNY TRSLAVMSMV GYILGLGDRH PSNLMLDRLS 
      2360       2370       2380       2390       2400
GKILHIDFGD CFEVAMTREK FPEKIPFRLT RMLTNAMEVT GLDGNYRITC 
      2410       2420       2430       2440       2450
HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNTKGNK RSRTRTDSYS 
      2460       2470       2480       2490       2500
AGQSVEILDG VELGEPAHKK TGTTVPESIH SFIGDGLVKP EALNKKAIQI 
      2510       2520       2530       2540 
INRVRDKLTG RDFSHDDTLD VPTQVELLIK QATSHENLCQ CYIGWCPFW
Length:2,549
Mass (Da):288,892
Last modified:November 1, 1995 - v1
<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:i7D9AD6E784882AB4
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B1AKP8B1AKP8_HUMAN
Serine/threonine-protein kinase mTO...
MTOR
754Annotation score:

Annotation score:2 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>
B1AKQ2B1AKQ2_HUMAN
Serine/threonine-protein kinase mTO...
MTOR
161Annotation score:

Annotation score:1 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAC39933 differs from that shown. Reason: Frameshift at positions 956 and 999.Curated
The sequence BAE06077 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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 conflicti353K → N in AAC39933 (PubMed:9653645).Curated1
Sequence conflicti359S → N in AAC39933 (PubMed:9653645).Curated1
Sequence conflicti364D → N in AAC39933 (PubMed:9653645).Curated1
Sequence conflicti390M → L in AAC39933 (PubMed:9653645).Curated1
Sequence conflicti430R → L in AAC39933 (PubMed:9653645).Curated1
Sequence conflicti455 – 457VLD → GVE in AAC39933 (PubMed:9653645).Curated3
Sequence conflicti461A → G in AAC39933 (PubMed:9653645).Curated1
Sequence conflicti482 – 484VFT → FFN in AAC39933 (PubMed:9653645).Curated3
Sequence conflicti489L → V in AAC39933 (PubMed:9653645).Curated1
Sequence conflicti513L → I in AAC39933 (PubMed:9653645).Curated1
Sequence conflicti539L → V in AAC39933 (PubMed:9653645).Curated1
Sequence conflicti553R → C in AAC39933 (PubMed:9653645).Curated1
Sequence conflicti857P → L in BAE06077 (Ref. 3) Curated1
Sequence conflicti1075I → S in AAC39933 (PubMed:9653645).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0415378A → S in a lung large cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_041538135M → T in a metastatic melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_078824624R → H in FCORD2; somatic mutation; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs913197212Ensembl.1
Natural variantiVAR_0415391083M → V1 PublicationCorresponds to variant dbSNP:rs56164650Ensembl.1
Natural variantiVAR_0415401134A → V1 PublicationCorresponds to variant dbSNP:rs28730685Ensembl.1
Natural variantiVAR_0415411178S → F1 PublicationCorresponds to variant dbSNP:rs55975118Ensembl.1
Natural variantiVAR_0788251376D → E Found in a patient with focal epilepsy; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs975577894Ensembl.1
Natural variantiVAR_0788261450Y → D in FCORD2; somatic mutation. 1 Publication1
Natural variantiVAR_0788271456W → G in FCORD2; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1085307114EnsemblClinVar.1
Natural variantiVAR_0788281459A → D in FCORD2; somatic mutation; increased TOR signaling. 1 Publication1
Natural variantiVAR_0788291459A → S in FCORD2; somatic mutation. 1 Publication1
Natural variantiVAR_0788301460L → P in FCORD2; somatic mutation; increased TOR signaling. 2 PublicationsCorresponds to variant dbSNP:rs1057519779EnsemblClinVar.1
Natural variantiVAR_0788311483C → R in FCORD2; somatic mutation; increased TOR signaling; increased kinase activity. 1 PublicationCorresponds to variant dbSNP:rs1057519914EnsemblClinVar.1
Natural variantiVAR_0788321490W → R in SKS. 1 Publication1
Natural variantiVAR_0788331595M → I in SKS. 1 PublicationCorresponds to variant dbSNP:rs869312671EnsemblClinVar.1
Natural variantiVAR_0788341709R → H in FCORD2; somatic mutation; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs587777895EnsemblClinVar.1
Natural variantiVAR_0750721799E → K in SKS; results in increased mTOR signaling. 2 PublicationsCorresponds to variant dbSNP:rs863225264EnsemblClinVar.1
Natural variantiVAR_0788351832A → T in SKS. 1 PublicationCorresponds to variant dbSNP:rs369088781EnsemblClinVar.1
Natural variantiVAR_0788361888F → C in SKS. 1 PublicationCorresponds to variant dbSNP:rs869312666EnsemblClinVar.1
Natural variantiVAR_0788371977T → K in FCORD2; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs587777893EnsemblClinVar.1
Natural variantiVAR_0415422011M → V in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication