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Entry version 179 (18 Sep 2019)
Sequence version 2 (15 Jun 2010)
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Protein

Serine/threonine-protein kinase mTOR

Gene

Mtor

Organism
Mus musculus (Mouse)
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:15467718, PubMed:15545625, PubMed:16221682, PubMed:16915281, PubMed:16962653, PubMed:18046414, PubMed:19440205, PubMed:21659604). MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins (PubMed:15467718, PubMed:15545625, PubMed:16221682, PubMed:16915281, PubMed:16962653, PubMed:18046414, PubMed:19440205, PubMed:21659604). Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2) (PubMed:15467718, PubMed:16962653, PubMed:21659604). Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis (By similarity). 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 (By similarity). 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 (By similarity). Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor (By similarity). In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1 (PubMed:11792863). To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A (PubMed:18046414). mTORC1 also negatively regulates autophagy through phosphorylation of ULK1 (PubMed:21258367). Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1 (PubMed:21258367). Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP (By similarity). Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions (By similarity). 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 (By similarity). As part of the mTORC2 complex MTOR may regulate other cellular processes including survival and organization of the cytoskeleton (By similarity). 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 (By similarity). 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 (By similarity). mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422' (By similarity). Regulates osteoclastogenesis by adjusting the expression of CEBPB isoforms (PubMed:19440205). Plays an important regulatory role in the circadian clock function; regulates period length and rhythm amplitude of the suprachiasmatic nucleus (SCN) and liver clocks (PubMed:29750810).By similarity11 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. 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.By similarity2 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

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 processBiological rhythms
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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

<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:2.7.11.11 Publication)
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 target protein 1
Short name:
RAPT1
<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
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 4

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:1928394 Mtor

<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, 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

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>Mutagenesisi2035S → R: Abolishes interaction with the FKBP1A-rapamycin complex. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1255165

<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_00000888091 – 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-acetylmethionineBy similarity1
Modified residuei567PhosphoserineBy similarity1
Modified residuei1162PhosphothreonineBy similarity1
Modified residuei1218N6-acetyllysineBy similarity1
Modified residuei1261PhosphoserineCombined sources1 Publication1
Modified residuei2159PhosphoserineBy similarity1
Modified residuei2164PhosphothreonineBy similarity1
Modified residuei2173Phosphothreonine; by PKB/AKT1By similarity1
Modified residuei2446Phosphothreonine; by RPS6KB1By similarity1
Modified residuei2448Phosphoserine; by RPS6KB11 Publication1
Modified residuei2478PhosphoserineCombined sources1
Modified residuei2481PhosphoserineCombined sources1

<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

Phosphorylation at Thr-2173 in the ATP-binding region by AKT1 strongly reduces kinase activity (By similarity). 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.By similarity2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9JLN9

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9JLN9

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

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PaxDbi
Q9JLN9

PeptideAtlas

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PeptideAtlasi
Q9JLN9

PRoteomics IDEntifications database

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PRIDEi
Q9JLN9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9JLN9

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

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PhosphoSitePlusi
Q9JLN9

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q9JLN9

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000028991 Expressed in 299 organ(s), highest expression level in epithelium of lens

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9JLN9 MM

<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 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 (By similarity).

Interacts with PLPP7 and PML.

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 (By similarity).

Interacts with MEAK7 (via C-terminal domain); the interaction increases upon nutrient stimulation (By similarity).

Interacts with TM4SF5; the interaction is positively regulated by arginine and is negatively regulated by leucine (By similarity).

By similarity7 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
208142, 22 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9JLN9

Database of interacting proteins

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DIPi
DIP-40570N

Protein interaction database and analysis system

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IntActi
Q9JLN9, 24 interactors

Molecular INTeraction database

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MINTi
Q9JLN9

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000099510

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q9JLN9

<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
Q9JLN9

Database of comparative protein structure models

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ModBasei
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>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 NBNBy similarityAdd BLAST651
Regioni2012 – 2144Sufficient for interaction with the FKBP1A/rapamycin complexAdd BLAST133
Regioni2258 – 2296Interaction with MLST8By similarityAdd 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.By similarity
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 (By similarity).By similarity

<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

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GeneTreei
ENSGT00930000151037

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000163215

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9JLN9

KEGG Orthology (KO)

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KOi
K07203

Identification of Orthologs from Complete Genome Data

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OMAi
LNIQRYP

Database of Orthologous Groups

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OrthoDBi
26975at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9JLN9

TreeFam database of animal gene trees

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TreeFami
TF105134

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.1070.11, 1 hit
1.20.120.150, 1 hit
1.25.10.10, 4 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR024585 DUF3385_TOR
IPR003152 FATC_dom
IPR009076 FRB_dom
IPR036738 FRB_sf
IPR011009 Kinase-like_dom_sf
IPR000403 PI3/4_kinase_cat_dom
IPR036940 PI3/4_kinase_cat_sf
IPR018936 PI3/4_kinase_CS
IPR003151 PIK-rel_kinase_FAT
IPR014009 PIK_FAT
IPR026683 TOR

The PANTHER Classification System

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PANTHERi
PTHR11139:SF9 PTHR11139:SF9, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF11865 DUF3385, 1 hit
PF02259 FAT, 1 hit
PF02260 FATC, 1 hit
PF08771 FRB_dom, 1 hit
PF00454 PI3_PI4_kinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47212 SSF47212, 1 hit
SSF48371 SSF48371, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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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>Sequences (2)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 describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q9JLN9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MLGTGPAVAT ASAATSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM
60 70 80 90 100
ELREMSQEES TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN
110 120 130 140 150
STRIGRFANY LRNLLPSSDP 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 AVQPQQPNAL VGLLGYSSPQ GLMGFGTSPS
360 370 380 390 400
PAKSTLVESR CCRDLMEEKF DQVCQWVLKC RSSKNSLIQM TILNLLPRLA
410 420 430 440 450
AFRPSAFTDT QYLQDTMNHV LSCVKKEKER TAAFQALGLL SVAVRSEFKV
460 470 480 490 500
YLPRVLDIIR AALPPKDFAH KRQKTVQVDA TVFTCISMLA RAMGPGIQQD
510 520 530 540 550
IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL KMLSLVLMHK
560 570 580 590 600
PLRHPGMPKG LAHQLASPGL TTLPEASDVA 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 VFMHDNSQGR IVSIKLLAAI
1110 1120 1130 1140 1150
QLFGANLDDY LHLLLPPIVK LFDAPEVPLP SRKAALETVD RLTESLDFTD
1160 1170 1180 1190 1200
YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV
1210 1220 1230 1240 1250
RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSS 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 NKLQQPEAAS GVLEYAMKHF GELEIQATWY
1460 1470 1480 1490 1500
EKLHEWEDAL VAYDKKMDTN KEDPELMLGR 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 TAHPQVTYAY
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 AATTAASAAA ATSTEGSNSE
1860 1870 1880 1890 1900
SEAESNENSP TPSPLQKKVT EDLSKTLLLY 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 GLDGNYRTTC
2410 2420 2430 2440 2450
HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNTKGNK RSRTRTDSYS
2460 2470 2480 2490 2500
AGQSVEILDG VELGEPAHKK AGTTVPESIH SFIGDGLVKP EALNKKAIQI
2510 2520 2530 2540
INRVRDKLTG RDFSHDDTLD VPTQVELLIK QATSHENLCQ CYIGWCPFW
Length:2,549
Mass (Da):288,789
Last modified:June 15, 2010 - v2
<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:i56302E5171FB6DBD
GO
Isoform 2 (identifier: Q9JLN9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     236-256: HTFEEAEKGFDETLAKEKGMN → VRDGSTQPLAKHFGLESCSWP
     257-2549: Missing.

Note: No experimental confirmation available.
Show »
Length:256
Mass (Da):28,467
Checksum:iF58320768DC9E928
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 conflicti33N → K in AAH43920 (PubMed:15489334).Curated1
Sequence conflicti628R → C in AAF73196 (Ref. 1) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_011909236 – 256HTFEE…EKGMN → VRDGSTQPLAKHFGLESCSW P in isoform 2. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_011910257 – 2549Missing in isoform 2. 1 PublicationAdd BLAST2293

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
AF152838 mRNA Translation: AAF73196.1
AL713995 Genomic DNA No translation available.
AL731654 Genomic DNA No translation available.
CU210865 Genomic DNA No translation available.
BC043920 mRNA Translation: AAH43920.1
BC112904 mRNA Translation: AAI12905.1
AK012031 mRNA Translation: BAB27985.2

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS18937.1 [Q9JLN9-1]

NCBI Reference Sequences

More...
RefSeqi
NP_064393.2, NM_020009.2 [Q9JLN9-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000057580; ENSMUSP00000054164; ENSMUSG00000028991 [Q9JLN9-2]
ENSMUST00000103221; ENSMUSP00000099510; ENSMUSG00000028991 [Q9JLN9-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
56717

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:56717

UCSC genome browser

More...
UCSCi
uc008vuq.3 mouse [Q9JLN9-2]
uc008vur.2 mouse [Q9JLN9-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AF152838 mRNA Translation: AAF73196.1
AL713995 Genomic DNA No translation available.
AL731654 Genomic DNA No translation available.
CU210865 Genomic DNA No translation available.
BC043920 mRNA Translation: AAH43920.1
BC112904 mRNA Translation: AAI12905.1
AK012031 mRNA Translation: BAB27985.2
CCDSiCCDS18937.1 [Q9JLN9-1]
RefSeqiNP_064393.2, NM_020009.2 [Q9JLN9-1]

3D structure databases

SMRiQ9JLN9
ModBaseiSearch...

Protein-protein interaction databases

BioGridi208142, 22 interactors
CORUMiQ9JLN9
DIPiDIP-40570N
IntActiQ9JLN9, 24 interactors
MINTiQ9JLN9
STRINGi10090.ENSMUSP00000099510

Chemistry databases

BindingDBiQ9JLN9
ChEMBLiCHEMBL1255165

PTM databases

iPTMnetiQ9JLN9
PhosphoSitePlusiQ9JLN9
SwissPalmiQ9JLN9

Proteomic databases

EPDiQ9JLN9
jPOSTiQ9JLN9
PaxDbiQ9JLN9
PeptideAtlasiQ9JLN9
PRIDEiQ9JLN9

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000057580; ENSMUSP00000054164; ENSMUSG00000028991 [Q9JLN9-2]
ENSMUST00000103221; ENSMUSP00000099510; ENSMUSG00000028991 [Q9JLN9-1]
GeneIDi56717
KEGGimmu:56717
UCSCiuc008vuq.3 mouse [Q9JLN9-2]
uc008vur.2 mouse [Q9JLN9-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2475
MGIiMGI:1928394 Mtor

Phylogenomic databases

eggNOGiKOG0891 Eukaryota
COG5032 LUCA
GeneTreeiENSGT00930000151037
HOGENOMiHOG000163215
InParanoidiQ9JLN9
KOiK07203
OMAiLNIQRYP
OrthoDBi26975at2759
PhylomeDBiQ9JLN9
TreeFamiTF105134

Enzyme and pathway databases

ReactomeiR-MMU-1257604 PIP3 activates AKT signaling
R-MMU-1632852 Macroautophagy
R-MMU-165159 mTOR signalling
R-MMU-166208 mTORC1-mediated signalling
R-MMU-3371571 HSF1-dependent transactivation
R-MMU-380972 Energy dependent regulation of mTOR by LKB1-AMPK
R-MMU-389357 CD28 dependent PI3K/Akt signaling
R-MMU-5218920 VEGFR2 mediated vascular permeability
R-MMU-5628897 TP53 Regulates Metabolic Genes
R-MMU-8943724 Regulation of PTEN gene transcription

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Mtor mouse

Protein Ontology

More...
PROi
PR:Q9JLN9

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000028991 Expressed in 299 organ(s), highest expression level in epithelium of lens
GenevisibleiQ9JLN9 MM

Family and domain databases

Gene3Di1.10.1070.11, 1 hit
1.20.120.150, 1 hit
1.25.10.10, 4 hits
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR024585 DUF3385_TOR
IPR003152 FATC_dom
IPR009076 FRB_dom
IPR036738 FRB_sf
IPR011009 Kinase-like_dom_sf
IPR000403 PI3/4_kinase_cat_dom
IPR036940 PI3/4_kinase_cat_sf
IPR018936 PI3/4_kinase_CS
IPR003151 PIK-rel_kinase_FAT
IPR014009 PIK_FAT
IPR026683 TOR
PANTHERiPTHR11139:SF9 PTHR11139:SF9, 1 hit
PfamiView protein in Pfam
PF11865 DUF3385, 1 hit
PF02259 FAT, 1 hit
PF02260 FATC, 1 hit
PF08771 FRB_dom, 1 hit
PF00454 PI3_PI4_kinase, 1 hit
SMARTiView protein in SMART
SM01346 DUF3385, 1 hit
SM01343 FATC, 1 hit
SM00146 PI3Kc, 1 hit
SUPFAMiSSF47212 SSF47212, 1 hit
SSF48371 SSF48371, 1 hit
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

More...
ProtoNeti
Search...

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 nameiMTOR_MOUSE
<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: Q9JLN9
Secondary accession number(s): Q2KHT0, Q811J5, Q9CST1
<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: April 27, 2001
Last sequence update: June 15, 2010
Last modified: September 18, 2019
This is version 179 of the entry and version 2 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 programChordata 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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