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UniProtKB - Q8N122 (RPTOR_HUMAN)

Entry version 184 (07 Oct 2020)
Sequence version 1 (01 Oct 2002)
Previous versions | rss
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Protein

Regulatory-associated protein of mTOR

Gene

RPTOR

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

Involved in the control of the mammalian target of rapamycin complex 1 (mTORC1) activity which regulates cell growth and survival, and autophagy in response to nutrient and hormonal signals; functions as a scaffold for recruiting mTORC1 substrates. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Involved in ciliogenesis.3 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

Biological processHost-virus interaction

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q8N122

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		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-5628897, TP53 Regulates Metabolic Genes
R-HSA-8943724, Regulation of PTEN gene transcription
R-HSA-9639288, Amino acids regulate mTORC1

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q8N122

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

More...SignaLinki		Q8N122

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q8N122

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Regulatory-associated protein of mTOR
Short name:
Raptor
Alternative name(s):
p150 target of rapamycin (TOR)-scaffold protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RPTOR
Synonyms:KIAA1303, RAPTOR
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic 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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000141564.13

Human Gene Nomenclature Database

More...HGNCi		HGNC:30287, RPTOR

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		607130, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q8N122

<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, Lysosome

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi722S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-792. 1 Publication1
Mutagenesisi792S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-722. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		57521

Open Targets

More...OpenTargetsi		ENSG00000141564

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA165432629

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q8N122, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3120040

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		RPTOR

Domain mapping of disease mutations (DMDM)

More...DMDMi		46577501

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000512001 – 1335Regulatory-associated protein of mTORAdd BLAST1335

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 residuei696Phosphoserine; by MAPK8Combined sources2 Publications1
Modified residuei706Phosphothreonine; by MAPK82 Publications1
Modified residuei719Phosphoserine; by RPS6KA1Combined sources1 Publication1
Modified residuei721Phosphoserine; by RPS6KA11 Publication1
Modified residuei722Phosphoserine; by AMPK and RPS6KA1Combined sources2 Publications1
Modified residuei738PhosphoserineCombined sources1
Modified residuei792Phosphoserine; by AMPK1 Publication1
Modified residuei855Phosphoserine1 Publication1
Modified residuei859Phosphoserine; by MTORCombined sources1 Publication1
Modified residuei863Phosphoserine; by MAPK8 and MTORCombined sources2 Publications1
Modified residuei865PhosphothreonineCombined sources1
Modified residuei877PhosphoserineCombined sources1 Publication1

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

Insulin-stimulated phosphorylation at Ser-863 by MTOR and MAPK8 up-regulates mTORC1 activity. Osmotic stress also induces phosphorylation at Ser-696, Thr-706 and Ser-863 by MAPK8. Ser-863 phosphorylation is required for phosphorylation at Ser-855 and Ser-859. In response to nutrient limitation, phosphorylated by AMPK; phosphorylation promotes interaction with 14-3-3 proteins, leading to negative regulation of the mTORC1 complex. In response to growth factors, phosphorylated at Ser-719, Ser-721 and Ser-722 by RPS6KA1, which stimulates mTORC1 activity.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q8N122

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q8N122

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q8N122

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q8N122

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

More...PaxDbi		Q8N122

PeptideAtlas

More...PeptideAtlasi		Q8N122

PRoteomics IDEntifications database

More...PRIDEi		Q8N122

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		27504
71521 [Q8N122-1]
71522 [Q8N122-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q8N122

MetOSite database of methionine sulfoxide sites

More...MetOSitei		Q8N122

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

More...PhosphoSitePlusi		Q8N122

<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

Highly expressed in skeletal muscle, and in a lesser extent in brain, lung, small intestine, kidney and placenta. Isoform 3 is widely expressed, with highest levels in nasal mucosa and pituitary and lowest in spleen.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000141564, Expressed in frontal cortex and 175 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q8N122, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q8N122, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000141564, Low tissue specificity

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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR (PubMed:12150925, PubMed:12408816, PubMed:17386266, PubMed:25940091). mTORC1 binds to and is inhibited by FKBP12-rapamycin (PubMed:12408816, PubMed:15066126). Binds directly to 4EBP1 and RPS6KB1 independently of its association with MTOR (PubMed:12150925, PubMed:12150926). Binds preferentially to poorly or non-phosphorylated forms of EIF4EBP1, and this binding is critical to the ability of MTOR to catalyze phosphorylation (PubMed:12747827).

Forms a complex with MTOR under both leucine-rich and -poor conditions.

Interacts with ULK1 in a nutrient-dependent manner; the interaction is reduced during starvation (PubMed:19211835).

Interacts (when phosphorylated by AMPK) with 14-3-3 protein, leading to inhibition of its activity (PubMed:18439900).

Interacts with SPAG5; SPAG5 competes with MTOR for RPTOR-binding, resulting in decreased mTORC1 formation.

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 G3BP1. The complex formed with G3BP1 AND SPAG5 is increased by oxidative stress (PubMed:23953116).

Interacts with HTR6 (PubMed:23027611).

Interacts with PIH1D1 (PubMed:24036451).

Interacts with LARP1 (PubMed:25940091).

Interacts with BRAT1 (PubMed:25657994).

Interacts with SIK3 (PubMed:30232230).

14 Publications

(Microbial infection) Interacts with vaccinia virus protein F17; this interaction dysregulates mTOR.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		121582, 264 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-503, mTORC1 complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q8N122

Database of interacting proteins

More...DIPi		DIP-39482N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q8N122

Protein interaction database and analysis system

More...IntActi		Q8N122, 67 interactors

Molecular INTeraction database

More...MINTi		Q8N122

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000307272

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q8N122, protein

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

Secondary structure

11335
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		Q8N122

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati1020 – 1061WD 1Add BLAST42
Repeati1065 – 1106WD 2Add BLAST42
Repeati1121 – 1160WD 3Add BLAST40
Repeati1164 – 1203WD 4Add BLAST40
Repeati1209 – 1249WD 5Add BLAST41
Repeati1251 – 1291WD 6Add BLAST41
Repeati1299 – 1335WD 7Add BLAST37

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi881 – 887Poly-Ser7

<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 WD repeat RAPTOR family.Curated

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1517, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00640000091541

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_061814_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q8N122

KEGG Orthology (KO)

More...KOi		K07204

Identification of Orthologs from Complete Genome Data

More...OMAi		HQFEDHL

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q8N122

TreeFam database of animal gene trees

More...TreeFami		TF105729

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.25.10.10, 1 hit
2.130.10.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011989, ARM-like
IPR016024, ARM-type_fold
IPR000357, HEAT
IPR004083, Raptor
IPR029347, Raptor_N
IPR015943, WD40/YVTN_repeat-like_dom_sf
IPR001680, WD40_repeat
IPR017986, WD40_repeat_dom
IPR036322, WD40_repeat_dom_sf

The PANTHER Classification System

More...PANTHERi		PTHR12848, PTHR12848, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02985, HEAT, 1 hit
PF14538, Raptor_N, 1 hit
PF00400, WD40, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01302, Raptor_N, 1 hit
SM00320, WD40, 7 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48371, SSF48371, 1 hit
SSF50978, SSF50978, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50294, WD_REPEATS_REGION, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q8N122-1) [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
MESEMLQSPL LGLGEEDEAD LTDWNLPLAF MKKRHCEKIE GSKSLAQSWR 
        60         70         80         90        100
MKDRMKTVSV ALVLCLNVGV DPPDVVKTTP CARLECWIDP LSMGPQKALE 
       110        120        130        140        150
TIGANLQKQY ENWQPRARYK QSLDPTVDEV KKLCTSLRRN AKEERVLFHY 
       160        170        180        190        200
NGHGVPRPTV NGEVWVFNKN YTQYIPLSIY DLQTWMGSPS IFVYDCSNAG 
       210        220        230        240        250
LIVKSFKQFA LQREQELEVA AINPNHPLAQ MPLPPSMKNC IQLAACEATE 
       260        270        280        290        300
LLPMIPDLPA DLFTSCLTTP IKIALRWFCM QKCVSLVPGV TLDLIEKIPG 
       310        320        330        340        350
RLNDRRTPLG ELNWIFTAIT DTIAWNVLPR DLFQKLFRQD LLVASLFRNF 
       360        370        380        390        400
LLAERIMRSY NCTPVSSPRL PPTYMHAMWQ AWDLAVDICL SQLPTIIEEG 
       410        420        430        440        450
TAFRHSPFFA EQLTAFQVWL TMGVENRNPP EQLPIVLQVL LSQVHRLRAL 
       460        470        480        490        500
DLLGRFLDLG PWAVSLALSV GIFPYVLKLL QSSARELRPL LVFIWAKILA 
       510        520        530        540        550
VDSSCQADLV KDNGHKYFLS VLADPYMPAE HRTMTAFILA VIVNSYHTGQ 
       560        570        580        590        600
EACLQGNLIA ICLEQLNDPH PLLRQWVAIC LGRIWQNFDS ARWCGVRDSA 
       610        620        630        640        650
HEKLYSLLSD PIPEVRCAAV FALGTFVGNS AERTDHSTTI DHNVAMMLAQ 
       660        670        680        690        700
LVSDGSPMVR KELVVALSHL VVQYESNFCT VALQFIEEEK NYALPSPATT 
       710        720        730        740        750
EGGSLTPVRD SPCTPRLRSV SSYGNIRAVA TARSLNKSLQ NLSLTEESGG 
       760        770        780        790        800
AVAFSPGNLS TSSSASSTLG SPENEEHILS FETIDKMRRA SSYSSLNSLI 
       810        820        830        840        850
GVSFNSVYTQ IWRVLLHLAA DPYPEVSDVA MKVLNSIAYK ATVNARPQRV 
       860        870        880        890        900
LDTSSLTQSA PASPTNKGVH IHQAGGSPPA SSTSSSSLTN DVAKQPVSRD 
       910        920        930        940        950
LPSGRPGTTG PAGAQYTPHS HQFPRTRKMF DKGPEQTADD ADDAAGHKSF 
       960        970        980        990       1000
ISATVQTGFC DWSARYFAQP VMKIPEEHDL ESQIRKEREW RFLRNSRVRR 
      1010       1020       1030       1040       1050
QAQQVIQKGI TRLDDQIFLN RNPGVPSVVK FHPFTPCIAV ADKDSICFWD 
      1060       1070       1080       1090       1100
WEKGEKLDYF HNGNPRYTRV TAMEYLNGQD CSLLLTATDD GAIRVWKNFA 
      1110       1120       1130       1140       1150
DLEKNPEMVT AWQGLSDMLP TTRGAGMVVD WEQETGLLMS SGDVRIVRIW 
      1160       1170       1180       1190       1200
DTDREMKVQD IPTGADSCVT SLSCDSHRSL IVAGLGDGSI RVYDRRMALS 
      1210       1220       1230       1240       1250
ECRVMTYREH TAWVVKASLQ KRPDGHIVSV SVNGDVRIFD PRMPESVNVL 
      1260       1270       1280       1290       1300
QIVKGLTALD IHPQADLIAC GSVNQFTAIY NSSGELINNI KYYDGFMGQR 
      1310       1320       1330 
VGAISCLAFH PHWPHLAVGS NDYYISVYSV EKRVR
Length:1,335
Mass (Da):149,038
Last modified:October 1, 2002 - 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:i688ED1943F45045A
GO
Isoform 2 (identifier: Q8N122-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     380-1335: Missing.

Show »
Length:379
Mass (Da):43,256
Checksum:iD67B01D4E68E859E
GO
Isoform 3 (identifier: Q8N122-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     504-661: Missing.

Show »
Length:1,177
Mass (Da):131,515
Checksum:i1CE0DA04E72105B2
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
I3L436I3L436_HUMAN
Regulatory-associated protein of mT...
RPTOR
235Annotation 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>
I3L2I3I3L2I3_HUMAN
Regulatory-associated protein of mT...
RPTOR
95Annotation 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>

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 conflicti217 – 218LE → RQ in BAA92541 (PubMed:10718198).Curated2

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_010174380 – 1335Missing in isoform 2. 1 PublicationAdd BLAST956
Alternative sequenceiVSP_054042504 – 661Missing in isoform 3. 1 PublicationAdd BLAST158

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
AY090663 mRNA Translation: AAM09075.1
AB082951 mRNA Translation: BAC06490.1
AC016245 Genomic DNA No translation available.
AC109327 Genomic DNA No translation available.
AC127496 Genomic DNA No translation available.
AC133012 Genomic DNA No translation available.
CH471099 Genomic DNA Translation: EAW89618.1
BC025180 mRNA Translation: AAH25180.1
BC033258 mRNA Translation: AAH33258.1
BC064515 mRNA Translation: AAH64515.1
BC136652 mRNA Translation: AAI36653.1
BC136654 mRNA Translation: AAI36655.1
AB037724 mRNA Translation: BAA92541.1
GQ183898 mRNA Translation: ACS44766.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS11773.1 [Q8N122-1]
CCDS54175.1 [Q8N122-3]

NCBI Reference Sequences

More...RefSeqi		NP_001156506.1, NM_001163034.1 [Q8N122-3]
NP_065812.1, NM_020761.2 [Q8N122-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000306801; ENSP00000307272; ENSG00000141564 [Q8N122-1]
ENST00000544334; ENSP00000442479; ENSG00000141564 [Q8N122-3]
ENST00000570891; ENSP00000460136; ENSG00000141564 [Q8N122-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		57521

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:57521

UCSC genome browser

More...UCSCi		uc002jys.5, human [Q8N122-1]

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
AY090663 mRNA Translation: AAM09075.1
AB082951 mRNA Translation: BAC06490.1
AC016245 Genomic DNA No translation available.
AC109327 Genomic DNA No translation available.
AC127496 Genomic DNA No translation available.
AC133012 Genomic DNA No translation available.
CH471099 Genomic DNA Translation: EAW89618.1
BC025180 mRNA Translation: AAH25180.1
BC033258 mRNA Translation: AAH33258.1
BC064515 mRNA Translation: AAH64515.1
BC136652 mRNA Translation: AAI36653.1
BC136654 mRNA Translation: AAI36655.1
AB037724 mRNA Translation: BAA92541.1
GQ183898 mRNA Translation: ACS44766.1
CCDSiCCDS11773.1 [Q8N122-1]
CCDS54175.1 [Q8N122-3]
RefSeqiNP_001156506.1, NM_001163034.1 [Q8N122-3]
NP_065812.1, NM_020761.2 [Q8N122-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5H64electron microscopy4.40B/b1-1335[»]
6BCUelectron microscopy3.43W/Y2-1335[»]
6BCXelectron microscopy3.00W/Y2-1335[»]
6SB0electron microscopy5.50N/Y1-1335[»]
6SB2electron microscopy6.20N/Y1-1335[»]
6U62electron microscopy3.18A1-1335[»]
SMRiQ8N122
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi121582, 264 interactors
ComplexPortaliCPX-503, mTORC1 complex
CORUMiQ8N122
DIPiDIP-39482N
ELMiQ8N122
IntActiQ8N122, 67 interactors
MINTiQ8N122
STRINGi9606.ENSP00000307272

Chemistry databases

ChEMBLiCHEMBL3120040

PTM databases

iPTMnetiQ8N122
MetOSiteiQ8N122
PhosphoSitePlusiQ8N122

Polymorphism and mutation databases

BioMutaiRPTOR
DMDMi46577501

Proteomic databases

EPDiQ8N122
jPOSTiQ8N122
MassIVEiQ8N122
MaxQBiQ8N122
PaxDbiQ8N122
PeptideAtlasiQ8N122
PRIDEiQ8N122
ProteomicsDBi27504
71521 [Q8N122-1]
71522 [Q8N122-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		4616, 591 antibodies

The CPTC Antibody Portal

More...CPTCi		Q8N122, 2 antibodies

The DNASU plasmid repository

More...DNASUi		57521

Genome annotation databases

EnsembliENST00000306801; ENSP00000307272; ENSG00000141564 [Q8N122-1]
ENST00000544334; ENSP00000442479; ENSG00000141564 [Q8N122-3]
ENST00000570891; ENSP00000460136; ENSG00000141564 [Q8N122-2]
GeneIDi57521
KEGGihsa:57521
UCSCiuc002jys.5, human [Q8N122-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		57521
DisGeNETi57521
EuPathDBiHostDB:ENSG00000141564.13

GeneCards: human genes, protein and diseases

More...GeneCardsi		RPTOR
HGNCiHGNC:30287, RPTOR
HPAiENSG00000141564, Low tissue specificity
MIMi607130, gene
neXtProtiNX_Q8N122
OpenTargetsiENSG00000141564
PharmGKBiPA165432629

Human Unidentified Gene-Encoded large proteins database

More...HUGEi		Search...

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1517, Eukaryota
GeneTreeiENSGT00640000091541
HOGENOMiCLU_061814_0_0_1
InParanoidiQ8N122
KOiK07204
OMAiHQFEDHL
PhylomeDBiQ8N122
TreeFamiTF105729

Enzyme and pathway databases

PathwayCommonsiQ8N122
ReactomeiR-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-5628897, TP53 Regulates Metabolic Genes
R-HSA-8943724, Regulation of PTEN gene transcription
R-HSA-9639288, Amino acids regulate mTORC1
SABIO-RKiQ8N122
SignaLinkiQ8N122
SIGNORiQ8N122

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		57521, 596 hits in 882 CRISPR screens

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

More...ChiTaRSi		RPTOR, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		RPTOR

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		57521
PharosiQ8N122, Tbio

Protein Ontology

More...PROi		PR:Q8N122
RNActiQ8N122, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000141564, Expressed in frontal cortex and 175 other tissues
ExpressionAtlasiQ8N122, baseline and differential
GenevisibleiQ8N122, HS

Family and domain databases

Gene3Di1.25.10.10, 1 hit
2.130.10.10, 2 hits
InterProiView protein in InterPro
IPR011989, ARM-like
IPR016024, ARM-type_fold
IPR000357, HEAT
IPR004083, Raptor
IPR029347, Raptor_N
IPR015943, WD40/YVTN_repeat-like_dom_sf
IPR001680, WD40_repeat
IPR017986, WD40_repeat_dom
IPR036322, WD40_repeat_dom_sf
PANTHERiPTHR12848, PTHR12848, 1 hit
PfamiView protein in Pfam
PF02985, HEAT, 1 hit
PF14538, Raptor_N, 1 hit
PF00400, WD40, 1 hit
SMARTiView protein in SMART
SM01302, Raptor_N, 1 hit
SM00320, WD40, 7 hits
SUPFAMiSSF48371, SSF48371, 1 hit
SSF50978, SSF50978, 1 hit
PROSITEiView protein in PROSITE
PS50294, WD_REPEATS_REGION, 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 nameiRPTOR_HUMAN
<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: Q8N122
Secondary accession number(s): B2RN36
, C6KEF2, F5H7J5, Q8N4V9, Q8TB32, Q9P2P3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 1, 2002
Last modified: October 7, 2020
This is version 184 of the entry and version 1 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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