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UniProtKB - Q15382 (RHEB_HUMAN)

Entry version 206 (13 Feb 2019)
Sequence version 1 (01 Nov 1996)
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Protein

GTP-binding protein Rheb

Gene

RHEB

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

Activates the protein kinase activity of mTORC1, and thereby plays a role in the regulation of apoptosis. Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Has low intrinsic GTPase activity.6 Publications

Miscellaneous

The conserved catalytic Gln-64 found in other Ras-like GTPases seems not to be involved in GTP hydrolysis in RHEB.Curated

<p>This subsection of the ‘Function’ 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

Alternates between an inactive form bound to GDP and an active form bound to GTP. Inactivated by TSC1-TSC2 via the GTPase activating protein (GAP) domain of TSC2.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi20Magnesium1 Publication1
Metal bindingi38Magnesium1 Publication1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei63GTP; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi16 – 21GTP2 Publications6
Nucleotide bindingi32 – 38GTP2 Publications7
Nucleotide bindingi119 – 122GTP2 Publications4
Nucleotide bindingi149 – 150GTP2 Publications2

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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

LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

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-380972 Energy dependent regulation of mTOR by LKB1-AMPK
R-HSA-5628897 TP53 Regulates Metabolic Genes
R-HSA-8943724 Regulation of PTEN gene transcription

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q15382

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

More...SignaLinki		Q15382

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q15382

<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:
GTP-binding protein Rheb
Alternative name(s):
Ras homolog enriched in brain
<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:RHEB
Synonyms:RHEB2
<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 7

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000106615.9

Human Gene Nomenclature Database

More...HGNCi		HGNC:10011 RHEB

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601293 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q15382

<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, Membrane

<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>Mutagenesisi15R → G: Partially resistant to inactivation by TSC1-TSC2. 1 Publication1
Mutagenesisi20S → N: Deficient in guanine nucleotide binding. Unable to rescue S6K1 from inactivation by amino-acid withdrawal. 2 Publications1
Mutagenesisi38T → M: Slightly impairs signaling through mTORC1, but still binds guanine nucleotides normally. 2 Publications1
Mutagenesisi39I → K: Impairs S6K1 activation, but still binds guanine nucleotides normally. 1 Publication1
Mutagenesisi40E → G: No effect. 1 Publication1
Mutagenesisi41N → A: Impairs interaction with MTOR. Impairs signaling through mTORC1, but still binds guanine nucleotides normally. 2 Publications1
Mutagenesisi43F → C: No effect. 1 Publication1
Mutagenesisi46L → A: Causes slight reduction in S6K1 activation. 1 Publication1
Mutagenesisi48T → A: Causes slightly reduced phosphorylation of EIF4EBP1. 1 Publication1
Mutagenesisi49V → A: Causes slightly reduced phosphorylation of EIF4EBP1. 1 Publication1
Mutagenesisi53E → A: Causes slightly reduced phosphorylation of EIF4EBP1. 1 Publication1
Mutagenesisi54Y → A: Partially deficient in guanine nucleotide binding. Fully impairs EIF4EBP1 phosphorylation and S6K1 activation. 1 Publication1
Mutagenesisi56L → A: Partially deficient in guanine nucleotide binding. Fully impairs EIF4EBP1 phosphorylation and S6K1 activation. 1 Publication1
Mutagenesisi60D → I: Deficient in guanine nucleotide binding. Unable to rescue S6K1 from inactivation by amino-acid withdrawal. 1 Publication1
Mutagenesisi64Q → L: Has a higher basal GTPase level, however, is still sensitive to TSC2 GAP activity. 1 Publication1
Mutagenesisi181C → S: Reduces the ability to rescue S6K1 from inactivation by amino-acid withdrawal. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		6009

Open Targets

More...OpenTargetsi		ENSG00000106615

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA34389

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3108656

Drug and drug target database

More...DrugBanki		DB04315 Guanosine-5'-Diphosphate
DB04137 Guanosine-5'-Triphosphate

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		RHEB

Domain mapping of disease mutations (DMDM)

More...DMDMi		6919957

<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_00000827081 – 181GTP-binding protein RhebAdd BLAST181
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000281365182 – 184Removed in mature form3

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 residuei130Phosphoserine; by MAPKAPK5By similarity1
Modified residuei181Cysteine methyl esterCombined sources2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi181S-farnesyl cysteineCombined sources2 Publications1

<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

Farnesylation is important for efficiently activating mTORC1-mediated signaling.
Phosphorylation by MAPKAPK5 impairs GTP-binding and inactivation.By similarity

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q15382

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q15382

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q15382

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

More...PaxDbi		Q15382

PeptideAtlas

More...PeptideAtlasi		Q15382

PRoteomics IDEntifications database

More...PRIDEi		Q15382

ProteomicsDB human proteome resource

More...ProteomicsDBi		60554

Consortium for Top Down Proteomics

More...TopDownProteomicsi		Q15382

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q15382

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

More...PhosphoSitePlusi		Q15382

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q15382

<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

Ubiquitous. Highest levels observed in skeletal and cardiac muscle.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000106615 Expressed in 180 organ(s), highest expression level in caudate nucleus

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q15382 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q15382 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB019436

<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

Binds to mTORC1 in a guanyl nucleotide-independent manner. Interacts directly with MTOR, MLST8 and RPTOR. Interacts with TSC2. Interacts (when prenylated) with PDE6D; this promotes release from membranes.4 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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		111941, 51 interactors

Database of interacting proteins

More...DIPi		DIP-42816N

Protein interaction database and analysis system

More...IntActi		Q15382, 19 interactors

Molecular INTeraction database

More...MINTi		Q15382

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000262187

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q15382

<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

1184
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1XTQX-ray2.00A1-169[»]
1XTRX-ray2.65A1-169[»]
1XTSX-ray2.80A1-169[»]
3SEAX-ray2.00A/B3-169[»]
3T5GX-ray1.70A1-181[»]
5YXHX-ray2.04A/B/C/D2-169[»]
6BCUelectron microscopy3.43R/S1-184[»]
6BSXX-ray1.65A/B/C/D1-169[»]
6BT0X-ray2.60A/B/C/D1-169[»]

Database of protein disorder

More...DisProti		DP00364

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q15382

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

More...SMRi		Q15382

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		Q15382

<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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi35 – 43Effector regionCurated9

<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 small GTPase superfamily. Rheb family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0395 Eukaryota
COG1100 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159945

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000233973

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG009351

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q15382

KEGG Orthology (KO)

More...KOi		K07208

Identification of Orthologs from Complete Genome Data

More...OMAi		FIENHFV

Database of Orthologous Groups

More...OrthoDBi		1320427at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q15382

TreeFam database of animal gene trees

More...TreeFami		TF314986

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR027417 P-loop_NTPase
IPR037586 RHEB
IPR005225 Small_GTP-bd_dom
IPR001806 Small_GTPase
IPR020849 Small_GTPase_Ras-type

The PANTHER Classification System

More...PANTHERi		PTHR24070 PTHR24070, 1 hit
PTHR24070:SF264 PTHR24070:SF264, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00071 Ras, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00231 small_GTP, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51421 RAS, 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>.<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

Q15382-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPQSKSRKIA ILGYRSVGKS SLTIQFVEGQ FVDSYDPTIE NTFTKLITVN 
        60         70         80         90        100
GQEYHLQLVD TAGQDEYSIF PQTYSIDING YILVYSVTSI KSFEVIKVIH 
       110        120        130        140        150
GKLLDMVGKV QIPIMLVGNK KDLHMERVIS YEEGKALAES WNAAFLESSA 
       160        170        180 
KENQTAVDVF RRIILEAEKM DGAASQGKSS CSVM
Length:184
Mass (Da):20,497
Last modified:November 1, 1996 - 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:i8F4C8080BDF928FD
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9J931C9J931_HUMAN
GTP-binding protein Rheb
RHEB
79Annotation 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>
F8WBL3F8WBL3_HUMAN
GTP-binding protein Rheb
RHEB
47Annotation 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>
C9J469C9J469_HUMAN
GTP-binding protein Rheb
RHEB
19Annotation 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 conflicti118G → W in BAA11211 (PubMed:8661031).Curated1

Natural variant

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_036310139E → K in a colorectal cancer sample; somatic mutation. 1 Publication1

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
Z29677 mRNA Translation: CAA82774.1
D78132 mRNA Translation: BAA11211.1
AF148645 mRNA Translation: AAF73125.1
AF493921 mRNA Translation: AAM12635.1
AK125446 mRNA Translation: BAG54198.1
BT006958 mRNA Translation: AAP35604.1
AC005996 Genomic DNA Translation: AAD15548.1
CH471173 Genomic DNA Translation: EAW53989.1
BC016155 mRNA Translation: AAH16155.1
BC107705 mRNA Translation: AAI07706.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS5927.1

Protein sequence database of the Protein Information Resource

More...PIRi		S68419 S41960

NCBI Reference Sequences

More...RefSeqi		NP_005605.1, NM_005614.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.283521
Hs.568850
Hs.647068

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000262187; ENSP00000262187; ENSG00000106615

Database of genes from NCBI RefSeq genomes

More...GeneIDi		6009

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:6009

UCSC genome browser

More...UCSCi		uc003wkh.1 human

Keywords - Coding sequence diversityi

Polymorphism

<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
Z29677 mRNA Translation: CAA82774.1
D78132 mRNA Translation: BAA11211.1
AF148645 mRNA Translation: AAF73125.1
AF493921 mRNA Translation: AAM12635.1
AK125446 mRNA Translation: BAG54198.1
BT006958 mRNA Translation: AAP35604.1
AC005996 Genomic DNA Translation: AAD15548.1
CH471173 Genomic DNA Translation: EAW53989.1
BC016155 mRNA Translation: AAH16155.1
BC107705 mRNA Translation: AAI07706.1
CCDSiCCDS5927.1
PIRiS68419 S41960
RefSeqiNP_005605.1, NM_005614.3
UniGeneiHs.283521
Hs.568850
Hs.647068

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XTQX-ray2.00A1-169[»]
1XTRX-ray2.65A1-169[»]
1XTSX-ray2.80A1-169[»]
3SEAX-ray2.00A/B3-169[»]
3T5GX-ray1.70A1-181[»]
5YXHX-ray2.04A/B/C/D2-169[»]
6BCUelectron microscopy3.43R/S1-184[»]
6BSXX-ray1.65A/B/C/D1-169[»]
6BT0X-ray2.60A/B/C/D1-169[»]
DisProtiDP00364
ProteinModelPortaliQ15382
SMRiQ15382
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111941, 51 interactors
DIPiDIP-42816N
IntActiQ15382, 19 interactors
MINTiQ15382
STRINGi9606.ENSP00000262187

Chemistry databases

BindingDBiQ15382
ChEMBLiCHEMBL3108656
DrugBankiDB04315 Guanosine-5'-Diphosphate
DB04137 Guanosine-5'-Triphosphate

PTM databases

iPTMnetiQ15382
PhosphoSitePlusiQ15382
SwissPalmiQ15382

Polymorphism and mutation databases

BioMutaiRHEB
DMDMi6919957

Proteomic databases

EPDiQ15382
jPOSTiQ15382
MaxQBiQ15382
PaxDbiQ15382
PeptideAtlasiQ15382
PRIDEiQ15382
ProteomicsDBi60554
TopDownProteomicsiQ15382

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		6009
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262187; ENSP00000262187; ENSG00000106615
GeneIDi6009
KEGGihsa:6009
UCSCiuc003wkh.1 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		6009
DisGeNETi6009
EuPathDBiHostDB:ENSG00000106615.9

GeneCards: human genes, protein and diseases

More...GeneCardsi		RHEB
HGNCiHGNC:10011 RHEB
HPAiCAB019436
MIMi601293 gene
neXtProtiNX_Q15382
OpenTargetsiENSG00000106615
PharmGKBiPA34389

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0395 Eukaryota
COG1100 LUCA
GeneTreeiENSGT00940000159945
HOGENOMiHOG000233973
HOVERGENiHBG009351
InParanoidiQ15382
KOiK07208
OMAiFIENHFV
OrthoDBi1320427at2759
PhylomeDBiQ15382
TreeFamiTF314986

Enzyme and pathway databases

ReactomeiR-HSA-1632852 Macroautophagy
R-HSA-165159 mTOR signalling
R-HSA-166208 mTORC1-mediated signalling
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
SABIO-RKiQ15382
SignaLinkiQ15382
SIGNORiQ15382

Miscellaneous databases

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

More...ChiTaRSi		RHEB human
EvolutionaryTraceiQ15382

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		RHEB

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

More...GenomeRNAii		6009

Protein Ontology

More...PROi		PR:Q15382

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000106615 Expressed in 180 organ(s), highest expression level in caudate nucleus
ExpressionAtlasiQ15382 baseline and differential
GenevisibleiQ15382 HS

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR037586 RHEB
IPR005225 Small_GTP-bd_dom
IPR001806 Small_GTPase
IPR020849 Small_GTPase_Ras-type
PANTHERiPTHR24070 PTHR24070, 1 hit
PTHR24070:SF264 PTHR24070:SF264, 1 hit
PfamiView protein in Pfam
PF00071 Ras, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00231 small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS51421 RAS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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 nameiRHEB_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: Q15382
Secondary accession number(s): B3KWN6
, D3DX13, Q53Y56, Q99444
<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: May 30, 2000
Last sequence update: November 1, 1996
Last modified: February 13, 2019
This is version 206 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, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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