Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
The new UniProt website is here! Take me to UniProt BETA

UniProtKB - P15208 (INSR_MOUSE)

Entry version 227 (25 May 2022)
Sequence version 2 (03 Oct 2012)
Previous versions | rss
Add a publicationFeedback
Protein

Insulin receptor

Gene

Insr

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

Receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as docking proteins for other signaling proteins that contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosine residues, including the p85 regulatory subunit of PI3K and SHP2. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway, which is responsible for most of the metabolic actions of insulin, and the Ras-MAPK pathway, which regulates expression of some genes and cooperates with the PI3K pathway to control cell growth and differentiation. Binding of the SH2 domains of PI3K to phosphotyrosines on IRS1 leads to the activation of PI3K and the generation of phosphatidylinositol-(3, 4, 5)-triphosphate (PIP3), a lipid second messenger, which activates several PIP3-dependent serine/threonine kinases, such as PDPK1 and subsequently AKT/PKB. The net effect of this pathway is to produce a translocation of the glucose transporter SLC2A4/GLUT4 from cytoplasmic vesicles to the cell membrane to facilitate glucose transport. Moreover, upon insulin stimulation, activated AKT/PKB is responsible for: anti-apoptotic effect of insulin by inducing phosphorylation of BAD; regulates the expression of gluconeogenic and lipogenic enzymes by controlling the activity of the winged helix or forkhead (FOX) class of transcription factors. Another pathway regulated by PI3K-AKT/PKB activation is mTORC1 signaling pathway which regulates cell growth and metabolism and integrates signals from insulin. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 thereby activating mTORC1 pathway. The Ras/RAF/MAP2K/MAPK pathway is mainly involved in mediating cell growth, survival and cellular differentiation of insulin. Phosphorylated IRS1 recruits GRB2/SOS complex, which triggers the activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to binding insulin, the insulin receptor can bind insulin-like growth factors (IGFI and IGFII). When present in a hybrid receptor with IGF1R, binds IGF1 (By similarity).

In adipocytes, inhibits lipolysis (PubMed:27322061).

By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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

Activated in response to insulin. Autophosphorylation activates the kinase activity. PTPN1, PTPRE and PTPRF dephosphorylate important tyrosine residues, thereby reducing INSR activity. Inhibited by ENPP1. GRB10 and GRB14 inhibit the catalytic activity of the INSR, they block access of substrates to the activated receptor. SOCS1 and SOCS3 act as negative regulators of INSR activity, they bind to the activated INRS and interfere with the phosphorylation of INSR substrates (By similarity). Interacts with PTPRF (By similarity). Interacts with ATIC; ATIC together with PRKAA2/AMPK2 and HACD3/PTPLAD1 is proposed to be part of a signaling netwok regulating INSR autophosphorylation and endocytosis (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei66Insulin-bindingBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei1023ATPPROSITE-ProRule annotation1
Binding sitei1047ATP1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1149Proton donor/acceptorBy similarity1
Binding sitei1167ATPPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi1094 – 1100ATPPROSITE-ProRule annotation7
Nucleotide bindingi1153 – 1154ATPPROSITE-ProRule annotation2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Receptor, Transferase, Tyrosine-protein kinase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.10.1, 3474

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-MMU-74713, IRS activation
R-MMU-74749, Signal attenuation
R-MMU-74751, Insulin receptor signalling cascade
R-MMU-74752, Signaling by Insulin receptor
R-MMU-77387, Insulin receptor recycling

<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:
Insulin receptor (EC:2.7.10.1)
Short name:
IR
Alternative name(s):
CD_antigen: CD220
Cleaved into the following 2 chains:
Insulin receptor subunit alpha
Insulin receptor subunit beta
<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:Insr
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <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 8

Organism-specific databases

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

More...MGIi		MGI:96575, Insr

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSMUSG00000005534

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini28 – 748ExtracellularCuratedAdd BLAST721
Topological domaini753 – 946ExtracellularCuratedAdd BLAST194
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei947 – 967HelicalSequence analysisAdd BLAST21
Topological domaini968 – 1372CytoplasmicCuratedAdd BLAST405

Keywords - Cellular componenti

Cell membrane, Endosome, Lysosome, 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%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>Mutagenesisi989Y → F: Abolishes interaction with IRS1 but not with IRS2. 2 Publications1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3187

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 27Add BLAST27
<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_000001669328 – 748Insulin receptor subunit alphaAdd BLAST721
ChainiPRO_0000016695753 – 1372Insulin receptor subunit betaAdd BLAST620

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi35 ↔ 53By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi43N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi52N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi105N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi138N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi153 ↔ 182By similarity
Disulfide bondi186 ↔ 209By similarity
Disulfide bondi196 ↔ 215By similarity
Disulfide bondi219 ↔ 228By similarity
Disulfide bondi223 ↔ 234By similarity
Disulfide bondi235 ↔ 243By similarity
Disulfide bondi239 ↔ 252By similarity
Glycosylationi242N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi255 ↔ 264By similarity
Disulfide bondi268 ↔ 280By similarity
Glycosylationi282N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi286 ↔ 311By similarity
Disulfide bondi293 ↔ 301By similarity
Disulfide bondi315 ↔ 328By similarity
Glycosylationi322N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi331 ↔ 335By similarity
Disulfide bondi339 ↔ 360By similarity
Glycosylationi364N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei400PhosphoserineBy similarity1
Modified residuei401PhosphotyrosineBy similarity1
Modified residuei407PhosphoserineBy similarity1
Glycosylationi424N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi445N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi462 ↔ 495By similarity
Glycosylationi541N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi551InterchainBy similarity
Glycosylationi635N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi653N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi676 ↔ 889By similarity
Glycosylationi700N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi759N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi772N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi815 ↔ 824By similarity
Glycosylationi910N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi923N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei989Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1175Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1179Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1180Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1345Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1351Phosphotyrosine; by autocatalysisBy similarity1

<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

Autophosphorylated on tyrosine residues in response to insulin (By similarity). Phosphorylation of Tyr-989 is required for IRS1-, SHC1-, and STAT5B-binding (By similarity). Dephosphorylated by PTPRE on Tyr-989, Tyr-1175, Tyr-1179 and Tyr-1180 residues (By similarity). Dephosphorylated by PTPRF and PTPN1 (By similarity). Dephosphorylated by PTPN2; down-regulates insulin-induced signaling.By similarity1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P15208

MaxQB - The MaxQuant DataBase

More...MaxQBi		P15208

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

More...PaxDbi		P15208

PeptideAtlas

More...PeptideAtlasi		P15208

PRoteomics IDEntifications database

More...PRIDEi		P15208

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		267252

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P15208

GlyConnect protein glycosylation platform

More...GlyConnecti		2393, 7 N-Linked glycans (4 sites)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P15208, 18 sites, 7 N-linked glycans (4 sites)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P15208

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

More...PhosphoSitePlusi		P15208

<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

More...Bgeei		ENSMUSG00000005534, Expressed in quadriceps femoris and 267 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P15208, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P15208, 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%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

Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains carry the insulin-binding regions, while the beta chains carry the kinase domain.

Forms a hybrid receptor with IGF1R, the hybrid is a tetramer consisting of 1 alpha chain and 1 beta chain of INSR and 1 alpha chain and 1 beta chain of IGF1R.

Interacts with SORBS1 but dissociates from it following insulin stimulation. Binds SH2B2 (By similarity). Activated form of INSR interacts (via Tyr-989) with the PTB/PID domains of IRS1 and SHC1. The sequences surrounding the phosphorylated NPXY motif contribute differentially to either IRS1 or SHC1 recognition.

Interacts (via tyrosines in the C-terminus) with IRS2 (via PTB domain and 591-786 AA); the 591-786 would be the primary anchor of IRS2 to INSR while the PTB domain would have a stabilizing action on the interaction with INSR.

Interacts with the SH2 domains of the 85 kDa regulatory subunit of PI3K (PIK3R1) in vitro, when autophosphorylated on tyrosine residues.

Interacts with SOCS7 (By similarity).

Interacts (via the phosphorylated Tyr-989), with SOCS3.

Interacts (via the phosphorylated Tyr-1175, Tyr-1179, Tyr-1180) with SOCS1.

Interacts with CAV2 (tyrosine-phosphorylated form); the interaction is increased with 'Tyr-27'phosphorylation of CAV2 (By similarity).

Interacts with ARRB2.

Interacts with GRB10; this interaction blocks the association between IRS1/IRS2 and INSR, significantly reduces insulin-stimulated tyrosine phosphorylation of IRS1 and IRS2 and thus decreases insulin signaling (By similarity).

Interacts with GRB7 (By similarity).

Interacts with PDPK1 (By similarity).

Interacts (via Tyr-1180) with GRB14 (via BPS domain); this interaction protects the tyrosines in the activation loop from dephosphorylation, but promotes dephosphorylation of Tyr-989, this results in decreased interaction with, and phosphorylation of, IRS1 (By similarity).

Interacts (via subunit alpha) with ENPP1 (via 485-599 AA); this interaction blocks autophosphorylation (By similarity).

Interacts with PTPRE; this interaction is dependent of Tyr-1175, Tyr-1179 and Tyr-1180 of the INSR (By similarity).

Interacts with STAT5B (via SH2 domain) (By similarity).

Interacts with PTPRF (By similarity).

Interacts with the insulin receptor SORL1; this interaction strongly increases its surface exposure, hence strengthens insulin signal reception (PubMed:27322061).

Interacts (tyrosine phosphorylated) with CCDC88A/GIV (via SH2-like region); binding requires autophosphorylation of the INSR C-terminal region (By similarity).

Interacts with GNAI3; the interaction is probably mediated by CCDC88A/GIV (By similarity).

Interacts with LMBRD1 (PubMed:24078630).

By similarity2 Publications

<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		200774, 28 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P15208

Database of interacting proteins

More...DIPi		DIP-41452N

Protein interaction database and analysis system

More...IntActi		P15208, 21 interactors

Molecular INTeraction database

More...MINTi		P15208

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000088837

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P15208

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P15208, protein

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

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P15208

Biological Magnetic Resonance Data Bank

More...BMRBi		P15208

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

More...SMRi		P15208

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P15208

<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 <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini626 – 728Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST103
Domaini744 – 838Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST95
Domaini843 – 937Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST95
Domaini1013 – 1288Protein kinasePROSITE-ProRule annotationAdd BLAST276

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>Regioni688 – 709DisorderedSequence analysisAdd BLAST22
Regioni735 – 743Insulin-bindingBy similarity9
Regioni986 – 989Important for interaction with IRS1, SHC1 and STAT5BBy similarity4
Regioni1349 – 1372DisorderedSequence analysisAdd BLAST24
Regioni1351 – 1354PIK3R1 bindingBy similarity4

<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 tetrameric insulin receptor binds insulin via non-identical regions from two alpha chains, primarily via the C-terminal region of the first INSR alpha chain. Residues from the leucine-rich N-terminus of the other INSR alpha chain also contribute to this insulin binding site. A secondary insulin-binding site is formed by residues at the junction of fibronectin type-III domain 1 and 2 (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 protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4258, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155404

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000288_166_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P15208

Identification of Orthologs from Complete Genome Data

More...OMAi		QYIPDDW

Database for complete collections of gene phylogenies

More...PhylomeDBi		P15208

TreeFam database of animal gene trees

More...TreeFami		TF351636

Family and domain databases

Conserved Domains Database

More...CDDi		cd00063, FN3, 2 hits
cd00064, FU, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.10, 3 hits
3.80.20.20, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR006211, Furin-like_Cys-rich_dom
IPR006212, Furin_repeat
IPR009030, Growth_fac_rcpt_cys_sf
IPR013783, Ig-like_fold
IPR040969, Insulin_TMD
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR000494, Rcpt_L-dom
IPR036941, Rcpt_L-dom_sf
IPR001245, Ser-Thr/Tyr_kinase_cat_dom
IPR008266, Tyr_kinase_AS
IPR020635, Tyr_kinase_cat_dom
IPR016246, Tyr_kinase_insulin-like_rcpt
IPR002011, Tyr_kinase_rcpt_2_CS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00041, fn3, 1 hit
PF00757, Furin-like, 1 hit
PF17870, Insulin_TMD, 1 hit
PF07714, PK_Tyr_Ser-Thr, 1 hit
PF01030, Recep_L_domain, 2 hits

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000620, Insulin_receptor, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00109, TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00060, FN3, 3 hits
SM00261, FU, 1 hit
SM00219, TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49265, SSF49265, 3 hits
SSF56112, SSF56112, 1 hit
SSF57184, SSF57184, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50853, FN3, 3 hits
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00109, PROTEIN_KINASE_TYR, 1 hit
PS00239, RECEPTOR_TYR_KIN_II, 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>Sequence (1+)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.

<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 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 2 potential isoforms that are computationally mapped.Show allAlign All

P15208-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGFGRGCETT AVPLLVAVAA LLVGTAGHLY PGEVCPGMDI RNNLTRLHEL 
        60         70         80         90        100
ENCSVIEGHL QILLMFKTRP EDFRDLSFPK LIMITDYLLL FRVYGLESLK 
       110        120        130        140        150
DLFPNLTVIR GSRLFFNYAL VIFEMVHLKE LGLYNLMNIT RGSVRIEKNN 
       160        170        180        190        200
ELCYLATIDW SRILDSVEDN YIVLNKDDNE ECGDVCPGTA KGKTNCPATV 
       210        220        230        240        250
INGQFVERCW THSHCQKVCP TICKSHGCTA EGLCCHKECL GNCSEPDDPT 
       260        270        280        290        300
KCVACRNFYL DGQCVETCPP PYYHFQDWRC VNFSFCQDLH FKCRNSRKPG 
       310        320        330        340        350
CHQYVIHNNK CIPECPSGYT MNSSNLMCTP CLGPCPKVCQ ILEGEKTIDS 
       360        370        380        390        400
VTSAQELRGC TVINGSLIIN IRGGNNLAAE LEANLGLIEE ISGFLKIRRS 
       410        420        430        440        450
YALVSLSFFR KLHLIRGETL EIGNYSFYAL DNQNLRQLWD WSKHNLTITQ 
       460        470        480        490        500
GKLFFHYNPK LCLSEIHKME EVSGTKGRQE RNDIALKTNG DQASCENELL 
       510        520        530        540        550
KFSFIRTSFD KILLRWEPYW PPDFRDLLGF MLFYKEAPYQ NVTEFDGQDA 
       560        570        580        590        600
CGSNSWTVVD IDPPQRSNDP KSQTPSHPGW LMRGLKPWTQ YAIFVKTLVT 
       610        620        630        640        650
FSDERRTYGA KSDIIYVQTD ATNPSVPLDP ISVSNSSSQI ILKWKPPSDP 
       660        670        680        690        700
NGNITHYLVY WERQAEDSEL FELDYCLKGL KLPSRTWSPP FESDDSQKHN 
       710        720        730        740        750
QSEYDDSASE CCSCPKTDSQ ILKELEESSF RKTFEDYLHN VVFVPRPSRK 
       760        770        780        790        800
RRSLEEVGNV TATTLTLPDF PNVSSTIVPT SQEEHRPFEK VVNKESLVIS 
       810        820        830        840        850
GLRHFTGYRI ELQACNQDSP DERCSVAAYV SARTMPEAKA DDIVGPVTHE 
       860        870        880        890        900
IFENNVVHLM WQEPKEPNGL IVLYEVSYRR YGDEELHLCV SRKHFALERG 
       910        920        930        940        950
CRLRGLSPGN YSVRVRATSL AGNGSWTEPT YFYVTDYLDV PSNIAKIIIG 
       960        970        980        990       1000
PLIFVFLFSV VIGSIYLFLR KRQPDGPMGP LYASSNPEYL SASDVFPSSV 
      1010       1020       1030       1040       1050
YVPDEWEVPR EKITLLRELG QGSFGMVYEG NAKDIIKGEA ETRVAVKTVN 
      1060       1070       1080       1090       1100
ESASLRERIE FLNEASVMKG FTCHHVVRLL GVVSKGQPTL VVMELMAHGD 
      1110       1120       1130       1140       1150
LKSHLRSLRP DAENNPGRPP PTLQEMIQMT AEIADGMAYL NAKKFVHRDL 
      1160       1170       1180       1190       1200
AARNCMVAHD FTVKIGDFGM TRDIYETDYY RKGGKGLLPV RWMSPESLKD 
      1210       1220       1230       1240       1250
GVFTASSDMW SFGVVLWEIT SLAEQPYQGL SNEQVLKFVM DGGYLDPPDN 
      1260       1270       1280       1290       1300
CPERLTDLMR MCWQFNPKMR PTFLEIVNLL KDDLHPSFPE VSFFYSEENK 
      1310       1320       1330       1340       1350
APESEELEME FEDMENVPLD RSSHCQREEA GGREGGSSLS IKRTYDEHIP 
      1360       1370 
YTHMNGGKKN GRVLTLPRSN PS
Length:1,372
Mass (Da):155,610
Last modified:October 3, 2012 - 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:iB0FA7DBD2AD4646A
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
A0A140LI30A0A140LI30_MOUSE
Insulin receptor
Insr
90Annotation 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>
B8Q3N4B8Q3N4_MOUSE
Insulin receptor
Insr
224Annotation 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 conflicti1089T → M in AAA39318 (PubMed:2557333).Curated1

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
J05149 mRNA Translation: AAA39318.1
AC168068 Genomic DNA No translation available.
M28869 Genomic DNA Translation: AAA39319.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS22059.1

Protein sequence database of the Protein Information Resource

More...PIRi		A34157

NCBI Reference Sequences

More...RefSeqi		NP_034698.2, NM_010568.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000091291; ENSMUSP00000088837; ENSMUSG00000005534

Database of genes from NCBI RefSeq genomes

More...GeneIDi		16337

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:16337

UCSC genome browser

More...UCSCi		uc009krc.2, mouse

<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
J05149 mRNA Translation: AAA39318.1
AC168068 Genomic DNA No translation available.
M28869 Genomic DNA Translation: AAA39319.1
CCDSiCCDS22059.1
PIRiA34157
RefSeqiNP_034698.2, NM_010568.3

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
1LK2X-ray1.35P423-430[»]
AlphaFoldDBiP15208
BMRBiP15208
SMRiP15208
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi200774, 28 interactors
CORUMiP15208
DIPiDIP-41452N
IntActiP15208, 21 interactors
MINTiP15208
STRINGi10090.ENSMUSP00000088837

Chemistry databases

BindingDBiP15208
ChEMBLiCHEMBL3187

PTM databases

CarbonylDBiP15208
GlyConnecti2393, 7 N-Linked glycans (4 sites)
GlyGeniP15208, 18 sites, 7 N-linked glycans (4 sites)
iPTMnetiP15208
PhosphoSitePlusiP15208

Proteomic databases

jPOSTiP15208
MaxQBiP15208
PaxDbiP15208
PeptideAtlasiP15208
PRIDEiP15208
ProteomicsDBi267252

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3403, 2152 antibodies from 52 providers

The DNASU plasmid repository

More...DNASUi		16337

Genome annotation databases

EnsembliENSMUST00000091291; ENSMUSP00000088837; ENSMUSG00000005534
GeneIDi16337
KEGGimmu:16337
UCSCiuc009krc.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3643
MGIiMGI:96575, Insr
VEuPathDBiHostDB:ENSMUSG00000005534

Phylogenomic databases

eggNOGiKOG4258, Eukaryota
GeneTreeiENSGT00940000155404
HOGENOMiCLU_000288_166_0_1
InParanoidiP15208
OMAiQYIPDDW
PhylomeDBiP15208
TreeFamiTF351636

Enzyme and pathway databases

BRENDAi2.7.10.1, 3474
ReactomeiR-MMU-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-MMU-74713, IRS activation
R-MMU-74749, Signal attenuation
R-MMU-74751, Insulin receptor signalling cascade
R-MMU-74752, Signaling by Insulin receptor
R-MMU-77387, Insulin receptor recycling

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		16337, 2 hits in 74 CRISPR screens

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

More...ChiTaRSi		Insr, mouse
EvolutionaryTraceiP15208

Protein Ontology

More...PROi		PR:P15208
RNActiP15208, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000005534, Expressed in quadriceps femoris and 267 other tissues
ExpressionAtlasiP15208, baseline and differential
GenevisibleiP15208, MM

Family and domain databases

CDDicd00063, FN3, 2 hits
cd00064, FU, 1 hit
Gene3Di2.60.40.10, 3 hits
3.80.20.20, 2 hits
InterProiView protein in InterPro
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR006211, Furin-like_Cys-rich_dom
IPR006212, Furin_repeat
IPR009030, Growth_fac_rcpt_cys_sf
IPR013783, Ig-like_fold
IPR040969, Insulin_TMD
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR000494, Rcpt_L-dom
IPR036941, Rcpt_L-dom_sf
IPR001245, Ser-Thr/Tyr_kinase_cat_dom
IPR008266, Tyr_kinase_AS
IPR020635, Tyr_kinase_cat_dom
IPR016246, Tyr_kinase_insulin-like_rcpt
IPR002011, Tyr_kinase_rcpt_2_CS
PfamiView protein in Pfam
PF00041, fn3, 1 hit
PF00757, Furin-like, 1 hit
PF17870, Insulin_TMD, 1 hit
PF07714, PK_Tyr_Ser-Thr, 1 hit
PF01030, Recep_L_domain, 2 hits
PIRSFiPIRSF000620, Insulin_receptor, 1 hit
PRINTSiPR00109, TYRKINASE
SMARTiView protein in SMART
SM00060, FN3, 3 hits
SM00261, FU, 1 hit
SM00219, TyrKc, 1 hit
SUPFAMiSSF49265, SSF49265, 3 hits
SSF56112, SSF56112, 1 hit
SSF57184, SSF57184, 1 hit
PROSITEiView protein in PROSITE
PS50853, FN3, 3 hits
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00109, PROTEIN_KINASE_TYR, 1 hit
PS00239, RECEPTOR_TYR_KIN_II, 1 hit

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 nameiINSR_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: P15208
Secondary accession number(s): F8VPU4
<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 1, 1990
Last sequence update: October 3, 2012
Last modified: May 25, 2022
This is version 227 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

3D-structure, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. MGD cross-references
    Mouse Genome Database (MGD) 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again