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UniProtKB - Q61526 (ERBB3_MOUSE)

Entry version 166 (13 Feb 2019)
Sequence version 2 (11 Oct 2005)
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Protein

Receptor tyrosine-protein kinase erbB-3

Gene

Erbb3

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

Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase. May also be activated by CSPG5.By similarity

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei740ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ 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 sitei832Proton acceptorPROSITE-ProRule annotation1

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 bindingi713 – 721ATPPROSITE-ProRule annotation9
Nucleotide bindingi786 – 788ATPPROSITE-ProRule annotation3
Nucleotide bindingi832 – 837ATPPROSITE-ProRule annotation6

<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

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-1227986 Signaling by ERBB2
R-MMU-1236394 Signaling by ERBB4
R-MMU-1250196 SHC1 events in ERBB2 signaling
R-MMU-1257604 PIP3 activates AKT signaling
R-MMU-1306955 GRB7 events in ERBB2 signaling
R-MMU-1358803 Downregulation of ERBB2:ERBB3 signaling
R-MMU-1963642 PI3K events in ERBB2 signaling
R-MMU-5673001 RAF/MAP kinase cascade
R-MMU-6785631 ERBB2 Regulates Cell Motility
R-MMU-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-MMU-8847993 ERBB2 Activates PTK6 Signaling
R-MMU-8863795 Downregulation of ERBB2 signaling

<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:
Receptor tyrosine-protein kinase erbB-3 (EC:2.7.10.1)
Alternative name(s):
Glial growth factor receptor
Proto-oncogene-like protein c-ErbB-3
<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:Erbb3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic 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_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

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

More...MGIi		MGI:95411 Erbb3

<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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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 domaini20 – 641ExtracellularSequence analysisAdd BLAST622
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei642 – 662HelicalSequence analysisAdd BLAST21
Topological domaini663 – 1339CytoplasmicSequence analysisAdd BLAST677

Keywords - Cellular componenti

Membrane

<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 – 19Sequence analysisAdd BLAST19
<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_000004223120 – 1339Receptor tyrosine-protein kinase erbB-3Add BLAST1320

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi126N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi186 ↔ 194By similarity
Disulfide bondi190 ↔ 202By similarity
Disulfide bondi210 ↔ 218By similarity
Disulfide bondi214 ↔ 226By similarity
Disulfide bondi227 ↔ 235By similarity
Disulfide bondi231 ↔ 243By similarity
Disulfide bondi246 ↔ 255By similarity
Glycosylationi250N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi259 ↔ 286By similarity
Disulfide bondi290 ↔ 301By similarity
Disulfide bondi305 ↔ 320By similarity
Disulfide bondi323 ↔ 327By similarity
Glycosylationi353N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi408N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi414N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi437N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi469N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi500 ↔ 509By similarity
Disulfide bondi504 ↔ 517By similarity
Disulfide bondi520 ↔ 529By similarity
Glycosylationi522N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi533 ↔ 549By similarity
Disulfide bondi552 ↔ 565By similarity
Disulfide bondi556 ↔ 573By similarity
Glycosylationi566N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi576 ↔ 585By similarity
Disulfide bondi589 ↔ 610By similarity
Disulfide bondi613 ↔ 621By similarity
Glycosylationi616N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi617 ↔ 629By similarity
<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 residuei684PhosphoserineBy similarity1
Modified residuei980PhosphoserineBy similarity1

<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

Autophosphorylated. Ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q61526

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

More...PaxDbi		Q61526

PeptideAtlas

More...PeptideAtlasi		Q61526

PRoteomics IDEntifications database

More...PRIDEi		Q61526

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q61526

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

More...PhosphoSitePlusi		Q61526

<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

In the muscle, expression localizes to the synaptic sites of muscle fibers.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000018166 Expressed in 293 organ(s), highest expression level in ileum

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q61526 MM

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

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

Monomer and homodimer. Heterodimer with each of the other ERBB receptors (Potential). Interacts with CSPG5, PA2G4, GRB7 and MUC1 (By similarity). Interacts with MYOC (PubMed:23897819). Found in a ternary complex with NRG1 and ITGAV:ITGB3 or ITGA6:ITGB4 (By similarity).By similarityCurated1 Publication

<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

WithEntry#Exp.IntActNotes
Erbb2P704242EBI-931878,EBI-2945468

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		199497, 1 interactor

Protein interaction database and analysis system

More...IntActi		Q61526, 2 interactors

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000080716

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q61526

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

More...SMRi		Q61526

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini707 – 964Protein kinasePROSITE-ProRule annotationAdd BLAST258

<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 cytoplasmic part of the receptor may interact with the SH2 or SH3 domains of many signal-transducing proteins.

<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. EGF receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1025 Eukaryota
ENOG410XNSR LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156107

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000230982

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG000490

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q61526

KEGG Orthology (KO)

More...KOi		K05084

Identification of Orthologs from Complete Genome Data

More...OMAi		SKTHLAM

Database of Orthologous Groups

More...OrthoDBi		81952at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q61526

TreeFam database of animal gene trees

More...TreeFami		TF106002

Family and domain databases

Conserved Domains Database

More...CDDi		cd00064 FU, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.80.20.20, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006211 Furin-like_Cys-rich_dom
IPR006212 Furin_repeat
IPR032778 GF_recep_IV
IPR009030 Growth_fac_rcpt_cys_sf
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
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
IPR016245 Tyr_kinase_EGF/ERB/XmrK_rcpt

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00757 Furin-like, 1 hit
PF14843 GF_recep_IV, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF01030 Recep_L_domain, 2 hits

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000619 TyrPK_EGF-R, 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
SM00261 FU, 5 hits
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 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>Sequencei

<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.

Q61526-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSAIGTLQVL GFLLSLARGS EMGNSQAVCP GTLNGLSVTG DADNQYQTLY 
        60         70         80         90        100
KLYEKCEVVM GNLEIVLTGH NADLSFLQWI REVTGYVLVA MNEFSVLPLP 
       110        120        130        140        150
NLRVVRGTQV YDGKFAIFVM LNYNTNSSHA LRQLRFTQLT EILLGGVYIE 
       160        170        180        190        200
KNDKLCHMDT IDWRDIVRVP DAEIVVKNNG GNCPPCHEVC KGRCWGPGPE 
       210        220        230        240        250
DCQILTKTIC APQCNGRCFG PNPNQCCHDE CAGGCSGPQD TDCFACRHFN 
       260        270        280        290        300
DSGACVPRCP APLVYNKLTF QLEPNPHIKY QYGGVCVASC PHNFVVDQTF 
       310        320        330        340        350
CVRACPADKM EVDKNGLKMC EPCRGLCPKA CEGTGSGSRY QTVDSSNIDG 
       360        370        380        390        400
FVNCTKILGN LDFLITGLNG DPWHKIPALD PEKLNVFRTV REITGYLNIQ 
       410        420        430        440        450
SWPPHMHNFS VFSNLTTIGG RSLYNRGFSL LIMKNLNVTS LGFRSLKEIS 
       460        470        480        490        500
AGRVYISANQ QLCYHHSLNW TRLLRGPAEE RLDIKYNRPL GECVAEGKVC 
       510        520        530        540        550
DPLCSSGGCW GPGPGQCLSC RNYSREGVCV THCNVLQGEP REFVHEAHCF 
       560        570        580        590        600
SCHPECQPME GTSTCNGSGS DACARCAHFR DGPHCVNSCP HGILGAKGPI 
       610        620        630        640        650
YKYPDAQNEC RPCHENCTQG CKGPELQDCL GQAEVLMSKP HLVIAVTVGL 
       660        670        680        690        700
TVIFLILGGS FLYWRGRRIQ NKRAMRRYLE RGESIEPLDP SEKANKVLAR 
       710        720        730        740        750
IFKETELRKL KVLGSGVFGT VHKGIWIPEG ESIKIPVCIK VIEDKSGRQS 
       760        770        780        790        800
FQAVTDHMLA VGSLDHAHIV RLLGLCPGSS LQLVTQYLPL GSLLDHVRQH 
       810        820        830        840        850
RETLGPQLLL NWGVQIAKGM YYLEEHSMVH RDLALRNVML KSPSQVQVAD 
       860        870        880        890        900
FGVADLLPPD DKQLLHSEAK TPIKWMALES IHFGKYTHQS DVWSYGVTVW 
       910        920        930        940        950
ELMTFGAEPY AGLRLAEIPD LLEKGERLAQ PQICTIDVYM VMVKCWMIDE 
       960        970        980        990       1000
NIRPTFKELA NEFTRMARDP PRYLVIKRAS GPGIPPAAEP SALSTKELQD 
      1010       1020       1030       1040       1050
AELEPDLDLD LDVEVEEEGL ATTLGSALSL PTGTLTRPRG SQSLLSPSSG 
      1060       1070       1080       1090       1100
YMPMNQSNLG EACLDSAVLG GREQFSRPIS LHPIPRGRQT SESSEGHVTG 
      1110       1120       1130       1140       1150
SEAELQERVS MCRSRSRSRS PRPRGDSAYH SQRHSLLTPV TPLSPPGLEE 
      1160       1170       1180       1190       1200
EDGNGYVMPD THLRGTSSSR EGTLSSVGLS SVLGTEEEDE DEEYEYMNRK 
      1210       1220       1230       1240       1250
RRGSPARPPR PGSLEELGYE YMDVGSDLSA SLGSTQSCPL HPMAIVPSAG 
      1260       1270       1280       1290       1300
TTPDEDYEYM NRRRGAGGSG GDYAAMGACP AAEQGYEEMR AFQGPGHQAP 
      1310       1320       1330 
HVRYARLKTL RSLEATDSAF DNPDYWHSRL FPKANAQRI
Length:1,339
Mass (Da):147,613
Last modified:October 11, 2005 - 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:i59D56FD9C9536FBE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti1067A → V in AAA93533 (PubMed:7589796).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
AY686636 mRNA Translation: AAT95433.1
BC029028 mRNA Translation: AAH29028.1
BC049279 mRNA Translation: AAH49279.1
BC106091 mRNA Translation: AAI06092.1
L47240 mRNA Translation: AAA93533.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS24283.1

NCBI Reference Sequences

More...RefSeqi		NP_034283.1, NM_010153.1

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Mm.373043

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000082059; ENSMUSP00000080716; ENSMUSG00000018166

Database of genes from NCBI RefSeq genomes

More...GeneIDi		13867

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:13867

UCSC genome browser

More...UCSCi		uc007hnm.1 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
AY686636 mRNA Translation: AAT95433.1
BC029028 mRNA Translation: AAH29028.1
BC049279 mRNA Translation: AAH49279.1
BC106091 mRNA Translation: AAI06092.1
L47240 mRNA Translation: AAA93533.1
CCDSiCCDS24283.1
RefSeqiNP_034283.1, NM_010153.1
UniGeneiMm.373043

3D structure databases

ProteinModelPortaliQ61526
SMRiQ61526
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199497, 1 interactor
IntActiQ61526, 2 interactors
STRINGi10090.ENSMUSP00000080716

PTM databases

iPTMnetiQ61526
PhosphoSitePlusiQ61526

Proteomic databases

MaxQBiQ61526
PaxDbiQ61526
PeptideAtlasiQ61526
PRIDEiQ61526

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000082059; ENSMUSP00000080716; ENSMUSG00000018166
GeneIDi13867
KEGGimmu:13867
UCSCiuc007hnm.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2065
MGIiMGI:95411 Erbb3

Phylogenomic databases

eggNOGiKOG1025 Eukaryota
ENOG410XNSR LUCA
GeneTreeiENSGT00940000156107
HOGENOMiHOG000230982
HOVERGENiHBG000490
InParanoidiQ61526
KOiK05084
OMAiSKTHLAM
OrthoDBi81952at2759
PhylomeDBiQ61526
TreeFamiTF106002

Enzyme and pathway databases

BRENDAi2.7.10.1 3474
ReactomeiR-MMU-1227986 Signaling by ERBB2
R-MMU-1236394 Signaling by ERBB4
R-MMU-1250196 SHC1 events in ERBB2 signaling
R-MMU-1257604 PIP3 activates AKT signaling
R-MMU-1306955 GRB7 events in ERBB2 signaling
R-MMU-1358803 Downregulation of ERBB2:ERBB3 signaling
R-MMU-1963642 PI3K events in ERBB2 signaling
R-MMU-5673001 RAF/MAP kinase cascade
R-MMU-6785631 ERBB2 Regulates Cell Motility
R-MMU-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-MMU-8847993 ERBB2 Activates PTK6 Signaling
R-MMU-8863795 Downregulation of ERBB2 signaling

Miscellaneous databases

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

More...ChiTaRSi		Erbb3 mouse

Protein Ontology

More...PROi		PR:Q61526

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000018166 Expressed in 293 organ(s), highest expression level in ileum
GenevisibleiQ61526 MM

Family and domain databases

CDDicd00064 FU, 3 hits
Gene3Di3.80.20.20, 2 hits
InterProiView protein in InterPro
IPR006211 Furin-like_Cys-rich_dom
IPR006212 Furin_repeat
IPR032778 GF_recep_IV
IPR009030 Growth_fac_rcpt_cys_sf
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
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
IPR016245 Tyr_kinase_EGF/ERB/XmrK_rcpt
PfamiView protein in Pfam
PF00757 Furin-like, 1 hit
PF14843 GF_recep_IV, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF01030 Recep_L_domain, 2 hits
PIRSFiPIRSF000619 TyrPK_EGF-R, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00261 FU, 5 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 2 hits
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 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 nameiERBB3_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: Q61526
Secondary accession number(s): Q3KQR1
, Q68J64, Q810U8, Q8K317
<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: December 15, 1998
Last sequence update: October 11, 2005
Last modified: February 13, 2019
This is version 166 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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