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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

GO - Biological processi

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

Molecular functionKinase, 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

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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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 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

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PRIDEi
Q61526

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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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

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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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
199497, 1 interactor

Protein interaction database and analysis system

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IntActi
Q61526, 2 interactors

STRING: functional protein association networks

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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

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ProteinModelPortali
Q61526

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

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SMRi
Q61526

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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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

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GeneTreei
ENSGT00940000156107

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000230982

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000490

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q61526

KEGG Orthology (KO)

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KOi
K05084

Identification of Orthologs from Complete Genome Data

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OMAi
SKTHLAM

Database of Orthologous Groups

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OrthoDBi
81952at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q61526

TreeFam database of animal gene trees

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TreeFami
TF106002

Family and domain databases

Conserved Domains Database

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CDDi
cd00064 FU, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.80.20.20, 2 hits

Integrated resource of protein families, domains and functional sites

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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

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PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00261 FU, 5 hits
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 2 hits

PROSITE; a protein domain and family database

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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

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

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CCDSi
CCDS24283.1

NCBI Reference Sequences

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RefSeqi
NP_034283.1, NM_010153.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.373043

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000082059; ENSMUSP00000080716; ENSMUSG00000018166

Database of genes from NCBI RefSeq genomes

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GeneIDi
13867

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:13867

UCSC genome browser

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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

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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

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ChiTaRSi
Erbb3 mouse

Protein Ontology

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PROi
PR:Q61526

The Stanford Online Universal Resource for Clones and ESTs

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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

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ProtoNeti
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<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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