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UniProtKB - Q8CBF3 (EPHB1_MOUSE)

Entry version 155 (12 Aug 2020)
Sequence version 1 (01 Mar 2003)
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Protein

Ephrin type-B receptor 1

Gene

Ephb1

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 binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Cognate/functional ephrin ligands for this receptor include EFNB1, EFNB2 and EFNB3. During nervous system development, regulates retinal axon guidance redirecting ipsilaterally ventrotemporal retinal ganglion cells axons at the optic chiasm midline. This probably requires repulsive interaction with EFNB2. In the adult nervous system together with EFNB3, regulates chemotaxis, proliferation and polarity of the hippocampus neural progenitors. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and synapse formation. May also regulate angiogenesis. More generally, may play a role in targeted cell migration and adhesion. Upon activation by EFNB1 and probably other ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively. Involved in the maintenance of the pool of satellite cells (muscle stem cells) by promoting their self-renewal and reducing their activation and differentiation (PubMed:27446912).5 Publications

<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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei651ATPPROSITE-ProRule annotation1
<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 sitei744Proton acceptorPROSITE-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 bindingi625 – 633ATPPROSITE-ProRule annotation9

<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
Biological processCell adhesion, Neurogenesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-2682334, EPH-Ephrin signaling
R-MMU-3928662, EPHB-mediated forward signaling
R-MMU-3928664, Ephrin signaling
R-MMU-3928665, EPH-ephrin mediated repulsion of cells

<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:
Ephrin type-B receptor 1 (EC:2.7.10.1)
<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:Ephb1
<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 9

Organism-specific databases

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

More...MGIi		MGI:1096337, Ephb1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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 domaini18 – 540ExtracellularSequence analysisAdd BLAST523
<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>Transmembranei541 – 563HelicalSequence analysisAdd BLAST23
Topological domaini564 – 984CytoplasmicSequence analysisAdd BLAST421

Keywords - Cellular componenti

Cell membrane, Cell projection, Endosome, 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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice development is apparently normal. However, they display a dramatic reduction of ipsilateral retinal projection. Mice do not develop neuropathic algesia and physical dependence to morphine.2 Publications

<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 – 17Sequence analysisAdd BLAST17
<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_000026031718 – 984Ephrin type-B receptor 1Add BLAST967

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi334N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi426N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi480N-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 residuei600PhosphotyrosineBy similarity1
Modified residuei928Phosphotyrosine; 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

Phosphorylated. Autophosphorylation is stimulated by the ligand EFNB1. Required for interaction with SH2 domain-containing interactors, for activation of the MAPK/ERK and JUN signaling cascades and for ubiquitination by CBL (By similarity).By similarity
Ubiquitinated; (EFNB1)ligand-induced poly- and/or multi-ubiquitination by CBL is regulated by SRC and leads to lysosomal degradation.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...PaxDbi		Q8CBF3

PeptideAtlas

More...PeptideAtlasi		Q8CBF3

PRoteomics IDEntifications database

More...PRIDEi		Q8CBF3

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q8CBF3, 3 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q8CBF3

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

More...PhosphoSitePlusi		Q8CBF3

<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

Expressed in neural stem and progenitor cells in the dentate gyrus (PubMed:18057206). Expressed in myogenic progenitor cells (PubMed:27446912).2 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed in growth cones of ventrotemporal (uncrossed) retinal ganglion cells that give rise to ipsilateral projections (at protein level) (PubMed:12971893, PubMed:18524895). In myogenic progenitor cells, initially expressed early during myogenic development (11.5 dpc), down-regulated during the fetal stage (lower levels at 17.5 dpc) to be re-expressed in postnatal satellite cells (PubMed:27446912).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000032537, Expressed in cardiac ventricle and 229 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q8CBF3, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q8CBF3, 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

Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses (By similarity).

Interacts with EPHB6; transphosphorylates EPHB6 to form an active signaling complex (By similarity).

Interacts with PICK1.

Interacts (through Tyr-594) with NCK1 (via SH2 domain); activates the JUN cascade to regulate cell adhesion. The ligand-activated form interacts (through Tyr-928) with GRB7 and GRB10 (via SH2 domains). The ligand-activated form interacts (residues within the catalytic domain) with GRB2 (via SH2 domain).

Interacts with GRB2, SHC1 and SRC; activates the MAPK/ERK cascade to regulate cell migration.

Interacts with CBL; regulates receptor degradation through ubiquitination.

Interacts with ACP1.

By similarity5 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		234781, 3 interactors

Protein interaction database and analysis system

More...IntActi		Q8CBF3, 1 interactor

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000035129

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q8CBF3, 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

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

More...SMRi		Q8CBF3

Database of comparative protein structure models

More...ModBasei		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%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>Domaini19 – 201Eph LBDPROSITE-ProRule annotationAdd BLAST183
Domaini322 – 432Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST111
Domaini433 – 528Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST96
Domaini619 – 882Protein kinasePROSITE-ProRule annotationAdd BLAST264
Domaini911 – 975SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi982 – 984PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi183 – 319Cys-richAdd BLAST137

<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. Ephrin receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0196, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155297

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000288_141_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q8CBF3

KEGG Orthology (KO)

More...KOi		K05110

Identification of Orthologs from Complete Genome Data

More...OMAi		MACKACP

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q8CBF3

TreeFam database of animal gene trees

More...TreeFami		TF315608

Family and domain databases

Conserved Domains Database

More...CDDi		cd10476, EphR_LBD_B1, 1 hit
cd00063, FN3, 2 hits
cd09551, SAM_EPH-B1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.150.50, 1 hit
2.60.120.260, 1 hit
2.60.40.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR027936, Eph_TM
IPR034231, EphB1_rcpt_lig-bd
IPR042819, EphB1_SAM
IPR001090, Ephrin_rcpt_lig-bd_dom
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR008979, Galactose-bd-like_sf
IPR009030, Growth_fac_rcpt_cys_sf
IPR013783, Ig-like_fold
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR001660, SAM
IPR013761, SAM/pointed_sf
IPR001245, Ser-Thr/Tyr_kinase_cat_dom
IPR011641, Tyr-kin_ephrin_A/B_rcpt-like
IPR008266, Tyr_kinase_AS
IPR020635, Tyr_kinase_cat_dom
IPR016257, Tyr_kinase_ephrin_rcpt
IPR001426, Tyr_kinase_rcpt_V_CS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF14575, EphA2_TM, 1 hit
PF01404, Ephrin_lbd, 1 hit
PF00041, fn3, 2 hits
PF07714, Pkinase_Tyr, 1 hit
PF00536, SAM_1, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000666, TyrPK_ephrin_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
SM00615, EPH_lbd, 1 hit
SM01411, Ephrin_rec_like, 1 hit
SM00060, FN3, 2 hits
SM00454, SAM, 1 hit
SM00219, TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47769, SSF47769, 1 hit
SSF49265, SSF49265, 1 hit
SSF49785, SSF49785, 1 hit
SSF56112, SSF56112, 1 hit
SSF57184, SSF57184, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01186, EGF_2, 1 hit
PS51550, EPH_LBD, 1 hit
PS50853, FN3, 2 hits
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00109, PROTEIN_KINASE_TYR, 1 hit
PS00790, RECEPTOR_TYR_KIN_V_1, 1 hit
PS00791, RECEPTOR_TYR_KIN_V_2, 1 hit
PS50105, SAM_DOMAIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)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 describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q8CBF3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MALDCLLLFL LASAVAAMEE TLMDTRTATA ELGWTANPAS GWEEVSGYDE 
        60         70         80         90        100
NLNTIRTYQV CNVFEPNQNN WLLTTFINRR GAHRIYTEMR FTVRDCSSLP 
       110        120        130        140        150
NVPGSCKETF NLYYYETDSV IATKKSAFWS EAPYLKVDTI AADESFSQVD 
       160        170        180        190        200
FGGRLMKVNT EVRSFGPLTR NGFYLAFQDY GACMSLLSVR VFFKKCPSIV 
       210        220        230        240        250
QNFAVFPETM TGAESTSLVI ARGTCIPNAE EVDVPIKLYC NGDGEWMVPI 
       260        270        280        290        300
GRCTCKPGYE PENSVACKAC PAGTFKASQE AEGCSHCPSN SRSPSEASPI 
       310        320        330        340        350
CTCRTGYYRA DFDPPEVACT SVPSGPRNVI SIVNETSIIL EWHPPRETGG 
       360        370        380        390        400
RDDVTYNIIC KKCRADRRSC SRCDDNVEFV PRQLGLTECR VSISSLWAHT 
       410        420        430        440        450
PYTFDIQAIN GVSSKSPFPP QHVSVNITTN QAAPSTVPIM HQVSATMRSI 
       460        470        480        490        500
TLSWPQPEQP NGIILDYEIR YYEKEHNEFN SSMARSQTNT ARIDGLRPGM 
       510        520        530        540        550
VYVVQVRART VAGYGKFSGK MCFQTLTDDD YKSELREQLP LIAGSAAAGV 
       560        570        580        590        600
VFVVSLVAIS IVCSRKRAYS KEAAYSDKLQ HYSTGRGSPG MKIYIDPFTY 
       610        620        630        640        650
EDPNEAVREF AKEIDVSFVK IEEVIGAGEF GEVYKGRLKL PGKREIYVAI 
       660        670        680        690        700
KTLKAGYSEK QRRDFLSEAS IMGQFDHPNI IRLEGVVTKS RPVMIITEFM 
       710        720        730        740        750
ENGALDSFLR QNDGQFTVIQ LVGMLRGIAA GMKYLSEMNY VHRDLAARNI 
       760        770        780        790        800
LVNSNLVCKV SDFGLSRYLQ DDTSDPTYTS SLGGKIPVRW TAPEAIAYRK 
       810        820        830        840        850
FTSASDVWSY GIVMWEVMSF GERPYWDMSN QDVINAIEQD YRLPPPMDCP 
       860        870        880        890        900
AALHQLMLDC WQKDRNSRPR FAEIVNTLDK MIRNPASLKT VATITAVPSQ 
       910        920        930        940        950
PLLDRSIPDF TAFTTVDDWL SAIKMVQYRD SFLTAGFTSL QLVTQMTSED 
       960        970        980 
LLRIGVTLAG HQKKILSSIH SMRVQMNQSP SVMA
Length:984
Mass (Da):109,881
Last modified:March 1, 2003 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE967019C82AA400A
GO
Isoform 2 (identifier: Q8CBF3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     588-628: Missing.

Show »
Length:943
Mass (Da):105,294
Checksum:iEF28BF1D7FE097C9
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q8CA63Q8CA63_MOUSE
Ephrin type-B receptor 1
Ephb1
456Annotation 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 conflicti72L → Q in BAE22386 (PubMed:16141072).Curated1
Sequence conflicti187L → P in BAE22386 (PubMed:16141072).Curated1
Sequence conflicti194K → I in AAH57301 (PubMed:15489334).Curated1
Sequence conflicti641P → Q in BAC29348 (PubMed:16141072).Curated1
Sequence conflicti678P → R in AAH57301 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_021595588 – 628Missing in isoform 2. 1 PublicationAdd BLAST41

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
AK036148 mRNA Translation: BAC29320.1
AK036211 mRNA Translation: BAC29348.1
AK135018 mRNA Translation: BAE22386.1
AC109247 Genomic DNA No translation available.
AC132684 Genomic DNA No translation available.
AC156635 Genomic DNA No translation available.
CT025594 Genomic DNA No translation available.
BC057301 mRNA Translation: AAH57301.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS40742.1 [Q8CBF3-1]
CCDS52901.1 [Q8CBF3-2]

NCBI Reference Sequences

More...RefSeqi		NP_001161768.1, NM_001168296.1 [Q8CBF3-2]
NP_775623.3, NM_173447.3 [Q8CBF3-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000035129; ENSMUSP00000035129; ENSMUSG00000032537 [Q8CBF3-1]
ENSMUST00000085169; ENSMUSP00000082261; ENSMUSG00000032537 [Q8CBF3-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		270190

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:270190

UCSC genome browser

More...UCSCi		uc009rfn.2, mouse [Q8CBF3-1]
uc012gzg.1, mouse [Q8CBF3-2]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK036148 mRNA Translation: BAC29320.1
AK036211 mRNA Translation: BAC29348.1
AK135018 mRNA Translation: BAE22386.1
AC109247 Genomic DNA No translation available.
AC132684 Genomic DNA No translation available.
AC156635 Genomic DNA No translation available.
CT025594 Genomic DNA No translation available.
BC057301 mRNA Translation: AAH57301.1
CCDSiCCDS40742.1 [Q8CBF3-1]
CCDS52901.1 [Q8CBF3-2]
RefSeqiNP_001161768.1, NM_001168296.1 [Q8CBF3-2]
NP_775623.3, NM_173447.3 [Q8CBF3-1]

3D structure databases

SMRiQ8CBF3
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi234781, 3 interactors
IntActiQ8CBF3, 1 interactor
STRINGi10090.ENSMUSP00000035129

PTM databases

GlyGeniQ8CBF3, 3 sites
iPTMnetiQ8CBF3
PhosphoSitePlusiQ8CBF3

Proteomic databases

PaxDbiQ8CBF3
PeptideAtlasiQ8CBF3
PRIDEiQ8CBF3

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		33398, 542 antibodies

Genome annotation databases

EnsembliENSMUST00000035129; ENSMUSP00000035129; ENSMUSG00000032537 [Q8CBF3-1]
ENSMUST00000085169; ENSMUSP00000082261; ENSMUSG00000032537 [Q8CBF3-2]
GeneIDi270190
KEGGimmu:270190
UCSCiuc009rfn.2, mouse [Q8CBF3-1]
uc012gzg.1, mouse [Q8CBF3-2]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2047
MGIiMGI:1096337, Ephb1

Phylogenomic databases

eggNOGiKOG0196, Eukaryota
GeneTreeiENSGT00940000155297
HOGENOMiCLU_000288_141_0_1
InParanoidiQ8CBF3
KOiK05110
OMAiMACKACP
PhylomeDBiQ8CBF3
TreeFamiTF315608

Enzyme and pathway databases

ReactomeiR-MMU-2682334, EPH-Ephrin signaling
R-MMU-3928662, EPHB-mediated forward signaling
R-MMU-3928664, Ephrin signaling
R-MMU-3928665, EPH-ephrin mediated repulsion of cells

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		270190, 0 hits in 18 CRISPR screens

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

More...ChiTaRSi		Ephb1, mouse

Protein Ontology

More...PROi		PR:Q8CBF3
RNActiQ8CBF3, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000032537, Expressed in cardiac ventricle and 229 other tissues
ExpressionAtlasiQ8CBF3, baseline and differential
GenevisibleiQ8CBF3, MM

Family and domain databases

CDDicd10476, EphR_LBD_B1, 1 hit
cd00063, FN3, 2 hits
cd09551, SAM_EPH-B1, 1 hit
Gene3Di1.10.150.50, 1 hit
2.60.120.260, 1 hit
2.60.40.10, 2 hits
InterProiView protein in InterPro
IPR027936, Eph_TM
IPR034231, EphB1_rcpt_lig-bd
IPR042819, EphB1_SAM
IPR001090, Ephrin_rcpt_lig-bd_dom
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR008979, Galactose-bd-like_sf
IPR009030, Growth_fac_rcpt_cys_sf
IPR013783, Ig-like_fold
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR001660, SAM
IPR013761, SAM/pointed_sf
IPR001245, Ser-Thr/Tyr_kinase_cat_dom
IPR011641, Tyr-kin_ephrin_A/B_rcpt-like
IPR008266, Tyr_kinase_AS
IPR020635, Tyr_kinase_cat_dom
IPR016257, Tyr_kinase_ephrin_rcpt
IPR001426, Tyr_kinase_rcpt_V_CS
PfamiView protein in Pfam
PF14575, EphA2_TM, 1 hit
PF01404, Ephrin_lbd, 1 hit
PF00041, fn3, 2 hits
PF07714, Pkinase_Tyr, 1 hit
PF00536, SAM_1, 1 hit
PIRSFiPIRSF000666, TyrPK_ephrin_receptor, 1 hit
PRINTSiPR00109, TYRKINASE
SMARTiView protein in SMART
SM00615, EPH_lbd, 1 hit
SM01411, Ephrin_rec_like, 1 hit
SM00060, FN3, 2 hits
SM00454, SAM, 1 hit
SM00219, TyrKc, 1 hit
SUPFAMiSSF47769, SSF47769, 1 hit
SSF49265, SSF49265, 1 hit
SSF49785, SSF49785, 1 hit
SSF56112, SSF56112, 1 hit
SSF57184, SSF57184, 1 hit
PROSITEiView protein in PROSITE
PS01186, EGF_2, 1 hit
PS51550, EPH_LBD, 1 hit
PS50853, FN3, 2 hits
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00109, PROTEIN_KINASE_TYR, 1 hit
PS00790, RECEPTOR_TYR_KIN_V_1, 1 hit
PS00791, RECEPTOR_TYR_KIN_V_2, 1 hit
PS50105, SAM_DOMAIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEPHB1_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: Q8CBF3
Secondary accession number(s): B1B1C2
, Q3UY27, Q6PG23, Q8CBE2
<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: November 28, 2006
Last sequence update: March 1, 2003
Last modified: August 12, 2020
This is version 155 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<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

Reference proteome

Documents

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