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Protein

Ephrin-B2

Gene

EFNB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors 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. Binds to receptor tyrosine kinase including EPHA4, EPHA3 and EPHB4. Together with EPHB4 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells. May play a role in constraining the orientation of longitudinally projecting axons.1 Publication
(Microbial infection) Acts as a receptor for Hendra virus and Nipah virus.4 Publications

<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

  • ephrin receptor binding Source: UniProtKB
  • protein tyrosine kinase activity Source: Reactome
  • virus receptor activity Source: UniProtKB-KW

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 functionDevelopmental protein, Host cell receptor for virus entry, Receptor
Biological processAngiogenesis, Differentiation, Host-virus interaction, Neurogenesis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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

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

More...
SignaLinki
P52799

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P52799

<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:
Ephrin-B2
Alternative name(s):
EPH-related receptor tyrosine kinase ligand 5
Short name:
LERK-5
HTK ligand
Short name:
HTK-L
<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:EFNB2
Synonyms:EPLG5, HTKL, LERK5
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 13

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000125266.6

Human Gene Nomenclature Database

More...
HGNCi
HGNC:3227 EFNB2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
600527 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P52799

<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 domaini28 – 229ExtracellularSequence analysisAdd BLAST202
<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>Transmembranei230 – 250HelicalSequence analysisAdd BLAST21
Topological domaini251 – 333CytoplasmicSequence analysisAdd BLAST83

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi121 – 122LW → YM: Complete loss of Nipah protein G binding. 1 Publication2

Organism-specific databases

DisGeNET

More...
DisGeNETi
1948

Open Targets

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OpenTargetsi
ENSG00000125266

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA27662

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
EFNB2

Domain mapping of disease mutations (DMDM)

More...
DMDMi
1706673

<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 – 27Sequence analysisAdd BLAST27
<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_000000839228 – 333Ephrin-B2Add BLAST306

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>Glycosylationi36N-linked (GlcNAc...) asparagineSequence analysis2 Publications1
<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 bondi62 ↔ 101Combined sources5 Publications
Disulfide bondi89 ↔ 153Combined sources5 Publications
Glycosylationi139N-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 residuei260PhosphoserineBy similarity1
Modified residuei274PhosphothreonineBy similarity1
Modified residuei277Omega-N-methylarginineBy 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

Inducible phosphorylation of tyrosine residues in the cytoplasmic domain.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P52799

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P52799

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P52799

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

More...
PaxDbi
P52799

PeptideAtlas

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PeptideAtlasi
P52799

PRoteomics IDEntifications database

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PRIDEi
P52799

ProteomicsDB human proteome resource

More...
ProteomicsDBi
56538

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
1937

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P52799

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

More...
PhosphoSitePlusi
P52799

<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

Lung and kidney.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000125266 Expressed in 231 organ(s), highest expression level in neocortex

CleanEx database of gene expression profiles

More...
CleanExi
HS_EFNB2

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P52799 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB009368
HPA008999

<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

Interacts with PDZRN3 (By similarity). Binds to the receptor tyrosine kinases EPHA4, EPHB4 and EPHA3.By similarity3 Publications
(Microbial infection) Interacts with Hendra virus and Nipah virus G protein (PubMed:16007075, PubMed:16477309, PubMed:17376907, PubMed:15998730).4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
108268, 68 interactors

Database of interacting proteins

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DIPi
DIP-46378N

Protein interaction database and analysis system

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IntActi
P52799, 9 interactors

Molecular INTeraction database

More...
MINTi
P52799

STRING: functional protein association networks

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STRINGi
9606.ENSP00000245323

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

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HLEX-ray2.05B28-165[»]
2I85NMR-A25-166[»]
2VSKX-ray3.30B/D28-165[»]
2VSMX-ray1.80B28-165[»]
2WO2X-ray2.45B27-167[»]
3GXUX-ray2.50B27-169[»]
4UF7X-ray1.70C/E27-167[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P52799

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

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SMRi
P52799

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...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P52799

<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>Domaini28 – 164Ephrin RBDPROSITE-ProRule annotationAdd BLAST137

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>Motifi331 – 333PDZ-bindingSequence analysis3

<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 ephrin family.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3858 Eukaryota
ENOG4111FMJ LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155868

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000220931

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG051448

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P52799

KEGG Orthology (KO)

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KOi
K05463

Identification of Orthologs from Complete Genome Data

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OMAi
NRDYYII

Database of Orthologous Groups

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OrthoDBi
903831at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P52799

Family and domain databases

Conserved Domains Database

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CDDi
cd10426 Ephrin-B_Ectodomain, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.420, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR008972 Cupredoxin
IPR031328 Ephrin
IPR034255 Ephrin-B_Ecto
IPR019765 Ephrin_CS
IPR001799 Ephrin_RBD

The PANTHER Classification System

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PANTHERi
PTHR11304 PTHR11304, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00812 Ephrin, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01347 EPHRIN

ProDom; a protein domain database

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ProDomi
View protein in ProDom or Entries sharing at least one domain
PD002533 Ephrin, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49503 SSF49503, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01299 EPHRIN_RBD_1, 1 hit
PS51551 EPHRIN_RBD_2, 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.

P52799-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAVRRDSVWK YCWGVLMVLC RTAISKSIVL EPIYWNSSNS KFLPGQGLVL
60 70 80 90 100
YPQIGDKLDI ICPKVDSKTV GQYEYYKVYM VDKDQADRCT IKKENTPLLN
110 120 130 140 150
CAKPDQDIKF TIKFQEFSPN LWGLEFQKNK DYYIISTSNG SLEGLDNQEG
160 170 180 190 200
GVCQTRAMKI LMKVGQDASS AGSTRNKDPT RRPELEAGTN GRSSTTSPFV
210 220 230 240 250
KPNPGSSTDG NSAGHSGNNI LGSEVALFAG IASGCIIFIV IIITLVVLLL
260 270 280 290 300
KYRRRHRKHS PQHTTTLSLS TLATPKRSGN NNGSEPSDII IPLRTADSVF
310 320 330
CPHYEKVSGD YGHPVYIVQE MPPQSPANIY YKV
Length:333
Mass (Da):36,923
Last modified:October 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6D9932A632626AEA
GO

Sequence databases

Select the link destinations:

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

More...
DDBJi
Links Updated
U16797 mRNA Translation: AAA99707.1
L38734 mRNA Translation: AAC41752.1
U81262 mRNA Translation: AAD03786.1
AL138689 Genomic DNA No translation available.
BC069342 mRNA Translation: AAH69342.1
BC074856 mRNA Translation: AAH74856.1
BC074857 mRNA Translation: AAH74857.1
BC105955 mRNA Translation: AAI05956.1
BC105956 mRNA Translation: AAI05957.1
BC105957 mRNA Translation: AAI05958.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS9507.1

Protein sequence database of the Protein Information Resource

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PIRi
I84743

NCBI Reference Sequences

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RefSeqi
NP_004084.1, NM_004093.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.149239

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000245323; ENSP00000245323; ENSG00000125266
ENST00000646441; ENSP00000493716; ENSG00000125266

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1948

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1948

UCSC genome browser

More...
UCSCi
uc001vqi.4 human

<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
U16797 mRNA Translation: AAA99707.1
L38734 mRNA Translation: AAC41752.1
U81262 mRNA Translation: AAD03786.1
AL138689 Genomic DNA No translation available.
BC069342 mRNA Translation: AAH69342.1
BC074856 mRNA Translation: AAH74856.1
BC074857 mRNA Translation: AAH74857.1
BC105955 mRNA Translation: AAI05956.1
BC105956 mRNA Translation: AAI05957.1
BC105957 mRNA Translation: AAI05958.1
CCDSiCCDS9507.1
PIRiI84743
RefSeqiNP_004084.1, NM_004093.3
UniGeneiHs.149239

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HLEX-ray2.05B28-165[»]
2I85NMR-A25-166[»]
2VSKX-ray3.30B/D28-165[»]
2VSMX-ray1.80B28-165[»]
2WO2X-ray2.45B27-167[»]
3GXUX-ray2.50B27-169[»]
4UF7X-ray1.70C/E27-167[»]
ProteinModelPortaliP52799
SMRiP52799
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108268, 68 interactors
DIPiDIP-46378N
IntActiP52799, 9 interactors
MINTiP52799
STRINGi9606.ENSP00000245323

PTM databases

GlyConnecti1937
iPTMnetiP52799
PhosphoSitePlusiP52799

Polymorphism and mutation databases

BioMutaiEFNB2
DMDMi1706673

Proteomic databases

EPDiP52799
jPOSTiP52799
MaxQBiP52799
PaxDbiP52799
PeptideAtlasiP52799
PRIDEiP52799
ProteomicsDBi56538

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
1948
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000245323; ENSP00000245323; ENSG00000125266
ENST00000646441; ENSP00000493716; ENSG00000125266
GeneIDi1948
KEGGihsa:1948
UCSCiuc001vqi.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1948
DisGeNETi1948
EuPathDBiHostDB:ENSG00000125266.6

GeneCards: human genes, protein and diseases

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GeneCardsi
EFNB2
HGNCiHGNC:3227 EFNB2
HPAiCAB009368
HPA008999
MIMi600527 gene
neXtProtiNX_P52799
OpenTargetsiENSG00000125266
PharmGKBiPA27662

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG3858 Eukaryota
ENOG4111FMJ LUCA
GeneTreeiENSGT00940000155868
HOGENOMiHOG000220931
HOVERGENiHBG051448
InParanoidiP52799
KOiK05463
OMAiNRDYYII
OrthoDBi903831at2759
PhylomeDBiP52799

Enzyme and pathway databases

ReactomeiR-HSA-2682334 EPH-Ephrin signaling
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-3928664 Ephrin signaling
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
SignaLinkiP52799
SIGNORiP52799

Miscellaneous databases

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

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ChiTaRSi
EFNB2 human
EvolutionaryTraceiP52799

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
EFNB2

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

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GenomeRNAii
1948

Protein Ontology

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PROi
PR:P52799

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000125266 Expressed in 231 organ(s), highest expression level in neocortex
CleanExiHS_EFNB2
GenevisibleiP52799 HS

Family and domain databases

CDDicd10426 Ephrin-B_Ectodomain, 1 hit
Gene3Di2.60.40.420, 1 hit
InterProiView protein in InterPro
IPR008972 Cupredoxin
IPR031328 Ephrin
IPR034255 Ephrin-B_Ecto
IPR019765 Ephrin_CS
IPR001799 Ephrin_RBD
PANTHERiPTHR11304 PTHR11304, 1 hit
PfamiView protein in Pfam
PF00812 Ephrin, 1 hit
PRINTSiPR01347 EPHRIN
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002533 Ephrin, 1 hit
SUPFAMiSSF49503 SSF49503, 1 hit
PROSITEiView protein in PROSITE
PS01299 EPHRIN_RBD_1, 1 hit
PS51551 EPHRIN_RBD_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiEFNB2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P52799
Secondary accession number(s): Q5JV56
<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: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 16, 2019
This is version 171 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
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