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Entry version 188 (03 Jul 2019)
Sequence version 1 (01 Oct 1996)
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Protein

Ephrin-B1

Gene

EFNB1

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 (PubMed:8070404, PubMed:7973638). Binding to Eph receptors residing on adjacent cells leads to contact-dependent bidirectional signaling into neighboring cells (PubMed:8070404, PubMed:7973638). Shows high affinity for the receptor tyrosine kinase EPHB1/ELK (PubMed:8070404, PubMed:7973638). Can also bind EPHB2 and EPHB3 (PubMed:8070404). Binds to, and induces collapse of, commissural axons/growth cones in vitro (By similarity). May play a role in constraining the orientation of longitudinally projecting axons (By similarity).By similarity2 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

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
Biological processDifferentiation, 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
P98172

SIGNOR Signaling Network Open Resource

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SIGNORi
P98172

<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-B1
Alternative name(s):
EFL-3
ELK ligand
Short name:
ELK-L
EPH-related receptor tyrosine kinase ligand 2
Short name:
LERK-2
Cleaved into the following 2 chains:
Ephrin-B1 C-terminal fragment1 Publication
Short name:
Ephrin-B1 CTF1 Publication
Ephrin-B1 intracellular domain1 Publication
Short name:
Ephrin-B1 ICD1 Publication
<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:EFNB1
Synonyms:EFL3, EPLG2, LERK2
<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 X

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:3226 EFNB1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
300035 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P98172

<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_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 – 237ExtracellularSequence analysisAdd BLAST210
<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>Transmembranei238 – 258HelicalSequence analysisAdd BLAST21
Topological domaini259 – 346CytoplasmicSequence analysisAdd BLAST88

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

<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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Craniofrontonasal syndrome (CFNS)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionX-linked inherited syndrome characterized by hypertelorism, coronal synostosis with brachycephaly, downslanting palpebral fissures, clefting of the nasal tip, joint anomalies, longitudinally grooved fingernails and other digital anomalies.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02312727P → R in CFNS. 1 Publication1
Natural variantiVAR_02312854P → L in CFNS. 2 PublicationsCorresponds to variant dbSNP:rs104894801EnsemblClinVar.1
Natural variantiVAR_02312962I → T in CFNS. 1 Publication1
Natural variantiVAR_02313098L → S in CFNS. 1 Publication1
Natural variantiVAR_023131111T → I in CFNS. 1 PublicationCorresponds to variant dbSNP:rs104894796EnsemblClinVar.1
Natural variantiVAR_023132115Q → P in CFNS. 1 Publication1
Natural variantiVAR_023133119P → H in CFNS. 2 Publications1
Natural variantiVAR_023134119P → S in CFNS. 1 Publication1
Natural variantiVAR_023135119P → T in CFNS. 1 Publication1
Natural variantiVAR_023136137T → A in CFNS. 1 Publication1
Natural variantiVAR_023137138S → F in CFNS. 1 Publication1
Natural variantiVAR_023138151G → S in CFNS. 2 PublicationsCorresponds to variant dbSNP:rs28936069EnsemblClinVar.1
Natural variantiVAR_023139151G → V in CFNS. 1 PublicationCorresponds to variant dbSNP:rs28936070EnsemblClinVar.1
Natural variantiVAR_023140153C → S in CFNS. 1 Publication1
Natural variantiVAR_023141153C → Y in CFNS. 1 Publication1
Natural variantiVAR_023143155T → P in CFNS. 1 Publication1
Natural variantiVAR_023144158M → I in CFNS. 1 PublicationCorresponds to variant dbSNP:rs28935170EnsemblClinVar.1
Natural variantiVAR_023145158M → V in CFNS. 1 PublicationCorresponds to variant dbSNP:rs28936071EnsemblClinVar.1
Natural variantiVAR_023146182S → R in CFNS. 1 Publication1

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>Mutagenesisi260 – 273Missing : The intracellular domain peptide fails to localize to the nucleus. 1 PublicationAdd BLAST14
Mutagenesisi344 – 346Missing : No effect on gamma-secretase mediated proteolysis of the C-terminal fragment. 1 Publication3

Keywords - Diseasei

Craniosynostosis, Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
1947

MalaCards human disease database

More...
MalaCardsi
EFNB1
MIMi304110 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000090776

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
1520 Craniofrontonasal dysplasia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27661

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
EFNB1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
1706668

<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 – 271 PublicationAdd 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_000000838728 – 346Ephrin-B1Add BLAST319
ChainiPRO_0000445791218 – 346Ephrin-B1 C-terminal fragmentCuratedAdd BLAST129
ChainiPRO_0000445792260 – 346Ephrin-B1 intracellular domainCuratedAdd BLAST87

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi64 ↔ 101PROSITE-ProRule annotation
Disulfide bondi89 ↔ 153PROSITE-ProRule annotation
<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>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 residuei281PhosphoserineCombined sources1
Modified residuei287PhosphoserineCombined sources1

<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.1 Publication
Proteolytically processed. The ectodomain is cleaved, probably by a metalloprotease, to produce a membrane-tethered C-terminal fragment. This fragment is then further processed by the gamma-secretase complex to yield a soluble intracellular domain peptide which can translocate to the nucleus. The intracellular domain peptide is highly labile suggesting that it is targeted for degradation by the proteasome.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P98172

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P98172

MaxQB - The MaxQuant DataBase

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MaxQBi
P98172

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

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PaxDbi
P98172

PeptideAtlas

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PeptideAtlasi
P98172

PRoteomics IDEntifications database

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PRIDEi
P98172

ProteomicsDB human proteome resource

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ProteomicsDBi
57806

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P98172

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

More...
PhosphoSitePlusi
P98172

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P98172

<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

Widely expressed (PubMed:8070404, PubMed:7973638). Detected in both neuronal and non-neuronal tissues (PubMed:8070404, PubMed:7973638). Seems to have particularly strong expression in retina, sciatic nerve, heart and spinal cord (PubMed:7973638).2 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated in response to TNF.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000090776 Expressed in 151 organ(s), highest expression level in metanephric glomerulus

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P98172 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB031489
HPA067188

<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 (via PDZ-binding motif) with GRIP1 and GRIP2 (via PDZ domain 6) (PubMed:10197531).

Interacts with TLE1 (PubMed:21429299). The intracellular domain peptide interacts with ZHX2; the interaction enhances ZHX2 transcriptional repression activity (By similarity).

By similarity2 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

WithEntry#Exp.IntActNotes
ERBB2P0462611EBI-538287,EBI-641062

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108267, 43 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P98172

Protein interaction database and analysis system

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IntActi
P98172, 16 interactors

Molecular INTeraction database

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MINTi
P98172

STRING: functional protein association networks

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STRINGi
9606.ENSP00000204961

<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

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SMRi
P98172

Database of comparative protein structure models

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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_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>Domaini30 – 164Ephrin RBDPROSITE-ProRule annotationAdd BLAST135

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni263 – 294Interaction with ZHX2By similarityAdd BLAST32

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>Motifi260 – 273Nuclear localization signal1 PublicationAdd BLAST14
Motifi344 – 346PDZ-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

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eggNOGi
KOG3858 Eukaryota
ENOG4111FMJ LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000160128

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000220931

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P98172

KEGG Orthology (KO)

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KOi
K05463

Identification of Orthologs from Complete Genome Data

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OMAi
FKKYHDY

Database of Orthologous Groups

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OrthoDBi
1275401at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P98172

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

More...
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

Superfamily database of structural and functional annotation

More...
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>. 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>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.

P98172-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARPGQRWLG KWLVAMVVWA LCRLATPLAK NLEPVSWSSL NPKFLSGKGL
60 70 80 90 100
VIYPKIGDKL DIICPRAEAG RPYEYYKLYL VRPEQAAACS TVLDPNVLVT
110 120 130 140 150
CNRPEQEIRF TIKFQEFSPN YMGLEFKKHH DYYITSTSNG SLEGLENREG
160 170 180 190 200
GVCRTRTMKI IMKVGQDPNA VTPEQLTTSR PSKEADNTVK MATQAPGSRG
210 220 230 240 250
SLGDSDGKHE TVNQEEKSGP GASGGSSGDP DGFFNSKVAL FAAVGAGCVI
260 270 280 290 300
FLLIIIFLTV LLLKLRKRHR KHTQQRAAAL SLSTLASPKG GSGTAGTEPS
310 320 330 340
DIIIPLRTTE NNYCPHYEKV SGDYGHPVYI VQEMPPQSPA NIYYKV
Length:346
Mass (Da):38,007
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:i473DD2F1A5BF89DE
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02312727P → R in CFNS. 1 Publication1
Natural variantiVAR_02312854P → L in CFNS. 2 PublicationsCorresponds to variant dbSNP:rs104894801EnsemblClinVar.1
Natural variantiVAR_02312962I → T in CFNS. 1 Publication1
Natural variantiVAR_02313098L → S in CFNS. 1 Publication1
Natural variantiVAR_023131111T → I in CFNS. 1 PublicationCorresponds to variant dbSNP:rs104894796EnsemblClinVar.1
Natural variantiVAR_023132115Q → P in CFNS. 1 Publication1
Natural variantiVAR_023133119P → H in CFNS. 2 Publications1
Natural variantiVAR_023134119P → S in CFNS. 1 Publication1
Natural variantiVAR_023135119P → T in CFNS. 1 Publication1
Natural variantiVAR_023136137T → A in CFNS. 1 Publication1
Natural variantiVAR_023137138S → F in CFNS. 1 Publication1
Natural variantiVAR_023138151G → S in CFNS. 2 PublicationsCorresponds to variant dbSNP:rs28936069EnsemblClinVar.1
Natural variantiVAR_023139151G → V in CFNS. 1 PublicationCorresponds to variant dbSNP:rs28936070EnsemblClinVar.1
Natural variantiVAR_023140153C → S in CFNS. 1 Publication1
Natural variantiVAR_023141153C → Y in CFNS. 1 Publication1
Natural variantiVAR_023142154R → H1 PublicationCorresponds to variant dbSNP:rs146636295Ensembl.1
Natural variantiVAR_023143155T → P in CFNS. 1 Publication1
Natural variantiVAR_023144158M → I in CFNS. 1 PublicationCorresponds to variant dbSNP:rs28935170EnsemblClinVar.1
Natural variantiVAR_023145158M → V in CFNS. 1 PublicationCorresponds to variant dbSNP:rs28936071EnsemblClinVar.1
Natural variantiVAR_059256172T → M. Corresponds to variant dbSNP:rs7889678Ensembl.1
Natural variantiVAR_023146182S → R in CFNS. 1 Publication1
Natural variantiVAR_023147189V → A. Corresponds to variant dbSNP:rs16989105EnsemblClinVar.1

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

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DDBJi
Links Updated
U09304 mRNA Translation: AAA53093.1
L37361 mRNA Translation: AAA52369.1
U09303 mRNA Translation: AAB41127.1
AL136092 Genomic DNA No translation available.
CH471132 Genomic DNA Translation: EAX05370.1
CH471132 Genomic DNA Translation: EAX05371.1
BC016649 mRNA Translation: AAH16649.1
BC052979 mRNA Translation: AAH52979.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS14391.1

Protein sequence database of the Protein Information Resource

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PIRi
S46993

NCBI Reference Sequences

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RefSeqi
NP_004420.1, NM_004429.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000204961; ENSP00000204961; ENSG00000090776

Database of genes from NCBI RefSeq genomes

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GeneIDi
1947

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:1947

UCSC genome browser

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UCSCi
uc004dxd.5 human

Keywords - Coding sequence diversityi

Polymorphism

<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
U09304 mRNA Translation: AAA53093.1
L37361 mRNA Translation: AAA52369.1
U09303 mRNA Translation: AAB41127.1
AL136092 Genomic DNA No translation available.
CH471132 Genomic DNA Translation: EAX05370.1
CH471132 Genomic DNA Translation: EAX05371.1
BC016649 mRNA Translation: AAH16649.1
BC052979 mRNA Translation: AAH52979.1
CCDSiCCDS14391.1
PIRiS46993
RefSeqiNP_004420.1, NM_004429.4

3D structure databases

SMRiP98172
ModBaseiSearch...

Protein-protein interaction databases

BioGridi108267, 43 interactors
CORUMiP98172
IntActiP98172, 16 interactors
MINTiP98172
STRINGi9606.ENSP00000204961

PTM databases

iPTMnetiP98172
PhosphoSitePlusiP98172

Polymorphism and mutation databases

BioMutaiEFNB1
DMDMi1706668

Proteomic databases

EPDiP98172
jPOSTiP98172
MaxQBiP98172
PaxDbiP98172
PeptideAtlasiP98172
PRIDEiP98172
ProteomicsDBi57806

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
1947
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000204961; ENSP00000204961; ENSG00000090776
GeneIDi1947
KEGGihsa:1947
UCSCiuc004dxd.5 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1947
DisGeNETi1947

GeneCards: human genes, protein and diseases

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GeneCardsi
EFNB1
HGNCiHGNC:3226 EFNB1
HPAiCAB031489
HPA067188
MalaCardsiEFNB1
MIMi300035 gene
304110 phenotype
neXtProtiNX_P98172
OpenTargetsiENSG00000090776
Orphaneti1520 Craniofrontonasal dysplasia
PharmGKBiPA27661

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3858 Eukaryota
ENOG4111FMJ LUCA
GeneTreeiENSGT00940000160128
HOGENOMiHOG000220931
InParanoidiP98172
KOiK05463
OMAiFKKYHDY
OrthoDBi1275401at2759
PhylomeDBiP98172

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
SignaLinkiP98172
SIGNORiP98172

Miscellaneous databases

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

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ChiTaRSi
EFNB1 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
EFNB1

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

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GenomeRNAii
1947
PMAP-CutDBiP98172

Protein Ontology

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PROi
PR:P98172

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000090776 Expressed in 151 organ(s), highest expression level in metanephric glomerulus
GenevisibleiP98172 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
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...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiEFNB1_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: P98172
Secondary accession number(s): D3DVU0
<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: July 3, 2019
This is version 188 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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