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Protein

Ephrin-B1

Gene

EFNB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to the receptor tyrosine kinases EPHB1 and EPHA1. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons (By similarity).By similarity
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 the receptor tyrosine kinases EPHB3 (preferred), EPHB1 and EPHA1. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons (By similarity).By similarity

GO - Molecular functioni

  • ephrin receptor binding Source: ProtInc

GO - Biological processi

  • axon guidance Source: GO_Central
  • cell adhesion Source: ProtInc
  • cell-cell signaling Source: ProtInc
  • embryonic pattern specification Source: Ensembl
  • ephrin receptor signaling pathway Source: GO_Central
  • neural crest cell migration Source: Ensembl
  • positive regulation of T cell proliferation Source: Ensembl
  • T cell costimulation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000090776-MONOMER.
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.

Names & Taxonomyi

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
Gene namesi
Name:EFNB1
Synonyms:EFL3, EPLG2, LERK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:3226. EFNB1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini28 – 237ExtracellularSequence analysisAdd BLAST210
Transmembranei238 – 258HelicalSequence analysisAdd BLAST21
Topological domaini259 – 346CytoplasmicSequence analysisAdd BLAST88

GO - Cellular componenti

  • cytoplasm Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • membrane raft Source: Ensembl
  • nucleus Source: Ensembl
  • plasma membrane Source: Reactome
  • synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

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.
See also OMIM:304110
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02312727P → R in CFNS. 1 Publication1
Natural variantiVAR_02312854P → L in CFNS. 2 PublicationsCorresponds to variant rs104894801dbSNPEnsembl.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 rs104894796dbSNPEnsembl.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 rs28936069dbSNPEnsembl.1
Natural variantiVAR_023139151G → V in CFNS. 1 PublicationCorresponds to variant rs28936070dbSNPEnsembl.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 rs28935170dbSNPEnsembl.1
Natural variantiVAR_023145158M → V in CFNS. 1 PublicationCorresponds to variant rs28936071dbSNPEnsembl.1
Natural variantiVAR_023146182S → R in CFNS. 1 Publication1

Keywords - Diseasei

Craniosynostosis, Disease mutation

Organism-specific databases

DisGeNETi1947.
MalaCardsiEFNB1.
MIMi304110. phenotype.
OpenTargetsiENSG00000090776.
Orphaneti1520. Craniofrontonasal dysplasia.
PharmGKBiPA27661.

Polymorphism and mutation databases

BioMutaiEFNB1.
DMDMi1706668.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 271 PublicationAdd BLAST27
ChainiPRO_000000838728 – 346Ephrin-B1Add BLAST319

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi64 ↔ 101PROSITE-ProRule annotation
Disulfide bondi89 ↔ 153PROSITE-ProRule annotation
Glycosylationi139N-linked (GlcNAc...)Sequence analysis1
Modified residuei281PhosphoserineCombined sources1
Modified residuei287PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP98172.
MaxQBiP98172.
PaxDbiP98172.
PeptideAtlasiP98172.
PRIDEiP98172.

PTM databases

iPTMnetiP98172.
PhosphoSitePlusiP98172.

Miscellaneous databases

PMAP-CutDBP98172.

Expressioni

Tissue specificityi

Heart, placenta, lung, liver, skeletal muscle, kidney, pancreas.

Inductioni

By TNF.

Gene expression databases

BgeeiENSG00000090776.
CleanExiHS_EFNB1.
GenevisibleiP98172. HS.

Organism-specific databases

HPAiCAB031489.

Interactioni

Subunit structurei

Interacts with GRIP1 and GRIP2. Interacts with TLE1.2 Publications

Binary interactionsi

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

GO - Molecular functioni

  • ephrin receptor binding Source: ProtInc

Protein-protein interaction databases

BioGridi108267. 34 interactors.
IntActiP98172. 13 interactors.
STRINGi9606.ENSP00000204961.

Structurei

3D structure databases

ProteinModelPortaliP98172.
SMRiP98172.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 164Ephrin RBDPROSITE-ProRule annotationAdd BLAST135

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi344 – 346PDZ-bindingSequence analysis3

Sequence similaritiesi

Belongs to the ephrin family.PROSITE-ProRule annotation
Contains 1 ephrin RBD (ephrin receptor-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
GeneTreeiENSGT00390000005839.
HOGENOMiHOG000220931.
HOVERGENiHBG051448.
InParanoidiP98172.
KOiK05463.
OMAiWALCRLA.
OrthoDBiEOG091G0BPC.
PhylomeDBiP98172.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR031328. Ephrin.
IPR019765. Ephrin_CS.
IPR001799. Ephrin_RBD.
[Graphical view]
PANTHERiPTHR11304. PTHR11304. 1 hit.
PfamiPF00812. Ephrin. 1 hit.
[Graphical view]
PRINTSiPR01347. EPHRIN.
ProDomiPD002533. Ephrin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF49503. SSF49503. 1 hit.
PROSITEiPS01299. EPHRIN_RBD_1. 1 hit.
PS51551. EPHRIN_RBD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
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 rs104894801dbSNPEnsembl.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 rs104894796dbSNPEnsembl.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 rs28936069dbSNPEnsembl.1
Natural variantiVAR_023139151G → V in CFNS. 1 PublicationCorresponds to variant rs28936070dbSNPEnsembl.1
Natural variantiVAR_023140153C → S in CFNS. 1 Publication1
Natural variantiVAR_023141153C → Y in CFNS. 1 Publication1
Natural variantiVAR_023142154R → H.1 PublicationCorresponds to variant rs146636295dbSNPEnsembl.1
Natural variantiVAR_023143155T → P in CFNS. 1 Publication1
Natural variantiVAR_023144158M → I in CFNS. 1 PublicationCorresponds to variant rs28935170dbSNPEnsembl.1
Natural variantiVAR_023145158M → V in CFNS. 1 PublicationCorresponds to variant rs28936071dbSNPEnsembl.1
Natural variantiVAR_059256172T → M.Corresponds to variant rs7889678dbSNPEnsembl.1
Natural variantiVAR_023146182S → R in CFNS. 1 Publication1
Natural variantiVAR_023147189V → A.Corresponds to variant rs16989105dbSNPEnsembl.1

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. Translation: CAB86409.1.
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.
UniGeneiHs.144700.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

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. Translation: CAB86409.1.
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.
UniGeneiHs.144700.

3D structure databases

ProteinModelPortaliP98172.
SMRiP98172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108267. 34 interactors.
IntActiP98172. 13 interactors.
STRINGi9606.ENSP00000204961.

PTM databases

iPTMnetiP98172.
PhosphoSitePlusiP98172.

Polymorphism and mutation databases

BioMutaiEFNB1.
DMDMi1706668.

Proteomic databases

EPDiP98172.
MaxQBiP98172.
PaxDbiP98172.
PeptideAtlasiP98172.
PRIDEiP98172.

Protocols and materials databases

DNASUi1947.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1947.
DisGeNETi1947.
GeneCardsiEFNB1.
HGNCiHGNC:3226. EFNB1.
HPAiCAB031489.
MalaCardsiEFNB1.
MIMi300035. gene.
304110. phenotype.
neXtProtiNX_P98172.
OpenTargetsiENSG00000090776.
Orphaneti1520. Craniofrontonasal dysplasia.
PharmGKBiPA27661.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
GeneTreeiENSGT00390000005839.
HOGENOMiHOG000220931.
HOVERGENiHBG051448.
InParanoidiP98172.
KOiK05463.
OMAiWALCRLA.
OrthoDBiEOG091G0BPC.
PhylomeDBiP98172.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000090776-MONOMER.
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

ChiTaRSiEFNB1. human.
GeneWikiiEFNB1.
GenomeRNAii1947.
PMAP-CutDBP98172.
PROiP98172.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000090776.
CleanExiHS_EFNB1.
GenevisibleiP98172. HS.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR031328. Ephrin.
IPR019765. Ephrin_CS.
IPR001799. Ephrin_RBD.
[Graphical view]
PANTHERiPTHR11304. PTHR11304. 1 hit.
PfamiPF00812. Ephrin. 1 hit.
[Graphical view]
PRINTSiPR01347. EPHRIN.
ProDomiPD002533. Ephrin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF49503. SSF49503. 1 hit.
PROSITEiPS01299. EPHRIN_RBD_1. 1 hit.
PS51551. EPHRIN_RBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEFNB1_HUMAN
AccessioniPrimary (citable) accession number: P98172
Secondary accession number(s): D3DVU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 169 of the entry and version 1 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.