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Protein

Ephrin-B1

Gene

EFNB1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiR-GGA-3928664. Ephrin signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin-B1
Alternative name(s):
CEK5 ligand
Short name:
CEK5-L
Gene namesi
Name:EFNB1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 231ExtracellularSequence analysisAdd BLAST206
Transmembranei232 – 252HelicalSequence analysisAdd BLAST21
Topological domaini253 – 334CytoplasmicSequence analysisAdd BLAST82

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000000839026 – 334Ephrin-B1Add BLAST309

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi60 ↔ 97PROSITE-ProRule annotation
Disulfide bondi85 ↔ 149PROSITE-ProRule annotation
Glycosylationi135N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

PTM databases

iPTMnetiO73612.

Interactioni

Subunit structurei

Binds to the receptor tyrosine kinase EPHB2. Interacts with GRIP1 and GRIP2 (By similarity).By similarity

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliO73612.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 160Ephrin RBDPROSITE-ProRule annotationAdd BLAST135

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi332 – 334PDZ-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

HOGENOMiHOG000220931.
HOVERGENiHBG051448.
InParanoidiO73612.
KOiK05463.
PhylomeDBiO73612.

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.

O73612-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARPRGGRWL LGVLLALCRL AAPLAKSLEP VSWSAGNPKF MSGKGLVIYP
60 70 80 90 100
EIGDKLDIIC PKAEPSKPYD YYKLYLVKKD QADACSTVMD PNVLVTCNRP
110 120 130 140 150
EQEIRFTIKF QEFSPNYMGL EFKRQQDYFI TSTSNGTLDG LENREGGVCQ
160 170 180 190 200
TRSMKIVMKV GQDPNAVIPE QLTTSRPSKE ADNTVKIVTQ SPRHKVPTVE
210 220 230 240 250
EPGKPGSVNQ NGQETQGPSD GFLSSKVAVF AAIGAGCVIF ILIIIFLVVL
260 270 280 290 300
LIKIRKRHRK HTQQRAAALS LSTLASPKCS GNAGSEPSDI IIPLRTTENN
310 320 330
YCPHYEKVSG DYGHPVYIVQ EMPPQSPANI YYKV
Length:334
Mass (Da):36,859
Last modified:August 1, 1998 - v1
Checksum:i48AF556E9ED56CD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72394 mRNA. Translation: AAC07986.1.
RefSeqiNP_990366.1. NM_205035.1.
UniGeneiGga.2142.
Gga.5416.

Genome annotation databases

GeneIDi395896.
KEGGigga:395896.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72394 mRNA. Translation: AAC07986.1.
RefSeqiNP_990366.1. NM_205035.1.
UniGeneiGga.2142.
Gga.5416.

3D structure databases

ProteinModelPortaliO73612.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiO73612.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi395896.
KEGGigga:395896.

Organism-specific databases

CTDi1947.

Phylogenomic databases

HOGENOMiHOG000220931.
HOVERGENiHBG051448.
InParanoidiO73612.
KOiK05463.
PhylomeDBiO73612.

Enzyme and pathway databases

ReactomeiR-GGA-3928664. Ephrin signaling.

Miscellaneous databases

PROiO73612.

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_CHICK
AccessioniPrimary (citable) accession number: O73612
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 1, 1998
Last modified: October 5, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.