Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P98172 (EFNB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:EFNB1
Synonyms:EFL3, EPLG2, LERK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

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.

Subunit structure

Interacts with GRIP1 and GRIP2. Ref.8

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

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

Induction

By TNF.

Post-translational modification

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

Involvement in disease

Craniofrontonasal syndrome (CFNS) [MIM:304110]: X-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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.13

Sequence similarities

Belongs to the ephrin family.

Contains 1 ephrin RBD (ephrin receptor-binding) domain.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell adhesion

Traceable author statement PubMed 8798744. Source: ProtInc

cell-cell signaling

Traceable author statement PubMed 8798744. Source: ProtInc

embryonic pattern specification

Inferred from electronic annotation. Source: Ensembl

ephrin receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

neural crest cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

integral component of plasma membrane

Traceable author statement PubMed 8660976. Source: ProtInc

membrane raft

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

synapse

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionephrin receptor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction PubMed 9883737. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ERBB2P0462611EBI-538287,EBI-641062

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.7
Chain28 – 346319Ephrin-B1
PRO_0000008387

Regions

Topological domain28 – 237210Extracellular Potential
Transmembrane238 – 25821Helical; Potential
Topological domain259 – 34688Cytoplasmic Potential
Domain30 – 164135Ephrin RBD
Motif344 – 3463PDZ-binding Potential

Amino acid modifications

Modified residue2871Phosphoserine Ref.9 Ref.10
Glycosylation1391N-linked (GlcNAc...) Potential
Disulfide bond64 ↔ 101 By similarity
Disulfide bond89 ↔ 153 By similarity

Natural variations

Natural variant271P → R in CFNS. Ref.13
VAR_023127
Natural variant541P → L in CFNS. Ref.11 Ref.13
VAR_023128
Natural variant621I → T in CFNS. Ref.12
VAR_023129
Natural variant981L → S in CFNS. Ref.12
VAR_023130
Natural variant1111T → I in CFNS. Ref.11
VAR_023131
Natural variant1151Q → P in CFNS. Ref.12
VAR_023132
Natural variant1191P → H in CFNS. Ref.12 Ref.13
VAR_023133
Natural variant1191P → S in CFNS. Ref.13
VAR_023134
Natural variant1191P → T in CFNS. Ref.12
VAR_023135
Natural variant1371T → A in CFNS. Ref.13
VAR_023136
Natural variant1381S → F in CFNS. Ref.13
VAR_023137
Natural variant1511G → S in CFNS. Ref.12 Ref.13
Corresponds to variant rs28936069 [ dbSNP | Ensembl ].
VAR_023138
Natural variant1511G → V in CFNS. Ref.12
Corresponds to variant rs28936070 [ dbSNP | Ensembl ].
VAR_023139
Natural variant1531C → S in CFNS. Ref.13
VAR_023140
Natural variant1531C → Y in CFNS. Ref.13
VAR_023141
Natural variant1541R → H. Ref.12
VAR_023142
Natural variant1551T → P in CFNS. Ref.12
VAR_023143
Natural variant1581M → I in CFNS. Ref.12
Corresponds to variant rs28935170 [ dbSNP | Ensembl ].
VAR_023144
Natural variant1581M → V in CFNS. Ref.12
Corresponds to variant rs28936071 [ dbSNP | Ensembl ].
VAR_023145
Natural variant1721T → M.
Corresponds to variant rs7889678 [ dbSNP | Ensembl ].
VAR_059256
Natural variant1821S → R in CFNS. Ref.13
VAR_023146
Natural variant1891V → A.
Corresponds to variant rs16989105 [ dbSNP | Ensembl ].
VAR_023147

Sequences

Sequence LengthMass (Da)Tools
P98172 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 473DD2F1A5BF89DE

FASTA34638,007
        10         20         30         40         50         60 
MARPGQRWLG KWLVAMVVWA LCRLATPLAK NLEPVSWSSL NPKFLSGKGL VIYPKIGDKL 

        70         80         90        100        110        120 
DIICPRAEAG RPYEYYKLYL VRPEQAAACS TVLDPNVLVT CNRPEQEIRF TIKFQEFSPN 

       130        140        150        160        170        180 
YMGLEFKKHH DYYITSTSNG SLEGLENREG GVCRTRTMKI IMKVGQDPNA VTPEQLTTSR 

       190        200        210        220        230        240 
PSKEADNTVK MATQAPGSRG SLGDSDGKHE TVNQEEKSGP GASGGSSGDP DGFFNSKVAL 

       250        260        270        280        290        300 
FAAVGAGCVI FLLIIIFLTV LLLKLRKRHR KHTQQRAAAL SLSTLASPKG GSGTAGTEPS 

       310        320        330        340 
DIIIPLRTTE NNYCPHYEKV SGDYGHPVYI VQEMPPQSPA NIYYKV 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors."
Beckmann M.P., Cerretti D.P., Baum P., Vanden Bos T., James L., Farrah T., Kozlosky C., Hollingsworth T., Shilling H., Maraskovsky E., Fletcher F.A., Lhotak V., Pawson T., Lyman S.D.
EMBO J. 13:3757-3762(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity."
Davis S., Gale N.W., Aldrich T.H., Maisonpierre P.C., Lhotak V., Pawson T., Goldfarb M., Yancopoulos G.D.
Science 266:816-819(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Assignment of the human Elk ligand gene, EPLG2, to chromosome region Xq12."
Fletcher F.A., Huebner K., Shaffer L.G., Monaco A., Mueller U., Kozlosky C., Druck T., Simoneaux D.K., Fairweather N., Chelly J., Cerretti D.P., Belmont J.W., Beckmann M.P., Lyman S.D.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye and Skin.
[7]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-42.
[8]"EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains."
Brueckner K., Pablo Labrador J., Scheiffele P., Herb A., Seeburg P.H., Klein R.
Neuron 22:511-524(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRIP1 AND GRIP2.
Tissue: Fetal brain.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Mutations of the ephrin-B1 gene cause craniofrontonasal syndrome."
Wieland I., Jakubiczka S., Muschke P., Cohen M., Thiele H., Gerlach K.L., Adams R.H., Wieacker P.
Am. J. Hum. Genet. 74:1209-1215(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CFNS LEU-54 AND ILE-111.
[12]"Mutations of ephrin-B1 (EFNB1), a marker of tissue boundary formation, cause craniofrontonasal syndrome."
Twigg S.R.F., Kan R., Babbs C., Bochukova E.G., Robertson S.P., Wall S.A., Morriss-Kay G.M., Wilkie A.O.M.
Proc. Natl. Acad. Sci. U.S.A. 101:8652-8657(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CFNS THR-62; SER-98; PRO-115; HIS-119; THR-119; SER-151; VAL-151; PRO-155; ILE-158 AND VAL-158, VARIANT HIS-154.
[13]"Twenty-six novel EFNB1 mutations in familial and sporadic craniofrontonasal syndrome (CFNS)."
Wieland I., Reardon W., Jakubiczka S., Franco B., Kress W., Vincent-Delorme C., Thierry P., Edwards M., Koenig R., Rusu C., Schweiger S., Thompson E., Tinschert S., Stewart F., Wieacker P.
Hum. Mutat. 26:113-118(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CFNS ARG-27; LEU-54; SER-119; HIS-119; ALA-137; PHE-138; SER-151; SER-153; TYR-153 AND ARG-182.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14391.1.
PIRS46993.
RefSeqNP_004420.1. NM_004429.4.
UniGeneHs.144700.

3D structure databases

ProteinModelPortalP98172.
SMRP98172. Positions 32-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108267. 13 interactions.
IntActP98172. 10 interactions.
STRING9606.ENSP00000204961.

PTM databases

PhosphoSiteP98172.

Polymorphism databases

DMDM1706668.

Proteomic databases

MaxQBP98172.
PaxDbP98172.
PeptideAtlasP98172.
PRIDEP98172.

Protocols and materials databases

DNASU1947.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000204961; ENSP00000204961; ENSG00000090776.
GeneID1947.
KEGGhsa:1947.
UCSCuc004dxd.4. human.

Organism-specific databases

CTD1947.
GeneCardsGC0XP068048.
HGNCHGNC:3226. EFNB1.
HPACAB031489.
MIM300035. gene.
304110. phenotype.
neXtProtNX_P98172.
Orphanet1520. Craniofrontonasal dysplasia.
PharmGKBPA27661.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262190.
HOGENOMHOG000220931.
HOVERGENHBG051448.
InParanoidP98172.
KOK05463.
OMAPDSFFNS.
OrthoDBEOG7288S5.
PhylomeDBP98172.

Enzyme and pathway databases

SignaLinkP98172.

Gene expression databases

BgeeP98172.
CleanExHS_EFNB1.
GenevestigatorP98172.

Family and domain databases

Gene3D2.60.40.420. 1 hit.
InterProIPR008972. Cupredoxin.
IPR001799. Ephrin.
IPR019765. Ephrin_CS.
[Graphical view]
PANTHERPTHR11304. PTHR11304. 1 hit.
PfamPF00812. Ephrin. 1 hit.
[Graphical view]
PRINTSPR01347. EPHRIN.
ProDomPD002533. Ephrin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF49503. SSF49503. 1 hit.
PROSITEPS01299. EPHRIN_RBD_1. 1 hit.
PS51551. EPHRIN_RBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEFNB1. human.
GeneWikiEFNB1.
GenomeRNAi1947.
NextBio7891.
PMAP-CutDBP98172.
PROP98172.
SOURCESearch...

Entry information

Entry nameEFNB1_HUMAN
AccessionPrimary (citable) accession number: P98172
Secondary accession number(s): D3DVU0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM