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P98172

- EFNB1_HUMAN

UniProt

P98172 - EFNB1_HUMAN

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Protein

Ephrin-B1

Gene

EFNB1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. ephrin receptor binding Source: RefGenome

GO - Biological processi

  1. axon guidance Source: RefGenome
  2. cell adhesion Source: ProtInc
  3. cell-cell signaling Source: ProtInc
  4. embryonic pattern specification Source: Ensembl
  5. ephrin receptor signaling pathway Source: RefGenome
  6. neural crest cell migration Source: Ensembl
  7. positive regulation of T cell proliferation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

SignaLinkiP98172.

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
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:3226. EFNB1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of plasma membrane Source: ProtInc
  4. membrane raft Source: Ensembl
  5. nucleus Source: Ensembl
  6. plasma membrane Source: RefGenome
  7. synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271P → R in CFNS. 1 Publication
VAR_023127
Natural varianti54 – 541P → L in CFNS. 2 Publications
VAR_023128
Natural varianti62 – 621I → T in CFNS. 1 Publication
VAR_023129
Natural varianti98 – 981L → S in CFNS. 1 Publication
VAR_023130
Natural varianti111 – 1111T → I in CFNS. 1 Publication
VAR_023131
Natural varianti115 – 1151Q → P in CFNS. 1 Publication
VAR_023132
Natural varianti119 – 1191P → H in CFNS. 2 Publications
VAR_023133
Natural varianti119 – 1191P → S in CFNS. 1 Publication
VAR_023134
Natural varianti119 – 1191P → T in CFNS. 1 Publication
VAR_023135
Natural varianti137 – 1371T → A in CFNS. 1 Publication
VAR_023136
Natural varianti138 – 1381S → F in CFNS. 1 Publication
VAR_023137
Natural varianti151 – 1511G → S in CFNS. 2 Publications
Corresponds to variant rs28936069 [ dbSNP | Ensembl ].
VAR_023138
Natural varianti151 – 1511G → V in CFNS. 1 Publication
Corresponds to variant rs28936070 [ dbSNP | Ensembl ].
VAR_023139
Natural varianti153 – 1531C → S in CFNS. 1 Publication
VAR_023140
Natural varianti153 – 1531C → Y in CFNS. 1 Publication
VAR_023141
Natural varianti155 – 1551T → P in CFNS. 1 Publication
VAR_023143
Natural varianti158 – 1581M → I in CFNS. 1 Publication
Corresponds to variant rs28935170 [ dbSNP | Ensembl ].
VAR_023144
Natural varianti158 – 1581M → V in CFNS. 1 Publication
Corresponds to variant rs28936071 [ dbSNP | Ensembl ].
VAR_023145
Natural varianti182 – 1821S → R in CFNS. 1 Publication
VAR_023146

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi304110. phenotype.
Orphaneti1520. Craniofrontonasal dysplasia.
PharmGKBiPA27661.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 346319Ephrin-B1PRO_0000008387Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi64 ↔ 101PROSITE-ProRule annotation
Disulfide bondi89 ↔ 153PROSITE-ProRule annotation
Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis
Modified residuei287 – 2871Phosphoserine2 Publications

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP98172.
PaxDbiP98172.
PeptideAtlasiP98172.
PRIDEiP98172.

PTM databases

PhosphoSiteiP98172.

Miscellaneous databases

PMAP-CutDBP98172.

Expressioni

Tissue specificityi

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

Inductioni

By TNF.

Gene expression databases

BgeeiP98172.
CleanExiHS_EFNB1.
GenevestigatoriP98172.

Organism-specific databases

HPAiCAB031489.

Interactioni

Subunit structurei

Interacts with GRIP1 and GRIP2.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi108267. 23 interactions.
IntActiP98172. 10 interactions.
STRINGi9606.ENSP00000204961.

Structurei

3D structure databases

ProteinModelPortaliP98172.
SMRiP98172. Positions 32-167.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 237210ExtracellularSequence AnalysisAdd
BLAST
Topological domaini259 – 34688CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei238 – 25821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 164135Ephrin RBDPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi344 – 3463PDZ-bindingSequence Analysis

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

eggNOGiNOG262190.
GeneTreeiENSGT00390000005839.
HOGENOMiHOG000220931.
HOVERGENiHBG051448.
InParanoidiP98172.
KOiK05463.
OMAiPDSFFNS.
OrthoDBiEOG7288S5.
PhylomeDBiP98172.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR001799. Ephrin.
IPR019765. Ephrin_CS.
[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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271P → R in CFNS. 1 Publication
VAR_023127
Natural varianti54 – 541P → L in CFNS. 2 Publications
VAR_023128
Natural varianti62 – 621I → T in CFNS. 1 Publication
VAR_023129
Natural varianti98 – 981L → S in CFNS. 1 Publication
VAR_023130
Natural varianti111 – 1111T → I in CFNS. 1 Publication
VAR_023131
Natural varianti115 – 1151Q → P in CFNS. 1 Publication
VAR_023132
Natural varianti119 – 1191P → H in CFNS. 2 Publications
VAR_023133
Natural varianti119 – 1191P → S in CFNS. 1 Publication
VAR_023134
Natural varianti119 – 1191P → T in CFNS. 1 Publication
VAR_023135
Natural varianti137 – 1371T → A in CFNS. 1 Publication
VAR_023136
Natural varianti138 – 1381S → F in CFNS. 1 Publication
VAR_023137
Natural varianti151 – 1511G → S in CFNS. 2 Publications
Corresponds to variant rs28936069 [ dbSNP | Ensembl ].
VAR_023138
Natural varianti151 – 1511G → V in CFNS. 1 Publication
Corresponds to variant rs28936070 [ dbSNP | Ensembl ].
VAR_023139
Natural varianti153 – 1531C → S in CFNS. 1 Publication
VAR_023140
Natural varianti153 – 1531C → Y in CFNS. 1 Publication
VAR_023141
Natural varianti154 – 1541R → H.1 Publication
VAR_023142
Natural varianti155 – 1551T → P in CFNS. 1 Publication
VAR_023143
Natural varianti158 – 1581M → I in CFNS. 1 Publication
Corresponds to variant rs28935170 [ dbSNP | Ensembl ].
VAR_023144
Natural varianti158 – 1581M → V in CFNS. 1 Publication
Corresponds to variant rs28936071 [ dbSNP | Ensembl ].
VAR_023145
Natural varianti172 – 1721T → M.
Corresponds to variant rs7889678 [ dbSNP | Ensembl ].
VAR_059256
Natural varianti182 – 1821S → R in CFNS. 1 Publication
VAR_023146
Natural varianti189 – 1891V → A.
Corresponds to variant rs16989105 [ dbSNP | Ensembl ].
VAR_023147

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.4. human.

Polymorphism databases

DMDMi1706668.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14391.1.
PIRi S46993.
RefSeqi NP_004420.1. NM_004429.4.
UniGenei Hs.144700.

3D structure databases

ProteinModelPortali P98172.
SMRi P98172. Positions 32-167.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108267. 23 interactions.
IntActi P98172. 10 interactions.
STRINGi 9606.ENSP00000204961.

PTM databases

PhosphoSitei P98172.

Polymorphism databases

DMDMi 1706668.

Proteomic databases

MaxQBi P98172.
PaxDbi P98172.
PeptideAtlasi P98172.
PRIDEi P98172.

Protocols and materials databases

DNASUi 1947.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000204961 ; ENSP00000204961 ; ENSG00000090776 .
GeneIDi 1947.
KEGGi hsa:1947.
UCSCi uc004dxd.4. human.

Organism-specific databases

CTDi 1947.
GeneCardsi GC0XP068048.
HGNCi HGNC:3226. EFNB1.
HPAi CAB031489.
MIMi 300035. gene.
304110. phenotype.
neXtProti NX_P98172.
Orphaneti 1520. Craniofrontonasal dysplasia.
PharmGKBi PA27661.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG262190.
GeneTreei ENSGT00390000005839.
HOGENOMi HOG000220931.
HOVERGENi HBG051448.
InParanoidi P98172.
KOi K05463.
OMAi PDSFFNS.
OrthoDBi EOG7288S5.
PhylomeDBi P98172.

Enzyme and pathway databases

SignaLinki P98172.

Miscellaneous databases

ChiTaRSi EFNB1. human.
GeneWikii EFNB1.
GenomeRNAii 1947.
NextBioi 7891.
PMAP-CutDB P98172.
PROi P98172.
SOURCEi Search...

Gene expression databases

Bgeei P98172.
CleanExi HS_EFNB1.
Genevestigatori P98172.

Family and domain databases

Gene3Di 2.60.40.420. 1 hit.
InterProi IPR008972. Cupredoxin.
IPR001799. Ephrin.
IPR019765. Ephrin_CS.
[Graphical view ]
PANTHERi PTHR11304. PTHR11304. 1 hit.
Pfami PF00812. Ephrin. 1 hit.
[Graphical view ]
PRINTSi PR01347. EPHRIN.
ProDomi PD002533. Ephrin. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF49503. SSF49503. 1 hit.
PROSITEi PS01299. EPHRIN_RBD_1. 1 hit.
PS51551. EPHRIN_RBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. 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.

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: October 29, 2014
This is version 148 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

External Data

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