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P98172

- EFNB1_HUMAN

UniProt

P98172 - EFNB1_HUMAN

Protein

Ephrin-B1

Gene

EFNB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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
    2. protein binding Source: UniProtKB

    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

    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

    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. 13 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.
    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

    MARPGQRWLG KWLVAMVVWA LCRLATPLAK NLEPVSWSSL NPKFLSGKGL    50
    VIYPKIGDKL DIICPRAEAG RPYEYYKLYL VRPEQAAACS TVLDPNVLVT 100
    CNRPEQEIRF TIKFQEFSPN YMGLEFKKHH DYYITSTSNG SLEGLENREG 150
    GVCRTRTMKI IMKVGQDPNA VTPEQLTTSR PSKEADNTVK MATQAPGSRG 200
    SLGDSDGKHE TVNQEEKSGP GASGGSSGDP DGFFNSKVAL FAAVGAGCVI 250
    FLLIIIFLTV LLLKLRKRHR KHTQQRAAAL SLSTLASPKG GSGTAGTEPS 300
    DIIIPLRTTE NNYCPHYEKV SGDYGHPVYI VQEMPPQSPA NIYYKV 346
    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. 13 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.
    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

    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 1, 2014
    This is version 147 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

    Dasty 3