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O15197

- EPHB6_HUMAN

UniProt

O15197 - EPHB6_HUMAN

Protein

Ephrin type-B receptor 6

Gene

EPHB6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 4 (20 Apr 2010)
      Previous versions | rss
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    Functioni

    Kinase-defective receptor for members of the ephrin-B family. Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion and migration by exerting both positive and negative effects upon stimulation with ephrin-B2. Inhibits JNK activation, T-cell receptor-induced IL-2 secretion and CD25 expression upon stimulation with ephrin-B2.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi676 – 6849ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ephrin receptor activity Source: ProtInc
    3. receptor activity Source: ProtInc

    GO - Biological processi

    1. calcium ion homeostasis Source: Ensembl
    2. parathyroid hormone secretion Source: Ensembl

    Keywords - Molecular functioni

    Receptor

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin type-B receptor 6
    Alternative name(s):
    HEP
    Tyrosine-protein kinase-defective receptor EPH-6
    Gene namesi
    Name:EPHB6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:3396. EPHB6.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. integral component of plasma membrane Source: InterPro

    Keywords - Cellular componenti

    Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27828.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 31311 PublicationAdd
    BLAST
    Chaini32 – 1021990Ephrin type-B receptor 6PRO_0000016837Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi480 – 4801N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Ligand-binding increases phosphorylation on tyrosine residues. Phosphorylation on tyrosine residues is mediated by transphosphorylation by the catalytically active EPHB1 in a ligand-independent manner. Tyrosine phosphorylation of the receptor may act as a switch on the functional transition from cell adhesion/attraction to de-adhesion/repulsion.2 Publications

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiO15197.
    PRIDEiO15197.

    PTM databases

    PhosphoSiteiO15197.

    Expressioni

    Tissue specificityi

    Expressed in brain. Expressed in non invasive breast carcinoma cell lines (at protein level). Strong expression in brain and pancreas, and weak expression in other tissues, such as heart, placenta, lung, liver, skeletal muscle and kidney. Expressed in breast non invasive tumors but not in metastatic lesions. Isoform 3 is expressed in cell lines of glioblastomas, anaplastic astrocytomas, gliosarcomas and astrocytomas. Isoform 3 is not detected in normal tissues.3 Publications

    Gene expression databases

    ArrayExpressiO15197.
    BgeeiO15197.
    CleanExiHS_EPHB6.
    GenevestigatoriO15197.

    Organism-specific databases

    HPAiHPA001351.

    Interactioni

    Subunit structurei

    Interacts with CBL and EPHB1. Interacts with FYN; this interaction takes place in a ligand-independent manner.2 Publications

    Protein-protein interaction databases

    BioGridi108365. 5 interactions.
    IntActiO15197. 7 interactions.
    MINTiMINT-1392963.
    STRINGi9606.ENSP00000376684.

    Structurei

    3D structure databases

    ProteinModelPortaliO15197.
    SMRiO15197. Positions 31-587, 621-926, 956-1007.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 594563ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini616 – 1021406CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei595 – 61521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 237205Eph LBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini369 – 486118Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini487 – 58296Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini670 – 919250Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini948 – 101265SAMPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1019 – 10213PDZ-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi166 – 17611Poly-SerAdd
    BLAST
    Compositional biasi219 – 366148Cys-richAdd
    BLAST
    Compositional biasi881 – 8844Poly-Pro

    Domaini

    The protein kinase domain is predicted to be catalytically inactive. Its extracellular domain is capable of promoting cell adhesion and migration in response to low concentrations of ephrin-B2, but its cytoplasmic domain is essential for cell repulsion and inhibition of migration induced by high concentrations of ephrin-B2.

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation
    Contains 1 Eph LBD (Eph ligand-binding) domain.PROSITE-ProRule annotation
    Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233856.
    HOVERGENiHBG062180.
    InParanoidiO15197.
    KOiK05114.
    OMAiEQAVAIQ.
    OrthoDBiEOG7VTDM6.
    PhylomeDBiO15197.
    TreeFamiTF314013.

    Family and domain databases

    Gene3Di1.10.150.50. 1 hit.
    2.60.120.260. 1 hit.
    2.60.40.10. 2 hits.
    InterProiIPR027936. Eph_TM.
    IPR001090. Ephrin_rcpt_lig-bd_dom.
    IPR003961. Fibronectin_type3.
    IPR008979. Galactose-bd-like.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR013783. Ig-like_fold.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
    IPR016257. Tyr_kinase_ephrin_rcpt.
    IPR001426. Tyr_kinase_rcpt_V_CS.
    [Graphical view]
    PfamiPF14575. EphA2_TM. 1 hit.
    PF01404. Ephrin_lbd. 1 hit.
    PF00041. fn3. 2 hits.
    PF07699. GCC2_GCC3. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF07647. SAM_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00615. EPH_lbd. 1 hit.
    SM00060. FN3. 2 hits.
    SM00454. SAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    SSF49265. SSF49265. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEiPS51550. EPH_LBD. 1 hit.
    PS50853. FN3. 2 hits.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
    PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
    PS50105. SAM_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O15197-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MATEGAAQLG NRVAGMVCSL WVLLLVSSVL ALEEVLLDTT GETSEIGWLT     50
    YPPGGWDEVS VLDDQRRLTR TFEACHVAGA PPGTGQDNWL QTHFVERRGA 100
    QRAHIRLHFS VRACSSLGVS GGTCRETFTL YYRQAEEPDS PDSVSSWHLK 150
    RWTKVDTIAA DESFPSSSSS SSSSSSAAWA VGPHGAGQRA GLQLNVKERS 200
    FGPLTQRGFY VAFQDTGACL ALVAVRLFSY TCPAVLRSFA SFPETQASGA 250
    GGASLVAAVG TCVAHAEPEE DGVGGQAGGS PPRLHCNGEG KWMVAVGGCR 300
    CQPGYQPARG DKACQACPRG LYKSSAGNAP CSPCPARSHA PNPAAPVCPC 350
    LEGFYRASSD PPEAPCTGPP SAPQELWFEV QGSALMLHWR LPRELGGRGD 400
    LLFNVVCKEC EGRQEPASGG GGTCHRCRDE VHFDPRQRGL TESRVLVGGL 450
    RAHVPYILEV QAVNGVSELS PDPPQAAAIN VSTSHEVPSA VPVVHQVSRA 500
    SNSITVSWPQ PDQTNGNILD YQLRYYDQAE DESHSFTLTS ETNTATVTQL 550
    SPGHIYGFQV RARTAAGHGP YGGKVYFQTL PQGELSSQLP ERLSLVIGSI 600
    LGALAFLLLA AITVLAVVFQ RKRRGTGYTE QLQQYSSPGL GVKYYIDPST 650
    YEDPCQAIRE LAREVDPAYI KIEEVIGTGS FGEVRQGRLQ PRGRREQTVA 700
    IQALWAGGAE SLQMTFLGRA AVLGQFQHPN ILRLEGVVTK SRPLMVLTEF 750
    MELGPLDSFL RQREGQFSSL QLVAMQRGVA AAMQYLSSFA FVHRSLSAHS 800
    VLVNSHLVCK VARLGHSPQG PSCLLRWAAP EVIAHGKHTT SSDVWSFGIL 850
    MWEVMSYGER PYWDMSEQEV LNAIEQEFRL PPPPGCPPGL HLLMLDTWQK 900
    DRARRPHFDQ LVAAFDKMIR KPDTLQAGGD PGERPSQALL TPVALDFPCL 950
    DSPQAWLSAI GLECYQDNFS KFGLCTFSDV AQLSLEDLPA LGITLAGHQK 1000
    KLLHHIQLLQ QHLRQQGSVE V 1021
    Length:1,021
    Mass (Da):110,700
    Last modified:April 20, 2010 - v4
    Checksum:iBF1D4D9BE34358A5
    GO
    Isoform 2 (identifier: O15197-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         16-292: Missing.

    Show »
    Length:744
    Mass (Da):81,211
    Checksum:i8BCF105B3B7A5B92
    GO
    Isoform 3 (identifier: O15197-3) [UniParc]FASTAAdd to Basket

    Also known as: EphB6v

    The sequence of this isoform differs from the canonical sequence as follows:
         487-540: VPSAVPVVHQ...DESHSFTLTS → GELFSLAFRI...YPHNNFPFAL
         541-1021: Missing.

    Show »
    Length:540
    Mass (Da):57,498
    Checksum:i3635871D1070FF27
    GO

    Sequence cautioni

    The sequence AAD03058.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAI10608.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAP20939.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA21560.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence EAL23775.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence EAW51902.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti122 – 1221G → S.2 Publications
    Corresponds to variant rs8177173 [ dbSNP | Ensembl ].
    VAR_019139
    Natural varianti170 – 1701S → T.1 Publication
    VAR_042190
    Natural varianti221 – 2211A → V.1 Publication
    VAR_042191
    Natural varianti282 – 2821P → H.1 Publication
    VAR_042192
    Natural varianti282 – 2821P → R.1 Publication
    Corresponds to variant rs8177143 [ dbSNP | Ensembl ].
    VAR_019140
    Natural varianti309 – 3091R → Q.1 Publication
    Corresponds to variant rs55728646 [ dbSNP | Ensembl ].
    VAR_042193
    Natural varianti324 – 3241S → A.2 Publications
    Corresponds to variant rs8177146 [ dbSNP | Ensembl ].
    VAR_019141
    Natural varianti332 – 3321S → L.1 Publication
    Corresponds to variant rs35189999 [ dbSNP | Ensembl ].
    VAR_042194
    Natural varianti360 – 3601D → N in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036091
    Natural varianti499 – 4991R → Q.1 Publication
    Corresponds to variant rs8177175 [ dbSNP | Ensembl ].
    VAR_019142
    Natural varianti603 – 6031A → P in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036092
    Natural varianti662 – 6621A → V.1 Publication
    Corresponds to variant rs35984674 [ dbSNP | Ensembl ].
    VAR_042195
    Natural varianti719 – 7191R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036093
    Natural varianti743 – 7431P → S in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
    VAR_042196
    Natural varianti813 – 8131R → H.1 Publication
    VAR_042197
    Natural varianti875 – 8751E → K in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_042198
    Natural varianti930 – 9301D → G in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036094
    Natural varianti993 – 9931I → V.1 Publication
    VAR_042199

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei16 – 292277Missing in isoform 2. 1 PublicationVSP_037496Add
    BLAST
    Alternative sequencei487 – 54054VPSAV…FTLTS → GELFSLAFRIPCLRSFEPPS LLLISSLVHPCRPPLKADPA PRDSYPHNNFPFAL in isoform 3. 1 PublicationVSP_037497Add
    BLAST
    Alternative sequencei541 – 1021481Missing in isoform 3. 1 PublicationVSP_037498Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D83492 mRNA. Translation: BAA21560.1. Different initiation.
    AY280502 Genomic DNA. Translation: AAP20939.1. Different initiation.
    AF107256 Genomic DNA. Translation: AAD03058.1. Different initiation.
    AC104597 Genomic DNA. No translation available.
    CH236959 Genomic DNA. Translation: EAL23775.1. Sequence problems.
    CH471198 Genomic DNA. Translation: EAW51900.1.
    CH471198 Genomic DNA. Translation: EAW51901.1.
    CH471198 Genomic DNA. Translation: EAW51902.1. Sequence problems.
    CH471198 Genomic DNA. Translation: EAW51903.1.
    BC051028 mRNA. No translation available.
    BC110606 mRNA. Translation: AAI10607.1.
    BC110607 mRNA. Translation: AAI10608.2. Different initiation.
    EU054308 mRNA. Translation: ABV55388.1.
    PIRiJC5526.
    RefSeqiNP_001267724.2. NM_001280795.2.
    NP_004436.4. NM_004445.5.
    UniGeneiHs.380089.

    Genome annotation databases

    EnsembliENST00000392957; ENSP00000376684; ENSG00000106123. [O15197-1]
    ENST00000442129; ENSP00000410789; ENSG00000106123. [O15197-1]
    GeneIDi2051.
    KEGGihsa:2051.
    UCSCiuc003wbs.3. human. [O15197-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D83492 mRNA. Translation: BAA21560.1 . Different initiation.
    AY280502 Genomic DNA. Translation: AAP20939.1 . Different initiation.
    AF107256 Genomic DNA. Translation: AAD03058.1 . Different initiation.
    AC104597 Genomic DNA. No translation available.
    CH236959 Genomic DNA. Translation: EAL23775.1 . Sequence problems.
    CH471198 Genomic DNA. Translation: EAW51900.1 .
    CH471198 Genomic DNA. Translation: EAW51901.1 .
    CH471198 Genomic DNA. Translation: EAW51902.1 . Sequence problems.
    CH471198 Genomic DNA. Translation: EAW51903.1 .
    BC051028 mRNA. No translation available.
    BC110606 mRNA. Translation: AAI10607.1 .
    BC110607 mRNA. Translation: AAI10608.2 . Different initiation.
    EU054308 mRNA. Translation: ABV55388.1 .
    PIRi JC5526.
    RefSeqi NP_001267724.2. NM_001280795.2.
    NP_004436.4. NM_004445.5.
    UniGenei Hs.380089.

    3D structure databases

    ProteinModelPortali O15197.
    SMRi O15197. Positions 31-587, 621-926, 956-1007.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108365. 5 interactions.
    IntActi O15197. 7 interactions.
    MINTi MINT-1392963.
    STRINGi 9606.ENSP00000376684.

    Chemistry

    BindingDBi O15197.
    ChEMBLi CHEMBL5836.
    GuidetoPHARMACOLOGYi 1834.

    PTM databases

    PhosphoSitei O15197.

    Proteomic databases

    PaxDbi O15197.
    PRIDEi O15197.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000392957 ; ENSP00000376684 ; ENSG00000106123 . [O15197-1 ]
    ENST00000442129 ; ENSP00000410789 ; ENSG00000106123 . [O15197-1 ]
    GeneIDi 2051.
    KEGGi hsa:2051.
    UCSCi uc003wbs.3. human. [O15197-1 ]

    Organism-specific databases

    CTDi 2051.
    GeneCardsi GC07P142552.
    HGNCi HGNC:3396. EPHB6.
    HPAi HPA001351.
    MIMi 602757. gene.
    neXtProti NX_O15197.
    PharmGKBi PA27828.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233856.
    HOVERGENi HBG062180.
    InParanoidi O15197.
    KOi K05114.
    OMAi EQAVAIQ.
    OrthoDBi EOG7VTDM6.
    PhylomeDBi O15197.
    TreeFami TF314013.

    Miscellaneous databases

    ChiTaRSi EPHB6. human.
    GeneWikii EPHB6.
    GenomeRNAii 2051.
    NextBioi 8339.
    PROi O15197.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15197.
    Bgeei O15197.
    CleanExi HS_EPHB6.
    Genevestigatori O15197.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    2.60.120.260. 1 hit.
    2.60.40.10. 2 hits.
    InterProi IPR027936. Eph_TM.
    IPR001090. Ephrin_rcpt_lig-bd_dom.
    IPR003961. Fibronectin_type3.
    IPR008979. Galactose-bd-like.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR013783. Ig-like_fold.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
    IPR016257. Tyr_kinase_ephrin_rcpt.
    IPR001426. Tyr_kinase_rcpt_V_CS.
    [Graphical view ]
    Pfami PF14575. EphA2_TM. 1 hit.
    PF01404. Ephrin_lbd. 1 hit.
    PF00041. fn3. 2 hits.
    PF07699. GCC2_GCC3. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF07647. SAM_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00615. EPH_lbd. 1 hit.
    SM00060. FN3. 2 hits.
    SM00454. SAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    SSF49265. SSF49265. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEi PS51550. EPH_LBD. 1 hit.
    PS50853. FN3. 2 hits.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
    PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
    PS50105. SAM_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression of a kinase-defective Eph-like receptor in the normal human brain."
      Matsuoka H., Iwata N., Ito M., Shimoyama M., Nagata A., Chihara K., Takai S., Matsui T.
      Biochem. Biophys. Res. Commun. 235:487-492(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    2. SeattleSNPs variation discovery resource
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-122; ARG-282; ALA-324 AND GLN-499.
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [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] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    7. "Identification of EphB6 variant-derived epitope peptides recognized by cytotoxic T-lymphocytes from HLA-A24+ malignant glioma patients."
      Jin M., Komohara Y., Shichijo S., Harada M., Yamanaka R., Miyamoto S., Nikawa J., Itoh K., Yamada A.
      Oncol. Rep. 19:1277-1283(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-1021 (ISOFORM 3).
    8. "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 32-46.
    9. "The kinase-null EphB6 receptor undergoes transphosphorylation in a complex with EphB1."
      Freywald A., Sharfe N., Roifman C.M.
      J. Biol. Chem. 277:3823-3828(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBL AND EPHB1, PHOSPHORYLATION.
    10. "The EphB6 receptor inhibits JNK activation in T lymphocytes and modulates T cell receptor-mediated responses."
      Freywald A., Sharfe N., Rashotte C., Grunberger T., Roifman C.M.
      J. Biol. Chem. 278:10150-10156(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Biphasic functions of the kinase-defective Ephb6 receptor in cell adhesion and migration."
      Matsuoka H., Obama H., Kelly M.L., Matsui T., Nakamoto M.
      J. Biol. Chem. 280:29355-29363(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FYN, PHOSPHORYLATION.
    12. "Erythropoietin-producing hepatocyte B6 variant-derived peptides with the ability to induce glioma-reactive cytotoxic T lymphocytes in human leukocyte antigen-A2+ glioma patients."
      Jin M., Komohara Y., Shichijo S., Yamanaka R., Nikawa J., Itoh K., Yamada A.
      Cancer Sci. 99:1656-1662(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    13. "EphB6 receptor significantly alters invasiveness and other phenotypic characteristics of human breast carcinoma cells."
      Fox B.P., Kandpal R.P.
      Oncogene 28:1706-1713(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    14. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASN-360; PRO-603; GLN-719 AND GLY-930.
    15. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-122; THR-170; VAL-221; HIS-282; GLN-309; ALA-324; LEU-332; VAL-662; SER-743; HIS-813; LYS-875 AND VAL-993.

    Entry informationi

    Entry nameiEPHB6_HUMAN
    AccessioniPrimary (citable) accession number: O15197
    Secondary accession number(s): A4D2I7
    , A8CDT5, D3DXD3, Q2TB23, Q2TB24
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: April 20, 2010
    Last modified: October 1, 2014
    This is version 158 of the entry and version 4 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 7
      Human chromosome 7: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3