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O09127

- EPHA8_MOUSE

UniProt

O09127 - EPHA8_MOUSE

Protein

Ephrin type-A receptor 8

Gene

Epha8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands 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. The GPI-anchored ephrin-A EFNA2, EFNA3, and EFNA5 are able to activate EPHA8 through phosphorylation. With EFNA5 may regulate integrin-mediated cell adhesion and migration on fibronectin substrate but also neurite outgrowth. During development of the nervous system plays also a role in axon guidance. Downstream effectors of the EPHA8 signaling pathway include FYN which promotes cell adhesion upon activation by EPHA8 and the MAP kinases in the stimulation of neurite outgrowth.6 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei666 – 6661ATPPROSITE-ProRule annotation
    Active sitei759 – 7591Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi640 – 6489ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. GPI-linked ephrin receptor activity Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: UniProtKB
    2. cell adhesion Source: UniProtKB-KW
    3. ephrin receptor signaling pathway Source: UniProtKB
    4. neuron projection development Source: UniProtKB
    5. neuron remodeling Source: UniProtKB
    6. positive regulation of MAPK cascade Source: UniProtKB
    7. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
    8. protein autophosphorylation Source: UniProtKB
    9. regulation of cell adhesion Source: UniProtKB
    10. regulation of cell adhesion mediated by integrin Source: UniProtKB
    11. substrate-dependent cell migration Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Cell adhesion, Neurogenesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin type-A receptor 8 (EC:2.7.10.1)
    Alternative name(s):
    EPH- and ELK-related kinase
    Tyrosine-protein kinase receptor EEK
    Gene namesi
    Name:Epha8
    Synonyms:Eek
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:109378. Epha8.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Cell projection. Early endosome membrane
    Note: Undergoes clathrin-mediated endocytosis upon EFNA5-binding and is targeted to early endosomes.

    GO - Cellular componenti

    1. early endosome membrane Source: UniProtKB-SubCell
    2. integral component of plasma membrane Source: UniProtKB
    3. neuron projection Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi615 – 6151Y → F: Reduced phosphorylation and reduced association with FYN. 2 Publications
    Mutagenesisi666 – 6661K → M or R: Kinase-dead. Loss of autophosphorylation but has no effect on regulation of cell adhesion. 1 Publication
    Mutagenesisi792 – 7921Y → F: Reduced phosphorylation. 1 Publication
    Mutagenesisi838 – 8381Y → F: Reduced tyrosine kinase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 1004978Ephrin type-A receptor 8PRO_0000016823Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi431 – 4311N-linked (GlcNAc...)Sequence Analysis
    Modified residuei615 – 6151Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei838 – 8381Phosphotyrosine; by autocatalysis2 Publications

    Post-translational modificationi

    Phosphorylated. Phosphorylation is stimulated upon binding of its ligands including EFNA2, EFNA3 and EFNA5. Autophosphorylation on Tyr-615 is critical for association with FYN. Autophosphorylation on Tyr-838 modulates tyrosine kinase activity.2 Publications
    Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation. ANKS1A prevents ubiquitination and degradation.1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiO09127.

    PTM databases

    PhosphoSiteiO09127.

    Expressioni

    Tissue specificityi

    Specifically expressed in the central nervous system.

    Developmental stagei

    First detected at E10.5 with high levels near the midline region of the tectum and to a lower extent in discrete regions of hindbrain, the dorsal horn, of the spinal cord and in the naso-lacrimal groove. The expression decreases at E12.5 and is barely detectable at E17.5. Not detected at postnatal stages.1 Publication

    Gene expression databases

    BgeeiO09127.
    CleanExiMM_EPHA8.
    GenevestigatoriO09127.

    Interactioni

    Subunit structurei

    Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses By similarity. May also form heterodimers with other ephrin receptors. Interacts with FYN; possible downstream effector of EPHA8 in regulation of cell adhesion. Interacts with PIK3CG; regulates integrin-mediated cell adhesion to substrate. Interacts with TIAM1; regulates clathrin-mediated endocytosis of EPHA8. Interacts with ANKS1A and ANKS1B; EPHA8 kinase activity-independent but stimulated by EPHA8 ubiquitination.By similarity6 Publications

    Protein-protein interaction databases

    IntActiO09127. 1 interaction.
    MINTiMINT-5312751.
    STRINGi10090.ENSMUSP00000030420.

    Structurei

    3D structure databases

    ProteinModelPortaliO09127.
    SMRiO09127. Positions 30-533, 595-900, 925-999.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 541515ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini563 – 1004442CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei542 – 56221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 208179Eph LBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini327 – 437111Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini438 – 53396Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini634 – 895262Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini929 – 99365SAMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni563 – 5697Mediates interaction with ANKS1A and ANKS1B
    Regioni588 – 64356Mediates interaction with PIK3CG and required for endocytosisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1002 – 10043PDZ-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi190 – 324135Cys-richAdd
    BLAST

    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.
    GeneTreeiENSGT00750000117255.
    HOGENOMiHOG000233856.
    HOVERGENiHBG062180.
    InParanoidiA3KG07.
    KOiK05109.
    OMAiVTTRATV.
    OrthoDBiEOG7VTDM6.
    TreeFamiTF315608.

    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.
    IPR020691. EphrinA_rcpt8.
    IPR003961. Fibronectin_type3.
    IPR008979. Galactose-bd-like.
    IPR013783. Ig-like_fold.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR021129. SAM_type1.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016257. Tyr_kinase_ephrin_rcpt.
    IPR001426. Tyr_kinase_rcpt_V_CS.
    [Graphical view]
    PANTHERiPTHR24416:SF274. PTHR24416:SF274. 1 hit.
    PfamiPF14575. EphA2_TM. 1 hit.
    PF01404. Ephrin_lbd. 1 hit.
    PF00041. fn3. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00536. SAM_1. 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.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    SSF49265. SSF49265. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS01186. EGF_2. 1 hit.
    PS51550. EPH_LBD. 1 hit.
    PS50853. FN3. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 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]

    Sequencei

    Sequence statusi: Complete.

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

    O09127-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPARARLSP ALWVVTAAAA ATCVSAGRGE VNLLDTSTIH GDWGWLTYPA     50
    HGWDSINEVD ESFRPIHTYQ VCNVMSPNQN NWLRTNWVPR DGARRVYAEI 100
    KFTLRDCNSI PGVLGTCKET FNLHYLESDR DLGASTQESQ FLKIDTIAAD 150
    ESFTGADLGV RRLKLNTEVR GVGPLSKRGF YLAFQDIGAC LAILSLRIYY 200
    KKCPAMVRNL AAFSEAVTGA DSSSLVEVRG QCVRHSEERD TPKMYCSAEG 250
    EWLVPIGKCV CSAGYEERRD ACMACELGFY KSAPGDQLCA RCPPHSHSAT 300
    PAAQTCRCDL SYYRAALDPP SAACTRPPSA PVNLISSVNG TSVTLEWAPP 350
    LDPGGRSDIT YNAVCRRCPW ALSHCEACGS GTRFVPQQTS LAQASLLVAN 400
    LLAHMNYSFW IEAVNGVSNL SPEPRSAAVV NITTNQAAPS QVVVIRQERA 450
    GQTSVSLLWQ EPEQPNGIIL EYEIKYYEKD KEMQSYSTLK AVTTRATVSG 500
    LKPGTRYVFQ VRARTSAGCG RFSQAMEVET GKPRPRYDTR TIVWICLTLI 550
    TGLVVLLLLL ICKKRHCGYS KAFQDSDEEK MHYQNGQAPP PVFLPLNHPP 600
    GKFPETQFSA EPHTYEEPGR AGRSFTREIE ASRIHIEKII GSGESGEVCY 650
    GRLQVPGQRD VPVAIKALKA GYTERQRQDF LSEAAIMGQF DHPNIIRLEG 700
    VVTRGRLAMI VTEYMENGSL DAFLRTHDGQ FTIVQLVGML RGVGAGMRYL 750
    SDLGYIHRDL AARNVLVDGR LVCKVSDFGL SRALEDDPEA AYTTAGGKIP 800
    IRWTAPEAIA FRTFSSASDV WSFGVVMWEV LAYGERPYWN MTNQDVISSV 850
    EEGYRLPAPM GCPRALHQLM LDCWHKDRAQ RPRFAHVVSV LDALVHSPES 900
    LRATATVSRC PPPAFARSCF DLRAGGSGNG DLTVGDWLDS IRMGRYRDHF 950
    AAGGYSSLGM VLRMNAQDVR ALGITLMGHQ KKILGSIQTM RAQLSSTQGP 1000
    RRHL 1004
    Length:1,004
    Mass (Da):110,705
    Last modified:July 27, 2011 - v2
    Checksum:i8530E8002A6FE502
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1000 – 10001P → R in AAB39218. (PubMed:9053851)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U72207 mRNA. Translation: AAB39218.1.
    AL627214 Genomic DNA. Translation: CAM46147.1.
    CCDSiCCDS18813.1.
    RefSeqiNP_031965.2. NM_007939.2.
    UniGeneiMm.1390.

    Genome annotation databases

    EnsembliENSMUST00000030420; ENSMUSP00000030420; ENSMUSG00000028661.
    GeneIDi13842.
    KEGGimmu:13842.
    UCSCiuc008vis.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U72207 mRNA. Translation: AAB39218.1 .
    AL627214 Genomic DNA. Translation: CAM46147.1 .
    CCDSi CCDS18813.1.
    RefSeqi NP_031965.2. NM_007939.2.
    UniGenei Mm.1390.

    3D structure databases

    ProteinModelPortali O09127.
    SMRi O09127. Positions 30-533, 595-900, 925-999.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O09127. 1 interaction.
    MINTi MINT-5312751.
    STRINGi 10090.ENSMUSP00000030420.

    PTM databases

    PhosphoSitei O09127.

    Proteomic databases

    PRIDEi O09127.

    Protocols and materials databases

    DNASUi 13842.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030420 ; ENSMUSP00000030420 ; ENSMUSG00000028661 .
    GeneIDi 13842.
    KEGGi mmu:13842.
    UCSCi uc008vis.1. mouse.

    Organism-specific databases

    CTDi 2046.
    MGIi MGI:109378. Epha8.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117255.
    HOGENOMi HOG000233856.
    HOVERGENi HBG062180.
    InParanoidi A3KG07.
    KOi K05109.
    OMAi VTTRATV.
    OrthoDBi EOG7VTDM6.
    TreeFami TF315608.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.

    Miscellaneous databases

    NextBioi 284680.
    PROi O09127.
    SOURCEi Search...

    Gene expression databases

    Bgeei O09127.
    CleanExi MM_EPHA8.
    Genevestigatori O09127.

    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.
    IPR020691. EphrinA_rcpt8.
    IPR003961. Fibronectin_type3.
    IPR008979. Galactose-bd-like.
    IPR013783. Ig-like_fold.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR021129. SAM_type1.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016257. Tyr_kinase_ephrin_rcpt.
    IPR001426. Tyr_kinase_rcpt_V_CS.
    [Graphical view ]
    PANTHERi PTHR24416:SF274. PTHR24416:SF274. 1 hit.
    Pfami PF14575. EphA2_TM. 1 hit.
    PF01404. Ephrin_lbd. 1 hit.
    PF00041. fn3. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00536. SAM_1. 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.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    SSF49265. SSF49265. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS01186. EGF_2. 1 hit.
    PS51550. EPH_LBD. 1 hit.
    PS50853. FN3. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 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. "The Eek receptor, a member of the Eph family of tyrosine protein kinases, can be activated by three different Eph family ligands."
      Park S., Sanchez M.P.
      Oncogene 14:533-542(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH EFNA2; EFNA3 AND EFNA5, PHOSPHORYLATION, TOPOLOGY, SUBCELLULAR LOCATION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Aberrant axonal projections in mice lacking EphA8 (Eek) tyrosine protein kinase receptors."
      Park S., Frisen J., Barbacid M.
      EMBO J. 16:3106-3114(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN AXON GUIDANCE, DEVELOPMENTAL STAGE.
    4. "Phosphorylation at Tyr-838 in the kinase domain of EphA8 modulates Fyn binding to the Tyr-615 site by enhancing tyrosine kinase activity."
      Choi S., Park S.
      Oncogene 18:5413-5422(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL ADHESION, INTERACTION WITH FYN, PHOSPHORYLATION AT TYR-615 AND TYR-838, MUTAGENESIS OF TYR-615 AND TYR-838.
    5. "The EphA8 receptor regulates integrin activity through p110gamma phosphatidylinositol-3 kinase in a tyrosine kinase activity-independent manner."
      Gu C., Park S.
      Mol. Cell. Biol. 21:4579-4597(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN INTEGRIN-MEDIATED CELL ADHESION, MUTAGENESIS OF TYR-615; LYS-666 AND TYR-792, INTERACTION WITH PIK3CG.
    6. "The p110 gamma PI-3 kinase is required for EphA8-stimulated cell migration."
      Gu C., Park S.
      FEBS Lett. 540:65-70(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL MIGRATION.
    7. "The EphA8 receptor induces sustained MAP kinase activation to promote neurite outgrowth in neuronal cells."
      Gu C., Shim S., Shin J., Kim J., Park J., Han K., Park S.
      Oncogene 24:4243-4256(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MAP KINASE ACTIVATION AND NEURITE OUTGROWTH, SUBCELLULAR LOCATION.
    8. "Identification of phosphotyrosine binding domain-containing proteins as novel downstream targets of the EphA8 signaling function."
      Shin J., Gu C., Park E., Park S.
      Mol. Cell. Biol. 27:8113-8126(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL MIGRATION AND NEURITE RETRACTION, INTERACTION WITH ANKS1A AND ANKS1B, SUBCELLULAR LOCATION.
    9. "The SAM domains of Anks family proteins are critically involved in modulating the degradation of EphA receptors."
      Kim J., Lee H., Kim Y., Yoo S., Park E., Park S.
      Mol. Cell. Biol. 30:1582-1592(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY CBL, INTERACTION WITH ANKS1A.
    10. "EphA8-ephrinA5 signaling and clathrin-mediated endocytosis is regulated by Tiam-1, a Rac-specific guanine nucleotide exchange factor."
      Yoo S., Shin J., Park S.
      Mol. Cells 29:603-609(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TIAM1.

    Entry informationi

    Entry nameiEPHA8_MOUSE
    AccessioniPrimary (citable) accession number: O09127
    Secondary accession number(s): A3KG07
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3