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P29322

- EPHA8_HUMAN

UniProt

P29322 - EPHA8_HUMAN

Protein

Ephrin type-A receptor 8

Gene

EPHA8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 2 (18 Oct 2001)
      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 By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei667 – 6671ATPPROSITE-ProRule annotation
    Active sitei760 – 7601Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi641 – 6499ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. GPI-linked ephrin receptor activity 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. 2681.
    SignaLinkiP29322.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin type-A receptor 8 (EC:2.7.10.1)
    Alternative name(s):
    EPH- and ELK-related kinase
    EPH-like kinase 3
    Short name:
    EK3
    Short name:
    hEK3
    Tyrosine-protein kinase receptor EEK
    Gene namesi
    Name:EPHA8
    Synonyms:EEK, HEK3, KIAA1459
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3391. EPHA8.

    Subcellular locationi

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

    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

    Organism-specific databases

    PharmGKBiPA27823.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 1005978Ephrin type-A receptor 8PRO_0000016822Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi407 – 4071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi432 – 4321N-linked (GlcNAc...)Sequence Analysis
    Modified residuei616 – 6161Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei839 – 8391Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Phosphorylated. Phosphorylation is stimulated upon binding of its ligands including EFNA2, EFNA3 and EFNA5. Autophosphorylation on Tyr-616 is critical for association with FYN. Autophosphorylation on Tyr-839 modulates tyrosine kinase activity By similarity.By similarity
    Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation. ANKS1A prevents ubiquitination and degradation By similarity.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP29322.
    PRIDEiP29322.

    PTM databases

    PhosphoSiteiP29322.

    Expressioni

    Gene expression databases

    BgeeiP29322.
    CleanExiHS_EPHA8.
    GenevestigatoriP29322.

    Organism-specific databases

    HPAiCAB009660.
    HPA031433.

    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. May also form heterodimers with other ephrin receptors By similarity. 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 similarity4 Publications

    Protein-protein interaction databases

    BioGridi108360. 10 interactions.
    IntActiP29322. 7 interactions.
    STRINGi9606.ENSP00000166244.

    Structurei

    Secondary structure

    1
    1005
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi456 – 4605
    Beta strandi472 – 48211
    Beta strandi488 – 49912
    Beta strandi507 – 5104
    Beta strandi512 – 5165
    Beta strandi527 – 5304
    Helixi632 – 6343
    Beta strandi635 – 6439
    Turni644 – 6463
    Beta strandi647 – 6548
    Beta strandi662 – 6698
    Helixi675 – 68814
    Beta strandi699 – 7035
    Helixi705 – 7073
    Beta strandi710 – 7145
    Helixi721 – 7266
    Turni727 – 7304
    Helixi734 – 75320
    Helixi763 – 7653
    Beta strandi766 – 7683
    Beta strandi774 – 7763
    Helixi802 – 8043
    Helixi807 – 8126
    Helixi817 – 83216
    Turni833 – 8353
    Turni838 – 8414
    Helixi844 – 8529
    Helixi865 – 87410
    Helixi879 – 8813
    Helixi885 – 89713
    Helixi935 – 9417
    Helixi945 – 9473
    Helixi948 – 9536
    Helixi959 – 9624
    Helixi967 – 9737
    Helixi978 – 99518

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UCVNMR-A933-1000[»]
    1X5LNMR-A437-534[»]
    3KULX-ray2.15A/B602-909[»]
    ProteinModelPortaliP29322.
    SMRiP29322. Positions 31-534, 570-901, 926-1000.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29322.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini28 – 542515ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini564 – 1005442CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei543 – 56321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 209179Eph LBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini328 – 438111Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini439 – 53496Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini635 – 896262Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini930 – 99465SAMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni564 – 5707Mediates interaction with ANKS1A and ANKS1BBy similarity
    Regioni589 – 64456Mediates interaction with PIK3CG and required for endocytosisBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1003 – 10053PDZ-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi191 – 325135Cys-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.
    HOGENOMiHOG000233856.
    HOVERGENiHBG062180.
    InParanoidiP29322.
    KOiK05109.
    OMAiVTTRATV.
    OrthoDBiEOG7VTDM6.
    PhylomeDBiP29322.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P29322-1) [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

    MAPARGRLPP ALWVVTAAAA AATCVSAARG EVNLLDTSTI HGDWGWLTYP     50
    AHGWDSINEV DESFQPIHTY QVCNVMSPNQ NNWLRTSWVP RDGARRVYAE 100
    IKFTLRDCNS MPGVLGTCKE TFNLYYLESD RDLGASTQES QFLKIDTIAA 150
    DESFTGADLG VRRLKLNTEV RSVGPLSKRG FYLAFQDIGA CLAILSLRIY 200
    YKKCPAMVRN LAAFSEAVTG ADSSSLVEVR GQCVRHSEER DTPKMYCSAE 250
    GEWLVPIGKC VCSAGYEERR DACVACELGF YKSAPGDQLC ARCPPHSHSA 300
    APAAQACHCD LSYYRAALDP PSSACTRPPS APVNLISSVN GTSVTLEWAP 350
    PLDPGGRSDI TYNAVCRRCP WALSRCEACG SGTRFVPQQT SLVQASLLVA 400
    NLLAHMNYSF WIEAVNGVSD LSPEPRRAAV VNITTNQAAP SQVVVIRQER 450
    AGQTSVSLLW QEPEQPNGII LEYEIKYYEK DKEMQSYSTL KAVTTRATVS 500
    GLKPGTRYVF QVRARTSAGC GRFSQAMEVE TGKPRPRYDT RTIVWICLTL 550
    ITGLVVLLLL LICKKRHCGY SKAFQDSDEE KMHYQNGQAP PPVFLPLHHP 600
    PGKLPEPQFY AEPHTYEEPG RAGRSFTREI EASRIHIEKI IGSGDSGEVC 650
    YGRLRVPGQR DVPVAIKALK AGYTERQRRD FLSEASIMGQ FDHPNIIRLE 700
    GVVTRGRLAM IVTEYMENGS LDTFLRTHDG QFTIMQLVGM LRGVGAGMRY 750
    LSDLGYVHRD LAARNVLVDS NLVCKVSDFG LSRVLEDDPD AAYTTTGGKI 800
    PIRWTAPEAI AFRTFSSASD VWSFGVVMWE VLAYGERPYW NMTNRDVISS 850
    VEEGYRLPAP MGCPHALHQL MLDCWHKDRA QRPRFSQIVS VLDALIRSPE 900
    SLRATATVSR CPPPAFVRSC FDLRGGSGGG GGLTVGDWLD SIRMGRYRDH 950
    FAAGGYSSLG MVLRMNAQDV RALGITLMGH QKKILGSIQT MRAQLTSTQG 1000
    PRRHL 1005
    Length:1,005
    Mass (Da):111,003
    Last modified:October 18, 2001 - v2
    Checksum:i6FBF85535E4212B3
    GO
    Isoform 2 (identifier: P29322-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         439-495: APSQVVVIRQ...SYSTLKAVTT → GRRRNSVPQR...DPELEALHCL
         496-1005: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:495
    Mass (Da):53,900
    Checksum:i6CD3AD67ACBCBCB8
    GO

    Sequence cautioni

    The sequence CAA41980.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti237 – 2371S → L in BAA95983. (PubMed:10819331)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451G → S.1 Publication
    Corresponds to variant rs45498698 [ dbSNP | Ensembl ].
    VAR_042153
    Natural varianti60 – 601V → L.1 Publication
    Corresponds to variant rs56402644 [ dbSNP | Ensembl ].
    VAR_042154
    Natural varianti123 – 1231N → K in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
    VAR_042155
    Natural varianti179 – 1791R → C in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042156
    Natural varianti198 – 1981R → L in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042157
    Natural varianti321 – 3211P → L.
    Corresponds to variant rs56656925 [ dbSNP | Ensembl ].
    VAR_061292
    Natural varianti444 – 4441V → M.
    Corresponds to variant rs2295021 [ dbSNP | Ensembl ].
    VAR_022107
    Natural varianti612 – 6121E → Q.1 Publication
    Corresponds to variant rs999765 [ dbSNP | Ensembl ].
    VAR_024514
    Natural varianti860 – 8601P → L in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_042158

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei439 – 49557APSQV…KAVTT → GRRRNSVPQRPGPPASPASD PSRDQSSAGDVLWAFRQVPL WPCAPHQDPELEALHCL in isoform 2. 1 PublicationVSP_041946Add
    BLAST
    Alternative sequencei496 – 1005510Missing in isoform 2. 1 PublicationVSP_041947Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL035703 Genomic DNA. Translation: CAB81612.1.
    AL035703 Genomic DNA. Translation: CAI22039.1.
    BC038796 mRNA. Translation: AAH38796.1.
    BC072417 mRNA. Translation: AAH72417.2.
    AB040892 mRNA. Translation: BAA95983.1.
    X59291 Genomic DNA. Translation: CAA41980.1. Different initiation.
    CCDSiCCDS225.1. [P29322-1]
    CCDS30626.1. [P29322-2]
    PIRiS23361.
    RefSeqiNP_001006944.1. NM_001006943.1. [P29322-2]
    NP_065387.1. NM_020526.3. [P29322-1]
    UniGeneiHs.283613.

    Genome annotation databases

    EnsembliENST00000166244; ENSP00000166244; ENSG00000070886. [P29322-1]
    ENST00000374644; ENSP00000363775; ENSG00000070886. [P29322-2]
    ENST00000538803; ENSP00000440274; ENSG00000070886. [P29322-2]
    GeneIDi2046.
    KEGGihsa:2046.
    UCSCiuc001bfw.3. human. [P29322-2]
    uc001bfx.1. human. [P29322-1]

    Polymorphism databases

    DMDMi19857975.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL035703 Genomic DNA. Translation: CAB81612.1 .
    AL035703 Genomic DNA. Translation: CAI22039.1 .
    BC038796 mRNA. Translation: AAH38796.1 .
    BC072417 mRNA. Translation: AAH72417.2 .
    AB040892 mRNA. Translation: BAA95983.1 .
    X59291 Genomic DNA. Translation: CAA41980.1 . Different initiation.
    CCDSi CCDS225.1. [P29322-1 ]
    CCDS30626.1. [P29322-2 ]
    PIRi S23361.
    RefSeqi NP_001006944.1. NM_001006943.1. [P29322-2 ]
    NP_065387.1. NM_020526.3. [P29322-1 ]
    UniGenei Hs.283613.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UCV NMR - A 933-1000 [» ]
    1X5L NMR - A 437-534 [» ]
    3KUL X-ray 2.15 A/B 602-909 [» ]
    ProteinModelPortali P29322.
    SMRi P29322. Positions 31-534, 570-901, 926-1000.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108360. 10 interactions.
    IntActi P29322. 7 interactions.
    STRINGi 9606.ENSP00000166244.

    Chemistry

    BindingDBi P29322.
    ChEMBLi CHEMBL4134.
    GuidetoPHARMACOLOGYi 1828.

    PTM databases

    PhosphoSitei P29322.

    Polymorphism databases

    DMDMi 19857975.

    Proteomic databases

    PaxDbi P29322.
    PRIDEi P29322.

    Protocols and materials databases

    DNASUi 2046.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000166244 ; ENSP00000166244 ; ENSG00000070886 . [P29322-1 ]
    ENST00000374644 ; ENSP00000363775 ; ENSG00000070886 . [P29322-2 ]
    ENST00000538803 ; ENSP00000440274 ; ENSG00000070886 . [P29322-2 ]
    GeneIDi 2046.
    KEGGi hsa:2046.
    UCSCi uc001bfw.3. human. [P29322-2 ]
    uc001bfx.1. human. [P29322-1 ]

    Organism-specific databases

    CTDi 2046.
    GeneCardsi GC01P022890.
    HGNCi HGNC:3391. EPHA8.
    HPAi CAB009660.
    HPA031433.
    MIMi 176945. gene.
    neXtProti NX_P29322.
    PharmGKBi PA27823.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233856.
    HOVERGENi HBG062180.
    InParanoidi P29322.
    KOi K05109.
    OMAi VTTRATV.
    OrthoDBi EOG7VTDM6.
    PhylomeDBi P29322.
    TreeFami TF315608.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    SignaLinki P29322.

    Miscellaneous databases

    EvolutionaryTracei P29322.
    GeneWikii EPHA8.
    GenomeRNAii 2046.
    NextBioi 8315.
    PROi P29322.
    SOURCEi Search...

    Gene expression databases

    Bgeei P29322.
    CleanExi HS_EPHA8.
    Genevestigatori P29322.

    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 DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "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] (ISOFORM 2).
      Tissue: Brain and Eye.
    3. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 153-1005 (ISOFORM 1), VARIANT GLN-612.
      Tissue: Brain.
    4. "eek and erk, new members of the eph subclass of receptor protein-tyrosine kinases."
      Chan J., Watt V.M.
      Oncogene 6:1057-1061(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 706-726.
    5. "Unified nomenclature for Eph family receptors and their ligands, the ephrins."
      Eph nomenclature committee
      Cell 90:403-404(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE.
    6. "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: INTERACTION WITH FYN.
    7. "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: INTERACTION WITH PIK3CG.
    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: INTERACTION WITH ANKS1B.
    9. "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: INTERACTION WITH TIAM1.
    10. "Solution structure of the second FN3 domain and of sterile alpha motif (SAM) domain of EPH receptor A8 protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 437-534 AND 932-1000.
    11. "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-45; LEU-60; LYS-123; CYS-179; LEU-198 AND LEU-860.

    Entry informationi

    Entry nameiEPHA8_HUMAN
    AccessioniPrimary (citable) accession number: P29322
    Secondary accession number(s): Q6IN80
    , Q8IUX6, Q9NUA9, Q9P269
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: October 18, 2001
    Last modified: October 1, 2014
    This is version 162 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3