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Q15375

- EPHA7_HUMAN

UniProt

Q15375 - EPHA7_HUMAN

Protein

Ephrin type-A receptor 7

Gene

EPHA7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 3 (01 May 2007)
      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. Among GPI-anchored ephrin-A ligands, EFNA5 is a cognate/functional ligand for EPHA7 and their interaction regulates brain development modulating cell-cell adhesion and repulsion. Has a repellent activity on axons and is for instance involved in the guidance of corticothalamic axons and in the proper topographic mapping of retinal axons to the colliculus. May also regulate brain development through a caspase(CASP3)-dependent proapoptotic activity. Forward signaling may result in activation of components of the ERK signaling pathway including MAP2K1, MAP2K2, MAPK1 AND MAPK3 which are phosphorylated upon activation of EPHA7.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei665 – 6651ATPPROSITE-ProRule annotation
    Active sitei758 – 7581Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi639 – 6479ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. axon guidance receptor activity Source: UniProtKB
    3. chemorepellent activity Source: UniProtKB
    4. GPI-linked ephrin receptor activity Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. brain development Source: UniProtKB
    2. branching morphogenesis of a nerve Source: UniProtKB
    3. ephrin receptor signaling pathway Source: UniProtKB
    4. negative chemotaxis Source: UniProtKB
    5. peptidyl-tyrosine phosphorylation Source: GOC
    6. phosphorylation Source: UniProtKB
    7. positive regulation of neuron apoptotic process Source: UniProtKB
    8. regulation of cell-cell adhesion Source: UniProtKB
    9. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    10. regulation of ERK1 and ERK2 cascade Source: UniProtKB
    11. regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
    12. regulation of protein autophosphorylation Source: UniProtKB
    13. retinal ganglion cell axon guidance Source: Ensembl

    Keywords - Molecular functioni

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

    Keywords - Biological processi

    Apoptosis, Neurogenesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    SignaLinkiQ15375.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin type-A receptor 7 (EC:2.7.10.1)
    Alternative name(s):
    EPH homology kinase 3
    Short name:
    EHK-3
    EPH-like kinase 11
    Short name:
    EK11
    Short name:
    hEK11
    Gene namesi
    Name:EPHA7
    Synonyms:EHK3, HEK11
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:3390. EPHA7.

    Subcellular locationi

    GO - Cellular componenti

    1. dendrite Source: Ensembl
    2. integral component of plasma membrane Source: InterPro
    3. neuromuscular junction Source: Ensembl
    4. neuronal cell body Source: Ensembl
    5. postsynaptic membrane Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27822.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 998971Ephrin type-A receptor 7PRO_0000016818Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi343 – 3431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence Analysis
    Modified residuei608 – 6081Phosphotyrosine; by autocatalysisSequence Analysis
    Modified residuei614 – 6141Phosphotyrosine; by autocatalysisSequence Analysis
    Modified residuei791 – 7911Phosphotyrosine; by autocatalysisSequence Analysis
    Modified residuei940 – 9401Phosphotyrosine; by autocatalysisSequence Analysis

    Post-translational modificationi

    Phosphorylated.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ15375.
    PaxDbiQ15375.
    PRIDEiQ15375.

    PTM databases

    PhosphoSiteiQ15375.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    BgeeiQ15375.
    CleanExiHS_EPHA7.
    GenevestigatoriQ15375.

    Organism-specific databases

    HPAiCAB010496.

    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. Interacts (via PDZ-binding motif) with GRIP1 and PICK1 (via PDZ domain) By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Efna1P527932EBI-1383428,EBI-5241529From a different organism.
    EPHA2P293173EBI-1383428,EBI-702104

    Protein-protein interaction databases

    BioGridi108359. 8 interactions.
    IntActiQ15375. 9 interactions.
    MINTiMINT-1538326.
    STRINGi9606.ENSP00000358309.

    Structurei

    Secondary structure

    1
    998
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 375
    Beta strandi48 – 514
    Beta strandi54 – 618
    Beta strandi67 – 748
    Beta strandi78 – 803
    Beta strandi83 – 864
    Beta strandi96 – 10611
    Turni109 – 1113
    Beta strandi121 – 13212
    Helixi140 – 1423
    Beta strandi144 – 1507
    Beta strandi168 – 1747
    Beta strandi178 – 19013
    Beta strandi192 – 20211
    Helixi611 – 6133
    Beta strandi614 – 6163
    Helixi617 – 6248
    Helixi630 – 6323
    Beta strandi633 – 6419
    Beta strandi643 – 65210
    Beta strandi655 – 6573
    Beta strandi660 – 6667
    Helixi673 – 68614
    Beta strandi697 – 7015
    Beta strandi703 – 7053
    Beta strandi708 – 7125
    Helixi719 – 7257
    Turni726 – 7283
    Helixi732 – 75120
    Helixi761 – 7633
    Beta strandi764 – 7663
    Beta strandi772 – 7743
    Helixi800 – 8023
    Helixi805 – 8106
    Helixi815 – 83016
    Turni836 – 8394
    Helixi842 – 8509
    Helixi863 – 87210
    Helixi877 – 8793
    Helixi883 – 89513
    Helixi897 – 8993
    Helixi928 – 9347
    Helixi938 – 9403
    Helixi941 – 9466
    Helixi952 – 9565
    Helixi960 – 9656
    Helixi971 – 98818

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2REIX-ray1.60A590-899[»]
    3DKOX-ray2.00A590-899[»]
    3H8MX-ray2.10A/B919-990[»]
    3NRUX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L32-204[»]
    ProteinModelPortaliQ15375.
    SMRiQ15375. Positions 30-899, 919-989.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15375.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini28 – 555528ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini577 – 998422CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei556 – 57621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 210179Eph LBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini331 – 441111Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini442 – 53796Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini633 – 894262Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini923 – 98765SAMPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi996 – 9983PDZ-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi192 – 328137Cys-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.
    HOVERGENiHBG062180.
    InParanoidiQ15375.
    KOiK05108.
    OMAiENSPKMH.
    OrthoDBiEOG7VTDM6.
    PhylomeDBiQ15375.
    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.
    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.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    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.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    SSF49265. SSF49265. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 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 (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15375-1) [UniParc]FASTAAdd to Basket

    Also known as: EPHA7-FL

    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

    MVFQTRYPSW IILCYIWLLR FAHTGEAQAA KEVLLLDSKA QQTELEWISS    50
    PPNGWEEISG LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV 100
    ELKFTLRDCN SLPGVLGTCK ETFNLYYYET DYDTGRNIRE NLYVKIDTIA 150
    ADESFTQGDL GERKMKLNTE VREIGPLSKK GFYLAFQDVG ACIALVSVKV 200
    YYKKCWSIIE NLAIFPDTVT GSEFSSLVEV RGTCVSSAEE EAENAPRMHC 250
    SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RGFYKSSSQD LQCSRCPTHS 300
    FSDKEGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE 350
    WSPPADNGGR NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV 400
    TVMDLLAHAN YTFEVEAVNG VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM 450
    KERVLQRSVE LSWQEPEHPN GVITEYEIKY YEKDQRERTY STVKTKSTSA 500
    SINNLKPGTV YVFQIRAFTA AGYGNYSPRL DVATLEEATG KMFEATAVSS 550
    EQNPVIIIAV VAVAGTIILV FMVFGFIIGR RHCGYSKADQ EGDEELYFHF 600
    KFPGTKTYID PETYEDPNRA VHQFAKELDA SCIKIERVIG AGEFGEVCSG 650
    RLKLPGKRDV AVAIKTLKVG YTEKQRRDFL CEASIMGQFD HPNVVHLEGV 700
    VTRGKPVMIV IEFMENGALD AFLRKHDGQF TVIQLVGMLR GIAAGMRYLA 750
    DMGYVHRDLA ARNILVNSNL VCKVSDFGLS RVIEDDPEAV YTTTGGKIPV 800
    RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM SNQDVIKAIE 850
    EGYRLPAPMD CPAGLHQLML DCWQKERAER PKFEQIVGIL DKMIRNPNSL 900
    KTPLGTCSRP ISPLLDQNTP DFTTFCSVGE WLQAIKMERY KDNFTAAGYN 950
    SLESVARMTI EDVMSLGITL VGHQKKIMSS IQTMRAQMLH LHGTGIQV 998
    Length:998
    Mass (Da):112,097
    Last modified:May 1, 2007 - v3
    Checksum:i479B9CA0D2BB06EB
    GO
    Isoform 2 (identifier: Q15375-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         540-544: Missing.

    Note: May be due to a competing donor splice site.

    Show »
    Length:993
    Mass (Da):111,504
    Checksum:i4DEE43AD86F2CA11
    GO
    Isoform 3 (identifier: Q15375-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         278-279: PC → RK
         280-998: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:279
    Mass (Da):31,833
    Checksum:i54A2687994762500
    GO
    Isoform 4 (identifier: Q15375-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         600-604: FKFPG → C

    Note: No experimental confirmation available.

    Show »
    Length:994
    Mass (Da):111,623
    Checksum:iE35ED97999DBF944
    GO
    Isoform 5 (identifier: Q15375-5) [UniParc]FASTAAdd to Basket

    Also known as: EPHA7-S

    The sequence of this isoform differs from the canonical sequence as follows:
         442-450: APSQVSGVM → GMFCVYLH
         451-998: Missing.

    Note: Expressed in lung cancer cells, lacks the kinase domain and is most probably secreted.

    Show »
    Length:449
    Mass (Da):50,521
    Checksum:i4E15BF1881AC175A
    GO

    Sequence cautioni

    The sequence BAD92506.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 3 (identifier: Q15375-3)
    Sequence conflicti278 – 2781R → C in AAH27940. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti138 – 1381I → V.2 Publications
    Corresponds to variant rs2278107 [ dbSNP | Ensembl ].
    VAR_022105
    Natural varianti170 – 1701E → K in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042150
    Natural varianti232 – 2321G → R in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_042151
    Natural varianti278 – 2781P → S.1 Publication
    Corresponds to variant rs2278106 [ dbSNP | Ensembl ].
    VAR_022106
    Natural varianti371 – 3711R → W in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036090
    Natural varianti903 – 9031P → S in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_042152

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei278 – 2792PC → RK in isoform 3. 1 PublicationVSP_014380
    Alternative sequencei280 – 998719Missing in isoform 3. 1 PublicationVSP_014381Add
    BLAST
    Alternative sequencei442 – 4509APSQVSGVM → GMFCVYLH in isoform 5. CuratedVSP_041943
    Alternative sequencei451 – 998548Missing in isoform 5. CuratedVSP_041944Add
    BLAST
    Alternative sequencei540 – 5445Missing in isoform 2. 3 PublicationsVSP_014382
    Alternative sequencei600 – 6045FKFPG → C in isoform 4. 1 PublicationVSP_041945

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L36642 mRNA. Translation: AAA74243.1.
    AK313529 mRNA. Translation: BAG36308.1.
    AB209269 mRNA. Translation: BAD92506.1. Different initiation.
    AL121966 Genomic DNA. Translation: CAC19520.2.
    AL354857, AL121966, AL591036 Genomic DNA. Translation: CAH72780.1.
    AL591036, AL121966, AL354857 Genomic DNA. Translation: CAH73650.1.
    AL121966, AL354857, AL591036 Genomic DNA. Translation: CAI19722.1.
    CH471051 Genomic DNA. Translation: EAW48518.1.
    BC027940 mRNA. Translation: AAH27940.1.
    BC126125 mRNA. Translation: AAI26126.1.
    BC126151 mRNA. Translation: AAI26152.1.
    BC143857 mRNA. Translation: AAI43858.1.
    BC143858 mRNA. Translation: AAI43859.1.
    CCDSiCCDS5031.1. [Q15375-1]
    PIRiI58351.
    RefSeqiNP_001275558.1. NM_001288629.1. [Q15375-2]
    NP_001275559.1. NM_001288630.1. [Q15375-3]
    NP_004431.1. NM_004440.3. [Q15375-1]
    XP_005248726.1. XM_005248669.1. [Q15375-4]
    UniGeneiHs.73962.

    Genome annotation databases

    EnsembliENST00000369297; ENSP00000358303; ENSG00000135333. [Q15375-3]
    ENST00000369303; ENSP00000358309; ENSG00000135333. [Q15375-1]
    GeneIDi2045.
    KEGGihsa:2045.
    UCSCiuc003poe.3. human. [Q15375-1]
    uc003pof.3. human. [Q15375-2]
    uc003pog.4. human. [Q15375-3]
    uc011eac.2. human. [Q15375-4]

    Polymorphism databases

    DMDMi146345416.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L36642 mRNA. Translation: AAA74243.1 .
    AK313529 mRNA. Translation: BAG36308.1 .
    AB209269 mRNA. Translation: BAD92506.1 . Different initiation.
    AL121966 Genomic DNA. Translation: CAC19520.2 .
    AL354857 , AL121966 , AL591036 Genomic DNA. Translation: CAH72780.1 .
    AL591036 , AL121966 , AL354857 Genomic DNA. Translation: CAH73650.1 .
    AL121966 , AL354857 , AL591036 Genomic DNA. Translation: CAI19722.1 .
    CH471051 Genomic DNA. Translation: EAW48518.1 .
    BC027940 mRNA. Translation: AAH27940.1 .
    BC126125 mRNA. Translation: AAI26126.1 .
    BC126151 mRNA. Translation: AAI26152.1 .
    BC143857 mRNA. Translation: AAI43858.1 .
    BC143858 mRNA. Translation: AAI43859.1 .
    CCDSi CCDS5031.1. [Q15375-1 ]
    PIRi I58351.
    RefSeqi NP_001275558.1. NM_001288629.1. [Q15375-2 ]
    NP_001275559.1. NM_001288630.1. [Q15375-3 ]
    NP_004431.1. NM_004440.3. [Q15375-1 ]
    XP_005248726.1. XM_005248669.1. [Q15375-4 ]
    UniGenei Hs.73962.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2REI X-ray 1.60 A 590-899 [» ]
    3DKO X-ray 2.00 A 590-899 [» ]
    3H8M X-ray 2.10 A/B 919-990 [» ]
    3NRU X-ray 2.30 A/B/C/D/E/F/G/H/I/J/K/L 32-204 [» ]
    ProteinModelPortali Q15375.
    SMRi Q15375. Positions 30-899, 919-989.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108359. 8 interactions.
    IntActi Q15375. 9 interactions.
    MINTi MINT-1538326.
    STRINGi 9606.ENSP00000358309.

    Chemistry

    BindingDBi Q15375.
    ChEMBLi CHEMBL4602.
    GuidetoPHARMACOLOGYi 1827.

    PTM databases

    PhosphoSitei Q15375.

    Polymorphism databases

    DMDMi 146345416.

    Proteomic databases

    MaxQBi Q15375.
    PaxDbi Q15375.
    PRIDEi Q15375.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369297 ; ENSP00000358303 ; ENSG00000135333 . [Q15375-3 ]
    ENST00000369303 ; ENSP00000358309 ; ENSG00000135333 . [Q15375-1 ]
    GeneIDi 2045.
    KEGGi hsa:2045.
    UCSCi uc003poe.3. human. [Q15375-1 ]
    uc003pof.3. human. [Q15375-2 ]
    uc003pog.4. human. [Q15375-3 ]
    uc011eac.2. human. [Q15375-4 ]

    Organism-specific databases

    CTDi 2045.
    GeneCardsi GC06M094007.
    HGNCi HGNC:3390. EPHA7.
    HPAi CAB010496.
    MIMi 602190. gene.
    neXtProti NX_Q15375.
    PharmGKBi PA27822.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG062180.
    InParanoidi Q15375.
    KOi K05108.
    OMAi ENSPKMH.
    OrthoDBi EOG7VTDM6.
    PhylomeDBi Q15375.
    TreeFami TF315608.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    SignaLinki Q15375.

    Miscellaneous databases

    EvolutionaryTracei Q15375.
    GeneWikii EPHA7.
    GenomeRNAii 2045.
    NextBioi 8311.
    PROi Q15375.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q15375.
    CleanExi HS_EPHA7.
    Genevestigatori Q15375.

    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.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    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.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    SSF49265. SSF49265. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 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. "cDNA cloning and tissue distribution of five human EPH-like receptor protein-tyrosine kinases."
      Fox G.M., Holst P.L., Chute H.T., Lindberg R.A., Janssen A.M., Basu R., Welcher A.A.
      Oncogene 10:897-905(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(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; 2; 3 AND 4), VARIANT VAL-138.
      Tissue: Brain.
    7. "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.
    8. "ALL1 fusion proteins induce deregulation of EphA7 and ERK phosphorylation in human acute leukemias."
      Nakanishi H., Nakamura T., Canaani E., Croce C.M.
      Proc. Natl. Acad. Sci. U.S.A. 104:14442-14447(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MAP2K1; MAP2K2; MAPK1 AND MAPK3 PHOSPHORYLATION.
    9. "Secreted form of EphA7 in lung cancer."
      Tsuboi M., Mori H., Bunai T., Kageyama S., Suzuki M., Okudela K., Takamochi K., Ogawa H., Niwa H., Shinmura K., Sugimura H.
      Int. J. Oncol. 36:635-640(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 5).
    10. "Ephrin A7 ligand binding domain."
      Walker J.R., Yermekbayeva L., Seitova A., Kania J., Bountra C., Weigelt J., Arrowsmith C.H., Edwards A.M., Bochkarev A., Dhe-Paganon S.
      Submitted (JUN-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 32-204.
    11. Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-371.
    12. "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] VAL-138; LYS-170; ARG-232; SER-278 AND SER-903.

    Entry informationi

    Entry nameiEPHA7_HUMAN
    AccessioniPrimary (citable) accession number: Q15375
    Secondary accession number(s): A0AUX7
    , B2R8W1, B7ZLJ9, B7ZLK0, Q59G40, Q5VTU0, Q8N368, Q9H124
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 156 of the entry and version 3 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 6
      Human chromosome 6: 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