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P21709

- EPHA1_HUMAN

UniProt

P21709 - EPHA1_HUMAN

Protein

Ephrin type-A receptor 1

Gene

EPHA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 4 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Receptor tyrosine kinase which binds promiscuously membrane-bound 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. Binds with a low affinity EFNA3 and EFNA4 and with a high affinity to EFNA1 which most probably constitutes its cognate/functional ligand. Upon activation by EFNA1 induces cell attachment to the extracellular matrix inhibiting cell spreading and motility through regulation of ILK and downstream RHOA and RAC. Plays also a role in angiogenesis and regulates cell proliferation. May play a role in apoptosis.3 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 sitei656 – 6561ATPPROSITE-ProRule annotation
    Active sitei749 – 7491Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi630 – 6389ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein kinase activity Source: UniProtKB
    3. protein kinase binding Source: UniProtKB
    4. transmembrane-ephrin receptor activity Source: UniProtKB

    GO - Biological processi

    1. activation of Rho GTPase activity Source: UniProtKB
    2. angiogenesis Source: UniProtKB-KW
    3. cell surface receptor signaling pathway Source: UniProtKB
    4. negative regulation of cell migration Source: UniProtKB
    5. negative regulation of protein kinase activity Source: UniProtKB
    6. peptidyl-tyrosine phosphorylation Source: UniProtKB
    7. positive regulation of angiogenesis Source: UniProtKB
    8. positive regulation of cell-matrix adhesion Source: UniProtKB
    9. positive regulation of cell migration Source: UniProtKB
    10. positive regulation of cell proliferation Source: UniProtKB
    11. positive regulation of stress fiber assembly Source: UniProtKB
    12. protein autophosphorylation Source: UniProtKB
    13. regulation of Rac GTPase activity Source: UniProtKB
    14. substrate adhesion-dependent cell spreading Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Angiogenesis, Cell adhesion

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    ReactomeiREACT_200759. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
    SignaLinkiP21709.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin type-A receptor 1 (EC:2.7.10.1)
    Short name:
    hEpha1
    Alternative name(s):
    EPH tyrosine kinase
    EPH tyrosine kinase 1
    Erythropoietin-producing hepatoma receptor
    Tyrosine-protein kinase receptor EPH
    Gene namesi
    Name:EPHA1
    Synonyms:EPH, EPHT, EPHT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:3385. EPHA1.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

    GO - Cellular componenti

    1. integral component of plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27817.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 976951Ephrin type-A receptor 1PRO_0000016798Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi414 – 4141N-linked (GlcNAc...)Sequence Analysis
    Modified residuei599 – 5991Phosphotyrosine; by autocatalysisSequence Analysis
    Modified residuei605 – 6051Phosphotyrosine; by autocatalysisSequence Analysis
    Modified residuei781 – 7811Phosphotyrosine; by autocatalysisSequence Analysis
    Modified residuei906 – 9061Phosphoserine1 Publication
    Modified residuei910 – 9101Phosphoserine1 Publication
    Modified residuei930 – 9301Phosphotyrosine; by autocatalysisSequence Analysis

    Post-translational modificationi

    Phosphorylated. Autophosphorylation is stimulated by its ligand EFNA1.1 Publication
    Ubiquitinated.1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP21709.
    PaxDbiP21709.
    PRIDEiP21709.

    PTM databases

    PhosphoSiteiP21709.

    Expressioni

    Tissue specificityi

    Overexpressed in several carcinomas.

    Gene expression databases

    BgeeiP21709.
    CleanExiHS_EPHA1.
    GenevestigatoriP21709.

    Organism-specific databases

    HPAiCAB026144.

    Interactioni

    Subunit structurei

    Homodimer. Forms a signaling complex with LCK; PTK2B/PYK2 and PI3-kinase upon activation by EFNA1; regulates T-lymphocytes migration. Interacts (via SAM domain) with ILK (via ANK repeats); stimulated by EFNA1 but independent of the kinase activity of EPHA1. Interacts (kinase activity-dependent) with PTK2/FAK1.2 Publications

    Protein-protein interaction databases

    BioGridi108355. 3 interactions.
    DIPiDIP-34886N.
    IntActiP21709. 2 interactions.
    STRINGi9606.ENSP00000275815.

    Structurei

    Secondary structure

    1
    976
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi538 – 5403
    Helixi545 – 57026
    Helixi918 – 9247
    Helixi928 – 9303
    Helixi931 – 9366
    Helixi942 – 9454
    Helixi950 – 9556
    Helixi961 – 97313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2K1KNMR-A/B536-573[»]
    2K1LNMR-A/B536-573[»]
    3HILX-ray2.00A/B911-974[»]
    3KKAX-ray2.40A/B911-974[»]
    ProteinModelPortaliP21709.
    SMRiP21709. Positions 24-538, 562-894, 911-974.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21709.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 547522ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini569 – 976408CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei548 – 56821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 209183Eph LBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini332 – 445114Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini447 – 53892Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini624 – 884261Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini913 – 97664SAMPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi974 – 9763PDZ-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi191 – 329139Cys-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.
    InParanoidiP21709.
    KOiK05102.
    OMAiQAYEDPA.
    OrthoDBiEOG7VTDM6.
    PhylomeDBiP21709.
    TreeFamiTF315363.

    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.
    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]
    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.
    SSF57184. SSF57184. 2 hits.
    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 (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: P21709-1) [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

    MERRWPLGLG LVLLLCAPLP PGARAKEVTL MDTSKAQGEL GWLLDPPKDG    50
    WSEQQQILNG TPLYMYQDCP MQGRRDTDHW LRSNWIYRGE EASRVHVELQ 100
    FTVRDCKSFP GGAGPLGCKE TFNLLYMESD QDVGIQLRRP LFQKVTTVAA 150
    DQSFTIRDLV SGSVKLNVER CSLGRLTRRG LYLAFHNPGA CVALVSVRVF 200
    YQRCPETLNG LAQFPDTLPG PAGLVEVAGT CLPHARASPR PSGAPRMHCS 250
    PDGEWLVPVG RCHCEPGYEE GGSGEACVAC PSGSYRMDMD TPHCLTCPQQ 300
    STAESEGATI CTCESGHYRA PGEGPQVACT GPPSAPRNLS FSASGTQLSL 350
    RWEPPADTGG RQDVRYSVRC SQCQGTAQDG GPCQPCGVGV HFSPGARGLT 400
    TPAVHVNGLE PYANYTFNVE AQNGVSGLGS SGHASTSVSI SMGHAESLSG 450
    LSLRLVKKEP RQLELTWAGS RPRSPGANLT YELHVLNQDE ERYQMVLEPR 500
    VLLTELQPDT TYIVRVRMLT PLGPGPFSPD HEFRTSPPVS RGLTGGEIVA 550
    VIFGLLLGAA LLLGILVFRS RRAQRQRQQR QRDRATDVDR EDKLWLKPYV 600
    DLQAYEDPAQ GALDFTRELD PAWLMVDTVI GEGEFGEVYR GTLRLPSQDC 650
    KTVAIKTLKD TSPGGQWWNF LREATIMGQF SHPHILHLEG VVTKRKPIMI 700
    ITEFMENGAL DAFLREREDQ LVPGQLVAML QGIASGMNYL SNHNYVHRDL 750
    AARNILVNQN LCCKVSDFGL TRLLDDFDGT YETQGGKIPI RWTAPEAIAH 800
    RIFTTASDVW SFGIVMWEVL SFGDKPYGEM SNQEVMKSIE DGYRLPPPVD 850
    CPAPLYELMK NCWAYDRARR PHFQKLQAHL EQLLANPHSL RTIANFDPRM 900
    TLRLPSLSGS DGIPYRTVSE WLESIRMKRY ILHFHSAGLD TMECVLELTA 950
    EDLTQMGITL PGHQKRILCS IQGFKD 976
    Length:976
    Mass (Da):108,127
    Last modified:January 11, 2011 - v4
    Checksum:i91EFCA69FFE17826
    GO
    Isoform 2 (identifier: P21709-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         446-490: ESLSGLSLRL...YELHVLNQDE → DPTLSLWTPR...APKPWGEPDL
         491-976: Missing.

    Show »
    Length:490
    Mass (Da):52,618
    Checksum:iC7BF2D396EE54F05
    GO
    Isoform 3 (identifier: P21709-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         446-474: ESLSGLSLRLVKKEPRQLELTWAGSRPRS → GERLRGAGTGTWWRQKGLRPQNKLMGRKP
         475-976: Missing.

    Show »
    Length:474
    Mass (Da):51,069
    Checksum:i6D263B013A90E9B5
    GO

    Sequence cautioni

    The sequence AAA36747.1 differs from that shown. Reason: Frameshift at positions 582, 595 and 601.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti398 – 3981G → A in AAD43440. (PubMed:10369740)Curated
    Sequence conflicti398 – 3981G → A in CAA81796. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti160 – 1601V → A.6 Publications
    Corresponds to variant rs4725617 [ dbSNP | Ensembl ].
    VAR_028265
    Natural varianti351 – 3511R → C.1 Publication
    Corresponds to variant rs56006153 [ dbSNP | Ensembl ].
    VAR_042115
    Natural varianti492 – 4921R → Q.1 Publication
    Corresponds to variant rs11768549 [ dbSNP | Ensembl ].
    VAR_028266
    Natural varianti575 – 5751R → Q.1 Publication
    Corresponds to variant rs35719334 [ dbSNP | Ensembl ].
    VAR_042116
    Natural varianti585 – 5851A → T.1 Publication
    Corresponds to variant rs34178823 [ dbSNP | Ensembl ].
    VAR_042117
    Natural varianti697 – 6971P → L.1 Publication
    Corresponds to variant rs34372369 [ dbSNP | Ensembl ].
    VAR_042118
    Natural varianti703 – 7031E → K in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication
    VAR_042119
    Natural varianti807 – 8071S → R.1 Publication
    Corresponds to variant rs56244405 [ dbSNP | Ensembl ].
    VAR_042120
    Natural varianti900 – 9001M → V.8 Publications
    Corresponds to variant rs6967117 [ dbSNP | Ensembl ].
    VAR_028267

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei446 – 49045ESLSG…LNQDE → DPTLSLWTPRVTVRPVSETG EERTEATRADLGGVPAPKPW GEPDL in isoform 2. 1 PublicationVSP_056010Add
    BLAST
    Alternative sequencei446 – 47429ESLSG…SRPRS → GERLRGAGTGTWWRQKGLRP QNKLMGRKP in isoform 3. 1 PublicationVSP_056011Add
    BLAST
    Alternative sequencei475 – 976502Missing in isoform 3. 1 PublicationVSP_056012Add
    BLAST
    Alternative sequencei491 – 976486Missing in isoform 2. 1 PublicationVSP_056013Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18391 mRNA. Translation: AAA36747.1. Frameshift.
    AF101171
    , AF101165, AF101166, AF101167, AF101168, AF101169, AF101170 Genomic DNA. Translation: AAD43440.1.
    EU826604 mRNA. Translation: ACF47640.1.
    EU826605 mRNA. Translation: ACF47641.1.
    AC092214 Genomic DNA. Translation: AAS07458.1.
    CH236959 Genomic DNA. Translation: EAL23789.1.
    CH471198 Genomic DNA. Translation: EAW51846.1.
    CH471198 Genomic DNA. Translation: EAW51847.1.
    BC130291 mRNA. Translation: AAI30292.1.
    Z27409 mRNA. Translation: CAA81796.1.
    CCDSiCCDS5884.1.
    PIRiA34076.
    RefSeqiNP_005223.4. NM_005232.4.
    UniGeneiHs.89839.

    Genome annotation databases

    EnsembliENST00000275815; ENSP00000275815; ENSG00000146904.
    GeneIDi2041.
    KEGGihsa:2041.
    UCSCiuc003wcz.3. human.

    Polymorphism databases

    DMDMi317373566.

    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
    M18391 mRNA. Translation: AAA36747.1 . Frameshift.
    AF101171
    , AF101165 , AF101166 , AF101167 , AF101168 , AF101169 , AF101170 Genomic DNA. Translation: AAD43440.1 .
    EU826604 mRNA. Translation: ACF47640.1 .
    EU826605 mRNA. Translation: ACF47641.1 .
    AC092214 Genomic DNA. Translation: AAS07458.1 .
    CH236959 Genomic DNA. Translation: EAL23789.1 .
    CH471198 Genomic DNA. Translation: EAW51846.1 .
    CH471198 Genomic DNA. Translation: EAW51847.1 .
    BC130291 mRNA. Translation: AAI30292.1 .
    Z27409 mRNA. Translation: CAA81796.1 .
    CCDSi CCDS5884.1.
    PIRi A34076.
    RefSeqi NP_005223.4. NM_005232.4.
    UniGenei Hs.89839.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2K1K NMR - A/B 536-573 [» ]
    2K1L NMR - A/B 536-573 [» ]
    3HIL X-ray 2.00 A/B 911-974 [» ]
    3KKA X-ray 2.40 A/B 911-974 [» ]
    ProteinModelPortali P21709.
    SMRi P21709. Positions 24-538, 562-894, 911-974.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108355. 3 interactions.
    DIPi DIP-34886N.
    IntActi P21709. 2 interactions.
    STRINGi 9606.ENSP00000275815.

    Chemistry

    BindingDBi P21709.
    ChEMBLi CHEMBL2363043.
    GuidetoPHARMACOLOGYi 1821.

    PTM databases

    PhosphoSitei P21709.

    Polymorphism databases

    DMDMi 317373566.

    Proteomic databases

    MaxQBi P21709.
    PaxDbi P21709.
    PRIDEi P21709.

    Protocols and materials databases

    DNASUi 2041.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000275815 ; ENSP00000275815 ; ENSG00000146904 .
    GeneIDi 2041.
    KEGGi hsa:2041.
    UCSCi uc003wcz.3. human.

    Organism-specific databases

    CTDi 2041.
    GeneCardsi GC07M143087.
    H-InvDB HIX0033699.
    HGNCi HGNC:3385. EPHA1.
    HPAi CAB026144.
    MIMi 179610. gene.
    neXtProti NX_P21709.
    PharmGKBi PA27817.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233856.
    HOVERGENi HBG062180.
    InParanoidi P21709.
    KOi K05102.
    OMAi QAYEDPA.
    OrthoDBi EOG7VTDM6.
    PhylomeDBi P21709.
    TreeFami TF315363.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    Reactomei REACT_200759. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
    SignaLinki P21709.

    Miscellaneous databases

    EvolutionaryTracei P21709.
    GeneWikii EPH_receptor_A1.
    GenomeRNAii 2041.
    NextBioi 8291.
    PROi P21709.
    SOURCEi Search...

    Gene expression databases

    Bgeei P21709.
    CleanExi HS_EPHA1.
    Genevestigatori P21709.

    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.
    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 ]
    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.
    SSF57184. SSF57184. 2 hits.
    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. "A novel putative tyrosine kinase receptor encoded by the eph gene."
      Hirai H., Maru Y., Hagiwara K., Nishida J., Takaku F.
      Science 238:1717-1720(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ALA-160 AND VAL-900.
    2. "Genomic structure of the EPHA1 receptor tyrosine kinase gene."
      Owshalimpur D., Kelley M.J.
      Mol. Cell. Probes 13:169-173(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-160 AND VAL-900.
    3. "Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
      Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
      Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), ALTERNATIVE SPLICING.
    4. "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].
    5. "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], VARIANTS ALA-160 AND VAL-900.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS ALA-160 AND VAL-900.
    7. "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 1), VARIANTS ALA-160 AND VAL-900.
      Tissue: Brain.
    8. "An EGFR/eph chimeric receptor possesses ligand stimulated tyrosine kinase activity and promotes cell growth."
      Tuzi N.L.
      Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 286-976 (ISOFORM 1), VARIANT VAL-900.
      Tissue: Placenta.
    9. "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.
    10. "Ephrin-A1 stimulates migration of CD8+CCR7+ T lymphocytes."
      Hjorthaug H.S., Aasheim H.C.
      Eur. J. Immunol. 37:2326-2336(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MIGRATION OF T-LYMPHOCYTES, INTERACTION WITH LCK; PTK2B/PYK2 AND PI3-KINASE.
    11. "EphA1 interacts with integrin-linked kinase and regulates cell morphology and motility."
      Yamazaki T., Masuda J., Omori T., Usui R., Akiyama H., Maru Y.
      J. Cell Sci. 122:243-255(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL SPREADING, FUNCTION IN CELL MIGRATION, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH PTK2/FAK1 AND ILK.
    12. "EphA1 receptor silencing by small interfering RNA has antiangiogenic and antitumor efficacy in hepatocellular carcinoma."
      Chen G., Wang Y., Zhou M., Shi H., Yu Z., Zhu Y., Yu F.
      Oncol. Rep. 23:563-570(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANGIOGENESIS, FUNCTION IN CELL PROLIFERATION.
    13. "Development and validation of a method for profiling post-translational modification activities using protein microarrays."
      Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
      PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-906 AND SER-910, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Spatial structure and pH-dependent conformational diversity of dimeric transmembrane domain of the receptor tyrosine kinase EphA1."
      Bocharov E.V., Mayzel M.L., Volynsky P.E., Goncharuk M.V., Ermolyuk Y.S., Schulga A.A., Artemenko E.O., Efremov R.G., Arseniev A.S.
      J. Biol. Chem. 283:29385-29395(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 536-573, HOMODIMERIZATION.
    16. "Sam domain of human ephrin type-a receptor 1 (epha1)."
      Structural genomics consortium (SGC)
      Submitted (JUN-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 911-974.
    17. "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] ALA-160; CYS-351; GLN-492; GLN-575; THR-585; LEU-697; LYS-703; ARG-807 AND VAL-900.
    18. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiEPHA1_HUMAN
    AccessioniPrimary (citable) accession number: P21709
    Secondary accession number(s): A1L3V3
    , B5A966, B5A967, Q15405
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 170 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

    3D-structure, Complete proteome, 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. 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