EPHA5_HUMAN
ID EPHA5_HUMAN Reviewed; 1037 AA.
AC P54756; Q7Z3F2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Ephrin type-A receptor 5;
DE EC=2.7.10.1;
DE AltName: Full=Brain-specific kinase;
DE AltName: Full=EPH homology kinase 1;
DE Short=EHK-1;
DE AltName: Full=EPH-like kinase 7;
DE Short=EK7;
DE Short=hEK7;
DE Flags: Precursor;
GN Name=EPHA5; Synonyms=BSK, EHK1, HEK7, TYRO4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9191074; DOI=10.1016/s0169-328x(96)00268-9;
RA Miescher G.C., Taylor V., Olivieri G., Mindermann T., Shrock E.,
RA Steck A.J.;
RT "Extensive splice variation and localization of the EHK-1 receptor tyrosine
RT kinase in adult human brain and glial tumors.";
RL Brain Res. Mol. Brain Res. 46:17-24(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-1037.
RC TISSUE=Brain;
RX PubMed=7898931;
RA Fox G.M., Holst P.L., Chute H.T., Lindberg R.A., Janssen A.M., Basu R.,
RA Welcher A.A.;
RT "cDNA cloning and tissue distribution of five human EPH-like receptor
RT protein-tyrosine kinases.";
RL Oncogene 10:897-905(1995).
RN [5]
RP IDENTIFICATION OF EFNA5 AS LIGAND, AND PHOSPHORYLATION.
RX PubMed=7748564; DOI=10.1016/0896-6273(95)90335-6;
RA Winslow J.W., Moran P., Valverde J., Shih A., Yuan J.Q., Wong S.C.,
RA Tsai S.P., Goddard A., Henzel W.J., Hefti F., Beck K.D., Caras I.W.;
RT "Cloning of AL-1, a ligand for an Eph-related tyrosine kinase receptor
RT involved in axon bundle formation.";
RL Neuron 14:973-981(1995).
RN [6]
RP NOMENCLATURE.
RX PubMed=9267020; DOI=10.1016/s0092-8674(00)80500-0;
RG Eph nomenclature committee;
RT "Unified nomenclature for Eph family receptors and their ligands, the
RT ephrins.";
RL Cell 90:403-404(1997).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10375373; DOI=10.1177/002215549904700702;
RA Olivieri G., Miescher G.C.;
RT "Immunohistochemical localization of EphA5 in the adult human central
RT nervous system.";
RL J. Histochem. Cytochem. 47:855-861(1999).
RN [8]
RP VARIANTS [LARGE SCALE ANALYSIS] THR-81; ALA-235; GLN-330; GLN-417; LYS-503;
RP CYS-506; GLU-582; THR-672; THR-673; ILE-856; ARG-959 AND SER-1032.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI-
CC anchored ephrin-A family ligands residing on adjacent cells, leading to
CC contact-dependent bidirectional signaling into neighboring cells. The
CC signaling pathway downstream of the receptor is referred to as forward
CC signaling while the signaling pathway downstream of the ephrin ligand
CC is referred to as reverse signaling. Among GPI-anchored ephrin-A
CC ligands, EFNA5 most probably constitutes the cognate/functional ligand
CC for EPHA5. Functions as an axon guidance molecule during development
CC and may be involved in the development of the retinotectal, entorhino-
CC hippocampal and hippocamposeptal pathways. Together with EFNA5 plays
CC also a role in synaptic plasticity in adult brain through regulation of
CC synaptogenesis. In addition to its function in the nervous system, the
CC interaction of EPHA5 with EFNA5 mediates communication between
CC pancreatic islet cells to regulate glucose-stimulated insulin secretion
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer
CC is composed of an ephrin dimer and a receptor dimer. Oligomerization is
CC probably required to induce biological responses (By similarity).
CC Interacts (via SAM domain) with SAMD5 (via SAM domain) (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q60629}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10375373};
CC Single-pass type I membrane protein {ECO:0000255}. Cell projection,
CC axon {ECO:0000250|UniProtKB:P54757}. Cell projection, dendrite
CC {ECO:0000269|PubMed:10375373, ECO:0000269|PubMed:9191074}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P54756-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P54756-2; Sequence=VSP_002999;
CC Name=3;
CC IsoId=P54756-3; Sequence=VSP_039118, VSP_039119;
CC -!- TISSUE SPECIFICITY: Almost exclusively expressed in the nervous system
CC in cortical neurons, cerebellar Purkinje cells and pyramidal neurons
CC within the cortex and hippocampus. Display an increasing gradient of
CC expression from the forebrain to hindbrain and spinal cord.
CC {ECO:0000269|PubMed:10375373, ECO:0000269|PubMed:9191074}.
CC -!- PTM: Phosphorylated. Phosphorylation is stimulated by the ligand EFNA5.
CC Dephosphorylation upon stimulation by glucose, inhibits EPHA5 forward
CC signaling and results in insulin secretion (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; X95425; CAA64700.1; -; mRNA.
DR EMBL; AC018683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC115223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX537946; CAD97914.1; -; mRNA.
DR EMBL; L36644; AAA74245.1; -; mRNA.
DR CCDS; CCDS3513.1; -. [P54756-1]
DR CCDS; CCDS3514.1; -. [P54756-2]
DR RefSeq; NP_001268694.1; NM_001281765.2.
DR RefSeq; NP_001268695.1; NM_001281766.2.
DR RefSeq; NP_001305690.1; NM_001318761.1. [P54756-3]
DR RefSeq; NP_004430.4; NM_004439.7. [P54756-1]
DR RefSeq; NP_872272.2; NM_182472.4. [P54756-2]
DR PDB; 2R2P; X-ray; 2.40 A; A=653-939.
DR PDB; 4ET7; X-ray; 2.60 A; A=59-235.
DR PDBsum; 2R2P; -.
DR PDBsum; 4ET7; -.
DR AlphaFoldDB; P54756; -.
DR SMR; P54756; -.
DR BioGRID; 108358; 22.
DR IntAct; P54756; 7.
DR MINT; P54756; -.
DR STRING; 9606.ENSP00000480763; -.
DR BindingDB; P54756; -.
DR ChEMBL; CHEMBL3987; -.
DR DrugBank; DB01254; Dasatinib.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; P54756; -.
DR GuidetoPHARMACOLOGY; 1825; -.
DR GlyGen; P54756; 7 sites.
DR iPTMnet; P54756; -.
DR PhosphoSitePlus; P54756; -.
DR BioMuta; EPHA5; -.
DR DMDM; 259016353; -.
DR EPD; P54756; -.
DR jPOST; P54756; -.
DR MassIVE; P54756; -.
DR MaxQB; P54756; -.
DR PaxDb; P54756; -.
DR PeptideAtlas; P54756; -.
DR PRIDE; P54756; -.
DR ProteomicsDB; 56712; -. [P54756-1]
DR ProteomicsDB; 56713; -. [P54756-2]
DR ProteomicsDB; 56714; -. [P54756-3]
DR TopDownProteomics; P54756-2; -. [P54756-2]
DR ABCD; P54756; 4 sequenced antibodies.
DR Antibodypedia; 12603; 538 antibodies from 35 providers.
DR DNASU; 2044; -.
DR Ensembl; ENST00000273854.7; ENSP00000273854.3; ENSG00000145242.14. [P54756-1]
DR Ensembl; ENST00000354839.8; ENSP00000346899.4; ENSG00000145242.14. [P54756-2]
DR GeneID; 2044; -.
DR KEGG; hsa:2044; -.
DR UCSC; uc003hcy.5; human. [P54756-1]
DR CTD; 2044; -.
DR DisGeNET; 2044; -.
DR GeneCards; EPHA5; -.
DR HGNC; HGNC:3389; EPHA5.
DR HPA; ENSG00000145242; Tissue enriched (brain).
DR MIM; 600004; gene.
DR neXtProt; NX_P54756; -.
DR OpenTargets; ENSG00000145242; -.
DR PharmGKB; PA27821; -.
DR VEuPathDB; HostDB:ENSG00000145242; -.
DR eggNOG; KOG0196; Eukaryota.
DR GeneTree; ENSGT00940000156266; -.
DR HOGENOM; CLU_000288_141_4_1; -.
DR InParanoid; P54756; -.
DR OMA; AWCIPAN; -.
DR OrthoDB; 933071at2759; -.
DR PhylomeDB; P54756; -.
DR TreeFam; TF315608; -.
DR BRENDA; 2.7.10.1; 2681.
DR PathwayCommons; P54756; -.
DR Reactome; R-HSA-2682334; EPH-Ephrin signaling.
DR Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR SignaLink; P54756; -.
DR SIGNOR; P54756; -.
DR BioGRID-ORCS; 2044; 11 hits in 1107 CRISPR screens.
DR ChiTaRS; EPHA5; human.
DR EvolutionaryTrace; P54756; -.
DR GeneWiki; EPH_receptor_A5; -.
DR GenomeRNAi; 2044; -.
DR Pharos; P54756; Tchem.
DR PRO; PR:P54756; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P54756; protein.
DR Bgee; ENSG00000145242; Expressed in cortical plate and 98 other tissues.
DR ExpressionAtlas; P54756; baseline and differential.
DR Genevisible; P54756; HS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005003; F:ephrin receptor activity; ISS:UniProtKB.
DR GO; GO:0005004; F:GPI-linked ephrin receptor activity; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0019933; P:cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; IEP:UniProtKB.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd10483; EphR_LBD_A5; 1.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR034277; EphA5_rcpt_lig-bd.
DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF01404; Ephrin_lbd; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS51550; EPH_LBD; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW Cell projection; Glycoprotein; Kinase; Membrane; Neurogenesis;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1037
FT /note="Ephrin type-A receptor 5"
FT /id="PRO_0000016812"
FT TOPO_DOM 25..573
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 595..1037
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 60..238
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 357..467
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 468..562
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 675..936
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 965..1029
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1035..1037
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 800
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 681..689
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 707
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 650
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 656
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 833
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000255"
FT MOD_RES 982
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..69
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039118"
FT VAR_SEQ 563
FT /note="F -> SV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039119"
FT VAR_SEQ 597..619
FT /note="SCCECGCGRASSLCAVAHPSLIW -> R (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002999"
FT VARIANT 81
FT /note="N -> T (in dbSNP:rs33932471)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042138"
FT VARIANT 235
FT /note="S -> A (in dbSNP:rs55710198)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042139"
FT VARIANT 330
FT /note="E -> Q (in dbSNP:rs56205382)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042140"
FT VARIANT 417
FT /note="R -> Q (in a lung adenocarcinoma sample; somatic
FT mutation; dbSNP:rs199614818)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042141"
FT VARIANT 503
FT /note="E -> K (in a lung large cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042142"
FT VARIANT 506
FT /note="Y -> C (in dbSNP:rs56074660)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_045912"
FT VARIANT 582
FT /note="G -> E (in a lung adenocarcinoma sample; somatic
FT mutation; dbSNP:rs1057520012)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042143"
FT VARIANT 672
FT /note="A -> T (in dbSNP:rs36050417)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042144"
FT VARIANT 673
FT /note="S -> T (in dbSNP:rs56359290)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042145"
FT VARIANT 856
FT /note="T -> I (in a lung squamous cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042146"
FT VARIANT 959
FT /note="H -> R (in dbSNP:rs56312931)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042147"
FT VARIANT 1032
FT /note="N -> S (in a lung large cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042148"
FT CONFLICT 11
FT /note="R -> H (in Ref. 1; CAA64700)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="G -> D (in Ref. 3; CAD97914)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="Y -> H (in Ref. 1; CAA64700)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="A -> V (in Ref. 3; CAD97914)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="S -> I (in Ref. 1; CAA64700)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="G -> E (in Ref. 3; CAD97914)"
FT /evidence="ECO:0000305"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:4ET7"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:4ET7"
FT STRAND 76..89
FT /evidence="ECO:0007829|PDB:4ET7"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:4ET7"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:4ET7"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:4ET7"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:4ET7"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:4ET7"
FT STRAND 148..157
FT /evidence="ECO:0007829|PDB:4ET7"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4ET7"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:4ET7"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:4ET7"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:4ET7"
FT STRAND 207..219
FT /evidence="ECO:0007829|PDB:4ET7"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:4ET7"
FT HELIX 663..665
FT /evidence="ECO:0007829|PDB:2R2P"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:2R2P"
FT STRAND 675..683
FT /evidence="ECO:0007829|PDB:2R2P"
FT STRAND 685..694
FT /evidence="ECO:0007829|PDB:2R2P"
FT STRAND 702..708
FT /evidence="ECO:0007829|PDB:2R2P"
FT HELIX 715..728
FT /evidence="ECO:0007829|PDB:2R2P"
FT STRAND 739..743
FT /evidence="ECO:0007829|PDB:2R2P"
FT STRAND 745..748
FT /evidence="ECO:0007829|PDB:2R2P"
FT STRAND 750..754
FT /evidence="ECO:0007829|PDB:2R2P"
FT HELIX 761..766
FT /evidence="ECO:0007829|PDB:2R2P"
FT TURN 767..770
FT /evidence="ECO:0007829|PDB:2R2P"
FT HELIX 774..793
FT /evidence="ECO:0007829|PDB:2R2P"
FT HELIX 803..805
FT /evidence="ECO:0007829|PDB:2R2P"
FT STRAND 806..808
FT /evidence="ECO:0007829|PDB:2R2P"
FT STRAND 814..816
FT /evidence="ECO:0007829|PDB:2R2P"
FT HELIX 842..844
FT /evidence="ECO:0007829|PDB:2R2P"
FT HELIX 847..852
FT /evidence="ECO:0007829|PDB:2R2P"
FT HELIX 857..873
FT /evidence="ECO:0007829|PDB:2R2P"
FT TURN 878..881
FT /evidence="ECO:0007829|PDB:2R2P"
FT HELIX 884..893
FT /evidence="ECO:0007829|PDB:2R2P"
FT HELIX 905..914
FT /evidence="ECO:0007829|PDB:2R2P"
FT HELIX 919..921
FT /evidence="ECO:0007829|PDB:2R2P"
FT HELIX 925..936
FT /evidence="ECO:0007829|PDB:2R2P"
SQ SEQUENCE 1037 AA; 114803 MW; 578C2F4D950DE419 CRC64;
MRGSGPRGAG RRRPPSGGGD TPITPASLAG CYSAPRRAPL WTCLLLCAAL RTLLASPSNE
VNLLDSRTVM GDLGWIAFPK NGWEEIGEVD ENYAPIHTYQ VCKVMEQNQN NWLLTSWISN
EGASRIFIEL KFTLRDCNSL PGGLGTCKET FNMYYFESDD QNGRNIKENQ YIKIDTIAAD
ESFTELDLGD RVMKLNTEVR DVGPLSKKGF YLAFQDVGAC IALVSVRVYY KKCPSVVRHL
AVFPDTITGA DSSQLLEVSG SCVNHSVTDE PPKMHCSAEG EWLVPIGKCM CKAGYEEKNG
TCQVCRPGFF KASPHIQSCG KCPPHSYTHE EASTSCVCEK DYFRRESDPP TMACTRPPSA
PRNAISNVNE TSVFLEWIPP ADTGGRKDVS YYIACKKCNS HAGVCEECGG HVRYLPRQSG
LKNTSVMMVD LLAHTNYTFE IEAVNGVSDL SPGARQYVSV NVTTNQAAPS PVTNVKKGKI
AKNSISLSWQ EPDRPNGIIL EYEIKYFEKD QETSYTIIKS KETTITAEGL KPASVYVFQI
RARTAAGYGV FSRRFEFETT PVFAASSDQS QIPVIAVSVT VGVILLAVVI GVLLSGSCCE
CGCGRASSLC AVAHPSLIWR CGYSKAKQDP EEEKMHFHNG HIKLPGVRTY IDPHTYEDPN
QAVHEFAKEI EASCITIERV IGAGEFGEVC SGRLKLPGKR ELPVAIKTLK VGYTEKQRRD
FLGEASIMGQ FDHPNIIHLE GVVTKSKPVM IVTEYMENGS LDTFLKKNDG QFTVIQLVGM
LRGISAGMKY LSDMGYVHRD LAARNILINS NLVCKVSDFG LSRVLEDDPE AAYTTRGGKI
PIRWTAPEAI AFRKFTSASD VWSYGIVMWE VVSYGERPYW EMTNQDVIKA VEEGYRLPSP
MDCPAALYQL MLDCWQKERN SRPKFDEIVN MLDKLIRNPS SLKTLVNASC RVSNLLAEHS
PLGSGAYRSV GEWLEAIKMG RYTEIFMENG YSSMDAVAQV TLEDLRRLGV TLVGHQKKIM
NSLQEMKVQL VNGMVPL
