CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014247
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ephrin type-A receptor 1 
Protein Synonyms/Alias
 mEpha1; Embryonic stem cell kinase; Tyrosine-protein kinase receptor ESK 
Gene Name
 Epha1 
Gene Synonyms/Alias
 Esk 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
788TYETQGGKIPIRWTAubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 28 210 Eph LBD.
 DOMAIN 333 438 Fibronectin type-III 1.
 DOMAIN 447 536 Fibronectin type-III 2.
 DOMAIN 625 885 Protein kinase.
 DOMAIN 914 977 SAM.
 NP_BIND 631 639 ATP (By similarity).
 MOTIF 975 977 PDZ-binding (Potential).
 ACT_SITE 750 750 Proton acceptor (By similarity).
 BINDING 657 657 ATP (By similarity).
 MOD_RES 600 600 Phosphotyrosine; by autocatalysis
 MOD_RES 606 606 Phosphotyrosine; by autocatalysis
 MOD_RES 782 782 Phosphotyrosine; by autocatalysis (By
 MOD_RES 907 907 Phosphoserine (By similarity).
 MOD_RES 911 911 Phosphoserine.
 CARBOHYD 415 415 N-linked (GlcNAc...) (Potential).
 CARBOHYD 479 479 N-linked (GlcNAc...) (Potential).  
Keyword
 3D-structure; Angiogenesis; ATP-binding; Cell adhesion; Cell membrane; Complete proteome; Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 977 AA 
Protein Sequence
MERRWPLGLA LLLLLLCAPL PPGARAEEVT LMDTSTAQGE LGWLLDPPET GWSEVQQMLN 60
GTPLYMYQDC PIQEGGDTDH WLRSNWIYRG EEASRIYVEL QFTVRDCKSF PGGAGPLGCK 120
ETFNLFYMES DQDVGIQLRR PLFQKVTTVA ADQSFTIRDL ASGSVKLNVE RCSLGHLTRR 180
GLYLAFHNPG SCVALVSVRV FYQRCAETVH GLAHFPDTLP GPGGLVEVAG TCLSHAQISL 240
GSSGTPRMHC SPDGEWLVPV GQCQCEPGYE ESSGNVGCTA CPTGFYRVDM NTLRCLKCPQ 300
HSIAESEGST ICTCENGHYR APGEGPQVAC TRPPSAPQNL SFSTSGTQLS LRWEPPRDTG 360
GRHDIRYSVE CLQCRGIAQD GGPCQPCGKG VHFSPAASGL TTSTVQVQGL EPYANYTFTV 420
KSQNRVSGLD SSSPSSASLS INMGHAESLS GLSLKLVKKE PRQLELTWAG SRPRNPGGNL 480
SYELHVLNQD EEWHQMVLEP RVLLTKLQPD TTYIVRVRTL TPLGPGPFSP DHEFRTSPPV 540
SRSLTGGEIV AVIFGLLLGI ALLIGIYVFR SRRGQRQRQQ RQRERTTNVD REDKLWLKPY 600
VDLQAYEDPA QGALDFAQEL DPAWLIVDTV IGEGEFGEVY RGALRLPSQD CKTVAIKTLK 660
DTSPDGYWWN FLREATIMGQ FNHPHILRLE GVITKRKPIM IITEFMENGA LDAFLKERED 720
QLAPGQLVAM LLGIASGMNC LSGHNYVHRD LAARNILVNQ NLCCKVSDFG LTRLLDDFDG 780
TYETQGGKIP IRWTAPEAIA HRIFTTASDV WSFGIVMWEV LSFGDKPYGE MSNQEVMKSI 840
EDGYRLPPPV DCPAPLYELM KNCWAYDRAR RPHFLQLQAH LEQLLTDPHS LRTIANFDPR 900
VTLRLPSLSG SDGIPYRSVS EWLESIRMKR YILHFRSAGL DTMECVLELT AEDLTQMGIT 960
LPGHQKRILC SIQGFKD 977 
Gene Ontology
 GO:0005887; C:integral to plasma membrane; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005005; F:transmembrane-ephrin receptor activity; ISS:UniProtKB.
 GO:0032862; P:activation of Rho GTPase activity; ISS:UniProtKB.
 GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
 GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
 GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
 GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
 GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
 GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
 GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
 GO:0001954; P:positive regulation of cell-matrix adhesion; ISS:UniProtKB.
 GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB.
 GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
 GO:0032314; P:regulation of Rac GTPase activity; ISS:UniProtKB.
 GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB. 
Interpro
 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_cat_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. 
Pfam
 PF01404; Ephrin_lbd
 PF00041; fn3
 PF07714; Pkinase_Tyr
 PF00536; SAM_1 
SMART
 SM00615; EPH_lbd
 SM00060; FN3
 SM00454; SAM
 SM00219; TyrKc 
PROSITE
 PS01186; EGF_2
 PS51550; EPH_LBD
 PS50853; FN3
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00109; PROTEIN_KINASE_TYR
 PS00790; RECEPTOR_TYR_KIN_V_1
 PS00791; RECEPTOR_TYR_KIN_V_2
 PS50105; SAM_DOMAIN 
PRINTS
 PR00109; TYRKINASE.