CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012545
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ephrin type-A receptor 7 
Protein Synonyms/Alias
 EPH homology kinase 3; EHK-3; EPH-like kinase 11; EK11; hEK11 
Gene Name
 EPHA7 
Gene Synonyms/Alias
 EHK3; HEK11 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
601EELYFHFKFPGTKTYubiquitination[1, 2, 3, 4]
606HFKFPGTKTYIDPETubiquitination[2, 3]
665RDVAVAIKTLKVGYTubiquitination[3]
797VYTTTGGKIPVRWTAubiquitination[2, 3]
892QIVGILDKMIRNPNSubiquitination[1, 2, 3, 4]
941AIKMERYKDNFTAAGubiquitination[3]
975ITLVGHQKKIMSSIQubiquitination[3]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 32 210 Eph LBD.
 DOMAIN 331 433 Fibronectin type-III 1.
 DOMAIN 443 535 Fibronectin type-III 2.
 DOMAIN 633 894 Protein kinase.
 DOMAIN 923 987 SAM.
 NP_BIND 639 647 ATP (By similarity).
 MOTIF 996 998 PDZ-binding (Potential).
 ACT_SITE 758 758 Proton acceptor (By similarity).
 BINDING 665 665 ATP (By similarity).
 MOD_RES 608 608 Phosphotyrosine; by autocatalysis
 MOD_RES 614 614 Phosphotyrosine; by autocatalysis
 MOD_RES 791 791 Phosphotyrosine; by autocatalysis
 MOD_RES 940 940 Phosphotyrosine; by autocatalysis
 CARBOHYD 343 343 N-linked (GlcNAc...) (Potential).
 CARBOHYD 410 410 N-linked (GlcNAc...) (Potential).  
Keyword
 3D-structure; Alternative splicing; Apoptosis; ATP-binding; Cell membrane; Complete proteome; Developmental protein; Glycoprotein; Kinase; Membrane; Neurogenesis; Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; Signal; Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 998 AA 
Protein Sequence
MVFQTRYPSW IILCYIWLLR FAHTGEAQAA KEVLLLDSKA QQTELEWISS PPNGWEEISG 60
LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV ELKFTLRDCN SLPGVLGTCK 120
ETFNLYYYET DYDTGRNIRE NLYVKIDTIA ADESFTQGDL GERKMKLNTE VREIGPLSKK 180
GFYLAFQDVG ACIALVSVKV YYKKCWSIIE NLAIFPDTVT GSEFSSLVEV RGTCVSSAEE 240
EAENAPRMHC SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RGFYKSSSQD LQCSRCPTHS 300
FSDKEGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE WSPPADNGGR 360
NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV TVMDLLAHAN YTFEVEAVNG 420
VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM KERVLQRSVE LSWQEPEHPN GVITEYEIKY 480
YEKDQRERTY STVKTKSTSA SINNLKPGTV YVFQIRAFTA AGYGNYSPRL DVATLEEATG 540
KMFEATAVSS EQNPVIIIAV VAVAGTIILV FMVFGFIIGR RHCGYSKADQ EGDEELYFHF 600
KFPGTKTYID PETYEDPNRA VHQFAKELDA SCIKIERVIG AGEFGEVCSG RLKLPGKRDV 660
AVAIKTLKVG YTEKQRRDFL CEASIMGQFD HPNVVHLEGV VTRGKPVMIV IEFMENGALD 720
AFLRKHDGQF TVIQLVGMLR GIAAGMRYLA DMGYVHRDLA ARNILVNSNL VCKVSDFGLS 780
RVIEDDPEAV YTTTGGKIPV RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM 840
SNQDVIKAIE EGYRLPAPMD CPAGLHQLML DCWQKERAER PKFEQIVGIL DKMIRNPNSL 900
KTPLGTCSRP ISPLLDQNTP DFTTFCSVGE WLQAIKMERY KDNFTAAGYN SLESVARMTI 960
EDVMSLGITL VGHQKKIMSS IQTMRAQMLH LHGTGIQV 998 
Gene Ontology
 GO:0030425; C:dendrite; IEA:Compara.
 GO:0005887; C:integral to plasma membrane; IEA:InterPro.
 GO:0031594; C:neuromuscular junction; IEA:Compara.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0045211; C:postsynaptic membrane; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008046; F:axon guidance receptor activity; ISS:UniProtKB.
 GO:0045499; F:chemorepellent activity; ISS:UniProtKB.
 GO:0005004; F:GPI-linked ephrin receptor activity; ISS:UniProtKB.
 GO:0007420; P:brain development; ISS:UniProtKB.
 GO:0048755; P:branching morphogenesis of a nerve; ISS:UniProtKB.
 GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB.
 GO:0022407; P:regulation of cell-cell adhesion; ISS:UniProtKB.
 GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
 GO:0070372; P:regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
 GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
 GO:0031952; P:regulation of protein autophosphorylation; ISS:UniProtKB.
 GO:0031290; P:retinal ganglion cell axon guidance; IEA:Compara. 
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.
 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. 
Pfam
 PF01404; Ephrin_lbd
 PF00041; fn3
 PF07699; GCC2_GCC3
 PF07714; Pkinase_Tyr
 PF07647; SAM_2 
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.