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0EPHA8_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameEPHA8
DescriptionEphrin type-a receptor 8 precursor (ec 2.7.1.112) (tyrosine-protein kinase receptor eek) (eph-and elk-related kinase) (hek3).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016021 integral to membrane (TAS)
0005886 plasma membrane (TAS)
0004871 signal transducer activity (TAS)
0006468 protein amino acid phosphorylation (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Protein kinases comprise a large family of enzymes that mediate the response of eukaryotic cells to external stimuli by phosphorylation of hydroxyamino acids. The enzymes fall into two broad classes.haracterised with respect to substrate specificity: serine/threonine specific and tyrosine specific . Tyrosine phosphorylating activity was originally detected in two viral transforming proteins .ut many retroviral transforming proteins and their cellular counterparts have since been shown to possess such activity. The growth factor receptors.hich are activated by ligand binding.nd theinsulin-related peptide receptor.re also family members.
  IPR001245:Tyrosine protein kinase
The sterile alpha motif (SAM) domain is a putative protein interaction module present in a wide variety of proteins involved in many biological processes. The SAM domain that spreads over around 70 residues is found in diverse eukaryotic organisms . SAM domains have been shown to homo- and hetero-oligomerise.orming multiple self-association architectures and also binding to various non-SAM domain-containing proteins .evertheless with a low affinity constant . SAM domains also appear to possess the ability to bind RNA . Smaug a protein that helps to establish a morphogen gradient in Drosophila embryos by repressing the translation of nanos (nos) mRNA binds to the 3 untranslated region (UTR) of nos mRNA via two similar hairpin structures. The 3D crystal structure of the Smaug RNA-binding region shows a cluster of positively charged residues on the Smaug-SAM domain.hich could be the RNA-binding surface. This electropositive potential is unique among all previously determined SAM-domain structures and is conserved among Smaug-SAM homologs. These results suggest that the SAM domain might have a primary role in RNA binding. Structural analyses show that the SAM domain is arranged in a small five-helix bundle with two large interfaces . In the case of the SAM domain of EphB2.ach of these interfaces is able to form dimers. The presence of these two distinct intermonomers binding surface suggest that SAM could form extended polymeric structures .
  IPR001660:Sterile alpha motif SAM
Fibronectins are multi-domain glycoproteins found in a soluble form in plasma.nd in an insoluble form in loose connective tissue and basement membranes . They contain multiple copies of 3 repeat regions (types I.I and III).hich bind to a variety of substances including heparin.ollagen.NA.ctin.ibrin and fibronectin receptors on cell surfaces. The wide variety of these substances means that fibronectins are involved in a number of important functions: e.g..ound healing; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellular cytoskeleton; and tumour metastasis . The role of fibronectin in cell differentiation is demonstrated by the marked reduction in the expression of its gene when neoplastic transformation occurs. Cell attachment has been found to be mediated by the binding of the tetrapeptide RGDS to integrins on the cell surface .lthough related sequences can also display cell adhesion activity.Plasma fibronectin occurs as a dimer of 2 different subunits.inked together by 2 disulphide bonds near the C-terminus. The difference in the 2 chains occurs in the type III repeat region and is caused by alternative splicing of the mRNA from one gene . The observation that.n a given protein.n individual repeat of one of the 3 types (e.g..he first FnIII repeat) shows much less similarity to its subsequent tandem repeats within that protein than to its equivalent repeat between fibronectins from other species.as suggested that the repeating structure of fibronectin arose at an early stage of evolution. It also seems to suggest that the structure is subject to high selective pressure .The fibronectin type III repeat region is an approximately 100 amino acid domain.ifferent tandem repeats of which contain binding sites for DNA.eparin and the cell surface . The superfamily of sequences believed to contain FnIII repeats represents 45 different families.he majority of which are involved in cell surface binding in some manner.r are receptor protein tyrosine kinases.r cytokine receptors.
  IPR003961:Fibronectin, type III
Eukaryotic protein kinases are enzymesthat belong to a very extensive family of proteins which share a conserved catalytic core common withboth serine/threonine and tyrosine protein kinases. There are a number of conserved regions in thecatalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is aglycine-rich stretch of residues in the vicinity of a lysine residue.hich has been shown to be involvedin ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residuewhich is important for the catalytic activity of the enzyme . This entry includes protein kinases from eukaryotes and viruses and may include some bacterial hits too.
  IPR000719:Protein kinase
Interactions between the Eph receptor tyrosine kinases and their membrane-bound ligands.phrins are promiscuous.ut largely fall into two groups: EphA receptors bind to GPI-anchored ephrin-A ligands.hile EphB receptors bind to ephrin-B proteins that have a transmembrane and cytoplasmic domain . Remarkably.phrin-B proteins transduce signals.uch that bidirectional signaling can occur upon interaction with Eph receptor. An importantrole of Eph receptors and ephrins is to mediate cell-contact-dependent repulsion. Eph receptors and ephrins also act at boundaries to channel neuronal growth cones along specific pathways.estrict the migration of neural crest cells.nd via bidirectional signaling prevent intermingling between hindbrain segments. Intriguingly.ph receptors and ephrins can also trigger an adhesiveresponse of endothelial cells and are required for the remodeling ofblood vessels .Biochemical studies suggest that the extent of multimerization ofEph receptors modulates the cellular response and that the actincytoskeleton is one major target of the intracellular pathways activated by Eph receptors .Eph receptors and ephrins have thus emerged as key regulators of therepulsion and adhesion of cells that underlie the establishment.aintenance.nd remodeling of patterns of cellular organization .
  IPR001090:Ephrin receptor, ligand binding
Fibronectins are multi-domain glycoproteins found in a soluble form in plasma.nd in an insoluble form in loose connective tissue and basement membranes . They contain multiple copies of 3 repeat regions (types I.I and III).hich bind to a variety of substances including heparin.ollagen.NA.ctin.ibrin and fibronectin receptors on cell surfaces. The wide variety of these substances means that fibronectins are involved in a number of important functions: e.g..ound healing; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellular cytoskeleton; and tumour metastasis . The role of fibronectin in cell differentiation is demonstrated by the marked reduction in the expression of its gene when neoplastic transformation occurs. Cell attachment has been found to be mediated by the binding of the tetrapeptide RGDS to integrins on the cell surface .lthough related sequences can also display cell adhesion activity.Plasma fibronectin occurs as a dimer of 2 different subunits.inked together by 2 disulphide bonds near the C-terminus. The difference in the 2 chains occurs in the type III repeat region and is caused by alternative splicing of the mRNA from one gene . The observation that.n a given protein.n individual repeat of one of the 3 types (e.g..he first FnIII repeat) shows much less similarity to its subsequent tandem repeats within that protein than to its equivalent repeat between fibronectins from other species.as suggested that the repeating structure of fibronectin arose at an early stage of evolution. It also seems to suggest that the structure is subject to high selective pressure .The fibronectin type III repeat region is an approximately 100 amino acid domain.ifferent tandem repeats of which contain binding sites for DNA.eparin and the cell surface . The superfamily of sequences believed to contain FnIII repeats represents 45 different families.he majority of which are involved in cell surface binding in some manner.r are receptor protein tyrosine kinases.r cytokine receptors.
  IPR003962:Fibronectin, type III subdomain
Fibronectin is composed of three repeating structural motifs.f which one is the FnIII module. The three modules form a linear sequence of multiple tandem copies connected by short linker peptides. The secondary structure of the FnIII10 module.hich is the only fibronectin module to possess an integrin binding RGD motif.onsists of two beta-sheets containing the antiparallel beta-strands ABE and DCFG.espectively.hich fold up to form a beta-sandwich. The RGD sequence is located in the loop connecting the beta-strands .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008957:Fibronectin, type III-like fold
Proteins containing a galactose-binding domain-like fold can be found in several different protein families.n both eukaryotes and prokaryotes. The common function of these domains is to bind to specific ligands.uch as cell-surface-attached carbohydrate substrates for galactose oxidase and sialidase .hospholipids on the outer side of the mammalian cell membrane for coagulation factor Va .embrane-anchored ephrin for the Eph family of receptor tyrosine kinases .nd a complex of broken single-stranded DNA and DNA polymerase beta for XRCC1 . The structure of the galactose-binding domain-like members consists of a beta-sandwich.n which the strands making up the sheets exhibit a jellyroll fold. There is a high degree of similarity in the beta-sandwich and in the loops between different family members.espite an often low level of sequence similarity.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008979:Galactose-binding like
Protein kinases () catalyze the phosphotransfer reaction fundamental to most signalling and regulatory processes in the eukaryotic cell . The catalytic subunit contains a core that is common to both serine/threonine and tyrosine protein kinases. The catalytic domain contains the nucleotide-binding site and the catalytic apparatus in an inter-lobe cleft. Structurally it shares functional and structural similarities with the ATP-grasp fold.hich is found in enzymes that catalyse the formation of an amide bond.nd with PIPK (phosphoinositol phosphate kinase). The three-dimensional fold of the protein kinase catalytic domain is similar to domains found in several other proteins. These include the catalytic domain of actin-fragmin kinase.n atypical protein kinase that regulates the F-actin capping activity in plasmodia ; the catalytic domain of phosphoinositide-3-kinase (PI3K).hich phosphorylates phosphoinositides and as such is involved in a number of fundamental cellular processes such as apoptosis.roliferation.otility and adhesion ; the catalytic domain of the MHCK/EF2 kinase.n atypical protein kinase that includes the TRP (transient channel potential) calcium-channel kinase involved in the modulation of calcium channels in eukaryotic cells in response to external signals ; choline kinase.hich catalyses the ATP-dependent phosphorylation of choline during the biosynthesis of phosphatidylcholine ; and 3.-aminoglycoside phosphotransferase type IIIa. bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics .
  IPR011009:Protein kinase-like
Sterile alpha motif (SAM) domains are known to be involved in diverse protein-protein interactions.ssociating with both SAM-containing and non-SAM-containing proteins pathway . SAM domains exhibit a conserved structure.onsisting of a 4-5-helical bundle of two orthogonally packed alpha-hairpins. However SAM domains display a diversity of function.eing involved in interactions with proteins.NA and RNA . The name sterile alpha motif arose from its presence in proteins that are essential for yeast sexual differentiation. The SAM domain has had various names.ncluding SPM.TN (pointed).EP (yeast sterility.ts-related.cG proteins).CR (N-terminal conserved region) and HLH (helix-loop-helix) domain.ll of which are related and can be classified as SAM domains. SAM domains occur in eukaryotic and in some bacterial proteins. Structures have been determined for several proteins that contain SAM domains.ncluding Ets-1 transcription factor.hich plays a role in the development and invasion of tumour cells by regulating the expression of matrix-degrading proteases ; Etv6 transcription factor.ene rearrangements of which have been demonstrated in several malignancies ; EphA4 receptor tyrosine kinase.hich is believed to be important for the correct localization of a motoneuron pool to a specific position in the spinal cord ; EphB2 receptor.hich is involved in spine morphogenesis via intersectin.dc42 and N-Wasp ; p73. p53 homologue involved in neuronal development ; and polyhomeotic.hich is a member of the Polycomb group of genes (Pc-G) required for the maintenance of the spatial expression pattern of homeotic genes .
  IPR013761:Sterile alpha motif-type
IPR001245:Pkinase_Tyr 
Evalue:-141.657577514648 
Location:635-892IPR001090:Ephrin_lbd 
Evalue:-135.187088012695 
Location:31-204IPR001660:SAM_1 
Evalue:-25.8538722991943 
Location:931-992IPR003961:fn3 
Evalue:-21.2291488647461 
Location:437-524IPR003961:fn3 
Evalue:-9.36653137207031 
Location:329-425IPR001426:RECEPTOR_TYR_KIN_V_2 
Evalue:0 
Location:247-267IPR000719:Prot_kinase 
Evalue:0 
Location:5-21
SequencesProtein: EPHA8_HUMAN (1005 aa)
mRNA: NM_020526
Local Annotation
Synapse Ontology
the plasma membrane of the postsynaptic neuron. It apposes with presynaptic actiove zone.
sdb:0108 postsynaptic plasma membrane  (Evidence:keywords)
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentK05109
  Level 3 annotation:
    Eph receptor A8
  Level 2 annotation:
    Cytokine receptors
    Axon guidance
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 74 residues, 22762590-22762809Exon2: 23 residues, 22768368-22768433Exon3: 223 residues, 22775296-22775960Exon4: 54 residues, 22785559-22785715Exon5: 114 residues, 22787950-22788286Exon6: 43 residues, 22792405-22792530Exon7: 56 residues, 22792603-22792766Exon8: 33 residues, 22794309-22794403Exon9: 24 residues, 22795185-22795253Exon10: 57 residues, 22796391-22796556Exon11: 64 residues, 22796755-22796941Exon12: 22 residues, 22797230-22797292Exon13: 72 residues, 22797917-22798127Exon14: 52 residues, 22799740-22799890Exon15: 65 residues, 22799977-22800168Exon16: 60 residues, 22800379-22800553Exon17: 658 residues, 22800706-22802674Exon18: 2 residues, -Jump to EPHA8_HUMAN  
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