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Protein

Ephrin type-A receptor 2

Gene

EPHA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis.9 Publications
(Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei646ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei739Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi619 – 627ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHost cell receptor for virus entry, Kinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processAngiogenesis, Apoptosis, Cell adhesion, Differentiation, Host-virus interaction
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.10.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-2682334 EPH-Ephrin signaling
R-HSA-3928663 EPHA-mediated growth cone collapse
R-HSA-3928665 EPH-ephrin mediated repulsion of cells

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P29317

SIGNOR Signaling Network Open Resource

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SIGNORi
P29317

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ephrin type-A receptor 2 (EC:2.7.10.1)
Alternative name(s):
Epithelial cell kinase
Tyrosine-protein kinase receptor ECK
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:EPHA2
Synonyms:ECK
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000142627.12

Human Gene Nomenclature Database

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HGNCi
HGNC:3386 EPHA2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
176946 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P29317

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini24 – 537ExtracellularSequence analysisAdd BLAST514
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei538 – 558HelicalSequence analysisAdd BLAST21
Topological domaini559 – 976CytoplasmicSequence analysisAdd BLAST418

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Cataract 6, multiple types (CTRCT6)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT6 includes posterior polar and age-related cortical cataracts, among others. Posterior polar cataract is a subcapsular opacity, usually disk-shaped, located at the back of the lens. Age-related cortical cataract is a developmental punctate opacity restricted to the cortex. The cataract is white or cerulean, increases in number with age, but rarely affects vision.
See also OMIM:116600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_062532721R → Q in CTRCT6; retained in the cytoplasm and constitutively active it alters EPHA2 signaling. 1 PublicationCorresponds to variant dbSNP:rs116506614EnsemblClinVar.1
Natural variantiVAR_058907940T → I in CTRCT6; reduced protein stability and reduced ability to stimulate cell migration in absence of its ephrin ligand. 2 PublicationsCorresponds to variant dbSNP:rs137853200EnsemblClinVar.1
Natural variantiVAR_058908948G → W in CTRCT6; reduced protein stability and reduced ability to stimulate cell migration in absence of its ephrin ligand. 2 PublicationsCorresponds to variant dbSNP:rs137853199EnsemblClinVar.1
Overexpressed in several cancer types and promotes malignancy.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi103R → E: Significantly reduced response to EFNA1. 1 Publication1
Mutagenesisi646K → M: Loss of kinase activity. 1 Publication1
Mutagenesisi739D → N: Increases serum-induced chemotaxis. Loss of EFNA1-dependent regulation of cell migration. 1 Publication1
Mutagenesisi897S → A or D: Loss of serum-induced phosphorylation by PKB. Loss of serum-induced chemotaxis. 1 Publication1

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
1969

MalaCards human disease database

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MalaCardsi
EPHA2
MIMi116600 phenotype

Open Targets

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OpenTargetsi
ENSG00000142627

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
98991 Early-onset nuclear cataract
98993 Early-onset posterior polar cataract
441447 Early-onset posterior subcapsular cataract
98994 Total early-onset cataract

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27818

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2068

Drug and drug target database

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DrugBanki
DB01254 Dasatinib
DB04395 Phosphoaminophosphonic Acid-Adenylate Ester
DB08896 Regorafenib

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1822

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
EPHA2

Domain mapping of disease mutations (DMDM)

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DMDMi
229462861

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 23Sequence analysisAdd BLAST23
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001680024 – 976Ephrin type-A receptor 2Add BLAST953

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi70 ↔ 188
Disulfide bondi105 ↔ 115
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi407N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi435N-linked (GlcNAc...) asparagine1 Publication1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei570PhosphoserineCombined sources1
Modified residuei575PhosphotyrosineCombined sources1
Modified residuei579PhosphoserineCombined sources1
Modified residuei588Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei594PhosphotyrosineBy similarity1
Modified residuei628PhosphotyrosineCombined sources1
Modified residuei647PhosphothreonineCombined sources1
Modified residuei735Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei772PhosphotyrosineBy similarity1
Modified residuei869PhosphoserineCombined sources1
Modified residuei892PhosphoserineCombined sources1
Modified residuei897Phosphoserine; by PKB/AKT1, RPS6KA1, RPS6KA3 AND PKACombined sources3 Publications1
Modified residuei901PhosphoserineCombined sources1 Publication1
Modified residuei921Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei930Phosphotyrosine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylates. Phosphorylated on tyrosine upon binding and activation by EFNA1. Phosphorylated residues Tyr-588 and Tyr-594 are required for binding VAV2 and VAV3 while phosphorylated residues Tyr-735 and Tyr-930 are required for binding PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3). These phosphorylated residues are critical for recruitment of VAV2 and VAV3 and PI3-kinase p85 subunit which transduce downstream signaling to activate RAC1 GTPase and cell migration. Dephosphorylation of Tyr-930 by PTPRF prevents the interaction of EPHA2 with NCK1. Phosphorylated at Ser-897 by PKB; serum-induced phosphorylation which targets EPHA2 to the cell leading edge and stimulates cell migration. Phosphorylation by PKB is inhibited by EFNA1-activated EPHA2 which regulates PKB activity via a reciprocal regulatory loop. Phosphorylated at Ser-897 in response to TNF by RPS6KA1 and RPS6KA3; RPS6KA-EPHA2 signaling pathway controls cell migration (PubMed:26158630). Phosphorylated at Ser-897 by PKA; blocks cell retraction induced by EPHA2 kinase activity (PubMed:27385333). Dephosphorylated by ACP1.6 Publications
Ubiquitinated by CHIP/STUB1. Ubiquitination is regulated by the HSP90 chaperone and regulates the receptor stability and activity through proteasomal degradation. ANKS1A prevents ubiquitination and degradation (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P29317

MaxQB - The MaxQuant DataBase

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MaxQBi
P29317

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P29317

PeptideAtlas

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PeptideAtlasi
P29317

PRoteomics IDEntifications database

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PRIDEi
P29317

ProteomicsDB human proteome resource

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ProteomicsDBi
54535

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
777

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P29317

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P29317

SwissPalm database of S-palmitoylation events

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SwissPalmi
P29317

UniCarbKB; an annotated and curated database of glycan structures

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UniCarbKBi
P29317

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in brain and glioma tissue and glioma cell lines (at protein level). Expressed most highly in tissues that contain a high proportion of epithelial cells, e.g. skin, intestine, lung, and ovary.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by UV irradiation via a TP53-independent, MAPK-dependent mechanism.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000142627 Expressed in 168 organ(s), highest expression level in ectocervix

CleanEx database of gene expression profiles

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CleanExi
HS_EPHA2

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P29317 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P29317 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB010464

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. Interacts with SLA. Interacts (phosphorylated form) with VAV2, VAV3 and PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3); critical for the EFNA1-induced activation of RAC1 which stimulates cell migration (By similarity). Interacts with INPPL1; regulates activated EPHA2 endocytosis and degradation. Interacts (inactivated form) with PTK2/FAK1 and interacts (EFNA1 ligand-activated form) with PTPN11; regulates integrin-mediated adhesion. Interacts with ARHGEF16, DOCK4 and ELMO2; mediates ligand-independent activation of RAC1 which stimulates cell migration. Interacts with CLDN4; phosphorylates CLDN4 and may regulate tight junctions. Interacts with ACP1. Interacts (via SAM domain) with ANKS1A (via SAM domain). Interacts with CEMIP. Interacts with NCK1; may regulate EPHA2 activity in cell migration and adhesion.By similarity10 Publications
(Microbial infection) Interacts with human herpes virus 8/HHV-8 glycoprotein L/gL and glycoprotein H/gH heterodimer; this interaction triggers EPHA2 phosphorylation and endocytosis, allowing virus entry.1 Publication
(Microbial infection) Interacts with Epstein-Barr virus/HHV-4 glycoprotein L/gL and glycoprotein H/gH heterodimer; this interaction facilitates virus internalization and fusion.2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108288, 127 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P29317

Database of interacting proteins

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DIPi
DIP-96N

Protein interaction database and analysis system

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IntActi
P29317, 38 interactors

Molecular INTeraction database

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MINTi
P29317

STRING: functional protein association networks

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STRINGi
9606.ENSP00000351209

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P29317

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1976
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P29317

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P29317

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P29317

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini28 – 206Eph LBDPROSITE-ProRule annotationAdd BLAST179
Domaini328 – 432Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST105
Domaini438 – 529Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST92
Domaini613 – 875Protein kinasePROSITE-ProRule annotationAdd BLAST263
Domaini904 – 968SAMPROSITE-ProRule annotationAdd BLAST65

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 206Mediates interaction with CLDN41 PublicationAdd BLAST206
Regioni606 – 906Mediates interaction with ARHGEF16 and ELMO21 PublicationAdd BLAST301
Regioni886 – 976Negatively regulates interaction with ARHGEF161 PublicationAdd BLAST91

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi974 – 976PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi188 – 325Cys-richAdd BLAST138

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0196 Eukaryota
COG0515 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000160786

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233856

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG062180

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P29317

KEGG Orthology (KO)

More...
KOi
K05103

Identification of Orthologs from Complete Genome Data

More...
OMAi
RQFTKID

Database of Orthologous Groups

More...
OrthoDBi
EOG091G00W0

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P29317

TreeFam database of animal gene trees

More...
TreeFami
TF315608

Family and domain databases

Conserved Domains Database

More...
CDDi
cd10480 EphR_LBD_A2, 1 hit
cd00063 FN3, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.260, 1 hit
2.60.40.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027936 Eph_TM
IPR034263 EphA2_rcpt_lig-bd
IPR001090 Ephrin_rcpt_lig-bd_dom
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR008979 Galactose-bd-like_sf
IPR009030 Growth_fac_rcpt_cys_sf
IPR013783 Ig-like_fold
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001660 SAM
IPR013761 SAM/pointed_sf
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 protein domain database

More...
Pfami
View protein in Pfam
PF14575 EphA2_TM, 1 hit
PF01404 Ephrin_lbd, 1 hit
PF00041 fn3, 2 hits
PF07714 Pkinase_Tyr, 1 hit
PF00536 SAM_1, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000666 TyrPK_ephrin_receptor, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00615 EPH_lbd, 1 hit
SM01411 Ephrin_rec_like, 1 hit
SM00060 FN3, 2 hits
SM00454 SAM, 1 hit
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47769 SSF47769, 1 hit
SSF49265 SSF49265, 1 hit
SSF49785 SSF49785, 1 hit
SSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P29317-1) [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
        10         20         30         40         50
MELQAARACF ALLWGCALAA AAAAQGKEVV LLDFAAAGGE LGWLTHPYGK
60 70 80 90 100
GWDLMQNIMN DMPIYMYSVC NVMSGDQDNW LRTNWVYRGE AERIFIELKF
110 120 130 140 150
TVRDCNSFPG GASSCKETFN LYYAESDLDY GTNFQKRLFT KIDTIAPDEI
160 170 180 190 200
TVSSDFEARH VKLNVEERSV GPLTRKGFYL AFQDIGACVA LLSVRVYYKK
210 220 230 240 250
CPELLQGLAH FPETIAGSDA PSLATVAGTC VDHAVVPPGG EEPRMHCAVD
260 270 280 290 300
GEWLVPIGQC LCQAGYEKVE DACQACSPGF FKFEASESPC LECPEHTLPS
310 320 330 340 350
PEGATSCECE EGFFRAPQDP ASMPCTRPPS APHYLTAVGM GAKVELRWTP
360 370 380 390 400
PQDSGGREDI VYSVTCEQCW PESGECGPCE ASVRYSEPPH GLTRTSVTVS
410 420 430 440 450
DLEPHMNYTF TVEARNGVSG LVTSRSFRTA SVSINQTEPP KVRLEGRSTT
460 470 480 490 500
SLSVSWSIPP PQQSRVWKYE VTYRKKGDSN SYNVRRTEGF SVTLDDLAPD
510 520 530 540 550
TTYLVQVQAL TQEGQGAGSK VHEFQTLSPE GSGNLAVIGG VAVGVVLLLV
560 570 580 590 600
LAGVGFFIHR RRKNQRARQS PEDVYFSKSE QLKPLKTYVD PHTYEDPNQA
610 620 630 640 650
VLKFTTEIHP SCVTRQKVIG AGEFGEVYKG MLKTSSGKKE VPVAIKTLKA
660 670 680 690 700
GYTEKQRVDF LGEAGIMGQF SHHNIIRLEG VISKYKPMMI ITEYMENGAL
710 720 730 740 750
DKFLREKDGE FSVLQLVGML RGIAAGMKYL ANMNYVHRDL AARNILVNSN
760 770 780 790 800
LVCKVSDFGL SRVLEDDPEA TYTTSGGKIP IRWTAPEAIS YRKFTSASDV
810 820 830 840 850
WSFGIVMWEV MTYGERPYWE LSNHEVMKAI NDGFRLPTPM DCPSAIYQLM
860 870 880 890 900
MQCWQQERAR RPKFADIVSI LDKLIRAPDS LKTLADFDPR VSIRLPSTSG
910 920 930 940 950
SEGVPFRTVS EWLESIKMQQ YTEHFMAAGY TAIEKVVQMT NDDIKRIGVR
960 970
LPGHQKRIAY SLLGLKDQVN TVGIPI
Length:976
Mass (Da):108,266
Last modified:May 5, 2009 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i845D7E1BBCCAACCC
GO
Isoform 2 (identifier: P29317-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     477-497: GDSNSYNVRRTEGFSVTLDDL → VTPRGAGLALAGPTAGDRLVT
     498-976: Missing.

Show »
Length:497
Mass (Da):54,305
Checksum:iEB5CEB75AE01F814
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti94 – 99IFIELK → NNFELN in AAA53375 (PubMed:2174105).Curated6

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05598999K → N. Corresponds to variant dbSNP:rs1058372Ensembl.1
Natural variantiVAR_042121391G → R1 PublicationCorresponds to variant dbSNP:rs34192549EnsemblClinVar.1
Natural variantiVAR_042122511T → M1 PublicationCorresponds to variant dbSNP:rs55747232EnsemblClinVar.1
Natural variantiVAR_042123568R → H1 PublicationCorresponds to variant dbSNP:rs56198600Ensembl.1
Natural variantiVAR_055990631M → T. Corresponds to variant dbSNP:rs34021505EnsemblClinVar.1
Natural variantiVAR_062532721R → Q in CTRCT6; retained in the cytoplasm and constitutively active it alters EPHA2 signaling. 1 PublicationCorresponds to variant dbSNP:rs116506614EnsemblClinVar.1
Natural variantiVAR_042124777G → S in a gastric adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs922655349Ensembl.1
Natural variantiVAR_042125876R → H1 PublicationCorresponds to variant dbSNP:rs35903225EnsemblClinVar.1
Natural variantiVAR_058907940T → I in CTRCT6; reduced protein stability and reduced ability to stimulate cell migration in absence of its ephrin ligand. 2 PublicationsCorresponds to variant dbSNP:rs137853200EnsemblClinVar.1
Natural variantiVAR_058908948G → W in CTRCT6; reduced protein stability and reduced ability to stimulate cell migration in absence of its ephrin ligand. 2 PublicationsCorresponds to variant dbSNP:rs137853199EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_056014477 – 497GDSNS…TLDDL → VTPRGAGLALAGPTAGDRLV T in isoform 2. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_056015498 – 976Missing in isoform 2. 1 PublicationAdd BLAST479

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M59371 mRNA Translation: AAA53375.1
EU826606 mRNA Translation: ACF47642.1
AL451042 Genomic DNA No translation available.
CH471167 Genomic DNA Translation: EAW51769.1
BC037166 mRNA Translation: AAH37166.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS169.1 [P29317-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A36355

NCBI Reference Sequences

More...
RefSeqi
NP_004422.2, NM_004431.4 [P29317-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.171596

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000358432; ENSP00000351209; ENSG00000142627 [P29317-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1969

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1969

UCSC genome browser

More...
UCSCi
uc001aya.2 human [P29317-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59371 mRNA Translation: AAA53375.1
EU826606 mRNA Translation: ACF47642.1
AL451042 Genomic DNA No translation available.
CH471167 Genomic DNA Translation: EAW51769.1
BC037166 mRNA Translation: AAH37166.1
CCDSiCCDS169.1 [P29317-1]
PIRiA36355
RefSeqiNP_004422.2, NM_004431.4 [P29317-1]
UniGeneiHs.171596

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MQBX-ray2.30A/B596-900[»]
2E8NNMR-A902-976[»]
2K9YNMR-A/B523-563[»]
2KSONMR-A908-972[»]
2X10X-ray3.00A27-534[»]
2X11X-ray4.83A27-534[»]
3C8XX-ray1.95A23-202[»]
3CZUX-ray2.65A23-202[»]
3FL7X-ray2.50A23-531[»]
3HEIX-ray2.00A/C/E/G/I/K/M/O28-201[»]
3HPNX-ray2.52A/B/C/D/E/F28-201[»]
3KKAX-ray2.40C/D/E903-971[»]
3MBWX-ray2.81A23-326[»]
3MX0X-ray3.51A/C27-435[»]
3SKJX-ray2.50E/F23-202[»]
4P2KX-ray1.50A590-876[»]
4PDOX-ray2.10A/B590-876[»]
4TRLX-ray2.45A590-876[»]
5EK7X-ray1.90A/B583-876[»]
5I9UX-ray1.89A596-900[»]
5I9VX-ray1.46A596-900[»]
5I9WX-ray1.36A596-900[»]
5I9XX-ray1.43A596-900[»]
5I9YX-ray1.23A596-900[»]
5I9ZX-ray1.70A596-900[»]
5IA0X-ray1.95A/B/C596-900[»]
5IA1X-ray2.04A596-900[»]
5IA2X-ray1.62A596-900[»]
5IA3X-ray1.79A596-900[»]
5IA4X-ray1.80A596-900[»]
5IA5X-ray1.78A596-900[»]
5NJZX-ray1.77A596-900[»]
5NK0X-ray1.60A596-900[»]
5NK1X-ray1.55A596-900[»]
5NK2X-ray1.65A596-900[»]
5NK3X-ray1.59A596-900[»]
5NK4X-ray1.45A596-900[»]
5NK5X-ray1.33A596-900[»]
5NK6X-ray1.27A596-900[»]
5NK7X-ray1.89A596-900[»]
5NK8X-ray1.76A596-900[»]
5NK9X-ray1.59A596-900[»]
5NKAX-ray1.38A596-900[»]
5NKBX-ray1.50A596-900[»]
5NKCX-ray1.45A596-900[»]
5NKDX-ray1.41A596-900[»]
5NKEX-ray1.39A596-900[»]
5NKFX-ray1.10A596-900[»]
5NKGX-ray1.10A596-900[»]
5NKHX-ray1.29A596-900[»]
5NKIX-ray1.68A596-900[»]
5NZ9NMR-A945-969[»]
6B9LX-ray3.20A/B/C/D27-200[»]
6F7MNMR-A945-969[»]
6F7NNMR-A951-963[»]
6FNFX-ray1.56A596-900[»]
6FNGX-ray1.04A596-900[»]
6FNHX-ray1.38A/B/C596-900[»]
ProteinModelPortaliP29317
SMRiP29317
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108288, 127 interactors
CORUMiP29317
DIPiDIP-96N
IntActiP29317, 38 interactors
MINTiP29317
STRINGi9606.ENSP00000351209

Chemistry databases

BindingDBiP29317
ChEMBLiCHEMBL2068
DrugBankiDB01254 Dasatinib
DB04395 Phosphoaminophosphonic Acid-Adenylate Ester
DB08896 Regorafenib
GuidetoPHARMACOLOGYi1822

PTM databases

GlyConnecti777
iPTMnetiP29317
PhosphoSitePlusiP29317
SwissPalmiP29317
UniCarbKBiP29317

Polymorphism and mutation databases

BioMutaiEPHA2
DMDMi229462861

Proteomic databases

EPDiP29317
MaxQBiP29317
PaxDbiP29317
PeptideAtlasiP29317
PRIDEiP29317
ProteomicsDBi54535

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1969
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358432; ENSP00000351209; ENSG00000142627 [P29317-1]
GeneIDi1969
KEGGihsa:1969
UCSCiuc001aya.2 human [P29317-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1969
DisGeNETi1969
EuPathDBiHostDB:ENSG00000142627.12

GeneCards: human genes, protein and diseases

More...
GeneCardsi
EPHA2
HGNCiHGNC:3386 EPHA2
HPAiCAB010464
MalaCardsiEPHA2
MIMi116600 phenotype
176946 gene
neXtProtiNX_P29317
OpenTargetsiENSG00000142627
Orphaneti98991 Early-onset nuclear cataract
98993 Early-onset posterior polar cataract
441447 Early-onset posterior subcapsular cataract
98994 Total early-onset cataract
PharmGKBiPA27818

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0196 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000160786
HOGENOMiHOG000233856
HOVERGENiHBG062180
InParanoidiP29317
KOiK05103
OMAiRQFTKID
OrthoDBiEOG091G00W0
PhylomeDBiP29317
TreeFamiTF315608

Enzyme and pathway databases

BRENDAi2.7.10.1 2681
ReactomeiR-HSA-2682334 EPH-Ephrin signaling
R-HSA-3928663 EPHA-mediated growth cone collapse
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
SignaLinkiP29317
SIGNORiP29317

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
EPHA2 human
EvolutionaryTraceiP29317

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
EPH_receptor_A2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
1969

Protein Ontology

More...
PROi
PR:P29317

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000142627 Expressed in 168 organ(s), highest expression level in ectocervix
CleanExiHS_EPHA2
ExpressionAtlasiP29317 baseline and differential
GenevisibleiP29317 HS

Family and domain databases

CDDicd10480 EphR_LBD_A2, 1 hit
cd00063 FN3, 2 hits
Gene3Di2.60.120.260, 1 hit
2.60.40.10, 2 hits
InterProiView protein in InterPro
IPR027936 Eph_TM
IPR034263 EphA2_rcpt_lig-bd
IPR001090 Ephrin_rcpt_lig-bd_dom
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR008979 Galactose-bd-like_sf
IPR009030 Growth_fac_rcpt_cys_sf
IPR013783 Ig-like_fold
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001660 SAM
IPR013761 SAM/pointed_sf
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
PfamiView protein in Pfam
PF14575 EphA2_TM, 1 hit
PF01404 Ephrin_lbd, 1 hit
PF00041 fn3, 2 hits
PF07714 Pkinase_Tyr, 1 hit
PF00536 SAM_1, 1 hit
PIRSFiPIRSF000666 TyrPK_ephrin_receptor, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00615 EPH_lbd, 1 hit
SM01411 Ephrin_rec_like, 1 hit
SM00060 FN3, 2 hits
SM00454 SAM, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF47769 SSF47769, 1 hit
SSF49265 SSF49265, 1 hit
SSF49785 SSF49785, 1 hit
SSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 1 hit
PROSITEiView protein in PROSITE
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEPHA2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P29317
Secondary accession number(s): B5A968, Q8N3Z2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: May 5, 2009
Last modified: December 5, 2018
This is version 219 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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