Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ephrin-A1

Gene

EFNA1

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

Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. Plays an important role in angiogenesis and tumor neovascularization. The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. Exerts anti-oncogenic effects in tumor cells through activation and down-regulation of EPHA2. Activates EPHA2 by inducing tyrosine phosphorylation which leads to its internalization and degradation. Acts as a negative regulator in the tumorigenesis of gliomas by down-regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal growth cone and regulates dendritic spine morphogenesis.2 Publications

<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

  • ephrin receptor binding Source: UniProtKB
  • signaling receptor binding Source: ProtInc

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

Biological processAngiogenesis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
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

More...
SignaLinki
P20827

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P20827

<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-A1
Alternative name(s):
EPH-related receptor tyrosine kinase ligand 1
Short name:
LERK-1
Immediate early response protein B61
Tumor necrosis factor alpha-induced protein 4
Short name:
TNF alpha-induced protein 4
Cleaved into the following chain:
<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:EFNA1
Synonyms:EPLG1, LERK1, TNFAIP4
<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

More...
EuPathDBi
HostDB:ENSG00000169242.11

Human Gene Nomenclature Database

More...
HGNCi
HGNC:3221 EFNA1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
191164 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P20827

<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

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

<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

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNET

More...
DisGeNETi
1942

Open Targets

More...
OpenTargetsi
ENSG00000169242

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA27656

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
EFNA1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
73920206

<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 – 181 PublicationAdd BLAST18
<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_000000835319 – 182Ephrin-A1Add BLAST164
ChainiPRO_000038963019 – ?Ephrin-A1, secreted form
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000008354183 – 205Removed in mature formSequence analysisAdd BLAST23

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi26N-linked (GlcNAc...) asparagine2 Publications1
<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 bondi51 ↔ 92Combined sources2 Publications
Disulfide bondi80 ↔ 140Combined sources2 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi182GPI-anchor amidated serineSequence analysis1

<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

Undergoes proteolysis by a metalloprotease to give rise to a soluble monomeric form.
N-Glycosylation is required for binding to EPHA2 receptor and inducing its internalization.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P20827

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P20827

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P20827

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

More...
PaxDbi
P20827

PeptideAtlas

More...
PeptideAtlasi
P20827

PRoteomics IDEntifications database

More...
PRIDEi
P20827

ProteomicsDB human proteome resource

More...
ProteomicsDBi
53809
53810 [P20827-2]

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
1209

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P20827

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

More...
PhosphoSitePlusi
P20827

<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

Brain. Down-regulated in primary glioma tissues compared to the normal tissues. The soluble monomeric form is expressed in the glioblastoma multiforme (GBM) and breast cancer cells (at protein level).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

By TNF and IL1B/interleukin-1 beta.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000169242 Expressed in 210 organ(s), highest expression level in right lobe of liver

CleanEx database of gene expression profiles

More...
CleanExi
HS_EFNA1

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P20827 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB032498

<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

Monomer. Homodimer. Forms heterodimers with EPHA2. Binds to the receptor tyrosine kinases EPHA2, EPHA3, EPHA4, EPHA5, EPHA6 and EPHA7. Also binds with low affinity to EPHA1.3 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

WithEntry#Exp.IntActNotes
EPHA2P293179EBI-715194,EBI-702104

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
108262, 8 interactors

Database of interacting proteins

More...
DIPi
DIP-98N

Protein interaction database and analysis system

More...
IntActi
P20827, 9 interactors

Molecular INTeraction database

More...
MINTi
P20827

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000357392

<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

1205
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
3CZUX-ray2.65B17-171[»]
3HEIX-ray2.00B/D/F/H/J/L/N/P18-147[»]
3MBWX-ray2.81B17-171[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P20827

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

More...
SMRi
P20827

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P20827

<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>Domaini19 – 151Ephrin RBDPROSITE-ProRule annotationAdd BLAST133

<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 ephrin family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3858 Eukaryota
ENOG4111FMJ LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000159919

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000234373

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG051447

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P20827

KEGG Orthology (KO)

More...
KOi
K05462

Identification of Orthologs from Complete Genome Data

More...
OMAi
PIHHQED

Database of Orthologous Groups

More...
OrthoDBi
1094764at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P20827

Family and domain databases

Conserved Domains Database

More...
CDDi
cd10425 Ephrin-A_Ectodomain, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.420, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008972 Cupredoxin
IPR031328 Ephrin
IPR034252 Ephrin-A_Ecto
IPR019765 Ephrin_CS
IPR001799 Ephrin_RBD

The PANTHER Classification System

More...
PANTHERi
PTHR11304 PTHR11304, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00812 Ephrin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01347 EPHRIN

ProDom; a protein domain database

More...
ProDomi
View protein in ProDom or Entries sharing at least one domain
PD002533 Ephrin, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49503 SSF49503, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01299 EPHRIN_RBD_1, 1 hit
PS51551 EPHRIN_RBD_2, 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: P20827-1) [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
MEFLWAPLLG LCCSLAAADR HTVFWNSSNP KFRNEDYTIH VQLNDYVDII
60 70 80 90 100
CPHYEDHSVA DAAMEQYILY LVEHEEYQLC QPQSKDQVRW QCNRPSAKHG
110 120 130 140 150
PEKLSEKFQR FTPFTLGKEF KEGHSYYYIS KPIHQHEDRC LRLKVTVSGK
160 170 180 190 200
ITHSPQAHDN PQEKRLAADD PEVRVLHSIG HSAAPRLFPL AWTVLLLPLL

LLQTP
Length:205
Mass (Da):23,787
Last modified:August 30, 2005 - 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:iEFF026BF4C12461F
GO
Isoform 2 (identifier: P20827-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     131-152: Missing.

Note: No experimental confirmation available.
Show »
Length:183
Mass (Da):21,246
Checksum:i8B9A70B6402577BD
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 conflicti180G → A in AAH32698 (PubMed:15489334).Curated1

Natural variant

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_014791159D → V4 PublicationsCorresponds to variant dbSNP:rs4745Ensembl.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_017543131 – 152Missing in isoform 2. CuratedAdd BLAST22

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
M57730 mRNA Translation: AAA58388.1
CR457416 mRNA Translation: CAG33697.1
AL691442 Genomic DNA No translation available.
CH471121 Genomic DNA Translation: EAW53131.1
CH471121 Genomic DNA Translation: EAW53132.1
BC032698 mRNA Translation: AAH32698.1
BC095432 mRNA Translation: AAH95432.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS1091.1 [P20827-1]
CCDS1092.1 [P20827-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
A36377

NCBI Reference Sequences

More...
RefSeqi
NP_004419.2, NM_004428.2 [P20827-1]
NP_872626.1, NM_182685.1 [P20827-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.516664
Hs.630847

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000368406; ENSP00000357391; ENSG00000169242 [P20827-2]
ENST00000368407; ENSP00000357392; ENSG00000169242 [P20827-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1942

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1942

UCSC genome browser

More...
UCSCi
uc001fhh.4 human [P20827-1]

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57730 mRNA Translation: AAA58388.1
CR457416 mRNA Translation: CAG33697.1
AL691442 Genomic DNA No translation available.
CH471121 Genomic DNA Translation: EAW53131.1
CH471121 Genomic DNA Translation: EAW53132.1
BC032698 mRNA Translation: AAH32698.1
BC095432 mRNA Translation: AAH95432.1
CCDSiCCDS1091.1 [P20827-1]
CCDS1092.1 [P20827-2]
PIRiA36377
RefSeqiNP_004419.2, NM_004428.2 [P20827-1]
NP_872626.1, NM_182685.1 [P20827-2]
UniGeneiHs.516664
Hs.630847

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CZUX-ray2.65B17-171[»]
3HEIX-ray2.00B/D/F/H/J/L/N/P18-147[»]
3MBWX-ray2.81B17-171[»]
ProteinModelPortaliP20827
SMRiP20827
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108262, 8 interactors
DIPiDIP-98N
IntActiP20827, 9 interactors
MINTiP20827
STRINGi9606.ENSP00000357392

PTM databases

GlyConnecti1209
iPTMnetiP20827
PhosphoSitePlusiP20827

Polymorphism and mutation databases

BioMutaiEFNA1
DMDMi73920206

Proteomic databases

EPDiP20827
jPOSTiP20827
MaxQBiP20827
PaxDbiP20827
PeptideAtlasiP20827
PRIDEiP20827
ProteomicsDBi53809
53810 [P20827-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1942
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368406; ENSP00000357391; ENSG00000169242 [P20827-2]
ENST00000368407; ENSP00000357392; ENSG00000169242 [P20827-1]
GeneIDi1942
KEGGihsa:1942
UCSCiuc001fhh.4 human [P20827-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1942
DisGeNETi1942
EuPathDBiHostDB:ENSG00000169242.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
EFNA1

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0116282
HIX0116386
HGNCiHGNC:3221 EFNA1
HPAiCAB032498
MIMi191164 gene
neXtProtiNX_P20827
OpenTargetsiENSG00000169242
PharmGKBiPA27656

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3858 Eukaryota
ENOG4111FMJ LUCA
GeneTreeiENSGT00940000159919
HOGENOMiHOG000234373
HOVERGENiHBG051447
InParanoidiP20827
KOiK05462
OMAiPIHHQED
OrthoDBi1094764at2759
PhylomeDBiP20827

Enzyme and pathway databases

ReactomeiR-HSA-2682334 EPH-Ephrin signaling
R-HSA-3928663 EPHA-mediated growth cone collapse
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
SignaLinkiP20827
SIGNORiP20827

Miscellaneous databases

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

More...
ChiTaRSi
EFNA1 human
EvolutionaryTraceiP20827

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Ephrin_A1

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

More...
GenomeRNAii
1942

Protein Ontology

More...
PROi
PR:P20827

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000169242 Expressed in 210 organ(s), highest expression level in right lobe of liver
CleanExiHS_EFNA1
GenevisibleiP20827 HS

Family and domain databases

CDDicd10425 Ephrin-A_Ectodomain, 1 hit
Gene3Di2.60.40.420, 1 hit
InterProiView protein in InterPro
IPR008972 Cupredoxin
IPR031328 Ephrin
IPR034252 Ephrin-A_Ecto
IPR019765 Ephrin_CS
IPR001799 Ephrin_RBD
PANTHERiPTHR11304 PTHR11304, 1 hit
PfamiView protein in Pfam
PF00812 Ephrin, 1 hit
PRINTSiPR01347 EPHRIN
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002533 Ephrin, 1 hit
SUPFAMiSSF49503 SSF49503, 1 hit
PROSITEiView protein in PROSITE
PS01299 EPHRIN_RBD_1, 1 hit
PS51551 EPHRIN_RBD_2, 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 nameiEFNA1_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: P20827
Secondary accession number(s): D3DV86
, Q5SR60, Q5SR61, Q6I9T9, Q8N578
<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: February 1, 1991
Last sequence update: August 30, 2005
Last modified: January 16, 2019
This is version 183 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, Direct protein sequencing, Reference proteome

Documents

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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again