Domains within Homo sapiens protein EPHA3_HUMAN (P29320)

Ephrin type-A receptor 3

Alternative representations: 1 /

Protein length983 aa
Source databaseUniProt
Identifiers EPHA3_HUMAN, P29320, ENSP00000337451.2, ENSP00000337451, Q9H2V3, Q9H2V4, A0A140VJJ0_HUMAN, A0A140VJJ0
Source gene ENSG00000044524
Alternative splicing EPHA3_HUMAN, P29320-2, C9JXA2_HUMAN

Domain architecture analysis

Display all proteins with similar:

Domain organisationProteins having all the domains as the query in the same order. Additional domains are allowed.
Domain compositionProteins with the same domain composition have at least one copy of each of the domains of the query.

This domain architecture was probably invented with the emergence of Coelomata

Predicted functional partners

EPHA3_HUMAN is shown as EPHA3 in the network

Click and drag to pan the network, and zoom by using your mouse wheel. Click the protein nodes for additional options.

The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.

Open the STRING annotation page for EPHA3

Protein EPHA3_HUMAN is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map04360Axon guidance

KEGG orthologous groups

KONameDescription
K08852ERN1serine/threonine-protein kinase/endoribonuclease IRE1 [EC:2.7.11.1 3.1.26.-]
K05105EPHA4, SEK, TYRO1Eph receptor A4 [EC:2.7.10.1]
K05104EPHA3, HEK, TYRO4Eph receptor A3 [EC:2.7.10.1]
K05112EPHB3, HEK2, ETK2Eph receptor B3 [EC:2.7.10.1]

Post-translational modifications

PTM annotation is taken from PTMcode, a resource of known and predicted functional associations between protein post-translational modifications (PTMs). There are 28 PTMs annotated in this protein:

PTMCount
Phosphorylation21
Ubiquitination3
N-linked glycosylation3
Acetylation1

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein EPHA3.

Orthologous groups

Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 9606.ENSP00000337451 in eggNOG.

OGTaxonomic classDescription
LCOG0478All organisms (root)serine/threonine-protein kinase/endoribonuclease IRE1 [EC:2.7.11.1 3.1.26.-],RAC serine/threonine-protein kinase [EC:2.7.11.1],pto-interacting protein 1 [EC:2.7.11.1]
KOG0196Eukaryota (superkingdom)Eph receptor A4 [EC:2.7.10.1],Eph receptor B1 [EC:2.7.10.1],Eph receptor B3 [EC:2.7.10.1]
HW3AUMetazoa (kingdom)Eph receptor A4 [EC:2.7.10.1],Eph receptor B1 [EC:2.7.10.1],Eph receptor B3 [EC:2.7.10.1]
93RHFChordata (phylum)Eph receptor B3 [EC:2.7.10.1],Eph receptor B2 [EC:2.7.10.1],Eph receptor A4 [EC:2.7.10.1]
5R0EBSarcopterygii (superclass)Eph receptor A4 [EC:2.7.10.1],EphA7 [EC:2.7.10.1],Eph receptor A6 [EC:2.7.10.1]
8ZJWKMammalia (class)Eph receptor A4 [EC:2.7.10.1],EphA7 [EC:2.7.10.1],Eph receptor A6 [EC:2.7.10.1]
4RA5NEuarchontoglires (superorder)Eph receptor A3 [EC:2.7.10.1]
4ZVMZPrimates (order)Eph receptor A3 [EC:2.7.10.1]
98INRHaplorrhini (suborder)Eph receptor A3 [EC:2.7.10.1]
BV8EMSimiiformes (infraorder)Eph receptor A3 [EC:2.7.10.1]
9EXPACatarrhini (parvorder)Eph receptor A3 [EC:2.7.10.1]
7KIM6Opisthokonta (clade)Eph receptor A4 [EC:2.7.10.1],Eph receptor B1 [EC:2.7.10.1],Eph receptor B3 [EC:2.7.10.1]
9GNB8Vertebrata (clade)Eph receptor A4 [EC:2.7.10.1],Eph receptor A6 [EC:2.7.10.1],EphA7 [EC:2.7.10.1]
H4NP0Bilateria (clade)Eph receptor A4 [EC:2.7.10.1],Eph receptor B1 [EC:2.7.10.1],Eph receptor B3 [EC:2.7.10.1]
FWYTPHominoidea (superfamily)Eph receptor A3 [EC:2.7.10.1]
5MZYRHominidae (family)Eph receptor A3 [EC:2.7.10.1]
5Y1YAHomininae (subfamily)Eph receptor A3 [EC:2.7.10.1]

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.

Confidently predicted domains, repeats, motifs and features:

Outlier homologues and homologues of known structure:

Features NOT shown in the diagram: