Domains within Homo sapiens protein ACTN4_HUMAN (O43707)

Alpha-actinin-4

Alternative representations: 1 /

Protein length911 aa
Source databaseUniProt
Identifiers ACTN4_HUMAN, O43707, ENSP00000252699.2, ENSP00000252699, ENSP00000489220.1, ENSP00000489220, A4K467, D6PXK4, O76048, G7NNI8_MACMU, G7NNI8, A0A0S2Z3G9_HUMAN, A0A0S2Z3G9, H2QG89_PANTR, H2QG89, F7HU82_MACMU, F7HU82, A0A2I2YSG9_GORGO, A0A2I2YSG9, A0A2K5TSS4_MACFA, A0A2K5TSS4, A0A0D9QVJ0_CHLSB, A0A0D9QVJ0, A0A2K6ME12_RHIBE, A0A2K6ME12, A0A2K6CAX8_MACNE, A0A2K6CAX8, A0A2K5LEJ8_CERAT, A0A2K5LEJ8, A0A2K6RRL9_RHIRO, A0A2K6RRL9, A0A2K5JXA8_COLAP, A0A2K5JXA8, H2NYP5_PONAB, H2NYP5, A0A2K5YJC3_MANLE, A0A2K5YJC3
Source gene ENSG00000130402
Alternative splicing ACTN4_HUMAN, O43707-2, K7EP19_HUMAN, ENSP00000465176.1, ENSP00000398393.1, F5GXS2_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.

Predicted functional partners

ACTN4_HUMAN is shown as ACTN4 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 ACTN4

Protein ACTN4_HUMAN is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map04510Focal adhesion
map04530Tight junction
map05412Arrhythmogenic right ventricular cardiomyopathy

KEGG orthologous groups

KONameDescription
K21073ACTN2_3actinin alpha 2/3
K05699ACTN1_4actinin alpha 1/4

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 54 PTMs annotated in this protein:

PTMCount
Phosphorylation29
Ubiquitination14
Acetylation9
Nitrosylation2

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein ACTN4.

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.ENSP00000252699 in eggNOG.

OGTaxonomic classDescription
LKOG0035All organisms (root)actinin alpha 1/4,actinin alpha 2/3,EH domain-binding protein 1
KOG0035Eukaryota (superkingdom)actinin alpha 1/4,actinin alpha 2/3,EH domain-binding protein 1
HT95JMetazoa (kingdom)actinin alpha 1/4,actinin alpha 2/3,kindlin 2
93E9WChordata (phylum)actinin alpha 1/4,actinin alpha 2/3
5RBHBSarcopterygii (superclass)actinin alpha 1/4
8Z2GJMammalia (class)actinin alpha 1/4
4R7PWEuarchontoglires (superorder)actinin alpha 1/4
4ZUCZPrimates (order)actinin alpha 1/4
98MSCHaplorrhini (suborder)actinin alpha 1/4
BVC8GSimiiformes (infraorder)actinin alpha 1/4
9ET93Catarrhini (parvorder)actinin alpha 1/4
7MPMDOpisthokonta (clade)actinin alpha 1/4,actinin alpha 2/3,calmodulin
H3JS9Bilateria (clade)actinin alpha 1/4,actinin alpha 2/3
9GU4MVertebrata (clade)actinin alpha 1/4,actinin alpha 2/3
FX3B0Hominoidea (superfamily)actinin alpha 1/4
5N7PAHominidae (family)actinin alpha 1/4
5Y0TAHomininae (subfamily)actinin alpha 1/4

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: