Domains within Rattus norvegicus protein A0A0G2JVC1_RAT (A0A0G2JVC1)

E3 ubiquitin-protein ligase Mdm2

Alternative representations: 1 /

Protein length483 aa
Source databaseUniProt
Identifiers A0A0G2JVC1_RAT, A0A0G2JVC1, ENSRNOP00000069425.1, ENSRNOP00000069425
Source gene ENSRNOG00000006304
Alternative splicing D3ZVH5_RAT, A0A0G2JVC1_RAT

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 cellular organisms

Predicted functional partners

A0A0G2JVC1_RAT is shown as Mdm2 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 Mdm2

Protein A0A0G2JVC1_RAT is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map03320PPAR signaling pathway
map00071Fatty acid degradation iPath3
map05206MicroRNAs in cancer
map05203Viral carcinogenesis
Some of these pathways are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

KEGG orthologous groups

KONameDescription
K01897ACSL, fadDlong-chain-fatty-acid---CoA ligase [EC:6.2.1.3] iPath3
K06643MDM2E3 ubiquitin-protein ligase Mdm2 [EC:2.3.2.27]
Some of these orthologous groups are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

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 1 PTMs annotated in this protein:

PTMCount
Ubiquitination1

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein ENSRNOG00000006304.

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 10116.ENSRNOP00000069425 in eggNOG.

OGTaxonomic classDescription
LCOG1022All organisms (root)long-chain acyl-CoA synthetase [EC:6.2.1.3],long-chain-fatty-acid--CoA ligase ACSBG [EC:6.2.1.3],E3 ubiquitin-protein ligase Mdm2 [EC:2.3.2.27]
KOG1256Eukaryota (superkingdom)long-chain acyl-CoA synthetase [EC:6.2.1.3],long-chain-fatty-acid--CoA ligase ACSBG [EC:6.2.1.3],E3 ubiquitin-protein ligase Mdm2 [EC:2.3.2.27]
HT5TZMetazoa (kingdom)protein Mdm4,E3 ubiquitin-protein ligase Mdm2 [EC:2.3.2.27]
93K6QChordata (phylum)E3 ubiquitin-protein ligase Mdm2 [EC:2.3.2.27]
5QCC1Sarcopterygii (superclass)E3 ubiquitin-protein ligase Mdm2 [EC:2.3.2.27]
8YXKUMammalia (class)E3 ubiquitin-protein ligase Mdm2 [EC:2.3.2.27]
4RN53Euarchontoglires (superorder)E3 ubiquitin-protein ligase Mdm2 [EC:2.3.2.27]
AI611Rodentia (order)E3 ubiquitin-protein ligase Mdm2 [EC:2.3.2.27]
8DE16Myomorpha (suborder)E3 ubiquitin-protein ligase Mdm2 [EC:2.3.2.27]
7KVMZOpisthokonta (clade)long-chain acyl-CoA synthetase [EC:6.2.1.3],long-chain-fatty-acid--CoA ligase ACSBG [EC:6.2.1.3],E3 ubiquitin-protein ligase Mdm2 [EC:2.3.2.27]
9FHKZVertebrata (clade)E3 ubiquitin-protein ligase Mdm2 [EC:2.3.2.27]
H6C1PBilateria (clade)protein Mdm4,E3 ubiquitin-protein ligase Mdm2 [EC:2.3.2.27]

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: