Domains within Homo sapiens protein ENSP00000318115.3

Alternative representations: 1 /

Protein length456 aa
Source databaseEnsembl
Identifiers ENSP00000318115.3, ENSP00000318115, ENSP00000445806.2, ENSP00000445806
Source gene ENSG00000105197
Alternative splicing ENSP00000318115.3, M0R2D2_HUMAN, TIM50_HUMAN, M0R2F8_HUMAN, M0R2Q2_HUMAN, M0R1Y4_HUMAN, M0R003_HUMAN, M0QXC3_HUMAN, M0R2Z3_HUMAN, M0R303_HUMAN, M0R047_HUMAN, M0R0C3_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 Eukaryota

Predicted functional partners

ENSP00000318115.3 is shown as TIMM50 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 TIMM50

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 7 PTMs annotated in this protein:

PTMCount
Ubiquitination3
Phosphorylation2
Nitrosylation1
Acetylation1

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein TIMM50.

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.ENSP00000445806 in eggNOG.

OGTaxonomic classDescription
LCOG5190All organisms (root)carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase [EC:3.1.3.16],CTD small phosphatase-like protein 2 [EC:3.1.3.-],mitochondrial import inner membrane translocase subunit TIM50
KOG2832Eukaryota (superkingdom)mitochondrial import inner membrane translocase subunit TIM50,carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase [EC:3.1.3.16],CTD small phosphatase-like protein 2 [EC:3.1.3.-]
HTSD7Metazoa (kingdom)mitochondrial import inner membrane translocase subunit TIM50,phosphatidylserine decarboxylase [EC:4.1.1.65]
94CTTChordata (phylum)mitochondrial import inner membrane translocase subunit TIM50
5QMF6Sarcopterygii (superclass)mitochondrial import inner membrane translocase subunit TIM50
8ZE5CMammalia (class)mitochondrial import inner membrane translocase subunit TIM50
4RF8GEuarchontoglires (superorder)mitochondrial import inner membrane translocase subunit TIM50
4ZP4QPrimates (order)mitochondrial import inner membrane translocase subunit TIM50
98NQ0Haplorrhini (suborder)mitochondrial import inner membrane translocase subunit TIM50
BVDDPSimiiformes (infraorder)mitochondrial import inner membrane translocase subunit TIM50
9EV0SCatarrhini (parvorder)mitochondrial import inner membrane translocase subunit TIM50
7IU7YOpisthokonta (clade)mitochondrial import inner membrane translocase subunit TIM50,phosphatidylserine decarboxylase [EC:4.1.1.65]
9GMEMVertebrata (clade)mitochondrial import inner membrane translocase subunit TIM50
H6I2BBilateria (clade)mitochondrial import inner membrane translocase subunit TIM50,phosphatidylserine decarboxylase [EC:4.1.1.65]
FX2ATHominoidea (superfamily)mitochondrial import inner membrane translocase subunit TIM50
5N7QSHominidae (family)mitochondrial import inner membrane translocase subunit TIM50
5XUDDHomininae (subfamily)mitochondrial import inner membrane translocase subunit TIM50

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: