Domains within Homo sapiens protein TRI47_HUMAN (Q96LD4)

Tripartite motif-containing protein 47

Alternative representations: 1 /

Protein length638 aa
Source databaseUniProt
Identifiers TRI47_HUMAN, Q96LD4, ENSP00000254816.1, ENSP00000254816, Q96AD0, Q96GU5, Q9BRN7, Q96LD4-2
Source gene ENSG00000132481
Alternative splicing TRI47_HUMAN, K7EQ30_HUMAN, A0A0M3HER3_HUMAN, ENSP00000465038.1

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 Euteleostomi

Predicted functional partners

TRI47_HUMAN is shown as TRIM47 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 TRIM47

Protein TRI47_HUMAN is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map04361Axon regeneration
map04120Ubiquitin mediated proteolysis
map05164Influenza A

KEGG orthologous groups

KONameDescription
K12012TRIM35tripartite motif-containing protein 35
K06712BTN, CD277butyrophilin
K12023TRIM47tripartite motif-containing protein 47

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 10 PTMs annotated in this protein:

PTMCount
Ubiquitination6
Phosphorylation3
Acetylation1

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein TRIM47.

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.ENSP00000254816 in eggNOG.

OGTaxonomic classDescription
LKOG2177All organisms (root)butyrophilin,tripartite motif-containing protein 2/3,deltex [EC:2.3.2.27]
KOG2177Eukaryota (superkingdom)butyrophilin,tripartite motif-containing protein 2/3,deltex [EC:2.3.2.27]
HVPGDMetazoa (kingdom)butyrophilin,tripartite motif-containing protein 35,tripartite motif-containing protein 2/3
93S94Chordata (phylum)butyrophilin,tripartite motif-containing protein 35,tripartite motif-containing protein 16
5R35KSarcopterygii (superclass)tripartite motif-containing protein 47,tripartite motif-containing protein 25 [EC:2.3.2.27],E3 ubiquitin-protein ligase RNF135 [EC:2.3.2.27]
8ZFSHMammalia (class)tripartite motif-containing protein 25 [EC:2.3.2.27],tripartite motif-containing protein 65,tripartite motif-containing protein 47
4R8EEEuarchontoglires (superorder)tripartite motif-containing protein 47
4ZWX9Primates (order)tripartite motif-containing protein 47
98AVEHaplorrhini (suborder)tripartite motif-containing protein 47
BV73GSimiiformes (infraorder)tripartite motif-containing protein 47
9ER8CCatarrhini (parvorder)tripartite motif-containing protein 47
7KUB7Opisthokonta (clade)butyrophilin,tripartite motif-containing protein 35,tripartite motif-containing protein 2/3
9FXMTVertebrata (clade)tripartite motif-containing protein 35,butyrophilin,tripartite motif-containing protein 16
H6GQGBilateria (clade)butyrophilin,tripartite motif-containing protein 35,tripartite motif-containing protein 2/3
FX32SHominoidea (superfamily)tripartite motif-containing protein 47
5N7A6Hominidae (family)tripartite motif-containing protein 47
5XW2KHomininae (subfamily)tripartite motif-containing protein 47

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: