Domains within Homo sapiens protein BRDT_HUMAN (Q58F21)

Bromodomain testis-specific protein

Alternative representations: 1 /

Protein length947 aa
Source databaseUniProt
Identifiers BRDT_HUMAN, Q58F21, ENSP00000354568.3, ENSP00000354568, ENSP00000384051.1, ENSP00000384051, A6NF68, B7Z811, B7Z890, B7ZAX7, D3DT32, O14789, Q05DQ4, Q6P5T1, Q7Z4A6, Q8IWI6, Q58F21-2, C9JLZ2_HUMAN, C9JLZ2, F8W0H2_HUMAN, F8W0H2, C9JMP1_HUMAN, C9JMP1, A0A2J8VD01_PONAB, A0A2J8VD01, A0A2J8MH88_PANTR, A0A2J8MH88, C9JDL5_HUMAN, C9JDL5, C9JD82_HUMAN, C9JD82, Q58F21-5, C9JJU3_HUMAN, C9JJU3, C9J1F7_HUMAN, C9J1F7, F8VZ63_HUMAN, F8VZ63
Source gene ENSG00000137948
Alternative splicing BRDT_HUMAN, ENSP00000359416.2, ENSP00000396351.1, ENSP00000416714.1, ENSP00000408625.1, ENSP00000400002.1, ENSP00000400199.1, ENSP00000404969.1, ENSP00000414349.1, ENSP00000447394.1, ENSP00000446599.1, C9JQ27_HUMAN, Q58F21-4, Q58F21-3

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 Fungi/Metazoa group

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 47 PTMs annotated in this protein:

PTMCount
Phosphorylation32
Acetylation9
Methylation3
O-linked glycosylation1
Caspase cleavage aspartic acid1
O-GlcNAc glycosylation1

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

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: