BRDT
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Official Full Name
bromodomain, testis-specific -
Overview
BRDT is similar to the RING3 protein family. It possesses 2 bromodomain motifs and a PEST sequence (a cluster of proline, glutamic acid, serine, and threonine residues), characteristic of proteins that undergo rapid intracellular degradation. The bromodomain is found in proteins that regulate transcription. Several transcript variants encoding multiple isoforms have been found for this gene. -
Synonyms
BRDT;bromodomain, testis-specific;bromodomain testis-specific protein;BRD6;cancer/testis antigen 9;CT9;RING3-like protein
Recombinant Proteins
- Human
- Mouse
- E.coli
- E. coli
- Mammalian Cell
- HEK293
- His
- His&Flag
- GST
- His&Fc&Avi
- Non
- His&SUMO
Involved Pathway
BRDT involved in several pathways and played different roles in them. We selected most pathways BRDT participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with BRDT were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|
Protein Function
BRDT has several biochemical functions, for example, histone binding,lysine-acetylated histone binding,transcription coactivator activity. Some of the functions are cooperated with other proteins, some of the functions could acted by BRDT itself. We selected most functions BRDT had, and list some proteins which have the same functions with BRDT. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| histone binding | HIST2H3C1,HIST1H3D,UIMC1,RCC1,HIST1H47,SERPINB1A,NCL,APBB1,HIST1H3I,ZMYND11 |
| transcription coactivator activity | NR1I2,MTF1,PCBD1,ASXL1,RARA,SMARCA2,ATF2,SP100,SRA1,MED26 |
| lysine-acetylated histone binding | BRD2,BRD9,TAF1L,PHIP,TAF1,PSME4B,PSME4,BAZ1B,ATAD2B,SMARCA4 |
Interacting Protein
BRDT has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with BRDT here. Most of them are supplied by our site. Hope this information will be useful for your research of BRDT.
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