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Bromodomain testis-specific protein (Bromodomain-containing female sterile homeotic-like protein) (RING3-like protein)

 BRDT_MOUSE              Reviewed;         956 AA.
Q91Y44; G3X8Z8; Q59HJ4;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
28-NOV-2012, sequence version 3.
25-OCT-2017, entry version 116.
RecName: Full=Bromodomain testis-specific protein;
AltName: Full=Bromodomain-containing female sterile homeotic-like protein;
AltName: Full=RING3-like protein;
Name=Brdt; Synonyms=Fsrg3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=15261828; DOI=10.1016/j.modgep.2004.03.002;
Shang E., Salazar G., Crowley T.E., Wang X., Lopez R.A., Wang X.,
Wolgemuth D.J.;
"Identification of unique, differentiation stage-specific patterns of
expression of the bromodomain-containing genes Brd2, Brd3, Brd4, and
Brdt in the mouse testis.";
Gene Expr. Patterns 4:513-519(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Testis;
Taniguchi Y.;
"The Brd paralogous genes: testis-specific expression of the splicing
variants.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, INTERACTION WITH HISTONE H4, AND MUTAGENESIS OF
50-PRO-PHE-51; VAL-55; 293-PRO-PHE-294 AND VAL-298.
PubMed=12861021; DOI=10.1128/MCB.23.15.5354-5365.2003;
Pivot-Pajot C., Caron C., Govin J., Vion A., Rousseaux S.,
Khochbin S.;
"Acetylation-dependent chromatin reorganization by BRDT, a testis-
specific bromodomain-containing protein.";
Mol. Cell. Biol. 23:5354-5365(2003).
[6]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=17728347; DOI=10.1242/dev.004481;
Shang E., Nickerson H.D., Wen D., Wang X., Wolgemuth D.J.;
"The first bromodomain of Brdt, a testis-specific member of the BET
sub-family of double-bromodomain-containing proteins, is essential for
male germ cell differentiation.";
Development 134:3507-3515(2007).
[7]
TISSUE SPECIFICITY.
PubMed=17049203; DOI=10.1016/j.ygeno.2006.09.002;
Paillisson A., Levasseur A., Gouret P., Callebaut I., Bontoux M.,
Pontarotti P., Monget P.;
"Bromodomain testis-specific protein is expressed in mouse oocyte and
evolves faster than its ubiquitously expressed paralogs BRD2, -3, and
-4.";
Genomics 89:215-223(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=22020252; DOI=10.1016/j.ydbio.2011.10.005;
Berkovits B.D., Wolgemuth D.J.;
"The first bromodomain of the testis-specific double bromodomain
protein Brdt is required for chromocenter organization that is
modulated by genetic background.";
Dev. Biol. 360:358-368(2011).
[10]
FUNCTION.
PubMed=22901802; DOI=10.1016/j.cell.2012.06.045;
Matzuk M.M., McKeown M.R., Filippakopoulos P., Li Q., Ma L.,
Agno J.E., Lemieux M.E., Picaud S., Yu R.N., Qi J., Knapp S.,
Bradner J.E.;
"Small-molecule inhibition of BRDT for male contraception.";
Cell 150:673-684(2012).
[11]
FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND INTERACTION
WITH CDK9 AND CCNT1.
PubMed=22922464; DOI=10.1038/emboj.2012.233;
Gaucher J., Boussouar F., Montellier E., Curtet S., Buchou T.,
Bertrand S., Hery P., Jounier S., Depaux A., Vitte A.L., Guardiola P.,
Pernet K., Debernardi A., Lopez F., Holota H., Imbert J.,
Wolgemuth D.J., Gerard M., Rousseaux S., Khochbin S.;
"Bromodomain-dependent stage-specific male genome programming by
Brdt.";
EMBO J. 31:3809-3820(2012).
[12]
FUNCTION, AND INTERACTION WITH SRSF2; DDX5; HNRNPK AND TARDBP.
PubMed=22570411; DOI=10.1093/nar/gks342;
Berkovits B.D., Wang L., Guarnieri P., Wolgemuth D.J.;
"The testis-specific double bromodomain-containing protein BRDT forms
a complex with multiple spliceosome components and is required for
mRNA splicing and 3'-UTR truncation in round spermatids.";
Nucleic Acids Res. 40:7162-7175(2012).
[13]
FUNCTION, AND DOMAIN.
PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014;
Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z.,
Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J.,
Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C.,
Panne D., Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.;
"Dynamic competing histone H4 K5K8 acetylation and butyrylation are
hallmarks of highly active gene promoters.";
Mol. Cell 62:169-180(2016).
[14]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 17-136 AND 257-382 IN COMPLEX
WITH HISTONE H4 PEPTIDE, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=19794495; DOI=10.1038/nature08397;
Moriniere J., Rousseaux S., Steuerwald U., Soler-Lopez M., Curtet S.,
Vitte A.L., Govin J., Gaucher J., Sadoul K., Hart D.J., Krijgsveld J.,
Khochbin S., Muller C.W., Petosa C.;
"Cooperative binding of two acetylation marks on a histone tail by a
single bromodomain.";
Nature 461:664-668(2009).
-!- FUNCTION: Testis-specific chromatin protein that specifically
binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and
H4K8ac, respectively) and plays a key role in spermatogenesis
(PubMed:12861021, PubMed:19794495, PubMed:22901802,
PubMed:22922464). Required in late pachytene spermatocytes: plays
a role in meiotic and post-meiotic cells by binding to acetylated
histones at the promoter of specific meiotic and post-meiotic
genes, facilitating their activation at the appropriate time. In
the post-meiotic phase of spermatogenesis, binds to
hyperacetylated histones and participates in their general removal
from DNA (PubMed:22901802). Also recognizes and binds a subset of
butyrylated histones: able to bind histone H4 butyrylated at 'Lys-
8' (H4K8ac), while it is not able to bind H4 butyrylated at 'Lys-
5' (H4K5ac) (PubMed:27105113). Also acts as a component of the
splicing machinery in pachytene spermatocytes and round spermatids
and participates in 3'-UTR truncation of specific mRNAs in post-
meiotic spermatids (PubMed:22570411). Required for chromocenter
organization, a structure comprised of peri-centromeric
heterochromatin (PubMed:22020252). {ECO:0000269|PubMed:12861021,
ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:22020252,
ECO:0000269|PubMed:22570411, ECO:0000269|PubMed:22901802,
ECO:0000269|PubMed:22922464, ECO:0000269|PubMed:27105113}.
-!- SUBUNIT: Interacts with SMARCE1 (By similarity). Interacts with
mRNA splicing machinery proteins SRSF2, DDX5, HNRNPK and TARDBP.
Interacts with the acetylated N-terminus of histone H1, H2, H3 and
H4. Interacts with P-TEFb components CDK9 and CCNT1/cyclin-T1.
{ECO:0000250|UniProtKB:Q58F21, ECO:0000269|PubMed:12861021,
ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:22570411,
ECO:0000269|PubMed:22922464}.
-!- INTERACTION:
Q9QWV9:Ccnt1; NbExp=2; IntAct=EBI-6260929, EBI-2655009;
Q99J95:Cdk9; NbExp=3; IntAct=EBI-6260929, EBI-2654963;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17728347,
ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:22020252}.
Note=Detected on chromatin (PubMed:19794495). Excluded from the
chromocenter. {ECO:0000269|PubMed:19794495,
ECO:0000269|PubMed:22020252}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q91Y44-1; Sequence=Displayed;
Name=2;
IsoId=Q91Y44-2; Sequence=VSP_019119, VSP_019120;
-!- TISSUE SPECIFICITY: Testis-specific. Expressed in germinal cells
from the early meiotic (pachytene) spermatocytes and during
spermiogenesis in the round and elongating spermatids until the
condensed late spermatids. No expression seen in spermatogonia.
{ECO:0000269|PubMed:15261828, ECO:0000269|PubMed:17049203,
ECO:0000269|PubMed:17728347}.
-!- DEVELOPMENTAL STAGE: First detected when type B spermatogonia give
rise to early meiotic cells (preleptotene, leptotene and zygotene)
at 10-12 days post partum (dpp), producing a clearly detectable
protein at 12 dpp (at protein level).
{ECO:0000269|PubMed:22922464}.
-!- DOMAIN: Bromo domains mediate interaction with histones that have
acetylated lysine residues at specific positions. Bromo domain 1
mediates binding with histone H4 acetylated at 'Lys-5' and 'Lys-8'
(H4K5ac and H4K8ac, respectively) (PubMed:19794495). The bromo
domains also recognize and bind a subset of butyrylated histones:
able to bind histone H4 butyrylated at 'Lys-8' (H4K8ac), while it
is not able to bind H4 butyrylated at 'Lys-5' (H4K5ac)
(PubMed:27105113). {ECO:0000269|PubMed:19794495,
ECO:0000269|PubMed:27105113}.
-!- DISRUPTION PHENOTYPE: Mice are viable but males are sterile,
producing fewer and morphologically abnormal sperm. Aberrant
morphogenesis are first detected in step 9 elongating spermatids,
and those elongated spermatids that are formed lack the
distinctive foci of heterochromatin at the peri-nuclear envelope.
Spermatid nuclei show a fragmented chromocenter.
{ECO:0000269|PubMed:17728347, ECO:0000269|PubMed:22020252,
ECO:0000269|PubMed:22922464}.
-!- MISCELLANEOUS: Brdt is a promising target for male contraception.
Inhibition by thienodiazepine inhibitor (+)-JQ1 that binds Asn-
108, prevents recognition of acetylated histone H4. Treatment of
mice with JQ1 reduces seminiferous tubule area, testis size and
spermatozoa number and motility without affecting hormone levels.
JQ1 causes a complete and reversible contraceptive effect in male
mice (PubMed:22901802). {ECO:0000305|PubMed:22901802}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Asking life to be
patient - Issue 144 of November 2012;
URL="http://web.expasy.org/spotlight/back_issues/144";
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EMBL; AF358660; AAK50736.1; -; mRNA.
EMBL; AB208640; BAD91553.1; -; mRNA.
EMBL; AC126598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466529; EDL20168.1; -; Genomic_DNA.
CCDS; CCDS19500.1; -. [Q91Y44-1]
CCDS; CCDS39197.1; -. [Q91Y44-2]
RefSeq; NP_001073342.1; NM_001079873.1. [Q91Y44-2]
RefSeq; NP_473395.2; NM_054054.2. [Q91Y44-1]
UniGene; Mm.182836; -.
PDB; 2WP1; X-ray; 2.10 A; A/B=257-382.
PDB; 2WP2; X-ray; 2.37 A; A/B=17-136.
PDBsum; 2WP1; -.
PDBsum; 2WP2; -.
ProteinModelPortal; Q91Y44; -.
SMR; Q91Y44; -.
BioGrid; 227777; 1.
DIP; DIP-48975N; -.
IntAct; Q91Y44; 6.
MINT; MINT-8409453; -.
STRING; 10090.ENSMUSP00000031215; -.
GuidetoPHARMACOLOGY; 2729; -.
iPTMnet; Q91Y44; -.
PhosphoSitePlus; Q91Y44; -.
PaxDb; Q91Y44; -.
PeptideAtlas; Q91Y44; -.
PRIDE; Q91Y44; -.
Ensembl; ENSMUST00000031215; ENSMUSP00000031215; ENSMUSG00000029279. [Q91Y44-1]
Ensembl; ENSMUST00000112677; ENSMUSP00000108297; ENSMUSG00000029279. [Q91Y44-2]
GeneID; 114642; -.
KEGG; mmu:114642; -.
UCSC; uc008ymb.1; mouse. [Q91Y44-2]
UCSC; uc008ymc.1; mouse. [Q91Y44-1]
CTD; 676; -.
MGI; MGI:1891374; Brdt.
eggNOG; KOG1474; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00760000119206; -.
HOGENOM; HOG000231200; -.
HOVERGEN; HBG004896; -.
InParanoid; Q91Y44; -.
KO; K11724; -.
OMA; ENQRDLG; -.
OrthoDB; EOG091G01QC; -.
TreeFam; TF317345; -.
ChiTaRS; Brdt; mouse.
EvolutionaryTrace; Q91Y44; -.
PRO; PR:Q91Y44; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029279; -.
CleanEx; MM_BRDT; -.
Genevisible; Q91Y44; MM.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0070577; F:lysine-acetylated histone binding; IMP:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0001207; P:histone displacement; IMP:UniProtKB.
GO; GO:0007141; P:male meiosis I; IMP:UniProtKB.
GO; GO:0007140; P:male meiotic nuclear division; IMP:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0051039; P:positive regulation of transcription involved in meiotic cell cycle; IMP:UniProtKB.
GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.20.920.10; -; 2.
InterPro; IPR031354; BRD4_CDT.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR027353; NET_dom.
Pfam; PF17035; BET; 1.
Pfam; PF17105; BRD4_CDT; 1.
Pfam; PF00439; Bromodomain; 2.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 2.
SUPFAM; SSF47370; SSF47370; 2.
PROSITE; PS00633; BROMODOMAIN_1; 2.
PROSITE; PS50014; BROMODOMAIN_2; 2.
PROSITE; PS51525; NET; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Bromodomain;
Chromatin regulator; Coiled coil; Complete proteome; Differentiation;
Meiosis; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Spermatogenesis; Transcription;
Transcription regulation.
CHAIN 1 956 Bromodomain testis-specific protein.
/FTId=PRO_0000239227.
DOMAIN 43 115 Bromo 1. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 286 358 Bromo 2. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 496 578 NET. {ECO:0000255|PROSITE-
ProRule:PRU00857}.
COILED 417 442 {ECO:0000255}.
COILED 844 940 {ECO:0000255}.
MOTIF 208 219 Nuclear localization signal.
{ECO:0000250|UniProtKB:Q58F21}.
COMPBIAS 446 496 Lys-rich.
COMPBIAS 625 639 Pro-rich.
COMPBIAS 643 689 Ser-rich.
BINDING 108 108 Histone H4K5ac.
{ECO:0000269|PubMed:19794495}.
BINDING 108 108 JQ1 inhibitor.
{ECO:0000250|UniProtKB:Q58F21}.
BINDING 113 113 Histone H4K5ac.
{ECO:0000269|PubMed:19794495}.
MOD_RES 186 186 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 323 326 GKMD -> VNTA (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_019119.
VAR_SEQ 327 956 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_019120.
MUTAGEN 50 51 PF->AA: Abolishes interaction with
histone H4 acetylated N-terminus; when
associated with A-55.
{ECO:0000269|PubMed:12861021}.
MUTAGEN 55 55 V->A: Abolishes interaction with histone
H4 acetylated N-terminus; when associated
with 50-AA-51.
{ECO:0000269|PubMed:12861021}.
MUTAGEN 293 294 PF->AA: Abolishes interaction with
histone H4 acetylated N-terminus; when
associated with A-298.
{ECO:0000269|PubMed:12861021}.
MUTAGEN 298 298 V->A: Abolishes interaction with histone
H4 acetylated N-terminus; when associated
with 293-AA-294.
{ECO:0000269|PubMed:12861021}.
CONFLICT 208 208 K -> R (in Ref. 2; BAD91553).
{ECO:0000305}.
CONFLICT 691 691 S -> F (in Ref. 1; AAK50736).
{ECO:0000305}.
HELIX 29 36 {ECO:0000244|PDB:2WP2}.
HELIX 38 43 {ECO:0000244|PDB:2WP2}.
HELIX 46 51 {ECO:0000244|PDB:2WP2}.
TURN 57 61 {ECO:0000244|PDB:2WP2}.
HELIX 65 68 {ECO:0000244|PDB:2WP2}.
HELIX 75 83 {ECO:0000244|PDB:2WP2}.
HELIX 90 107 {ECO:0000244|PDB:2WP2}.
HELIX 113 129 {ECO:0000244|PDB:2WP2}.
HELIX 264 282 {ECO:0000244|PDB:2WP1}.
HELIX 285 287 {ECO:0000244|PDB:2WP1}.
HELIX 288 291 {ECO:0000244|PDB:2WP1}.
HELIX 292 294 {ECO:0000244|PDB:2WP1}.
HELIX 300 303 {ECO:0000244|PDB:2WP1}.
HELIX 308 311 {ECO:0000244|PDB:2WP1}.
HELIX 318 326 {ECO:0000244|PDB:2WP1}.
HELIX 333 350 {ECO:0000244|PDB:2WP1}.
HELIX 356 372 {ECO:0000244|PDB:2WP1}.
STRAND 375 377 {ECO:0000244|PDB:2WP1}.
SEQUENCE 956 AA; 107255 MW; E727044706A67260 CRC64;
MSLPSRQTAI VNPPPPEYIN TKKSGRLTNQ LQFLQRVVLK ALWKHGFSWP FQQPVDAVKL
KLPDYYTIIK TPMDLNTIKK RLENKYYEKA SECIEDFNTM FSNCYLYNKT GDDIVVMAQA
LEKLFMQKLS QMPQEEQVVG GKERIKKDIQ QKIAVSSAKE QIPSKAAENV FKRQEIPSGL
PDISLSPLNM AQEAPPICDS QSLVQITKGV KRRADTTTPT TSIAKASSES PPTLRETKPV
NMPVKENTVK NVLPDSQQQH KVLKTVKVTE QLKHCSEILK EMLAKKHLPY AWPFYNPVDA
DALGLHNYYD VVKNPMDLGT IKGKMDNQEY KDAYEFAADV RLMFMNCYKY NPPDHEVVAM
ARTLQDVFEL HFAKIPDEPI ESMHACHLTT NSAQALSRES SSEASSGDAS SEDSEDERVQ
HLAKLQEQLN AVHQQLQVLS QVPLRKLKKK NEKSKRAPKR KKVNNRDENP RKKPKQMKQK
EKAKINQPKK KKPLLKSEEE DNAKPMNYDE KRQLSLDINK LPGDKLGRIV HIIQSREPSL
RNSNPDEIEI DFETLKASTL RELEKYVLAC LRKRSLKPQA KKVVRSKEEL HSEKKLELER
RLLDVNNQLN CRKRQTKRPA KVEKPPPPPP PPPPPPPPPE LASGSRLTDS SSSSGSGSGS
SSSSSGSSSS SSSSGSASSS SDSSSSDSSD SEPEIFPKFT GVKQNDLPPK ENIKQIQSSV
QDITSAEAPL AQQSTAPCGA PGKHSQQMLG CQVTQHLQAT ENTASVQTQP LSGDCKRVLL
GPPVVHTSAE SLTVLEPECH APAQKDIKIK NADSWKSLGK PVKASSVLKS SDELFNQFRK
AAIEKEVKAR TQEQMRKHLE HNAKDPKVSQ ENQREPGSGL TLESLSSKVQ DKSLEEDQSE
QQPPSEAQDV SKLWLLKDRN LAREKEQERR RREAMAGTID MTLQSDIMTM FENNFD


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31108 BRDT (22-138), GST-tag, Human Recombinant Protein,Human Bromodomain testis-specific protein, also known as BRDT, BRD6, and CT9, amino-acids 22 – 138 (GenBank Accession No. NM_207189) with N-terminal G 100
31024 BRD2, BD1 and BD2 (65-459), GST-tag, Human Recombinant Protein,Human Bromodomain containing 2, also known as BRD2, RING3 or RNF3, amino-acids 65 – 459 (GenBank Accession No. NM_005104) with N-termina 100
20-372-60134 bromodomain and PHD finger containing. 1 (BRPF1). transcript variant 1. mRNA - Mouse monoclonal anti-human BRPF1 antibody; Bromodomain and PHD finger-containing protein 1; BR140 protein Monoclonal 0.1 mg
BREA2 BRDT Gene bromodomain, testis-specific
E14100h Human Bromodomain, Testis Specific ELISA Kit 96T


 

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