BRDT_MOUSE
ID BRDT_MOUSE Reviewed; 956 AA.
AC Q91Y44; G3X8Z8; Q59HJ4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Bromodomain testis-specific protein;
DE AltName: Full=Bromodomain-containing female sterile homeotic-like protein;
DE AltName: Full=RING3-like protein;
GN Name=Brdt; Synonyms=Fsrg3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=15261828; DOI=10.1016/j.modgep.2004.03.002;
RA Shang E., Salazar G., Crowley T.E., Wang X., Lopez R.A., Wang X.,
RA Wolgemuth D.J.;
RT "Identification of unique, differentiation stage-specific patterns of
RT expression of the bromodomain-containing genes Brd2, Brd3, Brd4, and Brdt
RT in the mouse testis.";
RL Gene Expr. Patterns 4:513-519(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RA Taniguchi Y.;
RT "The Brd paralogous genes: testis-specific expression of the splicing
RT variants.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH HISTONE H4, AND MUTAGENESIS OF 50-PRO-PHE-51;
RP VAL-55; 293-PRO-PHE-294 AND VAL-298.
RX PubMed=12861021; DOI=10.1128/mcb.23.15.5354-5365.2003;
RA Pivot-Pajot C., Caron C., Govin J., Vion A., Rousseaux S., Khochbin S.;
RT "Acetylation-dependent chromatin reorganization by BRDT, a testis-specific
RT bromodomain-containing protein.";
RL Mol. Cell. Biol. 23:5354-5365(2003).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17728347; DOI=10.1242/dev.004481;
RA Shang E., Nickerson H.D., Wen D., Wang X., Wolgemuth D.J.;
RT "The first bromodomain of Brdt, a testis-specific member of the BET sub-
RT family of double-bromodomain-containing proteins, is essential for male
RT germ cell differentiation.";
RL Development 134:3507-3515(2007).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=17049203; DOI=10.1016/j.ygeno.2006.09.002;
RA Paillisson A., Levasseur A., Gouret P., Callebaut I., Bontoux M.,
RA Pontarotti P., Monget P.;
RT "Bromodomain testis-specific protein is expressed in mouse oocyte and
RT evolves faster than its ubiquitously expressed paralogs BRD2, -3, and -4.";
RL Genomics 89:215-223(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22020252; DOI=10.1016/j.ydbio.2011.10.005;
RA Berkovits B.D., Wolgemuth D.J.;
RT "The first bromodomain of the testis-specific double bromodomain protein
RT Brdt is required for chromocenter organization that is modulated by genetic
RT background.";
RL Dev. Biol. 360:358-368(2011).
RN [10]
RP FUNCTION.
RX PubMed=22901802; DOI=10.1016/j.cell.2012.06.045;
RA Matzuk M.M., McKeown M.R., Filippakopoulos P., Li Q., Ma L., Agno J.E.,
RA Lemieux M.E., Picaud S., Yu R.N., Qi J., Knapp S., Bradner J.E.;
RT "Small-molecule inhibition of BRDT for male contraception.";
RL Cell 150:673-684(2012).
RN [11]
RP FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP CDK9 AND CCNT1.
RX PubMed=22922464; DOI=10.1038/emboj.2012.233;
RA Gaucher J., Boussouar F., Montellier E., Curtet S., Buchou T., Bertrand S.,
RA Hery P., Jounier S., Depaux A., Vitte A.L., Guardiola P., Pernet K.,
RA Debernardi A., Lopez F., Holota H., Imbert J., Wolgemuth D.J., Gerard M.,
RA Rousseaux S., Khochbin S.;
RT "Bromodomain-dependent stage-specific male genome programming by Brdt.";
RL EMBO J. 31:3809-3820(2012).
RN [12]
RP FUNCTION, AND INTERACTION WITH SRSF2; DDX5; HNRNPK AND TARDBP.
RX PubMed=22570411; DOI=10.1093/nar/gks342;
RA Berkovits B.D., Wang L., Guarnieri P., Wolgemuth D.J.;
RT "The testis-specific double bromodomain-containing protein BRDT forms a
RT complex with multiple spliceosome components and is required for mRNA
RT splicing and 3'-UTR truncation in round spermatids.";
RL Nucleic Acids Res. 40:7162-7175(2012).
RN [13]
RP FUNCTION, AND DOMAIN.
RX PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014;
RA Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z.,
RA Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J.,
RA Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C., Panne D.,
RA Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.;
RT "Dynamic competing histone H4 K5K8 acetylation and butyrylation are
RT hallmarks of highly active gene promoters.";
RL Mol. Cell 62:169-180(2016).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 17-136 AND 257-382 IN COMPLEX WITH
RP HISTONE H4 PEPTIDE, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19794495; DOI=10.1038/nature08397;
RA Moriniere J., Rousseaux S., Steuerwald U., Soler-Lopez M., Curtet S.,
RA Vitte A.L., Govin J., Gaucher J., Sadoul K., Hart D.J., Krijgsveld J.,
RA Khochbin S., Muller C.W., Petosa C.;
RT "Cooperative binding of two acetylation marks on a histone tail by a single
RT bromodomain.";
RL Nature 461:664-668(2009).
CC -!- FUNCTION: Testis-specific chromatin protein that specifically binds
CC histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac,
CC respectively) and plays a key role in spermatogenesis (PubMed:12861021,
CC PubMed:19794495, PubMed:22901802, PubMed:22922464). Required in late
CC pachytene spermatocytes: plays a role in meiotic and post-meiotic cells
CC by binding to acetylated histones at the promoter of specific meiotic
CC and post-meiotic genes, facilitating their activation at the
CC appropriate time. In the post-meiotic phase of spermatogenesis, binds
CC to hyperacetylated histones and participates in their general removal
CC from DNA (PubMed:22901802). Also recognizes and binds a subset of
CC butyrylated histones: able to bind histone H4 butyrylated at 'Lys-8'
CC (H4K8ac), while it is not able to bind H4 butyrylated at 'Lys-5'
CC (H4K5ac) (PubMed:27105113). Also acts as a component of the splicing
CC machinery in pachytene spermatocytes and round spermatids and
CC participates in 3'-UTR truncation of specific mRNAs in post-meiotic
CC spermatids (PubMed:22570411). Required for chromocenter organization, a
CC structure comprised of peri-centromeric heterochromatin
CC (PubMed:22020252). {ECO:0000269|PubMed:12861021,
CC ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:22020252,
CC ECO:0000269|PubMed:22570411, ECO:0000269|PubMed:22901802,
CC ECO:0000269|PubMed:22922464, ECO:0000269|PubMed:27105113}.
CC -!- SUBUNIT: Interacts with SMARCE1 (By similarity). Interacts with mRNA
CC splicing machinery proteins SRSF2, DDX5, HNRNPK and TARDBP. Interacts
CC with the acetylated N-terminus of histone H1, H2, H3 and H4. Interacts
CC with P-TEFb components CDK9 and CCNT1/cyclin-T1.
CC {ECO:0000250|UniProtKB:Q58F21, ECO:0000269|PubMed:12861021,
CC ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:22570411,
CC ECO:0000269|PubMed:22922464}.
CC -!- INTERACTION:
CC Q91Y44; Q9QWV9: Ccnt1; NbExp=2; IntAct=EBI-6260929, EBI-2655009;
CC Q91Y44; Q99J95: Cdk9; NbExp=3; IntAct=EBI-6260929, EBI-2654963;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17728347,
CC ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:22020252}.
CC Note=Detected on chromatin (PubMed:19794495). Excluded from the
CC chromocenter. {ECO:0000269|PubMed:19794495,
CC ECO:0000269|PubMed:22020252}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91Y44-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91Y44-2; Sequence=VSP_019119, VSP_019120;
CC -!- TISSUE SPECIFICITY: Testis-specific. Expressed in germinal cells from
CC the early meiotic (pachytene) spermatocytes and during spermiogenesis
CC in the round and elongating spermatids until the condensed late
CC spermatids. No expression seen in spermatogonia.
CC {ECO:0000269|PubMed:15261828, ECO:0000269|PubMed:17049203,
CC ECO:0000269|PubMed:17728347}.
CC -!- DEVELOPMENTAL STAGE: First detected when type B spermatogonia give rise
CC to early meiotic cells (preleptotene, leptotene and zygotene) at 10-12
CC days post partum (dpp), producing a clearly detectable protein at 12
CC dpp (at protein level). {ECO:0000269|PubMed:22922464}.
CC -!- DOMAIN: Bromo domains mediate interaction with histones that have
CC acetylated lysine residues at specific positions. Bromo domain 1
CC mediates binding with histone H4 acetylated at 'Lys-5' and 'Lys-8'
CC (H4K5ac and H4K8ac, respectively) (PubMed:19794495). The bromo domains
CC also recognize and bind a subset of butyrylated histones: able to bind
CC histone H4 butyrylated at 'Lys-8' (H4K8ac), while it is not able to
CC bind H4 butyrylated at 'Lys-5' (H4K5ac) (PubMed:27105113).
CC {ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:27105113}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable but males are sterile, producing
CC fewer and morphologically abnormal sperm. Aberrant morphogenesis are
CC first detected in step 9 elongating spermatids, and those elongated
CC spermatids that are formed lack the distinctive foci of heterochromatin
CC at the peri-nuclear envelope. Spermatid nuclei show a fragmented
CC chromocenter. {ECO:0000269|PubMed:17728347,
CC ECO:0000269|PubMed:22020252, ECO:0000269|PubMed:22922464}.
CC -!- MISCELLANEOUS: Brdt is a promising target for male contraception.
CC Inhibition by thienodiazepine inhibitor (+)-JQ1 that binds Asn-108,
CC prevents recognition of acetylated histone H4. Treatment of mice with
CC JQ1 reduces seminiferous tubule area, testis size and spermatozoa
CC number and motility without affecting hormone levels. JQ1 causes a
CC complete and reversible contraceptive effect in male mice
CC (PubMed:22901802). {ECO:0000305|PubMed:22901802}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Asking life to be patient
CC - Issue 144 of November 2012;
CC URL="https://web.expasy.org/spotlight/back_issues/144";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF358660; AAK50736.1; -; mRNA.
DR EMBL; AB208640; BAD91553.1; -; mRNA.
DR EMBL; AC126598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466529; EDL20168.1; -; Genomic_DNA.
DR CCDS; CCDS19500.1; -. [Q91Y44-1]
DR CCDS; CCDS39197.1; -. [Q91Y44-2]
DR RefSeq; NP_001073342.1; NM_001079873.1. [Q91Y44-2]
DR RefSeq; NP_473395.2; NM_054054.2. [Q91Y44-1]
DR PDB; 2WP1; X-ray; 2.10 A; A/B=257-382.
DR PDB; 2WP2; X-ray; 2.37 A; A/B=17-136.
DR PDBsum; 2WP1; -.
DR PDBsum; 2WP2; -.
DR AlphaFoldDB; Q91Y44; -.
DR SMR; Q91Y44; -.
DR BioGRID; 227777; 2.
DR DIP; DIP-48975N; -.
DR IntAct; Q91Y44; 6.
DR MINT; Q91Y44; -.
DR STRING; 10090.ENSMUSP00000031215; -.
DR GuidetoPHARMACOLOGY; 2729; -.
DR iPTMnet; Q91Y44; -.
DR PhosphoSitePlus; Q91Y44; -.
DR MaxQB; Q91Y44; -.
DR PaxDb; Q91Y44; -.
DR PeptideAtlas; Q91Y44; -.
DR PRIDE; Q91Y44; -.
DR ProteomicsDB; 273763; -. [Q91Y44-1]
DR ProteomicsDB; 273764; -. [Q91Y44-2]
DR Antibodypedia; 3212; 135 antibodies from 23 providers.
DR DNASU; 114642; -.
DR Ensembl; ENSMUST00000031215; ENSMUSP00000031215; ENSMUSG00000029279. [Q91Y44-1]
DR Ensembl; ENSMUST00000112677; ENSMUSP00000108297; ENSMUSG00000029279. [Q91Y44-2]
DR GeneID; 114642; -.
DR KEGG; mmu:114642; -.
DR UCSC; uc008ymb.1; mouse. [Q91Y44-2]
DR UCSC; uc008ymc.1; mouse. [Q91Y44-1]
DR CTD; 676; -.
DR MGI; MGI:1891374; Brdt.
DR VEuPathDB; HostDB:ENSMUSG00000029279; -.
DR eggNOG; KOG1474; Eukaryota.
DR GeneTree; ENSGT00940000154549; -.
DR HOGENOM; CLU_001499_0_0_1; -.
DR InParanoid; Q91Y44; -.
DR OMA; FMQKIAQ; -.
DR OrthoDB; 619848at2759; -.
DR PhylomeDB; Q91Y44; -.
DR TreeFam; TF317345; -.
DR BioGRID-ORCS; 114642; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Brdt; mouse.
DR EvolutionaryTrace; Q91Y44; -.
DR PRO; PR:Q91Y44; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q91Y44; protein.
DR Bgee; ENSMUSG00000029279; Expressed in animal zygote and 191 other tissues.
DR Genevisible; Q91Y44; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0140566; F:histone reader activity; IMP:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0007141; P:male meiosis I; IMP:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051039; P:positive regulation of transcription involved in meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; IMP:UniProtKB.
DR CDD; cd05497; Bromo_Brdt_I_like; 1.
DR CDD; cd05498; Bromo_Brdt_II_like; 1.
DR Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 1.20.920.10; -; 2.
DR InterPro; IPR031354; BRD4_CDT.
DR InterPro; IPR043508; Bromo_Brdt_I.
DR InterPro; IPR043509; Bromo_Brdt_II.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR027353; NET_dom.
DR InterPro; IPR038336; NET_sf.
DR Pfam; PF17035; BET; 1.
DR Pfam; PF17105; BRD4_CDT; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS51525; NET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Bromodomain;
KW Chromatin regulator; Coiled coil; Differentiation; Meiosis;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Spermatogenesis; Transcription;
KW Transcription regulation.
FT CHAIN 1..956
FT /note="Bromodomain testis-specific protein"
FT /id="PRO_0000239227"
FT DOMAIN 43..115
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 286..358
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 496..578
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 210..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 417..442
FT /evidence="ECO:0000255"
FT COILED 844..940
FT /evidence="ECO:0000255"
FT MOTIF 208..219
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q58F21"
FT COMPBIAS 210..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..642
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 108
FT /note="Histone H4K5ac binding"
FT /evidence="ECO:0000269|PubMed:19794495"
FT SITE 113
FT /note="Histone H4K5ac binding"
FT /evidence="ECO:0000269|PubMed:19794495"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 323..326
FT /note="GKMD -> VNTA (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_019119"
FT VAR_SEQ 327..956
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_019120"
FT MUTAGEN 50..51
FT /note="PF->AA: Abolishes interaction with histone H4
FT acetylated N-terminus; when associated with A-55."
FT /evidence="ECO:0000269|PubMed:12861021"
FT MUTAGEN 55
FT /note="V->A: Abolishes interaction with histone H4
FT acetylated N-terminus; when associated with 50-AA-51."
FT /evidence="ECO:0000269|PubMed:12861021"
FT MUTAGEN 293..294
FT /note="PF->AA: Abolishes interaction with histone H4
FT acetylated N-terminus; when associated with A-298."
FT /evidence="ECO:0000269|PubMed:12861021"
FT MUTAGEN 298
FT /note="V->A: Abolishes interaction with histone H4
FT acetylated N-terminus; when associated with 293-AA-294."
FT /evidence="ECO:0000269|PubMed:12861021"
FT CONFLICT 208
FT /note="K -> R (in Ref. 2; BAD91553)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="S -> F (in Ref. 1; AAK50736)"
FT /evidence="ECO:0000305"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:2WP2"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:2WP2"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:2WP2"
FT TURN 57..61
FT /evidence="ECO:0007829|PDB:2WP2"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:2WP2"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:2WP2"
FT HELIX 90..107
FT /evidence="ECO:0007829|PDB:2WP2"
FT HELIX 113..129
FT /evidence="ECO:0007829|PDB:2WP2"
FT HELIX 264..282
FT /evidence="ECO:0007829|PDB:2WP1"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:2WP1"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:2WP1"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:2WP1"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:2WP1"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:2WP1"
FT HELIX 318..326
FT /evidence="ECO:0007829|PDB:2WP1"
FT HELIX 333..350
FT /evidence="ECO:0007829|PDB:2WP1"
FT HELIX 356..372
FT /evidence="ECO:0007829|PDB:2WP1"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:2WP1"
SQ 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
