ID BRD2_MOUSE Reviewed; 798 AA. AC Q7JJ13; O54795; O88411; Q3UGI0; Q5DTS6; Q794H7; Q794H9; Q99PC5; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 146. DE RecName: Full=Bromodomain-containing protein 2; DE AltName: Full=Female sterile homeotic-related protein 1 {ECO:0000303|PubMed:9811568}; DE Short=Fsrg-1 {ECO:0000303|PubMed:9811568}; GN Name=Brd2 {ECO:0000303|PubMed:19883376, ECO:0000312|MGI:MGI:99495}; GN Synonyms=Fsrg1 {ECO:0000303|PubMed:9811568}, Kiaa4005, Ring3 GN {ECO:0000303|PubMed:9693039}; 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], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RC TISSUE=Testis; RX PubMed=9811568; DOI=10.1242/jcs.111.23.3541; RA Rhee K., Brunori M., Besset V., Trousdale R., Wolgemuth D.J.; RT "Expression and potential role of Fsrg1, a murine bromodomain-containing RT homologue of the Drosophila gene female sterile homeotic."; RL J. Cell Sci. 111:3541-3550(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE RP [GENOMIC DNA / MRNA] OF 1-549 (ISOFORM 2), TISSUE SPECIFICITY, AND RP SUBCELLULAR LOCATION. RC STRAIN=129/SvJ, and CD-1; TISSUE=Testis; RX PubMed=9693039; DOI=10.1006/geno.1998.5262; RA Taniguchi Y., Matsuzaka Y., Fujimoto H., Miyado K., Kohda A., Okumura K., RA Kimura M., Inoko H.; RT "Nucleotide sequence of the ring3 gene in the class II region of the mouse RT MHC and its abundant expression in testicular germ cells."; RL Genomics 51:114-123(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9601950; DOI=10.1007/s002510050406; RA Thorpe K.L., Beck S.; RT "DNA sequence and structure of the mouse RING3 gene: identification of RT variant RING3 transcripts."; RL Immunogenetics 48:82-86(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=129/SvJ; RA Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., Hall J., RA Lasky S., Hood L.; RT "Sequence of the mouse major histocompatibility locus class II region."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Amnion, and Visual cortex; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Fetal brain; RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., RA Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by RT screening of terminal sequences of cDNA clones randomly sampled from size- RT fractionated libraries."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-503. RC STRAIN=C57BL/6J; RA Korf I.; RT "Complete sequence of UL26B06."; RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases. RN [8] RP FUNCTION, AND MUTAGENESIS OF VAL-102; TYR-112; TYR-154; ILE-161; VAL-375; RP TYR-385; TYR-427 AND VAL-434. RX PubMed=14731392; DOI=10.1016/s1097-2765(03)00482-9; RA Kanno T., Kanno Y., Siegel R.M., Jang M.K., Lenardo M.J., Ozato K.; RT "Selective recognition of acetylated histones by bromodomain proteins RT visualized in living cells."; RL Mol. Cell 13:33-43(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297 AND SER-300, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [10] RP DISRUPTION PHENOTYPE. RX PubMed=19883376; DOI=10.1042/bj20090928; RA Wang F., Liu H., Blanton W.P., Belkina A., Lebrasseur N.K., Denis G.V.; RT "Brd2 disruption in mice causes severe obesity without Type 2 diabetes."; RL Biochem. J. 425:71-83(2009). RN [11] RP DISRUPTION PHENOTYPE. RX PubMed=19301389; DOI=10.1002/dvdy.21911; RA Shang E., Wang X., Wen D., Greenberg D.A., Wolgemuth D.J.; RT "Double bromodomain-containing gene Brd2 is essential for embryonic RT development in mouse."; RL Dev. Dyn. 238:908-917(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-300 AND SER-304, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Kidney, Liver, Pancreas, Spleen, and 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 [13] RP FUNCTION, INTERACTION WITH STAT3, AND MUTAGENESIS OF TYR-154 AND TYR-427. RX PubMed=28262505; DOI=10.1016/j.molcel.2016.12.022; RA Cheung K.L., Zhang F., Jaganathan A., Sharma R., Zhang Q., Konuma T., RA Shen T., Lee J.Y., Ren C., Chen C.H., Lu G., Olson M.R., Zhang W., RA Kaplan M.H., Littman D.R., Walsh M.J., Xiong H., Zeng L., Zhou M.M.; RT "Distinct roles of Brd2 and Brd4 in potentiating the transcriptional RT program for th17 cell differentiation."; RL Mol. Cell 65:1068-1080(2017). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CTCF. RX PubMed=28388437; DOI=10.1016/j.molcel.2017.02.027; RA Hsu S.C., Gilgenast T.G., Bartman C.R., Edwards C.R., Stonestrom A.J., RA Huang P., Emerson D.J., Evans P., Werner M.T., Keller C.A., Giardine B., RA Hardison R.C., Raj A., Phillips-Cremins J.E., Blobel G.A.; RT "The BET protein BRD2 cooperates with CTCF to enforce transcriptional and RT architectural boundaries."; RL Mol. Cell 66:102-116(2017). CC -!- FUNCTION: Chromatin reader protein that specifically recognizes and CC binds histone H4 acetylated at 'Lys-5' and 'Lys-12' (H4K5ac and CC H4K12ac, respectively), thereby controlling gene expression and CC remodeling chromatin structures (PubMed:14731392). Recruits CC transcription factors and coactivators to target gene sites, and CC activates RNA polymerase II machinery for transcriptional elongation CC (By similarity). Plays a key role in genome compartmentalization via CC its association with CTCF and cohesin: recruited to chromatin by CTCF CC and promotes formation of topologically associating domains (TADs) via CC its ability to bind acetylated histones, contributing to CTCF boundary CC formation and enhancer insulation (PubMed:28388437). Also recognizes CC and binds acetylated non-histone proteins, such as STAT3 CC (PubMed:28262505). Involved in inflammatory response by regulating CC differentiation of naive CD4(+) T-cells into T-helper Th17: recognizes CC and binds STAT3 acetylated at 'Lys-87', promoting STAT3 recruitment to CC chromatin (PubMed:28262505). In addition to acetylated lysines, also CC recognizes and binds lysine residues on histones that are both CC methylated and acetylated on the same side chain to form N6-acetyl-N6- CC methyllysine (Kacme), an epigenetic mark of active chromatin associated CC with increased transcriptional initiation (By similarity). Specifically CC binds histone H4 acetyl-methylated at 'Lys-5' and 'Lys-12' (H4K5acme CC and H4K12acme, respectively) (By similarity). CC {ECO:0000250|UniProtKB:P25440, ECO:0000269|PubMed:14731392, CC ECO:0000269|PubMed:28262505, ECO:0000269|PubMed:28388437}. CC -!- SUBUNIT: Homodimer (By similarity). Interacts with E2F1 (By CC similarity). Interacts with (acetylated) STAT3; promoting STAT3 CC recruitment to chromatin (PubMed:28262505). Interacts with CTCF; CC promoting BRD2 recruitment to chromatin (PubMed:28388437). CC {ECO:0000250|UniProtKB:P25440, ECO:0000269|PubMed:28262505, CC ECO:0000269|PubMed:28388437}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9693039, CC ECO:0000269|PubMed:9811568}. Chromosome {ECO:0000269|PubMed:28388437}. CC Note=Detected on chromatin and nucleosomes. CC {ECO:0000269|PubMed:28388437}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q7JJ13-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7JJ13-2; Sequence=VSP_022601; CC -!- TISSUE SPECIFICITY: Predominantly expressed in the testis, followed by CC ovary, placenta, embryo and to a lower extent in somatic tissues. CC {ECO:0000269|PubMed:9693039, ECO:0000269|PubMed:9811568}. CC -!- DOMAIN: The first bromo domain specifically recognizes histone H4 CC acetylated at 'Lys-12' (H4K12ac) (By similarity). It also specifically CC binds histone H4 acetyl-methylated at 'Lys-5' and 'Lys-12' (H4K5acme CC and H4K12acme, respectively) (By similarity). The second bromo domain CC recognizes and binds histone H4 acetylated at 'Lys-5' and 'Lys-12' CC (H4K5ac and H4K12ac, respectively) (By similarity). CC {ECO:0000250|UniProtKB:P25440}. CC -!- DISRUPTION PHENOTYPE: Embryonic lethality by 11.5 days post coitum CC (dpc) (PubMed:19301389). Before death, embryos are smaller and exhibit CC abnormalities in the neural tube where the gene is highly expressed CC (PubMed:19301389). Mice with an hypomorphic allele display severe CC obesity without type 2 diabetes and are protected from inflammatory CC diseases (PubMed:19883376). {ECO:0000269|PubMed:19301389, CC ECO:0000269|PubMed:19883376}. CC -!- SIMILARITY: Belongs to the BET family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD90273.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AF045462; AAC24810.1; -; mRNA. DR EMBL; AB010246; BAA24377.1; -; mRNA. DR EMBL; AB010247; BAA24378.1; -; mRNA. DR EMBL; AB010248; BAA24379.1; -; mRNA. DR EMBL; AB212273; BAD97682.1; -; mRNA. DR EMBL; D89801; BAA25416.1; -; Genomic_DNA. DR EMBL; AL009226; CAA15818.1; -; Genomic_DNA. DR EMBL; AL009226; CAA15819.1; -; Genomic_DNA. DR EMBL; AF100956; AAC69907.1; -; Genomic_DNA. DR EMBL; AK147918; BAE28228.1; -; mRNA. DR EMBL; AK158970; BAE34749.1; -; mRNA. DR EMBL; AK168525; BAE40404.1; -; mRNA. DR EMBL; AK220444; BAD90273.1; ALT_INIT; mRNA. DR EMBL; AF318183; AAK07919.1; -; mRNA. DR CCDS; CCDS28641.1; -. [Q7JJ13-1] DR RefSeq; NP_001191902.1; NM_001204973.1. [Q7JJ13-1] DR RefSeq; NP_034368.2; NM_010238.3. [Q7JJ13-1] DR AlphaFoldDB; Q7JJ13; -. DR SMR; Q7JJ13; -. DR BioGRID; 199750; 8. DR STRING; 10090.ENSMUSP00000025193; -. DR iPTMnet; Q7JJ13; -. DR PhosphoSitePlus; Q7JJ13; -. DR EPD; Q7JJ13; -. DR jPOST; Q7JJ13; -. DR MaxQB; Q7JJ13; -. DR PaxDb; 10090-ENSMUSP00000109880; -. DR PeptideAtlas; Q7JJ13; -. DR ProteomicsDB; 265230; -. [Q7JJ13-1] DR ProteomicsDB; 265231; -. [Q7JJ13-2] DR Pumba; Q7JJ13; -. DR Antibodypedia; 28816; 449 antibodies from 39 providers. DR DNASU; 14312; -. DR Ensembl; ENSMUST00000025193.14; ENSMUSP00000025193.7; ENSMUSG00000024335.21. [Q7JJ13-1] DR Ensembl; ENSMUST00000095347.13; ENSMUSP00000092990.8; ENSMUSG00000024335.21. [Q7JJ13-2] DR Ensembl; ENSMUST00000114242.9; ENSMUSP00000109880.3; ENSMUSG00000024335.21. [Q7JJ13-1] DR GeneID; 14312; -. DR KEGG; mmu:14312; -. DR UCSC; uc008cbi.1; mouse. [Q7JJ13-1] DR AGR; MGI:99495; -. DR CTD; 6046; -. DR MGI; MGI:99495; Brd2. DR VEuPathDB; HostDB:ENSMUSG00000024335; -. DR eggNOG; KOG1474; Eukaryota. DR GeneTree; ENSGT00940000153385; -. DR HOGENOM; CLU_001499_0_4_1; -. DR InParanoid; Q7JJ13; -. DR OMA; MENREYH; -. DR OrthoDB; 152619at2759; -. DR PhylomeDB; Q7JJ13; -. DR TreeFam; TF317345; -. DR BioGRID-ORCS; 14312; 24 hits in 82 CRISPR screens. DR ChiTaRS; Brd2; mouse. DR PRO; PR:Q7JJ13; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; Q7JJ13; Protein. DR Bgee; ENSMUSG00000024335; Expressed in embryonic post-anal tail and 297 other cell types or tissues. DR ExpressionAtlas; Q7JJ13; baseline and differential. DR GO; GO:0000785; C:chromatin; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0016607; C:nuclear speck; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0140033; F:acetylation-dependent protein binding; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI. DR GO; GO:0140588; P:chromatin looping; IDA:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central. DR GO; GO:0001843; P:neural tube closure; IMP:MGI. DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB. DR GO; GO:2000330; P:positive regulation of T-helper 17 cell lineage commitment; IDA:UniProtKB. DR GO; GO:0071168; P:protein localization to chromatin; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA: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; Bromodomain-like; 2. 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 PANTHER; PTHR22880:SF240; BROMODOMAIN-CONTAINING PROTEIN 2; 1. DR PANTHER; PTHR22880; FALZ-RELATED BROMODOMAIN-CONTAINING PROTEINS; 1. DR Pfam; PF17035; BET; 1. DR Pfam; PF00439; Bromodomain; 2. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 2. DR SUPFAM; SSF47370; Bromodomain; 2. DR PROSITE; PS00633; BROMODOMAIN_1; 2. DR PROSITE; PS50014; BROMODOMAIN_2; 2. DR PROSITE; PS51525; NET; 1. DR Genevisible; Q7JJ13; MM. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Bromodomain; Chromatin regulator; KW Chromosome; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Transcription; Transcription regulation. FT CHAIN 1..798 FT /note="Bromodomain-containing protein 2" FT /id="PRO_0000274005" FT DOMAIN 90..162 FT /note="Bromo 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 363..435 FT /note="Bromo 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 630..712 FT /note="NET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 53..72 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 267..348 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 454..645 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 736..798 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 553..557 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 311..335 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 469..484 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 485..509 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 510..524 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 543..561 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 562..578 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 590..617 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 631..645 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 758..798 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 111 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_part="N(6)-acetyl-N(6)-methyl-L-lysine residue" FT /ligand_part_id="ChEBI:CHEBI:197459" FT /evidence="ECO:0000250|UniProtKB:P25440" FT BINDING 154 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_part="N(6)-acetyl-N(6)-methyl-L-lysine residue" FT /ligand_part_id="ChEBI:CHEBI:197459" FT /evidence="ECO:0000250|UniProtKB:P25440" FT BINDING 155 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_part="N(6)-acetyl-L-lysine residue" FT /ligand_part_id="ChEBI:CHEBI:61930" FT /evidence="ECO:0000250|UniProtKB:P25440" FT BINDING 155 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_part="N(6)-acetyl-N(6)-methyl-L-lysine residue" FT /ligand_part_id="ChEBI:CHEBI:197459" FT /evidence="ECO:0000250|UniProtKB:P25440" FT BINDING 156 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_part="N(6)-acetyl-N(6)-methyl-L-lysine residue" FT /ligand_part_id="ChEBI:CHEBI:197459" FT /evidence="ECO:0000250|UniProtKB:P25440" FT BINDING 159 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_part="N(6)-acetyl-L-lysine residue" FT /ligand_part_id="ChEBI:CHEBI:61930" FT /evidence="ECO:0000250|UniProtKB:P25440" FT BINDING 160 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_part="N(6)-acetyl-L-lysine residue" FT /ligand_part_id="ChEBI:CHEBI:61930" FT /evidence="ECO:0000250|UniProtKB:P25440" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P25440" FT MOD_RES 6 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P25440" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25440" FT MOD_RES 297 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 300 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 304 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 631 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25440" FT VAR_SEQ 1..46 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9693039" FT /id="VSP_022601" FT MUTAGEN 102 FT /note="V->A: In BD1-m4 mutant; reduced binding to histone FT H4 acetylated at 'Lys-12' (H4K12ac); when associated with FT A-112, A-154 and A-161. In m8 mutant; abolished binding to FT histone H4 acetylated at 'Lys-12' (H4K12ac); when FT associated with A-112, A-154, A-161, A-375, A-385, A-427 FT and A-434." FT /evidence="ECO:0000269|PubMed:14731392" FT MUTAGEN 112 FT /note="Y->A: In BD1-m4 mutant; reduced binding to histone FT H4 acetylated at 'Lys-12' (H4K12ac); when associated with FT A-102, A-154 and A-161. In m8 mutant; abolished binding to FT histone H4 acetylated at 'Lys-12' (H4K12ac); when FT associated with A-102, A-154, A-161, A-375, A-385, A-427 FT and A-434." FT /evidence="ECO:0000269|PubMed:14731392" FT MUTAGEN 154 FT /note="Y->A: In BD1-m4 mutant; reduced binding to histone FT H4 acetylated at 'Lys-12' (H4K12ac); when associated with FT A-102, A-112 and A-161. In m8 mutant; abolished binding to FT histone H4 acetylated at 'Lys-12' (H4K12ac); when FT associated with A-102, A-112, A-161, A-375, A-385, A-427 FT and A-434." FT /evidence="ECO:0000269|PubMed:14731392" FT MUTAGEN 154 FT /note="Y->F: Abolished interaction with acetylated STAT3." FT /evidence="ECO:0000269|PubMed:28262505" FT MUTAGEN 161 FT /note="I->A: In BD1-m4 mutant; reduced binding to histone FT H4 acetylated at 'Lys-12' (H4K12ac); when associated with FT A-102, A-112 and A-154. In m8 mutant; abolished binding to FT histone H4 acetylated at 'Lys-12' (H4K12ac); when FT associated with A-102, A-112, A-161, A-375, A-385, A-427 FT and A-434." FT /evidence="ECO:0000269|PubMed:14731392" FT MUTAGEN 375 FT /note="V->A: In BD2-m4 mutant; reduced binding to histone FT H4 acetylated at 'Lys-12' (H4K12ac); when associated with FT A-385, A-427 and A-434. In m8 mutant; abolished binding to FT histone H4 acetylated at 'Lys-12' (H4K12ac); when FT associated with A-102, A-112, A-154, A-161, A-385, A-427 FT and A-434." FT /evidence="ECO:0000269|PubMed:14731392" FT MUTAGEN 385 FT /note="Y->A: In BD2-m4 mutant; reduced binding to histone FT H4 acetylated at 'Lys-12' (H4K12ac); when associated with FT A-375, A-427 and A-434. In m8 mutant; abolished binding to FT histone H4 acetylated at 'Lys-12' (H4K12ac); when FT associated with A-102, A-112, A-154, A-161, A-375, A-427 FT and A-434." FT /evidence="ECO:0000269|PubMed:14731392" FT MUTAGEN 427 FT /note="Y->A: In BD2-m4 mutant; reduced binding to histone FT H4 acetylated at 'Lys-12' (H4K12ac); when associated with FT A-375, A-385 and A-434. In m8 mutant; abolished binding to FT histone H4 acetylated at 'Lys-12' (H4K12ac); when FT associated with A-102, A-112, A-154, A-161, A-375, A-385 FT and A-434." FT /evidence="ECO:0000269|PubMed:14731392" FT MUTAGEN 427 FT /note="Y->F: Abolished interaction with acetylated STAT3." FT /evidence="ECO:0000269|PubMed:28262505" FT MUTAGEN 434 FT /note="V->A: In BD2-m4 mutant; reduced binding to histone FT H4 acetylated at 'Lys-12' (H4K12ac); when associated with FT A-375, A-385 and A-427. In m8 mutant; abolished binding to FT histone H4 acetylated at 'Lys-12' (H4K12ac); when FT associated with A-102, A-112, A-154, A-161, A-375, A-385, FT and A-427434." FT /evidence="ECO:0000269|PubMed:14731392" FT CONFLICT 169 FT /note="E -> K (in Ref. 5; BAE28228)" FT /evidence="ECO:0000305" FT CONFLICT 199 FT /note="A -> G (in Ref. 1; AAC24810)" FT /evidence="ECO:0000305" FT CONFLICT 691 FT /note="P -> L (in Ref. 6; BAD90273)" FT /evidence="ECO:0000305" FT CONFLICT 765..767 FT /note="QVA -> LVP (in Ref. 1; AAC24810)" FT /evidence="ECO:0000305" SQ SEQUENCE 798 AA; 88067 MW; 08DD57FBF1385E96 CRC64; MLQNVTPHKL PGEGNAGLLG LGPEAAAPGK RIRKPSLLYE GFESPTMASV PALQLAPANP PPPEVSNPKK PGRVTNQLQY LHKVVMKALW KHQFAWPFRQ PVDAVKLGLP DYHKIIKQPM DMGTIKRRLE NNYYWAASEC MQDFNTMFTN CYIYNKPTDD IVLMAQTLEK IFLQKVASMP QEEQELVVTI PKNSHKKGAK LAALQGSITS AHQVPAVSSV SHTALYTPPP EIPTTVLNIP HPSVISSPLL KSLHSAGPPL LAVSAAPPAQ PLAKKKGVKR KADTTTPTPT AILAPGSPAS PPGSLEPKAA RLPPMRRESG RPIKPPRKDL PDSQQQHQSS KKGKLSEQLK HCNGILKELL SKKHAAYAWP FYKPVDASAL GLHDYHDIIK HPMDLSTVKR KMENRDYRDA QEFAADVRLM FSNCYKYNPP DHDVVAMARK LQDVFEFRYA KMPDEPLEPG PLPVSTALPP GLTKSSSESS SEESSSESSS EEEEEEEEDE DEEESESSDS EEERAHRLAE LQEQLRAVHE QLAALSQGPI SKPKRKREKK EKKKKRKAEK HRGRIGIDED DKGPRAPRPP QPKKSKKAGG GGSNATTLSH PGFGTSGGSS NKLPKKSQKT APPVLPTGYD SEEEEESRPM SYDEKRQLSL DINKLPGEKL GRVVHIIQAR EPSLRDSNPE EIEIDFETLK PSTLRELERY VLSCLRKKPR KPYTIRKPVG KTKEELALEK KRELEKRLQD VSGQLNSTKK PPKKASEKTE SSAQQVAVSR LSASSSSSDS SSSSSSSSSS DTSDSDSG //