BCL6_MOUSE
ID BCL6_MOUSE Reviewed; 707 AA.
AC P41183; Q61065;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=B-cell lymphoma 6 protein homolog;
GN Name=Bcl6; Synonyms=Bcl-6;
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].
RC STRAIN=BALB/cJ; TISSUE=Skeletal muscle;
RX PubMed=7478591;
RA Fukuda T., Miki T., Yoshida T., Hatano M., Ohashi K., Hirosawa S.,
RA Tokuhisa T.;
RT "The murine BCL6 gene is induced in activated lymphocytes as an immediate
RT early gene.";
RL Oncogene 11:1657-1663(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RX PubMed=8652841;
RA Allman D., Jain A., Dent A., Maile R.R., Selvaggi T., Kehry M.R.,
RA Staudt L.M.;
RT "BCL-6 expression during B-cell activation.";
RL Blood 87:5257-5268(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH BCL6B.
RX PubMed=9632807; DOI=10.1128/mcb.18.7.4235;
RA Okabe S., Fukuda T., Ishibashi K., Kojima S., Okada S., Hatano M.,
RA Ebara M., Saisho H., Tokuhisa T.;
RT "BAZF, a novel Bcl6 homolog, functions as a transcriptional repressor.";
RL Mol. Cell. Biol. 18:4235-4244(1998).
RN [5]
RP INTERACTION WITH ZBTB7, AND SUBCELLULAR LOCATION.
RX PubMed=9927193; DOI=10.1038/sj.onc.1202332;
RA Davies J.M., Hawe N., Kabarowski J., Huang Q.-H., Zhu J., Brand N.J.,
RA Leprince D., Dhordain P., Cook M., Moriss-Kay G., Zelent A.;
RT "Novel BTB/POZ domain zinc-finger protein, LRF, is a potential target of
RT the LAZ-3/BCL-6 oncogene.";
RL Oncogene 18:365-375(1999).
RN [6]
RP FUNCTION AS TRANSCRIPTIONAL REPRESSOR, AND DISRUPTION PHENOTYPE.
RX PubMed=10981963; DOI=10.1016/s1074-7613(00)00020-0;
RA Shaffer A.L., Yu X., He Y., Boldrick J., Chan E.P., Staudt L.M.;
RT "BCL-6 represses genes that function in lymphocyte differentiation,
RT inflammation, and cell cycle control.";
RL Immunity 13:199-212(2000).
RN [7]
RP FUNCTION IN MEMORY CD8(+) T-CELL MAINTENANCE, AND DISRUPTION PHENOTYPE.
RX PubMed=12021781; DOI=10.1038/ni802;
RA Ichii H., Sakamoto A., Hatano M., Okada S., Toyama H., Taki S., Arima M.,
RA Kuroda Y., Tokuhisa T.;
RT "Role for Bcl-6 in the generation and maintenance of memory CD8+ T-cells.";
RL Nat. Immunol. 3:558-563(2002).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=17828269; DOI=10.1038/ni1508;
RA Phan R.T., Saito M., Kitagawa Y., Means A.R., Dalla-Favera R.;
RT "Genotoxic stress regulates expression of the proto-oncogene Bcl6 in
RT germinal center B cells.";
RL Nat. Immunol. 8:1132-1139(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334; SER-362 AND SER-405, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, and Spleen;
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 [10]
RP FUNCTION IN MIRNA REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=23166356; DOI=10.1084/jem.20121387;
RA Basso K., Schneider C., Shen Q., Holmes A.B., Setty M., Leslie C.,
RA Dalla-Favera R.;
RT "BCL6 positively regulates AID and germinal center gene expression via
RT repression of miR-155.";
RL J. Exp. Med. 209:2455-2465(2012).
RN [11]
RP FUNCTION IN NEUROGENESIS, INTERACTION WITH NOTCH1 AND SIRT1, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=23160044; DOI=10.1038/nn.3264;
RA Tiberi L., van den Ameele J., Dimidschstein J., Piccirilli J., Gall D.,
RA Herpoel A., Bilheu A., Bonnefont J., Iacovino M., Kyba M., Bouschet T.,
RA Vanderhaeghen P.;
RT "BCL6 controls neurogenesis through Sirt1-dependent epigenetic repression
RT of selective Notch targets.";
RL Nat. Neurosci. 15:1627-1635(2012).
RN [12]
RP MUTAGENESIS OF ASN-21 AND HIS-116.
RX PubMed=23911289; DOI=10.1016/j.celrep.2013.06.016;
RA Hatzi K., Jiang Y., Huang C., Garrett-Bakelman F., Gearhart M.D.,
RA Giannopoulou E.G., Zumbo P., Kirouac K., Bhaskara S., Polo J.M.,
RA Kormaksson M., Mackerell A.D. Jr., Xue F., Mason C.E., Hiebert S.W.,
RA Prive G.G., Cerchietti L., Bardwell V.J., Elemento O., Melnick A.;
RT "A hybrid mechanism of action for BCL6 in B cells defined by formation of
RT functionally distinct complexes at enhancers and promoters.";
RL Cell Rep. 4:578-588(2013).
RN [13]
RP FUNCTION IN GERMINAL CENTER REACTIONS, DNA-BINDING, DOMAIN, INTERACTION
RP WITH SMRT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASN-21; HIS-116;
RP 377-LYS--LYS-380 AND 577-CYS--CYS-580.
RX PubMed=23455674; DOI=10.1038/ni.2543;
RA Huang C., Hatzi K., Melnick A.;
RT "Lineage-specific functions of Bcl-6 in immunity and inflammation are
RT mediated by distinct biochemical mechanisms.";
RL Nat. Immunol. 14:380-388(2013).
CC -!- FUNCTION: Transcriptional repressor mainly required for germinal center
CC (GC) formation and antibody affinity maturation which has different
CC mechanisms of action specific to the lineage and biological functions.
CC Forms complexes with different corepressors and histone deacetylases to
CC repress the transcriptional expression of different subsets of target
CC genes. Represses its target genes by binding directly to the DNA
CC sequence 5'-TTCCTAGAA-3' (BCL6-binding site) or indirectly by
CC repressing the transcriptional activity of transcription factors. In GC
CC B-cells, represses genes that function in differentiation,
CC inflammation, apoptosis and cell cycle control, also autoregulates its
CC transcriptional expression and up-regulates, indirectly, the expression
CC of some genes important for GC reactions, such as AICDA, through the
CC repression of microRNAs expression, like miR155. An important function
CC is to allow GC B-cells to proliferate very rapidly in response to T-
CC cell dependent antigens and tolerate the physiological DNA breaks
CC required for immunglobulin class switch recombination and somatic
CC hypermutation without inducing a p53/TP53-dependent apoptotic response.
CC In follicular helper CD4(+) T-cells (T(FH) cells), promotes the
CC expression of T(FH)-related genes but inhibits the differentiation of
CC T(H)1, T(H)2 and T(H)17 cells. Also required for the establishment and
CC maintenance of immunological memory for both T- and B-cells. Suppresses
CC macrophage proliferation through competition with STAT5 for STAT-
CC binding motifs binding on certain target genes, such as CCL2 and CCND2.
CC In response to genotoxic stress, controls cell cycle arrest in GC B-
CC cells in both p53/TP53-dependedent and -independent manners. Besides,
CC also controls neurogenesis through the alteration of the composition of
CC NOTCH-dependent transcriptional complexes at selective NOTCH targets,
CC such as HES5, including the recruitment of the deacetylase SIRT1 and
CC resulting in an epigenetic silencing leading to neuronal
CC differentiation. {ECO:0000269|PubMed:10981963,
CC ECO:0000269|PubMed:12021781, ECO:0000269|PubMed:23160044,
CC ECO:0000269|PubMed:23166356, ECO:0000269|PubMed:23455674}.
CC -!- SUBUNIT: Homodimer. Interacts (via BTB domain) with the corepressors
CC BCOR, NCOR1 and SMRT/NCOR2; the interactions are direct. Forms
CC preferably ternary complexes with BCOR and SMRT/NCOR2 on target gene
CC promoters but, on enhancer elements, interacts with SMRT/NCOR2 and
CC HDAC3 to repress proximal gene expression. Interacts with histone
CC deacetylases HDAC2, HDAC5 and HDAC9 (via the catalytic domain).
CC Interacts with ZBTB7 and BCL6B. Interacts with SCF(FBXO11) complex; the
CC interaction is independent of phosphorylation and promotes
CC ubiquitination. Interacts (when phosphorylated) with PIN1; the
CC interaction is required for BCL6 degradation upon genotoxic stress.
CC Interacts with ZBTB17; inhibits ZBTB17 transcriptional activity.
CC Interacts with CTBP1, autoinhibits its transcriptional expression.
CC Interacts with NOTCH1 NCID and SIRT1; leads to a epigenetic repression
CC of selective NOTCH1-target genes. Interacts (nor via BTB domain neither
CC acetylated) with the NuRD complex components CHD4, HDAC1, MBD3 and
CC MTA3; the interaction with MTA3 inhibits BCL6 acetylation and is
CC required for BCL6 transpriptional repression.
CC {ECO:0000269|PubMed:23160044, ECO:0000269|PubMed:23455674,
CC ECO:0000269|PubMed:9632807, ECO:0000269|PubMed:9927193}.
CC -!- INTERACTION:
CC P41183; Q8CGN4: Bcor; NbExp=2; IntAct=EBI-6253762, EBI-1216174;
CC P41183; Q7TPD1: Fbxo11; NbExp=2; IntAct=EBI-6253762, EBI-15955324;
CC P41183; Q9JKD8: Tbx21; NbExp=3; IntAct=EBI-6253762, EBI-3863870;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9927193}.
CC -!- TISSUE SPECIFICITY: Expressed at least in germinal center B-cells of
CC spleen. {ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:23166356}.
CC -!- DEVELOPMENTAL STAGE: Detected in the cerebral cortex from 12.5 dpc
CC until birth, with highest levels in the frontal and parietal parts of
CC the neocortex than the occipital parts. {ECO:0000269|PubMed:23160044}.
CC -!- DOMAIN: Interaction with corepressors through the BTB domain is needed
CC to facilitate the rapid proliferation and survival of GC B-cells but is
CC not involved in the T(FH) formation and BCL6-mediated suppression of
CC T(H)2 and T(H)17 differentiation required for GC formation.
CC {ECO:0000269|PubMed:23455674}.
CC -!- PTM: Phosphorylated by MAPK1 in response to antigen receptor activation
CC at Ser-334 and Ser-344. Phosphorylated by ATM in response to genotoxic
CC stress. Phosphorylation induces its degradation by ubiquitin/proteasome
CC pathway. {ECO:0000250|UniProtKB:P41182}.
CC -!- PTM: Polyubiquitinated. Polyubiquitinated by SCF(FBXO11), leading to
CC its degradation by the proteasome. Ubiquitinated by the SCF(FBXL17)
CC complex, leading to its degradation by the proteasome: ubiquitination
CC by the SCF(FBXL17) complex takes place when aberrant BTB domain dimers
CC are formed. {ECO:0000250|UniProtKB:P41182}.
CC -!- PTM: Acetylated at Lys-380 by EP300 which inhibits the interaction with
CC NuRD complex and the transcriptional repressor function. Deacetylated
CC by HDAC- and SIR2-dependent pathways. {ECO:0000250|UniProtKB:P41182}.
CC -!- DISRUPTION PHENOTYPE: More than 50% of lethality by 6 weeks of age.
CC Mice have infiltrates of inflammatory cells in their lungs, as well as
CC multinodular lesions with eosinophil infiltrations into the spleen,
CC significantly more T(H)2 and T(H)17 cells and up-regulated levels of
CC inflammtaroy chemokines in macrophages, but, express low levels of
CC memory CD8(+) T-cells and, in spleen, GC B and T(FH) cells are both
CC undetectable. B-cells express 10-fold lower levels of surface IgM than
CC control littermates and macrophages divide faster. From 12.5 dpc to at
CC least 21 days after birth, animals have reduced size of the cerebral
CC hemispheres and a reduced thickness of the frontal and parietal cortex
CC with all the cortical layers affected. At 12.5 and 15.5 dpc, marked
CC reduction of cell-cyle exit indicating defective transition from neural
CC progenitor Cells to postmitotic neurons. {ECO:0000269|PubMed:10981963,
CC ECO:0000269|PubMed:12021781, ECO:0000269|PubMed:23160044,
CC ECO:0000269|PubMed:23455674}.
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; D38377; BAA07456.1; -; mRNA.
DR EMBL; U41465; AAB17432.1; -; mRNA.
DR EMBL; BC052315; AAH52315.1; -; mRNA.
DR CCDS; CCDS28082.1; -.
DR RefSeq; NP_001334955.1; NM_001348026.1.
DR RefSeq; NP_033874.1; NM_009744.4.
DR RefSeq; XP_017172344.1; XM_017316855.1.
DR AlphaFoldDB; P41183; -.
DR SMR; P41183; -.
DR BioGRID; 198327; 8.
DR DIP; DIP-59432N; -.
DR IntAct; P41183; 4.
DR STRING; 10090.ENSMUSP00000023151; -.
DR iPTMnet; P41183; -.
DR PhosphoSitePlus; P41183; -.
DR jPOST; P41183; -.
DR PaxDb; P41183; -.
DR PRIDE; P41183; -.
DR ProteomicsDB; 273479; -.
DR Antibodypedia; 1434; 1130 antibodies from 50 providers.
DR DNASU; 12053; -.
DR Ensembl; ENSMUST00000023151; ENSMUSP00000023151; ENSMUSG00000022508.
DR GeneID; 12053; -.
DR KEGG; mmu:12053; -.
DR UCSC; uc007ytz.1; mouse.
DR CTD; 604; -.
DR MGI; MGI:107187; Bcl6.
DR VEuPathDB; HostDB:ENSMUSG00000022508; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156311; -.
DR HOGENOM; CLU_024196_1_0_1; -.
DR InParanoid; P41183; -.
DR OMA; RMPMANP; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P41183; -.
DR TreeFam; TF330912; -.
DR BioGRID-ORCS; 12053; 3 hits in 113 CRISPR screens.
DR ChiTaRS; Bcl6; mouse.
DR PRO; PR:P41183; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P41183; protein.
DR Bgee; ENSMUSG00000022508; Expressed in facial nucleus and 252 other tissues.
DR ExpressionAtlas; P41183; baseline and differential.
DR Genevisible; P41183; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0042382; C:paraspeckles; ISO:MGI.
DR GO; GO:0005657; C:replication fork; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0001161; F:intronic transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0030183; P:B cell differentiation; IGI:MGI.
DR GO; GO:0042100; P:B cell proliferation; IMP:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR GO; GO:0002467; P:germinal center formation; IMP:MGI.
DR GO; GO:0016575; P:histone deacetylation; IGI:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0048289; P:isotype switching to IgE isotypes; IMP:MGI.
DR GO; GO:0070661; P:leukocyte proliferation; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IMP:MGI.
DR GO; GO:2000773; P:negative regulation of cellular senescence; IMP:MGI.
DR GO; GO:0048294; P:negative regulation of isotype switching to IgE isotypes; IMP:MGI.
DR GO; GO:0070664; P:negative regulation of leukocyte proliferation; IMP:MGI.
DR GO; GO:0032764; P:negative regulation of mast cell cytokine production; IMP:MGI.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IGI:MGI.
DR GO; GO:1900099; P:negative regulation of plasma cell differentiation; IMP:MGI.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:MGI.
DR GO; GO:0045629; P:negative regulation of T-helper 2 cell differentiation; IGI:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0002829; P:negative regulation of type 2 immune response; IGI:MGI.
DR GO; GO:0002317; P:plasma cell differentiation; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:MGI.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IGI:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:MGI.
DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0021859; P:pyramidal neuron differentiation; IDA:MGI.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; IMP:MGI.
DR GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR GO; GO:0043380; P:regulation of memory T cell differentiation; IMP:MGI.
DR GO; GO:0042129; P:regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0045064; P:T-helper 2 cell differentiation; IGI:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0042092; P:type 2 immune response; IMP:MGI.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Acetylation; Activator; DNA-binding; Immunity; Inflammatory response;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..707
FT /note="B-cell lymphoma 6 protein homolog"
FT /id="PRO_0000047099"
FT DOMAIN 32..99
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 519..542
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 547..569
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 575..597
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 603..625
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 631..653
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 659..682
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 275..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..380
FT /note="Required for interaction with NuRD complex and for
FT transcriptional repressor activity"
FT REGION 405..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 344
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P41182"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 380
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000250|UniProtKB:P41182"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 21
FT /note="N->K: Abolishes interaction with NCOR2; mice have
FT impaired GC formation and immunoglobulin affinity
FT maturation with lower proliferation and survival of GC B-
FT cells but normal differentiation of helper T-cell subsets
FT and inflammatory response; in macrophages, no effect on
FT transcriptional repression of genes encoding inflammatory
FT molecules; when associated with A-116. In macrophages, no
FT effect on competition with STAT5 for DNA-binding and
FT transcriptional repression of genes encoding inflammatory
FT molecules; when associated with A-116 and 377-Q--Q-380."
FT /evidence="ECO:0000269|PubMed:23455674,
FT ECO:0000269|PubMed:23911289"
FT MUTAGEN 116
FT /note="H->A: Abolishes interaction with NCOR2; mice have
FT impaired GC formation and immunoglobulin affinity
FT maturation with lower proliferation and survival of GC B-
FT cells but normal differentiation of helper T-cell subsets
FT and inflammatory response; in macrophages, no effect on
FT transcriptional repression of genes encoding inflammatory
FT molecules; when associated with K-21. In macrophages, no
FT effect on competition with STAT5 for DNA-binding and
FT transcriptional repression of genes encoding inflammatory
FT molecules; when associated with K-21 and 377-Q--Q-380."
FT /evidence="ECO:0000269|PubMed:23455674,
FT ECO:0000269|PubMed:23911289"
FT MUTAGEN 377..380
FT /note="KKYK->QQYQ: In macrophages, no effect on
FT transcriptional repression of genes encoding inflammatory
FT molecules. In macrophages, no effect on competition with
FT STAT5 for DNA-binding and transcriptional repression of
FT genes encoding inflammatory molecules; when associated with
FT K-21 and A-116."
FT /evidence="ECO:0000269|PubMed:23455674"
FT MUTAGEN 577..580
FT /note="CNIC->GNIG: In macrophages, inhibits competition
FT with STAT5 for DNA-binding and abolishes transcriptional
FT repression of genes encoding inflammatory molecules."
FT /evidence="ECO:0000269|PubMed:23455674"
FT CONFLICT 456
FT /note="A -> G (in Ref. 2; AAB17432)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 78982 MW; 2051DD808D32D5EC CRC64;
MASPADSCIQ FTRHASDVLL NLNRLRSRDI LTDVVIVVSR EQFRAHKTVL MACSGLFYSI
FTDQLKCNLS VINLDPEISP EGFCILLDFM YTSRLNLREG NIMAVMTTAM YLQMEHVVDT
CRKFIKASEA EMAPALKPPR EEFLNSRMLM PHDIMAYRGR EVVENNMPLR NTPGCESRAF
APPLYSGLST PPASYPMYSH LPLSTFLFSD EELRDAPRMP VANPFPKERA LPCDSARQVP
NEYSRPAMEV SPSLCHSNIY SPKEAVPEEA RSDIHYSVPE GPKPAVPSAR NAPYFPCDKA
SKEEERPSSE DEIALHFEPP NAPLNRKGLV SPQSPQKSDC QPNSPTESCS SKNACILQAS
GSPPAKSPTD PKACNWKKYK FIVLNSLNQN AKPEGSEQAE LGRLSPRAYP APPACQPPME
PANLDLQSPT KLSASGEDST IPQASRLNNL VNRSLAGSPR SSSESHSPLY MHPPKCTSCG
SQSPQHTEMC LHTAGPTFPE EMGETQSEYS DSSCENGTFF CNECDCRFSE EASLKRHTLQ
THSDKPYKCD RCQASFRYKG NLASHKTVHT GEKPYRCNIC GAQFNRPANL KTHTRIHSGE
KPYKCETCGA RFVQVAHLRA HVLIHTGEKP YPCEICGTRF RHLQTLKSHL RIHTGEKPYH
CEKCNLHFRH KSQLRLHLRQ KHGAITNTKV QYRVSAADLP PELPKAC
