ID   BC11A_MOUSE             Reviewed;         773 AA.
AC   Q9QYE3; Q80T89; Q8BLC7; Q8BLR4; Q8BWX3; Q921V4; Q9D0V2; Q9JIT4; Q9JLK8;
AC   Q9JLK9;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=B-cell lymphoma/leukemia 11A;
DE            Short=BCL-11A;
DE   AltName: Full=B-cell CLL/lymphoma 11A;
DE   AltName: Full=COUP-TF-interacting protein 1;
DE   AltName: Full=Ecotropic viral integration site 9 protein;
DE            Short=EVI-9;
GN   Name=Bcl11a; Synonyms=Ctip1, Evi9, Kiaa1809;
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] (ISOFORMS 1; 2 AND 3), AND FUNCTION.
RC   STRAIN=BXH/2;
RX   PubMed=10757802; DOI=10.1128/mcb.20.9.3178-3186.2000;
RA   Nakamura T., Yamazaki Y., Saiki Y., Moriyama M., Largaespada D.A.,
RA   Jenkins N.A., Copeland N.G.;
RT   "Evi9 encodes a novel zinc finger protein that physically interacts with
RT   BCL6, a known human B-cell proto-oncogene product.";
RL   Mol. Cell. Biol. 20:3178-3186(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH NR2F1; NR2F6
RP   AND NR2F2.
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=10744719; DOI=10.1074/jbc.275.14.10315;
RA   Avram D., Fields A., Pretty On Top K., Nevrivy D.J., Ishmael J.E., Leid M.;
RT   "Isolation of a novel family of C(2)H(2) zinc finger proteins implicated in
RT   transcriptional repression mediated by chicken ovalbumin upstream promoter
RT   transcription factor (COUP-TF) orphan nuclear receptors.";
RL   J. Biol. Chem. 275:10315-10322(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain, Brain cortex, Corpora quadrigemina, Embryo, and Spinal
RC   cord;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 8).
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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   [6]
RP   FUNCTION.
RX   PubMed=12717432; DOI=10.1038/ni925;
RA   Liu P., Keller J.R., Ortiz M., Tessarollo L., Rachel R.A., Nakamura T.,
RA   Jenkins N.A., Copeland N.G.;
RT   "Bcl11a is essential for normal lymphoid development.";
RL   Nat. Immunol. 4:525-532(2003).
RN   [7]
RP   SUMOYLATION AT LYS-634, INTERACTION WITH PIAS3, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF LYS-123 AND LYS-637.
RX   PubMed=18681895; DOI=10.1111/j.1365-2443.2008.01216.x;
RA   Kuwata T., Nakamura T.;
RT   "BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes in
RT   its nuclear body.";
RL   Genes Cells 13:931-940(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-332; SER-337;
RP   SER-446; SER-447; SER-608; SER-625; SER-630 AND THR-701, PHOSPHORYLATION
RP   [LARGE SCALE ANALYSIS] AT THR-214 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT THR-162 (ISOFORM 6), AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, 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   [9]
RP   FUNCTION.
RX   PubMed=23644491; DOI=10.1038/ng.2628;
RA   Kadoch C., Hargreaves D.C., Hodges C., Elias L., Ho L., Ranish J.,
RA   Crabtree G.R.;
RT   "Proteomic and bioinformatic analysis of mammalian SWI/SNF complexes
RT   identifies extensive roles in human malignancy.";
RL   Nat. Genet. 45:592-601(2013).
RN   [10]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-271, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [11]
RP   DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND FUNCTION.
RX   PubMed=27453576; DOI=10.1016/j.ajhg.2016.05.030;
RG   DDD Study;
RA   Dias C., Estruch S.B., Grmaham S.A., McRae J., Sawiak S.J., Hurst J.A.,
RA   Joss S.K., Holder S.E., Morton J.E., Turner C., Thevenon J., Mellul K.,
RA   Sanchez-Andrade G., Ibarra-Soria X., Deriziotis P., Santos R.F., Lee S.C.,
RA   Faivre L., Kleefstra T., Liu P., Hurles M.E., Fisher S.E., Logan D.W.;
RT   "BCL11A haploinsufficiency causes an intellectual disability syndrome and
RT   dysregulates transcription.";
RL   Am. J. Hum. Genet. 99:253-274(2016).
CC   -!- FUNCTION: Transcription factor (By similarity). Associated with the BAF
CC       SWI/SNF chromatin remodeling complex (PubMed:23644491). Binds to the
CC       5'-TGACCA-3' sequence motif in regulatory regions of target genes (By
CC       similarity). May play a role in hematopoiesis (PubMed:10757802).
CC       Essential factor in lymphopoiesis, required for B-cell formation in
CC       fetal liver (PubMed:12717432). May function as a modulator of the
CC       transcriptional repression activity of NR2F2 (PubMed:10744719).
CC       {ECO:0000250|UniProtKB:Q9H165, ECO:0000269|PubMed:10744719,
CC       ECO:0000269|PubMed:10757802, ECO:0000269|PubMed:12717432,
CC       ECO:0000269|PubMed:23644491}.
CC   -!- SUBUNIT: Interacts with NR2F1, PIAS3, NR2F2 and NR2F6 (PubMed:18681895,
CC       PubMed:10744719). Interacts with TBR1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9H165, ECO:0000269|PubMed:10744719,
CC       ECO:0000269|PubMed:18681895}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18681895}. Nucleus
CC       {ECO:0000269|PubMed:18681895}. Note=Associates with the nuclear body.
CC       Colocalizes with SUMO1 and SENP2 in nuclear speckles.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=1; Synonyms=a;
CC         IsoId=Q9QYE3-1; Sequence=Displayed;
CC       Name=2; Synonyms=b;
CC         IsoId=Q9QYE3-10; Sequence=VSP_009557, VSP_009563;
CC       Name=3; Synonyms=c;
CC         IsoId=Q9QYE3-11; Sequence=VSP_009560;
CC       Name=4;
CC         IsoId=Q9QYE3-12; Sequence=VSP_009556, VSP_009564;
CC       Name=5;
CC         IsoId=Q9QYE3-13; Sequence=VSP_009561, VSP_009562;
CC       Name=6;
CC         IsoId=Q9QYE3-14; Sequence=VSP_009558, VSP_009561, VSP_009562;
CC       Name=7;
CC         IsoId=Q9QYE3-15; Sequence=VSP_009559;
CC       Name=8;
CC         IsoId=Q9QYE3-16; Sequence=VSP_009557;
CC   -!- TISSUE SPECIFICITY: Isoforms are expressed in a tissue-specific
CC       fashion. Isoforms 1, isoform 2, and isoform 3 are expressed at similar
CC       levels in testis, kidney and spleen. Isoform 1 is expressed in the
CC       stomach, and isoform 2 is expressed exclusively in the lung.
CC       Overexpression following proviral integration in hematopoietic cells
CC       results in the generation of myeloid leukemia.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in the developing embryo.
CC       Expressed in developing brain from 10.5 dpc, with highest expression in
CC       the forebrain between 12.5 dpc and 14.5 dpc. Central nervous system
CC       expression persists throughout the postnatal period in the cortex,
CC       hippocampus, olfactory buld, and, to a lesser extent, in the
CC       cerebellum. {ECO:0000269|PubMed:27453576}.
CC   -!- DOMAIN: The N-terminus is involved in protein dimerization and in
CC       transactivation of transcription. {ECO:0000250|UniProtKB:Q9H165}.
CC   -!- DOMAIN: Zinc finger domains are necessary for sequence-specific binding
CC       to DNA. {ECO:0000250|UniProtKB:Q9H165}.
CC   -!- PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:18681895}.
CC   -!- DISRUPTION PHENOTYPE: Germline biallelic loss of Bcl11a leads to
CC       perinatal lethality. Bcl11a +/- mice have a significantly decreased
CC       brain volume, affecting both gray and white matter. The limbic system
CC       (hippocampus and amygdala) is among the brain regions that are more
CC       severely affected. Bcl11a +/- mice display normal novelty-seeking
CC       behavior but show long-term social memory defects, impaired
CC       sociability, and increased physical activity. Bcl11a +/- mice show
CC       dynamic postnatal transcriptional dysregulation in the brain.
CC       {ECO:0000269|PubMed:27453576}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF63682.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAC65839.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF051525; AAF22430.1; -; mRNA.
DR   EMBL; AF169036; AAF65928.1; -; mRNA.
DR   EMBL; AF169037; AAF65929.1; -; mRNA.
DR   EMBL; AF186018; AAF63682.1; ALT_FRAME; mRNA.
DR   EMBL; AK004395; BAB23285.1; -; mRNA.
DR   EMBL; AK043677; BAC31616.1; -; mRNA.
DR   EMBL; AK045556; BAC32416.1; -; mRNA.
DR   EMBL; AK049700; BAC33881.1; -; mRNA.
DR   EMBL; AK122557; BAC65839.1; ALT_INIT; mRNA.
DR   EMBL; BC010585; AAH10585.1; -; mRNA.
DR   EMBL; BC051418; AAH51418.1; -; mRNA.
DR   CCDS; CCDS24483.1; -. [Q9QYE3-1]
DR   CCDS; CCDS48758.1; -. [Q9QYE3-13]
DR   CCDS; CCDS48759.1; -. [Q9QYE3-14]
DR   PIR; PT0706; PT0706.
DR   RefSeq; NP_001152761.1; NM_001159289.1. [Q9QYE3-13]
DR   RefSeq; NP_001152762.1; NM_001159290.1. [Q9QYE3-14]
DR   RefSeq; NP_001229863.1; NM_001242934.1.
DR   RefSeq; NP_057916.1; NM_016707.3. [Q9QYE3-1]
DR   AlphaFoldDB; Q9QYE3; -.
DR   SMR; Q9QYE3; -.
DR   BioGRID; 199546; 3.
DR   IntAct; Q9QYE3; 1.
DR   STRING; 10090.ENSMUSP00000105140; -.
DR   iPTMnet; Q9QYE3; -.
DR   PhosphoSitePlus; Q9QYE3; -.
DR   MaxQB; Q9QYE3; -.
DR   PaxDb; 10090-ENSMUSP00000000881; -.
DR   PeptideAtlas; Q9QYE3; -.
DR   ProteomicsDB; 273468; -. [Q9QYE3-1]
DR   ProteomicsDB; 273469; -. [Q9QYE3-10]
DR   ProteomicsDB; 273470; -. [Q9QYE3-11]
DR   ProteomicsDB; 273471; -. [Q9QYE3-12]
DR   ProteomicsDB; 273472; -. [Q9QYE3-13]
DR   ProteomicsDB; 273473; -. [Q9QYE3-14]
DR   ProteomicsDB; 273474; -. [Q9QYE3-15]
DR   ProteomicsDB; 273475; -. [Q9QYE3-16]
DR   Antibodypedia; 30518; 534 antibodies from 37 providers.
DR   DNASU; 14025; -.
DR   Ensembl; ENSMUST00000000881.13; ENSMUSP00000000881.7; ENSMUSG00000000861.16. [Q9QYE3-1]
DR   Ensembl; ENSMUST00000109516.8; ENSMUSP00000105142.2; ENSMUSG00000000861.16. [Q9QYE3-13]
DR   Ensembl; ENSMUST00000118955.2; ENSMUSP00000112948.2; ENSMUSG00000000861.16. [Q9QYE3-14]
DR   GeneID; 14025; -.
DR   KEGG; mmu:14025; -.
DR   UCSC; uc007ifs.2; mouse. [Q9QYE3-15]
DR   UCSC; uc007ifu.2; mouse. [Q9QYE3-1]
DR   UCSC; uc007ifv.2; mouse. [Q9QYE3-13]
DR   UCSC; uc007ifw.2; mouse. [Q9QYE3-14]
DR   AGR; MGI:106190; -.
DR   CTD; 53335; -.
DR   MGI; MGI:106190; Bcl11a.
DR   VEuPathDB; HostDB:ENSMUSG00000000861; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000156983; -.
DR   HOGENOM; CLU_1237453_0_0_1; -.
DR   InParanoid; Q9QYE3; -.
DR   OrthoDB; 5351439at2759; -.
DR   PhylomeDB; Q9QYE3; -.
DR   TreeFam; TF318131; -.
DR   BioGRID-ORCS; 14025; 0 hits in 79 CRISPR screens.
DR   ChiTaRS; Bcl11a; mouse.
DR   PRO; PR:Q9QYE3; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9QYE3; Protein.
DR   Bgee; ENSMUSG00000000861; Expressed in rostral migratory stream and 233 other cell types or tissues.
DR   ExpressionAtlas; Q9QYE3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
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:0098794; C:postsynapse; ISO:MGI.
DR   GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
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; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:0001067; F:transcription regulatory region nucleic acid binding; ISO:MGI.
DR   GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR   GO; GO:0010467; P:gene expression; IMP:MGI.
DR   GO; GO:2000173; P:negative regulation of branching morphogenesis of a nerve; ISO:MGI.
DR   GO; GO:0048671; P:negative regulation of collateral sprouting; ISO:MGI.
DR   GO; GO:2000171; P:negative regulation of dendrite development; ISO:MGI.
DR   GO; GO:1903860; P:negative regulation of dendrite extension; ISO:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR   GO; GO:1904800; P:negative regulation of neuron remodeling; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:ARUK-UCL.
DR   GO; GO:0048672; P:positive regulation of collateral sprouting; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR   GO; GO:0016925; P:protein sumoylation; IMP:UniProtKB.
DR   GO; GO:0050773; P:regulation of dendrite development; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0030217; P:T cell differentiation; IMP:MGI.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 2.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45993; B-CELL LYMPHOMA/LEUKEMIA 11; 1.
DR   PANTHER; PTHR45993:SF5; B-CELL LYMPHOMA_LEUKEMIA 11A; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
DR   Genevisible; Q9QYE3; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Isopeptide bond; Metal-binding;
KW   Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..773
FT                   /note="B-cell lymphoma/leukemia 11A"
FT                   /id="PRO_0000047103"
FT   ZN_FING         170..193
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         377..399
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         405..429
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..210
FT                   /note="Required for nuclear body formation and for SUMO1
FT                   recruitment"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          471..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..374
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..508
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..600
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..699
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        747..773
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H165"
FT   MOD_RES         271
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         332
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         337
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         446
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         447
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         608
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         625
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         630
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         701
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        123
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H165"
FT   CROSSLNK        164
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H165"
FT   CROSSLNK        620
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H165"
FT   CROSSLNK        634
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000269|PubMed:18681895"
FT   VAR_SEQ         1..423
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_009556"
FT   VAR_SEQ         1..286
FT                   /note="Missing (in isoform 2 and isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:10757802,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_009557"
FT   VAR_SEQ         1..52
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_009558"
FT   VAR_SEQ         131..773
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:12693553"
FT                   /id="VSP_009559"
FT   VAR_SEQ         212..744
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10757802"
FT                   /id="VSP_009560"
FT   VAR_SEQ         212..243
FT                   /note="GIPSGLGAECPSQPPLHGIHIADNNPFNLLRI -> LHTPPFGVVPRELKMC
FT                   GSFRMEAQEPLSSEKL (in isoform 5 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_009561"
FT   VAR_SEQ         244..773
FT                   /note="Missing (in isoform 5 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_009562"
FT   VAR_SEQ         726..773
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10757802"
FT                   /id="VSP_009563"
FT   VAR_SEQ         745..773
FT                   /note="PSHTPVRRSTPRAQDVWQFSDGSSRTLKF -> EYCGKVFKNCSNLTVHRRS
FT                   HTGERPYKCELCNYACAQSSKLTRHMKTHGQVGKDVYKCEICKMPFSVYSTLEKHMKKW
FT                   HSDRVLNNDIKTE (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_009564"
FT   MUTAGEN         123
FT                   /note="K->R: No effect on sumoylation."
FT                   /evidence="ECO:0000269|PubMed:18681895"
FT   MUTAGEN         637
FT                   /note="K->R: Abolishes sumoylation. No effect on nuclear
FT                   body location."
FT                   /evidence="ECO:0000269|PubMed:18681895"
FT   CONFLICT        104
FT                   /note="Q -> K (in Ref. 3; BAB23285)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129
FT                   /note="D -> G (in Ref. 4; BAC65839)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        211
FT                   /note="V -> G (in Ref. 1; AAF65929)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        673
FT                   /note="F -> L (in Ref. 2; AAF63682)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        699
FT                   /note="F -> L (in Ref. 1; AAF65928)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        743
FT                   /note="T -> I (in Ref. 2; AAF63682)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        773
FT                   /note="F -> L (in Ref. 2; AAF63682)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q9QYE3-13:214
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         Q9QYE3-14:162
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   773 AA;  83855 MW;  3BD10B7F14AA9EC4 CRC64;
     MSRRKQGKPQ HLSKREFSPE PLEAILTDDE PDHGPLGAPE GDHDLLTCGQ CQMNFPLGDI
     LIFIEHKRKQ CNGSLCLEKG VDKPPSPSPI EMKKASNPVE VGIQVTPEDD DCLSTSSRGI
     CPKQEHIADK LLHWRGLSSP RSAHGALIPT PGMSAEYAPQ GICKDEPSSY TCTTCKQPFT
     SAWFLLQHAQ NTHGLRIYLE SEHGSPLTPR VGIPSGLGAE CPSQPPLHGI HIADNNPFNL
     LRIPGSVSRE ASGLAEGRFP PTPPLFSPPP RHHLDPHRIE RLGAEEMALA THHPSAFDRV
     LRLNPMAMEP PAMDFSRRLR ELAGNTSSPP LSPGRPSPMQ RLLQPFQPGS KPPFLATPPL
     PPLQSAPPPS QPPVKSKSCE FCGKTFKFQS NLVVHRRSHT GEKPYKCNLC DHACTQASKL
     KRHMKTHMHK SSPMTVKSDD GLSTASSPEP GTSDLVGSAS SALKSVVAKF KSENDPNLIP
     ENGDEEEEED DEEEEEEEEE EEEELTESER VDYGFGLSLE AARHHENSSR GAVVGVGDEG
     RALPDVMQGM VLSSMQHFSE AFHQVLGEKH KRSHLAEAEG HRDTCDEDSV AGESDRIDDG
     TVNGRGCSPG ESASGGLSKK LLLGSPSSLS PFSKRIKLEK EFDLPPAAMP NTENVYSQWL
     AGYAASRQLK DPFLTFGDSR QSPFASSSEH SSENGSLRFS TPPGELDGGI SGRSGTGSGG
     STPHISGPGP GRPSSKEGRR SDTCPSHTPV RRSTPRAQDV WQFSDGSSRT LKF
//