BC11A_MOUSE
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 03-AUG-2022, entry version 179.
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 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};
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; 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.ENSMUSP00000000881; -.
DR iPTMnet; Q9QYE3; -.
DR PhosphoSitePlus; Q9QYE3; -.
DR MaxQB; Q9QYE3; -.
DR PaxDb; Q9QYE3; -.
DR PeptideAtlas; Q9QYE3; -.
DR PRIDE; 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; 473 antibodies from 37 providers.
DR DNASU; 14025; -.
DR Ensembl; ENSMUST00000000881; ENSMUSP00000000881; ENSMUSG00000000861. [Q9QYE3-1]
DR Ensembl; ENSMUST00000109516; ENSMUSP00000105142; ENSMUSG00000000861. [Q9QYE3-13]
DR Ensembl; ENSMUST00000118955; ENSMUSP00000112948; ENSMUSG00000000861. [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 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; 224109at2759; -.
DR PhylomeDB; Q9QYE3; -.
DR TreeFam; TF318131; -.
DR BioGRID-ORCS; 14025; 0 hits in 74 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 230 other tissues.
DR ExpressionAtlas; Q9QYE3; baseline and differential.
DR Genevisible; Q9QYE3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:0014069; C:postsynaptic density; 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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
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
