BC11B_HUMAN
ID BC11B_HUMAN Reviewed; 894 AA.
AC Q9C0K0; Q9H162;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=B-cell lymphoma/leukemia 11B;
DE Short=BCL-11B;
DE AltName: Full=B-cell CLL/lymphoma 11B;
DE AltName: Full=COUP-TF-interacting protein 2;
DE AltName: Full=Radiation-induced tumor suppressor gene 1 protein;
DE Short=hRit1;
GN Name=BCL11B; Synonyms=CTIP2, RIT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=11719382; DOI=10.1182/blood.v98.12.3413;
RA Satterwhite E., Sonoki T., Willis T.G., Harder L., Nowak R., Arriola E.L.,
RA Liu H., Price H.P., Gesk S., Steinemann D., Schlegelberger B., Oscier D.G.,
RA Siebert R., Tucker P.W., Dyer M.J.;
RT "The BCL11 gene family: involvement of BCL11A in lymphoid malignancies.";
RL Blood 98:3413-3420(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
RX PubMed=12565905; DOI=10.1016/s0006-291x(02)03069-3;
RA Wakabayashi Y., Inoue J., Takahashi Y., Matsuki A., Kosugi-Okano H.,
RA Shinbo T., Mishima Y., Niwa O., Kominami R.;
RT "Homozygous deletions and point mutations of the Rit1/Bcl11b gene in gamma-
RT ray induced mouse thymic lymphomas.";
RL Biochem. Biophys. Res. Commun. 301:598-603(2003).
RN [3]
RP FUNCTION, AND INTERACTION WITH EP300.
RX PubMed=16809611; DOI=10.1182/blood-2006-05-021790;
RA Cismasiu V.B., Ghanta S., Duque J., Albu D.I., Chen H.M., Kasturi R.,
RA Avram D.;
RT "BCL11B participates in the activation of IL2 gene expression in CD4+ T
RT lymphocytes.";
RL Blood 108:2695-2702(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; THR-120; SER-256;
RP THR-260; SER-277; SER-358; THR-376; SER-381; SER-398; THR-417; SER-483;
RP SER-488; SER-496; SER-497; SER-678 AND SER-765, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-851, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-591 AND LYS-887, SUMOYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-137 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-137; LYS-591; LYS-617; LYS-686;
RP LYS-723 AND LYS-887, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-137 (ISOFORM
RP 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] PRO-331.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [10]
RP VARIANTS VAL-32 AND SER-229.
RX PubMed=21220648; DOI=10.1001/archneurol.2010.351;
RA Daoud H., Valdmanis P.N., Gros-Louis F., Belzil V., Spiegelman D.,
RA Henrion E., Diallo O., Desjarlais A., Gauthier J., Camu W., Dion P.A.,
RA Rouleau G.A.;
RT "Resequencing of 29 candidate genes in patients with familial and sporadic
RT amyotrophic lateral sclerosis.";
RL Arch. Neurol. 68:587-593(2011).
RN [11]
RP FUNCTION, INTERACTION WITH EP300, INVOLVEMENT IN IMD49, VARIANT IMD49
RP LYS-441, AND CHARACTERIZATION OF VARIANT IMD49 LYS-441.
RX PubMed=27959755; DOI=10.1056/nejmoa1509164;
RA Punwani D., Zhang Y., Yu J., Cowan M.J., Rana S., Kwan A., Adhikari A.N.,
RA Lizama C.O., Mendelsohn B.A., Fahl S.P., Chellappan A., Srinivasan R.,
RA Brenner S.E., Wiest D.L., Puck J.M.;
RT "Multisystem anomalies in severe combined immunodeficiency with mutant
RT BCL11B.";
RL N. Engl. J. Med. 375:2165-2176(2016).
RN [12]
RP INVOLVEMENT IN IDDSFTA, VARIANT IMD49 LYS-807, AND VARIANT IDDSFTA
RP 499-GLU--SER-894 DEL.
RX PubMed=29985992; DOI=10.1093/brain/awy173;
RA Lessel D., Gehbauer C., Bramswig N.C., Schluth-Bolard C.,
RA Venkataramanappa S., van Gassen K.L.I., Hempel M., Haack T.B., Baresic A.,
RA Genetti C.A., Funari M.F.A., Lessel I., Kuhlmann L., Simon R., Liu P.,
RA Denecke J., Kuechler A., de Kruijff I., Shoukier M., Lek M., Mullen T.,
RA Luedecke H.J., Lerario A.M., Kobbe R., Krieger T., Demeer B., Lebrun M.,
RA Keren B., Nava C., Buratti J., Afenjar A., Shinawi M., Guillen Sacoto M.J.,
RA Gauthier J., Hamdan F.F., Laberge A.M., Campeau P.M., Louie R.J.,
RA Cathey S.S., Prinz I., Jorge A.A.L., Terhal P.A., Lenhard B., Wieczorek D.,
RA Strom T.M., Agrawal P.B., Britsch S., Tolosa E., Kubisch C.;
RT "BCL11B mutations in patients affected by a neurodevelopmental disorder
RT with reduced type 2 innate lymphoid cells.";
RL Brain 141:2299-2311(2018).
CC -!- FUNCTION: Key regulator of both differentiation and survival of T-
CC lymphocytes during thymocyte development in mammals. Essential in
CC controlling the responsiveness of hematopoietic stem cells to
CC chemotactic signals by modulating the expression of the receptors CCR7
CC and CCR9, which direct the movement of progenitor cells from the bone
CC marrow to the thymus (PubMed:27959755). Is a regulator of IL2 promoter
CC and enhances IL2 expression in activated CD4(+) T-lymphocytes
CC (PubMed:16809611). Tumor-suppressor that represses transcription
CC through direct, TFCOUP2-independent binding to a GC-rich response
CC element (By similarity). May also function in the P53-signaling pathway
CC (By similarity). {ECO:0000250|UniProtKB:Q99PV8,
CC ECO:0000269|PubMed:16809611, ECO:0000269|PubMed:27959755}.
CC -!- SUBUNIT: Interacts with TFCOUP1, SIRT1, ARP1 and EAR2 (By similarity).
CC Interacts with EP300; the interaction is detected in activated T-
CC lymphocytes, but not under resting conditions (PubMed:27959755).
CC {ECO:0000250|UniProtKB:Q99PV8, ECO:0000269|PubMed:27959755}.
CC -!- INTERACTION:
CC Q9C0K0; Q13547: HDAC1; NbExp=3; IntAct=EBI-6597578, EBI-301834;
CC Q9C0K0; Q92769: HDAC2; NbExp=3; IntAct=EBI-6597578, EBI-301821;
CC Q9C0K0; O43463: SUV39H1; NbExp=3; IntAct=EBI-6597578, EBI-349968;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q9C0K0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0K0-2; Sequence=VSP_009565;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and in malignant T-cell
CC lines derived from patients with adult T-cell leukemia/lymphoma.
CC -!- PTM: Sumoylated with SUMO1. {ECO:0000250}.
CC -!- DISEASE: Immunodeficiency 49 (IMD49) [MIM:617237]: A form of severe
CC combined immunodeficiency characterized by severe T-cell lymphopenia,
CC no detectable T-cell receptor excision circles, no naive helper CD4+ T-
CC cells, and impaired T-cell proliferative response. In addition to
CC primary immunodeficiency, affected individuals manifest multiple
CC abnormal systemic features, including severe delayed psychomotor
CC development, intellectual disability, spastic quadriplegia, and
CC craniofacial abnormalities. {ECO:0000269|PubMed:27959755,
CC ECO:0000269|PubMed:29985992}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Intellectual developmental disorder with speech delay,
CC dysmorphic facies, and T-cell abnormalities (IDDSFTA) [MIM:618092]: An
CC autosomal dominant developmental disorder with onset in first months of
CC life, and characterized by delayed psychomotor development with
CC intellectual disability and speech delay. Additional features include
CC autistic features, attention deficit-hyperactivity disorder, anxiety,
CC and other behavioral abnormalities. Some patients suffer from recurrent
CC infections, asthma and allergies. {ECO:0000269|PubMed:29985992}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to exon skipping. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BCL11BID392.html";
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DR EMBL; AJ404614; CAC17726.1; -; mRNA.
DR EMBL; AB043584; BAB32731.1; -; mRNA.
DR CCDS; CCDS9949.1; -. [Q9C0K0-2]
DR CCDS; CCDS9950.1; -. [Q9C0K0-1]
DR RefSeq; NP_001269166.1; NM_001282237.1.
DR RefSeq; NP_001269167.1; NM_001282238.1.
DR RefSeq; NP_075049.1; NM_022898.2. [Q9C0K0-2]
DR RefSeq; NP_612808.1; NM_138576.3. [Q9C0K0-1]
DR AlphaFoldDB; Q9C0K0; -.
DR SMR; Q9C0K0; -.
DR BioGRID; 122343; 68.
DR DIP; DIP-44025N; -.
DR IntAct; Q9C0K0; 11.
DR MINT; Q9C0K0; -.
DR STRING; 9606.ENSP00000349723; -.
DR iPTMnet; Q9C0K0; -.
DR MetOSite; Q9C0K0; -.
DR PhosphoSitePlus; Q9C0K0; -.
DR BioMuta; BCL11B; -.
DR DMDM; 44887723; -.
DR EPD; Q9C0K0; -.
DR jPOST; Q9C0K0; -.
DR MassIVE; Q9C0K0; -.
DR MaxQB; Q9C0K0; -.
DR PaxDb; Q9C0K0; -.
DR PeptideAtlas; Q9C0K0; -.
DR PRIDE; Q9C0K0; -.
DR ProteomicsDB; 80066; -. [Q9C0K0-1]
DR ProteomicsDB; 80067; -. [Q9C0K0-2]
DR Antibodypedia; 27407; 284 antibodies from 36 providers.
DR DNASU; 64919; -.
DR Ensembl; ENST00000345514.2; ENSP00000280435.6; ENSG00000127152.18. [Q9C0K0-2]
DR Ensembl; ENST00000357195.8; ENSP00000349723.3; ENSG00000127152.18. [Q9C0K0-1]
DR GeneID; 64919; -.
DR KEGG; hsa:64919; -.
DR MANE-Select; ENST00000357195.8; ENSP00000349723.3; NM_138576.4; NP_612808.1.
DR UCSC; uc001yga.5; human. [Q9C0K0-1]
DR CTD; 64919; -.
DR DisGeNET; 64919; -.
DR GeneCards; BCL11B; -.
DR HGNC; HGNC:13222; BCL11B.
DR HPA; ENSG00000127152; Group enriched (brain, lymphoid tissue, skin).
DR MalaCards; BCL11B; -.
DR MIM; 606558; gene.
DR MIM; 617237; phenotype.
DR MIM; 618092; phenotype.
DR neXtProt; NX_Q9C0K0; -.
DR OpenTargets; ENSG00000127152; -.
DR PharmGKB; PA25301; -.
DR VEuPathDB; HostDB:ENSG00000127152; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161060; -.
DR InParanoid; Q9C0K0; -.
DR OMA; QENMAGP; -.
DR PhylomeDB; Q9C0K0; -.
DR TreeFam; TF318131; -.
DR PathwayCommons; Q9C0K0; -.
DR SignaLink; Q9C0K0; -.
DR SIGNOR; Q9C0K0; -.
DR BioGRID-ORCS; 64919; 19 hits in 1092 CRISPR screens.
DR ChiTaRS; BCL11B; human.
DR GeneWiki; BCL11B; -.
DR GenomeRNAi; 64919; -.
DR Pharos; Q9C0K0; Tbio.
DR PRO; PR:Q9C0K0; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9C0K0; protein.
DR Bgee; ENSG00000127152; Expressed in thymus and 148 other tissues.
DR ExpressionAtlas; Q9C0K0; baseline and differential.
DR Genevisible; Q9C0K0; HS.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0046632; P:alpha-beta T cell differentiation; IEA:Ensembl.
DR GO; GO:0021902; P:commitment of neuronal cell to specific neuron type in forebrain; IEA:Ensembl.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IEA:Ensembl.
DR GO; GO:0035701; P:hematopoietic stem cell migration; IMP:UniProtKB.
DR GO; GO:0003334; P:keratinocyte development; IEA:Ensembl.
DR GO; GO:0097535; P:lymphoid lineage cell migration into thymus; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0071678; P:olfactory bulb axon guidance; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0043368; P:positive T cell selection; IEA:Ensembl.
DR GO; GO:0031077; P:post-embryonic camera-type eye development; IEA:Ensembl.
DR GO; GO:0010837; P:regulation of keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IEA:Ensembl.
DR GO; GO:0045664; P:regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0021773; P:striatal medium spiny neuron differentiation; IEA:Ensembl.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0033153; P:T cell receptor V(D)J recombination; IEA:Ensembl.
DR GO; GO:0070242; P:thymocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disease variant;
KW Intellectual disability; Isopeptide bond; Metal-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; SCID;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..894
FT /note="B-cell lymphoma/leukemia 11B"
FT /id="PRO_0000047104"
FT ZN_FING 221..251
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 427..454
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 455..482
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 796..823
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 824..853
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 854..884
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 370..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..425
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..547
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PV8"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PV8"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 293
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q99PV8"
FT MOD_RES 322
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q99PV8"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 376
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PV8"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99PV8"
FT MOD_RES 417
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 754
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99PV8"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PV8"
FT MOD_RES 851
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 591
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 617
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 686
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 723
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 887
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 143..213
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11719382"
FT /id="VSP_009565"
FT VARIANT 32
FT /note="E -> V (in a patient with amyotrophic lateral
FT sclerosis)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065741"
FT VARIANT 229
FT /note="P -> S (in a patient with amyotrophic lateral
FT sclerosis; dbSNP:rs749837100)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065742"
FT VARIANT 331
FT /note="S -> P (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035554"
FT VARIANT 441
FT /note="N -> K (in IMD49; loss of stimulation of T-
FT lymphocyte development; dominant negative loss of
FT activation of IL2 expression; results in reduced binding to
FT known canonical promoters and abnormal binding to novel DNA
FT sites not recognized by the wild-type protein; no effect on
FT interaction with EP300; dbSNP:rs750610248)"
FT /evidence="ECO:0000269|PubMed:27959755"
FT /id="VAR_078423"
FT VARIANT 499..894
FT /note="Missing (in IDDSFTA)"
FT /evidence="ECO:0000269|PubMed:29985992"
FT /id="VAR_081174"
FT VARIANT 807
FT /note="N -> K (in IMD49; dbSNP:rs888230251)"
FT /evidence="ECO:0000269|PubMed:29985992"
FT /id="VAR_081175"
FT CROSSLNK Q9C0K0-2:137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
SQ SEQUENCE 894 AA; 95519 MW; DF6C467AE2EEC122 CRC64;
MSRRKQGNPQ HLSQRELITP EADHVEAAIL EEDEGLEIEE PSGLGLMVGG PDPDLLTCGQ
CQMNFPLGDI LVFIEHKRKQ CGGSLGACYD KALDKDSPPP SSRSELRKVS EPVEIGIQVT
PDEDDHLLSP TKGICPKQEN IAGPCRPAQL PAVAPIAASS HPHSSVITSP LRALGALPPC
LPLPCCSARP VSGDGTQGEG QTEAPFGCQC QLSGKDEPSS YICTTCKQPF NSAWFLLQHA
QNTHGFRIYL EPGPASSSLT PRLTIPPPLG PEAVAQSPLM NFLGDSNPFN LLRMTGPILR
DHPGFGEGRL PGTPPLFSPP PRHHLDPHRL SAEEMGLVAQ HPSAFDRVMR LNPMAIDSPA
MDFSRRLREL AGNSSTPPPV SPGRGNPMHR LLNPFQPSPK SPFLSTPPLP PMPPGGTPPP
QPPAKSKSCE FCGKTFKFQS NLIVHRRSHT GEKPYKCQLC DHACSQASKL KRHMKTHMHK
AGSLAGRSDD GLSAASSPEP GTSELAGEGL KAADGDFRHH ESDPSLGHEP EEEDEEEEEE
EEELLLENES RPESSFSMDS ELSRNRENGG GGVPGVPGAG GGAAKALADE KALVLGKVME
NVGLGALPQY GELLADKQKR GAFLKRAAGG GDAGDDDDAG GCGDAGAGGA VNGRGGGFAP
GTEPFPGLFP RKPAPLPSPG LNSAAKRIKV EKDLELPPAA LIPSENVYSQ WLVGYAASRH
FMKDPFLGFT DARQSPFATS SEHSSENGSL RFSTPPGDLL DGGLSGRSGT ASGGSTPHLG
GPGPGRPSSK EGRRSDTCEY CGKVFKNCSN LTVHRRSHTG ERPYKCELCN YACAQSSKLT
RHMKTHGQIG KEVYRCDICQ MPFSVYSTLE KHMKKWHGEH LLTNDVKIEQ AERS
