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   27-MAR-2024, entry version 179.
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="https://atlasgeneticsoncology.org/gene/392/BCL11B";
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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; 69.
DR   DIP; DIP-44025N; -.
DR   IntAct; Q9C0K0; 11.
DR   MINT; Q9C0K0; -.
DR   STRING; 9606.ENSP00000349723; -.
DR   GlyGen; Q9C0K0; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000349723; -.
DR   PeptideAtlas; Q9C0K0; -.
DR   ProteomicsDB; 80066; -. [Q9C0K0-1]
DR   ProteomicsDB; 80067; -. [Q9C0K0-2]
DR   Antibodypedia; 27407; 339 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   AGR; HGNC:13222; -.
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; CFACGYC; -.
DR   OrthoDB; 5351439at2759; -.
DR   PhylomeDB; Q9C0K0; -.
DR   TreeFam; TF318131; -.
DR   PathwayCommons; Q9C0K0; -.
DR   SignaLink; Q9C0K0; -.
DR   SIGNOR; Q9C0K0; -.
DR   BioGRID-ORCS; 64919; 22 hits in 1169 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 149 other cell types or tissues.
DR   ExpressionAtlas; Q9C0K0; baseline and differential.
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: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   Gene3D; 3.30.160.60; Classic Zinc Finger; 5.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45993; B-CELL LYMPHOMA/LEUKEMIA 11; 1.
DR   PANTHER; PTHR45993:SF4; B-CELL LYMPHOMA_LEUKEMIA 11B; 1.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
DR   Genevisible; Q9C0K0; HS.
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
FT                   T-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
//