BC11B_MOUSE
ID BC11B_MOUSE Reviewed; 884 AA.
AC Q99PV8; Q8C2I1; Q99PV6; Q99PV7; Q9JLF8;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
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=mRit1;
GN Name=Bcl11b; Synonyms=Ctip2, Rit1;
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 VARIANTS THR-676;
RP CYS-783 AND SER-849.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH TFCOUP1; EAR2
RP AND ARP1.
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] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 331-884.
RC STRAIN=NOD; TISSUE=Thymus;
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 [5]
RP FUNCTION.
RX PubMed=12717433; DOI=10.1038/ni927;
RA Wakabayashi Y., Watanabe H., Inoue J., Takeda N., Sakata J., Mishima Y.,
RA Hitomi J., Yamamoto T., Utsuyama M., Niwa O., Aizawa S., Kominami R.;
RT "Bcl11b is required for differentiation and survival of alphabeta T
RT lymphocytes.";
RL Nat. Immunol. 4:533-539(2003).
RN [6]
RP INTERACTION WITH SIRT1.
RX PubMed=12930829; DOI=10.1074/jbc.m307477200;
RA Senawong T., Peterson V.J., Avram D., Shepherd D.M., Frye R.A., Minucci S.,
RA Leid M.;
RT "Involvement of the histone deacetylase SIRT1 in chicken ovalbumin upstream
RT promoter transcription factor (COUP-TF)-interacting protein 2-mediated
RT transcriptional repression.";
RL J. Biol. Chem. 278:43041-43050(2003).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-109; SER-128;
RP THR-260; THR-376; SER-381; SER-401; THR-406; THR-416; SER-495; SER-496;
RP THR-744 AND SER-762, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP SUMOYLATION WITH SUMO1.
RX PubMed=23213215; DOI=10.1073/pnas.1215366110;
RA Tirard M., Hsiao H.H., Nikolov M., Urlaub H., Melchior F., Brose N.;
RT "In vivo localization and identification of SUMOylated proteins in the
RT brain of His6-HA-SUMO1 knock-in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:21122-21127(2012).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-293 AND ARG-322, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and 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).
CC -!- FUNCTION: Key regulator of both differentiation and survival of T-
CC lymphocytes during thymocyte development in mammals (PubMed:12717433).
CC Essential in controlling the responsiveness of hematopoietic stem cells
CC to chemotactic signals by modulating the expression of receptors CCR7
CC and CCR9, which direct the movement of progenitor cells from the bone
CC marrow to the thymus (By similarity). Is a regulator of IL2 promoter
CC and enhances IL2 expression in activated CD4(+) T-lymphocytes
CC (PubMed:16809611). Tumor-suppressor protein involved in T-cell
CC lymphomas. May function on the P53-signaling pathway. Repress
CC transcription through direct, TFCOUP2-independent binding to a GC-rich
CC response element. {ECO:0000250|UniProtKB:Q9C0K0,
CC ECO:0000269|PubMed:12717433, ECO:0000269|PubMed:16809611}.
CC -!- SUBUNIT: Interacts with TFCOUP1, SIRT1, ARP1 and EAR2 (PubMed:10744719,
CC PubMed:12930829). Interacts with EP300; the interaction is detected in
CC activated T-lymphocytes, but not under resting conditions (By
CC similarity). {ECO:0000250|UniProtKB:Q9C0K0,
CC ECO:0000269|PubMed:10744719, ECO:0000269|PubMed:12930829}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q99PV8-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q99PV8-2; Sequence=VSP_009568;
CC Name=3; Synonyms=Gamma;
CC IsoId=Q99PV8-3; Sequence=VSP_009566;
CC -!- TISSUE SPECIFICITY: Expressed in brain and thymus. Expressed in splenic
CC CD4(+) T-lymphocytes (PubMed:16809611). {ECO:0000269|PubMed:16809611}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the developing embryo.
CC -!- PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:23213215}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to exon skipping. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to exon skipping. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF63683.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB043551; BAB32728.1; -; mRNA.
DR EMBL; AB043553; BAB32729.1; -; mRNA.
DR EMBL; AB043583; BAB32730.1; -; mRNA.
DR EMBL; AF186019; AAF63683.1; ALT_FRAME; mRNA.
DR EMBL; BC019503; AAH19503.1; -; mRNA.
DR EMBL; AK088588; BAC40438.1; -; mRNA.
DR CCDS; CCDS36552.1; -. [Q99PV8-2]
DR CCDS; CCDS36553.1; -. [Q99PV8-1]
DR CCDS; CCDS70419.1; -. [Q99PV8-3]
DR RefSeq; NP_001073352.1; NM_001079883.1. [Q99PV8-1]
DR RefSeq; NP_001273272.1; NM_001286343.1.
DR RefSeq; NP_067374.2; NM_021399.2. [Q99PV8-2]
DR AlphaFoldDB; Q99PV8; -.
DR SMR; Q99PV8; -.
DR BioGRID; 208391; 5.
DR IntAct; Q99PV8; 3.
DR STRING; 10090.ENSMUSP00000068258; -.
DR iPTMnet; Q99PV8; -.
DR PhosphoSitePlus; Q99PV8; -.
DR EPD; Q99PV8; -.
DR jPOST; Q99PV8; -.
DR MaxQB; Q99PV8; -.
DR PaxDb; Q99PV8; -.
DR PeptideAtlas; Q99PV8; -.
DR PRIDE; Q99PV8; -.
DR ProteomicsDB; 277113; -. [Q99PV8-1]
DR ProteomicsDB; 277114; -. [Q99PV8-2]
DR ProteomicsDB; 277115; -. [Q99PV8-3]
DR Antibodypedia; 27407; 284 antibodies from 36 providers.
DR DNASU; 58208; -.
DR Ensembl; ENSMUST00000066060; ENSMUSP00000068258; ENSMUSG00000048251. [Q99PV8-1]
DR Ensembl; ENSMUST00000109891; ENSMUSP00000105517; ENSMUSG00000048251. [Q99PV8-2]
DR GeneID; 58208; -.
DR KEGG; mmu:58208; -.
DR UCSC; uc007ozh.1; mouse. [Q99PV8-1]
DR UCSC; uc007ozi.1; mouse. [Q99PV8-2]
DR CTD; 64919; -.
DR MGI; MGI:1929913; Bcl11b.
DR VEuPathDB; HostDB:ENSMUSG00000048251; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161060; -.
DR InParanoid; Q99PV8; -.
DR OMA; QENMAGP; -.
DR OrthoDB; 224109at2759; -.
DR PhylomeDB; Q99PV8; -.
DR TreeFam; TF318131; -.
DR BioGRID-ORCS; 58208; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Bcl11b; mouse.
DR PRO; PR:Q99PV8; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q99PV8; protein.
DR Bgee; ENSMUSG00000048251; Expressed in dorsal striatum and 199 other tissues.
DR ExpressionAtlas; Q99PV8; baseline and differential.
DR Genevisible; Q99PV8; MM.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0046632; P:alpha-beta T cell differentiation; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0021953; P:central nervous system neuron differentiation; IGI:MGI.
DR GO; GO:0021902; P:commitment of neuronal cell to specific neuron type in forebrain; IGI:MGI.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
DR GO; GO:0035701; P:hematopoietic stem cell migration; ISS:UniProtKB.
DR GO; GO:0003334; P:keratinocyte development; IMP:MGI.
DR GO; GO:0097535; P:lymphoid lineage cell migration into thymus; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0070233; P:negative regulation of T cell apoptotic process; IMP:MGI.
DR GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IMP:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0071678; P:olfactory bulb axon guidance; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0043368; P:positive T cell selection; IMP:MGI.
DR GO; GO:0031077; P:post-embryonic camera-type eye development; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0010837; P:regulation of keratinocyte proliferation; IMP:MGI.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP:MGI.
DR GO; GO:0045664; P:regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0021773; P:striatal medium spiny neuron differentiation; IMP:MGI.
DR GO; GO:0070231; P:T cell apoptotic process; IMP:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR GO; GO:0033153; P:T cell receptor V(D)J recombination; IMP:MGI.
DR GO; GO:0070242; P:thymocyte apoptotic process; IMP:MGI.
DR GO; GO:0048538; P:thymus development; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
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; 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..884
FT /note="B-cell lymphoma/leukemia 11B"
FT /id="PRO_0000047105"
FT ZN_FING 221..251
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 426..453
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 454..481
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 786..813
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 814..843
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 844..874
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 370..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..424
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..544
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 119
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0K0"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0K0"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0K0"
FT MOD_RES 293
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 322
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0K0"
FT MOD_RES 376
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0K0"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 416
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0K0"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0K0"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0K0"
FT MOD_RES 744
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0K0"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 841
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0K0"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9C0K0"
FT CROSSLNK 587
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9C0K0"
FT CROSSLNK 676
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9C0K0"
FT CROSSLNK 713
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9C0K0"
FT CROSSLNK 877
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9C0K0"
FT VAR_SEQ 21..214
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12565905"
FT /id="VSP_009566"
FT VAR_SEQ 142..213
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10744719,
FT ECO:0000303|PubMed:12565905, ECO:0000303|PubMed:15489334"
FT /id="VSP_009568"
FT VARIANT 676
FT /note="K -> T (in gamma induced thymic lymphomas)"
FT /evidence="ECO:0000269|PubMed:12565905"
FT VARIANT 783
FT /note="R -> C (in gamma induced thymic lymphomas)"
FT /evidence="ECO:0000269|PubMed:12565905"
FT VARIANT 849
FT /note="C -> S (in gamma induced thymic lymphomas)"
FT /evidence="ECO:0000269|PubMed:12565905"
FT CONFLICT 20
FT /note="P -> R (in Ref. 1; BAB32730)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="P -> S (in Ref. 2; AAF63683)"
FT /evidence="ECO:0000305"
FT CONFLICT 806..807
FT /note="RS -> KN (in Ref. 2; AAF63683)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 884 AA; 94566 MW; 9A86B7E34450B2F2 CRC64;
MSRRKQGNPQ HLSQRELITP EADHVEATIL EEDEGLEIEE PSSLGLMVGG PDPDLLTCGQ
CQMNFPLGDI LVFIEHKKKQ CGGLGPCYDK VLDKSSPPPS SRSELRRVSE PVEIGIQVTP
DEDDHLLSPT KGICPKQENI AGPCRPAQLP SMAPIAASSS HPPTSVITSP LRALGVLPPC
FPLPCCGARP ISGDGTQGEG QMEAPFGCQC ELSGKDEPSS YICTTCKQPF NSAWFLLQHA
QNTHGFRIYL EPGPASTSLT PRLTIPPPLG PETVAQSPLM NFLGDSNPFN LLRMTGPILR
DHPGFGEGRL PGTPPLFSPP PRHHLDPHRL SAEEMGLVAQ HPSAFDRVMR LNPMAIDSPA
MDFSRRLREL AGNSSTPPPV SPGRGNPMHR LLNPFQPSPK SPFLSTPPLP PMPAGTPPPQ
PPAKSKSCEF CGKTFKFQSN LIVHRRSHTG EKPYKCQLCD HACSQASKLK RHMKTHMHKA
GSLAGRSDDG LSAASSPEPG TSELPGDLKA ADGDFRHHES DPSLGPEPED DEDEEEEEEE
LLLENESRPE SSFSMDSELG RGRENGGGVP PGVAGAGAAA AALADEKALA LGKVMEDAGL
GALPQYGEKR GAFLKRAGDT GDAGAVGCGD AGAPGAVNGR GGAFAPGAEP FPALFPRKPA
PLPSPGLGGP ALHAAKRIKV EKDLELPPAA LIPSENVYSQ WLVGYAASRH FMKDPFLGFT
DARQSPFATS SEHSSENGSL RFSTPPGDLL DGGLSGRSGT ASGGSTPHLG GPGPGRPSSK
EGRRSDTCEY CGKVFKNCSN LTVHRRSHTG ERPYKCELCN YACAQSSKLT RHMKTHGQIG
KEVYRCDICQ MPFSVYSTLE KHMKKWHGEH LLTNDVKIEQ AERS
