ID MYB_MOUSE Reviewed; 636 AA. AC P06876; E9QMG8; Q61929; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 27-MAR-2024, entry version 213. DE RecName: Full=Transcriptional activator Myb; DE AltName: Full=Proto-oncogene c-Myb; GN Name=Myb; 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 [GENOMIC DNA / MRNA]. RX PubMed=3010282; DOI=10.1073/pnas.83.10.3204; RA Bender T.P., Kuehl W.M.; RT "Murine myb protooncogene mRNA: cDNA sequence and evidence for 5' RT heterogeneity."; RL Proc. Natl. Acad. Sci. U.S.A. 83:3204-3208(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2998780; DOI=10.1002/j.1460-2075.1985.tb03884.x; RA Gonda T.J., Gough N.M., Dunn A.R., de Blaquiere J.; RT "Nucleotide sequence of cDNA clones of the murine myb proto-oncogene."; RL EMBO J. 4:2003-2008(1985). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3608990; DOI=10.1002/j.1460-2075.1987.tb02413.x; RA Watson R.J., Dyson P.J., McMahon J.; RT "Multiple c-myb transcript cap sites are variously utilized in cells of RT mouse haemopoietic origin."; RL EMBO J. 6:1643-1651(1987). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3033638; DOI=10.1073/pnas.84.10.3171; RA Rosson D., Dugan D., Reddy E.P.; RT "Aberrant splicing events that are induced by proviral integration: RT implications for myb oncogene activation."; RL Proc. Natl. Acad. Sci. U.S.A. 84:3171-3175(1987). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47. RX PubMed=2481264; DOI=10.1093/nar/17.23.9593; RA Sobieszczuk P.W., Gonda T.J., Dunn A.R.; RT "Structure and biological activity of the transcriptional initiation RT sequences of the murine c-myb oncogene."; RL Nucleic Acids Res. 17:9593-9611(1989). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 72-636. RX PubMed=3023843; DOI=10.1128/mcb.6.2.380-392.1986; RA Shen-Ong G.L.C., Morse H.C. III, Potter M., Mushinski F.; RT "Two modes of c-myb activation in virus-induced mouse myeloid tumors."; RL Mol. Cell. Biol. 6:380-392(1986). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 72-401. RX PubMed=3016644; DOI=10.1093/nar/14.13.5309; RA Lavu S., Reddy E.P.; RT "Structural organization and nucleotide sequence of mouse c-myb oncogene: RT activation in ABPL tumors is due to viral integration in an intron which RT results in the deletion of the 5' coding sequences."; RL Nucleic Acids Res. 14:5309-5320(1986). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-402. RX PubMed=3014527; DOI=10.1073/pnas.83.14.5010; RA Weinstein Y., Ihle J.N., Lavu S., Reddy P.E.; RT "Truncation of the c-myb gene by a retroviral integration in an interleukin RT 3-dependent myeloid leukemia cell line."; RL Proc. Natl. Acad. Sci. U.S.A. 83:5010-5014(1986). RN [11] RP DOMAIN C-TERMINAL. RX PubMed=2670562; DOI=10.1002/j.1460-2075.1989.tb03571.x; RA Gonda T.J., Buckmaster C., Ramsay R.G.; RT "Activation of c-myb by carboxy-terminal truncation: relationship to RT transformation of murine haemopoietic cells in vitro."; RL EMBO J. 8:1777-1783(1989). RN [12] RP NEGATIVE REGULATORY DOMAIN. RX PubMed=1923521; RA Hu Y., Ramsay R.G., Kanei-Ishii C., Ishii S., Gonda T.J.; RT "Transformation by carboxyl-deleted Myb reflects increased transactivating RT capacity and disruption of a negative regulatory domain."; RL Oncogene 6:1549-1553(1991). RN [13] RP DOMAIN LEUCINE-ZIPPER, AND NEGATIVE AUTOREGULATION. RX PubMed=8408047; DOI=10.1016/s0021-9258(20)80628-0; RA Nomura T., Sakai N., Sarai A., Sudo T., Kanei-Ishii C., Ramsay R.G., RA Favier D., Gonda T.J., Ishii S.; RT "Negative autoregulation of c-Myb activity by homodimer formation through RT the leucine zipper."; RL J. Biol. Chem. 268:21914-21923(1993). RN [14] RP INTERACTION WITH MYBBP1A1. RX PubMed=9447996; DOI=10.1128/mcb.18.2.989; RA Tavner F.J., Simpson R., Tashiro S., Favier D., Jenkins N.A., Gilbert D.J., RA Copeland N.G., Macmillan E.M., Lutwyche J., Keough R.A., Ishii S., RA Gonda T.J.; RT "Molecular cloning reveals that the p160 Myb-binding protein is a novel, RT predominantly nucleolar protein which may play a role in transactivation by RT Myb."; RL Mol. Cell. Biol. 18:989-1002(1998). RN [15] RP INTERACTION WITH MAF. RX PubMed=9566892; DOI=10.1128/mcb.18.5.2729; RA Hedge S.P., Kumar A., Kurschner C., Shapiro L.H.; RT "c-Maf interacts with c-Myb to regulate transcription of an early myeloid RT gene during differentiation."; RL Mol. Cell. Biol. 18:2729-2737(1998). RN [16] RP INTERACTION WITH HIPK2 AND NLK. RX PubMed=15082531; DOI=10.1101/gad.1170604; RA Kanei-Ishii C., Ninomiya-Tsuji J., Tanikawa J., Nomura T., Ishitani T., RA Kishida S., Kokura K., Kurahashi T., Ichikawa-Iwata E., Kim Y., RA Matsumoto K., Ishii S.; RT "Wnt-1 signal induces phosphorylation and degradation of c-Myb protein via RT TAK1, HIPK2, and NLK."; RL Genes Dev. 18:816-829(2004). RN [17] RP FUNCTION, MUTAGENESIS OF LYS-499 AND LYS-523, SUMOYLATION AT LYS-499 AND RP LYS-523, AND SUBCELLULAR LOCATION. RX PubMed=16162816; DOI=10.1091/mbc.e05-08-0731; RA Morita Y., Kanei-Ishii C., Nomura T., Ishii S.; RT "TRAF7 sequesters c-Myb to the cytoplasm by stimulating its sumoylation."; RL Mol. Biol. Cell 16:5433-5444(2005). RN [18] RP INTERACTION WITH MAF. RX PubMed=17823980; DOI=10.1002/eji.200636979; RA Peng S., Lalani S., Leavenworth J.W., Ho I.-C., Pauza M.E.; RT "c-Maf interacts with c-Myb to down-regulate Bcl-2 expression and increase RT apoptosis in peripheral CD4 cells."; RL Eur. J. Immunol. 37:2868-2880(2007). RN [19] RP STRUCTURE BY NMR OF 142-193. RX PubMed=1631139; DOI=10.1073/pnas.89.14.6428; RA Ogata K., Hojo H., Aimoto S., Nakai T., Nakamura H., Sarai A., Ishii S., RA Nishimura Y.; RT "Solution structure of a DNA-binding unit of Myb: a helix-turn-helix- RT related motif with conserved tryptophans forming a hydrophobic core."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6428-6432(1992). RN [20] RP STRUCTURE BY NMR OF 89-192. RX PubMed=8365401; DOI=10.1111/j.1432-1033.1993.tb18126.x; RA Jamin N., Gabrielsen O.S., Gilles N., Lirsac P.-N., Toma F.; RT "Secondary structure of the DNA-binding domain of the c-Myb oncoprotein in RT solution. A multidimensional double and triple heteronuclear NMR study."; RL Eur. J. Biochem. 216:147-154(1993). RN [21] RP STRUCTURE BY NMR OF 38-89; 90-141 AND 142-193. RX PubMed=7796266; DOI=10.1038/nsb0495-309; RA Ogata K., Morikawa S., Nakamura H., Hojo H., Yoshimura S., Zhang R., RA Aimoto S., Ametani Y., Hirata Z., Sarai A., Ishii S., Nishimura Y.; RT "Comparison of the free and DNA-complexed forms of the DNA-binding domain RT from c-Myb."; RL Nat. Struct. Biol. 2:309-320(1995). RN [22] RP STRUCTURE BY NMR OF 140-193. RX PubMed=8942977; DOI=10.1073/pnas.93.24.13583; RA Furukawa K., Oda M., Nakamura H.; RT "A small engineered protein lacks structural uniqueness by increasing the RT side-chain conformational entropy."; RL Proc. Natl. Acad. Sci. U.S.A. 93:13583-13588(1996). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 35-193 IN COMPLEX WITH HUMAN RP CEBPB. RX PubMed=11792321; DOI=10.1016/s0092-8674(01)00636-5; RA Tahirov T.H., Sato K., Ichikawa-Iwata E., Sasaki M., Inoue-Bungo T., RA Shiina M., Kimura K., Takata S., Fujikawa A., Morii H., Kumasaka T., RA Yamamoto M., Ishii S., Ogata K.; RT "Mechanism of c-Myb-C/EBP beta cooperation from separated sites on a RT promoter."; RL Cell 108:57-70(2002). CC -!- FUNCTION: Transcriptional activator; DNA-binding protein that CC specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important CC role in the control of proliferation and differentiation of CC hematopoietic progenitor cells. {ECO:0000269|PubMed:16162816}. CC -!- SUBUNIT: Binds to HIPK1 (By similarity). Interacts with HIPK2, MAF, CC MYBBP1A and NLK. {ECO:0000250, ECO:0000269|PubMed:11792321, CC ECO:0000269|PubMed:15082531, ECO:0000269|PubMed:17823980, CC ECO:0000269|PubMed:9447996, ECO:0000269|PubMed:9566892}. CC -!- INTERACTION: CC P06876; Q9QZR5: Hipk2; NbExp=2; IntAct=EBI-366934, EBI-366905; CC P06876; P38531: HSF3; Xeno; NbExp=2; IntAct=EBI-366934, EBI-16212976; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16162816}. CC -!- DOMAIN: Comprised of 3 domains; an N-terminal DNA-binding domain, a CC centrally located transcriptional activation domain and a C-terminal CC domain involved in transcriptional repression. CC -!- DOMAIN: C-terminal truncated mutants display increased transactivation. CC -!- PTM: SUMOylated by TRAF7; leading to MYB transcriptional activity CC inhibition. {ECO:0000269|PubMed:16162816}. CC -!- PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent CC proteasomal degradation. {ECO:0000250}. CC -!- PTM: Phosphorylated by NLK on multiple sites, which induces proteasomal CC degradation. CC -!- PTM: Phosphorylated by HIPK1. This phosphorylation reduces MYB CC transcription factor activity but not MYB protein levels (By CC similarity). {ECO:0000250}. 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; M21169; AAA39782.1; -; Genomic_DNA. DR EMBL; M12848; AAB59713.1; -; mRNA. DR EMBL; X02774; CAA26552.1; -; mRNA. DR EMBL; M20210; AAA39783.1; -; Genomic_DNA. DR EMBL; AC153556; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC011513; AAH11513.1; -; mRNA. DR EMBL; X04099; CAA27724.1; -; Genomic_DNA. DR EMBL; X04100; CAA27724.1; JOINED; Genomic_DNA. DR EMBL; X04101; CAA27724.1; JOINED; Genomic_DNA. DR EMBL; X04102; CAA27724.1; JOINED; Genomic_DNA. DR EMBL; X04103; CAA27724.1; JOINED; Genomic_DNA. DR EMBL; X04104; CAA27724.1; JOINED; Genomic_DNA. DR EMBL; X16389; CAA34425.1; -; Genomic_DNA. DR EMBL; X16390; CAA34426.1; -; Genomic_DNA. DR EMBL; M13989; AAA39787.1; -; Genomic_DNA. DR EMBL; K03547; AAA39786.1; -; Genomic_DNA. DR CCDS; CCDS35861.1; -. DR PIR; A25285; TVMSMB. DR RefSeq; NP_001185843.1; NM_001198914.1. DR RefSeq; NP_034978.3; NM_010848.3. DR PDB; 1GUU; X-ray; 1.60 A; A=38-89. DR PDB; 1GV2; X-ray; 1.68 A; A=89-193. DR PDB; 1GV5; X-ray; 1.58 A; A=90-141. DR PDB; 1GVD; X-ray; 1.45 A; A=90-141. DR PDB; 1H88; X-ray; 2.80 A; C=37-193. DR PDB; 1H89; X-ray; 2.45 A; C=37-193. DR PDB; 1IDY; NMR; -; A=141-193. DR PDB; 1IDZ; NMR; -; A=141-193. DR PDB; 1MBE; NMR; -; A=38-89. DR PDB; 1MBF; NMR; -; A=38-89. DR PDB; 1MBG; NMR; -; A=90-141. DR PDB; 1MBH; NMR; -; A=90-141. DR PDB; 1MBJ; NMR; -; A=142-193. DR PDB; 1MBK; NMR; -; A=142-193. DR PDB; 1MSE; NMR; -; C=90-193. DR PDB; 1MSF; NMR; -; C=90-193. DR PDB; 1SB0; NMR; -; B=291-315. DR PDB; 2AGH; NMR; -; A=291-315. DR PDB; 6DMX; X-ray; 2.80 A; A/C/F/H=284-315. DR PDB; 6DNQ; X-ray; 2.35 A; A/C=284-315. DR PDBsum; 1GUU; -. DR PDBsum; 1GV2; -. DR PDBsum; 1GV5; -. DR PDBsum; 1GVD; -. DR PDBsum; 1H88; -. DR PDBsum; 1H89; -. DR PDBsum; 1IDY; -. DR PDBsum; 1IDZ; -. DR PDBsum; 1MBE; -. DR PDBsum; 1MBF; -. DR PDBsum; 1MBG; -. DR PDBsum; 1MBH; -. DR PDBsum; 1MBJ; -. DR PDBsum; 1MBK; -. DR PDBsum; 1MSE; -. DR PDBsum; 1MSF; -. DR PDBsum; 1SB0; -. DR PDBsum; 2AGH; -. DR PDBsum; 6DMX; -. DR PDBsum; 6DNQ; -. DR AlphaFoldDB; P06876; -. DR BMRB; P06876; -. DR SMR; P06876; -. DR BioGRID; 201631; 12. DR ComplexPortal; CPX-685; c-Myb-C/EBPbeta complex. DR DIP; DIP-31713N; -. DR ELM; P06876; -. DR IntAct; P06876; 4. DR STRING; 10090.ENSMUSP00000139699; -. DR GlyGen; P06876; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P06876; -. DR PhosphoSitePlus; P06876; -. DR EPD; P06876; -. DR jPOST; P06876; -. DR PaxDb; 10090-ENSMUSP00000020158; -. DR ProteomicsDB; 293592; -. DR Antibodypedia; 4486; 1028 antibodies from 43 providers. DR DNASU; 17863; -. DR Ensembl; ENSMUST00000020158.9; ENSMUSP00000020158.7; ENSMUSG00000019982.16. DR GeneID; 17863; -. DR KEGG; mmu:17863; -. DR UCSC; uc007eog.1; mouse. DR AGR; MGI:97249; -. DR CTD; 4602; -. DR MGI; MGI:97249; Myb. DR VEuPathDB; HostDB:ENSMUSG00000019982; -. DR eggNOG; KOG0048; Eukaryota. DR GeneTree; ENSGT00940000156248; -. DR HOGENOM; CLU_015440_2_2_1; -. DR InParanoid; P06876; -. DR OrthoDB; 20023at2759; -. DR TreeFam; TF326257; -. DR BioGRID-ORCS; 17863; 11 hits in 84 CRISPR screens. DR EvolutionaryTrace; P06876; -. DR PRO; PR:P06876; -. DR Proteomes; UP000000589; Chromosome 10. DR RNAct; P06876; Protein. DR Bgee; ENSMUSG00000019982; Expressed in thymus and 208 other cell types or tissues. DR ExpressionAtlas; P06876; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; EXP:ComplexPortal. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0071987; F:WD40-repeat domain binding; IDA:MGI. DR GO; GO:0030183; P:B cell differentiation; IMP:MGI. DR GO; GO:0006816; P:calcium ion transport; IMP:MGI. DR GO; GO:0071354; P:cellular response to interleukin-6; IDA:MGI. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI. DR GO; GO:0048566; P:embryonic digestive tract development; IMP:MGI. DR GO; GO:0030218; P:erythrocyte differentiation; ISO:MGI. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI. DR GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central. DR GO; GO:0061515; P:myeloid cell development; NAS:ComplexPortal. DR GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:1901533; P:negative regulation of hematopoietic progenitor cell differentiation; ISO:MGI. DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; ISO:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:MGI. DR GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; ISO:MGI. DR GO; GO:1904899; P:positive regulation of hepatic stellate cell proliferation; ISO:MGI. DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI. DR GO; GO:2000845; P:positive regulation of testosterone secretion; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; ISO:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI. DR GO; GO:0048536; P:spleen development; IMP:MGI. DR GO; GO:0017145; P:stem cell division; IMP:MGI. DR GO; GO:0045064; P:T-helper 2 cell differentiation; ISO:MGI. DR GO; GO:0048538; P:thymus development; IMP:MGI. DR CDD; cd00167; SANT; 3. DR Gene3D; 1.10.10.60; Homeodomain-like; 3. DR InterPro; IPR015395; C-myb_C. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR017930; Myb_dom. DR InterPro; IPR001005; SANT/Myb. DR InterPro; IPR012642; Tscrpt_reg_Wos2-domain. DR PANTHER; PTHR45614:SF25; MYB PROTEIN; 1. DR PANTHER; PTHR45614; MYB PROTEIN-RELATED; 1. DR Pfam; PF09316; Cmyb_C; 1. DR Pfam; PF07988; LMSTEN; 1. DR Pfam; PF00249; Myb_DNA-binding; 3. DR SMART; SM00717; SANT; 3. DR SUPFAM; SSF46689; Homeodomain-like; 2. DR PROSITE; PS51294; HTH_MYB; 3. DR Genevisible; P06876; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; DNA-binding; Isopeptide bond; KW Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Repeat; KW Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1..636 FT /note="Transcriptional activator Myb" FT /id="PRO_0000197049" FT DOMAIN 35..86 FT /note="HTH myb-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625" FT DOMAIN 87..142 FT /note="HTH myb-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625" FT DOMAIN 143..193 FT /note="HTH myb-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625" FT DNA_BIND 63..86 FT /note="H-T-H motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625" FT DNA_BIND 115..138 FT /note="H-T-H motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625" FT DNA_BIND 166..189 FT /note="H-T-H motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625" FT REGION 90..193 FT /note="Interaction with HIPK2 and NLK" FT /evidence="ECO:0000269|PubMed:15082531" FT REGION 275..327 FT /note="Transcriptional activation domain" FT /evidence="ECO:0000250" FT REGION 328..460 FT /note="Negative regulatory domain" FT REGION 337..368 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 375..396 FT /note="Leucine-zipper" FT MOD_RES 467 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P10242" FT MOD_RES 476 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10242" FT MOD_RES 528 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10242" FT MOD_RES 530 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10242" FT CROSSLNK 476 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P10242" FT CROSSLNK 499 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000269|PubMed:16162816" FT CROSSLNK 523 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000269|PubMed:16162816" FT MUTAGEN 499 FT /note="K->R: Complete loss of TRAF7-mediated SUMOylatiom; FT when associated with R-523." FT /evidence="ECO:0000269|PubMed:16162816" FT MUTAGEN 523 FT /note="K->R: Complete loss of TRAF7-mediated SUMOylatiom; FT when associated with R-499." FT /evidence="ECO:0000269|PubMed:16162816" FT CONFLICT 105 FT /note="E -> K (in Ref. 2; CAA26552)" FT /evidence="ECO:0000305" FT CONFLICT 201 FT /note="E -> K (in Ref. 2; CAA26552)" FT /evidence="ECO:0000305" FT CONFLICT 267 FT /note="V -> A (in Ref. 1; AAB59713)" FT /evidence="ECO:0000305" FT CONFLICT 402 FT /note="F -> V (in Ref. 10; AAA39786)" FT /evidence="ECO:0000305" FT CONFLICT 411 FT /note="S -> N (in Ref. 2; CAA26552)" FT /evidence="ECO:0000305" FT CONFLICT 500 FT /note="Q -> R (in Ref. 2; CAA26552 and 6; AAH11513)" FT /evidence="ECO:0000305" FT CONFLICT 525 FT /note="E -> A (in Ref. 2; CAA26552)" FT /evidence="ECO:0000305" FT HELIX 45..58 FT /evidence="ECO:0007829|PDB:1GUU" FT HELIX 63..68 FT /evidence="ECO:0007829|PDB:1GUU" FT HELIX 75..86 FT /evidence="ECO:0007829|PDB:1GUU" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:1MBH" FT HELIX 97..110 FT /evidence="ECO:0007829|PDB:1GVD" FT HELIX 115..119 FT /evidence="ECO:0007829|PDB:1GVD" FT HELIX 127..136 FT /evidence="ECO:0007829|PDB:1GVD" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:1MSE" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:1MBK" FT HELIX 149..162 FT /evidence="ECO:0007829|PDB:1GV2" FT HELIX 163..165 FT /evidence="ECO:0007829|PDB:1MSF" FT HELIX 166..170 FT /evidence="ECO:0007829|PDB:1GV2" FT STRAND 173..175 FT /evidence="ECO:0007829|PDB:1MBK" FT HELIX 178..188 FT /evidence="ECO:0007829|PDB:1GV2" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:1IDY" FT HELIX 291..303 FT /evidence="ECO:0007829|PDB:6DNQ" FT HELIX 305..308 FT /evidence="ECO:0007829|PDB:6DNQ" SQ SEQUENCE 636 AA; 71422 MW; 0C6308E584726D01 CRC64; MARRPRHSIY SSDEDDEDIE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK LKKLVEQNGT DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK HLKGRIGKQC RERWHNHLNP EVKKTSWTEE EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA IKNHWNSTMR RKVEQEGYLQ EPSKASQTPV ATSFQKNNHL MGFGHASPPS QLSPSGQSSV NSEYPYYHIA EAQNISSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL LLMSTENELK GQQALPTQNH TCSYPGWHST SIVDQTRPHG DSAPVSCLGE HHATPSLPAD PGSLPEESAS PARCMIVHQG TILDNVKNLL EFAETLQFID SFLNTSSNHE SSGLDAPTLP STPLIGHKLT PCRDQTVKTQ KENSIFRTPA IKRSILESSP RTPTPFKHAL AAQEIKYGPL KMLPQTPSHA VEDLQDVIKQ ESDESGIVAE FQESGPPLLK KIKQEVESPT EKSGNFFCSN HWAENSLSTQ LFSQASPVAD APNILTSSVL MTPVSEDEDN VLKAFTVPKN RPLVGPLQPC SGAWEPASCG KTEDQMTASG PARKYVNAFS ARTLVM //