GenomeNet

Database: UniProt
Entry: P06876
LinkDB: P06876
Original site: P06876 
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   29-SEP-2021, entry version 201.
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;
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   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   [18]
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   [19]
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   [20]
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   [21]
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   [22]
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.
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.
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: 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   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.ENSMUSP00000020158; -.
DR   iPTMnet; P06876; -.
DR   PhosphoSitePlus; P06876; -.
DR   EPD; P06876; -.
DR   jPOST; P06876; -.
DR   PaxDb; P06876; -.
DR   PRIDE; P06876; -.
DR   ProteomicsDB; 293592; -.
DR   Antibodypedia; 4486; 933 antibodies.
DR   DNASU; 17863; -.
DR   Ensembl; ENSMUST00000020158; ENSMUSP00000020158; ENSMUSG00000019982.
DR   GeneID; 17863; -.
DR   KEGG; mmu:17863; -.
DR   UCSC; uc007eog.1; mouse.
DR   CTD; 4602; -.
DR   MGI; MGI:97249; Myb.
DR   VEuPathDB; HostDB:ENSMUSG00000019982; -.
DR   eggNOG; KOG0048; Eukaryota.
DR   GeneTree; ENSGT01040000241306; -.
DR   HOGENOM; CLU_015440_2_2_1; -.
DR   InParanoid; P06876; -.
DR   OrthoDB; 219341at2759; -.
DR   TreeFam; TF326257; -.
DR   BioGRID-ORCS; 17863; 9 hits in 66 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 266 other tissues.
DR   Genevisible; P06876; MM.
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: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:0006338; P:chromatin remodeling; ISO:MGI.
DR   GO; GO:0048566; P:embryonic digestive tract development; IMP: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:0030099; P:myeloid cell differentiation; IMP:MGI.
DR   GO; GO:1901533; P:negative regulation of hematopoietic progenitor cell differentiation; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:MGI.
DR   GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; ISO:MGI.
DR   GO; GO:0045624; P:positive regulation of T-helper cell differentiation; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0048536; P:spleen development; IMP:MGI.
DR   GO; GO:0017145; P:stem cell division; IMP:MGI.
DR   GO; GO:0048538; P:thymus development; IMP:MGI.
DR   CDD; cd00167; SANT; 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   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; SSF46689; 2.
DR   PROSITE; PS51294; HTH_MYB; 3.
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   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
//
DBGET integrated database retrieval system