MYB_MOUSE
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 03-AUG-2022, entry version 204.
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 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}.
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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.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; 946 antibodies from 43 providers.
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; ENSGT00940000156248; -.
DR HOGENOM; CLU_015440_2_2_1; -.
DR InParanoid; P06876; -.
DR OrthoDB; 219341at2759; -.
DR TreeFam; TF326257; -.
DR BioGRID-ORCS; 17863; 11 hits in 79 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 206 other tissues.
DR ExpressionAtlas; P06876; baseline and differential.
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:0090575; C:RNA polymerase II transcription regulator complex; IC: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: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:0061515; P:myeloid cell development; IC:ComplexPortal.
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
