MYBB_CHICK
ID MYBB_CHICK Reviewed; 686 AA.
AC Q03237;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Myb-related protein B;
DE Short=B-Myb;
DE AltName: Full=Myb-like protein 2;
GN Name=MYBL2; Synonyms=BMYB;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1425593; DOI=10.1002/j.1460-2075.1992.tb05564.x;
RA Foos G., Grimm S., Klempnauer K.-H.;
RT "Functional antagonism between members of the myb family: B-myb inhibits v-
RT myb-induced gene activation.";
RL EMBO J. 11:4619-4629(1992).
RN [2]
RP STRUCTURE BY NMR OF 79-186.
RX PubMed=9657674; DOI=10.1021/bi972861z;
RA McIntosh P.B., Frenkiel T.A., Wollborn U., McCormick J.E., Klempnauer K.H.,
RA Feeney J., Carr M.D.;
RT "Solution structure of the B-Myb DNA-binding domain: a possible role for
RT conformational instability of the protein in DNA binding and control of
RT gene expression.";
RL Biochemistry 37:9619-9629(1998).
CC -!- FUNCTION: Represses v-myb- and c-myb-mediated activation of the mim-1
CC gene, probably by competing with other myb proteins for binding sites.
CC It is an inhibitory member of the myb family.
CC -!- SUBUNIT: Component of the DREAM complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in hematopoietic and non hematopoietic
CC cells.
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DR EMBL; X67505; CAA47839.1; -; mRNA.
DR PIR; S28050; S28050.
DR RefSeq; NP_990649.1; NM_205318.1.
DR PDB; 1A5J; NMR; -; A=79-186.
DR PDBsum; 1A5J; -.
DR AlphaFoldDB; Q03237; -.
DR BMRB; Q03237; -.
DR SMR; Q03237; -.
DR STRING; 9031.ENSGALP00000005531; -.
DR PaxDb; Q03237; -.
DR GeneID; 396258; -.
DR KEGG; gga:396258; -.
DR CTD; 4605; -.
DR VEuPathDB; HostDB:geneid_396258; -.
DR eggNOG; KOG0048; Eukaryota.
DR InParanoid; Q03237; -.
DR OrthoDB; 219341at2759; -.
DR PhylomeDB; Q03237; -.
DR EvolutionaryTrace; Q03237; -.
DR PRO; PR:Q03237; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd00167; SANT; 3.
DR InterPro; IPR015395; C-myb_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR028311; MYBL2.
DR InterPro; IPR001005; SANT/Myb.
DR PANTHER; PTHR45614:SF30; PTHR45614:SF30; 2.
DR Pfam; PF09316; Cmyb_C; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
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; DNA-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..686
FT /note="Myb-related protein B"
FT /id="PRO_0000197060"
FT DOMAIN 26..77
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 78..133
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 134..184
FT /note="HTH myb-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 54..77
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 106..129
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 157..180
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:1A5J"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:1A5J"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:1A5J"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1A5J"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:1A5J"
FT TURN 148..152
FT /evidence="ECO:0007829|PDB:1A5J"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:1A5J"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:1A5J"
SQ SEQUENCE 686 AA; 77737 MW; 2D1209EAD6489D7B CRC64;
MARRSRGEDQ DELHCQDTDS DVPEQRDGRC KVKWTQEEDE QLKMLVRHYG QNDWKFLASH
FPNRSDQQCQ YRWLRVLNPD LVKGPWTKEE DQKVIELVKK YGTKQWTLIA KHLKGRLGKQ
CRERWHNHLN PEVKKSSWTE EEDRIIFEAH KVLGNRWAEI AKLLPGRTDN AVKNHWNSTI
KRKVDTGGFL NETKESQPLY LLVEVDDNES QSGTRAESQT IVPNWPVDIS EIKEEDVSDE
EVTGLQELPS ELPAADLAEH NEEGTPDDVV PEDASASVAS PYKWVVEAAN YLCPTSVPAL
NEALDMIESD PDGWCDLTQF DLPEEPSAGS SSSSNSPVRQ TPSKPTPSLP NVTEYRLDGH
TISDLSKSRK GELIPISPHA EVSFGTPPSV LKRQKKRKIS LSPVTENAPS TSLSFLDSCN
SMTPKSTPVK TLPFSPSQFL NFWTKQDTLE LENPSLTSTP VCSQKVIVTT PLHRDKTPLL
QKNSAFVTPD QKYVVDNTPH TPTPFKNALE KYGPIRPLPQ TPHLEEDLKE VLRSEAGIEL
IIEDDVKPHK QKRKQGLRRS PIKKVRKSLA LDIVDEDMTQ NMPALPKTIC FKRTQPVNFL
SRSLNLSSSN RKNDSGLLNR AFVQVQSEKM SYRKMPSHFR PPAPMTRAWK AVACGGTQDQ
LFMQEKARQF LGTLKQSHTS RTLILS
