MYB_CHICK
ID MYB_CHICK Reviewed; 641 AA.
AC P01103; P87467; Q788R2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Transcriptional activator Myb;
DE AltName: Full=Proto-oncogene c-Myb;
GN Name=MYB;
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=3025608; DOI=10.1128/mcb.6.11.3677-3684.1986;
RA Gerondakis S., Bishop J.M.;
RT "Structure of the protein encoded by the chicken proto-oncogene c-myb.";
RL Mol. Cell. Biol. 6:3677-3684(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3753748; DOI=10.1038/319604a0;
RA Rosson D., Reddy P.;
RT "Nucleotide sequence of chicken c-myb complementary DNA and implications
RT for myb oncogene activation.";
RL Nature 319:604-606(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176.
RC STRAIN=Brown leghorn; TISSUE=Thymus;
RX PubMed=2548166; DOI=10.1093/nar/17.14.5651;
RA Dvorak M., Urbanek P., Bartunek P., Paces V., Vlach J., Pecenka V.,
RA Arnold L., Travnicek M.;
RT "Transcription of the chicken myb proto-oncogene starts within a CpG
RT island.";
RL Nucleic Acids Res. 17:5651-5664(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX PubMed=3145493; DOI=10.1093/nar/16.24.11521;
RA Urbanek P., Dvorak P., Bartunek M., Vlach P., Pecenka J., Paces V.,
RA Travnicek M.;
RT "Nucleotide sequence of chicken myb proto-oncogene promoter region:
RT detection of an evolutionarily conserved element.";
RL Nucleic Acids Res. 16:11521-11530(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX PubMed=2710126; DOI=10.1128/mcb.9.2.837-843.1989;
RA Hahn S.L., Hahn M., Hayward W.S.;
RT "Structural organization of upstream exons and distribution of
RT transcription start sites in the chicken c-myb gene.";
RL Mol. Cell. Biol. 9:837-843(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 21-79 AND 73-79.
RC TISSUE=Thymus;
RX PubMed=2452755; DOI=10.1016/0014-5793(88)80422-8;
RA Soret J., Vellard M., Martinerie C., Perbal B.;
RT "Organization of 5'-proximal c-myb exons in chicken DNA. Implications for
RT c-myb tissue-specific transcription.";
RL FEBS Lett. 232:227-234(1988).
RN [7]
RP ALTERNATIVE SPLICING.
RX PubMed=8510928;
RA Schuur E.R., Dasgupta P., Reddy E.P., Rabinovich J.M., Baluda M.A.;
RT "Alternative splicing of the chicken c-myb exon 9A.";
RL Oncogene 8:1839-1847(1993).
RN [8]
RP TRUNCATION MUTATIONS.
RX PubMed=2072904; DOI=10.1128/mcb.11.8.3987-3996.1991;
RA Graesser F.A., Graf T., Lipsick J.S.;
RT "Protein truncation is required for the activation of the c-myb proto-
RT oncogene.";
RL Mol. Cell. Biol. 11:3987-3996(1991).
RN [9]
RP 3D-STRUCTURE MODELING OF 142-192.
RX PubMed=1817253; DOI=10.1093/protein/4.8.891;
RA Frampton J., Gibson T.J., Ness S.A., Doederlein G., Graf T.;
RT "Proposed structure for the DNA-binding domain of the Myb oncoprotein based
RT on model building and mutational analysis.";
RL Protein Eng. 4:891-901(1991).
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 -!- INTERACTION:
CC P01103; Q08752: PPID; Xeno; NbExp=2; IntAct=EBI-6502562, EBI-716596;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P01103-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P01103-2; Sequence=VSP_010978;
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: Truncation of either the N- or C-terminal of C-Myb leads to
CC increased transformation and transactivation potential.
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DR EMBL; M14129; AAA48962.1; -; mRNA.
DR EMBL; X03477; CAA27197.1; ALT_SEQ; mRNA.
DR EMBL; X14612; CAA32767.1; -; Genomic_DNA.
DR EMBL; X12495; CAA31015.1; -; Genomic_DNA.
DR EMBL; M24373; AAA48697.1; -; Genomic_DNA.
DR EMBL; M35509; AAA48698.1; -; Genomic_DNA.
DR EMBL; M35506; AAA48698.1; JOINED; Genomic_DNA.
DR EMBL; M35507; AAA48698.1; JOINED; Genomic_DNA.
DR EMBL; M35508; AAA48698.1; JOINED; Genomic_DNA.
DR EMBL; M35509; AAA48699.1; -; Genomic_DNA.
DR EMBL; M35507; AAA48699.1; JOINED; Genomic_DNA.
DR EMBL; M35508; AAA48699.1; JOINED; Genomic_DNA.
DR EMBL; X73660; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A25075; TVCHM.
DR RefSeq; NP_990637.1; NM_205306.1.
DR PDB; 5SVH; X-ray; 2.05 A; B=291-315.
DR PDBsum; 5SVH; -.
DR AlphaFoldDB; P01103; -.
DR BMRB; P01103; -.
DR SMR; P01103; -.
DR BioGRID; 676504; 1.
DR IntAct; P01103; 1.
DR STRING; 9031.ENSGALP00000022584; -.
DR BindingDB; P01103; -.
DR ChEMBL; CHEMBL2380186; -.
DR iPTMnet; P01103; -.
DR PaxDb; P01103; -.
DR GeneID; 396244; -.
DR KEGG; gga:396244; -.
DR CTD; 4602; -.
DR VEuPathDB; HostDB:geneid_396244; -.
DR eggNOG; KOG0048; Eukaryota.
DR InParanoid; P01103; -.
DR OrthoDB; 219341at2759; -.
DR PhylomeDB; P01103; -.
DR PRO; PR:P01103; -.
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:0010468; P:regulation of gene expression; TAS:AgBase.
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; 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; Activator; Alternative splicing; DNA-binding; Nucleus;
KW Proto-oncogene; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..641
FT /note="Transcriptional activator Myb"
FT /id="PRO_0000197050"
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 275..327
FT /note="Transcriptional activation domain"
FT /evidence="ECO:0000250"
FT REGION 317..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..465
FT /note="Negative regulatory domain"
FT /evidence="ECO:0000250"
FT REGION 376..397
FT /note="Leucine-zipper"
FT VAR_SEQ 402
FT /note="S -> SDPSSWGDLSSFEFFEDTDILAGKATSGTAVQLQHGGASACRPPGLP
FT ISNLSKTMSSQSPPGSPKSLSASQGSVAPWVLRKRRGHASPLASGPSSTLGLADGSSST
FT SKHSPVKSLPFSPSQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_010978"
FT HELIX 291..303
FT /evidence="ECO:0007829|PDB:5SVH"
SQ SEQUENCE 641 AA; 72467 MW; DDDD62BFD3B29187 CRC64;
MARRPRHSIY SSDDDEEDVE MYDHDYDGLL PKAGKRHLGK TRWTREEDEK LKKLVEQNGT
EDWKVIASFL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK
HLKGRIGKQC RERWHNHLNP EVKKTSWTEE EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA
IKNHWNSTMR RKVEQEGYLQ ESSKAGLPSA TTGFQKSSHL MAFAHNPPAG PLPGAGQAPL
GSDYPYYHIA EPQNVPGQIP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL
LLMSTENELK GQQALPTQNH TANYPGWHST TVADNTRTSG DNAPVSCLGE HHHCTPSPPV
DHGCLPEESA SPARCMIVHQ SNILDNVKNL LEFAETLQLI DSFLNTSSNH ENLNLDNPAL
TSTPVCGHKM SVTTPFHRDQ PFKTQKENHV FRTPAIKRSI LESSPRTPTP FKNALAAQEI
KYGPLKMLPQ TPTHLVEDLQ DVIKQESEES AIVAGLHESG PPLLKKIKQE VESPTDKAGN
FFCSNHWEGE NLNTQLFTHA STMEDVPNLL TSSILKMPVS EEEGSFHKAF AVPRNRPLAS
PMQHLNNAWE SASCGKTEDQ MALTDQARKY MAAFPTRTLV M
