MYC_CHICK
ID MYC_CHICK Reviewed; 416 AA.
AC P01109;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Myc proto-oncogene protein;
DE Short=c-Myc;
GN Name=MYC;
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 [GENOMIC DNA].
RX PubMed=6300896; DOI=10.1073/pnas.80.8.2146;
RA Watson D.K., Reddy E.P., Duesberg P.H., Papas T.S.;
RT "Nucleotide sequence analysis of the chicken c-myc gene reveals homologous
RT and unique coding regions by comparison with the transforming gene of avian
RT myelocytomatosis virus MC29, delta gag-myc.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:2146-2150(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2841585; DOI=10.1128/mcb.8.6.2659-2663.1988;
RA Hahn M., Hayward W.;
RT "Absence of missense mutations in activated c-myc genes in avian leukosis
RT virus-induced B-cell lymphomas.";
RL Mol. Cell. Biol. 8:2659-2663(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
RX PubMed=6087343; DOI=10.1073/pnas.81.15.4697;
RA Shih C.-K., Linial M., Goodenow M.M., Hayward W.S.;
RT "Nucleotide sequence 5' of the chicken c-myc coding region: localization of
RT a noncoding exon that is absent from myc transcripts in most avian leukosis
RT virus-induced lymphomas.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4697-4701(1984).
CC -!- FUNCTION: Transcription factor that binds DNA in a non-specific manner,
CC yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'.
CC Activates the transcription of growth-related genes.
CC {ECO:0000250|UniProtKB:P01106}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MAX.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:P01106}.
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DR EMBL; J00889; AAA48963.1; -; Genomic_DNA.
DR EMBL; M20006; AAA48700.1; -; Genomic_DNA.
DR PIR; A93944; FOCH.
DR RefSeq; NP_001026123.1; NM_001030952.1.
DR RefSeq; XP_015138575.1; XM_015283089.1.
DR AlphaFoldDB; P01109; -.
DR SMR; P01109; -.
DR BioGRID; 681305; 2.
DR MINT; P01109; -.
DR STRING; 9031.ENSGALP00000026259; -.
DR ChEMBL; CHEMBL1250349; -.
DR PaxDb; P01109; -.
DR Ensembl; ENSGALT00000080250; ENSGALP00000054503; ENSGALG00000033631.
DR GeneID; 420332; -.
DR KEGG; gga:420332; -.
DR CTD; 4609; -.
DR VEuPathDB; HostDB:geneid_420332; -.
DR eggNOG; KOG2483; Eukaryota.
DR GeneTree; ENSGT00940000155285; -.
DR HOGENOM; CLU_052560_0_0_1; -.
DR InParanoid; P01109; -.
DR OMA; EQLRNCC; -.
DR OrthoDB; 877891at2759; -.
DR PhylomeDB; P01109; -.
DR TreeFam; TF106001; -.
DR Reactome; R-GGA-5689880; Ub-specific processing proteases.
DR PRO; PR:P01109; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000033631; Expressed in granulocyte and 11 other tissues.
DR ExpressionAtlas; P01109; baseline and differential.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0071943; C:Myc-Max complex; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IEA:Ensembl.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0070888; F:E-box binding; IEA:Ensembl.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0001221; F:transcription coregulator binding; IEA:Ensembl.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl.
DR GO; GO:0048730; P:epidermis morphogenesis; IEP:AgBase.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0051782; P:negative regulation of cell division; IEA:Ensembl.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0045656; P:negative regulation of monocyte differentiation; IEA:Ensembl.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IEA:Ensembl.
DR GO; GO:1905643; P:positive regulation of DNA methylation; IEA:Ensembl.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IEA:Ensembl.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IEA:Ensembl.
DR GO; GO:0032986; P:protein-DNA complex disassembly; IEA:Ensembl.
DR GO; GO:0010564; P:regulation of cell cycle process; IEA:Ensembl.
DR GO; GO:0032204; P:regulation of telomere maintenance; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR003327; Myc-LZ.
DR InterPro; IPR002418; Tscrpt_reg_Myc.
DR InterPro; IPR012682; Tscrpt_reg_Myc_N.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF02344; Myc-LZ; 1.
DR Pfam; PF01056; Myc_N; 1.
DR PIRSF; PIRSF001705; Myc_protein; 1.
DR PRINTS; PR00044; LEUZIPPRMYC.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Glycoprotein; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..416
FT /note="Myc proto-oncogene protein"
FT /id="PRO_0000127313"
FT DOMAIN 331..383
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 144..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..411
FT /note="Leucine-zipper"
FT MOTIF 86..94
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT COMPBIAS 153..171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..244
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 61
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 416 AA; 46040 MW; 6B35E4BD3A1A5883 CRC64;
MPLSASLPSK NYDYDYDSVQ PYFYFEEEEE NFYLAAQQRG SELQPPAPSE DIWKKFELLP
TPPLSPSRRS SLAAASCFPS TADQLEMVTE LLGGDMVNQS FICDPDDESF VKSIIIQDCM
WSGFSAAAKL EKVVSEKLAT YQASRREGGP AAASRPGPPP SGPPPPPAGP AASAGLYLHD
LGAAAADCID PSVVFPYPLS ERAPRAAPPG ANPAALLGVD TPPTTSSDSE EEQEEDEEID
VVTLAEANES ESSTESSTEA SEEHCKPHHS PLVLKRCHVN IHQHNYAAPP STKVEYPAAK
RLKLDSGRVL KQISNNRKCS SPRTSDSEEN DKRRTHNVLE RQRRNELKLS FFALRDQIPE
VANNEKAPKV VILKKATEYV LSIQSDEHRL IAEKEQLRRR REQLKHKLEQ LRNSRA
