ID I3M553_ICTTR Unreviewed; 453 AA.
AC I3M553;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Myc proto-oncogene protein {ECO:0000256|ARBA:ARBA00013423, ECO:0000256|PIRNR:PIRNR001705};
GN Name=MYC {ECO:0000313|Ensembl:ENSSTOP00000004430.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000004430.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000004430.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|PIRNR:PIRNR001705}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. {ECO:0000256|PIRNR:PIRNR001705}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}. Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}.
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DR EMBL; AGTP01001535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3M553; -.
DR STRING; 43179.ENSSTOP00000004430; -.
DR Ensembl; ENSSTOT00000004938.3; ENSSTOP00000004430.3; ENSSTOG00000004944.3.
DR eggNOG; KOG2483; Eukaryota.
DR GeneTree; ENSGT00940000155285; -.
DR HOGENOM; CLU_052560_0_0_1; -.
DR InParanoid; I3M553; -.
DR TreeFam; TF106001; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
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:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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: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:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:1905761; F:SCF ubiquitin ligase complex binding; IEA:Ensembl.
DR GO; GO:0001221; F:transcription coregulator binding; IEA:Ensembl.
DR GO; GO:0140537; F:transcription regulator activator activity; 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:0051276; P:chromosome organization; IEA:Ensembl.
DR GO; GO:0006974; P:DNA damage response; IEA:Ensembl.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin formation; IEA:Ensembl.
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:0006879; P:intracellular iron ion homeostasis; 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:0060633; P:negative regulation of transcription initiation by RNA polymerase II; 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: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:0010332; P:response to gamma radiation; IEA:Ensembl.
DR CDD; cd11458; bHLHzip_c-Myc; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 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 PANTHER; PTHR45851; MYC PROTO-ONCOGENE; 1.
DR PANTHER; PTHR45851:SF1; MYC PROTO-ONCOGENE PROTEIN; 1.
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; HLH, helix-loop-helix DNA-binding domain; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR001705};
KW Nucleus {ECO:0000256|PIRNR:PIRNR001705};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT DOMAIN 368..420
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 215..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 381..451
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 215..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 50152 MW; 2049602A6C816E57 CRC64;
LDFLRVVENP AAATMPLNVS FANRNYDLDY DSVQPYFYCD EEENFYQQQQ QSELQPPAPS
EDIWKKFELL PTPPLSPSRR SGLCSPPYVT VASFSPPGDD DGGGGSFSTA DQLEMVTELL
GGDMVNQSFI CDPDDETFIK NIIIQDCMWS GFSAAAKLVS EKLASYQAAR KDSGCPSPAR
GHSGCSSSSL YLQDLSAAAS ECIDPSVVFP YPLNDSSSPK PCASPDSTAF SPSSDSLLSS
TESSPRASPE PLVLHEETPP TTSSDSEEEQ EDEEEIDVVS VEKRQPSARR SESVSPPAGS
HSKPPHSPLV LKRCHVSTHQ HNYAAPPSTR KDCPAAKRAK LDSGRVLKQI SNNRKCASPR
SSDTEENDKR RTHNVLERQR RNELKRSFFA LRDQIPELEN NEKAPKVIIL KKATAYILSL
QAEEQKLISE KDLLRKRREQ LKQKLEQLRN SCA
//
