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Database: UniProt
Entry: A0A2K5YPL3_MANLE
LinkDB: A0A2K5YPL3_MANLE
Original site: A0A2K5YPL3_MANLE 
ID   A0A2K5YPL3_MANLE        Unreviewed;       454 AA.
AC   A0A2K5YPL3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Myc proto-oncogene protein {ECO:0000256|ARBA:ARBA00013423, ECO:0000256|PIRNR:PIRNR001705};
GN   Name=MYC {ECO:0000313|Ensembl:ENSMLEP00000017498.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000017498.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000017498.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A2K5YPL3; -.
DR   STRING; 9568.ENSMLEP00000017498; -.
DR   Ensembl; ENSMLET00000040975.1; ENSMLEP00000017498.1; ENSMLEG00000032954.1.
DR   GeneTree; ENSGT00940000155285; -.
DR   OMA; STRKDCP; -.
DR   Proteomes; UP000233140; Unplaced.
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:UP000233140}.
FT   DOMAIN          369..421
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   REGION          216..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          382..452
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        216..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..380
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  50484 MW;  E58A8C2D522CA6A7 CRC64;
     LDFFPVVENQ QPPATMPLNV SFTNRNYDLD YDSVQPYFYC DEEENFYQQQ QQSELQPPAP
     SEDIWKKFEL LPTPPLSPSR RSGLCSPSYV AVTPFSPRGD NDGGGGSFST ADQLEMVTEL
     LGGDMVNQSF ICDPDDETFI KNIIIQDCMW SGFSAAAKLV SEKLASYQAA RKDSGSPNPA
     RGHSVCSTSS LYLQDLSAAA SECIDPSVVF PYPLNDSSSP KSCASPDSSA FSPSSDSLLS
     STESSPQASP EPLVLHEETP PTTSSDSEEE QEEEEEIDVV SVEKRQAPGK RSESGSPSAG
     GHSKPPHSPL VLKRCHVSTH QHNYAAPPST RKDYPAAKRV KLDSVRVLRQ ISNNRKCTSP
     RSSDTEENDK RRTHNVLERQ RRNELKRSFF ALRDQIPELE NNEKAPKVVI LKKATAYILS
     VQAEEQKLIS EKDLLRKRRE QLKHKLEQLR NSCA
//
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