ID   MYCN_MARMO              Reviewed;         460 AA.
AC   Q61976;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=N-myc proto-oncogene protein;
DE   AltName: Full=N-myc1;
GN   Name=MYCN; Synonyms=NMYC, NMYC1;
OS   Marmota monax (Woodchuck).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Marmota.
OX   NCBI_TaxID=9995;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=2395655; DOI=10.1093/nar/18.16.4918;
RA   Fourel G., Tiollais P., Buendia M.-A.;
RT   "Nucleotide sequence of the woodchuck N-myc gene (WN-myc1).";
RL   Nucleic Acids Res. 18:4918-4918(1990).
CC   -!- FUNCTION: Positively regulates the transcription of MYCNOS in
CC       neuroblastoma cells. {ECO:0000250|UniProtKB:P04198}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Binds DNA as a heterodimer with MAX. Interacts with KDM5A,
CC       KDM5B and HUWE1. Interacts with MYCNOS. Interacts with AURKA;
CC       interaction is phospho-independent and triggers AURKA activation; AURKA
CC       competes with FBXW7 for binding to unphosphorylated MYCN but not for
CC       binding to unphosphorylated MYCN. Interacts with FBXW7; FBXW7 competes
CC       with AURKA for binding to unphosphorylated MYCN but not for binding to
CC       phosphorylated MYCN. {ECO:0000250|UniProtKB:P04198}.
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:P04198}.
CC   -!- PTM: Phosphorylated by GSK3-beta which may promote its degradation.
CC       Phosphorylated by AURKA. {ECO:0000250|UniProtKB:P04198}.
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DR   EMBL; X53673; CAA37712.1; -; Genomic_DNA.
DR   EMBL; X53674; CAA37712.1; JOINED; Genomic_DNA.
DR   PIR; S11558; S11558.
DR   AlphaFoldDB; Q61976; -.
DR   SMR; Q61976; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR002418; Tscrpt_reg_Myc.
DR   InterPro; IPR012682; Tscrpt_reg_Myc_N.
DR   Pfam; PF00010; HLH; 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   DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene.
FT   CHAIN           1..460
FT                   /note="N-myc proto-oncogene protein"
FT                   /id="PRO_0000127324"
FT   DOMAIN          377..429
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          19..47
FT                   /note="Interaction with AURKA"
FT                   /evidence="ECO:0000250|UniProtKB:P04198"
FT   REGION          61..90
FT                   /note="Interaction with AURKA and FBXW7"
FT                   /evidence="ECO:0000250|UniProtKB:P04198"
FT   REGION          131..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          330..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..450
FT                   /note="Leucine-zipper"
FT   MOTIF           76..85
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:P04198"
FT   COMPBIAS        255..274
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         257
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:P04198"
FT   MOD_RES         259
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:P04198"
SQ   SEQUENCE   460 AA;  49192 MW;  8A16686C82F5B02E CRC64;
     MPSCTASTMP GMICKNPDLE FDSLQPCFYP DEDDFYFGGP DSTPPGEDIW KKFELLPTPP
     LSPSRAFSEQ SPEPSDWATE MLLPEADLWG NPAEEDAFGL GGLGGLTPNP VILQDCMWSG
     FSAREKLERA VSEKLQHGRG PPAAGPATPG AGAANPAGRG HGGTAGAGRA GAALPAELAH
     PAAECVDPAV VFPFPVNKRD PAPVPVAPAG SPAVGAAVAG AAAPASAAVA APPRLGGRPA
     NGGDHKALST SGEDTLSDSD DEDDEEEDEE EEIDVVTVEK RRSSSNSKAV TTFTITVRPK
     NAALGLGRAQ SSELILKRCV PIHQQHNYAA PSPYVESEDA PPQKKIKSEV SPRPLKSVIP
     PKAKSLSPRN SDSEDSERRR NHNILERQRR NDLRSSFLTL RDHVPELVKN EKAAKVVILK
     KATEYVHSLQ AEEHQLLLEK EKLQARQQQL LKKIELARTC