MYCN_RAT
ID MYCN_RAT Reviewed; 462 AA.
AC Q63379;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=N-myc proto-oncogene protein;
GN Name=Mycn; Synonyms=Nmyc, Nmyc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1719466;
RA Sugiyama A., Miyagi Y., Shirasawa Y., Kuchino Y.;
RT "Different usage of two polyadenylylation signals in transcription of the
RT N-myc gene in rat tumor cells.";
RL Oncogene 6:2027-2032(1991).
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; X63281; CAA44920.1; -; Genomic_DNA.
DR PIR; S20073; S20073.
DR RefSeq; NP_001013114.1; NM_001013096.1.
DR AlphaFoldDB; Q63379; -.
DR SMR; Q63379; -.
DR STRING; 10116.ENSRNOP00000008643; -.
DR iPTMnet; Q63379; -.
DR PhosphoSitePlus; Q63379; -.
DR PaxDb; Q63379; -.
DR GeneID; 298894; -.
DR KEGG; rno:298894; -.
DR CTD; 4613; -.
DR RGD; 1584995; Mycn.
DR eggNOG; KOG2588; Eukaryota.
DR InParanoid; Q63379; -.
DR OrthoDB; 877891at2759; -.
DR PhylomeDB; Q63379; -.
DR PRO; PR:Q63379; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISO:RGD.
DR GO; GO:0001502; P:cartilage condensation; ISO:RGD.
DR GO; GO:0042733; P:embryonic digit morphogenesis; ISO:RGD.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0045607; P:regulation of inner ear auditory receptor cell differentiation; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..462
FT /note="N-myc proto-oncogene protein"
FT /id="PRO_0000127326"
FT DOMAIN 379..431
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 133..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..452
FT /note="Leucine-zipper"
FT MOTIF 76..85
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P04198"
FT COMPBIAS 257..276
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 259
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P04198"
FT MOD_RES 261
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P04198"
SQ SEQUENCE 462 AA; 49695 MW; 493130B3E0CAAB16 CRC64;
MPSCTASTMP GMICKNPDLE FDSLQPCFYP DEDDFYFGGP DSTPPGEDIW KKFELLPTPP
LSPSRAFPEH SPEPSNWATE MLLPEADLWG NPAEEDAFGL GGLGGLTPNP VILQDCMWSG
FSAREKLERA VNEKLQHGHG PPGASSSCPA PGVGASSSGG RALGGSASAG RTGATLPTDL
SHPAAECVDP AVVFPFPVNK RESASVPAAP TSAPATSAVV TSVSVPAVAP VAAPARGSGR
PANSGEHKAL STSGEDTLSD SDDEDDEEED EEEEIDVVTV EKRRSSSNNK AVTTFTITVR
PKTSALGLGR AQPGELILKR CVPIHQQHNY AAPSPYVESE DAPPQKKIKS EASPRPLKSV
VPPKAKSLSP RNSDSEDSER RRNHNILERQ RRNDLRSSFL TLRDHVPELV KNEKAAKVVI
LKKATEYVHA LQANEHQLLL EKEKLQARQQ QLLKKIEHAR TC
