MYCN_CHICK
ID MYCN_CHICK Reviewed; 441 AA.
AC P18444;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=N-myc proto-oncogene protein;
GN Name=MYCN;
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=2183017; DOI=10.1128/mcb.10.5.2017-2026.1990;
RA Sawai S., Kato K., Wakamatsu Y., Kondoh H.;
RT "Organization and expression of the chicken N-myc gene.";
RL Mol. Cell. Biol. 10:2017-2026(1990).
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MAX.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; D90071; BAA14112.1; -; Genomic_DNA.
DR PIR; A34703; TVCHMC.
DR AlphaFoldDB; P18444; -.
DR SMR; P18444; -.
DR STRING; 9031.ENSGALP00000036097; -.
DR VEuPathDB; HostDB:geneid_421948; -.
DR eggNOG; KOG2588; Eukaryota.
DR InParanoid; P18444; -.
DR PhylomeDB; P18444; -.
DR Proteomes; UP000000539; Unplaced.
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; Reference proteome.
FT CHAIN 1..441
FT /note="N-myc proto-oncogene protein"
FT /id="PRO_0000127327"
FT DOMAIN 358..410
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 49..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..431
FT /note="Leucine-zipper"
FT COMPBIAS 152..166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..257
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 240
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250"
FT MOD_RES 242
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 441 AA; 48697 MW; 176B36CE768FC0CE CRC64;
MPGMISKNPD LEFDSLQPCF YPDEDDFYLC GPDSAPPGED IWKKFELLPT PPLSPSRAGL
QEPPPGGGSI AVGRGGPGEC RPVDPLDWAS ELLLLPPEAE LWGSTDGADF FETGLGASNN
LNSIIIQDCM WSAFSAREKL ERAVSEKLQS KPPAAAPPPP PPVVPTAACR RREQPQRGPG
RAELGGSVPE CVDPAVVFPF PVNKREAAVP SGGETPRGGR RPGPAGESRA SSSSGDDTLS
DSDDEDEEEE DDEEEIDVVT VEKRRSSSNK AVTTLTITVR PKNTTFPSVR TQQNELILKR
CAPIHQQHNY AAPSPYMESE DVPPQKKLKA EVPRPVKPMI QPKSKSSSPR NSDSEDSERR
RNHNILERQR RNDLRSSFLT LRDHVPELVK NEKAAKVVIL KKATEYVHSL QAEEQKLLLE
KEKLQARQQQ LLKKIEYKRT C