MYCN_SERCA
ID MYCN_SERCA Reviewed; 427 AA.
AC P26014;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=N-myc proto-oncogene protein;
GN Name=MYCN;
OS Serinus canaria (Island canary) (Fringilla canaria).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Fringillidae;
OC Carduelinae; Serinus.
OX NCBI_TaxID=9135;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1996121; DOI=10.1128/mcb.11.3.1770-1776.1991;
RA Collum R.G., Clayton D.F., Alt F.W.;
RT "Structure and expression of canary myc family genes.";
RL Mol. Cell. Biol. 11:1770-1776(1991).
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MAX.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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DR EMBL; M64598; AAA49540.1; -; Genomic_DNA.
DR EMBL; M64251; AAA49540.1; JOINED; Genomic_DNA.
DR PIR; A39695; A39695.
DR AlphaFoldDB; P26014; -.
DR SMR; P26014; -.
DR Proteomes; UP000694409; 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..427
FT /note="N-myc proto-oncogene protein"
FT /id="PRO_0000127328"
FT DOMAIN 343..396
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 45..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..417
FT /note="Leucine-zipper"
FT COMPBIAS 150..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..242
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 224
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250"
FT MOD_RES 226
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 427 AA; 47141 MW; 6631FFEE615AE54B CRC64;
MPGMVSKNPD LEFDSLQPCF YPDEDDFYLC GPDSAPPGED IWKKFELLPT PPLSPSRPAP
GAPSGRGPGA VGRSGSVGLP HDPVDWASEL LLLPPEADLW GGMDGGDFFE TGPGVTNNLN
SIIIQDCMWS GFSAREKLER AVTEKLQNKT PAAPPPPPGT AGSPPVPARS GRAVPECVDP
AVVFPFPVNK REAPAAEGLR RRRRARGDSR ASSSSSSSGD DTLSDSEDDE DEEEEDEEEE
IDVVTVEKRR SSTNKSVTTL TITVRPNNTT FSSVRTQQNG LILKRCAPIH QQHNYAAPSP
FVETEESPPQ KKLKVEVSRP VKPTIQPKLK SSSPRNSDSE DSERRRNHNI LERQRANDLR
SSFLTLRDHV LSELVQNEKA AKVVILKKAT EYVHSLQAEE QKLLLEKEKL QARQEQLLKK
IDYKRTC