ID MYC_HYLLA Reviewed; 439 AA. AC P49033; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 25-JAN-2012, entry version 73. DE RecName: Full=Myc proto-oncogene protein; DE AltName: Full=Proto-oncogene c-Myc; DE AltName: Full=Transcription factor p64; GN Name=MYC; OS Hylobates lar (Common gibbon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hylobatidae; Hylobates. OX NCBI_TaxID=9580; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92339896; PubMed=1634119; DOI=10.1016/0378-1119(92)90520-Y; RA Eladari M.E., Mohammad-Ali K., Argaut C., Galibert F.; RT "Gibbon and marmoset c-myc nucleotide sequences."; RL Gene 116:231-243(1992). CC -!- FUNCTION: Participates in the regulation of gene transcription. CC Binds DNA in a non-specific manner, yet also specifically CC recognizes the core sequence 5'-CAC[GA]TG-3'. Seems to activate CC the transcription of growth-related genes (By similarity). CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another CC bHLH protein. Binds DNA as a heterodimer with MAX. Interacts with CC TAF1C and SPAG9. Interacts with KDM5A and KDM5B. Interacts (when CC phosphorylated at Thr-58 and Ser-62) with FBXW7 (By similarity). CC Interacts with PIM2 (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm (By similarity). CC Nucleus, nucleolus (By similarity). CC -!- PTM: Phosphorylated by PRKDC. Phosphorylation at Thr-58 and Ser-62 CC by GSK3 is required for ubiquitination and degradation by the CC proteasome (By similarity). Phosphorylation at Ser-329 by PIM2 CC leads to the stabilization of MYC. Phosphorylation at Ser-62 by CC CDK2 prevents Ras-induced senescence (By similarity). CC -!- PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated CC at Thr-58 and Ser-62, leading to its degradation by the CC proteasome. In the nucleoplasm, ubiquitination is counteracted by CC USP28, which interacts with of FBXW7 (FBW7alpha), leading to its CC deubiquitination and preventing degradation. Also CC polyubiquitinated by the DCX(TRUSS) complex (By similarity). CC -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M88115; AAA35465.1; -; Genomic_DNA. DR PIR; JC1178; JC1178. DR ProteinModelPortal; P49033; -. DR SMR; P49033; 353-434. DR HOVERGEN; HBG000472; -. DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB. DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB. DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISS:UniProtKB. DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:UniProtKB. DR GO; GO:0042493; P:response to drug; ISS:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. DR InterPro; IPR011598; HLH_DNA-bd. DR InterPro; IPR003327; Myc-LZ. DR InterPro; IPR002418; Tscrpt_reg_Myc. DR InterPro; IPR012682; Tscrpt_reg_Myc_N. DR Gene3D; G3DSA:4.10.280.10; HLH_DNA_bd; 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_basic; 1. DR PROSITE; PS50888; HLH; 1. PE 3: Inferred from homology; KW Acetylation; Activator; DNA-binding; Glycoprotein; Nucleus; KW Phosphoprotein; Proto-oncogene; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1 439 Myc proto-oncogene protein. FT /FTId=PRO_0000127294. FT DOMAIN 368 407 Helix-loop-helix motif. FT DOMAIN 413 434 Leucine-zipper. FT DNA_BIND 354 367 Basic motif. FT COMPBIAS 33 37 Poly-Gln. FT COMPBIAS 88 91 Poly-Gly. FT MOD_RES 6 6 Phosphoserine (By similarity). FT MOD_RES 58 58 Phosphothreonine; by GSK3; alternate (By FT similarity). FT MOD_RES 62 62 Phosphoserine; by GSK3 and CDK2 (By FT similarity). FT MOD_RES 71 71 Phosphoserine (By similarity). FT MOD_RES 143 143 N6-acetyllysine; by PCAF (By similarity). FT MOD_RES 148 148 N6-acetyllysine (By similarity). FT MOD_RES 157 157 N6-acetyllysine; by PCAF (By similarity). FT MOD_RES 275 275 N6-acetyllysine; by PCAF (By similarity). FT MOD_RES 317 317 N6-acetyllysine; by PCAF (By similarity). FT MOD_RES 323 323 N6-acetyllysine; by PCAF (By similarity). FT MOD_RES 329 329 Phosphoserine; by PIM2; in vitro (By FT similarity). FT MOD_RES 344 344 Phosphoserine (By similarity). FT MOD_RES 348 348 Phosphoserine (By similarity). FT MOD_RES 371 371 N6-acetyllysine; by PCAF (By similarity). FT CARBOHYD 58 58 O-linked (GlcNAc); alternate (By FT similarity). SQ SEQUENCE 439 AA; 48820 MW; 272EB5D9FA89D64B CRC64; MPLNVSFTNR NYDLDYDSVQ PYFYCDEEEN FYQQQQQSEL QPPAPSEDIW KKFELLPTPP LSPSRRSGLC SPSYVAVTPF SPRGDNDGGG GSFSTADQLE MVTELLGGDM VNQSFICDPD DETFIKNIII QDCMWSGFSA AAKLVSEKLA SYQAARKDSS SPNPARGHSV CSTSSLYLQD LSAAASECID PSVVFPYPLN DSSSPKSCAS PDSSAFSPSS DSLLSSTESS PQASPEPLVL HEETPPTTSS DSEEEQEDEE EIDVVSVEKR QAPSKRSESG SPSAGGHSKP PHSPLVLKRC HVSTHQHNYA APPSTRKDYP AAKRVKLDSV RVLRQISNNR KCTSPRSSDT EENDKRRTHN VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSVQGEE QKLTSEKDLL RKRREQLKHK LEQLRNSCA //