CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001873
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Myc proto-oncogene protein 
Protein Synonyms/Alias
 Class E basic helix-loop-helix protein 39; bHLHe39; Proto-oncogene c-Myc; Transcription factor p64 
Gene Name
 MYC 
Gene Synonyms/Alias
 BHLHE39 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
52PSEDIWKKFELLPTPubiquitination[1]
143SGFSAAAKLVSEKLAacetylation[2]
148AAKLVSEKLASYQAAacetylation[3]
148AAKLVSEKLASYQAAubiquitination[1, 4, 5]
157ASYQAARKDSGSPNPacetylation[2]
157ASYQAARKDSGSPNPubiquitination[1]
275EKRQAPGKRSESGSPacetylation[2]
317AAPPSTRKDYPAAKRacetylation[2]
323RKDYPAAKRVKLDSVacetylation[2]
323RKDYPAAKRVKLDSVubiquitination[1]
355SDTEENVKRRTHNVLubiquitination[1]
371RQRRNELKRSFFALRacetylation[2]
389PELENNEKAPKVVILubiquitination[1, 5]
412SVQAEEQKLISEEDLubiquitination[1, 5]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Six lysine residues on c-Myc are direct substrates for acetylation by p300.
 Zhang K, Faiola F, Martinez E.
 Biochem Biophys Res Commun. 2005 Oct 14;336(1):274-80. [PMID: 16126174]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
 Participates in the regulation of gene transcription. Binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Seems to activate the transcription of growth-related genes. 
Sequence Annotation
 DOMAIN 354 406 bHLH.
 REGION 413 434 Leucine-zipper.
 MOD_RES 6 6 Phosphoserine.
 MOD_RES 8 8 Phosphothreonine; by RAF; in vitro.
 MOD_RES 58 58 Phosphothreonine; by GSK3; alternate.
 MOD_RES 62 62 Phosphoserine; by DYRK2, GSK3 and CDK2.
 MOD_RES 71 71 Phosphoserine.
 MOD_RES 143 143 N6-acetyllysine; by PCAF.
 MOD_RES 148 148 N6-acetyllysine.
 MOD_RES 157 157 N6-acetyllysine; by PCAF.
 MOD_RES 161 161 Phosphoserine.
 MOD_RES 275 275 N6-acetyllysine; by PCAF.
 MOD_RES 317 317 N6-acetyllysine; by PCAF.
 MOD_RES 323 323 N6-acetyllysine; by PCAF.
 MOD_RES 329 329 Phosphoserine; by PIM2; in vitro (By
 MOD_RES 371 371 N6-acetyllysine; by PCAF.
 CARBOHYD 58 58 O-linked (GlcNAc); alternate.  
Keyword
 3D-structure; Acetylation; Activator; Alternative splicing; Chromosomal rearrangement; Complete proteome; DNA-binding; Glycoprotein; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome; Transcription; Transcription regulation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 439 AA 
Protein Sequence
MPLNVSFTNR NYDLDYDSVQ PYFYCDEEEN FYQQQQQSEL QPPAPSEDIW KKFELLPTPP 60
LSPSRRSGLC SPSYVAVTPF SLRGDNDGGG GSFSTADQLE MVTELLGGDM VNQSFICDPD 120
DETFIKNIII QDCMWSGFSA AAKLVSEKLA SYQAARKDSG SPNPARGHSV CSTSSLYLQD 180
LSAAASECID PSVVFPYPLN DSSSPKSCAS QDSSAFSPSS DSLLSSTESS PQGSPEPLVL 240
HEETPPTTSS DSEEEQEDEE EIDVVSVEKR QAPGKRSESG SPSAGGHSKP PHSPLVLKRC 300
HVSTHQHNYA APPSTRKDYP AAKRVKLDSV RVLRQISNNR KCTSPRSSDT EENVKRRTHN 360
VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSVQAEE QKLISEEDLL 420
RKRREQLKHK LEQLRNSCA 439 
Gene Ontology
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0043234; C:protein complex; IDA:UniProtKB.
 GO:0005819; C:spindle; IEA:Compara.
 GO:0070888; F:E-box binding; IDA:UniProtKB.
 GO:0032403; F:protein complex binding; IDA:UniProtKB.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
 GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
 GO:0060070; P:canonical Wnt receptor signaling pathway; IDA:UniProtKB.
 GO:0007050; P:cell cycle arrest; IDA:UniProtKB.
 GO:0006879; P:cellular iron ion homeostasis; IDA:UniProtKB.
 GO:0035690; P:cellular response to drug; IDA:UniProtKB.
 GO:0034644; P:cellular response to UV; IEP:UniProtKB.
 GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
 GO:0006112; P:energy reserve metabolic process; NAS:UniProtKB.
 GO:0044346; P:fibroblast apoptotic process; TAS:UniProtKB.
 GO:0000165; P:MAPK cascade; IMP:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
 GO:0051782; P:negative regulation of cell division; IDA:UniProtKB.
 GO:0048147; P:negative regulation of fibroblast proliferation; IDA:UniProtKB.
 GO:0045656; P:negative regulation of monocyte differentiation; IMP:UniProtKB.
 GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISS:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0007219; P:Notch signaling pathway; TAS:Reactome.
 GO:0015671; P:oxygen transport; NAS:UniProtKB.
 GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
 GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:UniProtKB.
 GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:UniProtKB.
 GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB.
 GO:0090096; P:positive regulation of metanephric cap mesenchymal cell proliferation; ISS:UniProtKB.
 GO:2001022; P:positive regulation of response to DNA damage stimulus; IDA:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
 GO:0032204; P:regulation of telomere maintenance; IMP:BHF-UCL.
 GO:0006974; P:response to DNA damage stimulus; IDA:UniProtKB.
 GO:0010332; P:response to gamma radiation; IDA:UniProtKB.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome. 
Interpro
 IPR011598; bHLH_dom.
 IPR003327; Myc-LZ.
 IPR002418; Tscrpt_reg_Myc.
 IPR012682; Tscrpt_reg_Myc_N. 
Pfam
 PF00010; HLH
 PF02344; Myc-LZ
 PF01056; Myc_N 
SMART
 SM00353; HLH 
PROSITE
 PS50888; BHLH 
PRINTS
 PR00044; LEUZIPPRMYC.