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Protein Page:
Myc (mouse)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
Myc a proto-oncogenic transcription factor that plays a role in cell proliferation, apoptosis and in the development of human tumors.. Seems to activate the transcription of growth-related genes. Note: This description may include information from UniProtKB.
Protein type: DNA binding protein; Transcription factor
Cellular Component: nucleoplasm; nuclear body; protein complex; mitochondrion; axon; cytoplasm; nucleolus; spindle; intracellular; nucleus
Molecular Function: protein dimerization activity; protein binding; DNA binding; sequence-specific DNA binding; protein heterodimerization activity; double-stranded DNA binding; protein complex binding; transcription factor activity; transcription factor binding
Biological Process: positive regulation of catalytic activity; cellular iron ion homeostasis; positive regulation of transcription, DNA-dependent; transcription initiation; regulation of mitotic cell cycle; B cell apoptosis; positive regulation of caspase activity; middle ear morphogenesis; Wnt receptor signaling pathway through beta-catenin; regulation of apoptosis; positive regulation of fibroblast proliferation; positive regulation of mesenchymal cell proliferation; cell cycle arrest; negative regulation of protein binding; inner mitochondrial membrane organization and biogenesis; positive regulation of B cell apoptosis; transcription, DNA-dependent; regulation of telomere maintenance; positive regulation of cell cycle; glucose metabolic process; pyruvate transport; detection of mechanical stimulus involved in sensory perception of sound; DNA damage response, signal transduction resulting in induction of apoptosis; negative regulation of fibroblast proliferation; regulation of gene expression; regulation of oxidative phosphorylation; positive regulation of transcription from RNA polymerase II promoter; positive regulation of epithelial cell proliferation; response to alkaloid; transcription from RNA polymerase II promoter; lactic acid secretion; negative regulation of transcription from RNA polymerase II promoter; chromosome organization and biogenesis; response to radiation; regulation of transcription, DNA-dependent; amino acid transport; positive regulation of cell proliferation; response to gamma radiation; caspase activation; Wnt receptor signaling pathway; MAPKKK cascade; negative regulation of cell division; negative regulation of monocyte differentiation; chromatin remodeling; cell proliferation; negative regulation of glucose import; pigmentation; skeletal morphogenesis; ureteric bud branching; positive regulation of glycolysis; protein processing; response to DNA damage stimulus; transformation of host cell by virus
Reference #:  P01108 (UniProtKB)
Alt. Names/Synonyms: AU016757; bHLHe39; c-myc proto-oncogene; Myc; Myc proto-oncogene protein; Myc2; myelocytomatosis oncogene; Niard; Nird; Proto-oncogene c-Myc; Transcription factor p64
Gene Symbols: Myc
Molecular weight: 48,971 Da
Basal Isoelectric point: 5.52  Predict pI for various phosphorylation states
CST Pathways:  G1/S Checkpoint  |  Growth And Differentiation Control by MAPKs  |  Regulation of P38 MAPKs  |  Warburg Effect
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Myc

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  Source  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Sites Implicated In
apoptosis, inhibited: T358‑p, S373‑p, T400‑p
cell cycle regulation: T358‑p, S373‑p, T400‑p
cell differentiation, altered: T58‑p
cell growth, altered: S329‑p, T358‑p, S373‑p, T400‑p
transcription, altered: S62‑p, T358‑p, S373‑p, T400‑p
transcription, induced: S329‑p
transcription, inhibited: T358‑p, S373‑p, T400‑p
activity, inhibited: T358‑p, S373‑p, T400‑p
molecular association, regulation: T58‑p, S62‑p, S373‑p, T400‑p
phosphorylation: S62‑p
protein degradation: T58‑p
protein stabilization: S62‑p, S329‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       mouse

 
0 3 N6 __MPLNVNFTNRNYD
1 0 T8 MPLNVNFTNRNYDLD
1 0 Y12 VNFTNRNYDLDYDSV
1 2 Y16 NRNYDLDYDSVQPYF
1 0 Y22 DYDSVQPYFICDEEE
1 0 Y32 CDEEENFYHQQQQSE
0 1 K52 PSEDIWKKFELLPtP
43 35 T58-p KKFELLPtPPLsPsR
2 0 T58 KKFELLPTPPLsPsR
34 37 S62-p LLPtPPLsPsRRsGL
1 11 S64-p PtPPLsPsRRsGLCS
2 2 S67-p PLsPsRRsGLCSPSy
4 3 S71 sRRsGLCSPSyVAVA
1 1 Y74-p sGLCSPSyVAVAtSF
0 1 T79-p PSyVAVAtSFSPRED
1 0 S82 VAVAtSFSPREDDDG
0 1 S137-p IIQDCMWsGFsAAAK
0 1 S140-p DCMWsGFsAAAKLVS
2 0 K144 sGFsAAAKLVSEkLA
3 21 K149-a AAKLVSEkLASYQAA
0 55 K149-u AAKLVSEkLASYQAA
3 0 K158 ASYQAARKDSTSLSP
0 1 K158 ASYQAARKDSTSLSP
0 1 S162 AARKDSTSLSPARGH
1 0 S249 EETPPTTSSDSEEEQ
1 0 S250 ETPPTTSSDSEEEQE
2 0 S252 PPTTSSDSEEEQEDE
2 0 K275 EKRQTPAKRSESGSS
0 1 S281 AKRSESGSSPSRGHS
0 10 S293-p GHSKPPHsPLVLKRC
2 0 K317 AAPPSTRKDYPAAkR
4 5 K323-a RKDYPAAkRAKLDsG
0 1 K323 RKDYPAAKRAKLDsG
1 0 S329-p AkRAKLDsGRVLKQI
1 1 S343 ISNNRKCSSPRSSDT
1 0 S344 SNNRKCSSPRSSDTE
2 0 S347 RKCSSPRSSDTEEND
2 0 S348 KCSSPRSSDTEENDK
0 1 K355 SDTEENDKRRtHNVL
3 0 T358-p EENDKRRtHNVLERQ
2 0 K371 RQRRNELKRsFFALR
4 1 S373-p RRNELKRsFFALRDQ
0 4 K389 PELENNEKAPKVVIL
3 0 T400-p VVILKKAtAYILSIQ
0 1 K412 SIQADEHKLTSEkDL
1 0 K417-a EHKLTSEkDLLRKRR
  human

 
S6-p __MPLNVsFtNRNyD
T8-p MPLNVsFtNRNyDLD
Y12-p VsFtNRNyDLDyDSV
Y16-p NRNyDLDyDSVQPyF
Y22-p DyDSVQPyFYCDEEE
Y32-p CDEEENFyQQQQQSE
K52-u PSEDIWKkFELLPtP
T58-p KkFELLPtPPLsPsR
T58-gl KkFELLPtPPLsPsR
S62-p LLPtPPLsPsRRsGL
S64-p PtPPLsPsRRsGLCs
S67-p PLsPsRRsGLCsPSy
S71-p sRRsGLCsPSyVAVt
Y74-p sGLCsPSyVAVtPFs
T78-p sPSyVAVtPFsLRGD
S81-p yVAVtPFsLRGDNDG
S136 IIQDCMWSGFSAAAk
S139 DCMWSGFSAAAkLVS
K143-a SGFSAAAkLVSEkLA
K148-a AAkLVSEkLASYQAA
K148-u AAkLVSEkLASYQAA
K157-a ASYQAARkDSGsPNP
K157-u ASYQAARkDSGsPNP
S161-p AARkDSGsPNPARGH
S249-p EETPPTTssDsEEEQ
S250-p ETPPTTssDsEEEQE
S252-p PPTTssDsEEEQEDE
K275-a EKRQAPGkRSESGsP
S281-p GkRSESGsPSAGGHS
S293-p GHSKPPHsPLVLKRC
K317-a AAPPSTRkDYPAAkR
K323-a RkDYPAAkRVKLDSV
K323-u RkDYPAAkRVKLDSV
S329 AkRVKLDSVRVLRQI
T343-p ISNNRKCtsPRssDT
S344-p SNNRKCtsPRssDTE
S347-p RKCtsPRssDTEENV
S348-p KCtsPRssDTEENVk
K355-u sDTEENVkRRtHNVL
T358-p EENVkRRtHNVLERQ
K371-a RQRRNELkRsFFALR
S373-p RRNELkRsFFALRDQ
K389-u PELENNEkAPKVVIL
T400-p VVILKKAtAYILSVQ
K412-u SVQAEEQkLISEEDL
E417 EQkLISEEDLLRKRR
  rat

 
S6 __MPLNVSFANRNYD
A8 MPLNVSFANRNYDLD
Y12 VSFANRNYDLDYDSV
Y16 NRNYDLDYDSVQPYF
Y22 DYDSVQPYFICDEEE
Y32 CDEEENFYHQQQQSE
K52 PSEDIWKKFELLPTP
T58 KKFELLPTPPLSPSR
T58 KKFELLPTPPLSPSR
S62 LLPTPPLSPSRRSGL
S64 PTPPLSPSRRSGLCS
S67 PLSPSRRSGLCSPSY
S71 SRRSGLCSPSYVAVA
Y74 SGLCSPSYVAVATSF
T79 PSYVAVATSFSPRED
S82 VAVATSFSPREDDDG
S137 IIQDCMWSGFSAAAK
S140 DCMWSGFSAAAKLVS
K144 SGFSAAAKLVSEKLA
K149 AAKLVSEKLASYQAA
K149 AAKLVSEKLASYQAA
K158 ASYQAARKDSTSLSP
K158 ASYQAARKDSTSLSP
S162 AARKDSTSLSPARGH
S249 EETPPTTSSDSEEEQ
S250 ETPPTTSSDSEEEQD
S252 PPTTSSDSEEEQDDE
K275 EKRQPPAKRSESGSS
S281 AKRSESGSSPSRGHS
S293 GHSKPPHSPLVLKRC
K317 AAPPSTRKDYPAAKR
K323 RKDYPAAKRAKLDSG
K323 RKDYPAAKRAKLDSG
S329 AKRAKLDSGRVLKQI
S343 ISNNRKCSSPRSSDT
S344 SNNRKCSSPRSSDTE
S347 RKCSSPRSSDTEEND
S348 KCSSPRSSDTEENDK
K355 SDTEENDKRRTHNVL
T358 EENDKRRTHNVLERQ
K371 RQRRNELKRSFFALR
S373 RRNELKRSFFALRDQ
K389 PELENNEKAPKVVIL
T400 VVILKKATAYILSVQ
K412 SVQADEHKLISEKDL
K417 EHKLISEKDLLRKRR
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