MYOG_MOUSE - dbPTM
MYOG_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYOG_MOUSE
UniProt AC P12979
Protein Name Myogenin
Gene Name Myog
Organism Mus musculus (Mouse).
Sequence Length 224
Subcellular Localization Nucleus . Recruited to late myogenic gene promoter regulatory sequences with SMARCA4/BRG1/BAF190A and SWI/SNF chromatin-remodeling enzymes to promote chromatin-remodeling and transcription initiation in developing embryos.
Protein Description Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation, cell cycle exit and muscle atrophy. Essential for the development of functional embryonic skeletal fiber muscle differentiation. However is dispensable for postnatal skeletal muscle growth; phosphorylation by CAMK2G inhibits its transcriptional activity in respons to muscle activity. Required for the recruitment of the FACT complex to muscle-specific promoter regions, thus promoting gene expression initiation. During terminal myoblast differentiation, plays a role as a strong activator of transcription at loci with an open chromatin structure previously initiated by MYOD1. Together with MYF5 and MYOD1, co-occupies muscle-specific gene promoter core regions during myogenesis. Cooperates also with myocyte-specific enhancer factor MEF2D and BRG1-dependent recruitment of SWI/SNF chromatin-remodeling enzymes to alter chromatin structure at myogenic late gene promoters. Facilitates cell cycle exit during terminal muscle differentiation through the up-regulation of miR-20a expression, which in turn represses genes involved in cell cycle progression. Binds to the E-box containing (E1) promoter region of the miR-20a gene. Plays also a role in preventing reversal of muscle cell differentiation. Contributes to the atrophy-related gene expression in adult denervated muscles. Induces fibroblasts to differentiate into myoblasts..
Protein Sequence MELYETSPYFYQEPHFYDGENYLPVHLQGFEPPGYERTELSLSPEARGPLEEKGLGTPEHCPGQCLPWACKVCKRKSVSVDRRRAATLREKRRLKKVNEAFEALKRSTLLNPNQRLPKVEILRSAIQYIERLQALLSSLNQEERDLRYRGGGGPQPMVPSECNSHSASCSPEWGNALEFGPNPGDHLLAADPTDAHNLHSLTSIVDSITVEDMSVAFPDETMPN
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
61S-nitrosocysteineGLGTPEHCPGQCLPW
CCCCCCCCCCCHHHH
3.74-
61S-nitrosylationGLGTPEHCPGQCLPW
CCCCCCCCCCCHHHH
3.7422178444
65S-nitrosocysteinePEHCPGQCLPWACKV
CCCCCCCHHHHHHHH
6.46-
65S-nitrosylationPEHCPGQCLPWACKV
CCCCCCCHHHHHHHH
6.4622178444
70S-nitrosocysteineGQCLPWACKVCKRKS
CCHHHHHHHHHCCCC
2.76-
70S-nitrosylationGQCLPWACKVCKRKS
CCHHHHHHHHHCCCC
2.7622178444
77PhosphorylationCKVCKRKSVSVDRRR
HHHHCCCCCCCCHHH
24.53-
79PhosphorylationVCKRKSVSVDRRRAA
HHCCCCCCCCHHHHH
25.95-
87PhosphorylationVDRRRAATLREKRRL
CCHHHHHHHHHHHHH
25.9314751541

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
77SPhosphorylationKinaseCAMK2GQ923T9
Uniprot
79SPhosphorylationKinaseCAMK2GQ923T9
Uniprot
87TPhosphorylationKinaseKCC2AP11798
PhosphoELM
87TPhosphorylationKinaseCAMK2AP11275
PSP
87TPhosphorylationKinaseCAMK2GQ923T9
Uniprot
87TPhosphorylationKinasePRKCAP17252
GPS
87TPhosphorylationKinasePKCAP05696
PSP
-KUbiquitinationE3 ubiquitin ligaseFbxo32Q9CPU7
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
87TPhosphorylation

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Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MYOG_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EGLN3_HUMANEGLN3physical
17344222
EGLN3_MOUSEEgln3physical
17344222
VHL_HUMANVHLphysical
17344222
SKP1_MOUSESkp1aphysical
17242400
CUL1_MOUSECul1physical
17242400
CUL2_MOUSECul2physical
17242400
FBX32_MOUSEFbxo32physical
19631210

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYOG_MOUSE

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Related Literatures of Post-Translational Modification

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