MYOG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MYOG_HUMAN
• UniProt AC: P15173
• Protein Name: Myogenin
• Gene Name: MYOG
• Organism: Homo sapiens (Human).
• 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 (By similarity)..
• Protein Sequence: MELYETSPYFYQEPRFYDGENYLPVHLQGFEPPGYERTELTLSPEAPGPLEDKGLGTPEHCPGQCLPWACKVCKRKSVSVDRRRAATLREKRRLKKVNEAFEALKRSTLLNPNQRLPKVEILRSAIQYIERLQALLSSLNQEERDLRYRGGGGPQPGVPSECSSHSASCSPEWGSALEFSANPGDHLLTADPTDAHNLHSLTSIVDSITVEDVSVAFPDETMPN

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
4	Phosphorylation	----MELYETSPYFY ----CCCCCCCCCCC	12.12	-
9	Phosphorylation	ELYETSPYFYQEPRF CCCCCCCCCCCCCCC	18.06	-
11	Phosphorylation	YETSPYFYQEPRFYD CCCCCCCCCCCCCCC	13.21	-
22	Phosphorylation	RFYDGENYLPVHLQG CCCCCCCCCCEEECC	14.21	-
77	Phosphorylation	CKVCKRKSVSVDRRR HHHHCCCCCCCCHHH	24.53	-
79	Phosphorylation	VCKRKSVSVDRRRAA HHCCCCCCCCHHHHH	25.95	-
87	Phosphorylation	VDRRRAATLREKRRL CCHHHHHHHHHHHHH	25.93	-
128	Phosphorylation	ILRSAIQYIERLQAL HHHHHHHHHHHHHHH	9.91	29759185

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
77	S	Phosphorylation	Kinase	CAMK2G	Q13555	Uniprot
79	S	Phosphorylation	Kinase	CAMK2G	Q13555	Uniprot
87	T	Phosphorylation	Kinase	CAMK2G	Q13555	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO32	Q969P5	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
87	T	Phosphorylation	Phosphorylation of Thr-87 impairs both DNA-binding and trans-activation functions in contracting muscles (By similarity).	-

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SP1_HUMAN	SP1	physical	10082523
MEF2A_HUMAN	MEF2A	physical	1329097
RPB3_HUMAN	POLR2C	physical	12207009
TFE2_HUMAN	TCF3	physical	1325437
YMEL1_HUMAN	YME1L1	physical	21988832
TAF6L_HUMAN	TAF6L	physical	21988832
TRI43_HUMAN	TRIM43	physical	21988832
IF4E2_HUMAN	EIF4E2	physical	25416956
TXND9_HUMAN	TXNDC9	physical	25416956
CLUA1_HUMAN	CLUAP1	physical	25416956
HYPM_HUMAN	HYPM	physical	25416956
CC28A_HUMAN	CCDC28A	physical	25416956
TTC25_HUMAN	TTC25	physical	25416956
IKIP_HUMAN	IKBIP	physical	25416956
PACRL_HUMAN	PACRGL	physical	25416956
ITF2_HUMAN	TCF4	physical	26186194
TFE2_HUMAN	TCF3	physical	26186194
HTF4_HUMAN	TCF12	physical	26186194
NEST_HUMAN	NES	physical	26186194
TFE2_HUMAN	TCF3	physical	2163343
HNF1A_HUMAN	HNF1A	physical	1329097
HTF4_HUMAN	TCF12	physical	28514442
ITF2_HUMAN	TCF4	physical	28514442
TFE2_HUMAN	TCF3	physical	28514442
NEST_HUMAN	NES	physical	28514442
ID4_HUMAN	ID4	physical	28514442

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.