dbPTM

PRGC1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PRGC1_MOUSE
UniProt AC	O70343
Protein Name	Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
Gene Name	Ppargc1a
Organism	Mus musculus (Mouse).
Sequence Length	797
Subcellular Localization	Nucleus. Nucleus, PML body.
Protein Description	Transcriptional coactivator for steroid receptors and nuclear receptors. Greatly increases the transcriptional activity of PPARG and thyroid hormone receptor on the uncoupling protein promoter. Can regulate key mitochondrial genes that contribute to the program of adaptive thermogenesis. Plays an essential role in metabolic reprogramming in response to dietary availability through coordination of the expression of a wide array of genes involved in glucose and fatty acid metabolism. Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner. Also involved in the integration of the circadian rhythms and energy metabolism. Required for oscillatory expression of clock genes, such as ARNTL/BMAL1 and NR1D1, through the coactivation of RORA and RORC, and metabolic genes, such as PDK4 and PEPCK. Isoform 4 specifically activates the expression of IGF1 and suppresses myostatin expression in skeletal muscle leading to muscle fiber hypertrophy..
Protein Sequence	MAWDMCSQDSVWSDIECAALVGEDQPLCPDLPELDLSELDVNDLDTDSFLGGLKWCSDQSEIISNQYNNEPANIFEKIDEENEANLLAVLTETLDSLPVDEDGLPSFDALTDGAVTTDNEASPSSMPDGTPPPQEAEEPSLLKKLLLAPANTQLSYNECSGLSTQNHAANHTHRIRTNPAIVKTENSWSNKAKSICQQQKPQRRPCSELLKYLTTNDDPPHTKPTENRNSSRDKCASKKKSHTQPQSQHAQAKPTTLSLPLTPESPNDPKGSPFENKTIERTLSVELSGTAGLTPPTTPPHKANQDNPFKASPKLKPSCKTVVPPPTKRARYSECSGTQGSHSTKKGPEQSELYAQLSKSSGLSRGHEERKTKRPSLRLFGDHDYCQSLNSKTDILINISQELQDSRQLDFKDASCDWQGHICSSTDSGQCYLRETLEASKQVSPCSTRKQLQDQEIRAELNKHFGHPCQAVFDDKSDKTSELRDGDFSNEQFSKLPVFINSGLAMDGLFDDSEDESDKLSYPWDGTQPYSLFDVSPSCSSFNSPCRDSVSPPKSLFSQRPQRMRSRSRSFSRHRSCSRSPYSRSRSRSPGSRSSSRSCYYYESSHYRHRTHRNSPLYVRSRSRSPYSRRPRYDSYEAYEHERLKRDEYRKEHEKRESERAKQRERQKQKAIEERRVIYVGKIRPDTTRTELRDRFEVFGEIEECTVNLRDDGDSYGFITYRYTCDAFAALENGYTLRRSNETDFELYFCGRKQFFKSNYADLDTNSDDFDPASTKSKYDSLDFDSLLKEAQRSLRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
77	Acetylation	EPANIFEKIDEENEA CCCCHHHHCCCCCHH	44.71	15744310
144	Acetylation	EEPSLLKKLLLAPAN CCCCHHHHHHHCCCC	44.32	15744310
177	Phosphorylation	NHTHRIRTNPAIVKT CCCCCCCCCCCEEEC	43.09	17609368
183	Sumoylation	RTNPAIVKTENSWSN CCCCCEEECCCCCCH	43.97	-
183	Sumoylation	RTNPAIVKTENSWSN CCCCCEEECCCCCCH	43.97	-
183	Acetylation	RTNPAIVKTENSWSN CCCCCEEECCCCCCH	43.97	15744310
194	Phosphorylation	SWSNKAKSICQQQKP CCCHHHHHHHHCCCC	33.19	20351112
200	Acetylation	KSICQQQKPQRRPCS HHHHHCCCCCCCCHH	38.49	29977051
223	Acetylation	NDDPPHTKPTENRNS CCCCCCCCCCCCCCC	47.08	29977055
230	Phosphorylation	KPTENRNSSRDKCAS CCCCCCCCCHHHHHH	24.42	22871156
231	Phosphorylation	PTENRNSSRDKCASK CCCCCCCCHHHHHHC	48.31	19103600
241	Phosphorylation	KCASKKKSHTQPQSQ HHHHCCCCCCCCCCH	40.42	20351112
253	Acetylation	QSQHAQAKPTTLSLP CCHHCCCCCCEEECC	30.71	15744310
256	Phosphorylation	HAQAKPTTLSLPLTP HCCCCCCEEECCCCC	23.91	20351112
265	Phosphorylation	SLPLTPESPNDPKGS ECCCCCCCCCCCCCC	30.15	19103600
270	Acetylation	PESPNDPKGSPFENK CCCCCCCCCCCCCCC	74.92	15744310
272	Phosphorylation	SPNDPKGSPFENKTI CCCCCCCCCCCCCCE	32.32	19103600
277	Acetylation	KGSPFENKTIERTLS CCCCCCCCCEEEEEE	43.62	15744310
284	Phosphorylation	KTIERTLSVELSGTA CCEEEEEEEEEECCC	16.97	-
294	Phosphorylation	LSGTAGLTPPTTPPH EECCCCCCCCCCCCC	26.72	19103600
298	Phosphorylation	AGLTPPTTPPHKANQ CCCCCCCCCCCCCCC	40.37	19103600
312	Phosphorylation	QDNPFKASPKLKPSC CCCCCCCCCCCCCCC	24.13	19103600
320	Acetylation	PKLKPSCKTVVPPPT CCCCCCCCCCCCCCC	49.01	15744310
333	O-linked_Glycosylation	PTKRARYSECSGTQG CCCCCCHHHCCCCCC	26.94	29977041
346	Acetylation	QGSHSTKKGPEQSEL CCCCCCCCCHHHHHH	78.69	15744310
358	Phosphorylation	SELYAQLSKSSGLSR HHHHHHHHHCCCCCC	20.57	-
360	Phosphorylation	LYAQLSKSSGLSRGH HHHHHHHCCCCCCCC	26.68	-
361	Phosphorylation	YAQLSKSSGLSRGHE HHHHHHCCCCCCCCH	47.71	-
364	Phosphorylation	LSKSSGLSRGHEERK HHHCCCCCCCCHHHC	39.48	-
365	Methylation	SKSSGLSRGHEERKT HHCCCCCCCCHHHCC	56.37	29977043
412	Acetylation	DSRQLDFKDASCDWQ HHCCCCCCCCCCCCC	52.64	15744310
441	Acetylation	RETLEASKQVSPCST HHHHHHHCCCCCCCC	62.86	15744310
444	Phosphorylation	LEASKQVSPCSTRKQ HHHHCCCCCCCCHHH	20.07	19103600
447	Phosphorylation	SKQVSPCSTRKQLQD HCCCCCCCCHHHHHH	34.33	-
450	Acetylation	VSPCSTRKQLQDQEI CCCCCCHHHHHHHHH	56.29	15744310
538	Phosphorylation	SLFDVSPSCSSFNSP CCEECCCCCCCCCCC	21.08	17609368
568	Phosphorylation	PQRMRSRSRSFSRHR HHHHHHCCCHHHCCC	33.26	21646374
570	Phosphorylation	RMRSRSRSFSRHRSC HHHHCCCHHHCCCCC	28.90	17554339
572	Phosphorylation	RSRSRSFSRHRSCSR HHCCCHHHCCCCCCC	28.55	21646374
615	Phosphorylation	RHRTHRNSPLYVRSR CCCCCCCCCEEECCC	19.08	-
757	Acetylation	CGRKQFFKSNYADLD ECCHHHHHCCCCCCC	38.80	15744310
778	Acetylation	DPASTKSKYDSLDFD CCCCCHHHHHCCCHH	55.41	15744310

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
177	T	Phosphorylation	Kinase	AMPKA2	P54646	PSP
177	T	Phosphorylation	Kinase	PRKAA2	Q09137	GPS
177	T	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
177	T	Phosphorylation	Kinase	AMPK	-	Uniprot
194	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
241	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
241	S	Phosphorylation	Kinase	PKACA	P05132	PSP
256	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
538	S	Phosphorylation	Kinase	AMPKA2	P54646	PSP
538	S	Phosphorylation	Kinase	PRKAA2	Q09137	GPS
538	S	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
538	S	Phosphorylation	Kinase	AMPK	-	Uniprot
568	S	Phosphorylation	Kinase	RPS6KB1	P23443	GPS
570	S	Phosphorylation	Kinase	AKT1	P31749	PSP
570	S	Phosphorylation	Kinase	AKT2	Q60823	PSP
572	S	Phosphorylation	Kinase	RPS6KB1	P23443	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PRGC1_MOUSE !!

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 PRGC1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ERR1_MOUSE	Esrra	physical	19690166
NR1H3_MOUSE	Nr1h3	physical	20211142
HNF4A_MOUSE	Hnf4a	physical	15744310
MBB1A_MOUSE	Mybbp1a	physical	14744933
TYY1_MOUSE	Yy1	physical	18046414
EWS_MOUSE	Ewsr1	physical	25918410

Drug and Disease Associations

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

Regulatory Network of PRGC1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"AMP-activated protein kinase (AMPK) action in skeletal muscle viadirect phosphorylation of PGC-1alpha."; Jager S., Handschin C., St-Pierre J., Spiegelman B.M.; Proc. Natl. Acad. Sci. U.S.A. 104:12017-12022(2007). Cited for: PHOSPHORYLATION AT THR-177 AND SER-538, AND MUTAGENESIS OF THR-177 ANDSER-538.	17609368 [Abstract]