DCMC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DCMC_HUMAN
• UniProt AC: O95822
• Protein Name: Malonyl-CoA decarboxylase, mitochondrial
• Gene Name: MLYCD
• Organism: Homo sapiens (Human).
• Sequence Length: 493
• Subcellular Localization: Cytoplasm . Mitochondrion matrix . Peroxisome . Peroxisome matrix. Enzymatically active in all three subcellular compartments..
• Protein Description: Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation..
• Protein Sequence: MRGFGPGLTARRLLPLRLPPRPPGPRLASGQAAGALERAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNGVLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQGVELGTFLIKRVVKELQREFPHLGVFSSLSPIPGFTKWLLGLLNSQTKEHGRNELFTDSECKEISEITGGPINETLKLLLSSSEWVQSEKLVRALQTPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVLWRINWMADVSLRGITGSCGLMANYRYFLEETGPNSTSYLGSKIIKASEQVLSLVAQFQKNSKL

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
9	O-linked_Glycosylation	RGFGPGLTARRLLPL CCCCCCCCHHHHCCC	24.84	30379171
59	Acetylation	PAYELREKTPAPAEG CHHHHHHCCCCCCCC	54.07	-
131	Phosphorylation	QAEDRLRYALVPRYR HHHHHHHHHHHHHCH	14.63	22817900
168	Acetylation	LLEAQALKLVEGPDV HHHHHHHHHHCCCCH	54.20	-
168	Succinylation	LLEAQALKLVEGPDV HHHHHHHHHHCCCCH	54.20	-
168	Succinylation	LLEAQALKLVEGPDV HHHHHHHHHHCCCCH	54.20	-
204	Phosphorylation	LERVTWHSPCEVLQK CEEEEECCHHHHHHH	23.86	-
211	Acetylation	SPCEVLQKISEAEAV CHHHHHHHHHHHHCC	44.00	-
222	Succinylation	AEAVHPVKNWMDMKR HHCCCCCCCHHHHHH	49.71	-
222	Succinylation	AEAVHPVKNWMDMKR HHCCCCCCCHHHHHH	49.71	-
329	Phosphorylation	LGVFSSLSPIPGFTK CCCCCCCCCCCHHHH	23.80	-
356	Phosphorylation	HGRNELFTDSECKEI CCCCCCCCHHHHHHH	51.76	23403867
358	Phosphorylation	RNELFTDSECKEISE CCCCCCHHHHHHHHH	41.66	23403867
361	Acetylation	LFTDSECKEISEITG CCCHHHHHHHHHHHC	54.77	25038526
387	Phosphorylation	SSSEWVQSEKLVRAL CCCHHHHHHHHHHHH	27.38	28270605
389	Acetylation	SEWVQSEKLVRALQT CHHHHHHHHHHHHHH	58.49	-
405	Phosphorylation	LMRLCAWYLYGEKHR HHHHHHHHHHCCCCC	3.29	-
414	Phosphorylation	YGEKHRGYALNPVAN HCCCCCCCCCCCCEE	14.10	-
471	Phosphorylation	NSTSYLGSKIIKASE CCCCCCCHHHHHHHH	20.34	25627689
472	Acetylation	STSYLGSKIIKASEQ CCCCCCHHHHHHHHH	46.80	-
492	Acetylation	AQFQKNSKL------ HHHHHHCCC------	68.55	7665945

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of DCMC_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
472	K	Acetylation	Acetylation at Lys-472 activates malonyl-CoA decarboxylase activity.	-
472	K	Acetylation	Deacetylation at Lys-472 by SIRT4 represses activity, leading to promote lipogenesis (By similarity).	-
472	K	Carboxylation	Acetylation at Lys-472 activates malonyl-CoA decarboxylase activity.	-

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of DCMC_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 248360: Malonyl-CoA decarboxylase deficiency (MLYCD deficiency)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND MASSSPECTROMETRY.
PubMed: 17081983