ACS2L_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ACS2L_MOUSE
• UniProt AC: Q99NB1
• Protein Name: Acetyl-coenzyme A synthetase 2-like, mitochondrial
• Gene Name: Acss1
• Organism: Mus musculus (Mouse).
• Sequence Length: 682
• Subcellular Localization: Mitochondrion matrix .
• Protein Description: Important for maintaining normal body temperature during fasting and for energy homeostasis. Essential for energy expenditure under ketogenic conditions. Converts acetate to acetyl-CoA so that it can be used for oxidation through the tricarboxylic cycle to produce ATP and CO(2)..
• Protein Sequence: MAARSLGSGVGRLLRGLQGRSGQSGWSLSVSRSTATRLPGCVPAAAQPGSYPALSAQAAQEPAAFWGPLARDTLVWDTPYHTVWDCDFRTGKIGWFLGGQLNVSVNCLDQHVQKSPETIALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITFNQGLRGGRVVELKKIVDEAVKSCPTVQHVLVAHRTDTKVPMGSLDIPLEQEMAKEAPVCTPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDGRCTLVDTWWQTETGGICIAPRPSEDGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVSGALCISQAWPGMARTIYGDHQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSRGQDLGDTTTLEDPSVITEILSAFQKYEEQRAATN

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
5	Phosphorylation	---MAARSLGSGVGR ---CCCHHHHCHHHH	32.15	23737553
8	Phosphorylation	MAARSLGSGVGRLLR CCCHHHHCHHHHHHH	35.28	23737553
41	S-nitrosocysteine	TATRLPGCVPAAAQP CCCCCCCCCCHHCCC	2.90	-
41	S-nitrosylation	TATRLPGCVPAAAQP CCCCCCCCCCHHCCC	2.90	21278135
86	S-nitrosocysteine	PYHTVWDCDFRTGKI CCCEEEECCCCCCCE	2.90	-
86	S-nitrosylation	PYHTVWDCDFRTGKI CCCEEEECCCCCCCE	2.90	21278135
144	S-nitrosocysteine	RELLETTCRLANTLK HHHHHHHHHHHHHHH	4.36	-
144	S-nitrosylation	RELLETTCRLANTLK HHHHHHHHHHHHHHH	4.36	21278135
178	S-nitrosocysteine	AVAAMLACARIGAIH HHHHHHHHHHHCCEE	2.00	-
178	S-nitrosylation	AVAAMLACARIGAIH HHHHHHHHHHHCCEE	2.00	21278135
235	S-nitrosocysteine	VDEAVKSCPTVQHVL HHHHHHCCCCCCEEE	2.44	-
235	S-nitrosylation	VDEAVKSCPTVQHVL HHHHHHCCCCCCEEE	2.44	21278135
271	S-nitrosocysteine	MAKEAPVCTPESMSS HHHHCCCCCCCCCCC	5.24	-
271	S-nitrosylation	MAKEAPVCTPESMSS HHHHCCCCCCCCCCC	5.24	21278135
389	Acetylation	TAVRLLLKYGDAWVK HHHHHHHHHCCHHHH	47.35	24062335
491	S-nitrosylation	GDVSGALCISQAWPG CCCCHHEEEEECCCC	2.52	21278135
491	S-nitrosocysteine	GDVSGALCISQAWPG CCCCHHEEEEECCCC	2.52	-
608	Phosphorylation	VVNELKLSVATKIAK HHHHHHHHHHHHHHH	14.23	26745281
611	Phosphorylation	ELKLSVATKIAKYAV HHHHHHHHHHHHHCC	22.34	26745281
635	Acetylation	LPKTRSGKVMRRLLR CCCCCCHHHHHHHHH	33.82	16790548

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

Oops, there are no upstream regulatory protein records of ACS2L_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
635	K	Acetylation	Reversibly acetylated at Lys-635.	16790548

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ACS2L_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ACS2L_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases.";
Hallows W.C., Lee S., Denu J.M.;
Proc. Natl. Acad. Sci. U.S.A. 103:10230-10235(2006).
Cited for: FUNCTION, INTERACTION WITH SIRT3, ENZYME REGULATION, MASSSPECTROMETRY, AND ACETYLATION AT LYS-635.
PubMed: 16790548