BACH_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BACH_MOUSE
• UniProt AC: Q91V12
• Protein Name: Cytosolic acyl coenzyme A thioester hydrolase
• Gene Name: Acot7
• Organism: Mus musculus (Mouse).
• Sequence Length: 381
• Subcellular Localization: Isoform A: Cytoplasm.; Isoform D: Cytoplasm.
• Protein Description: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl-CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA..
• Protein Sequence: MKLLVGTLRLWEVGRQVAFSSLTPGQECSGLRKTFWAAMRAVRTRADHQKLGHCVTMGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVHVMSENILTGTKKLTNKATLWYVPLSLKNVDKVLEVPPIVYLRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDNSQKRYRAASAFFTYVSLNQEGKPMPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHTEPQP

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
2 (in isoform 2)	Phosphorylation	-	50.99	25266776
5 (in isoform 2)	Phosphorylation	-	8.79	26643407
6 (in isoform 2)	Phosphorylation	-	20.99	26643407
8 (in isoform 2)	Phosphorylation	-	3.31	23984901
43 (in isoform 4)	Phosphorylation	-	19.94	29233185
46 (in isoform 4)	Phosphorylation	-	20.30	26643407
47 (in isoform 4)	Phosphorylation	-	41.27	26643407
49 (in isoform 4)	Phosphorylation	-	43.12	23984901
50	Acetylation	RTRADHQKLGHCVTM HHHHHHHHHCCEEEE	53.68	23806337
101	Glutathionylation	NSQNGERCVAALARV CCCCHHHHHHHHHCC	1.81	24333276
158	Ubiquitination	GTKKLTNKATLWYVP CCEECCCCCEEEEEE	37.20	-
158	Succinylation	GTKKLTNKATLWYVP CCEECCCCCEEEEEE	37.20	23806337
158	Acetylation	GTKKLTNKATLWYVP CCEECCCCCEEEEEE	37.20	23806337
169	Acetylation	WYVPLSLKNVDKVLE EEEECCCCCHHHEEC	52.10	22733758
169	Ubiquitination	WYVPLSLKNVDKVLE EEEECCCCCHHHEEC	52.10	-
173	Ubiquitination	LSLKNVDKVLEVPPI CCCCCHHHEECCCCE	44.42	-
195	Phosphorylation	EEEGRKRYEAQKLER HHHHHHHHHHHHHHH	20.74	20561277
199	Acetylation	RKRYEAQKLERMETK HHHHHHHHHHHHHHH	60.40	-
284	Acetylation	DAINFHDKIRKGCVI CEEECCHHHCCCCEE	35.52	23236377
287	Malonylation	NFHDKIRKGCVITIS ECCHHHCCCCEEEEC	61.20	26320211
287	Acetylation	NFHDKIRKGCVITIS ECCHHHCCCCEEEEC	61.20	23806337
287	Succinylation	NFHDKIRKGCVITIS ECCHHHCCCCEEEEC	61.20	23806337
289	Glutathionylation	HDKIRKGCVITISGR CHHHCCCCEEEECCE	1.93	24333276
322	Ubiquitination	PVVDNSQKRYRAASA CCCCCHHHHHHHHHH	51.74	-
366	Phosphorylation	FEEGKGRYLQMKAKR HHCCCCHHHHHHHHH	15.23	29899451
370	Ubiquitination	KGRYLQMKAKRQGHT CCHHHHHHHHHCCCC	37.48	-
370	Acetylation	KGRYLQMKAKRQGHT CCHHHHHHHHHCCCC	37.48	23806337
370	Succinylation	KGRYLQMKAKRQGHT CCHHHHHHHHHCCCC	37.48	23806337

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BACH_MOUSE !!

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of BACH_MOUSE !!

Drug and Disease Associations

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