dbPTM

THIL_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	THIL_MOUSE
UniProt AC	Q8QZT1
Protein Name	Acetyl-CoA acetyltransferase, mitochondrial
Gene Name	Acat1
Organism	Mus musculus (Mouse).
Sequence Length	424
Subcellular Localization	Mitochondrion.
Protein Description	Plays a major role in ketone body metabolism..
Protein Sequence	MAALVALHGVVRRPLLRGLLQEVRCLERSYASKPTLNEVVIVSAIRTPIGSFLGSLASQPATKLGTAAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPISTPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCAENTAKKMNISRQEQDTYALSSYTRSKEAWDAGKFASEITPITISVKGKPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTITAANASTLNDGAAALVLMTAEAAQRLNVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVVLANIKMLEIDPQKVNIHGGAVSLGHPIGMSGARIVVHMAHALKPGEFGLASICNGGGGASALLIEKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	Acetylation	LERSYASKPTLNEVV HHHHHCCCCCCCEEE	33.57	23576753
33	Succinylation	LERSYASKPTLNEVV HHHHHCCCCCCCEEE	33.57	24315375
63	Acetylation	LASQPATKLGTAAIQ HHCCCCHHHHHHHHH	47.20	23576753
63	Malonylation	LASQPATKLGTAAIQ HHCCCCHHHHHHHHH	47.20	26320211
63	Succinylation	LASQPATKLGTAAIQ HHCCCCHHHHHHHHH	47.20	-
63	Succinylation	LASQPATKLGTAAIQ HHCCCCHHHHHHHHH	47.20	23806337
66	Phosphorylation	QPATKLGTAAIQGAI CCCHHHHHHHHHHHH	24.29	51457665
75	Acetylation	AIQGAIEKAGIPKEE HHHHHHHHHCCCHHH	45.88	23864654
75	Glutarylation	AIQGAIEKAGIPKEE HHHHHHHHHCCCHHH	45.88	24703693
75	Malonylation	AIQGAIEKAGIPKEE HHHHHHHHHCCCHHH	45.88	26320211
75	Succinylation	AIQGAIEKAGIPKEE HHHHHHHHHCCCHHH	45.88	-
75	Succinylation	AIQGAIEKAGIPKEE HHHHHHHHHCCCHHH	45.88	23806337
80	Acetylation	IEKAGIPKEEVKEVY HHHHCCCHHHHEEEE	65.66	23864654
80	Glutarylation	IEKAGIPKEEVKEVY HHHHCCCHHHHEEEE	65.66	24703693
80	Malonylation	IEKAGIPKEEVKEVY HHHHCCCHHHHEEEE	65.66	26320211
80	Succinylation	IEKAGIPKEEVKEVY HHHHCCCHHHHEEEE	65.66	26388266
84	Acetylation	GIPKEEVKEVYMGNV CCCHHHHEEEECCCC	44.75	23864654
84	Malonylation	GIPKEEVKEVYMGNV CCCHHHHEEEECCCC	44.75	26320211
84	Ubiquitination	GIPKEEVKEVYMGNV CCCHHHHEEEECCCC	44.75	-
87	Phosphorylation	KEEVKEVYMGNVIQG HHHHEEEECCCCCCC	10.61	20495213
116	S-nitrosocysteine	GLPISTPCTTVNKVC CCCCCCCCCHHHHHH	5.16	-
116	Glutathionylation	GLPISTPCTTVNKVC CCCCCCCCCHHHHHH	5.16	24333276
116	S-nitrosylation	GLPISTPCTTVNKVC CCCCCCCCCHHHHHH	5.16	24895380
116	S-palmitoylation	GLPISTPCTTVNKVC CCCCCCCCCHHHHHH	5.16	28526873
117	Phosphorylation	LPISTPCTTVNKVCA CCCCCCCCHHHHHHH	34.68	22817900
118	Phosphorylation	PISTPCTTVNKVCAS CCCCCCCHHHHHHHH	28.88	22817900
121	Acetylation	TPCTTVNKVCASGMK CCCCHHHHHHHHHHH	34.06	22826441
121	Malonylation	TPCTTVNKVCASGMK CCCCHHHHHHHHHHH	34.06	26320211
123	S-palmitoylation	CTTVNKVCASGMKAI CCHHHHHHHHHHHHH	2.39	28680068
139	S-nitrosocysteine	MASQSLMCGHQDVMV HHHCHHHCCCCCEEE	5.51	-
139	S-nitrosylation	MASQSLMCGHQDVMV HHHCHHHCCCCCEEE	5.51	22178444
152	Phosphorylation	MVAGGMESMSNVPYV EEECCHHHHCCCCCE	20.72	51457673
154	Phosphorylation	AGGMESMSNVPYVMS ECCHHHHCCCCCEEC	43.91	51457681
158	Phosphorylation	ESMSNVPYVMSRGAT HHHCCCCCEECCCCC	12.42	51457689
171	Acetylation	ATPYGGVKLEDLIVK CCCCCCCCHHHEEEC	49.81	23806337
171	Glutarylation	ATPYGGVKLEDLIVK CCCCCCCCHHHEEEC	49.81	24703693
171	Malonylation	ATPYGGVKLEDLIVK CCCCCCCCHHHEEEC	49.81	26073543
171	Succinylation	ATPYGGVKLEDLIVK CCCCCCCCHHHEEEC	49.81	-
171	Succinylation	ATPYGGVKLEDLIVK CCCCCCCCHHHEEEC	49.81	23806337
171	Ubiquitination	ATPYGGVKLEDLIVK CCCCCCCCHHHEEEC	49.81	-
178	Acetylation	KLEDLIVKDGLTDVY CHHHEEECCCCHHHH	38.80	23576753
178	Glutarylation	KLEDLIVKDGLTDVY CHHHEEECCCCHHHH	38.80	24703693
178	Malonylation	KLEDLIVKDGLTDVY CHHHEEECCCCHHHH	38.80	26073543
178	Succinylation	KLEDLIVKDGLTDVY CHHHEEECCCCHHHH	38.80	-
178	Succinylation	KLEDLIVKDGLTDVY CHHHEEECCCCHHHH	38.80	23806337
178	Ubiquitination	KLEDLIVKDGLTDVY CHHHEEECCCCHHHH	38.80	-
187	Acetylation	GLTDVYNKIHMGNCA CCHHHHHHHHCCCHH	19.12	23576753
187	Glutarylation	GLTDVYNKIHMGNCA CCHHHHHHHHCCCHH	19.12	24703693
187	Malonylation	GLTDVYNKIHMGNCA CCHHHHHHHHCCCHH	19.12	26320211
187	Succinylation	GLTDVYNKIHMGNCA CCHHHHHHHHCCCHH	19.12	-
187	Succinylation	GLTDVYNKIHMGNCA CCHHHHHHHHCCCHH	19.12	23806337
193	S-nitrosocysteine	NKIHMGNCAENTAKK HHHHCCCHHHHHHHH	4.10	-
193	Glutathionylation	NKIHMGNCAENTAKK HHHHCCCHHHHHHHH	4.10	24333276
193	S-nitrosylation	NKIHMGNCAENTAKK HHHHCCCHHHHHHHH	4.10	22178444
193	S-palmitoylation	NKIHMGNCAENTAKK HHHHCCCHHHHHHHH	4.10	28526873
199	Acetylation	NCAENTAKKMNISRQ CHHHHHHHHCCCCHH	50.98	23576753
199	Glutarylation	NCAENTAKKMNISRQ CHHHHHHHHCCCCHH	50.98	24703693
199	Malonylation	NCAENTAKKMNISRQ CHHHHHHHHCCCCHH	50.98	26320211
199	Succinylation	NCAENTAKKMNISRQ CHHHHHHHHCCCCHH	50.98	-
199	Succinylation	NCAENTAKKMNISRQ CHHHHHHHHCCCCHH	50.98	23806337
200	Malonylation	CAENTAKKMNISRQE HHHHHHHHCCCCHHH	34.41	25418362
204	Phosphorylation	TAKKMNISRQEQDTY HHHHCCCCHHHHCHH	23.94	22817900
210	Phosphorylation	ISRQEQDTYALSSYT CCHHHHCHHHHHHHC	15.47	25293948
211	Phosphorylation	SRQEQDTYALSSYTR CHHHHCHHHHHHHCC	17.52	25293948
214	Phosphorylation	EQDTYALSSYTRSKE HHCHHHHHHHCCCHH	17.08	59151853
215	Phosphorylation	QDTYALSSYTRSKEA HCHHHHHHHCCCHHH	31.23	25293948
216	Phosphorylation	DTYALSSYTRSKEAW CHHHHHHHCCCHHHH	11.64	25293948
217	Phosphorylation	TYALSSYTRSKEAWD HHHHHHHCCCHHHHH	30.34	25293948
220	Acetylation	LSSYTRSKEAWDAGK HHHHCCCHHHHHCCC	48.43	23576753
220	Glutarylation	LSSYTRSKEAWDAGK HHHHCCCHHHHHCCC	48.43	24703693
220	Malonylation	LSSYTRSKEAWDAGK HHHHCCCHHHHHCCC	48.43	26320211
220	Succinylation	LSSYTRSKEAWDAGK HHHHCCCHHHHHCCC	48.43	-
220	Succinylation	LSSYTRSKEAWDAGK HHHHCCCHHHHHCCC	48.43	23806337
227	Acetylation	KEAWDAGKFASEITP HHHHHCCCCCCCCCC	39.20	23576753
227	Succinylation	KEAWDAGKFASEITP HHHHHCCCCCCCCCC	39.20	-
227	Succinylation	KEAWDAGKFASEITP HHHHHCCCCCCCCCC	39.20	23806337
230	Phosphorylation	WDAGKFASEITPITI HHCCCCCCCCCCEEE	32.44	22324799
233	Phosphorylation	GKFASEITPITISVK CCCCCCCCCEEEEEC	12.46	26643407
236	Phosphorylation	ASEITPITISVKGKP CCCCCCEEEEECCCC	14.38	23984901
238	Phosphorylation	EITPITISVKGKPDV CCCCEEEEECCCCCE	14.77	26643407
240	Acetylation	TPITISVKGKPDVVV CCEEEEECCCCCEEE	55.19	23806337
240	Glutarylation	TPITISVKGKPDVVV CCEEEEECCCCCEEE	55.19	24703693
240	Malonylation	TPITISVKGKPDVVV CCEEEEECCCCCEEE	55.19	26320211
240	Succinylation	TPITISVKGKPDVVV CCEEEEECCCCCEEE	55.19	-
240	Succinylation	TPITISVKGKPDVVV CCEEEEECCCCCEEE	55.19	23806337
242	Acetylation	ITISVKGKPDVVVKE EEEEECCCCCEEECC	32.12	23576753
242	Malonylation	ITISVKGKPDVVVKE EEEEECCCCCEEECC	32.12	26320211
242	Succinylation	ITISVKGKPDVVVKE EEEEECCCCCEEECC	32.12	-
242	Succinylation	ITISVKGKPDVVVKE EEEEECCCCCEEECC	32.12	23806337
242	Ubiquitination	ITISVKGKPDVVVKE EEEEECCCCCEEECC	32.12	27667366
248	Acetylation	GKPDVVVKEDEEYKR CCCCEEECCCCCCCC	48.08	23576753
248	Succinylation	GKPDVVVKEDEEYKR CCCCEEECCCCCCCC	48.08	26388266
254	Acetylation	VKEDEEYKRVDFSKV ECCCCCCCCCCHHHC	49.58	23576753
254	Succinylation	VKEDEEYKRVDFSKV ECCCCCCCCCCHHHC	49.58	26388266
260	Acetylation	YKRVDFSKVPKLKTV CCCCCHHHCCCCEEE	63.65	23576753
260	Glutarylation	YKRVDFSKVPKLKTV CCCCCHHHCCCCEEE	63.65	24703693
260	Malonylation	YKRVDFSKVPKLKTV CCCCCHHHCCCCEEE	63.65	26073543
260	Succinylation	YKRVDFSKVPKLKTV CCCCCHHHCCCCEEE	63.65	-
260	Succinylation	YKRVDFSKVPKLKTV CCCCCHHHCCCCEEE	63.65	23806337
260	Ubiquitination	YKRVDFSKVPKLKTV CCCCCHHHCCCCEEE	63.65	-
263	Acetylation	VDFSKVPKLKTVFQK CCHHHCCCCEEEEEE	66.65	24062335
263	Succinylation	VDFSKVPKLKTVFQK CCHHHCCCCEEEEEE	66.65	-
263	Succinylation	VDFSKVPKLKTVFQK CCHHHCCCCEEEEEE	66.65	23806337
265	Acetylation	FSKVPKLKTVFQKEN HHHCCCCEEEEEECC	49.09	23806337
265	Malonylation	FSKVPKLKTVFQKEN HHHCCCCEEEEEECC	49.09	26320211
265	Succinylation	FSKVPKLKTVFQKEN HHHCCCCEEEEEECC	49.09	-
265	Succinylation	FSKVPKLKTVFQKEN HHHCCCCEEEEEECC	49.09	23806337
265	Ubiquitination	FSKVPKLKTVFQKEN HHHCCCCEEEEEECC	49.09	-
270	Acetylation	KLKTVFQKENGTITA CCEEEEEECCCEEEE	41.50	23576753
270	Malonylation	KLKTVFQKENGTITA CCEEEEEECCCEEEE	41.50	26073543
270	Succinylation	KLKTVFQKENGTITA CCEEEEEECCCEEEE	41.50	23806337
304	Acetylation	AAQRLNVKPLARIAA HHHHCCCCCHHHHHH	32.99	23864654
304	Glutarylation	AAQRLNVKPLARIAA HHHHCCCCCHHHHHH	32.99	24703693
304	Malonylation	AAQRLNVKPLARIAA HHHHCCCCCHHHHHH	32.99	26073543
304	Ubiquitination	AAQRLNVKPLARIAA HHHHCCCCCHHHHHH	32.99	27667366
328	Nitration	DFPLAPAYAVPKVLK CCCCCHHHHHHHHHH	13.68	-
328	Phosphorylation	DFPLAPAYAVPKVLK CCCCCHHHHHHHHHH	13.68	8234157
332	Acetylation	APAYAVPKVLKYAGL CHHHHHHHHHHHCCC	54.31	22733758
335	Acetylation	YAVPKVLKYAGLKKE HHHHHHHHHCCCCHH	35.72	23576753
335	Glutarylation	YAVPKVLKYAGLKKE HHHHHHHHHCCCCHH	35.72	24703693
335	Malonylation	YAVPKVLKYAGLKKE HHHHHHHHHCCCCHH	35.72	26073543
335	Succinylation	YAVPKVLKYAGLKKE HHHHHHHHHCCCCHH	35.72	-
335	Ubiquitination	YAVPKVLKYAGLKKE HHHHHHHHHCCCCHH	35.72	-
340	Acetylation	VLKYAGLKKEDIAMW HHHHCCCCHHHEEEE	53.88	23864654
370	Acetylation	MLEIDPQKVNIHGGA EEEECCCCEEECCCC	42.51	23954790
370	Malonylation	MLEIDPQKVNIHGGA EEEECCCCEEECCCC	42.51	26320211
370	Ubiquitination	MLEIDPQKVNIHGGA EEEECCCCEEECCCC	42.51	-
400	Acetylation	VHMAHALKPGEFGLA EEHHHCCCCCCCCCC	52.33	24062335
400	Malonylation	VHMAHALKPGEFGLA EEHHHCCCCCCCCCC	52.33	26073543
410	S-nitrosocysteine	EFGLASICNGGGGAS CCCCCHHCCCCCCCH	3.42	-
410	S-nitrosylation	EFGLASICNGGGGAS CCCCCHHCCCCCCCH	3.42	21278135

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
265	K	Succinylation		23806337
Succinylation at Lys-265, adjacent to a coenzyme A binding site.

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 THIL_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of THIL_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of THIL_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-171; LYS-187; LYS-227 ANDLYS-335, AND MASS SPECTROMETRY.	16916647 [Abstract]

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