dbPTM

THIL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	THIL_HUMAN
UniProt AC	P24752
Protein Name	Acetyl-CoA acetyltransferase, mitochondrial
Gene Name	ACAT1
Organism	Homo sapiens (Human).
Sequence Length	427
Subcellular Localization	Mitochondrion.
Protein Description	Plays a major role in ketone body metabolism..
Protein Sequence	MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	LLRSGARSRSPLLRR HHHCCCCCCCHHHHH	36.25	28634120
16	Phosphorylation	RSGARSRSPLLRRLV HCCCCCCCHHHHHHH	22.58	82900251
48	Phosphorylation	EVVIVSATRTPIGSF EEEEEEEECCCCHHH	27.80	961860225
66	Acetylation	LSLLPATKLGSIAIQ HHCCCCCHHHHHHHH	53.62	25038526
66	Succinylation	LSLLPATKLGSIAIQ HHCCCCCHHHHHHHH	53.62	-
66	Succinylation	LSLLPATKLGSIAIQ HHCCCCCHHHHHHHH	53.62	-
69	Phosphorylation	LPATKLGSIAIQGAI CCCCHHHHHHHHHHH	21.20	28857561
78	2-Hydroxyisobutyrylation	AIQGAIEKAGIPKEE HHHHHHHHHCCCHHH	45.88	-
78	Acetylation	AIQGAIEKAGIPKEE HHHHHHHHHCCCHHH	45.88	25953088
78	Succinylation	AIQGAIEKAGIPKEE HHHHHHHHHCCCHHH	45.88	-
78	Succinylation	AIQGAIEKAGIPKEE HHHHHHHHHCCCHHH	45.88	-
83	Acetylation	IEKAGIPKEEVKEAY HHHHCCCHHHHHHHH	65.66	19608861
87	2-Hydroxyisobutyrylation	GIPKEEVKEAYMGNV CCCHHHHHHHHHHCC	39.65	-
87	Acetylation	GIPKEEVKEAYMGNV CCCHHHHHHHHHHCC	39.65	25038526
87	Ubiquitination	GIPKEEVKEAYMGNV CCCHHHHHHHHHHCC	39.65	-
90	Phosphorylation	KEEVKEAYMGNVLQG HHHHHHHHHHCCCCC	13.47	22322629
91	Sulfoxidation	EEVKEAYMGNVLQGG HHHHHHHHHCCCCCC	3.97	28183972
116	Phosphorylation	LGAGLPISTPCTTIN HCCCCCCCCCCHHHH	25.10	20068231
117	Phosphorylation	GAGLPISTPCTTINK CCCCCCCCCCHHHHH	24.09	20068231
120	Phosphorylation	LPISTPCTTINKVCA CCCCCCCHHHHHHHH	31.73	28857561
121	Phosphorylation	PISTPCTTINKVCAS CCCCCCHHHHHHHHH	29.30	28857561
124	Acetylation	TPCTTINKVCASGMK CCCHHHHHHHHHHHH	34.54	23749302
128	Phosphorylation	TINKVCASGMKAIMM HHHHHHHHHHHHHHH	34.00	-
128 (in isoform 2)	Phosphorylation	-	34.00	18669648
131	Acetylation	KVCASGMKAIMMASQ HHHHHHHHHHHHHHC	37.98	30582497
137	Phosphorylation	MKAIMMASQSLMCGH HHHHHHHHCHHHCCC	11.47	46157431
139	Phosphorylation	AIMMASQSLMCGHQD HHHHHHCHHHCCCCC	18.64	28464451
150 (in isoform 2)	Phosphorylation	-	7.25	18669648
167	Phosphorylation	PYVMNRGSTPYGGVK CEEECCCCCCCCCCC	23.99	21601212
170	Phosphorylation	MNRGSTPYGGVKLED ECCCCCCCCCCCHHH	26.97	22985185
174	Acetylation	STPYGGVKLEDLIVK CCCCCCCCHHHEEEE	49.81	19608861
174	Malonylation	STPYGGVKLEDLIVK CCCCCCCCHHHEEEE	49.81	26320211
174	Succinylation	STPYGGVKLEDLIVK CCCCCCCCHHHEEEE	49.81	-
174	Succinylation	STPYGGVKLEDLIVK CCCCCCCCHHHEEEE	49.81	-
174	Ubiquitination	STPYGGVKLEDLIVK CCCCCCCCHHHEEEE	49.81	21890473
181	2-Hydroxyisobutyrylation	KLEDLIVKDGLTDVY CHHHEEEECCCHHHH	38.80	-
181	Acetylation	KLEDLIVKDGLTDVY CHHHEEEECCCHHHH	38.80	19608861
181	Succinylation	KLEDLIVKDGLTDVY CHHHEEEECCCHHHH	38.80	-
181	Succinylation	KLEDLIVKDGLTDVY CHHHEEEECCCHHHH	38.80	21890473
181	Ubiquitination	KLEDLIVKDGLTDVY CHHHEEEECCCHHHH	38.80	21890473
190	Acetylation	GLTDVYNKIHMGSCA CCHHHHHHHCCCCHH	19.12	23749302
190	Malonylation	GLTDVYNKIHMGSCA CCHHHHHHHCCCCHH	19.12	26320211
190	Succinylation	GLTDVYNKIHMGSCA CCHHHHHHHCCCCHH	19.12	-
190	Succinylation	GLTDVYNKIHMGSCA CCHHHHHHHCCCCHH	19.12	-
190	Ubiquitination	GLTDVYNKIHMGSCA CCHHHHHHHCCCCHH	19.12	19608861
195	Phosphorylation	YNKIHMGSCAENTAK HHHHCCCCHHHHHHH	11.54	28857561
196	Glutathionylation	NKIHMGSCAENTAKK HHHCCCCHHHHHHHH	4.57	22555962
202	2-Hydroxyisobutyrylation	SCAENTAKKLNIARN CHHHHHHHHHCCCCC	56.61	-
202	Acetylation	SCAENTAKKLNIARN CHHHHHHHHHCCCCC	56.61	19608861
202	Succinylation	SCAENTAKKLNIARN CHHHHHHHHHCCCCC	56.61	-
202	Succinylation	SCAENTAKKLNIARN CHHHHHHHHHCCCCC	56.61	23954790
203	Acetylation	CAENTAKKLNIARNE HHHHHHHHHCCCCCC	44.28	24889757
214	Phosphorylation	ARNEQDAYAINSYTR CCCCCCHHHHHHHHH	19.12	28152594
218	Phosphorylation	QDAYAINSYTRSKAA CCHHHHHHHHHHHHH	23.05	28857561
219	Phosphorylation	DAYAINSYTRSKAAW CHHHHHHHHHHHHHH	11.15	28152594
220	Phosphorylation	AYAINSYTRSKAAWE HHHHHHHHHHHHHHH	28.43	28152594
222	Phosphorylation	AINSYTRSKAAWEAG HHHHHHHHHHHHHCC	20.88	46157437
223	Acetylation	INSYTRSKAAWEAGK HHHHHHHHHHHHCCC	38.54	-
223	Succinylation	INSYTRSKAAWEAGK HHHHHHHHHHHHCCC	38.54	-
223	Succinylation	INSYTRSKAAWEAGK HHHHHHHHHHHHCCC	38.54	-
230	Acetylation	KAAWEAGKFGNEVIP HHHHHCCCCCCEEEE	58.09	23954790
230	Succinylation	KAAWEAGKFGNEVIP HHHHHCCCCCCEEEE	58.09	-
230	Succinylation	KAAWEAGKFGNEVIP HHHHHCCCCCCEEEE	58.09	-
230	Ubiquitination	KAAWEAGKFGNEVIP HHHHHCCCCCCEEEE	58.09	-
239	Phosphorylation	GNEVIPVTVTVKGQP CCEEEEEEEEECCCC	12.71	28857561
241	Phosphorylation	EVIPVTVTVKGQPDV EEEEEEEEECCCCCE	13.72	28857561
243	Acetylation	IPVTVTVKGQPDVVV EEEEEEECCCCCEEE	42.32	26051181
243	Malonylation	IPVTVTVKGQPDVVV EEEEEEECCCCCEEE	42.32	26320211
243	Succinylation	IPVTVTVKGQPDVVV EEEEEEECCCCCEEE	42.32	-
243	Succinylation	IPVTVTVKGQPDVVV EEEEEEECCCCCEEE	42.32	27452117
251	Acetylation	GQPDVVVKEDEEYKR CCCCEEECCCCCCCC	48.08	19608861
251	Malonylation	GQPDVVVKEDEEYKR CCCCEEECCCCCCCC	48.08	26320211
251	Succinylation	GQPDVVVKEDEEYKR CCCCEEECCCCCCCC	48.08	23954790
257	2-Hydroxyisobutyrylation	VKEDEEYKRVDFSKV ECCCCCCCCCCHHHC	49.58	-
257	Acetylation	VKEDEEYKRVDFSKV ECCCCCCCCCCHHHC	49.58	25953088
262	Phosphorylation	EYKRVDFSKVPKLKT CCCCCCHHHCCCCEE	28.42	24275569
263	2-Hydroxyisobutyrylation	YKRVDFSKVPKLKTV CCCCCHHHCCCCEEE	63.65	-
263	Acetylation	YKRVDFSKVPKLKTV CCCCCHHHCCCCEEE	63.65	19608861
263	Malonylation	YKRVDFSKVPKLKTV CCCCCHHHCCCCEEE	63.65	26320211
263	Succinylation	YKRVDFSKVPKLKTV CCCCCHHHCCCCEEE	63.65	-
263	Succinylation	YKRVDFSKVPKLKTV CCCCCHHHCCCCEEE	63.65	23954790
263	Ubiquitination	YKRVDFSKVPKLKTV CCCCCHHHCCCCEEE	63.65	19608861
266	Succinylation	VDFSKVPKLKTVFQK CCHHHCCCCEEEEEE	66.65	-
266	Succinylation	VDFSKVPKLKTVFQK CCHHHCCCCEEEEEE	66.65	-
268	2-Hydroxyisobutyrylation	FSKVPKLKTVFQKEN HHHCCCCEEEEEECC	49.09	-
268	Malonylation	FSKVPKLKTVFQKEN HHHCCCCEEEEEECC	49.09	26320211
268	Succinylation	FSKVPKLKTVFQKEN HHHCCCCEEEEEECC	49.09	-
268	Succinylation	FSKVPKLKTVFQKEN HHHCCCCEEEEEECC	49.09	27452117
273	Acetylation	KLKTVFQKENGTVTA CCEEEEEECCCEEEE	41.50	-
273	Malonylation	KLKTVFQKENGTVTA CCEEEEEECCCEEEE	41.50	26320211
273	Succinylation	KLKTVFQKENGTVTA CCEEEEEECCCEEEE	41.50	27452117
279	Phosphorylation	QKENGTVTAANASTL EECCCEEEECCCHHC	21.64	21712546
285	Phosphorylation	VTAANASTLNDGAAA EEECCCHHCCCCHHH	27.46	63770301
302	Acetylation	LMTADAAKRLNVTPL HHCHHHHHHCCCCHH	60.17	25953088
302	Succinylation	LMTADAAKRLNVTPL HHCHHHHHHCCCCHH	60.17	23954790
302	Ubiquitination	LMTADAAKRLNVTPL HHCHHHHHHCCCCHH	60.17	-
307	Phosphorylation	AAKRLNVTPLARIVA HHHHCCCCHHHHHHH	16.12	23312004
338	Acetylation	YAASMVLKDVGLKKE HHHHHHHHHCCCCHH	38.67	25038526
373	Acetylation	MLEIDPQKVNINGGA EEEECCCCCCCCCCC	42.51	25038526
403	Acetylation	GHLTHALKQGEYGLA HHHHHHHHCCCCCCH	57.97	25953088
407	Phosphorylation	HALKQGEYGLASICN HHHHCCCCCCHHHCC	25.02	19702290

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
407	Y	Phosphorylation	Kinase	FGFR1	P11362	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
268	K	Succinylation		-
Succinylation at Lys-268, 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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
THIM_HUMAN	ACAA2	physical	22939629
TOPB1_HUMAN	TOPBP1	physical	22939629
TMM65_HUMAN	TMEM65	physical	22939629
TIM44_HUMAN	TIMM44	physical	22939629
TOM7_HUMAN	TOMM7	physical	22939629
UBL4A_HUMAN	UBL4A	physical	22939629
TTF2_HUMAN	TTF2	physical	22939629
XPO2_HUMAN	CSE1L	physical	22939629
UBP2L_HUMAN	UBAP2L	physical	22939629
SPYA_HUMAN	AGXT	physical	21988832
THIL_HUMAN	ACAT1	physical	17371050
ABCB7_HUMAN	ABCB7	physical	26344197
THIM_HUMAN	ACAA2	physical	26344197
CRIP1_HUMAN	CRIP1	physical	26344197
DDB1_HUMAN	DDB1	physical	26344197
DLDH_HUMAN	DLD	physical	26344197
DUS3L_HUMAN	DUS3L	physical	26344197
ERCC2_HUMAN	ERCC2	physical	26344197
ILVBL_HUMAN	ILVBL	physical	26344197
SFXN1_HUMAN	SFXN1	physical	26344197
SFXN3_HUMAN	SFXN3	physical	26344197
SGMR1_HUMAN	SIGMAR1	physical	26344197
UCRI_HUMAN	UQCRFS1	physical	26344197
ODPA_HUMAN	PDHA1	physical	24486017
PDP1_HUMAN	PDP1	physical	24486017

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
203750	3-ketothiolase deficiency (3KTD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00795	Sulfasalazine

Regulatory Network of THIL_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83; LYS-174; LYS-181;LYS-251 AND LYS-263, AND MASS SPECTROMETRY.	19608861 [Abstract]

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