CISY_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CISY_MOUSE
• UniProt AC: Q9CZU6
• Protein Name: Citrate synthase, mitochondrial
• Gene Name: Cs
• Organism: Mus musculus (Mouse).
• Sequence Length: 464
• Subcellular Localization: Mitochondrion matrix.
• Protein Sequence: MALLTAATRLLGAKNSSCLVLAARHASASSTNLKDVLSNLIPKEQARIKTFKQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRAKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIGAIDSRLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPNILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLMKFVDSK

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
8	Phosphorylation	MALLTAATRLLGAKN CHHHHHHHHHHCCCC	21.27	24759943
17	Phosphorylation	LLGAKNSSCLVLAAR HHCCCCCHHHHHHHH	22.36	24759943
34	Acetylation	SASSTNLKDVLSNLI CCCCCCHHHHHHHCC	48.11	23576753
43	Ubiquitination	VLSNLIPKEQARIKT HHHHCCCHHHHHHHH	56.30	-
43	Malonylation	VLSNLIPKEQARIKT HHHHCCCHHHHHHHH	56.30	26320211
43	Glutarylation	VLSNLIPKEQARIKT HHHHCCCHHHHHHHH	56.30	24703693
43	Acetylation	VLSNLIPKEQARIKT HHHHCCCHHHHHHHH	56.30	23864654
49	Acetylation	PKEQARIKTFKQQHG CHHHHHHHHHHHHHC	42.21	23576753
49	Succinylation	PKEQARIKTFKQQHG CHHHHHHHHHHHHHC	42.21	26388266
52	Acetylation	QARIKTFKQQHGKTV HHHHHHHHHHHCCEE	55.04	23864654
52	Succinylation	QARIKTFKQQHGKTV HHHHHHHHHHHCCEE	55.04	26388266
52	Glutarylation	QARIKTFKQQHGKTV HHHHHHHHHHHCCEE	55.04	24703693
57	Succinylation	TFKQQHGKTVVGQIT HHHHHHCCEEEEEEE	35.70	23806337
57	Acetylation	TFKQQHGKTVVGQIT HHHHHHCCEEEEEEE	35.70	23806337
57	Succinylation	TFKQQHGKTVVGQIT HHHHHHCCEEEEEEE	35.70	-
76	Ubiquitination	YGGMRGMKGLVYETS CCCCCCCCCEEEEEE	52.49	-
76	Malonylation	YGGMRGMKGLVYETS CCCCCCCCCEEEEEE	52.49	26073543
76	Succinylation	YGGMRGMKGLVYETS CCCCCCCCCEEEEEE	52.49	-
76	Acetylation	YGGMRGMKGLVYETS CCCCCCCCCEEEEEE	52.49	2383727
76	Succinylation	YGGMRGMKGLVYETS CCCCCCCCCEEEEEE	52.49	-
97	Phosphorylation	GIRFRGYSIPECQKM CCCCCCCCCHHHHHH	34.19	23684622
101	Glutathionylation	RGYSIPECQKMLPKA CCCCCHHHHHHCCCC	3.85	24333276
101	S-nitrosylation	RGYSIPECQKMLPKA CCCCCHHHHHHCCCC	3.85	24895380
101	S-palmitoylation	RGYSIPECQKMLPKA CCCCCHHHHHHCCCC	3.85	26165157
101	S-nitrosocysteine	RGYSIPECQKMLPKA CCCCCHHHHHHCCCC	3.85	-
103	Succinylation	YSIPECQKMLPKAKG CCCHHHHHHCCCCCC	54.80	23806337
103	Acetylation	YSIPECQKMLPKAKG CCCHHHHHHCCCCCC	54.80	23864654
103	Succinylation	YSIPECQKMLPKAKG CCCHHHHHHCCCCCC	54.80	-
103	Ubiquitination	YSIPECQKMLPKAKG CCCHHHHHHCCCCCC	54.80	-
193	Succinylation	AEGMNRAKYWELIYE HHCCCHHHHHHHHHH	47.89	23806337
193	Acetylation	AEGMNRAKYWELIYE HHCCCHHHHHHHHHH	47.89	23806337
193	Succinylation	AEGMNRAKYWELIYE HHCCCHHHHHHHHHH	47.89	-
211	S-nitrosylation	DLIAKLPCVAAKIYR HHHHHCHHHHHHHHH	4.75	21278135
211	S-nitrosocysteine	DLIAKLPCVAAKIYR HHHHHCHHHHHHHHH	4.75	-
215	Ubiquitination	KLPCVAAKIYRNLYR HCHHHHHHHHHHHHH	30.45	22790023
225	Phosphorylation	RNLYREGSSIGAIDS HHHHHCCCCCCCCCC	17.65	25521595
226	Phosphorylation	NLYREGSSIGAIDSR HHHHCCCCCCCCCCC	35.58	27742792
232	Phosphorylation	SSIGAIDSRLDWSHN CCCCCCCCCCCCCCC	28.73	28833060
321	Glutarylation	QLQKEVGKDVSDEKL HHHHHHCCCCCHHHH	61.20	24703693
321	Acetylation	QLQKEVGKDVSDEKL HHHHHHCCCCCHHHH	61.20	23576753
321	Succinylation	QLQKEVGKDVSDEKL HHHHHHCCCCCHHHH	61.20	23806337
321	Succinylation	QLQKEVGKDVSDEKL HHHHHHCCCCCHHHH	61.20	-
327	Glutarylation	GKDVSDEKLRDYIWN CCCCCHHHHHHHHHH	54.54	24703693
327	Ubiquitination	GKDVSDEKLRDYIWN CCCCCHHHHHHHHHH	54.54	27667366
327	Succinylation	GKDVSDEKLRDYIWN CCCCCHHHHHHHHHH	54.54	23806337
327	Succinylation	GKDVSDEKLRDYIWN CCCCCHHHHHHHHHH	54.54	-
327	Acetylation	GKDVSDEKLRDYIWN CCCCCHHHHHHHHHH	54.54	23576753
345	Phosphorylation	SGRVVPGYGHAVLRK CCCCCCCCCCEEECC	10.32	25195567
359	S-nitrosylation	KTDPRYSCQREFALK CCCCCCCHHHHHHHH	3.07	21278135
359	S-nitrosocysteine	KTDPRYSCQREFALK CCCCCCCHHHHHHHH	3.07	-
366	Acetylation	CQREFALKHLPKDPM HHHHHHHHHCCCCHH	39.40	2394919
366	Ubiquitination	CQREFALKHLPKDPM HHHHHHHHHCCCCHH	39.40	27667366
370	Acetylation	FALKHLPKDPMFKLV HHHHHCCCCHHHHHH	79.44	2391839
370	Ubiquitination	FALKHLPKDPMFKLV HHHHHCCCCHHHHHH	79.44	22790023
370	Malonylation	FALKHLPKDPMFKLV HHHHHCCCCHHHHHH	79.44	26320211
375	Succinylation	LPKDPMFKLVAQLYK CCCCHHHHHHHHHHH	35.48	23806337
375	Acetylation	LPKDPMFKLVAQLYK CCCCHHHHHHHHHHH	35.48	23576753
375	Succinylation	LPKDPMFKLVAQLYK CCCCHHHHHHHHHHH	35.48	-
381	Phosphorylation	FKLVAQLYKIVPNIL HHHHHHHHHHHHHHH	6.13	-
382	Succinylation	KLVAQLYKIVPNILL HHHHHHHHHHHHHHH	45.91	26388266
382	Acetylation	KLVAQLYKIVPNILL HHHHHHHHHHHHHHH	45.91	23576753
393	Malonylation	NILLEQGKAKNPWPN HHHHHCCCCCCCCCC	56.75	26320211
393	Acetylation	NILLEQGKAKNPWPN HHHHHCCCCCCCCCC	56.75	23576753
393	Succinylation	NILLEQGKAKNPWPN HHHHHCCCCCCCCCC	56.75	-
393	Ubiquitination	NILLEQGKAKNPWPN HHHHHCCCCCCCCCC	56.75	-
393	Succinylation	NILLEQGKAKNPWPN HHHHHCCCCCCCCCC	56.75	23806337
395	"N6,N6,N6-trimethyllysine"	LLEQGKAKNPWPNVD HHHCCCCCCCCCCCC	68.01	-
395	Methylation	LLEQGKAKNPWPNVD HHHCCCCCCCCCCCC	68.01	-
450	Acetylation	GFPLERPKSMSTDGL CCCCCCCCCCCCCCC	66.08	23201123
450	Succinylation	GFPLERPKSMSTDGL CCCCCCCCCCCCCCC	66.08	-
450	Ubiquitination	GFPLERPKSMSTDGL CCCCCCCCCCCCCCC	66.08	27667366
450	Malonylation	GFPLERPKSMSTDGL CCCCCCCCCCCCCCC	66.08	26073543
450	Glutarylation	GFPLERPKSMSTDGL CCCCCCCCCCCCCCC	66.08	24703693
450	Succinylation	GFPLERPKSMSTDGL CCCCCCCCCCCCCCC	66.08	23806337
459	Acetylation	MSTDGLMKFVDSK-- CCCCCCHHHHCCC--	47.48	23576753
459	Ubiquitination	MSTDGLMKFVDSK-- CCCCCCHHHHCCC--	47.48	27667366
459	Succinylation	MSTDGLMKFVDSK-- CCCCCCHHHHCCC--	47.48	23806337
459	Succinylation	MSTDGLMKFVDSK-- CCCCCCHHHHCCC--	47.48	-
464	Acetylation	LMKFVDSK------- CHHHHCCC-------	60.95	6273231

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
225	S	Phosphorylation	Kinase	AKT1	P31749	PSP
225	S	Phosphorylation	Kinase	AKT1	P31750	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
395	K	Methylation	Trimethylation at Lys-395 by CSKMT decreases citrate synthase 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 CISY_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CISY_MOUSE !!

Drug and Disease Associations

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