SUCA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SUCA_MOUSE
• UniProt AC: Q9WUM5
• Protein Name: Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03222}
• Gene Name: Suclg1 {ECO:0000255|HAMAP-Rule:MF_03222}
• Organism: Mus musculus (Mouse).
• Sequence Length: 346
• Subcellular Localization: Mitochondrion .
• Protein Description: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and specificity for either ATP or GTP is provided by different beta subunits..
• Protein Sequence: MTATVVAAAATATMVSSSSGLAAARLLSRTFLLQQNGIRHGSYTASRKHIYIDKNTKIICQGFTGKQGTFHSQQALEYGTKLVGGTTPGKGGQKHLGLPVFNTVKEAKEKTGATASVIYVPPPFAAAAINEAIDAEIPLVVCITEGIPQQDMVRVKHRLTRQGTTRLIGPNCPGVINPGECKIGIMPGHIHKKGRIGIVSRSGTLTYEAVHQTTQVGLGQSLCIGIGGDPFNGTDFIDCLEVFLNDPATEGIILIGEIGGHAEENAAAFLKEHNSGPKAKPVVSFIAGITAPPGRRMGHAGAIIAGGKGGAKEKISALQSAGVVVSMSPAQLGTTIYKEFEKRKML

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	Phosphorylation	------MTATVVAAA ------CCHHHHHHH	30.91	-
48	Acetylation	GSYTASRKHIYIDKN CCEECCCCEEEECCC	31.68	24062335
54	Acetylation	RKHIYIDKNTKIICQ CCEEEECCCCEEEEC	57.89	23576753
54	Succinylation	RKHIYIDKNTKIICQ CCEEEECCCCEEEEC	57.89	23954790
57	Succinylation	IYIDKNTKIICQGFT EEECCCCEEEECCCC	39.19	-
57	Succinylation	IYIDKNTKIICQGFT EEECCCCEEEECCCC	39.19	23806337
57	Malonylation	IYIDKNTKIICQGFT EEECCCCEEEECCCC	39.19	26320211
57	Glutarylation	IYIDKNTKIICQGFT EEECCCCEEEECCCC	39.19	24703693
57	Ubiquitination	IYIDKNTKIICQGFT EEECCCCEEEECCCC	39.19	-
57	Acetylation	IYIDKNTKIICQGFT EEECCCCEEEECCCC	39.19	23576753
60	S-nitrosylation	DKNTKIICQGFTGKQ CCCCEEEECCCCCCC	3.54	24895380
60	S-nitrosocysteine	DKNTKIICQGFTGKQ CCCCEEEECCCCCCC	3.54	-
60	S-palmitoylation	DKNTKIICQGFTGKQ CCCCEEEECCCCCCC	3.54	28526873
60	Glutathionylation	DKNTKIICQGFTGKQ CCCCEEEECCCCCCC	3.54	24333276
66	Ubiquitination	ICQGFTGKQGTFHSQ EECCCCCCCCEECHH	42.36	-
66	Acetylation	ICQGFTGKQGTFHSQ EECCCCCCCCEECHH	42.36	23576753
66	Malonylation	ICQGFTGKQGTFHSQ EECCCCCCCCEECHH	42.36	26320211
66	Glutarylation	ICQGFTGKQGTFHSQ EECCCCCCCCEECHH	42.36	24703693
66	Succinylation	ICQGFTGKQGTFHSQ EECCCCCCCCEECHH	42.36	23806337
66	Succinylation	ICQGFTGKQGTFHSQ EECCCCCCCCEECHH	42.36	-
80	Phosphorylation	QQALEYGTKLVGGTT HHHHHHCCEEECCCC	21.94	24719451
81	Acetylation	QALEYGTKLVGGTTP HHHHHCCEEECCCCC	36.49	23576753
81	Succinylation	QALEYGTKLVGGTTP HHHHHCCEEECCCCC	36.49	24315375
87	Phosphorylation	TKLVGGTTPGKGGQK CEEECCCCCCCCCCC	33.06	25338131
90	Acetylation	VGGTTPGKGGQKHLG ECCCCCCCCCCCCCC	62.16	2395363
90	Ubiquitination	VGGTTPGKGGQKHLG ECCCCCCCCCCCCCC	62.16	27667366
90	Succinylation	VGGTTPGKGGQKHLG ECCCCCCCCCCCCCC	62.16	26388266
94	Succinylation	TPGKGGQKHLGLPVF CCCCCCCCCCCCCCC	44.03	-
94	Malonylation	TPGKGGQKHLGLPVF CCCCCCCCCCCCCCC	44.03	26320211
94	Acetylation	TPGKGGQKHLGLPVF CCCCCCCCCCCCCCC	44.03	23576753
94	Ubiquitination	TPGKGGQKHLGLPVF CCCCCCCCCCCCCCC	44.03	-
105	Acetylation	LPVFNTVKEAKEKTG CCCCCCHHHHHHHHC	50.33	23576753
105	Succinylation	LPVFNTVKEAKEKTG CCCCCCHHHHHHHHC	50.33	26388266
164	Phosphorylation	HRLTRQGTTRLIGPN EEHHHCCCEEEECCC	10.62	23984901
165	Phosphorylation	RLTRQGTTRLIGPNC EHHHCCCEEEECCCC	30.24	23984901
172	S-palmitoylation	TRLIGPNCPGVINPG EEEECCCCCCCCCCC	3.32	28526873
172	S-nitrosylation	TRLIGPNCPGVINPG EEEECCCCCCCCCCC	3.32	24895380
172	Glutathionylation	TRLIGPNCPGVINPG EEEECCCCCCCCCCC	3.32	24333276
181	S-nitrosylation	GVINPGECKIGIMPG CCCCCCCCCEEEECC	4.89	24895380
181	S-palmitoylation	GVINPGECKIGIMPG CCCCCCCCCEEEECC	4.89	28526873
192	Acetylation	IMPGHIHKKGRIGIV EECCCCCCCCCEEEE	57.21	23864654
193	Acetylation	MPGHIHKKGRIGIVS ECCCCCCCCCEEEEE	38.98	2395381
280	Ubiquitination	HNSGPKAKPVVSFIA CCCCCCCCCCEEEEE	44.46	17451654
308	Ubiquitination	GAIIAGGKGGAKEKI CEEEECCCCCHHHHH	53.94	27667366
308	Acetylation	GAIIAGGKGGAKEKI CEEEECCCCCHHHHH	53.94	2384513
312	Acetylation	AGGKGGAKEKISALQ ECCCCCHHHHHHHHH	63.92	2384521
314	Acetylation	GKGGAKEKISALQSA CCCCHHHHHHHHHHC	41.05	6269795
338	Acetylation	QLGTTIYKEFEKRKM HHCCHHHHHHHHHHC	52.67	23806337
338	Succinylation	QLGTTIYKEFEKRKM HHCCHHHHHHHHHHC	52.67	23806337
338	Succinylation	QLGTTIYKEFEKRKM HHCCHHHHHHHHHHC	52.67	-
342	Succinylation	TIYKEFEKRKML--- HHHHHHHHHHCC---	63.74	26388266
342	Acetylation	TIYKEFEKRKML--- HHHHHHHHHHCC---	63.74	2384529

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SUCA_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 SUCA_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of SUCA_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Ubiquitylation

"A proteomics approach to identify the ubiquitinated proteins in mouseheart.";
Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K.,Choi H.W., Park Z.-Y., Yoo Y.J.;
Biochem. Biophys. Res. Commun. 357:731-736(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-280, AND MASSSPECTROMETRY.
PubMed: 17451654