SUCB2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SUCB2_MOUSE
• UniProt AC: Q9Z2I8
• Protein Name: Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03221}
• Gene Name: Suclg2 {ECO:0000255|HAMAP-Rule:MF_03221}
• Organism: Mus musculus (Mouse).
• Sequence Length: 433
• Subcellular Localization: Mitochondrion .
• Protein Description: GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit..
• Protein Sequence: MASPVAIAAQAGKLLRERALRPLLAVRSQAGHLTPRRWLNLQEYQSKKLMSEHGVRVQRFFVANTAKEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPKVVGELAQQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSHNGPVIVGSPQGGVDIEEVAASSPELIFKEQIDIFEGIKDSQAQRMAENLGFLGSLKNQAADQITKLYHLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAARYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYEAFKLLTSDPKVEAILVNIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQNILKSSGLPITSAVDLEDAAKKAVASVAKK

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
45	Ubiquitination	WLNLQEYQSKKLMSE CCCHHHHHHHHHHHH	48.28	27667366
67	Acetylation	FFVANTAKEALEAAK EEECHHHHHHHHHHH	41.29	23576753
67	Ubiquitination	FFVANTAKEALEAAK EEECHHHHHHHHHHH	41.29	-
67	Succinylation	FFVANTAKEALEAAK EEECHHHHHHHHHHH	41.29	23806337
67	Succinylation	FFVANTAKEALEAAK EEECHHHHHHHHHHH	41.29	-
67	Malonylation	FFVANTAKEALEAAK EEECHHHHHHHHHHH	41.29	26320211
67	Glutarylation	FFVANTAKEALEAAK EEECHHHHHHHHHHH	41.29	24703693
74	Succinylation	KEALEAAKRLNAKEI HHHHHHHHHCCHHHH	65.55	26388266
74	Glutarylation	KEALEAAKRLNAKEI HHHHHHHHHCCHHHH	65.55	24703693
74	Acetylation	KEALEAAKRLNAKEI HHHHHHHHHCCHHHH	65.55	23576753
79	Succinylation	AAKRLNAKEIVLKAQ HHHHCCHHHHHHHHH	47.07	-
79	Succinylation	AAKRLNAKEIVLKAQ HHHHCCHHHHHHHHH	47.07	23806337
79	Acetylation	AAKRLNAKEIVLKAQ HHHHCCHHHHHHHHH	47.07	23806337
84	Acetylation	NAKEIVLKAQILAGG CHHHHHHHHHHHHCC	27.61	23576753
94	Succinylation	ILAGGRGKGVFNSGL HHHCCCCCCCCCCCC	51.01	-
94	Ubiquitination	ILAGGRGKGVFNSGL HHHCCCCCCCCCCCC	51.01	27667366
94	Acetylation	ILAGGRGKGVFNSGL HHHCCCCCCCCCCCC	51.01	23806337
94	Malonylation	ILAGGRGKGVFNSGL HHHCCCCCCCCCCCC	51.01	26320211
102	Acetylation	GVFNSGLKGGVHLTK CCCCCCCCCCEECCC	58.08	7622873
102	Malonylation	GVFNSGLKGGVHLTK CCCCCCCCCCEECCC	58.08	26320211
102	Ubiquitination	GVFNSGLKGGVHLTK CCCCCCCCCCEECCC	58.08	-
109	Acetylation	KGGVHLTKDPKVVGE CCCEECCCCHHHHHH	77.66	23864654
112	Succinylation	VHLTKDPKVVGELAQ EECCCCHHHHHHHHH	60.74	24315375
112	Acetylation	VHLTKDPKVVGELAQ EECCCCHHHHHHHHH	60.74	23576753
129	Ubiquitination	IGYNLATKQTPKEGV HCCCCCCCCCCCCCC	46.71	-
129	Malonylation	IGYNLATKQTPKEGV HCCCCCCCCCCCCCC	46.71	26320211
133	Acetylation	LATKQTPKEGVKVNK CCCCCCCCCCCCCCE	71.18	23576753
140	Succinylation	KEGVKVNKVMVAEAL CCCCCCCEEEEEEHH	34.39	24315375
140	Acetylation	KEGVKVNKVMVAEAL CCCCCCCEEEEEEHH	34.39	23576753
162	Phosphorylation	LAILMDRSHNGPVIV HHHHHCCCCCCCEEE	19.62	21743459
171	Phosphorylation	NGPVIVGSPQGGVDI CCCEEEECCCCCCCH	11.80	29472430
191	Acetylation	SSPELIFKEQIDIFE CCHHHHHHHHHHHHC	41.54	23954790
201	Succinylation	IDIFEGIKDSQAQRM HHHHCCCCHHHHHHH	63.28	23954790
201	Ubiquitination	IDIFEGIKDSQAQRM HHHHCCCCHHHHHHH	63.28	-
201	Acetylation	IDIFEGIKDSQAQRM HHHHCCCCHHHHHHH	63.28	23576753
203	Phosphorylation	IFEGIKDSQAQRMAE HHCCCCHHHHHHHHH	23.55	23140645
217	Phosphorylation	ENLGFLGSLKNQAAD HHHCHHHHHHHHHHH	38.01	22817900
219	Succinylation	LGFLGSLKNQAADQI HCHHHHHHHHHHHHH	49.03	23954790
219	Ubiquitination	LGFLGSLKNQAADQI HCHHHHHHHHHHHHH	49.03	-
219	Acetylation	LGFLGSLKNQAADQI HCHHHHHHHHHHHHH	49.03	23576753
228	Succinylation	QAADQITKLYHLFLK HHHHHHHHHHHHHHC	48.99	24315375
228	Acetylation	QAADQITKLYHLFLK HHHHHHHHHHHHHHC	48.99	23576753
256	S-nitrosocysteine	TPEGQVVCFDAKINF CCCCCEEEEECEECC	2.41	-
256	S-palmitoylation	TPEGQVVCFDAKINF CCCCCEEEEECEECC	2.41	28526873
256	S-nitrosylation	TPEGQVVCFDAKINF CCCCCEEEEECEECC	2.41	21278135
272	Acetylation	DNAEFRQKDIFAMDD CCHHHHHHCEEEECC	48.84	23576753
272	Succinylation	DNAEFRQKDIFAMDD CCHHHHHHCEEEECC	48.84	23954790
280	Acetylation	DIFAMDDKSENEPIE CEEEECCCCCCCCCC	56.24	23864654
281	Phosphorylation	IFAMDDKSENEPIEN EEEECCCCCCCCCCC	53.28	26525534
339	Succinylation	LDLGGGVKEAQVYEA EECCCCCHHHHHHHH	51.08	23806337
339	Acetylation	LDLGGGVKEAQVYEA EECCCCCHHHHHHHH	51.08	23806337
339	Succinylation	LDLGGGVKEAQVYEA EECCCCCHHHHHHHH	51.08	-
348	Acetylation	AQVYEAFKLLTSDPK HHHHHHHHHHCCCCC	50.03	23576753
387	Acetylation	ACRELELKVPLVVRL HHHHHCCCCCEEEEE	32.22	23576753
387	Ubiquitination	ACRELELKVPLVVRL HHHHHCCCCCEEEEE	32.22	22790023
407	Acetylation	QEAQNILKSSGLPIT HHHHHHHHHCCCCCC	38.49	23576753
414	Phosphorylation	KSSGLPITSAVDLED HHCCCCCCCCCCHHH	14.53	29472430
415	Phosphorylation	SSGLPITSAVDLEDA HCCCCCCCCCCHHHH	27.32	30352176
424	Succinylation	VDLEDAAKKAVASVA CCHHHHHHHHHHHHH	42.88	23954790
424	Acetylation	VDLEDAAKKAVASVA CCHHHHHHHHHHHHH	42.88	23576753
425	Acetylation	DLEDAAKKAVASVAK CHHHHHHHHHHHHHC	43.28	2391013
432	Acetylation	KAVASVAKK------ HHHHHHHCC------	57.78	23576753
433	Acetylation	AVASVAKK------- HHHHHHCC-------	56.70	6568585

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

Oops, there are no upstream regulatory protein records of SUCB2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SUCB2_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 SUCB2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of SUCB2_MOUSE !!

Drug and Disease Associations

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