dbPTM

SUCB1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SUCB1_MOUSE
UniProt AC	Q9Z2I9
Protein Name	Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial {ECO:0000255\|HAMAP-Rule:MF_03220}
Gene Name	Sucla2 {ECO:0000255\|HAMAP-Rule:MF_03220}
Organism	Mus musculus (Mouse).
Sequence Length	463
Subcellular Localization	Mitochondrion .
Protein Description	ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP 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	MAASMFYGRQLAAAALRSHRPQTTLRAAAQVLGNSGLFNKHGLQVQQQQQRTLSLHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFTSGLKGGVKIVFSPEEAKAVSSQMIGQKLITKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKEPIDIVEGIKKEQAVTLAQKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEDSDGKVLCMDAKINFDSNSAYRQKKIFDLQDWSQEDERDKEAANADINYIGLDGSIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVQQVTEAFKLITSDKKVQAILVNIFGGIMRCDVIAQGIVMAVKDLEIRIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAAKMVVKLSEIVTLAKEAHVDVKFQLPI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
78	Malonylation	VPKGFVAKSSDEAYA CCCCEEECCCHHHHH	45.23	26320211
78	Acetylation	VPKGFVAKSSDEAYA CCCCEEECCCHHHHH	45.23	23576753
78	Succinylation	VPKGFVAKSSDEAYA CCCCEEECCCHHHHH	45.23	26388266
78	Ubiquitination	VPKGFVAKSSDEAYA CCCCEEECCCHHHHH	45.23	-
80	Phosphorylation	KGFVAKSSDEAYAIA CCEEECCCHHHHHHH	38.47	26525534
84	Phosphorylation	AKSSDEAYAIAKKLG ECCCHHHHHHHHHHC	9.11	-
88	Malonylation	DEAYAIAKKLGSKDV HHHHHHHHHHCCCCE	42.28	26320211
88	Succinylation	DEAYAIAKKLGSKDV HHHHHHHHHHCCCCE	42.28	-
88	Ubiquitination	DEAYAIAKKLGSKDV HHHHHHHHHHCCCCE	42.28	27667366
88	Succinylation	DEAYAIAKKLGSKDV HHHHHHHHHHCCCCE	42.28	23806337
88	Acetylation	DEAYAIAKKLGSKDV HHHHHHHHHHCCCCE	42.28	23576753
89	Acetylation	EAYAIAKKLGSKDVV HHHHHHHHHCCCCEE	49.40	23954790
93	Malonylation	IAKKLGSKDVVIKAQ HHHHHCCCCEEEEEE	53.39	26320211
93	Acetylation	IAKKLGSKDVVIKAQ HHHHHCCCCEEEEEE	53.39	23806337
93	Succinylation	IAKKLGSKDVVIKAQ HHHHHCCCCEEEEEE	53.39	23806337
98	Acetylation	GSKDVVIKAQVLAGG CCCCEEEEEEEECCC	22.58	6269771
108	Malonylation	VLAGGRGKGTFTSGL EECCCCCCCCCCCCC	54.11	26320211
108	Succinylation	VLAGGRGKGTFTSGL EECCCCCCCCCCCCC	54.11	23806337
108	Acetylation	VLAGGRGKGTFTSGL EECCCCCCCCCCCCC	54.11	23806337
116	Ubiquitination	GTFTSGLKGGVKIVF CCCCCCCCCCEEEEE	58.08	27667366
116	Succinylation	GTFTSGLKGGVKIVF CCCCCCCCCCEEEEE	58.08	24315375
116	Acetylation	GTFTSGLKGGVKIVF CCCCCCCCCCEEEEE	58.08	2395537
116	Malonylation	GTFTSGLKGGVKIVF CCCCCCCCCCEEEEE	58.08	26320211
120	Acetylation	SGLKGGVKIVFSPEE CCCCCCEEEEECHHH	36.11	23864654
125	Ubiquitination	GVKIVFSPEEAKAVS CEEEEECHHHHHHHH	31.79	27667366
129	Acetylation	VFSPEEAKAVSSQMI EECHHHHHHHHHHHH	53.23	23576753
129	Succinylation	VFSPEEAKAVSSQMI EECHHHHHHHHHHHH	53.23	26388266
133	Phosphorylation	EEAKAVSSQMIGQKL HHHHHHHHHHHCCEE	19.71	-
139	Ubiquitination	SSQMIGQKLITKQTG HHHHHCCEECCCCCC	36.32	27667366
139	Acetylation	SSQMIGQKLITKQTG HHHHHCCEECCCCCC	36.32	23576753
139	Succinylation	SSQMIGQKLITKQTG HHHHHCCEECCCCCC	36.32	24315375
143	Succinylation	IGQKLITKQTGEKGR HCCEECCCCCCCCCC	38.58	24315375
143	Malonylation	IGQKLITKQTGEKGR HCCEECCCCCCCCCC	38.58	26320211
143	Acetylation	IGQKLITKQTGEKGR HCCEECCCCCCCCCC	38.58	23576753
145	Phosphorylation	QKLITKQTGEKGRIC CEECCCCCCCCCCCC	49.19	20495213
148	Acetylation	ITKQTGEKGRICNQV CCCCCCCCCCCCCEE	55.63	2395561
148	Succinylation	ITKQTGEKGRICNQV CCCCCCCCCCCCCEE	55.63	26388266
152	S-palmitoylation	TGEKGRICNQVLVCE CCCCCCCCCEEEEEE	2.54	28526873
152	S-nitrosylation	TGEKGRICNQVLVCE CCCCCCCCCEEEEEE	2.54	24895380
153	Ubiquitination	GEKGRICNQVLVCER CCCCCCCCEEEEEEC	32.40	27667366
158	S-palmitoylation	ICNQVLVCERKYPRR CCCEEEEEECCCCCC	3.51	28526873
158	S-nitrosylation	ICNQVLVCERKYPRR CCCEEEEEECCCCCC	3.51	24895380
176	Phosphorylation	FAITMERSFQGPVLI EEEEECCCCCCCEEE	14.49	23140645
176	Ubiquitination	FAITMERSFQGPVLI EEEEECCCCCCCEEE	14.49	27667366
205	Succinylation	ENPEAIVKEPIDIVE CCHHHHHCCCCCHHC	52.22	26388266
215	Succinylation	IDIVEGIKKEQAVTL CCHHCCCCHHHHHHH	62.20	26388266
215	Acetylation	IDIVEGIKKEQAVTL CCHHCCCCHHHHHHH	62.20	23954790
216	Succinylation	DIVEGIKKEQAVTLA CHHCCCCHHHHHHHH	53.81	26388266
216	Acetylation	DIVEGIKKEQAVTLA CHHCCCCHHHHHHHH	53.81	23576753
225	Succinylation	QAVTLAQKMGFPSNI HHHHHHHHHCCCHHH	35.07	23954790
225	Acetylation	QAVTLAQKMGFPSNI HHHHHHHHHCCCHHH	35.07	23954790
249	Acetylation	KLYNLFLKYDATMVE HHHHHHHHCCCEEEE	33.48	23954790
264	Phosphorylation	INPMVEDSDGKVLCM ECCCCCCCCCCEEEE	34.45	26525534
267	Acetylation	MVEDSDGKVLCMDAK CCCCCCCCEEEEEEE	36.70	23864654
270	S-nitrosylation	DSDGKVLCMDAKINF CCCCCEEEEEEEECC	2.31	21278135
270	S-nitrosocysteine	DSDGKVLCMDAKINF CCCCCEEEEEEEECC	2.31	-
279	Phosphorylation	DAKINFDSNSAYRQK EEEECCCCCHHHHHH	28.66	27742792
281	Phosphorylation	KINFDSNSAYRQKKI EECCCCCHHHHHHCE	30.54	27742792
283	Phosphorylation	NFDSNSAYRQKKIFD CCCCCHHHHHHCEEC	17.25	28833060
286	Acetylation	SNSAYRQKKIFDLQD CCHHHHHHCEECCCC	38.55	6269769
295	Phosphorylation	IFDLQDWSQEDERDK EECCCCCCHHHHHHH	31.79	26525534
341	Phosphorylation	IIKLHGGTPANFLDV HHHHCCCCCCCEEEC	24.66	22817900
362	Acetylation	QQVTEAFKLITSDKK HHHHHHHHHHCCCCC	46.13	23954790
368	Acetylation	FKLITSDKKVQAILV HHHHCCCCCHHHHEE	55.39	23576753
384	S-nitrosylation	IFGGIMRCDVIAQGI CCCHHHHHHHHHHCC	2.44	21278135
384	S-nitrosocysteine	IFGGIMRCDVIAQGI CCCHHHHHHHHHHCC	2.44	-
417	Acetylation	GTRVDDAKALIADSG CCCCCCHHHHHCCCC	51.20	23864654
417	Ubiquitination	GTRVDDAKALIADSG CCCCCCHHHHHCCCC	51.20	-
426	Acetylation	LIADSGLKILACDDL HHCCCCCEEEEECCH	38.92	23864654
430	S-palmitoylation	SGLKILACDDLDEAA CCCEEEEECCHHHHH	3.61	28526873
430	S-nitrosylation	SGLKILACDDLDEAA CCCEEEEECCHHHHH	3.61	24895380
430	Glutathionylation	SGLKILACDDLDEAA CCCEEEEECCHHHHH	3.61	24333276
430	S-nitrosocysteine	SGLKILACDDLDEAA CCCEEEEECCHHHHH	3.61	-
438	Acetylation	DDLDEAAKMVVKLSE CCHHHHHHHHHHHHH	39.00	23576753
451	Acetylation	SEIVTLAKEAHVDVK HHHHHHHHHCCCCEE	59.55	23201123

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 SUCB1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SUCB1_MOUSE !!

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 SUCB1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SUCB1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of SUCB1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND MASSSPECTROMETRY.	17114649 [Abstract]