SUCB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SUCB1_HUMAN
• UniProt AC: Q9P2R7
• 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: Homo sapiens (Human).
• 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. [PubMed: 15877282 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 (By similarity]
• Protein Sequence: MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMSMELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVKIVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENMVKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDERDKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI

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
4	Phosphorylation	----MAASMFYGRLV ----CCCHHHHHHHH	10.41	20068231
7	Phosphorylation	-MAASMFYGRLVAVA -CCCHHHHHHHHHHH	7.84	27642862
56 (in isoform 2)	Ubiquitination	-	22.29	21890473
70	Phosphorylation	LLQEAGVSVPKGYVA HHHHHCCCCCCCCCC	31.61	-
75	Phosphorylation	GVSVPKGYVAKSPDE CCCCCCCCCCCCHHH	11.89	-
78	Ubiquitination	VPKGYVAKSPDEAYA CCCCCCCCCHHHHHH	53.10	21890473
78	Acetylation	VPKGYVAKSPDEAYA CCCCCCCCCHHHHHH	53.10	19608861
78	Malonylation	VPKGYVAKSPDEAYA CCCCCCCCCHHHHHH	53.10	26320211
78 (in isoform 1)	Ubiquitination	-	53.10	21890473
79	Phosphorylation	PKGYVAKSPDEAYAI CCCCCCCCHHHHHHH	28.04	26657352
84	Phosphorylation	AKSPDEAYAIAKKLG CCCHHHHHHHHHHHC	9.11	28152594
88	2-Hydroxyisobutyrylation	DEAYAIAKKLGSKDV HHHHHHHHHHCCCCE	42.28	-
88	Ubiquitination	DEAYAIAKKLGSKDV HHHHHHHHHHCCCCE	42.28	-
88	Succinylation	DEAYAIAKKLGSKDV HHHHHHHHHHCCCCE	42.28	27452117
88	Succinylation	DEAYAIAKKLGSKDV HHHHHHHHHHCCCCE	42.28	-
88	Malonylation	DEAYAIAKKLGSKDV HHHHHHHHHHCCCCE	42.28	26320211
88	Acetylation	DEAYAIAKKLGSKDV HHHHHHHHHHCCCCE	42.28	23749302
89	Ubiquitination	EAYAIAKKLGSKDVV HHHHHHHHHCCCCEE	49.40	-
89	Acetylation	EAYAIAKKLGSKDVV HHHHHHHHHCCCCEE	49.40	2401879
93	Ubiquitination	IAKKLGSKDVVIKAQ HHHHHCCCCEEEEEE	53.39	-
93	Malonylation	IAKKLGSKDVVIKAQ HHHHHCCCCEEEEEE	53.39	26320211
106	Methylation	AQVLAGGRGKGTFES EEEECCCCCCCCHHC	42.61	54559111
108	Ubiquitination	VLAGGRGKGTFESGL EECCCCCCCCHHCCC	54.11	-
108	Malonylation	VLAGGRGKGTFESGL EECCCCCCCCHHCCC	54.11	26320211
108	Acetylation	VLAGGRGKGTFESGL EECCCCCCCCHHCCC	54.11	2402293
116	Malonylation	GTFESGLKGGVKIVF CCHHCCCCCCEEEEE	58.08	26320211
116	Ubiquitination	GTFESGLKGGVKIVF CCHHCCCCCCEEEEE	58.08	-
116	Acetylation	GTFESGLKGGVKIVF CCHHCCCCCCEEEEE	58.08	2402295
120	Ubiquitination	SGLKGGVKIVFSPEE CCCCCCEEEEECHHH	36.11	-
124	Phosphorylation	GGVKIVFSPEEAKAV CCEEEEECHHHHHHH	22.10	21815630
129	Ubiquitination	VFSPEEAKAVSSQMI EECHHHHHHHHHHHH	53.23	-
129	Acetylation	VFSPEEAKAVSSQMI EECHHHHHHHHHHHH	53.23	25038526
132	Phosphorylation	PEEAKAVSSQMIGKK HHHHHHHHHHHHCCC	21.51	-
138	Ubiquitination	VSSQMIGKKLFTKQT HHHHHHCCCCCCCCC	35.06	-
138	Acetylation	VSSQMIGKKLFTKQT HHHHHHCCCCCCCCC	35.06	25953088
138	2-Hydroxyisobutyrylation	VSSQMIGKKLFTKQT HHHHHHCCCCCCCCC	35.06	-
139	Acetylation	SSQMIGKKLFTKQTG HHHHHCCCCCCCCCC	43.55	-
143	2-Hydroxyisobutyrylation	IGKKLFTKQTGEKGR HCCCCCCCCCCCCCC	38.23	-
143	Ubiquitination	IGKKLFTKQTGEKGR HCCCCCCCCCCCCCC	38.23	19608861
143	Malonylation	IGKKLFTKQTGEKGR HCCCCCCCCCCCCCC	38.23	26320211
143	Acetylation	IGKKLFTKQTGEKGR HCCCCCCCCCCCCCC	38.23	19608861
167	Phosphorylation	RKYPRREYYFAITME CCCCCCEEEEEEEEE	11.32	22210691
168	Phosphorylation	KYPRREYYFAITMER CCCCCEEEEEEEEEE	5.04	20068231
172	Phosphorylation	REYYFAITMERSFQG CEEEEEEEEEECCCC	15.00	20068231
186	Phosphorylation	GPVLIGSSHGGVNIE CCEEEECCCCCCCHH	22.42	22210691
215	2-Hydroxyisobutyrylation	IDIEEGIKKEQALQL CCHHHCCCHHHHHHH	62.20	-
216	Malonylation	DIEEGIKKEQALQLA CHHHCCCHHHHHHHH	53.81	26320211
216	Ubiquitination	DIEEGIKKEQALQLA CHHHCCCHHHHHHHH	53.81	-
216	2-Hydroxyisobutyrylation	DIEEGIKKEQALQLA CHHHCCCHHHHHHHH	53.81	-
216	Acetylation	DIEEGIKKEQALQLA CHHHCCCHHHHHHHH	53.81	-
235	Phosphorylation	FPPNIVESAAENMVK CCHHHHHHHHHHHHH	23.14	-
244	Phosphorylation	AENMVKLYSLFLKYD HHHHHHHHHHHHHCC	9.52	28152594
279	Phosphorylation	DAKINFDSNSAYRQK EEEECCCCCHHHHHH	28.66	23401153
281	Phosphorylation	KINFDSNSAYRQKKI EECCCCCHHHHHHCE	30.54	30108239
283	Phosphorylation	NFDSNSAYRQKKIFD CCCCCHHHHHHCEEC	17.25	27251275
287	Ubiquitination	NSAYRQKKIFDLQDW CHHHHHHCEECHHHH	40.02	-
295	Phosphorylation	IFDLQDWTQEDERDK EECHHHHCCCCHHHH	30.30	-
302	Acetylation	TQEDERDKDAAKANL CCCCHHHHHHHHHCC	56.33	25953088
341	Phosphorylation	IIKLHGGTPANFLDV HHHHCCCCCCCEEEC	24.66	-
368	Acetylation	FKLITSDKKVLAILV HHHHCCCHHHHHHHH	44.54	25953088
395 (in isoform 2)	Ubiquitination	-	2.40	21890473
417	Ubiquitination	GTRVDDAKALIADSG CCCCCCHHHHHCCCC	51.20	21890473
417 (in isoform 1)	Ubiquitination	-	51.20	21890473
417	2-Hydroxyisobutyrylation	GTRVDDAKALIADSG CCCCCCHHHHHCCCC	51.20	-
426	2-Hydroxyisobutyrylation	LIADSGLKILACDDL HHCCCCCEEEEECCH	38.92	-
430	Glutathionylation	SGLKILACDDLDEAA CCCEEEEECCHHHHH	3.61	22555962
444	Phosphorylation	ARMVVKLSEIVTLAK HHHHHHHHHHHHHHH	21.40	20068231
448	Phosphorylation	VKLSEIVTLAKQAHV HHHHHHHHHHHHCCC	27.02	20068231

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

Oops, there are no upstream regulatory protein records of SUCB1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SUCB1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SUCB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AR6P1_HUMAN	ARL6IP1	physical	25416956
ATRAP_HUMAN	AGTRAP	physical	25416956
CKLF5_HUMAN	CMTM5	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
ODO2_HUMAN	DLST	physical	26344197
RAB2A_HUMAN	RAB2A	physical	26344197
SSRD_HUMAN	SSR4	physical	26344197
MAP2_HUMAN	METAP2	physical	28514442
RAD21_HUMAN	RAD21	physical	28514442
DNLZ_HUMAN	DNLZ	physical	28514442
IF2M_HUMAN	MTIF2	physical	28514442
CQ080_HUMAN	C17orf80	physical	28514442
ZMY19_HUMAN	ZMYND19	physical	28514442
IQGA2_HUMAN	IQGAP2	physical	28514442
GTPBA_HUMAN	GTPBP10	physical	28514442
MKLN1_HUMAN	MKLN1	physical	28514442
SYHM_HUMAN	HARS2	physical	28514442
MCCA_HUMAN	MCCC1	physical	28514442
OZF_HUMAN	ZNF146	physical	28514442
LONP2_HUMAN	LONP2	physical	28514442
EFGM_HUMAN	GFM1	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 612073: Mitochondrial DNA depletion syndrome 5 (MTDPS5)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00139: Succinic acid

Related Literatures of Post-Translational Modification

Acetylation

"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-78 AND LYS-143, AND MASSSPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-84, AND MASSSPECTROMETRY.
PubMed: 15592455