SUCA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SUCA_HUMAN
• UniProt AC: P53597
• 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: Homo sapiens (Human).
• 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: MTATLAAAADIATMVSGSSGLAAARLLSRSFLLPQNGIRHCSYTASRQHLYVDKNTKIICQGFTGKQGTFHSQQALEYGTKLVGGTTPGKGGQTHLGLPVFNTVKEAKEQTGATASVIYVPPPFAAAAINEAIEAEIPLVVCITEGIPQQDMVRVKHKLLRQEKTRLIGPNCPGVINPGECKIGIMPGHIHKKGRIGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFIDCLEIFLNDSATEGIILIGEIGGNAEENAAEFLKQHNSGPNSKPVVSFIAGLTAPPGRRMGHAGAIIAGGKGGAKEKISALQSAGVVVSMSPAQLGTTIYKEFEKRKML

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	------MTATLAAAA ------CCHHHHHHH	28.48	23663014
4	Phosphorylation	----MTATLAAAADI ----CCHHHHHHHHH	14.04	23663014
13	Phosphorylation	AAAADIATMVSGSSG HHHHHHHHHHCCCHH	20.59	23663014
16	Phosphorylation	ADIATMVSGSSGLAA HHHHHHHCCCHHHHH	23.33	23663014
18	Phosphorylation	IATMVSGSSGLAAAR HHHHHCCCHHHHHHH	17.46	23663014
19	Phosphorylation	ATMVSGSSGLAAARL HHHHCCCHHHHHHHH	41.15	23663014
28	Phosphorylation	LAAARLLSRSFLLPQ HHHHHHHHHHHCCCC	30.39	24275569
54	Ubiquitination	RQHLYVDKNTKIICQ CCEEEECCCCEEEEC	57.37	19608861
54	2-Hydroxyisobutyrylation	RQHLYVDKNTKIICQ CCEEEECCCCEEEEC	57.37	-
54	Acetylation	RQHLYVDKNTKIICQ CCEEEECCCCEEEEC	57.37	19608861
54	Succinylation	RQHLYVDKNTKIICQ CCEEEECCCCEEEEC	57.37	23954790
57	Succinylation	LYVDKNTKIICQGFT EEECCCCEEEECCCC	39.19	-
57	Acetylation	LYVDKNTKIICQGFT EEECCCCEEEECCCC	39.19	25953088
57	Succinylation	LYVDKNTKIICQGFT EEECCCCEEEECCCC	39.19	-
57	2-Hydroxyisobutyrylation	LYVDKNTKIICQGFT EEECCCCEEEECCCC	39.19	-
57	Malonylation	LYVDKNTKIICQGFT EEECCCCEEEECCCC	39.19	26320211
57	Ubiquitination	LYVDKNTKIICQGFT EEECCCCEEEECCCC	39.19	29967540
66	Succinylation	ICQGFTGKQGTFHSQ EECCCCCCCCEECHH	42.36	-
66	Ubiquitination	ICQGFTGKQGTFHSQ EECCCCCCCCEECHH	42.36	22817900
66	Acetylation	ICQGFTGKQGTFHSQ EECCCCCCCCEECHH	42.36	25953088
66	Malonylation	ICQGFTGKQGTFHSQ EECCCCCCCCEECHH	42.36	26320211
66	Succinylation	ICQGFTGKQGTFHSQ EECCCCCCCCEECHH	42.36	-
69	Phosphorylation	GFTGKQGTFHSQQAL CCCCCCCEECHHHHH	18.71	27080861
72	Phosphorylation	GKQGTFHSQQALEYG CCCCEECHHHHHHHC	21.57	27080861
80	Phosphorylation	QQALEYGTKLVGGTT HHHHHHCCEEECCCC	21.94	27080861
81	Ubiquitination	QALEYGTKLVGGTTP HHHHHCCEEECCCCC	36.49	29967540
81	Acetylation	QALEYGTKLVGGTTP HHHHHCCEEECCCCC	36.49	25953088
86	Phosphorylation	GTKLVGGTTPGKGGQ CCEEECCCCCCCCCC	24.72	28152594
87	Phosphorylation	TKLVGGTTPGKGGQT CEEECCCCCCCCCCC	33.06	28152594
90	Ubiquitination	VGGTTPGKGGQTHLG ECCCCCCCCCCCCCC	62.16	29967540
90	Malonylation	VGGTTPGKGGQTHLG ECCCCCCCCCCCCCC	62.16	26320211
94	Phosphorylation	TPGKGGQTHLGLPVF CCCCCCCCCCCCEEC	23.49	28152594
105	2-Hydroxyisobutyrylation	LPVFNTVKEAKEQTG CEECCCHHHHHHHHC	50.33	-
105	Acetylation	LPVFNTVKEAKEQTG CEECCCHHHHHHHHC	50.33	25038526
105	Ubiquitination	LPVFNTVKEAKEQTG CEECCCHHHHHHHHC	50.33	23503661
108	Ubiquitination	FNTVKEAKEQTGATA CCCHHHHHHHHCCCE	51.99	23503661
182	Ubiquitination	VINPGECKIGIMPGH CCCCCCCCEEEECCC	39.40	29967540
192	Ubiquitination	IMPGHIHKKGRIGIV EECCCCCCCCCEEEE	57.21	29967540
192	Acetylation	IMPGHIHKKGRIGIV EECCCCCCCCCEEEE	57.21	2380203
308	Ubiquitination	GAIIAGGKGGAKEKI CEEEECCCCCHHHHH	53.94	23503661
308	Acetylation	GAIIAGGKGGAKEKI CEEEECCCCCHHHHH	53.94	2401561
312	Ubiquitination	AGGKGGAKEKISALQ ECCCCCHHHHHHHHH	63.92	23503661
312	Acetylation	AGGKGGAKEKISALQ ECCCCCHHHHHHHHH	63.92	2401563
314	Ubiquitination	GKGGAKEKISALQSA CCCCHHHHHHHHHHC	41.05	23503661
316	O-linked_Glycosylation	GGAKEKISALQSAGV CCHHHHHHHHHHCCE	33.71	28510447
320	Phosphorylation	EKISALQSAGVVVSM HHHHHHHHCCEEEEC	28.04	-
335	Phosphorylation	SPAQLGTTIYKEFEK CHHHHCCHHHHHHHH	22.10	22210691
337	Phosphorylation	AQLGTTIYKEFEKRK HHHCCHHHHHHHHHH	11.45	22210691
338	Succinylation	QLGTTIYKEFEKRKM HHCCHHHHHHHHHHC	52.67	-
338	Succinylation	QLGTTIYKEFEKRKM HHCCHHHHHHHHHHC	52.67	-
338	Acetylation	QLGTTIYKEFEKRKM HHCCHHHHHHHHHHC	52.67	25038526

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

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

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SUCB2_HUMAN	SUCLG2	physical	22939629
SUCB1_HUMAN	SUCLA2	physical	22939629
ODO1_HUMAN	OGDH	physical	26344197
SDHB_HUMAN	SDHB	physical	26344197
SUCB1_HUMAN	SUCLA2	physical	26344197
SUCB1_HUMAN	SUCLA2	physical	28514442
SYAM_HUMAN	AARS2	physical	28514442
RPC3_HUMAN	POLR3C	physical	28514442
SYLM_HUMAN	LARS2	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 245400: Mitochondrial DNA depletion syndrome 9 (MTDPS9)
• 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-54, AND MASS SPECTROMETRY.
PubMed: 19608861