AT5G2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AT5G2_HUMAN
• UniProt AC: Q06055
• Protein Name: ATP synthase F(0) complex subunit C2, mitochondrial {ECO:0000305}
• Gene Name: ATP5MC2 {ECO:0000312|HGNC:HGNC:842}
• Organism: Homo sapiens (Human).
• Sequence Length: 141
• Subcellular Localization: Mitochondrion membrane; Multi-pass membrane protein.
• Protein Description: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element..
• Protein Sequence: MFACSKFVSTPSLVKSTSQLLSRPLSAVVLKRPEILTDESLSSLAVSCPLTSLVSSRSFQTSAISRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM

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
10 (in isoform 3)	Phosphorylation	-	16.17	-
11 (in isoform 2)	Phosphorylation	-	20.40	-
13 (in isoform 2)	Phosphorylation	-	6.23	-
31	Ubiquitination	PLSAVVLKRPEILTD CCHHHHHCCCCCCCC	55.06	21963094
47	Ubiquitination	SLSSLAVSCPLTSLV CHHHHHHHCCHHHHH	12.38	21963094
55	Phosphorylation	CPLTSLVSSRSFQTS CCHHHHHCCCCCCCC	25.90	24719451
70	Phosphorylation	AISRDIDTAAKFIGA CCCCCHHHHHHHHCC	28.93	26437602
72	Ubiquitination	SRDIDTAAKFIGAGA CCCHHHHHHHHCCCC	14.91	-
81	Phosphorylation	FIGAGAATVGVAGSG HHCCCCCEEECCCCC	19.77	28787133
87	Phosphorylation	ATVGVAGSGAGIGTV CEEECCCCCCCHHHH	18.74	28787133
88	Ubiquitination	TVGVAGSGAGIGTVF EEECCCCCCCHHHHH	27.23	21963094
93	Phosphorylation	GSGAGIGTVFGSLII CCCCCHHHHHHHHHH	15.67	23612710
97	Phosphorylation	GIGTVFGSLIIGYAR CHHHHHHHHHHHHCC	12.63	28787133
107	Phosphorylation	IGYARNPSLKQQLFS HHHCCCHHHHHHHHH	52.31	23612710
109	Methylation	YARNPSLKQQLFSYA HCCCHHHHHHHHHHH	40.09	30530489

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

Oops, there are no upstream regulatory protein records of AT5G2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
109	K	Methylation	Trimethylated by ATPSCKMT at Lys-109.	30530489

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of AT5G2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TYDP2_HUMAN	TDP2	physical	21988832

Drug and Disease Associations

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