AT5G3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AT5G3_HUMAN
• UniProt AC: P48201
• Protein Name: ATP synthase F(0) complex subunit C3, mitochondrial {ECO:0000305}
• Gene Name: ATP5MC3 {ECO:0000312|HGNC:HGNC:843}
• Organism: Homo sapiens (Human).
• Sequence Length: 142
• 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: MFACAKLACTPSLIRAGSRVAYRPISASVLSRPEASRTGEGSTVFNGAQNGVSQLIQREFQTSAISRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM

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
6	Ubiquitination	--MFACAKLACTPSL --CCCHHHHCCCHHH	36.18	22505724
22	Phosphorylation	RAGSRVAYRPISASV HCCCCEEECCCCHHH	17.67	-
26	Phosphorylation	RVAYRPISASVLSRP CEEECCCCHHHHCCC	19.71	23828894
28	Phosphorylation	AYRPISASVLSRPEA EECCCCHHHHCCCCH	19.46	23828894
31	Phosphorylation	PISASVLSRPEASRT CCCHHHHCCCCHHCC	43.57	23828894
36	Phosphorylation	VLSRPEASRTGEGST HHCCCCHHCCCCCCC	28.81	23828894
71	Phosphorylation	AISRDIDTAAKFIGA CHHCCHHHHHHHHCC	28.93	26437602
82	Phosphorylation	FIGAGAATVGVAGSG HHCCCCCEEECCCCC	19.77	28787133
88	Phosphorylation	ATVGVAGSGAGIGTV CEEECCCCCCCHHHH	18.74	28787133
94	Phosphorylation	GSGAGIGTVFGSLII CCCCCHHHHHHHHHH	15.67	23612710
98	Phosphorylation	GIGTVFGSLIIGYAR CHHHHHHHHHHHHCC	12.63	28787133
108	Phosphorylation	IGYARNPSLKQQLFS HHHCCCHHHHHHHHH	52.31	23612710
110	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 AT5G3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
110	K	Methylation	Trimethylated by ATPSCKMT at Lys-110.	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 AT5G3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
COKA1_HUMAN	COL20A1	physical	28514442
ATPB_HUMAN	ATP5B	physical	28514442
GHDC_HUMAN	GHDC	physical	28514442
ATPD_HUMAN	ATP5D	physical	28514442
GOGA4_HUMAN	GOLGA4	physical	28514442

Drug and Disease Associations

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