AT5G1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AT5G1_HUMAN
• UniProt AC: P05496
• Protein Name: ATP synthase F(0) complex subunit C1, mitochondrial {ECO:0000305}
• Gene Name: ATP5MC1 {ECO:0000312|HGNC:HGNC:841}
• Organism: Homo sapiens (Human).
• Sequence Length: 136
• 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: MQTAGALFISPALIRCCTRGLIRPVSASFLNSPVNSSKQPSYSNFPLQVARREFQTSVVSRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM

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
32	Phosphorylation	VSASFLNSPVNSSKQ CCHHHHCCCCCCCCC	32.16	25627689
38	Ubiquitination	NSPVNSSKQPSYSNF CCCCCCCCCCCCCCC	67.08	-
41	Phosphorylation	VNSSKQPSYSNFPLQ CCCCCCCCCCCCCHH	38.40	24043423
42	Phosphorylation	NSSKQPSYSNFPLQV CCCCCCCCCCCCHHH	17.83	24043423
43	Phosphorylation	SSKQPSYSNFPLQVA CCCCCCCCCCCHHHH	36.01	24043423
43	O-linked_Glycosylation	SSKQPSYSNFPLQVA CCCCCCCCCCCHHHH	36.01	OGP
65	Phosphorylation	VVSRDIDTAAKFIGA HHCCCHHHHHHHHCC	28.93	26437602
76	Phosphorylation	FIGAGAATVGVAGSG HHCCCCCEEECCCCC	19.77	28787133
82	Phosphorylation	ATVGVAGSGAGIGTV CEEECCCCCCCHHHH	18.74	28787133
88	Phosphorylation	GSGAGIGTVFGSLII CCCCCHHHHHHHHHH	15.67	23612710
92	Phosphorylation	GIGTVFGSLIIGYAR CHHHHHHHHHHHHCC	12.63	28787133
102	Phosphorylation	IGYARNPSLKQQLFS HHHCCCHHHHHHHHH	52.31	23612710
104	Methylation	YARNPSLKQQLFSYA HCCCHHHHHHHHHHH	40.09	15010464

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

Oops, there are no upstream regulatory protein records of AT5G1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
104	K	Methylation	Trimethylated by ATPSCKMT at Lys-104.	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 AT5G1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRI69_HUMAN	TRIM69	physical	25416956

Drug and Disease Associations

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