ATP5MC1 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_1902600Biological processproton transmembrane transport
GO_0015986Biological processproton motive force-driven ATP synthesis
GO_0005753Cellular componentmitochondrial proton-transporting ATP synthase complex
GO_0000276Cellular componentmitochondrial proton-transporting ATP synthase complex, coupling factor F(o)
GO_0005743Cellular componentmitochondrial inner membrane
GO_0005739Cellular componentmitochondrion
GO_0015078Molecular functionproton transmembrane transporter activity
GO_0005515Molecular functionprotein binding
GO_0008289Molecular functionlipid binding

IV. Literature review

[source]
Gene nameATP5MC1
Protein nameATP synthase F(0) complex subunit C1, mitochondrial (ATP synthase lipid-binding protein) (ATP synthase membrane subunit c locus 1) (ATP synthase proteolipid P1) (ATP synthase proton-transporting mitochondrial F(0) complex subunit C1) (ATPase protein 9) (ATPase subunit c)
ATP synthase membrane subunit c locus 1
ATP synthase lipid-binding protein (ATPase protein 9) (ATPase subunit c)
SynonymsATP5G1
hCG_27507
DescriptionFUNCTION: 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.

FUNCTION: 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. .

FUNCTION: 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. .

FUNCTION: 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. .

AccessionsENST00000393366.7
ENST00000504591.2
ENST00000506855.1
I3L0Y5
Q6FIH7
ENST00000503641.5
ENST00000355938.9
ENST00000514808.5
E7EPU7
P05496
E7EQ97
D6R9H7