UniProt Accession

 ATPG_HUMAN; P36542; A8KA31; Q5VYP3; Q6I9V2; Q96AS8 

Genbank Protein ID

 D16561; D16561; D16562; D16563; AK292896; CR457403; AL353754; AL158044; AL353754; AL158044; AL158044; AL353754; AL158044; AL353754; CH471072; CH471072; BC000470; BC000931; BC013394; BC016812; BC020824 

Genbank Nucleotide ID

 BAA03994.1; BAA03995.1; BAA03996.1; BAA03997.1; BAF85585.1; CAG33684.1; CAH73453.1; CAH73453.1; CAH73454.1; CAH73454.1; CAI12960.1; CAI12960.1; CAI12961.1; CAI12961.1; EAW86372.1; EAW86373.1; AAH00470.1; AAH00931.1; AAH13394.1; AAH16812.1; AAH20824.1 

Protein Name

 ATP synthase subunit gamma, mitochondrial 

Protein Synonyms/Alias

 F-ATPase gamma subunit 

Gene Name

 ATP5C1 

Gene Synonyms/Alias

 ATP5C; ATP5CL1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
154	DQFLVAFKEVGRKPP	acetylation	[1]
154	DQFLVAFKEVGRKPP	ubiquitination	[2]
262	TAMDNASKNASEMID	ubiquitination	[2]
270	NASEMIDKLTLTFNR	ubiquitination	[2]

Reference

 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 

Functional 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(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. 

Sequence Annotation

 MOD_RES 55 55 N6-acetyllysine.
 MOD_RES 79 79 N6-acetyllysine (By similarity).
 MOD_RES 90 90 N6-acetyllysine (By similarity).
 MOD_RES 115 115 N6-acetyllysine (By similarity).
 MOD_RES 146 146 Phosphoserine (By similarity).
 MOD_RES 154 154 N6-acetyllysine.
 MOD_RES 197 197 N6-acetyllysine.  

Keyword

 Acetylation; Alternative splicing; ATP synthesis; CF(1); Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein; Reference proteome; Transit peptide; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 298 AA 

Protein Sequence

Gene Ontology

 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic core F(1); NAS:UniProtKB.
 GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
 GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
 GO:0022857; F:transmembrane transporter activity; IC:UniProtKB.
 GO:0006200; P:ATP catabolic process; IDA:GOC.
 GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB.
 GO:0006119; P:oxidative phosphorylation; NAS:UniProtKB.
 GO:0022904; P:respiratory electron transport chain; TAS:Reactome. 

Interpro

 IPR000131; ATPase_F1-cplx_gsu.
 IPR023632; ATPase_F1_gsu_CS.
 IPR023633; ATPase_F1_gsu_dom. 

Pfam

 PF00231; ATP-synt 

SMART

  

PROSITE

 PS00153; ATPASE_GAMMA 

PRINTS

 PR00126; ATPASEGAMMA.