UniProt Accession

 ATP5L_HUMAN; O75964; A8K0K3; Q96BV6; Q9UBZ7 

Genbank Protein ID

 AF092124; AF087846; AF070655; AL050277; CR533494; CR542211; AK289568; CH471065; BC015128; BC070165 

Genbank Nucleotide ID

 AAC61597.1; AAP97159.1; AAD20961.1; CAB43378.1; CAG38525.1; CAG47007.1; BAF82257.1; EAW67376.1; AAH15128.1; AAH70165.1 

Protein Name

 ATP synthase subunit g, mitochondrial 

Protein Synonyms/Alias

 ATPase subunit g 

Gene Name

 ATP5L 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
24	NAAVTYSKPRLATFW	acetylation	[1]
24	NAAVTYSKPRLATFW	ubiquitination	[2, 3, 4]
55	RAIQSLKKIVNSAQT	ubiquitination	[5]
66	SAQTGSFKQLTVKEA	ubiquitination	[2, 3, 4]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 

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(0) domain. Minor subunit located with subunit a in the membrane. 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 24 24 N6-acetyllysine.
 MOD_RES 54 54 N6-acetyllysine (By similarity).
 MOD_RES 66 66 N6-acetyllysine (By similarity).  

Keyword

 Acetylation; ATP synthesis; CF(0); Complete proteome; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 103 AA 

Protein Sequence

Gene Ontology

 GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
 GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
 GO:0015078; F:hydrogen ion transmembrane transporter activity; 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:0022904; P:respiratory electron transport chain; TAS:Reactome. 

Interpro

 IPR016702; ATP-Synthase_su_G_mt_met.
 IPR006808; ATPase_F0-cplx_gsu_mt. 

Pfam

 PF04718; ATP-synt_G 

SMART

  

PROSITE

  

PRINTS