UniProt Accession

 ATP5H_HUMAN; O75947; B2R5L6; Q9H3J4 

Genbank Protein ID

 AF087135; AF070650; AF061735; AK312230; CH471099; BC032245; BC038092 

Genbank Nucleotide ID

 AAC36338.1; AAD20956.1; AAG43146.1; BAG35163.1; EAW89228.1; AAH32245.1; AAH38092.1 

Protein Name

 ATP synthase subunit d, mitochondrial 

Protein Synonyms/Alias

 ATPase subunit d 

Gene Name

 ATP5H 

Gene Synonyms/Alias

 My032 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
32	KAIASSLKSWNETLT	ubiquitination	[1, 2]
58	AIDWAYYKANVAKAG	ubiquitination	[3]
72	GLVDDFEKKFNALKV	acetylation	[4]
73	LVDDFEKKFNALKVP	ubiquitination	[5]
78	EKKFNALKVPVPEDK	acetylation	[6]
85	KVPVPEDKYTAQVDA	acetylation	[4, 6, 7, 8]
85	KVPVPEDKYTAQVDA	ubiquitination	[3]
95	AQVDAEEKEDVKSCA	acetylation	[4, 6, 7, 8, 9]
117	ARIVEYEKEMEKMKN	acetylation	[4, 6, 7]
148	PETKLDKKKYPYWPH	acetylation	[4]
149	ETKLDKKKYPYWPHQ	acetylation	[4]
149	ETKLDKKKYPYWPHQ	ubiquitination	[1, 2]

Reference

 [1] 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]
 [2] 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]
 [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] 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]
 [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]
 [6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [9] 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] 

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 and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 63 63 N6-acetyllysine (By similarity).
 MOD_RES 78 78 N6-acetyllysine (By similarity).
 MOD_RES 85 85 N6-acetyllysine.
 MOD_RES 95 95 N6-acetyllysine.
 MOD_RES 99 99 N6-acetyllysine (By similarity).
 MOD_RES 117 117 N6-acetyllysine.
 MOD_RES 149 149 N6-acetyllysine.  

Keyword

 Acetylation; Alternative splicing; CF(0); Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 161 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

 IPR008689; ATPase_F0-cplx_dsu_mt. 

Pfam

 PF05873; Mt_ATP-synt_D 

SMART

  

PROSITE

  

PRINTS