CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005832
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP synthase subunit delta, mitochondrial 
Protein Synonyms/Alias
 F-ATPase delta subunit 
Gene Name
 ATP5D 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
136AAKANLEKAQAELVGacetylation[1, 2]
136AAKANLEKAQAELVGubiquitination[3]
165EANEALVKALE****acetylation[4]
165EANEALVKALE****ubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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
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 turnover 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 of the central stalk which is part of the complex rotary element. 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
 CROSSLNK 136 136 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 ATP synthesis; CF(1); Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Isopeptide bond; Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transit peptide; Transport; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 168 AA 
Protein Sequence
MLPAALLRRP GLGRLVRHAR AYAEAAAAPA AASGPNQMSF TFASPTQVFF NGANVRQVDV 60
PTLTGAFGIL AAHVPTLQVL RPGLVVVHAE DGTTSKYFVS SGSIAVNADS SVQLLAEEAV 120
TLDMLDLGAA KANLEKAQAE LVGTADEATR AEIQIRIEAN EALVKALE 168 
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; NAS:UniProtKB.
 GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; NAS:UniProtKB.
 GO:0006119; P:oxidative phosphorylation; NAS:UniProtKB.
 GO:0022904; P:respiratory electron transport chain; TAS:Reactome.
 GO:0046688; P:response to copper ion; NAS:UniProtKB. 
Interpro
 IPR001469; ATPase_F1-cplx_dsu/esu.
 IPR020547; ATPase_F1-cplx_dsu/esu_C.
 IPR020546; ATPase_F1-cplx_dsu/esu_N. 
Pfam
 PF02823; ATP-synt_DE_N 
SMART
  
PROSITE
  
PRINTS