CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031930
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 V-type proton ATPase catalytic subunit A 
Protein Synonyms/Alias
 cDNA FLJ51804, highly similar to Vacuolar ATP synthase catalytic subunit A, ubiquitous isoform (EC 3.6.3.14) 
Gene Name
 ATP6V1A 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
99SALSRDIKWDFTPCKubiquitination[1, 2, 3]
106KWDFTPCKNLRVGSHubiquitination[1, 2, 3]
130VSENSLIKHKIMLPPubiquitination[1, 3]
187QVRPVTEKLPANHPLubiquitination[1, 2, 3]
223PGAFGCGKTVISQSLubiquitination[2, 3]
232VISQSLSKYSNSDVIubiquitination[1, 3]
274GKVESIMKRTALVANubiquitination[3]
360YERAGRVKCLGNPERubiquitination[1, 3, 4]
434ALDEYYDKHFTEFVPacetylation[4]
434ALDEYYDKHFTEFVPubiquitination[1, 3, 5]
447VPLRTKAKEILQEEEubiquitination[1, 2, 3, 6, 7]
480KITLEVAKLIKDDFLubiquitination[5]
483LEVAKLIKDDFLQQNubiquitination[1, 2, 3, 4, 7]
531TTAQSDNKITWSIIRubiquitination[1]
547HMGDILYKLSSMKFKubiquitination[1, 2, 3, 4, 5, 7, 8]
554KLSSMKFKDPLKDGEubiquitination[3]
558MKFKDPLKDGEAKIKubiquitination[1]
565KDGEAKIKSDYAQLLubiquitination[1, 2, 3, 7]
Reference
 [1] 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]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [7] 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]
 [8] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Hydrogen ion transport; Ion transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 584 AA 
Protein Sequence
MAGAAMYELV RVGHSELVGE IIRLEGDMAT IQVYEETSGV SVGDPVLRTG KPLSVELGPG 60
IMGAIFDGIQ RPLSDISSQT QSIYIPRGVN VSALSRDIKW DFTPCKNLRV GSHITGGDIY 120
GIVSENSLIK HKIMLPPRNR GTVTYIAPPG NYDTSDVVLE LEFEGVKEKF TMVQVWPVRQ 180
VRPVTEKLPA NHPLLTGQRV LDALFPCVQG GTTAIPGAFG CGKTVISQSL SKYSNSDVII 240
YVGCGERGNE MSEVLRDFPE LTMEVDGKVE SIMKRTALVA NTSNMPVAAR EASIYTGITL 300
SEYFRDMGYH VSMMADSTSR WAEALREISG RLAEMPADSG YPAYLGARLA SFYERAGRVK 360
CLGNPEREGS VSIVGAVSPP GGDFSDPVTS ATLGIVQVFW GLDKKLAQRK HFPSVNWLIS 420
YSKYMRALDE YYDKHFTEFV PLRTKAKEIL QEEEDLAEIV QLVGKASLAE TDKITLEVAK 480
LIKDDFLQQN GYTPYDRFCP FYKTVGMLSN MIAFYDMARR AVETTAQSDN KITWSIIREH 540
MGDILYKLSS MKFKDPLKDG EAKIKSDYAQ LLEDMQNAFR SLED 584 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IEA:Compara.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005902; C:microvillus; IEA:Compara.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
 GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. 
Interpro
 IPR020003; ATPase_a/bsu_AS.
 IPR004100; ATPase_a/bsu_N.
 IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
 IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
 IPR024034; ATPase_F1_bsu/V1_C.
 IPR005725; ATPase_V1-cplx_asu.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00006; ATP-synt_ab
 PF00306; ATP-synt_ab_C
 PF02874; ATP-synt_ab_N 
SMART
  
PROSITE
 PS00152; ATPASE_ALPHA_BETA 
PRINTS