CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023813
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 V-type proton ATPase 116 kDa subunit a isoform 2 
Protein Synonyms/Alias
 V-ATPase 116 kDa isoform a2; Lysosomal H(+)-transporting ATPase V0 subunit a2; TJ6; Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2 
Gene Name
 ATP6V0A2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
92SPPAPPLKQVLEMQEubiquitination[1, 2, 3, 4, 5, 6, 7]
172CMQRLGAKLGFVSGLubiquitination[1, 4, 5, 6, 8, 9]
279DLYTVLHKTEDYLRQacetylation[10]
279DLYTVLHKTEDYLRQubiquitination[1, 2, 5, 6, 9]
290YLRQVLCKAAESVYSubiquitination[9]
363FMNIIPTKETPPTRIubiquitination[1, 2, 5, 6, 9]
374PTRIRTNKFTEGFQNubiquitination[1, 2, 6, 9]
693SGYTLIRKDSEEEVSubiquitination[9]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] 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]
 [10] 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] 
Functional Description
 Part of the proton channel of V-ATPases. Essential component of the endosomal pH-sensing machinery. May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH. 
Sequence Annotation
 MOD_RES 695 695 Phosphoserine.
 MOD_RES 700 700 Phosphoserine (By similarity).  
Keyword
 Cell membrane; Complete proteome; Endosome; Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 856 AA 
Protein Sequence
MGSLFRSETM CLAQLFLQSG TAYECLSALG EKGLVQFRDL NQNVSSFQRK FVGEVKRCEE 60
LERILVYLVQ EINRADIPLP EGEASPPAPP LKQVLEMQEQ LQKLEVELRE VTKNKEKLRK 120
NLLELIEYTH MLRVTKTFVK RNVEFEPTYE EFPSLESDSL LDYSCMQRLG AKLGFVSGLI 180
NQGKVEAFEK MLWRVCKGYT IVSYAELDES LEDPETGEVI KWYVFLISFW GEQIGHKVKK 240
ICDCYHCHVY PYPNTAEERR EIQEGLNTRI QDLYTVLHKT EDYLRQVLCK AAESVYSRVI 300
QVKKMKAIYH MLNMCSFDVT NKCLIAEVWC PEADLQDLRR ALEEGSRESG ATIPSFMNII 360
PTKETPPTRI RTNKFTEGFQ NIVDAYGVGS YREVNPALFT IITFPFLFAV MFGDFGHGFV 420
MFLFALLLVL NENHPRLNQS QEIMRMFFNG RYILLLMGLF SVYTGLIYND CFSKSVNLFG 480
SGWNVSAMYS SSHPPAEHKK MVLWNDSVVR HNSILQLDPS IPGVFRGPYP LGIDPIWNLA 540
TNRLTFLNSF KMKMSVILGI IHMTFGVILG IFNHLHFRKK FNIYLVSIPE LLFMLCIFGY 600
LIFMIFYKWL VFSAETSRVA PSILIEFINM FLFPASKTSG LYTGQEYVQR VLLVVTALSV 660
PVLFLGKPLF LLWLHNGRSC FGVNRSGYTL IRKDSEEEVS LLGSQDIEEG NHQVEDGCRE 720
MACEEFNFGE ILMTQVIHSI EYCLGCISNT ASYLRLWALS LAHAQLSDVL WAMLMRVGLR 780
VDTTYGVLLL LPVIALFAVL TIFILLIMEG LSAFLHAIRL HWVEFQNKFY VGAGTKFVPF 840
SFSLLSSKFN NDDSVA 856 
Gene Ontology
 GO:0001669; C:acrosomal vesicle; IEA:Compara.
 GO:0010008; C:endosome membrane; TAS:Reactome.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
 GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
 GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
 GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
 GO:0006955; P:immune response; TAS:ProtInc.
 GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
 GO:0051701; P:interaction with host; TAS:Reactome.
 GO:0090382; P:phagosome maturation; TAS:Reactome.
 GO:0033572; P:transferrin transport; TAS:Reactome.
 GO:0055085; P:transmembrane transport; TAS:Reactome. 
Interpro
 IPR002490; V-ATPase_116kDa_su.
 IPR026028; V-type_ATPase_116kDa_su_euka. 
Pfam
 PF01496; V_ATPase_I 
SMART
  
PROSITE
  
PRINTS