CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004554
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 V-type proton ATPase catalytic subunit A 
Protein Synonyms/Alias
 V-ATPase subunit A; Vacuolar proton pump subunit A; Endonuclease PI-SceI; Sce VMA intein; VMA1-derived endonuclease; VDE 
Gene Name
 VMA1 
Gene Synonyms/Alias
 CLS8; TFP1; YDL185W; D1286 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
117QRPLKAIKEESQSIYacetylation[1]
117QRPLKAIKEESQSIYubiquitination[2]
139PALDRTIKWQFTPGKacetylation[1]
146KWQFTPGKFQVGDHIubiquitination[2]
206LEVEFDGKKSDFTLYacetylation[1]
207EVEFDGKKSDFTLYHacetylation[1]
336TMYSVVQKSQHRAHKacetylation[1]
355REVPELLKFTCNATHacetylation[1]
407GRIVELVKEVSKSYPacetylation[1]
407GRIVELVKEVSKSYPubiquitination[2]
411ELVKEVSKSYPISEGubiquitination[2]
480FDYMQKSKFHLTIEGacetylation[1]
536LNLCAEYKDRKEPQVacetylation[1]
536LNLCAEYKDRKEPQVubiquitination[2]
545RKEPQVAKTVNLYSKacetylation[1]
552KTVNLYSKVVRGNGIacetylation[1]
552KTVNLYSKVVRGNGIubiquitination[2]
803EYFRDQGKNVSMIADubiquitination[2]
842FPAYLGAKLASFYERubiquitination[2]
852SFYERAGKAVALGSPubiquitination[2]
917NTSVSYSKYTNVLNKubiquitination[2]
924KYTNVLNKFYDSNYPubiquitination[2]
941PVLRDRMKEILSNAEubiquitination[2]
1024ANGANWSKLADSTGDubiquitination[2]
1033ADSTGDVKHAVSSSKacetylation[1]
1033ADSTGDVKHAVSSSKubiquitination[2]
1040KHAVSSSKFFEPSRGacetylation[1]
1049FEPSRGEKEVHGEFEacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca(2+) homeostasis. This is a catalytic subunit. 
Sequence Annotation
 DOMAIN 494 642 DOD-type homing endonuclease.
 NP_BIND 257 264 ATP (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 131 131 Phosphothreonine.
 MOD_RES 858 858 Phosphoserine.
 MOD_RES 928 928 Phosphoserine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Autocatalytic cleavage; Complete proteome; Direct protein sequencing; DNA-binding; Endonuclease; Hydrogen ion transport; Hydrolase; Intron homing; Ion transport; Membrane; Nuclease; Nucleotide-binding; Phosphoprotein; Protein splicing; Reference proteome; Transport; Vacuole. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1071 AA 
Protein Sequence
MAGAIENARK EIKRISLEDH AESEYGAIYS VSGPVVIAEN MIGCAMYELV KVGHDNLVGE 60
VIRIDGDKAT IQVYEETAGL TVGDPVLRTG KPLSVELGPG LMETIYDGIQ RPLKAIKEES 120
QSIYIPRGID TPALDRTIKW QFTPGKFQVG DHISGGDIYG SVFENSLISS HKILLPPRSR 180
GTITWIAPAG EYTLDEKILE VEFDGKKSDF TLYHTWPVRV PRPVTEKLSA DYPLLTGQRV 240
LDALFPCVQG GTTCIPGAFG CGKTVISQSL SKYSNSDAII YVGCFAKGTN VLMADGSIEC 300
IENIEVGNKV MGKDGRPREV IKLPRGRETM YSVVQKSQHR AHKSDSSREV PELLKFTCNA 360
THELVVRTPR SVRRLSRTIK GVEYFEVITF EMGQKKAPDG RIVELVKEVS KSYPISEGPE 420
RANELVESYR KASNKAYFEW TIEARDLSLL GSHVRKATYQ TYAPILYEND HFFDYMQKSK 480
FHLTIEGPKV LAYLLGLWIG DGLSDRATFS VDSRDTSLME RVTEYAEKLN LCAEYKDRKE 540
PQVAKTVNLY SKVVRGNGIR NNLNTENPLW DAIVGLGFLK DGVKNIPSFL STDNIGTRET 600
FLAGLIDSDG YVTDEHGIKA TIKTIHTSVR DGLVSLARSL GLVVSVNAEP AKVDMNGTKH 660
KISYAIYMSG GDVLLNVLSK CAGSKKFRPA PAAAFARECR GFYFELQELK EDDYYGITLS 720
DDSDHQFLLA NQVVVHNCGE RGNEMAEVLM EFPELYTEMS GTKEPIMKRT TLVANTSNMP 780
VAAREASIYT GITLAEYFRD QGKNVSMIAD SSSRWAEALR EISGRLGEMP ADQGFPAYLG 840
AKLASFYERA GKAVALGSPD RTGSVSIVAA VSPAGGDFSD PVTTATLGIT QVFWGLDKKL 900
AQRKHFPSIN TSVSYSKYTN VLNKFYDSNY PEFPVLRDRM KEILSNAEEL EQVVQLVGKS 960
ALSDSDKITL DVATLIKEDF LQQNGYSTYD AFCPIWKTFD MMRAFISYHD EAQKAVANGA 1020
NWSKLADSTG DVKHAVSSSK FFEPSRGEKE VHGEFEKLLS TMQERFAEST D 1071 
Gene Ontology
 GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
 GO:0000329; C:fungal-type vacuole membrane; IDA:UniProtKB.
 GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; TAS:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0004520; F:endodeoxyribonuclease activity; TAS:SGD.
 GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; TAS:SGD.
 GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
 GO:0044267; P:cellular protein metabolic process; IDA:SGD.
 GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
 GO:0006314; P:intron homing; TAS:SGD.
 GO:0007035; P:vacuolar acidification; IMP:SGD. 
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.
 IPR003586; Hint_dom_C.
 IPR003587; Hint_dom_N.
 IPR007868; Hom_end_hint.
 IPR007869; Homing_endonuc_PI-Sce.
 IPR027434; Homing_endonucl.
 IPR006142; INTEIN.
 IPR004042; Intein_endonuc.
 IPR006141; Intein_splice_site.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00006; ATP-synt_ab
 PF00306; ATP-synt_ab_C
 PF02874; ATP-synt_ab_N
 PF05204; Hom_end
 PF05203; Hom_end_hint 
SMART
 SM00305; HintC
 SM00306; HintN 
PROSITE
 PS00152; ATPASE_ALPHA_BETA
 PS50818; INTEIN_C_TER
 PS50819; INTEIN_ENDONUCLEASE
 PS50817; INTEIN_N_TER 
PRINTS
 PR00379; INTEIN.