CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004419
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 V-type proton ATPase subunit B 
Protein Synonyms/Alias
 V-ATPase subunit B; V-ATPase 57 kDa subunit; Vacuolar proton pump subunit B 
Gene Name
 VMA2 
Gene Synonyms/Alias
 VAT2; YBR127C; YBR1002 
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
13KELFAINKKAVEQGFacetylation[1]
14ELFAINKKAVEQGFNubiquitination[2, 3]
23VEQGFNVKPRLNYNTacetylation[1]
23VEQGFNVKPRLNYNTubiquitination[3]
90TSGIDVKKTTVEFTGubiquitination[3]
125RPIDNGPKVFAEDYLubiquitination[3]
169NSIARGQKIPIFSASubiquitination[3]
226LETARFFKQDFEENGacetylation[1]
226LETARFFKQDFEENGubiquitination[3]
384PSLSRLMKSAIGEGMubiquitination[3]
394IGEGMTRKDHGDVSNubiquitination[3]
406VSNQLYAKYAIGKDAacetylation[1]
411YAKYAIGKDAAAMKAubiquitination[3]
441EFLEKFEKTFITQGAacetylation[1]
441EFLEKFEKTFITQGAubiquitination[3]
470SLLRIYPKEMLNRISubiquitination[3]
479MLNRISPKILDEFYDacetylation[1]
479MLNRISPKILDEFYDubiquitination[3]
508TRSSGKKKDASQEESubiquitination[2, 3]
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] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [3] 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, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-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. 
Sequence Annotation
 MOD_RES 4 4 Phosphoserine.
 MOD_RES 137 137 Phosphoserine.
 MOD_RES 503 503 Phosphoserine.
 MOD_RES 504 504 Phosphoserine.
 MOD_RES 511 511 Phosphoserine; by ATM or ATR.
 MOD_RES 515 515 Phosphoserine.  
Keyword
 Complete proteome; Direct protein sequencing; Hydrogen ion transport; Hydrolase; Ion transport; Phosphoprotein; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 517 AA 
Protein Sequence
MVLSDKELFA INKKAVEQGF NVKPRLNYNT VSGVNGPLVI LEKVKFPRYN EIVNLTLPDG 60
TVRQGQVLEI RGDRAIVQVF EGTSGIDVKK TTVEFTGESL RIPVSEDMLG RIFDGSGRPI 120
DNGPKVFAED YLDINGSPIN PYARIYPEEM ISTGVSAIDT MNSIARGQKI PIFSASGLPH 180
NEIAAQICRQ AGLVRPTKDV HDGHEENFSI VFAAMGVNLE TARFFKQDFE ENGSLERTSL 240
FLNLANDPTI ERIITPRLAL TTAEYLAYQT ERHVLTILTD MSSYADALRE VSAAREEVPG 300
RRGYPGYMYT DLSTIYERAG RVEGRNGSIT QIPILTMPND DITHPIPDLT GYITEGQIFV 360
DRQLHNKGIY PPINVLPSLS RLMKSAIGEG MTRKDHGDVS NQLYAKYAIG KDAAAMKAVV 420
GEEALSIEDK LSLEFLEKFE KTFITQGAYE DRTVFESLDQ AWSLLRIYPK EMLNRISPKI 480
LDEFYDRARD DADEDEEDPD TRSSGKKKDA SQEESLI 517 
Gene Ontology
 GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
 GO:0016021; C:integral to membrane; ISM:SGD.
 GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IMP:SGD.
 GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
 GO:0006874; P:cellular calcium ion homeostasis; IMP: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.
 IPR005723; ATPase_V1-cplx_bsu.
 IPR027417; P-loop_NTPase.
 IPR022879; V-ATPase_su_B/beta. 
Pfam
 PF00006; ATP-synt_ab
 PF00306; ATP-synt_ab_C
 PF02874; ATP-synt_ab_N 
SMART
  
PROSITE
 PS00152; ATPASE_ALPHA_BETA 
PRINTS