CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009566
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 V-type proton ATPase subunit B, brain isoform 
Protein Synonyms/Alias
 V-ATPase subunit B 2; Endomembrane proton pump 58 kDa subunit; Vacuolar proton pump subunit B 2 
Gene Name
 Atp6v1b2 
Gene Synonyms/Alias
 Atp6b2; Vat2 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
48SQPRLTYKTVSGVNGacetylation[1]
64LVILDHVKFPRYAEIacetylation[1]
81LTLPDGTKRSGQVLEacetylation[1]
108GTSGIDAKKTSCEFTacetylation[1]
108GTSGIDAKKTSCEFTubiquitination[2]
137RVFNGSGKPIDRGPVubiquitination[2]
460EFLQKFEKNFITQGPacetylation[1]
460EFLQKFEKNFITQGPubiquitination[2]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
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. 
Sequence Annotation
 MOD_RES 404 404 Phosphoserine (By similarity).
 MOD_RES 498 498 Phosphoserine (By similarity).  
Keyword
 Complete proteome; Direct protein sequencing; Hydrogen ion transport; Hydrolase; Ion transport; Membrane; Phosphoprotein; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 511 AA 
Protein Sequence
MALRAMRGIV NGAAPELPVP TGGPMAGARE QALAVSRNYL SQPRLTYKTV SGVNGPLVIL 60
DHVKFPRYAE IVHLTLPDGT KRSGQVLEVS GSKAVVQVFE GTSGIDAKKT SCEFTGDILR 120
TPVSEDMLGR VFNGSGKPID RGPVVLAEDF LDIMGQPINP QCRIYPEEMI QTGISAIDGM 180
NSIARGQKIP IFSAAGLPHN EIAAQICRQA GLVKKSKDVV DYSEENFAIV FAAMGVNMET 240
ARFFKSDFEE NGSMDNVCLF LNLANDPTIE RIITPRLALT TAEFLAYQCE KHVLVILTDM 300
SSYAEALREV SAAREEVPGR RGFPGYMYTD LATIYERAGR VEGRNGSITQ IPILTMPNDD 360
ITHPIPDLTG YITEGQIYVD RQLHNRQIYP PINVLPSLSR LMKSAIGEGM TRKDHADVSN 420
QLYACYAIGK DVQAMKAVVG EEALTSDDLL YLEFLQKFEK NFITQGPYEN RTVYETLDIG 480
WQLLRIFPKE MLKRIPQSTL SEFYPRDSAK H 511 
Gene Ontology
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0005794; C:Golgi apparatus; IEA:Compara.
 GO:0016021; C:integral to membrane; IDA:RGD.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005902; C:microvillus; IEA:Compara.
 GO:0005886; C:plasma membrane; ISS:UniProtKB.
 GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0016820; F:hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances; IEA:InterPro.
 GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
 GO:0046034; P:ATP metabolic process; IEA:InterPro.
 GO:0007035; P:vacuolar acidification; TAS:RGD. 
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