CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008301
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 V-type proton ATPase catalytic subunit A 
Protein Synonyms/Alias
 V-ATPase subunit A; V-ATPase 69 kDa subunit; Vacuolar proton pump subunit alpha 
Gene Name
 Atp6v1a 
Gene Synonyms/Alias
 Atp6a1; Atp6a2; Atp6v1a1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
84DPVLRTGKPLSVELGubiquitination[1]
132SALSRDIKWEFIPSKubiquitination[1]
139KWEFIPSKNLRVGSHubiquitination[1]
163VNENSLIKHKIMLPPubiquitination[1]
165ENSLIKHKIMLPPRNubiquitination[1]
202EFEGVKEKFSMVQVWubiquitination[1]
220QVRPVTEKLPANHPLubiquitination[1]
467ALDEYYDKHFTEFVPubiquitination[1]
480VPLRTKAKEILQEEEubiquitination[1]
513KITLEVAKLIKDDFLubiquitination[1]
516LEVAKLIKDDFLQQNubiquitination[1]
580HMGEILYKLSSMKFKubiquitination[1]
598KDGEAKIKADYAQLLubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
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. 
Sequence Annotation
 NP_BIND 250 257 ATP (Potential).
 MOD_RES 374 374 Phosphotyrosine.
 MOD_RES 384 384 Phosphoserine.  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Direct protein sequencing; Hydrogen ion transport; Hydrolase; Ion transport; Nucleotide-binding; Phosphoprotein; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 617 AA 
Protein Sequence
MDFSKLPKIR DEDKESTFGY VHGVSGPVVT ACDMAGAAMY ELVRVGHSEL VGEIIRLEGD 60
MATIQVYEET SGVSVGDPVL RTGKPLSVEL GPGIMGAIFD GIQRPLSDIS SQTQSIYIPR 120
GVNVSALSRD IKWEFIPSKN LRVGSHITGG DIYGIVNENS LIKHKIMLPP RNRGSVTYIA 180
PPGNYDASDV VLELEFEGVK EKFSMVQVWP VRQVRPVTEK LPANHPLLTG QRVLDALFPC 240
VQGGTTAIPG AFGCGKTVIS QSLSKYSNSD VIIYVGCGER GNEMSEVLRD FPELTMEVDG 300
KVESIMKRTA LVANTSNMPV AAREASIYTG ITLSEYFRDM GYHVSMMADS TSRWAEALRE 360
ISGRLAEMPA DSGYPAYLGA RLASFYERAG RVKCLGNPER EGSVSIVGAV SPPGGDFSDP 420
VTSATLGIVQ VFWGLDKKLA QRKHFPSVNW LISYSKYMRA LDEYYDKHFT EFVPLRTKAK 480
EILQEEEDLA EIVQLVGKAS LAETDKITLE VAKLIKDDFL QQNGYTPYDR FCPFYKTVGM 540
LSNMISFYDM ARRAVETTAQ SDNKITWSII REHMGEILYK LSSMKFKDPV KDGEAKIKAD 600
YAQLLEDMQN AFRSLED 617 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005902; C:microvillus; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 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.
 IPR022878; V-ATPase_su_A/alpha. 
Pfam
 PF00006; ATP-synt_ab
 PF00306; ATP-synt_ab_C
 PF02874; ATP-synt_ab_N 
SMART
  
PROSITE
 PS00152; ATPASE_ALPHA_BETA 
PRINTS