CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021988
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable cation-transporting ATPase 13A2 
Protein Synonyms/Alias
  
Gene Name
 ATP13A2 
Gene Synonyms/Alias
 PARK9 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
68PLLLFRWKPLWGVRLubiquitination[1, 2]
143AVPEGAWKDTAQLHKubiquitination[1, 2, 3]
150KDTAQLHKSEEAVSVubiquitination[4]
160EAVSVGQKRVLRYYLubiquitination[3]
213LQDQMVRKAIYGPNVubiquitination[3]
532VMGVVPLKGQAFLPLubiquitination[5]
693RVVALASKPLPTVPSubiquitination[3, 4]
729LVMRNLLKPQTTPVIubiquitination[3]
804PTAVNGVKDPDQAASubiquitination[4]
839IIVKHFPKLLPKVLVubiquitination[3, 6]
843HFPKLLPKVLVQGTVubiquitination[1, 2]
859ARMAPEQKTELVCELubiquitination[3]
868ELVCELQKLQYCVGMubiquitination[3]
1160RASKKRFKQLERELAubiquitination[3]
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] 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]
 [3] 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]
 [4] 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]
 [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] 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] 
Functional Description
 May play a role in intracellular cation homeostasis and the maintenance of neuronal integrity. 
Sequence Annotation
 ACT_SITE 513 513 4-aspartylphosphate intermediate (By
 METAL 878 878 Magnesium (By similarity).
 METAL 882 882 Magnesium (By similarity).  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Disease mutation; Hydrolase; Lysosome; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Parkinsonism; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1180 AA 
Protein Sequence
MSADSSPLVG STPTGYGTLT IGTSIDPLSS SVSSVRLSGY CGSPWRVIGY HVVVWMMAGI 60
PLLLFRWKPL WGVRLRLRPC NLAHAETLVI EIRDKEDSSW QLFTVQVQTE AIGEGSLEPS 120
PQSQAEDGRS QAAVGAVPEG AWKDTAQLHK SEEAVSVGQK RVLRYYLFQG QRYIWIETQQ 180
AFYQVSLLDH GRSCDDVHRS RHGLSLQDQM VRKAIYGPNV ISIPVKSYPQ LLVDEALNPY 240
YGFQAFSIAL WLADHYYWYA LCIFLISSIS ICLSLYKTRK QSQTLRDMVK LSMRVCVCRP 300
GGEEEWVDSS ELVPGDCLVL PQEGGLMPCD AALVAGECMV NESSLTGESI PVLKTALPEG 360
LGPYCAETHR RHTLFCGTLI LQARAYVGPH VLAVVTRTGF CTAKGGLVSS ILHPRPINFK 420
FYKHSMKFVA ALSVLALLGT IYSIFILYRN RVPLNEIVIR ALDLVTVVVP PALPAAMTVC 480
TLYAQSRLRR QGIFCIHPLR INLGGKLQLV CFDKTGTLTE DGLDVMGVVP LKGQAFLPLV 540
PEPRRLPVGP LLRALATCHA LSRLQDTPVG DPMDLKMVES TGWVLEEEPA ADSAFGTQVL 600
AVMRPPLWEP QLQAMEEPPV PVSVLHRFPF SSALQRMSVV VAWPGATQPE AYVKGSPELV 660
AGLCNPETVP TDFAQMLQSY TAAGYRVVAL ASKPLPTVPS LEAAQQLTRD TVEGDLSLLG 720
LLVMRNLLKP QTTPVIQALR RTRIRAVMVT GDNLQTAVTV ARGCGMVAPQ EHLIIVHATH 780
PERGQPASLE FLPMESPTAV NGVKDPDQAA SYTVEPDPRS RHLALSGPTF GIIVKHFPKL 840
LPKVLVQGTV FARMAPEQKT ELVCELQKLQ YCVGMCGDGA NDCGALKAAD VGISLSQAEA 900
SVVSPFTSSM ASIECVPMVI REGRCSLDTS FSVFKYMALY SLTQFISVLI LYTINTNLGD 960
LQFLAIDLVI TTTVAVLMSR TGPALVLGRV RPPGALLSVP VLSSLLLQMV LVTGVQLGGY 1020
FLTLAQPWFV PLNRTVAAPD NLPNYENTVV FSLSSFQYLI LAAAVSKGAP FRRPLYTNVP 1080
FLVALALLSS VLVGLVLVPG LLQGPLALRN ITDTGFKLLL LGLVTLNFVG AFMLESVLDQ 1140
CLPACLRRLR PKRASKKRFK QLERELAEQP WPPLPAGPLR 1180 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005764; C:lysosome; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006200; P:ATP catabolic process; IEA:GOC. 
Interpro
 IPR004014; ATPase_P-typ_cation-transptr_N.
 IPR006544; ATPase_P-typ_Cation_typ_V.
 IPR023299; ATPase_P-typ_cyto_domN.
 IPR018303; ATPase_P-typ_P_site.
 IPR008250; ATPase_P-typ_transduc_dom_A.
 IPR001757; Cation_transp_P_typ_ATPase.
 IPR023214; HAD-like_dom. 
Pfam
 PF00122; E1-E2_ATPase
 PF12409; P5-ATPase 
SMART
 SM00831; Cation_ATPase_N 
PROSITE
 PS00154; ATPASE_E1_E2 
PRINTS
 PR00119; CATATPASE.