CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021688
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable cation-transporting ATPase 13A1 
Protein Synonyms/Alias
  
Gene Name
 ATP13A1 
Gene Synonyms/Alias
 ATP13A; KIAA1825; CGI-152 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
143PSKATFVKVVPTPNNubiquitination[1, 2, 3, 4]
176VLSFEFQKIKYSYDAubiquitination[2, 5]
178SFEFQKIKYSYDALEubiquitination[5]
186YSYDALEKKQFLPVAubiquitination[2]
187SYDALEKKQFLPVAFubiquitination[5, 6]
226EKKFGSNKAEMVVPDubiquitination[5]
239PDFSELFKERATAPFubiquitination[2, 5]
297EIRKMGNKPHMIQVYubiquitination[5]
308IQVYRSRKWRPIASDubiquitination[1, 4, 5, 7]
361GESVPQMKEPIEDLSubiquitination[8]
404QKATTGLKPVDSGCVubiquitination[5]
425GFNTSQGKLLRTILFubiquitination[2, 5, 7]
435RTILFGVKRVTANNLubiquitination[2, 5]
534VEVCCFDKTGTLTSDubiquitination[5]
555VAGLRDGKEVTPVSSubiquitination[2, 5, 7, 9]
592LVGDPLEKAMLTAVDubiquitination[7]
607WTLTKDEKVFPRSIKubiquitination[5]
614KVFPRSIKTQGLKIHubiquitination[5]
631FHFASALKRMSVLASubiquitination[5]
691RVLALGYKELGHLTHubiquitination[5]
730CPLKADSKAVIREIQubiquitination[5]
950DESTPIVKLGDASIAubiquitination[2, 7]
963IAAPFTSKLSSIQCIubiquitination[5]
1038ISRSKPLKTLSRERPubiquitination[2]
1083AQARSPEKQEQFVDLubiquitination[2]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] 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]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [9] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
  
Sequence Annotation
 ACT_SITE 533 533 4-aspartylphosphate intermediate (By
 METAL 864 864 Magnesium (By similarity).
 METAL 868 868 Magnesium (By similarity).
 MOD_RES 899 899 Phosphoserine.
 MOD_RES 935 935 Phosphoserine (By similarity).
 CARBOHYD 287 287 N-linked (GlcNAc...) (Potential).
 CARBOHYD 420 420 N-linked (GlcNAc...).  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Glycoprotein; Hydrolase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1204 AA 
Protein Sequence
MAAAAAVGNA VPCGARPCGV RPDGQPKPGP QPRALLAAGP ALIANGDELV AAVWPYRRLA 60
LLRRLTVLPF AGLLYPAWLG AAAAGCWGWG SSWVQIPEAA LLVLATICLA HALTVLSGHW 120
SVHAHCALTC TPEYDPSKAT FVKVVPTPNN GSTELVALHR NEGEDGLEVL SFEFQKIKYS 180
YDALEKKQFL PVAFPVGNAF SYYQSNRGFQ EDSEIRAAEK KFGSNKAEMV VPDFSELFKE 240
RATAPFFVFQ VFCVGLWCLD EYWYYSVFTL SMLVAFEASL VQQQMRNMSE IRKMGNKPHM 300
IQVYRSRKWR PIASDEIVPG DIVSIGRSPQ ENLVPCDVLL LRGRCIVDEA MLTGESVPQM 360
KEPIEDLSPD RVLDLQADSR LHVIFGGTKV VQHIPPQKAT TGLKPVDSGC VAYVLRTGFN 420
TSQGKLLRTI LFGVKRVTAN NLETFIFILF LLVFAIAAAA YVWIEGTKDP SRNRYKLFLE 480
CTLILTSVVP PELPIELSLA VNTSLIALAK LYMYCTEPFR IPFAGKVEVC CFDKTGTLTS 540
DSLVVRGVAG LRDGKEVTPV SSIPVETHRA LASCHSLMQL DDGTLVGDPL EKAMLTAVDW 600
TLTKDEKVFP RSIKTQGLKI HQRFHFASAL KRMSVLASYE KLGSTDLCYI AAVKGAPETL 660
HSMFSQCPPD YHHIHTEISR EGARVLALGY KELGHLTHQQ AREVKREALE CSLKFVGFIV 720
VSCPLKADSK AVIREIQNAS HRVVMITGDN PLTACHVAQE LHFIEKAHTL ILQPPSEKGR 780
QCEWRSIDGS IVLPLARGSP KALALEYALC LTGDGLAHLQ ATDPQQLLRL IPHVQVFARV 840
APKQKEFVIT SLKELGYVTL MCGDGTNDVG ALKHADVGVA LLANAPERVV ERRRRPRDSP 900
TLSNSGIRAT SRTAKQRSGL PPSEEQPTSQ RDRLSQVLRD LEDESTPIVK LGDASIAAPF 960
TSKLSSIQCI CHVIKQGRCT LVTTLQMFKI LALNALILAY SQSVLYLEGV KFSDFQATLQ 1020
GLLLAGCFLF ISRSKPLKTL SRERPLPNIF NLYTILTVML QFFVHFLSLV YLYREAQARS 1080
PEKQEQFVDL YKEFEPSLVN STVYIMAMAM QMATFAINYK GPPFMESLPE NKPLVWSLAV 1140
SLLAIIGLLL GSSPDFNSQF GLVDIPVEFK LVIAQVLLLD FCLALLADRV LQFFLGTPKL 1200
KVPS 1204 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 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
 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 
SMART
  
PROSITE
 PS00154; ATPASE_E1_E2 
PRINTS
 PR00119; CATATPASE.