CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021473
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable cation-transporting ATPase 13A3 
Protein Synonyms/Alias
 ATPase family homolog up-regulated in senescence cells 1 
Gene Name
 ATP13A3 
Gene Synonyms/Alias
 AFURS1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
65TCVRAAIKDCEVVLLubiquitination[1]
85FKMWFCAKIRVLSLEacetylation[2]
100TYPVSSPKSMSNKLSubiquitination[1, 3]
128ENRHRISKYSQTESQubiquitination[1, 3, 4, 5, 6, 7, 8]
160IHNFDFLKGLDEGVSubiquitination[4]
174SCTSIYEKHSAGLTKubiquitination[3, 8]
188KGMHAYRKLLYGVNEubiquitination[1]
342PNPSVDVKGIGDELYubiquitination[1, 7]
355LYNPETHKRHTLFCGubiquitination[1, 3, 4, 5, 7]
377FYTGELVKAIVVRTGubiquitination[1, 3]
389RTGFSTSKGQLVRSIubiquitination[1, 3, 7, 8]
727IIMQNKLKQETPAVLubiquitination[1]
892ANDCGALKRAHGGISubiquitination[1]
914VASPFTSKTPSISCVubiquitination[3, 4, 8]
1169ESVDRWGKCCLPWALubiquitination[3]
1215TEAKALVKENGSCQIubiquitination[3]
Reference
 [1] 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]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [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] 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]
 [5] 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]
 [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]
 [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] 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 498 498 4-aspartylphosphate intermediate (By
 METAL 883 883 Magnesium (By similarity).
 METAL 887 887 Magnesium (By similarity).
 MOD_RES 98 98 Phosphoserine.
 MOD_RES 817 817 Phosphoserine.  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Hydrolase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1226 AA 
Protein Sequence
MDREERKTIN QGQEDEMEIY GYNLSRWKLA IVSLGVICSG GFLLLLLYWM PEWRVKATCV 60
RAAIKDCEVV LLRTTDEFKM WFCAKIRVLS LETYPVSSPK SMSNKLSNGH AVCLIENPTE 120
ENRHRISKYS QTESQQIRYF THHSVKYFWN DTIHNFDFLK GLDEGVSCTS IYEKHSAGLT 180
KGMHAYRKLL YGVNEIAVKV PSVFKLLIKE VLNPFYIFQL FSVILWSTDE YYYYALAIVV 240
MSIVSIVSSL YSIRKQYVML HDMVATHSTV RVSVCRVNEE IEEIFSTDLV PGDVMVIPLN 300
GTIMPCDAVL INGTCIVNES MLTGESVPVT KTNLPNPSVD VKGIGDELYN PETHKRHTLF 360
CGTTVIQTRF YTGELVKAIV VRTGFSTSKG QLVRSILYPK PTDFKLYRDA YLFLLCLVAV 420
AGIGFIYTII NSILNEVQVG VIIIESLDII TITVPPALPA AMTAGIVYAQ RRLKKIGIFC 480
ISPQRINICG QLNLVCFDKT GTLTEDGLDL WGIQRVENAR FLSPEENVCN EMLVKSQFVA 540
CMATCHSLTK IEGVLSGDPL DLKMFEAIGW ILEEATEEET ALHNRIMPTV VRPPKQLLPE 600
STPAGNQEME LFELPATYEI GIVRQFPFSS ALQRMSVVAR VLGDRKMDAY MKGAPEAIAG 660
LCKPETVPVD FQNVLEDFTK QGFRVIALAH RKLESKLTWH KVQNISRDAI ENNMDFMGLI 720
IMQNKLKQET PAVLEDLHKA NIRTVMVTGD SMLTAVSVAR DCGMILPQDK VIIAEALPPK 780
DGKVAKINWH YADSLTQCSH PSAIDPEAIP VKLVHDSLED LQMTRYHFAM NGKSFSVILE 840
HFQDLVPKLM LHGTVFARMA PDQKTQLIEA LQNVDYFVGM CGDGANDCGA LKRAHGGISL 900
SELEASVASP FTSKTPSISC VPNLIREGRA ALITSFCVFK FMALYSIIQY FSVTLLYSIL 960
SNLGDFQFLF IDLAIILVVV FTMSLNPAWK ELVAQRPPSG LISGALLFSV LSQIIICIGF 1020
QSLGFFWVKQ QPWYEVWHPK SDACNTTGSG FWNSSHVDNE TELDEHNIQN YENTTVFFIS 1080
SFQYLIVAIA FSKGKPFRQP CYKNYFFVFS VIFLYIFILF IMLYPVASVD QVLQIVCVPY 1140
QWRVTMLIIV LVNAFVSITV EESVDRWGKC CLPWALGCRK KTPKAKYMYL AQELLVDPEW 1200
PPKPQTTTEA KALVKENGSC QIITIT 1226 
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
 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
 PF00690; Cation_ATPase_N
 PF00122; E1-E2_ATPase
 PF12409; P5-ATPase 
SMART
  
PROSITE
 PS00154; ATPASE_E1_E2 
PRINTS
 PR00119; CATATPASE.