CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001108
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable phospholipid-transporting ATPase IIA 
Protein Synonyms/Alias
 ATPase class II type 9A 
Gene Name
 ATP9A 
Gene Synonyms/Alias
 ATPIIA; KIAA0611 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
14LQPVRQKKRMDSRPRmethylation[1]
48VWLGHPEKRDQRYPRubiquitination[2, 3]
181IFLRTSEKNGSCFLRubiquitination[4, 5]
199LDGETDWKLRLPVACubiquitination[4]
367WVIRRDSKIPGTVVRubiquitination[4]
392ISYLLTDKTGTLTQNubiquitination[4]
404TQNEMIFKRLHLGTVubiquitination[4]
447KGPTLTTKVRRTMSSubiquitination[6]
486TDQAEAEKQYEDSCRubiquitination[4]
604RVLVVAKKSLAEEQYubiquitination[4]
622EARYVQAKLSVHDRSubiquitination[4]
680VWMLTGDKLETATCTubiquitination[4]
765CRCAPTQKAQIVRLLubiquitination[4]
778LLQERTGKLTCAVGDubiquitination[4]
805CGVGVEGKEGKQASLubiquitination[4]
911MLYPELYKDLLKGRPubiquitination[6]
1044FSPPSYSKLTS****ubiquitination[4]
Reference
 [1] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [2] 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]
 [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] 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]
 [5] 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]
 [6] 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] 
Functional Description
  
Sequence Annotation
 ACT_SITE 391 391 4-aspartylphosphate intermediate (By
 METAL 785 785 Magnesium (By similarity).
 METAL 789 789 Magnesium (By similarity).  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Endosome; Golgi apparatus; Hydrolase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1047 AA 
Protein Sequence
MTDNIPLQPV RQKKRMDSRP RAGCCEWLRC CGGGEARPRT VWLGHPEKRD QRYPRNVINN 60
QKYNFFTFLP GVLFNQFKYF FNLYFLLLAC SQFVPEMRLG ALYTYWVPLG FVLAVTVIRE 120
AVEEIRCYVR DKEVNSQVYS RLTARGTVKV KSSNIQVGDL IIVEKNQRVP ADMIFLRTSE 180
KNGSCFLRTD QLDGETDWKL RLPVACTQRL PTAADLLQIR SYVYAEEPNI DIHNFVGTFT 240
REDSDPPISE SLSIENTLWA GTVVASGTVV GVVLYTGREL RSVMNTSNPR SKIGLFDLEV 300
NCLTKILFGA LVVVSLVMVA LQHFAGRWYL QIIRFLLLFS NIIPISLRVN LDMGKIVYSW 360
VIRRDSKIPG TVVRSSTIPE QLGRISYLLT DKTGTLTQNE MIFKRLHLGT VAYGLDSMDE 420
VQSHIFSIYT QQSQDPPAQK GPTLTTKVRR TMSSRVHEAV KAIALCHNVT PVYESNGVTD 480
QAEAEKQYED SCRVYQASSP DEVALVQWTE SVGLTLVGRD QSSMQLRTPG DQILNFTILQ 540
IFPFTYESKR MGIIVRDEST GEITFYMKGA DVVMAGIVQY NDWLEEECGN MAREGLRVLV 600
VAKKSLAEEQ YQDFEARYVQ AKLSVHDRSL KVATVIESLE MEMELLCLTG VEDQLQADVR 660
PTLETLRNAG IKVWMLTGDK LETATCTAKN AHLVTRNQDI HVFRLVTNRG EAHLELNAFR 720
RKHDCALVIS GDSLEVCLKY YEYEFMELAC QCPAVVCCRC APTQKAQIVR LLQERTGKLT 780
CAVGDGGNDV SMIQESDCGV GVEGKEGKQA SLAADFSITQ FKHLGRLLMV HGRNSYKRSA 840
ALSQFVIHRS LCISTMQAVF SSVFYFASVP LYQGFLIIGY STIYTMFPVF SLVLDKDVKS 900
EVAMLYPELY KDLLKGRPLS YKTFLIWVLI SIYQGSTIMY GALLLFESEF VHIVAISFTS 960
LILTELLMVA LTIQTWHWLM TVAELLSLAC YIASLVFLHE FIDVYFIATL SFLWKVSVIT 1020
LVSCLPLYVL KYLRRRFSPP SYSKLTS 1047 
Gene Ontology
 GO:0005769; C:early endosome; IDA:UniProtKB.
 GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
 GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0055037; C:recycling endosome; IDA:UniProtKB.
 GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0004012; F:phospholipid-translocating ATPase activity; IEA:EC.
 GO:0045332; P:phospholipid translocation; NAS:UniProtKB. 
Interpro
 IPR023299; ATPase_P-typ_cyto_domN.
 IPR018303; ATPase_P-typ_P_site.
 IPR006539; ATPase_P-typ_Plipid-transp.
 IPR008250; ATPase_P-typ_transduc_dom_A.
 IPR001757; Cation_transp_P_typ_ATPase.
 IPR023214; HAD-like_dom. 
Pfam
 PF00122; E1-E2_ATPase
 PF00702; Hydrolase 
SMART
  
PROSITE
 PS00154; ATPASE_E1_E2 
PRINTS
 PR00119; CATATPASE.