CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-028765
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Probable phospholipid-transporting ATPase IIA 
Protein Synonyms/Alias
  
Gene Name
 Atp9a 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
106VWLGHPEKRDQRYPRubiquitination[1]
190IRCYVRDKEMNSQVYphosphoglycerylation[2]
239IFLRTSEKNGSCFLRubiquitination[1]
544TDQAEAEKQFEDSCRubiquitination[1]
680EARYVQAKLSVHDRSubiquitination[1]
957LVLDKDVKSEVAMLYubiquitination[1]
969MLYPELYKDLLKGRPubiquitination[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]
 [2] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237] 
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Hydrolase; Magnesium; Membrane; Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1105 AA 
Protein Sequence
MVRPCPSVGP RGRLRAWPGA RDLAPALRAR PARCRRLLPL PRGGAEAAGS AGGAAGGDMT 60
DSIPLQPVRH KKRVDSRPRA GCCEWLRCCG GGEPRPRTVW LGHPEKRDQR YPRNVINNQK 120
YNFFTFLPGV LFSQFRYFFN FYFLLLACSQ FVPEMRLGAL YTYWVPLGFV LAVTIIREAV 180
EEIRCYVRDK EMNSQVYSRL TSRGTVKVKS SNIQVGDLIL VEKNQRVPAD MIFLRTSEKN 240
GSCFLRTDQL DGETDWKLRL PVACTQRLPT AADLLQIRSY VYAEEPNIDI HNFLGTFTRE 300
DSDPPISESL SIENTLWAGT VIASGTVVGV VLYTGRELRS VMNTSDPRSK IGLFDLEVNC 360
LTKILFGALV VVSLVMVALQ HFAGRWYLQI IRFLLLFSNI IPISLRVNLD MGKIVYSWVI 420
RRDSKIPGTV VRSSTIPEQL GRISYLLTDK TGTLTQNEMV FKRLHLGTVA YGLDSMDEVQ 480
SHIFSIYTQQ SQDPPAQKGP TVTTKVRRTM SSRVHEAVKA IALCHNVTPV YESNGVTDQA 540
EAEKQFEDSC RVYQASSPDE VALVQWTESV GLTLVGRDQS SMQLRTPGDQ VLNLTILQVF 600
PFTYESKRMG IIVRDESTGE ITFYMKGADV VMAGIVQYND WLEEECGNMA REGLRVLVVA 660
KKSLTEEQYQ DFEARYVQAK LSVHDRSLKV ATVIESLEME MELLCLTGVE DQLQADVRPT 720
LETLRNAGIK VWMLTGDKLE TATCTAKNAH LVTRNQDIHV FRLVTNRGEA HLELNAFRRK 780
HDCALVISGD SLEVCLKYYE YEFMELACQC PAVVCCRCAP TQKAQIVRLL QERTGKLTCA 840
VGDGGNDVSM IQESDCGVGV EGKEGKQASL AADFSITQFK HLGRLLMVHG RNSYKRSAAL 900
SQFVIHRSLC ISTMQAVFSS VFYFASVPLY QGFLIIGYST IYTMFPVFSL VLDKDVKSEV 960
AMLYPELYKD LLKGRPLSYK TFLIWVLISI YQGSTIMYGA LLLFESEFVH IVAISFTSLI 1020
LTELLMVALT IQTWHWLMTV AELLSLACYI ASLVFLHEFI DVYFIATLSF LWKVSVITLV 1080
SCLPLYVLKY LRRRFSPPSY SKLTS 1105 
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:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0004012; F:phospholipid-translocating ATPase activity; IEA:InterPro. 
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.