CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-043998
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Probable phospholipid-transporting ATPase IF 
Protein Synonyms/Alias
  
Gene Name
 ATP11B 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
229ECSINGMKYQEINGRubiquitination[1]
413CIGGEIEKTRIHVDEubiquitination[2]
424HVDEFALKGLRTLCIubiquitination[1]
537ILELINQKSDSECAEubiquitination[2]
Reference
 [1] 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]
 [2] 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
  
Keyword
 ATP-binding; Complete proteome; Hydrolase; Magnesium; Membrane; Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 970 AA 
Protein Sequence
XLDTLVAVIE CQQPEADLYR FMGRMIITQQ MEEIVRPLGP ESLLLRGARL KNTKEIFGVA 60
VYTGMETKMA LNYKSKSQKR SAVEKSMNTF LIIYLVILIS EAVISTILKY TWQAEEKWDE 120
PWYNQKTEHQ RNSSKILRFI SDFLAFLVLY NFIIPISLYV TVEMQKFLGS FFIGWDLDLY 180
HEESDQKAQV NTSDLNEELG QVEYVFTDKT GTLTENEMQF RECSINGMKY QEINGRLVPE 240
GPTPDSSEGN LSYLSSLSHL NNLSHLTTSS SFRTSPENET ELIKEHDLFF KAVSLCHTVQ 300
ISNVQTDCTG DGPWQSNLAP SQLEYYASSP DEKALVEAAA RIGIVFIGNS EETMEVKTLG 360
KLERYKLLHI LEFDSDRRRM SVIVQAPSGE KLLFAKGAES SILPKCIGGE IEKTRIHVDE 420
FALKGLRTLC IAYRKFTSKE YEEIDKRIFE ARTALQQREE KLAAVFQFIE KDLILLGATA 480
VEDRLQDKVR ETIEALRMAG IKVWVLTGDK HETAVSVSLS CGHFHRTMNI LELINQKSDS 540
ECAEQLRQLA RRITEDHVIQ HGLVVDGTSL SLALREHEKL FMEVCRNCSA VLCCRMAPLQ 600
KAKVIRLIKI SPEKPITLAV GDGANDVSMI QEAHVGIGIM GKEGRQAARN SDYAIARFKF 660
LSKLLFVHGH FYYIRIATLV QYFFYKNVCF ITPQFLYQFY CLFSQQTLYD SVYLTLYNIC 720
FTSLPILIYS LLEQHVDPHV LQNKPTLYRD ISKNRLLSIK TFLYWTILGF SHAFIFFFGS 780
YLLIGKDTSL LGNGQMFGNW TFGTLVFTVM VITVTVKMAL ETHFWTWINH LVTWGSIIFY 840
FVFSLFYGGI LWPFLGSQNM YFVFIQLLSS GSAWFAIILM VVTCLFLDII KKVFDRHLHP 900
TSTEKAQMYS NTVALSDEFI ALQPLSRARN QLSKLSLLKQ MQVSSAWTPC AVSRKEKQRV 960
HLLEECWNEL 970 
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.
 IPR001757; Cation_transp_P_typ_ATPase.
 IPR023214; HAD-like_dom. 
Pfam
 PF00702; Hydrolase 
SMART
  
PROSITE
 PS00154; ATPASE_E1_E2 
PRINTS
 PR00119; CATATPASE.