CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000793
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable phospholipid-transporting ATPase IIB 
Protein Synonyms/Alias
 ATPase class II type 9B 
Gene Name
 ATP9B 
Gene Synonyms/Alias
 ATPIIB; NEO1L; HUSSY-20 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
481TQNEMIFKRLHLGTVubiquitination[1]
711ESRYTQAKLSMHDRSubiquitination[1]
897GIEGKEGKQASLAADubiquitination[1]
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
Functional Description
  
Sequence Annotation
 ACT_SITE 468 468 4-aspartylphosphate intermediate (By
 METAL 874 874 Magnesium (By similarity).
 METAL 878 878 Magnesium (By similarity).  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Golgi apparatus; Hydrolase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1147 AA 
Protein Sequence
MADQIPLYPV RSAAAAAANR KRAAYYSAAG PRPGADRHSR YQLEDESAHL DEMPLMMSEE 60
GFENEESDYH TLPRARIMQR KRGLEWFVCD GWKFLCTSCC GWLINICRRK KELKARTVWL 120
GCPEKCEEKH PRNSIKNQKY NVFTFIPGVL YEQFKFFLNL YFLVISCSQF VPALKIGYLY 180
TYWAPLGFVL AVTMTREAID EFRRFQRDKE VNSQLYSKLT VRGKVQVKSS DIQVGDLIIV 240
EKNQRIPSDM VFLRTSEKAG SCFIRTDQLD GETDWKLKVA VSCTQQLPAL GDLFSISAYV 300
YAQKPQMDIH SFEGTFTRED SDPPIHESLS IENTLWASTI VASGTVIGVV IYTGKETRSV 360
MNTSNPKNKV GLLDLELNRL TKALFLALVA LSIVMVTLQG FVGPWYRNLF RFLLLFSYII 420
PISLRVNLDM GKAVYGWMMM KDENIPGTVV RTSTIPEELG RLVYLLTDKT GTLTQNEMIF 480
KRLHLGTVSY GADTMDEIQS HVRDSYSQMQ SQAGGNNTGS TPLRKAQSSA PKVRKSVSSR 540
IHEAVKAIVL CHNVTPVYES RAGVTEETEF AEADQDFSDE NRTYQASSPD EVALVQWTES 600
VGLTLVSRDL TSMQLKTPSG QVLSFCILQL FPFTSESKRM GVIVRDESTA EITFYMKGAD 660
VAMSPIVQYN DWLEEECGNM AREGLRTLVV AKKALTEEQY QDFESRYTQA KLSMHDRSLK 720
VAAVVESLER EMELLCLTGV EDQLQADVRP TLEMLRNAGI KIWMLTGDKL ETATCIAKSS 780
HLVSRTQDIH IFRQVTSRGE AHLELNAFRR KHDCALVISG DSLEVCLKYY EHEFVELACQ 840
CPAVVCCRCS PTQKARIVTL LQQHTGRRTC AIGDGGNDVS MIQAADCGIG IEGKEGKQAS 900
LAADFSITQF RHIGRLLMVH GRNSYKRSAA LGQFVMHRGL IISTMQAVFS SVFYFASVPL 960
YQGFLMVGYA TIYTMFPVFS LVLDQDVKPE MAMLYPELYK DLTKGRSLSF KTFLIWVLIS 1020
IYQGGILMYG ALVLFESEFV HVVAISFTAL ILTELLMVAL TVRTWHWLMV VAEFLSLGCY 1080
VSSLAFLNEY FGIGRVSFGA FLDVAFITTV TFLWKVSAIT VVSCLPLYVL KYLRRKLSPP 1140
SYCKLAS 1147 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; NAS:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
 GO:0015247; F:aminophospholipid transporter activity; NAS:UniProtKB.
 GO:0005524; F:ATP binding; NAS:UniProtKB.
 GO:0019829; F:cation-transporting ATPase activity; NAS:UniProtKB.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0004012; F:phospholipid-translocating ATPase activity; IEA:EC.
 GO:0072600; P:establishment of protein localization to Golgi; IMP:UniProtKB.
 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.