CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010729
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
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
124VWLGCPEKCEEKHPRubiquitination[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
Functional Description
  
Sequence Annotation
 ACT_SITE 467 467 4-aspartylphosphate intermediate (By
 METAL 873 873 Magnesium (By similarity).
 METAL 877 877 Magnesium (By similarity).  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Golgi apparatus; Hydrolase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1146 AA 
Protein Sequence
MADQIPLYPV RSAGAAASHR RAAYYSSAGP GPGADRRGRY QLEDESAHLD EMPLMMSEEG 60
FENDESDYHT LPRARITRRK RGLEWFVCGG WKFLCTSCCD WLINVCQRKK ELKARTVWLG 120
CPEKCEEKHP RNSIKNQKYN VFTFIPGVLY EQFKFFLNLY FLVVSCSQFV PALKIGYLYT 180
YWAPLGFVLA VTIAREAIDE FRRFQRDKEM NSQLYSKLTV RGKVQVKSSD IQVGDLIIVE 240
KNQRIPSDMV FLRTSEKAGS CFIRTDQLDG ETDWKLKVAV SCTQRLPALG DLFSISAYVY 300
AQKPQLDIHS FEGTFTREDS DPPIHESLSI ENTLWASTIV ASGTVIGVVI YTGKETRSVM 360
NTSNPNNKVG LLDLELNQLT KALFLALVVL SVVMVTLQGF AGPWYRNLFR FLLLFSYIIP 420
ISLRVNLDMG KAAYGWMIMK DENIPGTVVR TSTIPEELGR LVYLLTDKTG TLTQNEMVFK 480
RLHLGTVSYG TDTMDEIQSH VLNSYLQVHS QPSGHNPSSA PLRRSQSSTP KVKKSVSSRI 540
HEAVKAIALC HNVTPVYEAR AGITGETEFA EADQDFSDEN RTYQASSPDE VALVRWTESV 600
GLTLVSRDLA SMQLKTPSGQ VLTYCILQMF PFTSESKRMG IIVRDESTAE ITFYMKGADV 660
AMSTIVQYND WLEEECGNMA REGLRTLVVA KRTLTEEQYQ DFESRYSQAK LSIHDRALKV 720
AAVVESLERE MELLCLTGVE DQLQADVRPT LEMLRNAGIK IWMLTGDKLE TATCIAKSSH 780
LVSRTQDIHV FRPVTSRGEA HLELNAFRRK HDCALVISGD SLEVCLRYYE HELVELACQC 840
PAVVCCRCSP TQKAHIVTLL RQHTRKRTCA IGDGGNDVSM IQAADCGIGI EGKEGKQASL 900
AADFSITQFR HIGRLLMVHG RNSYKRSAAL GQFVMHRGLI ISTMQAVFSS VFYFASVPLY 960
QGFLMVGYAT IYTMFPVFSL VLDQDVKPEM AILYPELYKD LTKGRSLSFK TFLIWVLISI 1020
YQGGILMYGA LLLFEDEFVH VVAISFTALI LTELLMVALT IRTWHWLMVV AEFLSLGCYV 1080
ASLAFLNEYF GIGRVSFGAF LDVAFITTVT FLWKVSAITV VSCLPLYVLK YLKRKLSPPS 1140
YSKLSS 1146 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
 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:EC. 
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.