CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010730
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable phospholipid-transporting ATPase IH 
Protein Synonyms/Alias
 ATPase IS; ATPase class VI type 11A 
Gene Name
 ATP11A 
Gene Synonyms/Alias
 ATPIH; ATPIS; KIAA1021 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
529GFTYLRLKDNYMEILubiquitination[1]
590FPRVIEGKVDQIRARubiquitination[1, 2]
632CKLLQAAKVALQDREubiquitination[1]
668VEDRLQEKAADTIEAubiquitination[1]
678DTIEALQKAGIKVWVubiquitination[1]
702AATCYACKLFRRNTQubiquitination[3]
716QLLELTTKRIEEQSLubiquitination[1, 2]
732DVLFELSKTVLRHSGubiquitination[2]
809LQKAQIVKLIKFSKEubiquitination[1]
812AQIVKLIKFSKEHPIubiquitination[2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] 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]
 [3] 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] 
Functional Description
  
Sequence Annotation
 ACT_SITE 414 414 4-aspartylphosphate intermediate (By
 METAL 825 825 Magnesium (By similarity).
 METAL 829 829 Magnesium (By similarity).  
Keyword
 ATP-binding; Cell membrane; Complete proteome; Endoplasmic reticulum; Endosome; Hydrolase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1134 AA 
Protein Sequence
MDCSLVRTLV HRYCAGEENW VDSRTIYVGH REPPPGAEAY IPQRYPDNRI VSSKYTFWNF 60
IPKNLFEQFR RVANFYFLII FLVQLIIDTP TSPVTSGLPL FFVITVTAIK QGYEDWLRHK 120
ADNAMNQCPV HFIQHGKLVR KQSRKLRVGD IVMVKEDETF PCDLIFLSSN RGDGTCHVTT 180
ASLDGESSHK THYAVQDTKG FHTEEDIGGL HATIECEQPQ PDLYKFVGRI NVYSDLNDPV 240
VRPLGSENLL LRGATLKNTE KIFGVAIYTG METKMALNYQ SKSQKRSAVE KSMNAFLIVY 300
LCILISKALI NTVLKYMWQS EPFRDEPWYN QKTESERQRN LFLKAFTDFL AFMVLFNYII 360
PVSMYVTVEM QKFLGSYFIT WDEDMFDEET GEGPLVNTSD LNEELGQVEY IFTDKTGTLT 420
ENNMEFKECC IEGHVYVPHV ICNGQVLPES SGIDMIDSSP SVNGREREEL FFRALCLCHT 480
VQVKDDDSVD GPRKSPDGGK SCVYISSSPD EVALVEGVQR LGFTYLRLKD NYMEILNREN 540
HIERFELLEI LSFDSVRRRM SVIVKSATGE IYLFCKGADS SIFPRVIEGK VDQIRARVER 600
NAVEGLRTLC VAYKRLIQEE YEGICKLLQA AKVALQDREK KLAEAYEQIE KDLTLLGATA 660
VEDRLQEKAA DTIEALQKAG IKVWVLTGDK METAAATCYA CKLFRRNTQL LELTTKRIEE 720
QSLHDVLFEL SKTVLRHSGS LTRDNLSGLS ADMQDYGLII DGAALSLIMK PREDGSSGNY 780
RELFLEICRS CSAVLCCRMA PLQKAQIVKL IKFSKEHPIT LAIGDGANDV SMILEAHVGI 840
GVIGKEGRQA ARNSDYAIPK FKHLKKMLLV HGHFYYIRIS ELVQYFFYKN VCFIFPQFLY 900
QFFCGFSQQT LYDTAYLTLY NISFTSLPIL LYSLMEQHVG IDVLKRDPTL YRDVAKNALL 960
RWRVFIYWTL LGLFDALVFF FGAYFVFENT TVTSNGQIFG NWTFGTLVFT VMVFTVTLKL 1020
ALDTHYWTWI NHFVIWGSLL FYVVFSLLWG GVIWPFLNYQ RMYYVFIQML SSGPAWLAIV 1080
LLVTISLLPD VLKKVLCRQL WPTATERVQT KSQCLSVEQS TIFMLSQTSS SLSF 1134 
Gene Ontology
 GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
 GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0055037; C:recycling endosome; 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 
SMART
  
PROSITE
 PS00154; ATPASE_E1_E2 
PRINTS
 PR00119; CATATPASE.