CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023685
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable phospholipid-transporting ATPase IA 
Protein Synonyms/Alias
 ATPase class I type 8A member 1; Chromaffin granule ATPase II 
Gene Name
 ATP8A1 
Gene Synonyms/Alias
 ATPIA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
27KTDDVSEKTSLADQEubiquitination[1]
1075EVQELEAKSQDPGAVubiquitination[1]
1086PGAVVLGKSLTERAQubiquitination[1]
1143IRAYDTTKQRPDEW*ubiquitination[1]
Reference
 [1] 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
Functional Description
 May play a role in the transport of aminophospholipids from the outer to the inner leaflet of various membranes and the maintenance of asymmetric distribution of phospholipids, mainly in secretory vesicles. 
Sequence Annotation
 NP_BIND 741 748 ATP (Potential).
 NP_BIND 1095 1102 ATP (Potential).
 ACT_SITE 409 409 4-aspartylphosphate intermediate (By
 METAL 801 801 Magnesium (By similarity).
 METAL 805 805 Magnesium (By similarity).
 MOD_RES 9 9 Phosphoserine (By similarity).
 MOD_RES 25 25 Phosphoserine.
 MOD_RES 28 28 Phosphothreonine (By similarity).
 MOD_RES 29 29 Phosphoserine (By similarity).
 MOD_RES 269 269 Phosphotyrosine (By similarity).  
Keyword
 Alternative splicing; ATP-binding; Cell membrane; Complete proteome; Cytoplasmic vesicle; Endoplasmic reticulum; Hydrolase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1164 AA 
Protein Sequence
MPTMRRTVSE IRSRAEGYEK TDDVSEKTSL ADQEEVRTIF INQPQLTKFC NNHVSTAKYN 60
IITFLPRFLY SQFRRAANSF FLFIALLQQI PDVSPTGRYT TLVPLLFILA VAAIKEIIED 120
IKRHKADNAV NKKQTQVLRN GAWEIVHWEK VAVGEIVKVT NGEHLPADLI SLSSSEPQAM 180
CYIETSNLDG ETNLKIRQGL PATSDIKDVD SLMRISGRIE CESPNRHLYD FVGNIRLDGH 240
GTVPLGADQI LLRGAQLRNT QWVHGIVVYT GHDTKLMQNS TSPPLKLSNV ERITNVQILI 300
LFCILIAMSL VCSVGSAIWN RRHSGKDWYL NLNYGGASNF GLNFLTFIIL FNNLIPISLL 360
VTLEVVKFTQ AYFINWDLDM HYEPTDTAAM ARTSNLNEEL GQVKYIFSDK TGTLTCNVMQ 420
FKKCTIAGVA YGQNSQFGDE KTFSDSSLLE NLQNNHPTAP IICEFLTMMA VCHTAVPERE 480
GDKIIYQAAS PDEGALVRAA KQLNFVFTGR TPDSVIIDSL GQEERYELLN VLEFTSARKR 540
MSVIVRTPSG KLRLYCKGAD TVIYDRLAET SKYKEITLKH LEQFATEGLR TLCFAVAEIS 600
ESDFQEWRAV YQRASTSVQN RLLKLEESYE LIEKNLQLLG ATAIEDKLQD QVPETIETLM 660
KADIKIWILT GDKQETAINI GHSCKLLKKN MGMIVINEGS LDGTRETLSR HCTTLGDALR 720
KENDFALIID GKTLKYALTF GVRQYFLDLA LSCKAVICCR VSPLQKSEVV EMVKKQVKVV 780
TLAIGDGAND VSMIQTAHVG VGISGNEGLQ AANSSDYSIA QFKYLKNLLM IHGAWNYNRV 840
SKCILYCFYK NIVLYIIEIW FAFVNGFSGQ ILFERWCIGL YNVMFTAMPP LTLGIFERSC 900
RKENMLKYPE LYKTSQNALD FNTKVFWVHC LNGLFHSVIL FWFPLKALQY GTAFGNGKTS 960
DYLLLGNFVY TFVVITVCLK AGLETSYWTW FSHIAIWGSI ALWVVFFGIY SSLWPAIPMA 1020
PDMSGEAAML FSSGVFWMGL LFIPVASLLL DVVYKVIKRT AFKTLVDEVQ ELEAKSQDPG 1080
AVVLGKSLTE RAQLLKNVFK KNHVNLYRSE SLQQNLLHGY AFSQDENGIV SQSEVIRAYD 1140
TTKQRPDEW 1149 
Gene Ontology
 GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
 GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; NAS:UniProtKB.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 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: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.