CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023684
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]
594KYKEITLKHLEQFATubiquitination[2, 3]
922CRKENMLKYPELYKTubiquitination[2, 3]
1078VIKRTAFKTLVDEVQubiquitination[1]
1090EVQELEAKSQDPGAVubiquitination[4]
1101PGAVVLGKSLTERAQubiquitination[2, 3, 4, 5, 6]
1111TERAQLLKNVFKKNHubiquitination[2, 3]
1158IRAYDTTKQRPDEW*ubiquitination[4]
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] 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]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] 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]
 [5] 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]
 [6] 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
 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 YGHVPEPEDY GCSPDEWQNS QFGDEKTFSD SSLLENLQNN HPTAPIICEF 480
LTMMAVCHTA VPEREGDKII YQAASPDEGA LVRAAKQLNF VFTGRTPDSV IIDSLGQEER 540
YELLNVLEFT SARKRMSVIV RTPSGKLRLY CKGADTVIYD RLAETSKYKE ITLKHLEQFA 600
TEGLRTLCFA VAEISESDFQ EWRAVYQRAS TSVQNRLLKL EESYELIEKN LQLLGATAIE 660
DKLQDQVPET IETLMKADIK IWILTGDKQE TAINIGHSCK LLKKNMGMIV INEGSLDGTR 720
ETLSRHCTTL GDALRKENDF ALIIDGKTLK YALTFGVRQY FLDLALSCKA VICCRVSPLQ 780
KSEVVEMVKK QVKVVTLAIG DGANDVSMIQ TAHVGVGISG NEGLQAANSS DYSIAQFKYL 840
KNLLMIHGAW NYNRVSKCIL YCFYKNIVLY IIEIWFAFVN GFSGQILFER WCIGLYNVMF 900
TAMPPLTLGI FERSCRKENM LKYPELYKTS QNALDFNTKV FWVHCLNGLF HSVILFWFPL 960
KALQYGTAFG NGKTSDYLLL GNFVYTFVVI TVCLKAGLET SYWTWFSHIA IWGSIALWVV 1020
FFGIYSSLWP AIPMAPDMSG EAAMLFSSGV FWMGLLFIPV ASLLLDVVYK VIKRTAFKTL 1080
VDEVQELEAK SQDPGAVVLG KSLTERAQLL KNVFKKNHVN LYRSESLQQN LLHGYAFSQD 1140
ENGIVSQSEV IRAYDTTKQR PDEW 1164 
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.