CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-040310
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Probable phospholipid-transporting ATPase IA 
Protein Synonyms/Alias
  
Gene Name
 Atp8a1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
26KTDDVSEKTSLADQEubiquitination[1]
159VGDIVIIKGKEYIPAubiquitination[1]
206LPATSDIKDIDSLMRubiquitination[1]
497VPEREGDKIIYQAASubiquitination[1]
515GALVRAAKQLNFVFTubiquitination[1]
593KYKEITLKHLEQFATubiquitination[1]
921CRKENMLKYPELYKTubiquitination[1]
1089EVQELEAKSQDPGAVubiquitination[1]
1100PGAVVLGKSLTERAQubiquitination[1]
1110TERAQLLKNVFKKNHubiquitination[1]
1157IRAYDTTKQRPDEW*ubiquitination[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
  
Keyword
 ATP-binding; Complete proteome; Hydrolase; Magnesium; Membrane; Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1163 AA 
Protein Sequence
XTMRRTVSEI RSRAEGYEKT DDVSEKTSLA DQEEVRTIFI NQPQLTKFCN NHVSTAKYNV 60
ITFLPRFLYS QFRRAANSFF LFIALLQQIP DVSPTGRYTT LVPLLFILAV AAIKEIIEDI 120
KRHKADNAVN KKQTQVLRNG AWEIVHWEKV NVGDIVIIKG KEYIPADTVL LSSSEPQAMC 180
YIETSNLDGE TNLKIRQGLP ATSDIKDIDS LMRISGRIEC ESPNRHLYDF VGNIRLDGHG 240
TVPLGADQIL LRGAQLRNTQ WVHGIVVYTG HDTKLMQNST SPPLKLSNVE RITNVQILIL 300
FCILIAMSLV CSVGSAIWNR RHSGKDWYLH LHYGGASNFG LNFLTFIILF NNLIPISLLV 360
TLEVVKFTQA YFINWDLDMH YEPTDTAAMA RTSNLNEELG QVKYIFSDKT GTLTCNVMQF 420
KKCTIAGVAY GHVPEPEDYG CSPDEWQSSQ FGDEKTFNDP SLLDNLQNNH PTAPIICEFL 480
TMMAVCHTAV PEREGDKIIY QAASPDEGAL VRAAKQLNFV FTGRTPDSVI IDSLGQEERY 540
ELLNVLEFTS ARKRMSVVVR TPSGKLRLYC KGADTVIYER LAETSKYKEI TLKHLEQFAT 600
EGLRTLCFAV AEISESDFEE WRAVYHRAST SVQNRLLKLE ESYELIEKNL QLLGATAIED 660
KLQDQVPETI ETLMKADIKI WILTGDKQET AINIGHSCRL LKRNMGMIVI NEGSLDGTRE 720
TLSRHCTTLG DALRKENDFA LIIDGKTLKY ALTFGVRQYF LDLALSCKAV ICCRVSPLQK 780
SEVVEMVKKQ VKVITLAIGD GANDVSMIQT AHVGVGISGN EGLQAANSSD YSIAQFKYLK 840
NLLMVHGAWN YNRVSKCILY CFYKNIVLYI IEIWFAFVNG FSGQILFERW CIGLYNVMFT 900
AMPPLTLGIF ERSCRKENML KYPELYKTSQ NALDFNTKVF WVHCLNGLFH SVILFWFPLK 960
ALQYGTVFGN GKTSDYLLLG NFVYTFVVIT VCLKAGLETS YWTWFSHIAI WGSIALWVVF 1020
FGIYSSLWPA VPMAPDMSGE AAMLFSSGVF WVGLLSIPVA SLLLDVLYKV IKRTAFKTLV 1080
DEVQELEAKS QDPGAVVLGK SLTERAQLLK NVFKKNHVNL YRSESLQQNL LHGYAFSQDE 1140
NGIVSQSEVI RAYDTTKQRP DEW 1163 
Gene Ontology
 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:InterPro. 
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.