CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039118
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Protein Atp8a1 
Protein Synonyms/Alias
  
Gene Name
 Atp8a1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
11KTDDVSEKTSLADQEubiquitination[1]
144VGDIVIIKGKEFIPAubiquitination[1]
556ERLAESSKYKEITLKacetylation[2]
631GATAIEDKLQDQVPEacetylation[2]
891CRKENMLKYPELYKTubiquitination[1]
Reference
 [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113]
 [2] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
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
 1133 AA 
Protein Sequence
GYEKTDDVSE KTSLADQEEV RTIFINQPQL TKFCNNHVST AKYNVITFLP RFLYSQFRRA 60
ANSFFLFIAL LQQIPDVSPT GRYTTLVPLL FILAVAAIKE IIEDIKRHKA DNAVNKKQTQ 120
VLRNGAWEIV HWEKVNVGDI VIIKGKEFIP ADTVLLSSSE PQAMCYIETS NLDGETNLKI 180
RQGLPATSDI KDIDSLMRIS GRIECESPNR HLYDFVGNIR LDGHGTVPLG ADQILLRGAQ 240
LRNTQWVHGI VVYTGHDTKL MQNSTSPPLK LSNVERITNV QILILFCILI AMSLVCSVGS 300
AIWNRRHSGK DWYLHLHYGG ASNFGLNFLT FIILFNNLIP ISLLVTLEVV KFTQAYFINW 360
DLDMHYEPTD TAAMARTSNL NEELGQVKYI FSDKTGTLTC NVMQFKKCTI AGVAYGQSSQ 420
FGDEKTFNDP SLLENLQNNH PTAPIICEFL TMMAVCHTAV PERDGEKIIY QAASPDEGAL 480
VRAAKQLNFV FTGRTPDSVI IDSLGQEERY ELLNVLEFTS SRKRMSVVVR TPSGKLRLYC 540
KGADTVIYER LAESSKYKEI TLKHLEQFAT EGLRTLCFAV AEISESDFEE WRAVYQRAST 600
SVQNRLLKLE ESYELIEKNL QLLGATAIED KLQDQVPETI ETLMKADIKI WILTGDKQET 660
AINIGHSCRL LRRNMGMIVI NEGSLDGTRE TLSRHCTTLG DALRKENDFA LIIDGKTLKY 720
ALTFGVRQYF LDLALSCKAV ICCRVSPLQK SEVVEMVKKQ VKVITLAIGD GANDVSMIQT 780
AHVGVGISGN EGLQAANSSD YSIAQFKYLK NLLMVHGAWN YNRVSKCILY CFYKNIVLYI 840
IEIWFAFVNG FSGQILFERW CIGLYNVMFT AMPPLTLGIF ERSCRKENML KYPELYKTSQ 900
NALDFNTKVF WVHCLNGLFH SVILFWFPLK ALQYGTVFGN GKTSDYLLLG NFVYTFVVIT 960
VCLKAGLETS YWTWFSHIAI WGSIALWVVF FGIYSSLWPA VPMAPDMSGE AAMLFSSGVF 1020
WVGLLSIPVA SLLLDVLYKV IKRTAFKTLV DEVQELEAKS QDPGAVVLGK SLTERAQLLK 1080
NVFKKNHVNL YRSESLQQNL LHGYAFSQDE NGIVSQSEVI RAYDTTKQRP DEW 1133 
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.