CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039897
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Probable phospholipid-transporting ATPase IK 
Protein Synonyms/Alias
  
Gene Name
 ATP8B3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55RNSAFTWKVQANNRAubiquitination[1]
70YNGQFKEKVILCWQRubiquitination[1]
172PCQILMGKSFKQKKWubiquitination[1]
178GKSFKQKKWQDLCVGubiquitination[1]
243KELATIKKMASFQGTubiquitination[1]
273CLEWNDKKYSLDIGNubiquitination[1]
443VEYIFSDKTGTLTQNubiquitination[1, 2]
456QNILTFNKCCISGRVubiquitination[1]
480PAGSSIFKGLRVPENubiquitination[1, 3, 4, 5]
Reference
 [1] 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]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [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]
 [4] 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]
 [5] 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
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 562 AA 
Protein Sequence
MGDSPGRGAP ERRHKAQPGR ARKYEWRPEG PTSMGSLGQR EDLQDEDRNS AFTWKVQANN 60
RAYNGQFKEK VILCWQRKKY KTNVIRTAKY NFYSFLPLNL YEQFHRVSNL FFLIIIILQS 120
IPDISTLPWF SLSTPMVCLL FIRATRDLVD DMGRHKSDRA INNRPCQILM GKSFKQKKWQ 180
DLCVGDVVCL RKDNIVPADM LLLASTEPSS LCYVETVDID GETNLKFRQA LMVTHKELAT 240
IKKMASFQGT VTCEAPNSRM HHFVGCLEWN DKKYSLDIGN LLLRGCRIRN TDTCYGLVIY 300
AGFDTKIMKN CGKIHLKRTK LDLLMNKLVV VIFISVVLVC LVLAFGFGFS VKEFKDHHYY 360
LSGVHGSSVA AESFFVFWSF LILLSVTIPM SMFILSEFIY LGNSVFIDWD VQMYYKPQDV 420
PAKARSTSLN DHLGQVEYIF SDKTGTLTQN ILTFNKCCIS GRVYGAAPTP ELPAGSSIFK 480
GLRVPENQSH VWPHAQHLRP NLNQGTVARW PGFLWRGPGK FFFFFEAESH SVYPGRNAVV 540
QSWLTAISTS QVQAILLAQP PE 562 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:InterPro.
 GO:0005524; F:ATP binding; 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. 
Pfam
 PF00122; E1-E2_ATPase 
SMART
  
PROSITE
 PS00154; ATPASE_E1_E2 
PRINTS