CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-042333
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 AMP deaminase 2 
Protein Synonyms/Alias
  
Gene Name
 AMPD2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
169DSDLQLYKEQGEGQGubiquitination[1]
200VTISGEEKCGVPFTDubiquitination[2]
213TDLLDAAKSVVRALFubiquitination[2]
247YLQQLAEKPLETRTYubiquitination[1, 2, 3]
460NTFHRFDKFNAKYNPubiquitination[2, 4]
464RFDKFNAKYNPIGESubiquitination[1]
479VLREIFIKTDNRVSGubiquitination[1, 2, 4]
504MSDLEESKYQNAELRubiquitination[1]
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] 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]
 [3] 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]
 [4] 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
 861 AA 
Protein Sequence
XLDVAEPGPS RCRSDSPAVA AVVPAMASYP SGSGKPKAKY PFKKRASLQA STAAPEARGG 60
LGAPPLQSAR SLPGPAPCLK HFPLDLRTSM DGKCKEIAEE LFTRSLAESE LRSAPYEFPE 120
ESPIEQLEER RQRLERQISQ DVKLEPDILL RAKQDFLKTD SDSDLQLYKE QGEGQGDRSL 180
RERDVLEREF QRVTISGEEK CGVPFTDLLD AAKSVVRALF IREKYMALSL QSFCPTTRRY 240
LQQLAEKPLE TRTYEQGPDT PVSADAPVHP PALEQHPYEH CEPSTMPGDL GLGLRMVRGV 300
VHVYTRREPD EHCSEVELPY PDLQEFVADV NVLMALIING PIKSFCYRRL QYLSSKFQMH 360
VLLNEMKELA AQKKVPHRDF YNIRKVDTHI HASSCMNQKH LLRFIKRAMK RHLEEIVHVE 420
QGREQTLREV FESMNLTAYD LSVDTLDVHA DRNTFHRFDK FNAKYNPIGE SVLREIFIKT 480
DNRVSGKYFA HIIKEVMSDL EESKYQNAEL RLSIYGRSRD EWDKLARWAV MHRVHSPNVR 540
WLVQVPRLFD VYRTKGQLAN FQEMLENIFL PLFEATVHPA SHPELHLFLE HVDGFDSVDD 600
ESKPENHVFN LESPLPEAWV EEDNPPYAYY LYYTFANMAM LNHLRRQRGF HTFVLRPHCG 660
EAGPIHHLVS AFMLAENISH GLLLRKAPVL QYLYYLAQIG IAMSPLSNNS LFLSYHRNPL 720
PEYLSRGLMV SLSTDDPLQF HFTKVRAQQA ARRAGEPLME EYSIATQVWK LSSCDMCELA 780
RNSVLMSGFS HKVKSHWLGP NYTKEGPEGN DIRRTNVPDI RVGYRYETLC QELALITQAV 840
QSEMLETIPE EAGITMSPGP Q 861 
Gene Ontology
 GO:0003876; F:AMP deaminase activity; IEA:InterPro.
 GO:0006188; P:IMP biosynthetic process; IEA:InterPro. 
Interpro
 IPR006650; A/AMP_deam_AS.
 IPR001365; A/AMP_deaminase_dom.
 IPR006329; AMP_deaminase. 
Pfam
 PF00962; A_deaminase 
SMART
  
PROSITE
 PS00485; A_DEAMINASE 
PRINTS