CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-028191
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 CG32549, isoform E 
Protein Synonyms/Alias
 GH28326p 
Gene Name
 CG32549-RE 
Gene Synonyms/Alias
 CG32549; Dmel_CG32549 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
18QPQPQQQKPLQKHSSacetylation[1]
Reference
 [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702] 
Functional Description
  
Sequence Annotation
 ACT_SITE 95 95 Nucleophile (By similarity).
 ACT_SITE 97 97 Proton donor (By similarity).
 METAL 95 95 Magnesium (By similarity).
 METAL 97 97 Magnesium; via carbonyl oxygen (By
 METAL 394 394 Magnesium (By similarity).  
Keyword
 Complete proteome; Hydrolase; Magnesium; Metal-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 630 AA 
Protein Sequence
MPQPKQNQQK QPQPQQQKPL QKHSSTSSTI IAKPEKERER TQTIGETDMD QSVLNGLAVG 60
ADGTAGYHGH KRELGHRVFV NRSLHLENIK YYGFDMDYTL AEYKSPQYEQ LGFNLVKERL 120
VFMGYPKEIL QFEYDPTFPV RGLWFDTLYG NLLKVDAYGN ILVCVHGFEF IKHHQVYELY 180
PNKFLKLDES RVYVLNTLFN LPETYLLACL VDFLTNSSDF VRVERGIKAG DLLFTYKSIF 240
QDVRRAVDWV HSDGDLKRRT TQNMAHYVKK DERLPTVLSR IRESGAKLFM LTNSDYTYTN 300
EIMTYLFDFP HGATPDEPHR DWKTYFDVIV VDARKPLFFD EGTVLRQVDT KTGSLKIGTH 360
VGPLQPGQVY SGGSCELFTK FINAKGKDVL YVGDHIFGDI LKSKKIRGWR TFLIVPELVR 420
ELHVWTDECQ LFAELQNLDI KLGDLYRDLD SSAKVKPDIS QLRTCIRDVT HKMDMSYGMM 480
GSLFRSGSRQ TFFSSQVVRY ADVYAATLLN LIYYPFSYMF RAPAMLLPHE STVAHDQAHQ 540
PPPPLGPVPV PATGAASVAA SPDEPARILA GTAEHVKDPK DLHRASSIVH TRPSTPTVVT 600
HTHDEDYSEE EETPSGAESS TEAVRDASED 630 
Gene Ontology
 GO:0008253; F:5'-nucleotidase activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 
Interpro
 IPR023214; HAD-like_dom.
 IPR008380; HAD-SF_hydro_IG_5-nucl.
 IPR016695; Pur_nucleotidase. 
Pfam
 PF05761; 5_nucleotid 
SMART
  
PROSITE
  
PRINTS