CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010849
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 AMP deaminase 3 
Protein Synonyms/Alias
 AMP deaminase isoform E; Erythrocyte AMP deaminase 
Gene Name
 AMPD3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
32QVRLLAEKVFAKVLRubiquitination[1]
36LAEKVFAKVLREEDSubiquitination[1]
44VLREEDSKDALSLFTubiquitination[1]
70AKERELQKELAEQKSubiquitination[1]
76QKELAEQKSVETAKRubiquitination[1]
166QAAKSLAKALMIREKubiquitination[1]
307LNEMSEFKELKSNPHubiquitination[1]
310MSEFKELKSNPHRDFubiquitination[1]
357PDRTVAEKRGRKITLubiquitination[1]
401RFDKFNSKYNPVGASubiquitination[1]
416ELRDLYLKTENYLGGubiquitination[1]
431EYFARMVKEVARELEubiquitination[1]
441ARELEESKYQYSEPRubiquitination[1]
722LSHQEKQKFLGQNYYubiquitination[1]
730FLGQNYYKEGPEGNDubiquitination[1]
740PEGNDIRKTNVAQIRubiquitination[1]
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] 
Functional Description
 AMP deaminase plays a critical role in energy metabolism. 
Sequence Annotation
 REGION 388 393 Substrate binding (By similarity).
 REGION 664 667 Substrate binding (By similarity).
 ACT_SITE 608 608 Proton acceptor (By similarity).
 METAL 317 317 Zinc; catalytic (By similarity).
 METAL 319 319 Zinc; catalytic (By similarity).
 METAL 586 586 Zinc; catalytic (By similarity).
 METAL 663 663 Zinc; catalytic (By similarity).
 BINDING 319 319 Substrate (By similarity).
 BINDING 589 589 Substrate (By similarity).
 MOD_RES 107 107 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Disease mutation; Hydrolase; Metal-binding; Nucleotide metabolism; Phosphoprotein; Polymorphism; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 767 AA 
Protein Sequence
MALSSEPAEM PRQFPKLNIS EVDEQVRLLA EKVFAKVLRE EDSKDALSLF TVPEDCPIGQ 60
KEAKERELQK ELAEQKSVET AKRKKSFKMI RSQSLSLQMP PQQDWKGPPA ASPAMSPTTP 120
VVTGATSLPT PAPYAMPEFQ RVTISGDYCA GITLEDYEQA AKSLAKALMI REKYARLAYH 180
RFPRITSQYL GHPRADTAPP EEGLPDFHPP PLPQEDPYCL DDAPPNLDYL VHMQGGILFV 240
YDNKKMLEHQ EPHSLPYPDL ETYTVDMSHI LALITDGPTK TYCHRRLNFL ESKFSLHEML 300
NEMSEFKELK SNPHRDFYNV RKVDTHIHAA ACMNQKHLLR FIKHTYQTEP DRTVAEKRGR 360
KITLRQVFDG LHMDPYDLTV DSLDVHAGRQ TFHRFDKFNS KYNPVGASEL RDLYLKTENY 420
LGGEYFARMV KEVARELEES KYQYSEPRLS IYGRSPEEWP NLAYWFIQHK VYSPNMRWII 480
QVPRIYDIFR SKKLLPNFGK MLENIFLPLF KATINPQDHR ELHLFLKYVT GFDSVDDESK 540
HSDHMFSDKS PNPDVWTSEQ NPPYSYYLYY MYANIMVLNN LRRERGLSTF LFRPHCGEAG 600
SITHLVSAFL TADNISHGLL LKKSPVLQYL YYLAQIPIAM SPLSNNSLFL EYSKNPLREF 660
LHKGLHVSLS TDDPMQFHYT KEALMEEYAI AAQVWKLSTC DLCEIARNSV LQSGLSHQEK 720
QKFLGQNYYK EGPEGNDIRK TNVAQIRMAF RYETLCNELS FLSDAMKSEE ITALTN 776 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0003876; F:AMP deaminase activity; TAS:ProtInc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006196; P:AMP catabolic process; TAS:ProtInc.
 GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
 GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
 GO:0043101; P:purine-containing compound salvage; TAS:Reactome. 
Interpro
 IPR006650; A/AMP_deam_AS.
 IPR001365; A/AMP_deaminase_dom.
 IPR006329; AMP_deaminase. 
Pfam
 PF00962; A_deaminase 
SMART
  
PROSITE
 PS00485; A_DEAMINASE 
PRINTS