CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010850
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 AMP deaminase 2 
Protein Synonyms/Alias
 AMP deaminase isoform L 
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
109PGPAPCLKHFPLDLRubiquitination[1]
229VTISGEEKCGVPFTDubiquitination[1]
242TDLLDAAKSVVRALFubiquitination[1]
276YLQQLAEKPLETRTYubiquitination[1]
489NTFHRFDKFNAKYNPubiquitination[1]
493RFDKFNAKYNPIGESubiquitination[2]
508VLREIFIKTDNRVSGubiquitination[1]
516TDNRVSGKYFAHIIKacetylation[3]
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] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 AMP deaminase plays a critical role in energy metabolism. 
Sequence Annotation
 REGION 489 494 Substrate binding (By similarity).
 REGION 765 768 Substrate binding (By similarity).
 ACT_SITE 709 709 Proton acceptor (By similarity).
 METAL 418 418 Zinc; catalytic (By similarity).
 METAL 420 420 Zinc; catalytic (By similarity).
 METAL 687 687 Zinc; catalytic (By similarity).
 METAL 764 764 Zinc; catalytic (By similarity).
 BINDING 420 420 Substrate (By similarity).
 BINDING 690 690 Substrate (By similarity).
 MOD_RES 76 76 Phosphoserine.
 MOD_RES 118 118 Phosphoserine.
 MOD_RES 145 145 Phosphotyrosine (By similarity).
 MOD_RES 151 151 Phosphoserine.
 MOD_RES 168 168 Phosphoserine.
 MOD_RES 188 188 Phosphothreonine.
 MOD_RES 190 190 Phosphoserine.
 MOD_RES 192 192 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Hydrolase; Metal-binding; Nucleotide metabolism; Phosphoprotein; Polymorphism; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 879 AA 
Protein Sequence
MRNRGQGLFR LRSRCFLHQS LPLGAGRRKG LDVAEPGPSR CRSDSPAVAA VVPAMASYPS 60
GSGKPKAKYP FKKRASLQAS TAAPEARGGL GAPPLQSARS LPGPAPCLKH FPLDLRTSMD 120
GKCKEIAEEL FTRSLAESEL RSAPYEFPEE SPIEQLEERR QRLERQISQD VKLEPDILLR 180
AKQDFLKTDS DSDLQLYKEQ GEGQGDRSLR ERDVLEREFQ RVTISGEEKC GVPFTDLLDA 240
AKSVVRALFI REKYMALSLQ SFCPTTRRYL QQLAEKPLET RTYEQGPDTP VSADAPVHPP 300
ALEQHPYEHC EPSTMPGDLG LGLRMVRGVV HVYTRREPDE HCSEVELPYP DLQEFVADVN 360
VLMALIINGP IKSFCYRRLQ YLSSKFQMHV LLNEMKELAA QKKVPHRDFY NIRKVDTHIH 420
ASSCMNQKHL LRFIKRAMKR HLEEIVHVEQ GREQTLREVF ESMNLTAYDL SVDTLDVHAD 480
RNTFHRFDKF NAKYNPIGES VLREIFIKTD NRVSGKYFAH IIKEVMSDLE ESKYQNAELR 540
LSIYGRSRDE WDKLARWAVM HRVHSPNVRW LVQVPRLFDV YRTKGQLANF QEMLENIFLP 600
LFEATVHPAS HPELHLFLEH VDGFDSVDDE SKPENHVFNL ESPLPEAWVE EDNPPYAYYL 660
YYTFANMAML NHLRRQRGFH TFVLRPHCGE AGPIHHLVSA FMLAENISHG LLLRKAPVLQ 720
YLYYLAQIGI AMSPLSNNSL FLSYHRNPLP EYLSRGLMVS LSTDDPLQFH FTKEPLMEEY 780
SIATQVWKLS SCDMCELARN SVLMSGFSHK VKSHWLGPNY TKEGPEGNDI RRTNVPDIRV 840
GYRYETLCQE LALITQAVQS EMLETIPEEA GITMSPGPQ 879 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0003876; F:AMP deaminase activity; NAS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
 GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
 GO:0006163; P:purine nucleotide metabolic process; NAS:UniProtKB.
 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