CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010945
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
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
462TDNKISGKYFAHIIKacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 AMP deaminase plays a critical role in energy metabolism. 
Sequence Annotation
 REGION 435 440 Substrate binding (By similarity).
 REGION 711 714 Substrate binding (By similarity).
 ACT_SITE 655 655 Proton acceptor (By similarity).
 METAL 364 364 Zinc; catalytic (By similarity).
 METAL 366 366 Zinc; catalytic (By similarity).
 METAL 633 633 Zinc; catalytic (By similarity).
 METAL 710 710 Zinc; catalytic (By similarity).
 BINDING 366 366 Substrate (By similarity).
 BINDING 636 636 Substrate (By similarity).
 MOD_RES 21 21 Phosphoserine (By similarity).
 MOD_RES 63 63 Phosphoserine (By similarity).
 MOD_RES 90 90 Phosphotyrosine (By similarity).
 MOD_RES 96 96 Phosphoserine (By similarity).
 MOD_RES 113 113 Phosphoserine (By similarity).
 MOD_RES 133 133 Phosphothreonine (By similarity).
 MOD_RES 135 135 Phosphoserine (By similarity).
 MOD_RES 137 137 Phosphoserine (By similarity).  
Keyword
 Complete proteome; Hydrolase; Metal-binding; Nucleotide metabolism; Phosphoprotein; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 824 AA 
Protein Sequence
MASYPGPGKS KAKYPFKKRA SLQASAAAPE ARSGLGASPL QSARSLPGTA PCLKHFPLDL 60
RTSMDGKCKE IAEELFSRSL AESELRSAPY EFPEESPIEQ LEERRQRLER QISQDVKLEP 120
DILLRAKQDF LKTDSDSDLQ LYKEQGEGQG DRGLWERDVV LEREFQRVII SGEEKCGVPF 180
TDLLDAAKSV VRALFIREKY MALSLQSFCP TTRRYLQQLA EKPLETRTYE QSPDTPVSAD 240
APVHPPALEQ HPYEHCEPST MPGDLGLGLR MVRGVVHVYT RRDPDEHCPE VELPYPDLQE 300
FVADVNVLMA LIINGPIKSF CYRRLQYLSS KFQMHVLLNE MKELAAQKKV PHRDFYNIRK 360
VDTHIHASSC MNQKHLLRFI KRAMKRHLEE IVHVEQGREQ TLREVFESMN LTAYDLSVDT 420
LDVHADRNTF HRFDKFNAKY NPIGESVLRE IFIKTDNKIS GKYFAHIIKE VMSDLEESKY 480
QNAELRLSIY GRSRDEWDKL ARWAVNHRVH SPNVRWLVQV PRLFDVYRTK GQLANFQEML 540
ENIFLPLFEA TVHPASHPEL HLFLEHVDGF DSVDDESKPE NHVFNLESPL PEAWVEEDNP 600
PYAYYLYYTF ANMAMLNHLR RQRGFHTFVL RPHCGEAGPI HHLVSAFMLA ENISHGLLLR 660
KAPVLQYLYY LAQIGIAMSP LSNNSLFLSY HRNPLPEYLS RGLMVSLSTD DPLQFHFTKE 720
PLMEEYSIAT QVWKLSSCDM CELARNSVLM SGFSHKVKSH WLGPNYTKEG PEGNDIRRTN 780
VPDIRVGYRY ETLCQELALI TQAVQSEMLE TIPEEVGIVM SPGP 824 
Gene Ontology
 GO:0003876; F:AMP deaminase activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway. 
Interpro
 IPR006650; A/AMP_deam_AS.
 IPR001365; A/AMP_deaminase_dom.
 IPR006329; AMP_deaminase. 
Pfam
 PF00962; A_deaminase 
SMART
  
PROSITE
 PS00485; A_DEAMINASE 
PRINTS