CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003837
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Adenosylhomocysteinase 
Protein Synonyms/Alias
 AdoHcyase; S-adenosyl-L-homocysteine hydrolase 
Gene Name
 Ahcy 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
4****MADKLPYKVADacetylation[1]
8MADKLPYKVADIGLAacetylation[1]
43REMYSASKPLKGARIacetylation[1]
166TGVHNLYKMMANGILacetylation[1]
204ESLIDGIKRATDVMIacetylation[1]
318LNENAVEKVNIKPQVacetylation[1]
322AVEKVNIKPQVDRYLacetylation[1]
389GVHFLPKKLDEAVAEubiquitination[2]
401VAEAHLGKLNVKLTKacetylation[1]
405HLGKLNVKLTKLTEKacetylation[1]
412KLTKLTEKQAQYLGMacetylation[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]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113
Functional Description
 Adenosylhomocysteine is a competitive inhibitor of S- adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine. 
Sequence Annotation
 NP_BIND 157 159 NAD.
 NP_BIND 222 227 NAD.
 NP_BIND 299 301 NAD.
 NP_BIND 426 430 NAD.
 BINDING 57 57 Substrate.
 BINDING 131 131 Substrate.
 BINDING 156 156 Substrate.
 BINDING 186 186 Substrate.
 BINDING 190 190 Substrate.
 BINDING 243 243 NAD.
 BINDING 248 248 NAD.
 BINDING 346 346 NAD.
 BINDING 353 353 NAD.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; NAD; One-carbon metabolism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 432 AA 
Protein Sequence
MADKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMREMYS ASKPLKGARI AGCLHMTVET 60
AVLIETLVAL GAEVRWSSCN IFSTQDHAAA AIAKAGIPVF AWKGETDEEY LWCIEQTLHF 120
KDGPLNMILD DGGDLTNLIH TKHPQLLSGI RGISEETTTG VHNLYKMMAN GILKVPAINV 180
NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI 240
ITEIDPINAL QAAMEGYEVT TMDEACKEGN IFVTTTGCVD IILGRHFEQM KDDAIVCNIG 300
HFDVEIDVKW LNENAVEKVN IKPQVDRYLL KNGHRIILLA EGRLVNLGCA MGHPSFVMSN 360
SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG KLNVKLTKLT EKQAQYLGMP 420
INGPFKPDHY RY 432 
Gene Ontology
 GO:0005829; C:cytosol; IDA:RGD.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0043005; C:neuron projection; IDA:RGD.
 GO:0005634; C:nucleus; IDA:RGD.
 GO:0004013; F:adenosylhomocysteinase activity; IDA:RGD.
 GO:0030554; F:adenyl nucleotide binding; IDA:RGD.
 GO:0042802; F:identical protein binding; IDA:RGD.
 GO:0051287; F:NAD binding; IDA:RGD.
 GO:0002439; P:chronic inflammatory response to antigenic stimulus; IMP:RGD.
 GO:0042745; P:circadian sleep/wake cycle; IDA:RGD.
 GO:0071268; P:homocysteine biosynthetic process; IMP:RGD.
 GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
 GO:0001666; P:response to hypoxia; IEP:RGD.
 GO:0007584; P:response to nutrient; IDA:RGD.
 GO:0019510; P:S-adenosylhomocysteine catabolic process; IDA:RGD. 
Interpro
 IPR000043; Adenosylhomocysteinase.
 IPR015878; Ado_hCys_hydrolase_NAD-bd.
 IPR016040; NAD(P)-bd_dom.
 IPR020082; S-Ado-L-homoCys_hydrolase_CS. 
Pfam
 PF05221; AdoHcyase
 PF00670; AdoHcyase_NAD 
SMART
 SM00996; AdoHcyase
 SM00997; AdoHcyase_NAD 
PROSITE
 PS00738; ADOHCYASE_1
 PS00739; ADOHCYASE_2 
PRINTS