CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011543
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 S-methyl-5'-thioadenosine phosphorylase 
Protein Synonyms/Alias
 5'-methylthioadenosine phosphorylase; MTA phosphorylase; MTAP; MTAPase; Multicopy enhancer of UAS2 
Gene Name
 MEU1 
Gene Synonyms/Alias
 YLR017W; L1595 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
237MSVIPEAKLARECELubiquitination[1]
317IKKSISTKPEAMSKEacetylation[2]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S- adenosylmethionine. Has broad substrate specificity with 6- aminopurine nucleosides as preferred substrates. Seems to be implicated in the regulation of the expression of the ADH2 gene. 
Sequence Annotation
 REGION 88 89 Phosphate binding (By similarity).
 REGION 121 122 Phosphate binding (By similarity).
 REGION 254 256 Substrate binding (By similarity).
 BINDING 41 41 Phosphate (By similarity).
 BINDING 230 230 Substrate; via amide nitrogen (By
 BINDING 231 231 Phosphate (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Glycosyltransferase; Nucleus; Purine salvage; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 337 AA 
Protein Sequence
MNRIKNTFSV AKRLKLSKVM TNSELPSIFE GTVDLGIIGG TGLYNLDCLE PIALLPPMVT 60
PWGTTSSPVT ISQFVGTNSH FHVAFIARHG INHEYPPTKV PFRANMAALK NLNCKAVLSF 120
SAVGSLQPHI KPRDFVLPQQ IIDRTKGIRH SSYFNDEGLV GHVGFGQPFS QKFAEYIYQF 180
KNEITNPESE EPCHLHYDKD MTVVCMEGPQ FSTRAESKMY RMFGGHVINM SVIPEAKLAR 240
ECELPYQMIC MSTDYDAWRD EAEPVTVETV IGNLTNNGRN ANILASKIIV SMAKEIPEFM 300
HTGDGLRGSI KKSISTKPEA MSKETLERLR YLFPNYW 337 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003729; F:mRNA binding; IDA:SGD.
 GO:0004645; F:phosphorylase activity; IEA:InterPro.
 GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IDA:SGD.
 GO:0006537; P:glutamate biosynthetic process; IMP:SGD.
 GO:0019509; P:L-methionine salvage from methylthioadenosine; IDA:SGD.
 GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW. 
Interpro
 IPR010044; MTAP.
 IPR000845; Nucleoside_phosphorylase_d.
 IPR001369; PNP/MTAP.
 IPR018099; Purine_phosphorylase-2_CS. 
Pfam
 PF01048; PNP_UDP_1 
SMART
  
PROSITE
 PS01240; PNP_MTAP_2 
PRINTS