CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012008
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 
Gene Name
 MTAP 
Gene Synonyms/Alias
 MSAP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
32ILEGRTEKYVDTPFGubiquitination[1]
40YVDTPFGKPSDALILubiquitination[1, 2, 3, 4]
49SDALILGKIKNVDCVubiquitination[1, 4]
51ALILGKIKNVDCVLLacetylation[5]
71QHTIMPSKVNYQANIubiquitination[1, 3]
157EVLIETAKKLGLRCHubiquitination[4]
248KENANKAKSLLLTTIubiquitination[1, 4]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330
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. 
Sequence Annotation
 REGION 60 61 Phosphate binding.
 REGION 93 94 Phosphate binding.
 REGION 220 222 Substrate binding.
 BINDING 18 18 Phosphate.
 BINDING 196 196 Substrate; via amide nitrogen.
 BINDING 197 197 Phosphate.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Glycosyltransferase; Nucleus; Polymorphism; Purine salvage; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 283 AA 
Protein Sequence
MASGTTTTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI KNVDCVLLAR 60
HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE EIQPGDIVII DQFIDRTTMR 120
PQSFYDGSHS CARGVCHIPM AEPFCPKTRE VLIETAKKLG LRCHSKGTMV TIEGPRFSSR 180
AESFMFRTWG ADVINMTTVP EVVLAKEAGI CYASIAMATD YDCWKEHEEA VSVDRVLKTL 240
KENANKAKSL LLTTIPQIGS TEWSETLHNL KNMAQFSVLL PRH 283 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0004645; F:phosphorylase activity; TAS:ProtInc.
 GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; TAS:Reactome.
 GO:0019509; P:L-methionine salvage from methylthioadenosine; TAS:Reactome.
 GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
 GO:0006595; P:polyamine metabolic process; TAS:Reactome.
 GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
 GO:0033574; P:response to testosterone stimulus; IEA:Compara. 
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