UniProt Accession

 B4DUC8_HUMAN; B4DUC8 

Genbank Protein ID

 AL359922; AL449423; AK300592 

Genbank Nucleotide ID

 BAG62290.1 

Protein Name

 S-methyl-5'-thioadenosine phosphorylase 

Protein Synonyms/Alias

 5'-methylthioadenosine phosphorylase 

Gene Name

 MTAP 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
49	ILEGRTEKYVDTPFG	ubiquitination	[1, 2]
57	YVDTPFGKPSDALIL	ubiquitination	[1, 2, 3, 4, 5]
66	SDALILGKIKNVDCV	ubiquitination	[1, 2]
88	QHTIMPSKVNYQANI	ubiquitination	[2, 4, 5, 6]
174	EVLIETAKKLGLRCH	ubiquitination	[1]
265	KENANKAKSLLLTTI	ubiquitination	[1, 2]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] 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] 

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 (By similarity). 

Sequence Annotation

 REGION 77 78 Phosphate binding (By similarity).
 REGION 110 111 Phosphate binding (By similarity).
 REGION 237 239 Substrate binding (By similarity).
 BINDING 35 35 Phosphate (By similarity).
 BINDING 213 213 Substrate; via amide nitrogen (By
 BINDING 214 214 Phosphate (By similarity).  

Keyword

 Complete proteome; Cytoplasm; Glycosyltransferase; Nucleus; Purine salvage; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 300 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0004645; F:phosphorylase activity; IEA:InterPro.
 GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:HAMAP.
 GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:HAMAP.
 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