Q13126 (MTAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-methyl-5'-thioadenosine phosphorylase
EC=2.4.2.28

Alternative name(s):
5'-methylthioadenosine phosphorylase
Short name=MTA phosphorylase
Short name=MTAP
Short name=MTAPase

Gene names

Name:	MTAP
Synonyms:	MSAP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	283 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8
Catalytic activity	S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate. HAMAP-Rule MF_03155
Enzyme regulation	Inhibited by 5'-methylthiotubercin and 5'-chloroformycin. HAMAP-Rule MF_03155
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route): step 1/1. HAMAP-Rule MF_03155
Subunit structure	Homotrimer. Ref.8 Ref.9
Subcellular location	Cytoplasm. Nucleus By similarity.
Tissue specificity	Ubiquitously expressed.
Involvement in disease	Diaphyseal medullary stenosis with malignant fibrous histiocytoma (DMSMFH) [MIM:112250]: An autosomal dominant bone dysplasia characterized by pathologic fractures due to abnormal cortical growth and diaphyseal medullary stenosis. The fractures heal poorly, and there is progressive bowing of the lower extremities. Some patients show a limb-girdle myopathy, with muscle weakness and atrophy. Approximately 35% of affected individuals develop an aggressive form of bone sarcoma consistent with malignant fibrous histiocytoma or osteosarcoma. Note: The disease is caused by mutations affecting the gene represented in this entry. DMSMFH causing mutations found in MTAP exon 9 result in exon skipping and dysregulated alternative splicing of all MTAP isoforms (Ref.3). Ref.3 Loss of MTAP activity may play a role in human cancer. MTAP loss has been reported in a number of cancers, including osteosarcoma, malignant melanoma and gastric cancer.
Sequence similarities	Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Biophysicochemical properties	Kinetic parameters: KM=5 µM for S-methyl-5'-thioadenosine Ref.8 Ref.9 KM=580 µM for phosphate KM=23 µM for adenine KM=8 µM for S-methyl-5-thio-alpha-D-ribose 1-phosphate pH dependence: Optimum pH is 7.2-7.6.

Ontologies

Keywords
Biological process	Purine salvage
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-methionine salvage from methylthioadenosine Traceable author statement. Source: Reactome nucleobase-containing compound metabolic process Traceable author statement Ref.9. Source: ProtInc polyamine metabolic process Traceable author statement. Source: Reactome purine ribonucleoside salvage Inferred from electronic annotation. Source: UniProtKB-KW response to testosterone stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	S-methyl-5-thioadenosine phosphorylase activity Traceable author statement. Source: Reactome phosphorylase activity Traceable author statement Ref.9. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13126-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q13126-2)

Also known as: MTAP_v1;

The sequence of this isoform differs from the canonical sequence as follows:
     272-283: NMAQFSVLLPRH → MIKFQMILSE...KDQTYICMKS

Isoform 3 (identifier: Q13126-3)

Also known as: MTAP_v2;

The sequence of this isoform differs from the canonical sequence as follows:
     272-283: NMAQFSVLLPRH → MIKFQMILSEGYHPFNIQESPFYRGLLDFPSVGHGRGEILPLSPLDLAGYCFQQPMQPPCPDS

Isoform 4 (identifier: Q13126-4)

Also known as: MTAP_v3;

The sequence of this isoform differs from the canonical sequence as follows:
     272-283: NMAQFSVLLPRH → VRSAFQLPP

Isoform 5 (identifier: Q13126-5)

Also known as: MTAP_v4;

The sequence of this isoform differs from the canonical sequence as follows:
     231-283: VSVDRVLKTL...AQFSVLLPRH → MIKFQMILSE...KDQTYICMKS

Isoform 6 (identifier: Q13126-6)

Also known as: MTAP_v5;

The sequence of this isoform differs from the canonical sequence as follows:
     231-283: VSVDRVLKTL...AQFSVLLPRH → MIKFQMILSE...QPMQPPCPDS

Isoform 7 (identifier: Q13126-7)

Also known as: MTAP_v6;

The sequence of this isoform differs from the canonical sequence as follows:
     232-283: SVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH → RSAFQLPP

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 283

283

S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155

PRO_0000184545

Regions

Region

60 – 61

2

Phosphate binding HAMAP-Rule MF_03155

Region

93 – 94

2

Phosphate binding HAMAP-Rule MF_03155

Region

220 – 222

3

Substrate binding HAMAP-Rule MF_03155

Sites

Binding site

18

1

Phosphate

Binding site

196

1

Substrate; via amide nitrogen

Binding site

197

1

Phosphate

Site

178

1

Important for substrate specificity

Site

233

1

Important for substrate specificity

Natural variations

Alternative sequence

231 – 283

53

VSVDR…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGKKC LSAPAIILRPPQPRGTVTTF KVSWSKDQTYICMKS in isoform 5.

VSP_044071

Alternative sequence

231 – 283

53

VSVDR…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGEIL PLSPLDLAGYCFQQPMQPPC PDS in isoform 6.

VSP_044072

Alternative sequence

232 – 283

52

SVDRV…LLPRH → RSAFQLPP in isoform 7.

VSP_044073

Alternative sequence

272 – 283

12

NMAQF…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGKKC LSAPAIILRPPQPRGTVTTF KVSWSKDQTYICMKS in isoform 2.

VSP_044074

Alternative sequence

272 – 283

12

NMAQF…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGEIL PLSPLDLAGYCFQQPMQPPC PDS in isoform 3.

VSP_044075

Alternative sequence

272 – 283

12

NMAQF…LLPRH → VRSAFQLPP in isoform 4.

VSP_044076

Natural variant

56

1

V → I. Ref.1 Ref.4 Ref.7
Corresponds to variant rs7023954 [ dbSNP | Ensembl ].

VAR_031470

Experimental info

Sequence conflict

218

1

A → G in AAG38871. Ref.2

Sequence conflict

218

1

A → G in AAR24607. Ref.2

Secondary structure

1

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283

Helix Strand Turn

Details...

Beta strand

11 – 16

6

Helix

23 – 25

3

Beta strand

26 – 32

7

Beta strand

45 – 50

6

Beta strand

53 – 59

7

Turn

60 – 65

6

Helix

69 – 71

3

Helix

74 – 83

10

Beta strand

87 – 97

11

Beta strand

107 – 109

3

Beta strand

112 – 116

5

Beta strand

126 – 128

3

Beta strand

134 – 136

3

Beta strand

140 – 142

3

Helix

146 – 158

13

Beta strand

163 – 165

3

Beta strand

168 – 172

5

Helix

180 – 188

9

Beta strand

193 – 197

5

Helix

198 – 207

10

Beta strand

211 – 220

10

Turn

222 – 224

3

Beta strand

225 – 228

4

Helix

233 – 258

26

Helix

264 – 275

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 3, 2007. Version 2. Checksum: 3B34C565EB5B99DA	FASTA	283	31,236
	10 20 30 40 50 60 MASGTTTTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI KNVDCVLLAR 70 80 90 100 110 120 HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE EIQPGDIVII DQFIDRTTMR 130 140 150 160 170 180 PQSFYDGSHS CARGVCHIPM AEPFCPKTRE VLIETAKKLG LRCHSKGTMV TIEGPRFSSR 190 200 210 220 230 240 AESFMFRTWG ADVINMTTVP EVVLAKEAGI CYASIAMATD YDCWKEHEEA VSVDRVLKTL 250 260 270 280 KENANKAKSL LLTTIPQIGS TEWSETLHNL KNMAQFSVLL PRH
	Isoform 2 (MTAP_v1) [UniParc]. Checksum: 1681DA9B0DFB66EE	FASTA	346	38,356
	10 20 30 40 50 60 MASGTTTTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI KNVDCVLLAR 70 80 90 100 110 120 HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE EIQPGDIVII DQFIDRTTMR 130 140 150 160 170 180 PQSFYDGSHS CARGVCHIPM AEPFCPKTRE VLIETAKKLG LRCHSKGTMV TIEGPRFSSR 190 200 210 220 230 240 AESFMFRTWG ADVINMTTVP EVVLAKEAGI CYASIAMATD YDCWKEHEEA VSVDRVLKTL 250 260 270 280 290 300 KENANKAKSL LLTTIPQIGS TEWSETLHNL KMIKFQMILS EGYHPFNIQE SPFYRGLLDF 310 320 330 340 PSVGHGRGKK CLSAPAIILR PPQPRGTVTT FKVSWSKDQT YICMKS
	Isoform 3 (MTAP_v2) [UniParc]. Checksum: 3CD3E1A173FC3465	FASTA	334	36,936
	10 20 30 40 50 60 MASGTTTTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI KNVDCVLLAR 70 80 90 100 110 120 HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE EIQPGDIVII DQFIDRTTMR 130 140 150 160 170 180 PQSFYDGSHS CARGVCHIPM AEPFCPKTRE VLIETAKKLG LRCHSKGTMV TIEGPRFSSR 190 200 210 220 230 240 AESFMFRTWG ADVINMTTVP EVVLAKEAGI CYASIAMATD YDCWKEHEEA VSVDRVLKTL 250 260 270 280 290 300 KENANKAKSL LLTTIPQIGS TEWSETLHNL KMIKFQMILS EGYHPFNIQE SPFYRGLLDF 310 320 330 PSVGHGRGEI LPLSPLDLAG YCFQQPMQPP CPDS
	Isoform 4 (MTAP_v3) [UniParc]. Checksum: 68C30E7ABA7B8AB6	FASTA	280	30,838
	10 20 30 40 50 60 MASGTTTTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI KNVDCVLLAR 70 80 90 100 110 120 HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE EIQPGDIVII DQFIDRTTMR 130 140 150 160 170 180 PQSFYDGSHS CARGVCHIPM AEPFCPKTRE VLIETAKKLG LRCHSKGTMV TIEGPRFSSR 190 200 210 220 230 240 AESFMFRTWG ADVINMTTVP EVVLAKEAGI CYASIAMATD YDCWKEHEEA VSVDRVLKTL 250 260 270 280 KENANKAKSL LLTTIPQIGS TEWSETLHNL KVRSAFQLPP
	Isoform 5 (MTAP_v4) [UniParc]. Checksum: D50D41EC7E7123EB	FASTA	305	33,797
	10 20 30 40 50 60 MASGTTTTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI KNVDCVLLAR 70 80 90 100 110 120 HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE EIQPGDIVII DQFIDRTTMR 130 140 150 160 170 180 PQSFYDGSHS CARGVCHIPM AEPFCPKTRE VLIETAKKLG LRCHSKGTMV TIEGPRFSSR 190 200 210 220 230 240 AESFMFRTWG ADVINMTTVP EVVLAKEAGI CYASIAMATD YDCWKEHEEA MIKFQMILSE 250 260 270 280 290 300 GYHPFNIQES PFYRGLLDFP SVGHGRGKKC LSAPAIILRP PQPRGTVTTF KVSWSKDQTY ICMKS
	Isoform 6 (MTAP_v5) [UniParc]. Checksum: 3968FB0DFD63A981	FASTA	293	32,376
	10 20 30 40 50 60 MASGTTTTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI KNVDCVLLAR 70 80 90 100 110 120 HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE EIQPGDIVII DQFIDRTTMR 130 140 150 160 170 180 PQSFYDGSHS CARGVCHIPM AEPFCPKTRE VLIETAKKLG LRCHSKGTMV TIEGPRFSSR 190 200 210 220 230 240 AESFMFRTWG ADVINMTTVP EVVLAKEAGI CYASIAMATD YDCWKEHEEA MIKFQMILSE 250 260 270 280 290 GYHPFNIQES PFYRGLLDFP SVGHGRGEIL PLSPLDLAGY CFQQPMQPPC PDS
	Isoform 7 (MTAP_v6) [UniParc]. Checksum: DD08ECE4DF322F02	FASTA	239	26,278
	10 20 30 40 50 60 MASGTTTTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI KNVDCVLLAR 70 80 90 100 110 120 HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE EIQPGDIVII DQFIDRTTMR 130 140 150 160 170 180 PQSFYDGSHS CARGVCHIPM AEPFCPKTRE VLIETAKKLG LRCHSKGTMV TIEGPRFSSR 190 200 210 220 230 AESFMFRTWG ADVINMTTVP EVVLAKEAGI CYASIAMATD YDCWKEHEEA VRSAFQLPP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Construction of a 2.8-megabase yeast artificial chromosome contig and cloning of the human methylthioadenosine phosphorylase gene from the tumor suppressor region on 9p21." Olopade O.I., Pomykala H.M., Hagos F., Sveen L.W., Espinosa R. III, Dreyling M.H., Gursky S., Stadler W.M., le Beau M.M., Bohlander S.K. Proc. Natl. Acad. Sci. U.S.A. 92:6489-6493(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-56. Tissue: Epidermis.
[2]	"Genomic cloning of methylthioadenosine phosphorylase: a purine metabolic enzyme deficient in multiple different cancers." Nobori T., Takabayashi K., Tran P., Orvis L., Batova A., Yu A.L., Carson D.A. Proc. Natl. Acad. Sci. U.S.A. 93:6203-6208(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Placenta.
[3]	"Primate genome gain and loss: a bone dysplasia, muscular dystrophy, and bone cancer syndrome resulting from mutated retroviral-derived MTAP transcripts." Camacho-Vanegas O., Camacho S.C., Till J., Miranda-Lorenzo I., Terzo E., Ramirez M.C., Schramm V., Cordovano G., Watts G., Mehta S., Kimonis V., Hoch B., Philibert K.D., Raabe C.A., Bishop D.F., Glucksman M.J., Martignetti J.A. Am. J. Hum. Genet. 90:614-627(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6 AND 7), INVOLVEMENT IN DMSMFH.
[4]	"Identification of human methylthioadenosine phosphorylase (MTAP) mRNA mutation in colon cancer cell line COLO 205." Li Q., Cao W.-X., Zhang Y., Shi M.-M., Liu B.-Y., Zhu Z.-G., Lin Y.-Z. Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-56. Tissue: Colon.
[5]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-56. Tissue: Brain.
[8]	"Purification and characterization of 5'-deoxy-5'-methylthioadenosine phosphorylase from human placenta." Della Ragione F., Carteni-Farina M., Gragnaniello V., Schettino M.I., Zappia V. J. Biol. Chem. 261:12324-12329(1986) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[9]	"Purification and characterization of recombinant human 5'-methylthioadenosine phosphorylase: definite identification of coding cDNA." Ragione F.D., Takabayashi K., Mastropietro S., Mercurio C., Oliva A., Russo G.L., Pietra V.D., Borriello A., Nobori T., Carson D.A., Zappia V. Biochem. Biophys. Res. Commun. 223:514-519(1996) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[10]	"Methylthioadenosine phosphorylase gene deletions are common in osteosarcoma." Garcia-Castellano J.M., Villanueva A., Healey J.H., Sowers R., Cordon-Cardo C., Huvos A., Bertino J.R., Meyers P., Gorlick R. Clin. Cancer Res. 8:782-787(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN OSTEOSARCOMA.
[11]	"Methylthioadenosine phosphorylase deficiency in Japanese osteosarcoma patients." Miyazaki S., Nishioka J., Shiraishi T., Matsumine A., Uchida A., Nobori T. Int. J. Oncol. 31:1069-1076(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN OSTEOSARCOMA.
[12]	"Direct and tumor microenvironment mediated influences of 5'-deoxy-5'-(methylthio)adenosine on tumor progression of malignant melanoma." Stevens A.P., Spangler B., Wallner S., Kreutz M., Dettmer K., Oefner P.J., Bosserhoff A.K. J. Cell. Biochem. 106:210-219(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MALIGNANT MELANOMA.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Downregulation of methylthioadenosine phosphorylase by homozygous deletion in gastric carcinoma." Kim J., Kim M.A., Min S.Y., Jee C.D., Lee H.E., Kim W.H. Genes Chromosomes Cancer 50:421-433(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN GASTRIC CANCER.
[15]	"The structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase at 1.7-A resolution provides insights into substrate binding and catalysis." Appleby T.C., Erion M.D., Ealick S.E. Structure 7:629-641(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MTA.
[16]	"Structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design." Lee J.E., Settembre E.C., Cornell K.A., Riscoe M.K., Sufrin J.R., Ealick S.E., Howell P.L. Biochemistry 43:5159-5169(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS.
[17]	"Picomolar transition state analogue inhibitors of human 5'-methylthioadenosine phosphorylase and X-ray structure with MT-immucillin-A." Singh V., Shi W., Evans G.B., Tyler P.C., Furneaux R.H., Almo S.C., Schramm V.L. Biochemistry 43:9-18(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[18]	"The impact of human leukocyte antigen (HLA) micropolymorphism on ligand specificity within the HLA-B*41 allotypic family." Bade-Doding C., Theodossis A., Gras S., Kjer-Nielsen L., Eiz-Vesper B., Seltsam A., Huyton T., Rossjohn J., McCluskey J., Blasczyk R. Haematologica 96:110-118(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 227-237.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U22233 mRNA. Translation: AAA81646.1.
L40432 mRNA. Translation: AAG38871.1.
L42634 , L42627, L42628, L42629, L42630, L42631, L42632, L42633 Genomic DNA. Translation: AAR24607.2.
HE654772 mRNA. Translation: CCF77345.1.
HE654773 mRNA. Translation: CCF77346.1.
HE654774 mRNA. Translation: CCF77347.1.
HE654775 mRNA. Translation: CCF77348.1.
HE654776 mRNA. Translation: CCF77349.1.
HE654777 mRNA. Translation: CCF77350.1.
AY712791 mRNA. Translation: AAU04442.1.
AL359922 Genomic DNA. Translation: CAI16481.1.
CH471071 Genomic DNA. Translation: EAW58606.1.
BC026106 mRNA. Translation: AAH26106.1.

IPI

IPI00011876.

PIR

I38969.

RefSeq

NP_002442.2. NM_002451.3.

UniGene

Hs.193268.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CB0	X-ray	1.70	A	1-283	[»]
1CG6	X-ray	1.70	A	1-283	[»]
1K27	X-ray	1.95	A	1-283	[»]
1SD1	X-ray	2.03	A	1-283	[»]
1SD2	X-ray	2.10	A	1-283	[»]
3LN5	X-ray	1.90	C	227-237	[»]
3OZC	X-ray	1.93	A	1-283	[»]
3OZD	X-ray	2.10	A/B	1-283	[»]
3OZE	X-ray	2.00	A/B/C/D/E/F	1-283	[»]

ProteinModelPortal

Q13126.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13126. 6 interactions.

MINT

MINT-268764.

STRING

9606.ENSP00000369519.

PTM databases

PhosphoSite

Q13126.

Polymorphism databases

DMDM

143811423.

2D gel databases

REPRODUCTION-2DPAGE

Q13126.

UCD-2DPAGE

Q13126.

Proteomic databases

PaxDb

Q13126.

PRIDE

Q13126.

Protocols and materials databases

DNASU

4507.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000380172; ENSP00000369519; ENSG00000099810.
ENST00000580900; ENSP00000463424; ENSG00000099810.

GeneID

4507.

KEGG

hsa:4507.

UCSC

uc003zph.3. human.

Organism-specific databases

CTD

4507.

GeneCards

GC09P021792.

H-InvDB

HIX0007954.
HIX0025895.

HGNC

HGNC:7413. MTAP.

MIM

112250. phenotype.
156540. gene.

neXtProt

NX_Q13126.

Orphanet

85182. Diaphyseal medullary stenosis - bone malignancy.

PharmGKB

PA31220.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0005.

HOGENOM

HOG000228986.

HOVERGEN

HBG002487.

InParanoid

Q13126.

KO

K00772.

OMA

VVPDQFI.

OrthoDB

EOG4B8JDJ.

PhylomeDB

Q13126.

Enzyme and pathway databases

BioCyc

MetaCyc:HS01913-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

Q13126.

UniPathway

UPA00904; UER00873.

Gene expression databases

ArrayExpress

Q13126.

Bgee

Q13126.

CleanEx

HS_MTAP.

Genevestigator

Q13126.

GermOnline

ENSG00000099810. Homo sapiens.

Family and domain databases

HAMAP

MF_01963. MTAP.

InterPro

IPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]

PANTHER

PTHR11904. PTHR11904. 1 hit.

Pfam

PF01048. PNP_UDP_1. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01694. MTAP. 1 hit.

PROSITE

PS01240. PNP_MTAP_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q13126.

ChEMBL

CHEMBL4941.

ChiTaRS

MTAP. human.

DrugBank

DB00173. Adenine.

EvolutionaryTrace

Q13126.

GenomeRNAi

4507.

NextBio

17416.

SOURCE

Search...

Entry information

Entry name

MTAP_HUMAN

Accession

Primary (citable) accession number: Q13126
Secondary accession number(s): I2G7M5 , I2G7M6, I2G7M7, I2G7M8, I2G7M9, I2G7N0, Q5T3P3, Q9H010

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	April 3, 2007
Last modified:	May 1, 2013
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.