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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

MTAP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation1 Publication

Catalytic activityi

S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation

Enzyme regulationi

Inhibited by 5'-methylthiotubercin and 5'-chloroformycin.

Kineticsi

  1. KM=5 µM for S-methyl-5'-thioadenosine2 Publications
  2. KM=580 µM for phosphate2 Publications
  3. KM=23 µM for adenine2 Publications
  4. KM=8 µM for S-methyl-5-thio-alpha-D-ribose 1-phosphate2 Publications

pH dependencei

Optimum pH is 7.2-7.6.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei18 – 181Phosphate
Sitei178 – 1781Important for substrate specificity
Binding sitei196 – 1961Substrate; via amide nitrogen
Binding sitei197 – 1971Phosphate
Sitei233 – 2331Important for substrate specificity

GO - Molecular functioni

  1. phosphorylase activity Source: ProtInc
  2. S-methyl-5-thioadenosine phosphorylase activity Source: Reactome

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. L-methionine biosynthetic process from methylthioadenosine Source: Reactome
  3. methylation Source: Ensembl
  4. nucleobase-containing compound metabolic process Source: ProtInc
  5. polyamine metabolic process Source: Reactome
  6. purine ribonucleoside salvage Source: UniProtKB-KW
  7. response to testosterone Source: Ensembl
  8. small molecule metabolic process Source: Reactome
  9. sulfur amino acid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Enzyme and pathway databases

BioCyciMetaCyc:HS01913-MONOMER.
ReactomeiREACT_75881. Methionine salvage pathway.
SABIO-RKQ13126.
SignaLinkiQ13126.
UniPathwayiUPA00904; UER00873.

Names & Taxonomyi

Protein namesi
Recommended name:
S-methyl-5'-thioadenosine phosphorylaseUniRule annotation (EC:2.4.2.28UniRule annotation)
Alternative name(s):
5'-methylthioadenosine phosphorylaseUniRule annotation
Short name:
MTA phosphorylaseUniRule annotation
Short name:
MTAPUniRule annotation
Short name:
MTAPaseUniRule annotation
Gene namesi
Name:MTAPUniRule annotation
Synonyms:MSAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:7413. MTAP.

Subcellular locationi

Cytoplasm. Nucleus UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Diaphyseal medullary stenosis with malignant fibrous histiocytoma1 Publication

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 (PubMed:22464254).

Disease descriptionAn 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.

See also OMIM:112250

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.

Organism-specific databases

MIMi112250. phenotype.
Orphaneti85182. Diaphyseal medullary stenosis - bone malignancy.
PharmGKBiPA31220.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 283283S-methyl-5'-thioadenosine phosphorylasePRO_0000184545Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ13126.
PaxDbiQ13126.
PRIDEiQ13126.

2D gel databases

REPRODUCTION-2DPAGEQ13126.
UCD-2DPAGEQ13126.

PTM databases

PhosphoSiteiQ13126.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiQ13126.
CleanExiHS_MTAP.
ExpressionAtlasiQ13126. baseline and differential.
GenevestigatoriQ13126.

Interactioni

Subunit structurei

Homotrimer.UniRule annotation5 Publications

Protein-protein interaction databases

BioGridi110611. 22 interactions.
IntActiQ13126. 6 interactions.
MINTiMINT-268764.
STRINGi9606.ENSP00000369519.

Structurei

Secondary structure

1
283
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 166Combined sources
Helixi23 – 253Combined sources
Beta strandi26 – 327Combined sources
Beta strandi45 – 506Combined sources
Beta strandi53 – 597Combined sources
Turni60 – 656Combined sources
Helixi69 – 713Combined sources
Helixi74 – 8310Combined sources
Beta strandi87 – 9711Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi112 – 1165Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi140 – 1423Combined sources
Helixi146 – 15813Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi168 – 1725Combined sources
Helixi180 – 1889Combined sources
Beta strandi193 – 1975Combined sources
Helixi198 – 20710Combined sources
Beta strandi211 – 22010Combined sources
Turni222 – 2243Combined sources
Beta strandi225 – 2284Combined sources
Helixi233 – 25826Combined sources
Helixi264 – 27512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CB0X-ray1.70A1-283[»]
1CG6X-ray1.70A1-283[»]
1K27X-ray1.95A1-283[»]
1SD1X-ray2.03A1-283[»]
1SD2X-ray2.10A1-283[»]
3LN5X-ray1.90C227-237[»]
3OZCX-ray1.93A1-283[»]
3OZDX-ray2.10A/B1-283[»]
3OZEX-ray2.00A/B/C/D/E/F1-283[»]
ProteinModelPortaliQ13126.
SMRiQ13126. Positions 9-281.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13126.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni60 – 612Phosphate binding
Regioni93 – 942Phosphate binding
Regioni220 – 2223Substrate binding

Sequence similaritiesi

Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0005.
GeneTreeiENSGT00550000074874.
HOGENOMiHOG000228986.
HOVERGENiHBG002487.
KOiK00772.
OrthoDBiEOG771270.
PhylomeDBiQ13126.
TreeFamiTF312883.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP.
InterProiIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01694. MTAP. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13126-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MASGTTTTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI
60 70 80 90 100
KNVDCVLLAR HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE
110 120 130 140 150
EIQPGDIVII DQFIDRTTMR PQSFYDGSHS CARGVCHIPM AEPFCPKTRE
160 170 180 190 200
VLIETAKKLG LRCHSKGTMV TIEGPRFSSR AESFMFRTWG ADVINMTTVP
210 220 230 240 250
EVVLAKEAGI CYASIAMATD YDCWKEHEEA VSVDRVLKTL KENANKAKSL
260 270 280
LLTTIPQIGS TEWSETLHNL KNMAQFSVLL PRH
Length:283
Mass (Da):31,236
Last modified:April 3, 2007 - v2
Checksum:i3B34C565EB5B99DA
GO
Isoform 2 (identifier: Q13126-2) [UniParc]FASTAAdd to basket

Also known as: MTAP_v1

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

Show »
Length:346
Mass (Da):38,356
Checksum:i1681DA9B0DFB66EE
GO
Isoform 3 (identifier: Q13126-3) [UniParc]FASTAAdd to basket

Also known as: MTAP_v2

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

Show »
Length:334
Mass (Da):36,936
Checksum:i3CD3E1A173FC3465
GO
Isoform 4 (identifier: Q13126-4) [UniParc]FASTAAdd to basket

Also known as: MTAP_v3

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

Show »
Length:280
Mass (Da):30,838
Checksum:i68C30E7ABA7B8AB6
GO
Isoform 5 (identifier: Q13126-5) [UniParc]FASTAAdd to basket

Also known as: MTAP_v4

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

Show »
Length:305
Mass (Da):33,797
Checksum:iD50D41EC7E7123EB
GO
Isoform 6 (identifier: Q13126-6) [UniParc]FASTAAdd to basket

Also known as: MTAP_v5

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

Show »
Length:293
Mass (Da):32,376
Checksum:i3968FB0DFD63A981
GO
Isoform 7 (identifier: Q13126-7) [UniParc]FASTAAdd to basket

Also known as: MTAP_v6

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

Show »
Length:239
Mass (Da):26,278
Checksum:iDD08ECE4DF322F02
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti218 – 2181A → G in AAG38871 (PubMed:8650244).Curated
Sequence conflicti218 – 2181A → G in AAR24607 (PubMed:8650244).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti56 – 561V → I.3 Publications
Corresponds to variant rs7023954 [ dbSNP | Ensembl ].
VAR_031470

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei231 – 28353VSVDR…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGKKC LSAPAIILRPPQPRGTVTTF KVSWSKDQTYICMKS in isoform 5. 1 PublicationVSP_044071Add
BLAST
Alternative sequencei231 – 28353VSVDR…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGEIL PLSPLDLAGYCFQQPMQPPC PDS in isoform 6. 1 PublicationVSP_044072Add
BLAST
Alternative sequencei232 – 28352SVDRV…LLPRH → RSAFQLPP in isoform 7. 1 PublicationVSP_044073Add
BLAST
Alternative sequencei272 – 28312NMAQF…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGKKC LSAPAIILRPPQPRGTVTTF KVSWSKDQTYICMKS in isoform 2. 1 PublicationVSP_044074Add
BLAST
Alternative sequencei272 – 28312NMAQF…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGEIL PLSPLDLAGYCFQQPMQPPC PDS in isoform 3. 1 PublicationVSP_044075Add
BLAST
Alternative sequencei272 – 28312NMAQF…LLPRH → VRSAFQLPP in isoform 4. 1 PublicationVSP_044076Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6509.1. [Q13126-1]
PIRiI38969.
RefSeqiNP_002442.2. NM_002451.3. [Q13126-1]
UniGeneiHs.193268.

Genome annotation databases

EnsembliENST00000380172; ENSP00000369519; ENSG00000099810. [Q13126-1]
ENST00000580900; ENSP00000463424; ENSG00000099810. [Q13126-3]
GeneIDi4507.
KEGGihsa:4507.
UCSCiuc003zph.3. human. [Q13126-1]
uc031tcz.1. human. [Q13126-3]
uc031tda.1. human. [Q13126-6]
uc031tdb.1. human. [Q13126-4]
uc031tdc.1. human. [Q13126-2]
uc031tdd.1. human. [Q13126-5]
uc031tde.1. human. [Q13126-7]

Polymorphism databases

DMDMi143811423.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6509.1. [Q13126-1]
PIRiI38969.
RefSeqiNP_002442.2. NM_002451.3. [Q13126-1]
UniGeneiHs.193268.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CB0X-ray1.70A1-283[»]
1CG6X-ray1.70A1-283[»]
1K27X-ray1.95A1-283[»]
1SD1X-ray2.03A1-283[»]
1SD2X-ray2.10A1-283[»]
3LN5X-ray1.90C227-237[»]
3OZCX-ray1.93A1-283[»]
3OZDX-ray2.10A/B1-283[»]
3OZEX-ray2.00A/B/C/D/E/F1-283[»]
ProteinModelPortaliQ13126.
SMRiQ13126. Positions 9-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110611. 22 interactions.
IntActiQ13126. 6 interactions.
MINTiMINT-268764.
STRINGi9606.ENSP00000369519.

Chemistry

BindingDBiQ13126.
ChEMBLiCHEMBL4941.
DrugBankiDB00173. Adenine.

PTM databases

PhosphoSiteiQ13126.

Polymorphism databases

DMDMi143811423.

2D gel databases

REPRODUCTION-2DPAGEQ13126.
UCD-2DPAGEQ13126.

Proteomic databases

MaxQBiQ13126.
PaxDbiQ13126.
PRIDEiQ13126.

Protocols and materials databases

DNASUi4507.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380172; ENSP00000369519; ENSG00000099810. [Q13126-1]
ENST00000580900; ENSP00000463424; ENSG00000099810. [Q13126-3]
GeneIDi4507.
KEGGihsa:4507.
UCSCiuc003zph.3. human. [Q13126-1]
uc031tcz.1. human. [Q13126-3]
uc031tda.1. human. [Q13126-6]
uc031tdb.1. human. [Q13126-4]
uc031tdc.1. human. [Q13126-2]
uc031tdd.1. human. [Q13126-5]
uc031tde.1. human. [Q13126-7]

Organism-specific databases

CTDi4507.
GeneCardsiGC09P021792.
H-InvDBHIX0007954.
HIX0025895.
HGNCiHGNC:7413. MTAP.
MIMi112250. phenotype.
156540. gene.
neXtProtiNX_Q13126.
Orphaneti85182. Diaphyseal medullary stenosis - bone malignancy.
PharmGKBiPA31220.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0005.
GeneTreeiENSGT00550000074874.
HOGENOMiHOG000228986.
HOVERGENiHBG002487.
KOiK00772.
OrthoDBiEOG771270.
PhylomeDBiQ13126.
TreeFamiTF312883.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00873.
BioCyciMetaCyc:HS01913-MONOMER.
ReactomeiREACT_75881. Methionine salvage pathway.
SABIO-RKQ13126.
SignaLinkiQ13126.

Miscellaneous databases

ChiTaRSiMTAP. human.
EvolutionaryTraceiQ13126.
GeneWikiiMTAP.
GenomeRNAii4507.
NextBioi17416.
PROiQ13126.
SOURCEiSearch...

Gene expression databases

BgeeiQ13126.
CleanExiHS_MTAP.
ExpressionAtlasiQ13126. baseline and differential.
GenevestigatoriQ13126.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP.
InterProiIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01694. MTAP. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiMTAP_HUMAN
AccessioniPrimary (citable) accession number: Q13126
Secondary accession number(s): I2G7M5
, I2G7M6, I2G7M7, I2G7M8, I2G7M9, I2G7N0, Q5T3P3, Q9H010
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 3, 2007
Last modified: March 4, 2015
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.