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Q13126

- MTAP_HUMAN

UniProt

Q13126 - MTAP_HUMAN

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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

MTAP

Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 PublicationUniRule annotation

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. nucleobase-containing compound metabolic process Source: ProtInc
  4. polyamine metabolic process Source: Reactome
  5. purine ribonucleoside salvage Source: UniProtKB-KW
  6. small molecule metabolic process Source: Reactome
  7. 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: UniProt
  4. nucleus Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
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 (PubMed:22464254).1 Publication
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.

Organism-specific databases

HPAiHPA046915.

Interactioni

Subunit structurei

Homotrimer.5 PublicationsUniRule annotation

Protein-protein interaction databases

BioGridi110611. 20 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. Align

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 .
CCDSi CCDS6509.1. [Q13126-1 ]
PIRi I38969.
RefSeqi NP_002442.2. NM_002451.3. [Q13126-1 ]
UniGenei Hs.193268.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali Q13126.
SMRi Q13126. Positions 9-281.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110611. 20 interactions.
IntActi Q13126. 6 interactions.
MINTi MINT-268764.
STRINGi 9606.ENSP00000369519.

Chemistry

BindingDBi Q13126.
ChEMBLi CHEMBL4941.
DrugBanki DB00173. Adenine.

PTM databases

PhosphoSitei Q13126.

Polymorphism databases

DMDMi 143811423.

2D gel databases

REPRODUCTION-2DPAGE Q13126.
UCD-2DPAGE Q13126.

Proteomic databases

MaxQBi Q13126.
PaxDbi Q13126.
PRIDEi Q13126.

Protocols and materials databases

DNASUi 4507.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380172 ; ENSP00000369519 ; ENSG00000099810 . [Q13126-1 ]
ENST00000580900 ; ENSP00000463424 ; ENSG00000099810 . [Q13126-3 ]
GeneIDi 4507.
KEGGi hsa:4507.
UCSCi uc003zph.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

CTDi 4507.
GeneCardsi GC09P021792.
H-InvDB HIX0007954.
HIX0025895.
HGNCi HGNC:7413. MTAP.
HPAi HPA046915.
MIMi 112250. phenotype.
156540. gene.
neXtProti NX_Q13126.
Orphaneti 85182. Diaphyseal medullary stenosis - bone malignancy.
PharmGKBi PA31220.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0005.
GeneTreei ENSGT00550000074874.
HOGENOMi HOG000228986.
HOVERGENi HBG002487.
KOi K00772.
OrthoDBi EOG771270.
PhylomeDBi Q13126.
TreeFami TF312883.

Enzyme and pathway databases

UniPathwayi UPA00904 ; UER00873 .
BioCyci MetaCyc:HS01913-MONOMER.
Reactomei REACT_75881. Methionine salvage pathway.
SABIO-RK Q13126.
SignaLinki Q13126.

Miscellaneous databases

ChiTaRSi MTAP. human.
EvolutionaryTracei Q13126.
GeneWikii MTAP.
GenomeRNAii 4507.
NextBioi 17416.
PROi Q13126.
SOURCEi Search...

Gene expression databases

Bgeei Q13126.
CleanExi HS_MTAP.
ExpressionAtlasi Q13126. baseline and differential.
Genevestigatori Q13126.

Family and domain databases

Gene3Di 3.40.50.1580. 1 hit.
HAMAPi MF_01963. MTAP.
InterProi IPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view ]
PANTHERi PTHR11904. PTHR11904. 1 hit.
Pfami PF01048. PNP_UDP_1. 1 hit.
[Graphical view ]
SUPFAMi SSF53167. SSF53167. 1 hit.
TIGRFAMsi TIGR01694. MTAP. 1 hit.
PROSITEi PS01240. PNP_MTAP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 155 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