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Q13126 (MTAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Protein existenceEvidence 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 HAMAP-Rule MF_03155.

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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 283283S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155
PRO_0000184545

Regions

Region60 – 612Phosphate binding HAMAP-Rule MF_03155
Region93 – 942Phosphate binding HAMAP-Rule MF_03155
Region220 – 2223Substrate binding HAMAP-Rule MF_03155

Sites

Binding site181Phosphate
Binding site1961Substrate; via amide nitrogen
Binding site1971Phosphate
Site1781Important for substrate specificity
Site2331Important for substrate specificity

Amino acid modifications

Modified residue511N6-acetyllysine By similarity

Natural variations

Alternative sequence231 – 28353VSVDR…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGKKC LSAPAIILRPPQPRGTVTTF KVSWSKDQTYICMKS in isoform 5.
VSP_044071
Alternative sequence231 – 28353VSVDR…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGEIL PLSPLDLAGYCFQQPMQPPC PDS in isoform 6.
VSP_044072
Alternative sequence232 – 28352SVDRV…LLPRH → RSAFQLPP in isoform 7.
VSP_044073
Alternative sequence272 – 28312NMAQF…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGKKC LSAPAIILRPPQPRGTVTTF KVSWSKDQTYICMKS in isoform 2.
VSP_044074
Alternative sequence272 – 28312NMAQF…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGEIL PLSPLDLAGYCFQQPMQPPC PDS in isoform 3.
VSP_044075
Alternative sequence272 – 28312NMAQF…LLPRH → VRSAFQLPP in isoform 4.
VSP_044076
Natural variant561V → I. Ref.1 Ref.4 Ref.7
Corresponds to variant rs7023954 [ dbSNP | Ensembl ].
VAR_031470

Experimental info

Sequence conflict2181A → G in AAG38871. Ref.2
Sequence conflict2181A → G in AAR24607. Ref.2

Secondary structure

............................................... 283
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: 3B34C565EB5B99DA

FASTA28331,236
        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 

« Hide

Isoform 2 (MTAP_v1) [UniParc].

Checksum: 1681DA9B0DFB66EE
Show »

FASTA34638,356
Isoform 3 (MTAP_v2) [UniParc].

Checksum: 3CD3E1A173FC3465
Show »

FASTA33436,936
Isoform 4 (MTAP_v3) [UniParc].

Checksum: 68C30E7ABA7B8AB6
Show »

FASTA28030,838
Isoform 5 (MTAP_v4) [UniParc].

Checksum: D50D41EC7E7123EB
Show »

FASTA30533,797
Isoform 6 (MTAP_v5) [UniParc].

Checksum: 3968FB0DFD63A981
Show »

FASTA29332,376
Isoform 7 (MTAP_v6) [UniParc].

Checksum: DD08ECE4DF322F02
Show »

FASTA23926,278

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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 expand/collapse EMBL AC list , 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.
PIRI38969.
RefSeqNP_002442.2. NM_002451.3.
XP_005251520.1. XM_005251463.1.
XP_005251521.1. XM_005251464.1.
UniGeneHs.193268.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ13126.
SMRQ13126. Positions 9-281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110611. 20 interactions.
IntActQ13126. 6 interactions.
MINTMINT-268764.
STRING9606.ENSP00000369519.

Chemistry

BindingDBQ13126.
ChEMBLCHEMBL4941.
DrugBankDB00173. Adenine.

PTM databases

PhosphoSiteQ13126.

Polymorphism databases

DMDM143811423.

2D gel databases

REPRODUCTION-2DPAGEQ13126.
UCD-2DPAGEQ13126.

Proteomic databases

PaxDbQ13126.
PRIDEQ13126.

Protocols and materials databases

DNASU4507.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380172; ENSP00000369519; ENSG00000099810. [Q13126-1]
ENST00000580900; ENSP00000463424; ENSG00000099810. [Q13126-3]
GeneID4507.
KEGGhsa:4507.
UCSCuc003zph.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

CTD4507.
GeneCardsGC09P021792.
H-InvDBHIX0007954.
HIX0025895.
HGNCHGNC:7413. MTAP.
HPAHPA046915.
MIM112250. phenotype.
156540. gene.
neXtProtNX_Q13126.
Orphanet85182. Diaphyseal medullary stenosis - bone malignancy.
PharmGKBPA31220.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228986.
HOVERGENHBG002487.
InParanoidQ13126.
KOK00772.
OrthoDBEOG771270.
PhylomeDBQ13126.
TreeFamTF312883.

Enzyme and pathway databases

BioCycMetaCyc:HS01913-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ13126.
SignaLinkQ13126.
UniPathwayUPA00904; UER00873.

Gene expression databases

ArrayExpressQ13126.
BgeeQ13126.
CleanExHS_MTAP.
GenevestigatorQ13126.

Family and domain databases

Gene3D3.40.50.1580. 1 hit.
HAMAPMF_01963. MTAP.
InterProIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERPTHR11904. PTHR11904. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01694. MTAP. 1 hit.
PROSITEPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMTAP. human.
EvolutionaryTraceQ13126.
GeneWikiMTAP.
GenomeRNAi4507.
NextBio17416.
PROQ13126.
SOURCESearch...

Entry information

Entry nameMTAP_HUMAN
AccessionPrimary (citable) accession number: Q13126
Secondary accession number(s): I2G7M5 expand/collapse secondary AC list , 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: March 19, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM