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Q9CQ65

- MTAP_MOUSE

UniProt

Q9CQ65 - MTAP_MOUSE

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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene
Mtap
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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 By similarity.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

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

GO - Molecular functioni

  1. phosphorylase activity Source: InterPro
  2. S-methyl-5-thioadenosine phosphorylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. L-methionine salvage from methylthioadenosine Source: UniProtKB-HAMAP
  2. purine ribonucleoside salvage Source: UniProtKB-KW
  3. response to testosterone Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Enzyme and pathway databases

ReactomeiREACT_199099. Methionine salvage pathway.
UniPathwayiUPA00904; UER00873.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Mtap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1914152. Mtap.

Subcellular locationi

Cytoplasm. Nucleus By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 283283S-methyl-5'-thioadenosine phosphorylaseUniRule annotationPRO_0000184546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9CQ65.
PaxDbiQ9CQ65.
PRIDEiQ9CQ65.

2D gel databases

REPRODUCTION-2DPAGEQ9CQ65.

PTM databases

PhosphoSiteiQ9CQ65.

Expressioni

Gene expression databases

BgeeiQ9CQ65.
CleanExiMM_MTAP.
GenevestigatoriQ9CQ65.

Interactioni

Subunit structurei

Homotrimer By similarity.UniRule annotation

Protein-protein interaction databases

BioGridi211799. 1 interaction.
IntActiQ9CQ65. 2 interactions.
MINTiMINT-1855322.
STRINGi10090.ENSMUSP00000061092.

Structurei

3D structure databases

ProteinModelPortaliQ9CQ65.
SMRiQ9CQ65. Positions 9-281.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0005.
GeneTreeiENSGT00550000074874.
HOGENOMiHOG000228986.
HOVERGENiHBG002487.
InParanoidiQ9CQ65.
KOiK00772.
OMAiCEAQLCY.
OrthoDBiEOG771270.
PhylomeDBiQ9CQ65.
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]

Sequencei

Sequence statusi: Complete.

Q9CQ65-1 [UniParc]FASTAAdd to Basket

« Hide

MASGSACTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI    50
KNVDCVLLAR HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE 100
EIQPGDMVII DQFIDRTSLR PQTFYDGSHC SARGVCHIPM AEPFCPKTRE 150
VLIETAKKLG LRCHSKGTIV TIEGPRFSSR AESLIFRTWG ADVVNMTTVP 200
EVVLAKEAGI CYASIAMATD YDCWKEHEEA VSVDGVLKTM KENANKAKSL 250
LLTTIPQIGS MEWSETLRNL KNMAQFSVLP PRH 283
Length:283
Mass (Da):31,062
Last modified:June 1, 2001 - v1
Checksum:iBF64441F41AE81EA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB056100 mRNA. Translation: BAB32865.1.
AK005064 mRNA. Translation: BAB23788.1.
AK011421 mRNA. Translation: BAB27609.1.
AK167319 mRNA. Translation: BAE39421.1.
BC003858 mRNA. Translation: AAH03858.1.
CCDSiCCDS18349.1.
RefSeqiNP_077753.1. NM_024433.2.
UniGeneiMm.28500.

Genome annotation databases

EnsembliENSMUST00000058030; ENSMUSP00000061092; ENSMUSG00000062937.
GeneIDi66902.
KEGGimmu:66902.
UCSCiuc008tof.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB056100 mRNA. Translation: BAB32865.1 .
AK005064 mRNA. Translation: BAB23788.1 .
AK011421 mRNA. Translation: BAB27609.1 .
AK167319 mRNA. Translation: BAE39421.1 .
BC003858 mRNA. Translation: AAH03858.1 .
CCDSi CCDS18349.1.
RefSeqi NP_077753.1. NM_024433.2.
UniGenei Mm.28500.

3D structure databases

ProteinModelPortali Q9CQ65.
SMRi Q9CQ65. Positions 9-281.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 211799. 1 interaction.
IntActi Q9CQ65. 2 interactions.
MINTi MINT-1855322.
STRINGi 10090.ENSMUSP00000061092.

Chemistry

BindingDBi Q9CQ65.
ChEMBLi CHEMBL2663.

PTM databases

PhosphoSitei Q9CQ65.

2D gel databases

REPRODUCTION-2DPAGE Q9CQ65.

Proteomic databases

MaxQBi Q9CQ65.
PaxDbi Q9CQ65.
PRIDEi Q9CQ65.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000058030 ; ENSMUSP00000061092 ; ENSMUSG00000062937 .
GeneIDi 66902.
KEGGi mmu:66902.
UCSCi uc008tof.2. mouse.

Organism-specific databases

CTDi 4507.
MGIi MGI:1914152. Mtap.

Phylogenomic databases

eggNOGi COG0005.
GeneTreei ENSGT00550000074874.
HOGENOMi HOG000228986.
HOVERGENi HBG002487.
InParanoidi Q9CQ65.
KOi K00772.
OMAi CEAQLCY.
OrthoDBi EOG771270.
PhylomeDBi Q9CQ65.
TreeFami TF312883.

Enzyme and pathway databases

UniPathwayi UPA00904 ; UER00873 .
Reactomei REACT_199099. Methionine salvage pathway.

Miscellaneous databases

NextBioi 322973.
PROi Q9CQ65.
SOURCEi Search...

Gene expression databases

Bgeei Q9CQ65.
CleanExi MM_MTAP.
Genevestigatori Q9CQ65.

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. "Molecular characterization of 5'-deoxy-5'-methylthioadenosine phosphorylase-deficient mutant clones of murine lymphoma cell line R1.1."
    Kadariya Y., Nishioka J., Nakamura A., Kato-Nakazawa K., Nobori T.
    Cancer Sci. 94:519-522(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo, Liver and Placenta.
  3. "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].
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiMTAP_MOUSE
AccessioniPrimary (citable) accession number: Q9CQ65
Secondary accession number(s): Q3TJS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 24, 2002
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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