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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

Mtap

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.UniRule annotation

Catalytic activityi

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

Pathway:iL-methionine biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. S-methyl-5'-thioadenosine phosphorylase (Mtap)
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route), the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei18 – 181PhosphateUniRule annotation
Sitei178 – 1781Important for substrate specificityUniRule annotation
Binding sitei196 – 1961Substrate; via amide nitrogenUniRule annotation
Binding sitei197 – 1971PhosphateUniRule annotation
Sitei233 – 2331Important for substrate specificityUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Enzyme and pathway databases

BRENDAi2.4.2.28. 3474.
ReactomeiREACT_310863. Methionine salvage pathway.
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:Mtap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1914152. Mtap.

Subcellular locationi

  • Cytoplasm
  • Nucleus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 283283S-methyl-5'-thioadenosine phosphorylasePRO_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.
GenevisibleiQ9CQ65. MM.

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9CQ65.
SMRiQ9CQ65. Positions 9-281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0005.
GeneTreeiENSGT00550000074874.
HOGENOMiHOG000228986.
HOVERGENiHBG002487.
InParanoidiQ9CQ65.
KOiK00772.
OMAiMTNHTEA.
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

        10         20         30         40         50
MASGSACTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI
60 70 80 90 100
KNVDCVLLAR HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE
110 120 130 140 150
EIQPGDMVII DQFIDRTSLR PQTFYDGSHC SARGVCHIPM AEPFCPKTRE
160 170 180 190 200
VLIETAKKLG LRCHSKGTIV TIEGPRFSSR AESLIFRTWG ADVVNMTTVP
210 220 230 240 250
EVVLAKEAGI CYASIAMATD YDCWKEHEEA VSVDGVLKTM KENANKAKSL
260 270 280
LLTTIPQIGS MEWSETLRNL KNMAQFSVLP PRH
Length:283
Mass (Da):31,062
Last modified:June 1, 2001 - v1
Checksum:iBF64441F41AE81EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9CQ65.
SMRiQ9CQ65. Positions 9-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiQ9CQ65.
ChEMBLiCHEMBL2663.

PTM databases

PhosphoSiteiQ9CQ65.

2D gel databases

REPRODUCTION-2DPAGEQ9CQ65.

Proteomic databases

MaxQBiQ9CQ65.
PaxDbiQ9CQ65.
PRIDEiQ9CQ65.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4507.
MGIiMGI:1914152. Mtap.

Phylogenomic databases

eggNOGiCOG0005.
GeneTreeiENSGT00550000074874.
HOGENOMiHOG000228986.
HOVERGENiHBG002487.
InParanoidiQ9CQ65.
KOiK00772.
OMAiMTNHTEA.
OrthoDBiEOG771270.
PhylomeDBiQ9CQ65.
TreeFamiTF312883.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00873.
BRENDAi2.4.2.28. 3474.
ReactomeiREACT_310863. Methionine salvage pathway.

Miscellaneous databases

ChiTaRSiMtap. mouse.
NextBioi322973.
PROiQ9CQ65.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQ65.
CleanExiMM_MTAP.
GenevisibleiQ9CQ65. MM.

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. "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: June 24, 2015
This is version 116 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

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.