P31153A8K511B4DN45D6W5L1Q53SP5METK2_HUMANS-adenosylmethionine synthase isoform type-2AdoMet synthase 22.5.1.6Methionine adenosyltransferase 2MAT 2Methionine adenosyltransferase IIMAT-IIMAT2AAMS2MATA2Homo sapiensHumanEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomoMolecular cloning and developmental expression of a human kidney S-adenosylmethionine synthetase.NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)TISSUE SPECIFICITYActivation of a novel isoform of methionine adenosyl transferase 2A and increased S-adenosylmethionine turnover in lung epithelial cells exposed to hyperoxia.NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)Complete sequencing and characterization of 21,243 full-length human cDNAs.NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2)Generation and annotation of the DNA sequences of human chromosomes 2 and 4.NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)Cloning, expression, and functional characterization of the beta regulatory subunit of human methionine adenosyltransferase (MAT II).FUNCTIONCATALYTIC ACTIVITYSUBUNITPATHWAYA quantitative atlas of mitotic phosphorylation.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Lysine acetylation targets protein complexes and co-regulates major cellular functions.ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Initial characterization of the human central proteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]NADP+ binding to the regulatory subunit of methionine adenosyltransferase II increases intersubunit binding affinity in the hetero-trimer.CATALYTIC ACTIVITYSUBUNITPATHWAYFUNCTIONToward a comprehensive characterization of a human cancer cell phosphoproteome.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]The U6 snRNA m(6)A methyltransferase METTL16 regulates SAM synthetase intron retention.POST-TRANSCRIPTIONAL REGULATIONS-Adenosylmethionine synthesis is regulated by selective N6-adenosine methylation and mRNA degradation involving METTL16 and YTHDC1.POST-TRANSCRIPTIONAL REGULATIONSite-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-228 AND LYS-234IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Splice site m6A methylation prevents binding of U2AF35 to inhibit RNA splicing.POST-TRANSCRIPTIONAL REGULATIONInsight into S-adenosylmethionine biosynthesis from the crystal structures of the human methionine adenosyltransferase catalytic and regulatory subunits.X-RAY CRYSTALLOGRAPHY (1.21 ANGSTROMS) IN COMPLEX WITH S-ADENOSYLMETHIONINEStructure and function study of the complex that synthesizes S-adenosylmethionine.X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) IN COMPLEXES WITH ATP ANALOG; S-ADENOSYL-L-METHIONINE AND MAGNESIUMFUNCTIONCATALYTIC ACTIVITYPATHWAYSUBUNITCrystallography captures catalytic steps in human methionine adenosyltransferase enzymes.X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS) IN COMPLEXTES WITH ATP ANALOG; S-ADENOSYL-L-METHIONINE; MAGNESIUM AND POTASSIUMCOFACTORCatalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionineMg(2+)Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.K(+)Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.Heterotrimer; composed of a catalytic MAT2A homodimer that binds one regulatory MAT2B chain (PubMed:10644686, PubMed:23189196). Heterohexamer; composed of a central, catalytic MAT2A homotetramer flanked on either side by a regulatory MAT2B chain (PubMed:25075345).P31153Q96IK1-2false3P31153Q96NX5false3P31153Q6ZP82false3P31153Q8IUI8false3P31153Q6P1L5false3P31153P15976-2false3P31153P80217-2false3P31153Q8WZ19false3P31153Q9UIH9false3P31153Q00266false7P31153P31153false8P31153Q9NZL9false3P31153P02795false3P31153Q9BRX2false3P31153O43663false3P31153O43741false3P31153P57052false3P31153Q8N488false3P31153P08195-4false3P31153Q13573false3P31153Q86W54-2false3P31153O95789-4false3P31153-11P31153-22Detected in kidney.Protein expression is regulated by post-transcriptional regulation: in presence of S-adenosyl-L-methionine, METTL16 binds and methylates the first hairpin of the 3'-UTR region of MAT2A mRNA, preventing recognition of their 3'-splice site by U2AF1/U2AF35, thereby inhibiting splicing and protein production of S-adenosylmethionine synthase (PubMed:28525753, PubMed:29262316, PubMed:33930289). In S-adenosyl-L-methionine-limiting conditions, METTL16 binds the 3'-UTR region of MAT2A mRNA without methylating it due to the lack of a methyl donor, preventing N6-methylation and promoting expression of MAT2A (PubMed:28525753).Belongs to the AdoMet synthase family.3D-structureAcetylationAlternative splicingATP-bindingIsopeptide bondMagnesiumMetal-bindingNucleotide-bindingOne-carbon metabolismPhosphoproteinPotassiumReference proteomeTransferaseUbl conjugationATPligand shared between two neighboring subunitsMg(2+)K(+)L-methionineligand shared between two neighboring subunitsL-methionineligand shared between two neighboring subunitsATPligand shared between two neighboring subunitsATPligand shared between two neighboring subunitsATPligand shared between two neighboring subunitsL-methionineligand shared between two neighboring subunitsATPligand shared between two neighboring subunitsATPligand shared between two neighboring subunitsATPligand shared between two neighboring subunitsL-methionineligand shared between two neighboring subunitsATPligand shared between two neighboring subunitsMNGQLNGFHEAFIEEGTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKGFDYKTCNVLVALEQQSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDSKTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGRDSFPWEVPKKLKY
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