ID MAT2B_HUMAN Reviewed; 334 AA. AC Q9NZL9; B2R5Y6; Q1WAI7; Q27J92; Q3LIE8; Q567T7; Q6NYC7; Q9BS89; Q9H3E1; AC Q9UJ54; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 178. DE RecName: Full=Methionine adenosyltransferase 2 subunit beta; DE AltName: Full=Methionine adenosyltransferase II beta; DE Short=MAT II beta; DE AltName: Full=Putative dTDP-4-keto-6-deoxy-D-glucose 4-reductase; GN Name=MAT2B; Synonyms=TGR; GN ORFNames=MSTP045, Nbla02999, UNQ2435/PRO4995; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-20 AND RP 240-257, SUBUNIT, FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=10644686; DOI=10.1074/jbc.275.4.2359; RA LeGros H.L., Halim A.-B., Geller A.M., Kotb M.; RT "Cloning, expression, and functional characterization of the beta RT regulatory subunit of human methionine adenosyltransferase (MAT II)."; RL J. Biol. Chem. 275:2359-2366(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Sturla L., Zanardi D., Bisso A., Damonte G., Fasano M., De Flora A., RA Tonetti M.; RT "Occurrence of a novel metabolic pathway converting dTDP-D-glucose in human RT cells."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5). RA Yang H., Magilnick N., Lu S.C.; RT "Alternative splicing of the MAT2B gene."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Neuroblastoma; RX PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5; RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., RA Hirato J., Nakagawara A.; RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of the RT genesis and biology of neuroblastoma."; RL Cancer Lett. 197:63-68(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Amygdala; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP THR-293. RC TISSUE=Pancreas, Placenta, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-334. RC TISSUE=Heart; RA Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y., RA Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y., RA Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., RA Zhao M.S., Hui R.T.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [11] RP TISSUE SPECIFICITY. RX PubMed=11337507; DOI=10.1074/jbc.m102816200; RA LeGros L., Halim A.-B., Chamberlin M.E., Geller A., Kotb M.; RT "Regulation of the human MAT2B gene encoding the regulatory beta subunit of RT methionine adenosyltransferase, MAT II."; RL J. Biol. Chem. 276:24918-24924(2001). RN [12] RP EXPRESSION IN HEPATOMA. RX PubMed=12671891; DOI=10.1053/gast.2003.50151; RA Martinez-Chantar M.L., Garcia-Trevijano E.R., Latasa M.U., Martin-Duce A., RA Fortes P., Caballeria J., Avila M.A., Mato J.M.; RT "Methionine adenosyltransferase II beta subunit gene expression provides a RT proliferative advantage in human hepatoma."; RL Gastroenterology 124:940-948(2003). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP FUNCTION, SUBUNIT, NADP-BINDING, AND PATHWAY. RX PubMed=23189196; DOI=10.1371/journal.pone.0050329; RA Gonzalez B., Garrido F., Ortega R., Martinez-Julvez M., RA Revilla-Guarinos A., Perez-Pertejo Y., Velazquez-Campoy A., RA Sanz-Aparicio J., Pajares M.A.; RT "NADP+ binding to the regulatory subunit of methionine adenosyltransferase RT II increases intersubunit binding affinity in the hetero-trimer."; RL PLoS ONE 7:E50329-E50329(2012). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-309, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] {ECO:0007744|PDB:2YDX, ECO:0007744|PDB:2YDY} RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 28-334 IN COMPLEX WITH NADP, AND RP FUNCTION. RX PubMed=23425511; DOI=10.1042/bj20121580; RA Shafqat N., Muniz J.R., Pilka E.S., Papagrigoriou E., von Delft F., RA Oppermann U., Yue W.W.; RT "Insight into S-adenosylmethionine biosynthesis from the crystal structures RT of the human methionine adenosyltransferase catalytic and regulatory RT subunits."; RL Biochem. J. 452:27-36(2013). RN [19] {ECO:0007744|PDB:4KTT, ECO:0007744|PDB:4KTV, ECO:0007744|PDB:4NDN} RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) OF 22-334 IN COMPLEX WITH MAT2A, RP SUBUNIT, REGION, FUNCTION, AND PATHWAY. RX PubMed=25075345; DOI=10.1107/s2052252514012585; RA Murray B., Antonyuk S.V., Marina A., Van Liempd S.M., Lu S.C., Mato J.M., RA Hasnain S.S., Rojas A.L.; RT "Structure and function study of the complex that synthesizes S- RT adenosylmethionine."; RL IUCrJ 1:240-249(2014). CC -!- FUNCTION: Regulatory subunit of S-adenosylmethionine synthetase 2, an CC enzyme that catalyzes the formation of S-adenosylmethionine from CC methionine and ATP. Regulates MAT2A catalytic activity by changing its CC kinetic properties, increasing its affinity for L-methionine CC (PubMed:10644686, PubMed:23189196, PubMed:25075345). Can bind NADP (in CC vitro) (PubMed:23189196, PubMed:23425511). CC {ECO:0000269|PubMed:10644686, ECO:0000269|PubMed:23189196, CC ECO:0000269|PubMed:23425511, ECO:0000269|PubMed:25075345}. CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; CC S-adenosyl-L-methionine from L-methionine: step 1/1. CC {ECO:0000269|PubMed:10644686, ECO:0000269|PubMed:23189196, CC ECO:0000269|PubMed:25075345}. CC -!- SUBUNIT: Heterotrimer; composed of a catalytic MAT2A homodimer that CC binds one regulatory MAT2B chain (PubMed:10644686, PubMed:23189196). CC Heterohexamer; composed of a central, catalytic MAT2A homotetramer CC flanked on either side by a regulatory MAT2B chain (PubMed:25075345). CC NADP binding increases the affinity for MAT2A (PubMed:23189196). CC {ECO:0000269|PubMed:10644686, ECO:0000269|PubMed:25075345, CC ECO:0000305|PubMed:23189196}. CC -!- INTERACTION: CC Q9NZL9; O00505: KPNA3; NbExp=6; IntAct=EBI-10317491, EBI-358297; CC Q9NZL9; O00629: KPNA4; NbExp=3; IntAct=EBI-10317491, EBI-396343; CC Q9NZL9; P31153: MAT2A; NbExp=3; IntAct=EBI-10317491, EBI-1050743; CC Q9NZL9; O60733: PLA2G6; NbExp=3; IntAct=EBI-10317491, EBI-12089905; CC Q9NZL9; Q15276: RABEP1; NbExp=3; IntAct=EBI-10317491, EBI-447043; CC Q9NZL9; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-10317491, EBI-11139477; CC Q9NZL9; P14373: TRIM27; NbExp=3; IntAct=EBI-10317491, EBI-719493; CC Q9NZL9; PRO_0000449627 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-10317491, EBI-25475877; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q9NZL9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NZL9-2; Sequence=VSP_025534; CC Name=3; CC IsoId=Q9NZL9-3; Sequence=VSP_025538, VSP_025539; CC Name=4; CC IsoId=Q9NZL9-4; Sequence=VSP_025534, VSP_025540; CC Name=5; CC IsoId=Q9NZL9-5; Sequence=VSP_025535, VSP_025536, VSP_025537; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10644686, CC ECO:0000269|PubMed:11337507}. CC -!- MISCELLANEOUS: Its expression in hepatoma cell lines may lead to CC increase DNA synthesis and thereby participate in cell proliferation. CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family. CC MAT2B subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG39296.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF182814; AAF28477.1; -; mRNA. DR EMBL; AJ243721; CAB56837.1; -; mRNA. DR EMBL; DQ395260; ABD59011.1; -; mRNA. DR EMBL; DQ413183; ABD85290.1; -; mRNA. DR EMBL; AL136664; CAB66599.1; -; mRNA. DR EMBL; AB073390; BAE45720.1; -; mRNA. DR EMBL; AY358695; AAQ89058.1; -; mRNA. DR EMBL; AK312365; BAG35283.1; -; mRNA. DR EMBL; CH471062; EAW61517.1; -; Genomic_DNA. DR EMBL; BC005218; AAH05218.1; -; mRNA. DR EMBL; BC066645; AAH66645.1; -; mRNA. DR EMBL; BC093030; AAH93030.1; -; mRNA. DR EMBL; AF113225; AAG39296.1; ALT_INIT; mRNA. DR CCDS; CCDS4364.1; -. [Q9NZL9-2] DR CCDS; CCDS4365.1; -. [Q9NZL9-1] DR RefSeq; NP_037415.1; NM_013283.4. [Q9NZL9-1] DR RefSeq; NP_877725.1; NM_182796.2. [Q9NZL9-2] DR PDB; 2YDX; X-ray; 2.80 A; A/B/C/D/E=28-334. DR PDB; 2YDY; X-ray; 2.25 A; A=28-334. DR PDB; 4KTT; X-ray; 2.59 A; E/F=22-334. DR PDB; 4KTV; X-ray; 3.30 A; E/F=22-334. DR PDB; 4NDN; X-ray; 2.34 A; E/F=22-334. DR PDBsum; 2YDX; -. DR PDBsum; 2YDY; -. DR PDBsum; 4KTT; -. DR PDBsum; 4KTV; -. DR PDBsum; 4NDN; -. DR AlphaFoldDB; Q9NZL9; -. DR SMR; Q9NZL9; -. DR BioGRID; 118166; 104. DR ComplexPortal; CPX-948; S-adenosylmethionine synthase, MAT2A-MAT2B variant. DR CORUM; Q9NZL9; -. DR IntAct; Q9NZL9; 18. DR MINT; Q9NZL9; -. DR STRING; 9606.ENSP00000325425; -. DR DrugBank; DB00134; Methionine. DR GlyGen; Q9NZL9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NZL9; -. DR MetOSite; Q9NZL9; -. DR PhosphoSitePlus; Q9NZL9; -. DR SwissPalm; Q9NZL9; -. DR BioMuta; MAT2B; -. DR DMDM; 74719662; -. DR REPRODUCTION-2DPAGE; IPI00002324; -. DR EPD; Q9NZL9; -. DR jPOST; Q9NZL9; -. DR MassIVE; Q9NZL9; -. DR MaxQB; Q9NZL9; -. DR PaxDb; 9606-ENSP00000325425; -. DR PeptideAtlas; Q9NZL9; -. DR ProteomicsDB; 83432; -. [Q9NZL9-1] DR ProteomicsDB; 83433; -. [Q9NZL9-2] DR ProteomicsDB; 83434; -. [Q9NZL9-3] DR ProteomicsDB; 83435; -. [Q9NZL9-4] DR ProteomicsDB; 83436; -. [Q9NZL9-5] DR Pumba; Q9NZL9; -. DR Antibodypedia; 28655; 269 antibodies from 30 providers. DR DNASU; 27430; -. DR Ensembl; ENST00000280969.9; ENSP00000280969.5; ENSG00000038274.18. [Q9NZL9-2] DR Ensembl; ENST00000321757.11; ENSP00000325425.6; ENSG00000038274.18. [Q9NZL9-1] DR Ensembl; ENST00000518095.5; ENSP00000428046.1; ENSG00000038274.18. [Q9NZL9-3] DR Ensembl; ENST00000694943.1; ENSP00000511609.1; ENSG00000038274.18. [Q9NZL9-3] DR GeneID; 27430; -. DR KEGG; hsa:27430; -. DR MANE-Select; ENST00000321757.11; ENSP00000325425.6; NM_013283.5; NP_037415.1. DR UCSC; uc003lzj.5; human. [Q9NZL9-1] DR AGR; HGNC:6905; -. DR CTD; 27430; -. DR DisGeNET; 27430; -. DR GeneCards; MAT2B; -. DR HGNC; HGNC:6905; MAT2B. DR HPA; ENSG00000038274; Low tissue specificity. DR MIM; 605527; gene. DR neXtProt; NX_Q9NZL9; -. DR OpenTargets; ENSG00000038274; -. DR PharmGKB; PA30648; -. DR VEuPathDB; HostDB:ENSG00000038274; -. DR eggNOG; KOG1430; Eukaryota. DR GeneTree; ENSGT00390000006721; -. DR HOGENOM; CLU_045518_0_0_1; -. DR InParanoid; Q9NZL9; -. DR OMA; IRTAWVY; -. DR OrthoDB; 3080056at2759; -. DR PhylomeDB; Q9NZL9; -. DR TreeFam; TF332849; -. DR BioCyc; MetaCyc:HS00531-MONOMER; -. DR BRENDA; 2.5.1.6; 2681. DR PathwayCommons; Q9NZL9; -. DR Reactome; R-HSA-156581; Methylation. DR Reactome; R-HSA-5689880; Ub-specific processing proteases. DR SignaLink; Q9NZL9; -. DR SIGNOR; Q9NZL9; -. DR UniPathway; UPA00315; UER00080. DR BioGRID-ORCS; 27430; 13 hits in 1168 CRISPR screens. DR ChiTaRS; MAT2B; human. DR EvolutionaryTrace; Q9NZL9; -. DR GenomeRNAi; 27430; -. DR Pharos; Q9NZL9; Tbio. DR PRO; PR:Q9NZL9; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q9NZL9; Protein. DR Bgee; ENSG00000038274; Expressed in secondary oocyte and 206 other cell types or tissues. DR ExpressionAtlas; Q9NZL9; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0048269; C:methionine adenosyltransferase complex; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:LIFEdb. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0048270; F:methionine adenosyltransferase regulator activity; IDA:UniProtKB. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IDA:UniProtKB. DR CDD; cd05254; dTDP_HR_like_SDR_e; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR005913; dTDP_dehydrorham_reduct. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR029903; RmlD-like-bd. DR PANTHER; PTHR10491; DTDP-4-DEHYDRORHAMNOSE REDUCTASE; 1. DR PANTHER; PTHR10491:SF4; METHIONINE ADENOSYLTRANSFERASE 2 SUBUNIT BETA; 1. DR Pfam; PF04321; RmlD_sub_bind; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR Genevisible; Q9NZL9; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; NADP; KW One-carbon metabolism; Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:10644686" FT CHAIN 2..334 FT /note="Methionine adenosyltransferase 2 subunit beta" FT /id="PRO_0000287520" FT REGION 319..334 FT /note="Required for interaction with MAT2A" FT /evidence="ECO:0000269|PubMed:25075345" FT BINDING 37..40 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007744|PDB:2YDX" FT BINDING 60..62 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007744|PDB:2YDX" FT BINDING 71..72 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007744|PDB:2YDX" FT BINDING 93 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007744|PDB:2YDX" FT BINDING 97 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007744|PDB:2YDX" FT BINDING 159 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007744|PDB:2YDX" FT BINDING 185 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007744|PDB:2YDX" FT MOD_RES 309 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..21 FT /note="MVGREKELSIHFVPGSCRLVE -> MPEMPEDMEQ (in isoform 2 FT and isoform 4)" FT /evidence="ECO:0000303|PubMed:12975309, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2, FT ECO:0000303|Ref.3" FT /id="VSP_025534" FT VAR_SEQ 1..20 FT /note="MVGREKELSIHFVPGSCRLV -> MPEMPEDMEQ (in isoform 5)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_025535" FT VAR_SEQ 87..93 FT /note="PHVIVHC -> VLLTALS (in isoform 5)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_025536" FT VAR_SEQ 94..334 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_025537" FT VAR_SEQ 241..259 FT /note="DPSIKGTFHWSGNEQMTKY -> VRRIPESCLSEGPLCLFHA (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:12880961" FT /id="VSP_025538" FT VAR_SEQ 260..334 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12880961" FT /id="VSP_025539" FT VAR_SEQ 279..295 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_025540" FT VARIANT 293 FT /note="A -> T (in dbSNP:rs17849948)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_032318" FT CONFLICT 150 FT /note="E -> G (in Ref. 9; AAH93030)" FT /evidence="ECO:0000305" FT CONFLICT 302 FT /note="T -> I (in Ref. 9; AAH66645)" FT /evidence="ECO:0000305" FT STRAND 30..34 FT /evidence="ECO:0007829|PDB:2YDY" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:2YDY" FT HELIX 39..49 FT /evidence="ECO:0007829|PDB:2YDY" FT TURN 50..52 FT /evidence="ECO:0007829|PDB:2YDY" FT STRAND 54..58 FT /evidence="ECO:0007829|PDB:2YDY" FT TURN 60..62 FT /evidence="ECO:0007829|PDB:4KTV" FT TURN 64..66 FT /evidence="ECO:0007829|PDB:4NDN" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:4NDN" FT HELIX 79..85 FT /evidence="ECO:0007829|PDB:2YDY" FT STRAND 88..92 FT /evidence="ECO:0007829|PDB:2YDY" FT HELIX 99..104 FT /evidence="ECO:0007829|PDB:4NDN" FT HELIX 106..113 FT /evidence="ECO:0007829|PDB:4NDN" FT HELIX 115..126 FT /evidence="ECO:0007829|PDB:2YDY" FT STRAND 130..136 FT /evidence="ECO:0007829|PDB:2YDY" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:2YDY" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:2YDY" FT HELIX 158..173 FT /evidence="ECO:0007829|PDB:2YDY" FT STRAND 178..182 FT /evidence="ECO:0007829|PDB:2YDY" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:2YDY" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:2YDY" FT HELIX 198..200 FT /evidence="ECO:0007829|PDB:2YDY" FT HELIX 201..205 FT /evidence="ECO:0007829|PDB:2YDY" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:4KTV" FT STRAND 211..214 FT /evidence="ECO:0007829|PDB:2YDY" FT STRAND 216..219 FT /evidence="ECO:0007829|PDB:2YDY" FT HELIX 224..239 FT /evidence="ECO:0007829|PDB:2YDY" FT STRAND 246..249 FT /evidence="ECO:0007829|PDB:2YDY" FT HELIX 258..268 FT /evidence="ECO:0007829|PDB:2YDY" FT STRAND 276..279 FT /evidence="ECO:0007829|PDB:2YDY" FT STRAND 285..287 FT /evidence="ECO:0007829|PDB:2YDY" FT HELIX 298..302 FT /evidence="ECO:0007829|PDB:2YDY" FT HELIX 311..319 FT /evidence="ECO:0007829|PDB:2YDY" FT HELIX 320..322 FT /evidence="ECO:0007829|PDB:2YDY" FT HELIX 324..327 FT /evidence="ECO:0007829|PDB:4NDN" FT TURN 330..333 FT /evidence="ECO:0007829|PDB:2YDX" SQ SEQUENCE 334 AA; 37552 MW; 6AAA5381BAF3F65F CRC64; MVGREKELSI HFVPGSCRLV EEEVNIPNRR VLVTGATGLL GRAVHKEFQQ NNWHAVGCGF RRARPKFEQV NLLDSNAVHH IIHDFQPHVI VHCAAERRPD VVENQPDAAS QLNVDASGNL AKEAAAVGAF LIYISSDYVF DGTNPPYREE DIPAPLNLYG KTKLDGEKAV LENNLGAAVL RIPILYGEVE KLEESAVTVM FDKVQFSNKS ANMDHWQQRF PTHVKDVATV CRQLAEKRML DPSIKGTFHW SGNEQMTKYE MACAIADAFN LPSSHLRPIT DSPVLGAQRP RNAQLDCSKL ETLGIGQRTP FRIGIKESLW PFLIDKRWRQ TVFH //