MAT2B_HUMAN
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 03-AUG-2022, entry version 169.
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; 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 -!- 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};
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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; 64.
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; Q9NZL9; -.
DR PeptideAtlas; Q9NZL9; -.
DR PRIDE; 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 Antibodypedia; 28655; 244 antibodies from 30 providers.
DR DNASU; 27430; -.
DR Ensembl; ENST00000280969.9; ENSP00000280969.5; ENSG00000038274.17. [Q9NZL9-2]
DR Ensembl; ENST00000321757.11; ENSP00000325425.6; ENSG00000038274.17. [Q9NZL9-1]
DR Ensembl; ENST00000518095.5; ENSP00000428046.1; ENSG00000038274.17. [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 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; AGETTWH; -.
DR PhylomeDB; Q9NZL9; -.
DR TreeFam; TF332849; -.
DR BioCyc; MetaCyc:HS00531-MON; -.
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; 12 hits in 1088 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 204 other tissues.
DR ExpressionAtlas; Q9NZL9; baseline and differential.
DR Genevisible; Q9NZL9; HS.
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 InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR PANTHER; PTHR10491; PTHR10491; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
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
