Full text data of MAT2B
MAT2B
(TGR)
[Confidence: low (only semi-automatic identification from reviews)]
Methionine adenosyltransferase 2 subunit beta (Methionine adenosyltransferase II beta; MAT II beta; Putative dTDP-4-keto-6-deoxy-D-glucose 4-reductase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Methionine adenosyltransferase 2 subunit beta (Methionine adenosyltransferase II beta; MAT II beta; Putative dTDP-4-keto-6-deoxy-D-glucose 4-reductase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NZL9
ID MAT2B_HUMAN Reviewed; 334 AA.
AC Q9NZL9; B2R5Y6; Q1WAI7; Q27J92; Q3LIE8; Q567T7; Q6NYC7; Q9BS89;
read moreAC Q9H3E1; Q9UJ54;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 105.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT human 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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
RT the 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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J.,
RA Cao H.Q., Zhao Y., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q.,
RA Yuan J.G., Liew C.C., 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
RT subunit of 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.,
RA Martin-Duce A., Fortes P., Caballeria J., Avila M.A., Mato J.M.;
RT "Methionine adenosyltransferase II beta subunit gene expression
RT provides a 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Non-catalytic regulatory subunit of S-adenosylmethionine
CC synthetase 2 (MAT2A), an enzyme that catalyzes the formation of S-
CC adenosylmethionine from methionine and ATP. Regulates the activity
CC of S-adenosylmethionine synthetase 2 by changing its kinetic
CC properties, rendering the enzyme more susceptible to S-
CC adenosylmethionine inhibition.
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine
CC biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
CC -!- SUBUNIT: Heterotetramer composed of 2 catalytic alpha subunits
CC (alpha and alpha') (MAT2A) and 1 copy of beta subunit (MAT2B).
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 Note=No experimental confirmation available;
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.
CC -!- MISCELLANEOUS: Its expression in hepatoma cell lines may lead to
CC increase DNA synthesis and thereby participate in cell
CC proliferation.
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase
CC family. MAT2B subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG39296.1; Type=Erroneous initiation;
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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 RefSeq; NP_037415.1; NM_013283.4.
DR RefSeq; NP_877725.1; NM_182796.2.
DR UniGene; Hs.54642; -.
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 PDBsum; 2YDX; -.
DR PDBsum; 2YDY; -.
DR ProteinModelPortal; Q9NZL9; -.
DR SMR; Q9NZL9; 28-334.
DR MINT; MINT-2819994; -.
DR DrugBank; DB00134; L-Methionine.
DR DrugBank; DB00118; S-Adenosylmethionine.
DR PhosphoSite; Q9NZL9; -.
DR DMDM; 74719662; -.
DR REPRODUCTION-2DPAGE; IPI00002324; -.
DR PaxDb; Q9NZL9; -.
DR PRIDE; Q9NZL9; -.
DR DNASU; 27430; -.
DR Ensembl; ENST00000280969; ENSP00000280969; ENSG00000038274.
DR Ensembl; ENST00000321757; ENSP00000325425; ENSG00000038274.
DR Ensembl; ENST00000518095; ENSP00000428046; ENSG00000038274.
DR GeneID; 27430; -.
DR KEGG; hsa:27430; -.
DR UCSC; uc003lzk.4; human.
DR CTD; 27430; -.
DR GeneCards; GC05P162930; -.
DR HGNC; HGNC:6905; MAT2B.
DR HPA; HPA037721; -.
DR HPA; HPA037722; -.
DR MIM; 605527; gene.
DR neXtProt; NX_Q9NZL9; -.
DR PharmGKB; PA30648; -.
DR eggNOG; COG1091; -.
DR HOVERGEN; HBG105851; -.
DR InParanoid; Q9NZL9; -.
DR KO; K00789; -.
DR OMA; YDCHLST; -.
DR OrthoDB; EOG74FF26; -.
DR PhylomeDB; Q9NZL9; -.
DR BRENDA; 2.5.1.6; 2681.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00315; UER00080.
DR ChiTaRS; MAT2B; human.
DR EvolutionaryTrace; Q9NZL9; -.
DR GenomeRNAi; 27430; -.
DR NextBio; 50469; -.
DR PRO; PR:Q9NZL9; -.
DR ArrayExpress; Q9NZL9; -.
DR Bgee; Q9NZL9; -.
DR Genevestigator; Q9NZL9; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0048269; C:methionine adenosyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:InterPro.
DR GO; GO:0048270; F:methionine adenosyltransferase regulator activity; IDA:UniProtKB.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; TAS:Reactome.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0000096; P:sulfur amino acid metabolic process; TAS:Reactome.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR Pfam; PF04321; RmlD_sub_bind; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Direct protein sequencing; One-carbon metabolism; Polymorphism;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 334 Methionine adenosyltransferase 2 subunit
FT beta.
FT /FTId=PRO_0000287520.
FT VAR_SEQ 1 21 MVGREKELSIHFVPGSCRLVE -> MPEMPEDMEQ (in
FT isoform 2 and isoform 4).
FT /FTId=VSP_025534.
FT VAR_SEQ 1 20 MVGREKELSIHFVPGSCRLV -> MPEMPEDMEQ (in
FT isoform 5).
FT /FTId=VSP_025535.
FT VAR_SEQ 87 93 PHVIVHC -> VLLTALS (in isoform 5).
FT /FTId=VSP_025536.
FT VAR_SEQ 94 334 Missing (in isoform 5).
FT /FTId=VSP_025537.
FT VAR_SEQ 241 259 DPSIKGTFHWSGNEQMTKY -> VRRIPESCLSEGPLCLFH
FT A (in isoform 3).
FT /FTId=VSP_025538.
FT VAR_SEQ 260 334 Missing (in isoform 3).
FT /FTId=VSP_025539.
FT VAR_SEQ 279 295 Missing (in isoform 4).
FT /FTId=VSP_025540.
FT VARIANT 293 293 A -> T (in dbSNP:rs17849948).
FT /FTId=VAR_032318.
FT CONFLICT 150 150 E -> G (in Ref. 9; AAH93030).
FT CONFLICT 302 302 T -> I (in Ref. 9; AAH66645).
FT STRAND 30 34
FT TURN 35 37
FT HELIX 39 49
FT TURN 50 52
FT STRAND 54 58
FT TURN 64 66
FT STRAND 67 69
FT HELIX 79 85
FT STRAND 88 92
FT HELIX 99 104
FT HELIX 106 113
FT HELIX 115 126
FT STRAND 130 136
FT HELIX 137 139
FT STRAND 142 144
FT HELIX 158 173
FT STRAND 178 182
FT STRAND 184 186
FT HELIX 192 194
FT HELIX 198 200
FT HELIX 201 205
FT STRAND 211 214
FT STRAND 216 219
FT HELIX 224 239
FT STRAND 246 249
FT HELIX 258 268
FT STRAND 276 279
FT STRAND 285 287
FT HELIX 298 302
FT HELIX 311 319
FT HELIX 320 322
FT TURN 330 333
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
//
ID MAT2B_HUMAN Reviewed; 334 AA.
AC Q9NZL9; B2R5Y6; Q1WAI7; Q27J92; Q3LIE8; Q567T7; Q6NYC7; Q9BS89;
read moreAC Q9H3E1; Q9UJ54;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 105.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT human 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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
RT the 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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J.,
RA Cao H.Q., Zhao Y., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q.,
RA Yuan J.G., Liew C.C., 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
RT subunit of 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.,
RA Martin-Duce A., Fortes P., Caballeria J., Avila M.A., Mato J.M.;
RT "Methionine adenosyltransferase II beta subunit gene expression
RT provides a 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Non-catalytic regulatory subunit of S-adenosylmethionine
CC synthetase 2 (MAT2A), an enzyme that catalyzes the formation of S-
CC adenosylmethionine from methionine and ATP. Regulates the activity
CC of S-adenosylmethionine synthetase 2 by changing its kinetic
CC properties, rendering the enzyme more susceptible to S-
CC adenosylmethionine inhibition.
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine
CC biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
CC -!- SUBUNIT: Heterotetramer composed of 2 catalytic alpha subunits
CC (alpha and alpha') (MAT2A) and 1 copy of beta subunit (MAT2B).
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 Note=No experimental confirmation available;
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.
CC -!- MISCELLANEOUS: Its expression in hepatoma cell lines may lead to
CC increase DNA synthesis and thereby participate in cell
CC proliferation.
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase
CC family. MAT2B subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG39296.1; Type=Erroneous initiation;
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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 RefSeq; NP_037415.1; NM_013283.4.
DR RefSeq; NP_877725.1; NM_182796.2.
DR UniGene; Hs.54642; -.
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 PDBsum; 2YDX; -.
DR PDBsum; 2YDY; -.
DR ProteinModelPortal; Q9NZL9; -.
DR SMR; Q9NZL9; 28-334.
DR MINT; MINT-2819994; -.
DR DrugBank; DB00134; L-Methionine.
DR DrugBank; DB00118; S-Adenosylmethionine.
DR PhosphoSite; Q9NZL9; -.
DR DMDM; 74719662; -.
DR REPRODUCTION-2DPAGE; IPI00002324; -.
DR PaxDb; Q9NZL9; -.
DR PRIDE; Q9NZL9; -.
DR DNASU; 27430; -.
DR Ensembl; ENST00000280969; ENSP00000280969; ENSG00000038274.
DR Ensembl; ENST00000321757; ENSP00000325425; ENSG00000038274.
DR Ensembl; ENST00000518095; ENSP00000428046; ENSG00000038274.
DR GeneID; 27430; -.
DR KEGG; hsa:27430; -.
DR UCSC; uc003lzk.4; human.
DR CTD; 27430; -.
DR GeneCards; GC05P162930; -.
DR HGNC; HGNC:6905; MAT2B.
DR HPA; HPA037721; -.
DR HPA; HPA037722; -.
DR MIM; 605527; gene.
DR neXtProt; NX_Q9NZL9; -.
DR PharmGKB; PA30648; -.
DR eggNOG; COG1091; -.
DR HOVERGEN; HBG105851; -.
DR InParanoid; Q9NZL9; -.
DR KO; K00789; -.
DR OMA; YDCHLST; -.
DR OrthoDB; EOG74FF26; -.
DR PhylomeDB; Q9NZL9; -.
DR BRENDA; 2.5.1.6; 2681.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00315; UER00080.
DR ChiTaRS; MAT2B; human.
DR EvolutionaryTrace; Q9NZL9; -.
DR GenomeRNAi; 27430; -.
DR NextBio; 50469; -.
DR PRO; PR:Q9NZL9; -.
DR ArrayExpress; Q9NZL9; -.
DR Bgee; Q9NZL9; -.
DR Genevestigator; Q9NZL9; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0048269; C:methionine adenosyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:InterPro.
DR GO; GO:0048270; F:methionine adenosyltransferase regulator activity; IDA:UniProtKB.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; TAS:Reactome.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0000096; P:sulfur amino acid metabolic process; TAS:Reactome.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR Pfam; PF04321; RmlD_sub_bind; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Direct protein sequencing; One-carbon metabolism; Polymorphism;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 334 Methionine adenosyltransferase 2 subunit
FT beta.
FT /FTId=PRO_0000287520.
FT VAR_SEQ 1 21 MVGREKELSIHFVPGSCRLVE -> MPEMPEDMEQ (in
FT isoform 2 and isoform 4).
FT /FTId=VSP_025534.
FT VAR_SEQ 1 20 MVGREKELSIHFVPGSCRLV -> MPEMPEDMEQ (in
FT isoform 5).
FT /FTId=VSP_025535.
FT VAR_SEQ 87 93 PHVIVHC -> VLLTALS (in isoform 5).
FT /FTId=VSP_025536.
FT VAR_SEQ 94 334 Missing (in isoform 5).
FT /FTId=VSP_025537.
FT VAR_SEQ 241 259 DPSIKGTFHWSGNEQMTKY -> VRRIPESCLSEGPLCLFH
FT A (in isoform 3).
FT /FTId=VSP_025538.
FT VAR_SEQ 260 334 Missing (in isoform 3).
FT /FTId=VSP_025539.
FT VAR_SEQ 279 295 Missing (in isoform 4).
FT /FTId=VSP_025540.
FT VARIANT 293 293 A -> T (in dbSNP:rs17849948).
FT /FTId=VAR_032318.
FT CONFLICT 150 150 E -> G (in Ref. 9; AAH93030).
FT CONFLICT 302 302 T -> I (in Ref. 9; AAH66645).
FT STRAND 30 34
FT TURN 35 37
FT HELIX 39 49
FT TURN 50 52
FT STRAND 54 58
FT TURN 64 66
FT STRAND 67 69
FT HELIX 79 85
FT STRAND 88 92
FT HELIX 99 104
FT HELIX 106 113
FT HELIX 115 126
FT STRAND 130 136
FT HELIX 137 139
FT STRAND 142 144
FT HELIX 158 173
FT STRAND 178 182
FT STRAND 184 186
FT HELIX 192 194
FT HELIX 198 200
FT HELIX 201 205
FT STRAND 211 214
FT STRAND 216 219
FT HELIX 224 239
FT STRAND 246 249
FT HELIX 258 268
FT STRAND 276 279
FT STRAND 285 287
FT HELIX 298 302
FT HELIX 311 319
FT HELIX 320 322
FT TURN 330 333
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
//
MIM
605527
*RECORD*
*FIELD* NO
605527
*FIELD* TI
*605527 METHIONINE ADENOSYLTRANSFERASE II, BETA; MAT2B
*FIELD* TX
Methionine adenosyltransferase (MAT; EC 2.5.1.6) catalyzes the
read morebiosynthesis of S-adenosylmethionine (AdoMet) from methionine and ATP.
MAT II is a broadly expressed MAT consisting of catalytic alpha and
noncatalytic beta subunits encoded by MAT2A (601468) and MAT2B,
respectively. For additional general information on MAT, see 601468.
LeGros et al. (2000) designed degenerate PCR primers to tryptic peptide
sequence of MAT2B purified from human lymphocytes. They amplified a
partial cDNA from Jurkat cells and extended the cDNA using 3-prime and
5-prime RACE. A full-length MAT2B cDNA amplified from normal human
peripheral blood mononuclear cell RNA encodes a 334-amino acid protein
with a molecular mass of 38 kD. LeGros et al. (2000) predicted 2
prominent hydrophobic segments from the sequence. MAT2B has sequence
similarity with bacterial enzymes that catalyze the reduction of
TDP-linked sugars; however, antibodies to MAT2B do not react with E.
coli or yeast extracts.
LeGros et al. (2000) expressed a recombinant histone-tagged MAT2B that
had no MAT catalytic activity alone. However, the recombinant MAT2B
associated spontaneously with the alpha subunit from human and E. coli,
lowering the Km of MAT II for L-methionine, thus confirming a regulatory
role for the beta subunit.
*FIELD* RF
1. LeGros, H. L., Jr.; Halim, A.-B.; Geller, A. M.; Kotb, M.: Cloning,
expression, and functional characterization of the beta regulatory
subunit of human methionine adenosyltransferase (MAT II). J. Biol.
Chem. 275: 2359-2366, 2000.
*FIELD* CD
Dawn Watkins-Chow: 1/4/2001
*FIELD* ED
carol: 01/04/2001
carol: 1/4/2001
*RECORD*
*FIELD* NO
605527
*FIELD* TI
*605527 METHIONINE ADENOSYLTRANSFERASE II, BETA; MAT2B
*FIELD* TX
Methionine adenosyltransferase (MAT; EC 2.5.1.6) catalyzes the
read morebiosynthesis of S-adenosylmethionine (AdoMet) from methionine and ATP.
MAT II is a broadly expressed MAT consisting of catalytic alpha and
noncatalytic beta subunits encoded by MAT2A (601468) and MAT2B,
respectively. For additional general information on MAT, see 601468.
LeGros et al. (2000) designed degenerate PCR primers to tryptic peptide
sequence of MAT2B purified from human lymphocytes. They amplified a
partial cDNA from Jurkat cells and extended the cDNA using 3-prime and
5-prime RACE. A full-length MAT2B cDNA amplified from normal human
peripheral blood mononuclear cell RNA encodes a 334-amino acid protein
with a molecular mass of 38 kD. LeGros et al. (2000) predicted 2
prominent hydrophobic segments from the sequence. MAT2B has sequence
similarity with bacterial enzymes that catalyze the reduction of
TDP-linked sugars; however, antibodies to MAT2B do not react with E.
coli or yeast extracts.
LeGros et al. (2000) expressed a recombinant histone-tagged MAT2B that
had no MAT catalytic activity alone. However, the recombinant MAT2B
associated spontaneously with the alpha subunit from human and E. coli,
lowering the Km of MAT II for L-methionine, thus confirming a regulatory
role for the beta subunit.
*FIELD* RF
1. LeGros, H. L., Jr.; Halim, A.-B.; Geller, A. M.; Kotb, M.: Cloning,
expression, and functional characterization of the beta regulatory
subunit of human methionine adenosyltransferase (MAT II). J. Biol.
Chem. 275: 2359-2366, 2000.
*FIELD* CD
Dawn Watkins-Chow: 1/4/2001
*FIELD* ED
carol: 01/04/2001
carol: 1/4/2001