Full text data of MAT2A
MAT2A
(AMS2, MATA2)
[Confidence: low (only semi-automatic identification from reviews)]
S-adenosylmethionine synthase isoform type-2; AdoMet synthase 2; 2.5.1.6 (Methionine adenosyltransferase 2; MAT 2; Methionine adenosyltransferase II; MAT-II)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
S-adenosylmethionine synthase isoform type-2; AdoMet synthase 2; 2.5.1.6 (Methionine adenosyltransferase 2; MAT 2; Methionine adenosyltransferase II; MAT-II)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P31153
ID METK2_HUMAN Reviewed; 395 AA.
AC P31153; A8K511; D6W5L1; Q53SP5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1993, sequence version 1.
DT 22-JAN-2014, entry version 143.
DE RecName: Full=S-adenosylmethionine synthase isoform type-2;
DE Short=AdoMet synthase 2;
DE EC=2.5.1.6;
DE AltName: Full=Methionine adenosyltransferase 2;
DE Short=MAT 2;
DE AltName: Full=Methionine adenosyltransferase II;
DE Short=MAT-II;
GN Name=MAT2A; Synonyms=AMS2, MATA2;
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].
RC TISSUE=Kidney;
RX PubMed=1426236; DOI=10.1016/0014-5793(92)81405-B;
RA Horikawa S., Tsukada K.;
RT "Molecular cloning and developmental expression of a human kidney S-
RT adenosylmethionine synthetase.";
RL FEBS Lett. 312:37-41(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=16413417; DOI=10.1016/j.freeradbiomed.2005.09.004;
RA Panayiotidis M.I., Stabler S.P., Ahmad A., Pappa A., Legros L.H. Jr.,
RA Hernandez-Saavedra D., Schneider B.K., Allen R.H., Vasiliou V.,
RA McCord J.M., Kotb M., White C.W.;
RT "Activation of a novel isoform of methionine adenosyl transferase 2A
RT and increased S-adenosylmethionine turnover in lung epithelial cells
RT exposed to hyperoxia.";
RL Free Radic. Biol. Med. 40:348-358(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [7]
RP SUBUNIT.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
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: Catalyzes the formation of S-adenosylmethionine from
CC methionine and ATP.
CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate +
CC diphosphate + S-adenosyl-L-methionine.
CC -!- COFACTOR: Binds 2 divalent ions per subunit. Magnesium or cobalt
CC (By similarity).
CC -!- COFACTOR: Binds 1 potassium ion per subunit (By similarity).
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 -!- PTM: The alpha' subunit is a post-translationally modified version
CC of MAT2A.
CC -!- SIMILARITY: Belongs to the AdoMet synthase family.
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DR EMBL; X68836; CAA48726.1; -; mRNA.
DR EMBL; DQ083239; AAY85355.1; -; mRNA.
DR EMBL; AK291126; BAF83815.1; -; mRNA.
DR EMBL; AC016753; AAY24339.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99511.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99513.1; -; Genomic_DNA.
DR EMBL; BC001686; AAH01686.1; -; mRNA.
DR EMBL; BC001854; AAH01854.1; -; mRNA.
DR PIR; S27257; S27257.
DR RefSeq; NP_005902.1; NM_005911.5.
DR UniGene; Hs.516157; -.
DR PDB; 2P02; X-ray; 1.21 A; A=1-395.
DR PDBsum; 2P02; -.
DR ProteinModelPortal; P31153; -.
DR SMR; P31153; 16-395.
DR IntAct; P31153; 17.
DR STRING; 9606.ENSP00000303147; -.
DR DrugBank; DB00134; L-Methionine.
DR DrugBank; DB00118; S-Adenosylmethionine.
DR PhosphoSite; P31153; -.
DR DMDM; 400245; -.
DR REPRODUCTION-2DPAGE; IPI00010157; -.
DR PaxDb; P31153; -.
DR PeptideAtlas; P31153; -.
DR PRIDE; P31153; -.
DR DNASU; 4144; -.
DR Ensembl; ENST00000306434; ENSP00000303147; ENSG00000168906.
DR GeneID; 4144; -.
DR KEGG; hsa:4144; -.
DR UCSC; uc002spr.3; human.
DR CTD; 4144; -.
DR GeneCards; GC02P085766; -.
DR H-InvDB; HIX0117562; -.
DR HGNC; HGNC:6904; MAT2A.
DR HPA; CAB009968; -.
DR HPA; HPA043028; -.
DR MIM; 601468; gene.
DR neXtProt; NX_P31153; -.
DR PharmGKB; PA30647; -.
DR eggNOG; COG0192; -.
DR HOGENOM; HOG000245710; -.
DR HOVERGEN; HBG001562; -.
DR InParanoid; P31153; -.
DR KO; K00789; -.
DR OMA; YYAHKIL; -.
DR PhylomeDB; P31153; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00315; UER00080.
DR ChiTaRS; MAT2A; human.
DR EvolutionaryTrace; P31153; -.
DR GenomeRNAi; 4144; -.
DR NextBio; 16276; -.
DR PRO; PR:P31153; -.
DR ArrayExpress; P31153; -.
DR Bgee; P31153; -.
DR CleanEx; HS_MAT2A; -.
DR Genevestigator; P31153; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
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; IEA:UniProtKB-UniPathway.
DR GO; GO:0000096; P:sulfur amino acid metabolic process; TAS:Reactome.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR InterPro; IPR022631; ADOMET_SYNTHASE_CS.
DR InterPro; IPR022630; S-AdoMet_synt_C.
DR InterPro; IPR022629; S-AdoMet_synt_central.
DR InterPro; IPR022628; S-AdoMet_synt_N.
DR InterPro; IPR002133; S-AdoMet_synthetase.
DR InterPro; IPR022636; S-AdoMet_synthetase_sfam.
DR PANTHER; PTHR11964; PTHR11964; 1.
DR Pfam; PF02773; S-AdoMet_synt_C; 1.
DR Pfam; PF02772; S-AdoMet_synt_M; 1.
DR Pfam; PF00438; S-AdoMet_synt_N; 1.
DR PIRSF; PIRSF000497; MAT; 1.
DR SUPFAM; SSF55973; SSF55973; 3.
DR TIGRFAMs; TIGR01034; metK; 1.
DR PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
DR PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cobalt; Complete proteome;
KW Magnesium; Metal-binding; Nucleotide-binding; One-carbon metabolism;
KW Phosphoprotein; Potassium; Reference proteome; Transferase.
FT CHAIN 1 395 S-adenosylmethionine synthase isoform
FT type-2.
FT /FTId=PRO_0000174435.
FT NP_BIND 131 136 ATP (Potential).
FT METAL 31 31 Magnesium (By similarity).
FT METAL 57 57 Potassium (By similarity).
FT METAL 283 283 Potassium (By similarity).
FT METAL 291 291 Magnesium (By similarity).
FT BINDING 159 159 ATP (Potential).
FT MOD_RES 81 81 N6-acetyllysine.
FT MOD_RES 114 114 Phosphoserine.
FT STRAND 17 25
FT HELIX 30 48
FT STRAND 53 61
FT STRAND 64 72
FT HELIX 79 90
FT HELIX 95 97
FT TURN 101 103
FT STRAND 104 111
FT HELIX 115 121
FT TURN 122 124
FT HELIX 127 129
FT STRAND 132 134
FT STRAND 136 143
FT HELIX 152 169
FT STRAND 176 191
FT STRAND 194 209
FT HELIX 215 224
FT HELIX 227 230
FT HELIX 233 235
FT STRAND 241 245
FT HELIX 254 256
FT TURN 266 273
FT HELIX 290 307
FT STRAND 312 320
FT STRAND 328 333
FT HELIX 342 352
FT HELIX 357 364
FT TURN 365 367
FT HELIX 371 374
FT STRAND 375 377
FT STRAND 379 382
FT HELIX 386 388
SQ SEQUENCE 395 AA; 43661 MW; 2E7D1B91CC4F7BDD CRC64;
MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQISDA VLDAHLQQDP DAKVACETVA
KTGMILLAGE ITSRAAVDYQ KVVREAVKHI GYDDSSKGFD YKTCNVLVAL EQQSPDIAQG
VHLDRNEEDI GAGDQGLMFG YATDETEECM PLTIVLAHKL NAKLAELRRN GTLPWLRPDS
KTQVTVQYMQ DRGAVLPIRV HTIVISVQHD EEVCLDEMRD ALKEKVIKAV VPAKYLDEDT
IYHLQPSGRF VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW
VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK KNFDLRPGVI
VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY
//
ID METK2_HUMAN Reviewed; 395 AA.
AC P31153; A8K511; D6W5L1; Q53SP5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1993, sequence version 1.
DT 22-JAN-2014, entry version 143.
DE RecName: Full=S-adenosylmethionine synthase isoform type-2;
DE Short=AdoMet synthase 2;
DE EC=2.5.1.6;
DE AltName: Full=Methionine adenosyltransferase 2;
DE Short=MAT 2;
DE AltName: Full=Methionine adenosyltransferase II;
DE Short=MAT-II;
GN Name=MAT2A; Synonyms=AMS2, MATA2;
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].
RC TISSUE=Kidney;
RX PubMed=1426236; DOI=10.1016/0014-5793(92)81405-B;
RA Horikawa S., Tsukada K.;
RT "Molecular cloning and developmental expression of a human kidney S-
RT adenosylmethionine synthetase.";
RL FEBS Lett. 312:37-41(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=16413417; DOI=10.1016/j.freeradbiomed.2005.09.004;
RA Panayiotidis M.I., Stabler S.P., Ahmad A., Pappa A., Legros L.H. Jr.,
RA Hernandez-Saavedra D., Schneider B.K., Allen R.H., Vasiliou V.,
RA McCord J.M., Kotb M., White C.W.;
RT "Activation of a novel isoform of methionine adenosyl transferase 2A
RT and increased S-adenosylmethionine turnover in lung epithelial cells
RT exposed to hyperoxia.";
RL Free Radic. Biol. Med. 40:348-358(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [7]
RP SUBUNIT.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
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: Catalyzes the formation of S-adenosylmethionine from
CC methionine and ATP.
CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate +
CC diphosphate + S-adenosyl-L-methionine.
CC -!- COFACTOR: Binds 2 divalent ions per subunit. Magnesium or cobalt
CC (By similarity).
CC -!- COFACTOR: Binds 1 potassium ion per subunit (By similarity).
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 -!- PTM: The alpha' subunit is a post-translationally modified version
CC of MAT2A.
CC -!- SIMILARITY: Belongs to the AdoMet synthase family.
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DR EMBL; X68836; CAA48726.1; -; mRNA.
DR EMBL; DQ083239; AAY85355.1; -; mRNA.
DR EMBL; AK291126; BAF83815.1; -; mRNA.
DR EMBL; AC016753; AAY24339.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99511.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99513.1; -; Genomic_DNA.
DR EMBL; BC001686; AAH01686.1; -; mRNA.
DR EMBL; BC001854; AAH01854.1; -; mRNA.
DR PIR; S27257; S27257.
DR RefSeq; NP_005902.1; NM_005911.5.
DR UniGene; Hs.516157; -.
DR PDB; 2P02; X-ray; 1.21 A; A=1-395.
DR PDBsum; 2P02; -.
DR ProteinModelPortal; P31153; -.
DR SMR; P31153; 16-395.
DR IntAct; P31153; 17.
DR STRING; 9606.ENSP00000303147; -.
DR DrugBank; DB00134; L-Methionine.
DR DrugBank; DB00118; S-Adenosylmethionine.
DR PhosphoSite; P31153; -.
DR DMDM; 400245; -.
DR REPRODUCTION-2DPAGE; IPI00010157; -.
DR PaxDb; P31153; -.
DR PeptideAtlas; P31153; -.
DR PRIDE; P31153; -.
DR DNASU; 4144; -.
DR Ensembl; ENST00000306434; ENSP00000303147; ENSG00000168906.
DR GeneID; 4144; -.
DR KEGG; hsa:4144; -.
DR UCSC; uc002spr.3; human.
DR CTD; 4144; -.
DR GeneCards; GC02P085766; -.
DR H-InvDB; HIX0117562; -.
DR HGNC; HGNC:6904; MAT2A.
DR HPA; CAB009968; -.
DR HPA; HPA043028; -.
DR MIM; 601468; gene.
DR neXtProt; NX_P31153; -.
DR PharmGKB; PA30647; -.
DR eggNOG; COG0192; -.
DR HOGENOM; HOG000245710; -.
DR HOVERGEN; HBG001562; -.
DR InParanoid; P31153; -.
DR KO; K00789; -.
DR OMA; YYAHKIL; -.
DR PhylomeDB; P31153; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00315; UER00080.
DR ChiTaRS; MAT2A; human.
DR EvolutionaryTrace; P31153; -.
DR GenomeRNAi; 4144; -.
DR NextBio; 16276; -.
DR PRO; PR:P31153; -.
DR ArrayExpress; P31153; -.
DR Bgee; P31153; -.
DR CleanEx; HS_MAT2A; -.
DR Genevestigator; P31153; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
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; IEA:UniProtKB-UniPathway.
DR GO; GO:0000096; P:sulfur amino acid metabolic process; TAS:Reactome.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR InterPro; IPR022631; ADOMET_SYNTHASE_CS.
DR InterPro; IPR022630; S-AdoMet_synt_C.
DR InterPro; IPR022629; S-AdoMet_synt_central.
DR InterPro; IPR022628; S-AdoMet_synt_N.
DR InterPro; IPR002133; S-AdoMet_synthetase.
DR InterPro; IPR022636; S-AdoMet_synthetase_sfam.
DR PANTHER; PTHR11964; PTHR11964; 1.
DR Pfam; PF02773; S-AdoMet_synt_C; 1.
DR Pfam; PF02772; S-AdoMet_synt_M; 1.
DR Pfam; PF00438; S-AdoMet_synt_N; 1.
DR PIRSF; PIRSF000497; MAT; 1.
DR SUPFAM; SSF55973; SSF55973; 3.
DR TIGRFAMs; TIGR01034; metK; 1.
DR PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
DR PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cobalt; Complete proteome;
KW Magnesium; Metal-binding; Nucleotide-binding; One-carbon metabolism;
KW Phosphoprotein; Potassium; Reference proteome; Transferase.
FT CHAIN 1 395 S-adenosylmethionine synthase isoform
FT type-2.
FT /FTId=PRO_0000174435.
FT NP_BIND 131 136 ATP (Potential).
FT METAL 31 31 Magnesium (By similarity).
FT METAL 57 57 Potassium (By similarity).
FT METAL 283 283 Potassium (By similarity).
FT METAL 291 291 Magnesium (By similarity).
FT BINDING 159 159 ATP (Potential).
FT MOD_RES 81 81 N6-acetyllysine.
FT MOD_RES 114 114 Phosphoserine.
FT STRAND 17 25
FT HELIX 30 48
FT STRAND 53 61
FT STRAND 64 72
FT HELIX 79 90
FT HELIX 95 97
FT TURN 101 103
FT STRAND 104 111
FT HELIX 115 121
FT TURN 122 124
FT HELIX 127 129
FT STRAND 132 134
FT STRAND 136 143
FT HELIX 152 169
FT STRAND 176 191
FT STRAND 194 209
FT HELIX 215 224
FT HELIX 227 230
FT HELIX 233 235
FT STRAND 241 245
FT HELIX 254 256
FT TURN 266 273
FT HELIX 290 307
FT STRAND 312 320
FT STRAND 328 333
FT HELIX 342 352
FT HELIX 357 364
FT TURN 365 367
FT HELIX 371 374
FT STRAND 375 377
FT STRAND 379 382
FT HELIX 386 388
SQ SEQUENCE 395 AA; 43661 MW; 2E7D1B91CC4F7BDD CRC64;
MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQISDA VLDAHLQQDP DAKVACETVA
KTGMILLAGE ITSRAAVDYQ KVVREAVKHI GYDDSSKGFD YKTCNVLVAL EQQSPDIAQG
VHLDRNEEDI GAGDQGLMFG YATDETEECM PLTIVLAHKL NAKLAELRRN GTLPWLRPDS
KTQVTVQYMQ DRGAVLPIRV HTIVISVQHD EEVCLDEMRD ALKEKVIKAV VPAKYLDEDT
IYHLQPSGRF VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW
VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK KNFDLRPGVI
VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY
//
MIM
601468
*RECORD*
*FIELD* NO
601468
*FIELD* TI
*601468 METHIONINE ADENOSYLTRANSFERASE II, ALPHA; MAT2A
;;MATA2;;
MAT II, KIDNEY-SPECIFIC;;
read moreS-ADENOSYLMETHIONINE SYNTHETASE 2; SAMS2
*FIELD* TX
Methionine adenosyltransferase (EC 2.5.1.6) catalyzes the biosynthesis
of S-adenosylmethionine (AdoMet) from methionine and ATP. AdoMet is the
major methyl donor for many of the transmethylation reactions in the
body. Chamberlin et al. (1996) noted that AdoMet also participates in
the transsulfuration pathway and, after decarboxylation, serves as a
propylamine group donor in the biosynthesis of polyamines. Three forms
of MAT have been identified in mammalian tissues. MAT I and MAT III,
which are encoded by the single-copy MAT1A gene (610550), represent
tetramers and dimers, respectively, formed from identical alpha-1
subunits and are synthesized primarily in the liver. MAT II, encoded by
a separate gene, which was cloned by Horikawa and Tsukada (1992), is
found in fetal liver (and to a lesser extent in adult liver) as well as
in kidney, brain, testis, and lymphocytes. Horikawa and Tsukada (1992)
showed that the 395-amino acid MAT II shares 84% amino acid similarity
with the human liver MAT I/III protein.
Mao et al. (1998) cloned the 5-prime flanking region of the MAT2A gene.
They identified 2 major transcriptional start sites, one located within
10 nucleotides downstream and the other 158 nucleotides upstream from
the TATA box. The MAT2A promoter is highly GC rich, especially in the
first 300 bp. The promoter contains several potential SP1-, v-myb-, and
GATA-binding sites, as well as potential binding sites for C/EBP, HSF2,
c-myb, and STATx. Mao et al. (1998) showed that the MAT2A promoter can
efficiently drive expression from a reporter gene in both Jurkat and 293
cells. The authors identified regions of the promoter that are important
for cell-specific MAT2A expression.
By in situ hybridization, De La Rosa et al. (1995) mapped the MATA2 gene
to 2p11.2.
*FIELD* RF
1. Chamberlin, M. E.; Ubagai, T.; Mudd, S. H.; Wilson, W. G.; Leonard,
J. V.; Chou, J. Y.: Demyelination of the brain is associated with
methionine adenosyltransferase I/III deficiency. J. Clin. Invest. 98:
1021-1027, 1996.
2. De La Rosa, J.; Ostrowski, J.; Hryniewicz, M. M.; Kredich, N. M.;
Kotb, M.; LeGros, H. L., Jr.; Valentine, M.; Geller, A. M.: Chromosomal
localization and catalytic properties of the recombinant alpha subunit
of human lymphocyte methionine adenosyltransferase. J. Biol. Chem. 270:
21860-21868, 1995.
3. Horikawa, S.; Tsukada, K.: Molecular cloning and developmental
expression of a human kidney S-adenosylmethionine synthetase. FEBS
Lett. 312: 37-41, 1992.
4. Mao, Z.; Liu, S.; Cai, J.; Huang, Z.-Z.; Lu, S. C.: Cloning and
functional characterization of the 5-prime-flanking region of human
methionine adenosyltransferase 2A gene. Biochem. Biophys. Res. Commun. 248:
479-484, 1998.
*FIELD* CN
Patti M. Sherman - updated: 5/31/2000
*FIELD* CD
Victor A. McKusick: 10/15/1996
*FIELD* ED
carol: 11/10/2006
carol: 6/7/2000
psherman: 5/31/2000
dkim: 12/16/1998
terry: 3/13/1997
mark: 10/15/1996
*RECORD*
*FIELD* NO
601468
*FIELD* TI
*601468 METHIONINE ADENOSYLTRANSFERASE II, ALPHA; MAT2A
;;MATA2;;
MAT II, KIDNEY-SPECIFIC;;
read moreS-ADENOSYLMETHIONINE SYNTHETASE 2; SAMS2
*FIELD* TX
Methionine adenosyltransferase (EC 2.5.1.6) catalyzes the biosynthesis
of S-adenosylmethionine (AdoMet) from methionine and ATP. AdoMet is the
major methyl donor for many of the transmethylation reactions in the
body. Chamberlin et al. (1996) noted that AdoMet also participates in
the transsulfuration pathway and, after decarboxylation, serves as a
propylamine group donor in the biosynthesis of polyamines. Three forms
of MAT have been identified in mammalian tissues. MAT I and MAT III,
which are encoded by the single-copy MAT1A gene (610550), represent
tetramers and dimers, respectively, formed from identical alpha-1
subunits and are synthesized primarily in the liver. MAT II, encoded by
a separate gene, which was cloned by Horikawa and Tsukada (1992), is
found in fetal liver (and to a lesser extent in adult liver) as well as
in kidney, brain, testis, and lymphocytes. Horikawa and Tsukada (1992)
showed that the 395-amino acid MAT II shares 84% amino acid similarity
with the human liver MAT I/III protein.
Mao et al. (1998) cloned the 5-prime flanking region of the MAT2A gene.
They identified 2 major transcriptional start sites, one located within
10 nucleotides downstream and the other 158 nucleotides upstream from
the TATA box. The MAT2A promoter is highly GC rich, especially in the
first 300 bp. The promoter contains several potential SP1-, v-myb-, and
GATA-binding sites, as well as potential binding sites for C/EBP, HSF2,
c-myb, and STATx. Mao et al. (1998) showed that the MAT2A promoter can
efficiently drive expression from a reporter gene in both Jurkat and 293
cells. The authors identified regions of the promoter that are important
for cell-specific MAT2A expression.
By in situ hybridization, De La Rosa et al. (1995) mapped the MATA2 gene
to 2p11.2.
*FIELD* RF
1. Chamberlin, M. E.; Ubagai, T.; Mudd, S. H.; Wilson, W. G.; Leonard,
J. V.; Chou, J. Y.: Demyelination of the brain is associated with
methionine adenosyltransferase I/III deficiency. J. Clin. Invest. 98:
1021-1027, 1996.
2. De La Rosa, J.; Ostrowski, J.; Hryniewicz, M. M.; Kredich, N. M.;
Kotb, M.; LeGros, H. L., Jr.; Valentine, M.; Geller, A. M.: Chromosomal
localization and catalytic properties of the recombinant alpha subunit
of human lymphocyte methionine adenosyltransferase. J. Biol. Chem. 270:
21860-21868, 1995.
3. Horikawa, S.; Tsukada, K.: Molecular cloning and developmental
expression of a human kidney S-adenosylmethionine synthetase. FEBS
Lett. 312: 37-41, 1992.
4. Mao, Z.; Liu, S.; Cai, J.; Huang, Z.-Z.; Lu, S. C.: Cloning and
functional characterization of the 5-prime-flanking region of human
methionine adenosyltransferase 2A gene. Biochem. Biophys. Res. Commun. 248:
479-484, 1998.
*FIELD* CN
Patti M. Sherman - updated: 5/31/2000
*FIELD* CD
Victor A. McKusick: 10/15/1996
*FIELD* ED
carol: 11/10/2006
carol: 6/7/2000
psherman: 5/31/2000
dkim: 12/16/1998
terry: 3/13/1997
mark: 10/15/1996