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Database: UniProt
Entry: Q9H2M3
LinkDB: Q9H2M3
Original site: Q9H2M3 
ID   BHMT2_HUMAN             Reviewed;         363 AA.
AC   Q9H2M3; B7Z516; Q9NXX7;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   01-OCT-2014, entry version 102.
DE   RecName: Full=S-methylmethionine--homocysteine S-methyltransferase BHMT2;
DE            Short=SMM-hcy methyltransferase;
DE            EC=2.1.1.10;
DE   AltName: Full=Betaine--homocysteine S-methyltransferase 2;
GN   Name=BHMT2;
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), TISSUE SPECIFICITY, AND
RP   POSSIBLE INTERACTION WITH PRNP.
RX   PubMed=11087663; DOI=10.1006/geno.2000.6319;
RA   Chadwick L.H., McCandless S.E., Silverman G.L., Schwartz S.,
RA   Westaway D., Nadeau J.H.;
RT   "Betaine-homocysteine methyltransferase-2: cDNA cloning, gene
RT   sequence, physical mapping, and expression of the human and mouse
RT   genes.";
RL   Genomics 70:66-73(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 11-363 (ISOFORM 1).
RC   TISSUE=Adipose tissue, and Kidney;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA   Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA   Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA   Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA   Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA   Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA   Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA   Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA   Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
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   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND ZINC-BINDING.
RX   PubMed=18230605; DOI=10.1074/jbc.M710449200;
RA   Szegedi S.S., Castro C.C., Koutmos M., Garrow T.A.;
RT   "Betaine-homocysteine S-methyltransferase-2 is an S-methylmethionine-
RT   homocysteine methyltransferase.";
RL   J. Biol. Chem. 283:8939-8945(2008).
CC   -!- FUNCTION: Involved in the regulation of homocysteine metabolism.
CC       Converts homocysteine to methionine using S-methylmethionine (SMM)
CC       as a methyl donor. {ECO:0000269|PubMed:18230605}.
CC   -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L-
CC       methionine. {ECO:0000269|PubMed:18230605}.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit.
CC       {ECO:0000269|PubMed:18230605}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-methionine from L-homocysteine (BhmT route): step
CC       1/1.
CC   -!- SUBUNIT: Homotetramer (By similarity). May interact with PRNP.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H2M3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H2M3-2; Sequence=VSP_042938;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in liver and kidney and at reduced
CC       levels in the brain, heart, and skeletal muscle.
CC       {ECO:0000269|PubMed:11087663}.
CC   -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00333}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA90880.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF257473; AAG41356.1; -; mRNA.
DR   EMBL; AK000008; BAA90880.1; ALT_INIT; mRNA.
DR   EMBL; AK298298; BAH12752.1; -; mRNA.
DR   EMBL; AC008502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC020665; AAH20665.1; -; mRNA.
DR   CCDS; CCDS4045.1; -. [Q9H2M3-1]
DR   CCDS; CCDS54871.1; -. [Q9H2M3-2]
DR   RefSeq; NP_001171476.1; NM_001178005.1. [Q9H2M3-2]
DR   RefSeq; NP_060084.2; NM_017614.4. [Q9H2M3-1]
DR   UniGene; Hs.114172; -.
DR   ProteinModelPortal; Q9H2M3; -.
DR   SMR; Q9H2M3; 10-362.
DR   BioGrid; 117245; 1.
DR   STRING; 9606.ENSP00000255192; -.
DR   ChEMBL; CHEMBL2163167; -.
DR   DrugBank; DB00134; L-Methionine.
DR   PhosphoSite; Q9H2M3; -.
DR   DMDM; 74733563; -.
DR   PaxDb; Q9H2M3; -.
DR   PRIDE; Q9H2M3; -.
DR   DNASU; 23743; -.
DR   Ensembl; ENST00000255192; ENSP00000255192; ENSG00000132840. [Q9H2M3-1]
DR   Ensembl; ENST00000521567; ENSP00000430278; ENSG00000132840. [Q9H2M3-2]
DR   GeneID; 23743; -.
DR   KEGG; hsa:23743; -.
DR   UCSC; uc003kft.3; human. [Q9H2M3-1]
DR   UCSC; uc011cth.2; human. [Q9H2M3-2]
DR   CTD; 23743; -.
DR   GeneCards; GC05P078401; -.
DR   HGNC; HGNC:1048; BHMT2.
DR   HPA; HPA044573; -.
DR   MIM; 605932; gene.
DR   neXtProt; NX_Q9H2M3; -.
DR   PharmGKB; PA25351; -.
DR   eggNOG; COG0646; -.
DR   HOGENOM; HOG000231636; -.
DR   HOVERGEN; HBG080367; -.
DR   InParanoid; Q9H2M3; -.
DR   OMA; PEGDMHD; -.
DR   OrthoDB; EOG79GT7C; -.
DR   PhylomeDB; Q9H2M3; -.
DR   TreeFam; TF329202; -.
DR   BioCyc; MetaCyc:HS05696-MONOMER; -.
DR   UniPathway; UPA00051; UER00083.
DR   ChiTaRS; BHMT2; human.
DR   GenomeRNAi; 23743; -.
DR   NextBio; 46663; -.
DR   PRO; PR:Q9H2M3; -.
DR   ArrayExpress; Q9H2M3; -.
DR   Bgee; Q9H2M3; -.
DR   CleanEx; HS_BHMT2; -.
DR   Genevestigator; Q9H2M3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt.
DR   GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IDA:BHF-UCL.
DR   GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IDA:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IDA:BHF-UCL.
DR   GO; GO:0071267; P:L-methionine salvage; IDA:BHF-UCL.
DR   GO; GO:0046500; P:S-adenosylmethionine metabolic process; IDA:BHF-UCL.
DR   GO; GO:0033477; P:S-methylmethionine metabolic process; IDA:BHF-UCL.
DR   Gene3D; 3.20.20.330; -; 1.
DR   InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT.
DR   InterPro; IPR003726; S_MeTrfase.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   PIRSF; PIRSF037505; Betaine_HMT; 1.
DR   SUPFAM; SSF82282; SSF82282; 1.
DR   PROSITE; PS50970; HCY; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Metal-binding;
KW   Methyltransferase; Phosphoprotein; Reference proteome; Transferase;
KW   Zinc.
FT   CHAIN         1    363       S-methylmethionine--homocysteine S-
FT                                methyltransferase BHMT2.
FT                                /FTId=PRO_0000273224.
FT   DOMAIN       11    305       Hcy-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   METAL       208    208       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   METAL       290    290       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   METAL       291    291       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   MOD_RES     321    321       Phosphoserine. {ECO:0000250}.
FT   VAR_SEQ      87    150       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_042938.
SQ   SEQUENCE   363 AA;  40354 MW;  92D35414D2D56003 CRC64;
     MAPAGRPGAK KGILERLESG EVVIGDGSFL ITLEKRGYVK AGLWTPEAVI EHPDAVRQLH
     MEFLRAGSNV MQTFTFSASE DNMESKWEDV NAAACDLARE VAGKGDALVA GGICQTSIYK
     YQKDEARIKK LFRQQLEVFA WKNVDFLIAE YFEHVEEAVW AVEVLKESDR PVAVTMCIGP
     EGDMHDITPG ECAVRLVKAG ASIVGVNCRF GPDTSLKTME LMKEGLEWAG LKAHLMVQPL
     GFHAPDCGKE GFVDLPEYPF GLESRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA
     IAEELAPERG FLPPASEKHG SWGSGLDMHT KPWIRARARR EYWENLLPAS GRPFCPSLSK
     PDF
//
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