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Reviewed, UniProtKB/Swiss-Prot Q9H2M3 (BHMT2_HUMAN)

Last modified November 3, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Betaine--homocysteine S-methyltransferase 2
    EC=2.1.1.5
Gene names
Name: BHMT2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline By similarity.

Catalytic activity

Trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

Amine and polyamine degradation; betaine degradation; sarcosine from betaine: step 1/2.

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (BhmT route): step 1/1.

Subunit structure

Homotetramer By similarity. May interact with PRNP.

Tissue specificity

Expressed in liver and kidney and at reduced levels in the brain, heart, and skeletal muscle. Ref.1

Sequence similarities

Contains 1 Hcy-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 363363Betaine--homocysteine S-methyltransferase 2
PRO_0000273224

Regions

Domain11 – 305295Hcy-binding

Sites

Metal binding2081Zinc By similarity
Metal binding2901Zinc By similarity
Metal binding2911Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9H2M3-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 92D35414D2D56003

FASTA36340,354
        10         20         30         40         50         60 
MAPAGRPGAK KGILERLESG EVVIGDGSFL ITLEKRGYVK AGLWTPEAVI EHPDAVRQLH 

        70         80         90        100        110        120 
MEFLRAGSNV MQTFTFSASE DNMESKWEDV NAAACDLARE VAGKGDALVA GGICQTSIYK 

       130        140        150        160        170        180 
YQKDEARIKK LFRQQLEVFA WKNVDFLIAE YFEHVEEAVW AVEVLKESDR PVAVTMCIGP 

       190        200        210        220        230        240 
EGDMHDITPG ECAVRLVKAG ASIVGVNCRF GPDTSLKTME LMKEGLEWAG LKAHLMVQPL 

       250        260        270        280        290        300 
GFHAPDCGKE GFVDLPEYPF GLESRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA 

       310        320        330        340        350        360 
IAEELAPERG FLPPASEKHG SWGSGLDMHT KPWIRARARR EYWENLLPAS GRPFCPSLSK 


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References

« Hide 'large scale' references
[1]"Betaine-homocysteine methyltransferase-2: cDNA cloning, gene sequence, physical mapping, and expression of the human and mouse genes."
Chadwick L.H., McCandless S.E., Silverman G.L., Schwartz S., Westaway D., Nadeau J.H.
Genomics 70:66-73(2000) [PubMed: 11087663] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, POSSIBLE INTERACTION WITH PRNP.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-363.
Tissue: Adipose tissue.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF257473 mRNA. Translation: AAG41356.1.
BC020665 mRNA. Translation: AAH20665.1.
AK000008 mRNA. Translation: BAA90880.1. Different initiation.
IPIIPI00014363.
RefSeqNP_060084.2.
UniGeneHs.114172

3D structure databases

HSSPHSSP built from PDB template 1LT7 based on UniProtKB Q93088.
SMRQ9H2M3. Positions 10-362.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9H2M3.

PTM databases

PhosphoSiteQ9H2M3.

Proteomic databases

PRIDEQ9H2M3.

Genome annotation databases

EnsemblENST00000255192; ENSP00000255192; ENSG00000132840; Homo sapiens. [Genome view]
GeneID23743.
KEGGhsa:23743.
NMPDRfig|9606.3.peg.25449.
UCSCuc003kft.1. human.

Organism-specific databases

CTD23743.
GeneCardsGC05P078401.
HGNCHGNC:1048. BHMT2.
MIM605932. gene.
PharmGKBPA25351.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9H2M3.
OMAKGGFVDL.

Enzyme and pathway databases

BRENDA2.1.1.5. 247.

Gene expression databases

ArrayExpressQ9H2M3.
BgeeQ9H2M3.
CleanExHS_BHMT2.
GenevestigatorQ9H2M3.

Family and domain databases

InterProIPR017226. Betaine-hCys_S-MeTrfase_BHMT.
IPR003726. S_MeTrfase.
[Graphical view]
Gene3DG3DSA:3.20.20.330. S_methyl_trans. 1 hit.
PfamPF02574. S-methyl_trans. 1 hit.
[Graphical view]
PIRSFPIRSF037505. Betaine_HMT. 1 hit.
PROSITEPS50970. HCY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00134. L-Methionine.
NextBio46663.
SOURCESearch...

Entry information

Entry nameBHMT2_HUMAN
AccessionPrimary (citable) accession number: Q9H2M3
Secondary accession number(s): Q9NXX7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: March 1, 2001
Last modified: November 3, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents