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Q9H2M3 (BHMT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-methylmethionine--homocysteine S-methyltransferase BHMT2

Short name=SMM-hcy methyltransferase
EC=2.1.1.10
Alternative name(s):
Betaine--homocysteine S-methyltransferase 2
Gene names
Name:BHMT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the regulation of homocysteine metabolism. Converts homocysteine to methionine using S-methylmethionine (SMM) as a methyl donor. Ref.5

Catalytic activity

S-methyl-L-methionine + L-homocysteine = 2 L-methionine. Ref.5

Cofactor

Binds 1 zinc ion per subunit. Ref.5

Pathway

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 caution

The sequence BAA90880.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H2M3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9H2M3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     87-150: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 363363S-methylmethionine--homocysteine S-methyltransferase BHMT2
PRO_0000273224

Regions

Domain11 – 305295Hcy-binding

Sites

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

Amino acid modifications

Modified residue3211Phosphoserine By similarity

Natural variations

Alternative sequence87 – 15064Missing in isoform 2.
VSP_042938

Sequences

Sequence LengthMass (Da)Tools
Isoform 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 


PDF 

« Hide

Isoform 2 [UniParc].

Checksum: 763335314695E79E
Show »

FASTA29933,167

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, POSSIBLE INTERACTION WITH PRNP.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-363 (ISOFORM 1).
Tissue: Adipose tissue and Kidney.
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Liver.
[5]"Betaine-homocysteine S-methyltransferase-2 is an S-methylmethionine-homocysteine methyltransferase."
Szegedi S.S., Castro C.C., Koutmos M., Garrow T.A.
J. Biol. Chem. 283:8939-8945(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ZINC-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF257473 mRNA. Translation: AAG41356.1.
AK000008 mRNA. Translation: BAA90880.1. Different initiation.
AK298298 mRNA. Translation: BAH12752.1.
AC008502 Genomic DNA. No translation available.
BC020665 mRNA. Translation: AAH20665.1.
CCDSCCDS4045.1. [Q9H2M3-1]
CCDS54871.1. [Q9H2M3-2]
RefSeqNP_001171476.1. NM_001178005.1. [Q9H2M3-2]
NP_060084.2. NM_017614.4. [Q9H2M3-1]
UniGeneHs.114172.

3D structure databases

ProteinModelPortalQ9H2M3.
SMRQ9H2M3. Positions 10-362.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117245. 1 interaction.
STRING9606.ENSP00000255192.

Chemistry

ChEMBLCHEMBL2163167.
DrugBankDB00134. L-Methionine.

PTM databases

PhosphoSiteQ9H2M3.

Polymorphism databases

DMDM74733563.

Proteomic databases

PaxDbQ9H2M3.
PRIDEQ9H2M3.

Protocols and materials databases

DNASU23743.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000255192; ENSP00000255192; ENSG00000132840. [Q9H2M3-1]
ENST00000521567; ENSP00000430278; ENSG00000132840. [Q9H2M3-2]
GeneID23743.
KEGGhsa:23743.
UCSCuc003kft.3. human. [Q9H2M3-1]
uc011cth.2. human. [Q9H2M3-2]

Organism-specific databases

CTD23743.
GeneCardsGC05P078401.
HGNCHGNC:1048. BHMT2.
HPAHPA044573.
MIM605932. gene.
neXtProtNX_Q9H2M3.
PharmGKBPA25351.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0646.
HOGENOMHOG000231636.
HOVERGENHBG080367.
InParanoidQ9H2M3.
OMAPEGDMHD.
OrthoDBEOG79GT7C.
PhylomeDBQ9H2M3.
TreeFamTF329202.

Enzyme and pathway databases

BioCycMetaCyc:HS05696-MONOMER.
UniPathwayUPA00051; UER00083.

Gene expression databases

ArrayExpressQ9H2M3.
BgeeQ9H2M3.
CleanExHS_BHMT2.
GenevestigatorQ9H2M3.

Family and domain databases

Gene3D3.20.20.330. 1 hit.
InterProIPR017226. Betaine-hCys_S-MeTrfase_BHMT.
IPR003726. S_MeTrfase.
[Graphical view]
PfamPF02574. S-methyl_trans. 1 hit.
[Graphical view]
PIRSFPIRSF037505. Betaine_HMT. 1 hit.
SUPFAMSSF82282. SSF82282. 1 hit.
PROSITEPS50970. HCY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBHMT2. human.
GenomeRNAi23743.
NextBio46663.
PROQ9H2M3.
SOURCESearch...

Entry information

Entry nameBHMT2_HUMAN
AccessionPrimary (citable) accession number: Q9H2M3
Secondary accession number(s): B7Z516, Q9NXX7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 5

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