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Q91VF2 (HNMT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histamine N-methyltransferase
Short name=HMT
EC=2.1.1.8
Gene names
Name:Hnmt
Synonyms:Hmt
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine By similarity.

Catalytic activity

S-adenosyl-L-methionine + histamine = S-adenosyl-L-homocysteine + N(tau)-methylhistamine.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the methyltransferase superfamily. HNMT family.

Biophysicochemical properties

Kinetic parameters:

KM=5.8 µM for S-adenosyl-L-methionine Ref.1

KM=5.3 µM for histamine

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Histamine N-methyltransferase
PRO_0000084022

Sites

Binding site281Substrate By similarity
Binding site601S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site891S-adenosyl-L-methionine By similarity
Binding site941S-adenosyl-L-methionine By similarity
Binding site1201S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site1431S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site2841Substrate By similarity

Amino acid modifications

Modified residue31Phosphoserine Ref.5
Modified residue101Phosphoserine Ref.5
Modified residue181Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q91VF2 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 04FA324ED14A51CA

FASTA29533,665
        10         20         30         40         50         60 
MASCMRSLFS DQGRYVESFR RFLNNSTEHQ CMQEFMDKKL PGIIARIGEA KAEIKILSVG 

        70         80         90        100        110        120 
GGAGEVDLQI LSKVQAQYPG ICINNEVVEP SAEQIVKYKE LVAKTSNMEN IKFSWHKETS 

       130        140        150        160        170        180 
SEYQKRMLEE EEEPPKWDFI HMIQMLYYVK DIPATLKFFH GLLAASAKIL IILVSGTSGW 

       190        200        210        220        230        240 
EKLWKKYGSR LPRDDLCQYV TSSDLAQILD DLGIKYECYD LVSTMDITDC FIDGNENGDL 

       250        260        270        280        290 
LWDFLTETCN FSKTAPLDLK AEIMKDLQEP EFSVKKEGKV LFNNNLSFIV VEANV

« Hide

References

« Hide 'large scale' references
[1]"Mouse histamine N-methyltransferase: cDNA cloning, expression, gene cloning and chromosomal localization."
Wang L., Yan L., McGuire C., Kozak C.A., Wang M., Kim U.J., Siciliano M., Weinshilboum R.M.
Inflamm. Res. 50:300-308(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], BIOPHYSICOCHEMICAL PROPERTIES.
Strain: BALB/c.
Tissue: Liver.
[2]"Genomic structure of the rat and mouse histamine N-methyltransferase gene."
Kitanaka N., Kitanaka J., Oue T., Tada Y., Tanaka T., Takemura M.
Jpn. J. Pharmacol. 88:85-92(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/Sv and ddY.
Tissue: Liver.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum and Liver.
[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].
Tissue: Mammary gland.
[5]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-10 AND SER-18, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF297037 mRNA. Translation: AAL09305.1.
AF298150 expand/collapse EMBL AC list , AF297039, AF297040, AF297041, AF297042, AF297043 Genomic DNA. Translation: AAL09306.1.
AB070523 Genomic DNA. Translation: BAB84320.1.
AB070524 mRNA. Translation: BAB84318.1.
AK050129 mRNA. Translation: BAC34081.1.
AK160131 mRNA. Translation: BAE35648.1.
BC033928 mRNA. Translation: AAH33928.1.
IPIIPI00126826.
RefSeqNP_536710.1. NM_080462.2.
UniGeneMm.33120.

3D structure databases

ProteinModelPortalQ91VF2.
SMRQ91VF2. Positions 5-293.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000110141.

PTM databases

PhosphoSiteQ91VF2.

Proteomic databases

PaxDbQ91VF2.
PRIDEQ91VF2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000051416; ENSMUSP00000062747; ENSMUSG00000026986.
ENSMUST00000114497; ENSMUSP00000110141; ENSMUSG00000026986.
ENSMUST00000114498; ENSMUSP00000110142; ENSMUSG00000026986.
GeneID140483.
KEGGmmu:140483.

Organism-specific databases

CTD3176.
MGIMGI:2153181. Hnmt.

Phylogenomic databases

eggNOGNOG39680.
GeneTreeENSGT00390000002862.
HOGENOMHOG000231790.
HOVERGENHBG051914.
InParanoidQ91VF2.
KOK00546.
OMAWKKYGSR.
OrthoDBEOG4NCMDJ.

Gene expression databases

ArrayExpressQ91VF2.
BgeeQ91VF2.
CleanExMM_HNMT.
GenevestigatorQ91VF2.
GermOnlineENSMUSG00000026986. Mus musculus.

Family and domain databases

InterProIPR016673. Histamine_N-methyltransferase.
[Graphical view]
PANTHERPTHR32330. PTHR32330. 1 hit.
PIRSFPIRSF016616. HHMT. 1 hit.
ProtoNetSearch...

Other

NextBio369786.
SOURCESearch...

Entry information

Entry nameHNMT_MOUSE
AccessionPrimary (citable) accession number: Q91VF2
Secondary accession number(s): Q3TVH0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: December 1, 2001
Last modified: April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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