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P21964 (COMT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Catechol O-methyltransferase

EC=2.1.1.6
Gene names
Name:COMT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.

Catalytic activity

S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol.

Cofactor

Binds 1 magnesium ion per subunit.

Subcellular location

Isoform Soluble: Cytoplasm.

Isoform Membrane-bound: Cell membrane; Single-pass type II membrane protein; Extracellular side.

Tissue specificity

Brain, liver, placenta, lymphocytes and erythrocytes.

Post-translational modification

The N-terminus is blocked.

Polymorphism

Two alleles, COMT*1 or COMT*H with Val-158 and COMT*2 or COMT*L with Met-158 are responsible for a three to four-fold difference in enzymatic activity.

Low enzyme activity alleles are associated with genetic susceptibility to alcoholism [MIM:103780].

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family.

Mass spectrometry

Molecular mass is 24352±2 Da from positions 52 - 271. Determined by ESI. Ref.11

Ontologies

Keywords
   Biological processCatecholamine metabolism
Neurotransmitter degradation
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative initiation
Polymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandMagnesium
Metal-binding
S-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdopamine catabolic process

Inferred from electronic annotation. Source: Ensembl

estrogen metabolic process

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from electronic annotation. Source: Ensembl

learning

Inferred from electronic annotation. Source: Ensembl

methylation

Traceable author statement. Source: Reactome

multicellular organismal reproductive process

Inferred from electronic annotation. Source: Ensembl

negative regulation of dopamine metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

neurotransmitter biosynthetic process

Traceable author statement. Source: Reactome

neurotransmitter catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of homocysteine metabolic process

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

response to pain

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrion

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionO-methyltransferase activity

Traceable author statement Ref.1. Source: ProtInc

catechol O-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

XRN2Q9H0D61EBI-372265,EBI-372110

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Membrane-bound (identifier: P21964-1)

Also known as: MB-COMT;

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 Soluble (identifier: P21964-2)

Also known as: S-COMT;

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Catechol O-methyltransferase
PRO_0000020971

Regions

Transmembrane7 – 2620Helical; Signal-anchor for type II membrane protein; Potential
Region167 – 1704S-adenosyl-L-methionine binding

Sites

Metal binding1911Magnesium
Metal binding2191Magnesium
Metal binding2201Magnesium
Binding site921S-adenosyl-L-methionine; via amide nitrogen
Binding site1141S-adenosyl-L-methionine By similarity
Binding site1221S-adenosyl-L-methionine
Binding site1401S-adenosyl-L-methionine
Binding site1411S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site1691S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site1911S-adenosyl-L-methionine
Binding site1941Substrate
Binding site2201Substrate
Binding site2491Substrate

Natural variations

Alternative sequence1 – 5050Missing in isoform Soluble.
VSP_018778
Natural variant341C → S. Ref.2 Ref.18
Corresponds to variant rs6270 [ dbSNP | Ensembl ].
VAR_013925
Natural variant721A → S Correlated with reduced enzyme activity; could be a risk allele for schizophrenia. Ref.7 Ref.18 Ref.20
Corresponds to variant rs6267 [ dbSNP | Ensembl ].
VAR_013926
Natural variant1021A → T.
Corresponds to variant rs5031015 [ dbSNP | Ensembl ].
VAR_020274
Natural variant1461A → V.
Corresponds to variant rs4986871 [ dbSNP | Ensembl ].
VAR_020275
Natural variant1581V → M in allele COMT*2; associated with low enzyme activity and thermolability; may increase the tendency to develop high blood pressure and abdominal obesity. Ref.5 Ref.7 Ref.9 Ref.16 Ref.21 Ref.22
Corresponds to variant rs4680 [ dbSNP | Ensembl ].
VAR_005139

Experimental info

Sequence conflict2451Q → N AA sequence Ref.12

Secondary structure

..................................... 271
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Membrane-bound (MB-COMT) [UniParc].

Last modified May 1, 1992. Version 2.
Checksum: D2547A1C399AC758

FASTA27130,037
        10         20         30         40         50         60 
MPEAPPLLLA AVLLGLVLLV VLLLLLRHWG WGLCLIGWNE FILQPIHNLL MGDTKEQRIL 

        70         80         90        100        110        120 
NHVLQHAEPG NAQSVLEAID TYCEQKEWAM NVGDKKGKIV DAVIQEHQPS VLLELGAYCG 

       130        140        150        160        170        180 
YSAVRMARLL SPGARLITIE INPDCAAITQ RMVDFAGVKD KVTLVVGASQ DIIPQLKKKY 

       190        200        210        220        230        240 
DVDTLDMVFL DHWKDRYLPD TLLLEECGLL RKGTVLLADN VICPGAPDFL AHVRGSSCFE 

       250        260        270 
CTHYQSFLEY REVVDGLEKA IYKGPGSEAG P 

« Hide

Isoform Soluble (S-COMT) [UniParc].

Checksum: F17399A01E493B63
Show »

FASTA22124,449

References

« Hide 'large scale' references
[1]"Cloning and characterization of human placental catechol-O-methyltransferase cDNA."
Lundstroem K., Salminen M., Jalanko A., Savolainen R., Ulmanen I.
DNA Cell Biol. 10:181-189(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"Human catechol-O-methyltransferase: cloning and expression of the membrane-associated form."
Bertocci B., Miggiano V., da Prada M., Dembic Z., Lahm H.-W., Malherbe P.
Proc. Natl. Acad. Sci. U.S.A. 88:1416-1420(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-34.
[3]"Genomic organization of the human catechol O-methyltransferase gene and its expression from two distinct promoters."
Tenhunen J., Salminen M., Lundstroem K., Kiviluoto T., Savolainen R., Ulmanen I.
Eur. J. Biochem. 223:1049-1059(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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].
[5]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-158.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]NIEHS SNPs program
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-72 AND MET-158.
[8]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT MET-158.
[10]"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: Brain and Skin.
[11]"Mass spectrometric analysis of human soluble catechol O-methyltransferase expressed in Escherichia coli. Identification of a product of ribosomal frameshifting and of reactive cysteines involved in S-adenosyl-L-methionine binding."
Vilbois F., Caspers P., da Prada M., Lang G., Karrer C., Lahm H.W., Cesura A.M.
Eur. J. Biochem. 222:377-386(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 52-61, MASS SPECTROMETRY.
[12]"Purification and partial sequence analysis of the soluble catechol-O-methyltransferase from human placenta: comparison to the rat liver enzyme."
Tilgmann C., Kalkkinen N.
Biochem. Biophys. Res. Commun. 174:995-1002(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 59-271.
Tissue: Placenta.
[13]"Cell-free synthesis of rat and human catechol O-methyltransferase. Insertion of the membrane-bound form into microsomal membranes in vitro."
Ulmanen I., Lundstroem K.
Eur. J. Biochem. 202:1013-1020(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE TWO FORMS.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Crystal structures of human 108V and 108M catechol O-methyltransferase."
Rutherford K., Le Trong I., Stenkamp R.E., Parson W.W.
J. Mol. Biol. 380:120-130(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 52-264 OF MUTANTS VAL-108 AND MET-108 IN COMPLEX WITH SUBSTRATE ANALOG 3,5-DINITROCATECHOL; MAGNESIUM AND S-ADENOSYL-L-METHIONINE.
[16]"Human catechol-O-methyltransferase pharmacogenetics: description of a functional polymorphism and its potential application to neuropsychiatric disorders."
Lachman H.M., Papolos D.F., Saito T., Yu Y.-M., Szumlanski C.L., Weinshilboum R.M.
Pharmacogenetics 6:243-250(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT COMT*2 MET-158.
[17]"Association between the functional variant of the catechol-O-methyltransferase (COMT) gene and type 1 alcoholism."
Tiihonen J., Hallikainen T., Lachman H., Saito T., Volavka J., Kauhanen J., Salonen J.T., Ryynaenen O.-P., Koulu M., Karvonen M.K., Pohjalainen T., Syvaelahti E., Hietala J.
Mol. Psychiatry 4:286-289(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ALCOHOLISM.
[18]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-34 AND SER-72.
[19]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[20]"Association of Ala72Ser polymorphism with COMT enzyme activity and the risk of schizophrenia in Koreans."
Lee S.-G., Joo Y., Kim B., Chung S., Kim H.-L., Lee I., Choi B., Kim C., Song K.
Hum. Genet. 116:319-328(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT SER-72, POSSIBLE INVOLVEMENT IN SCHIZOPHRENIA.
[21]"The V108M mutation decreases the structural stability of catechol O-methyltransferase."
Rutherford K., Alphandery E., McMillan A., Daggett V., Parson W.W.
Biochim. Biophys. Acta 1784:1098-1105(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT COMT*2 MET-158.
[22]"Catechol O-methyltransferase val158-met polymorphism is associated with abdominal obesity and blood pressure in men."
Annerbrink K., Westberg L., Nilsson S., Rosmond R., Holm G., Eriksson E.
Metabolism 57:708-711(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT COMT*2 MET-158.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

Catechol-O-methyl transferase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M65212 mRNA. Translation: AAA68927.1.
M65213 mRNA. Translation: AAA68928.1.
M58525 mRNA. Translation: AAA68929.1.
Z26491 Genomic DNA. Translation: CAA81263.1.
AK290440 mRNA. Translation: BAF83129.1.
CR456422 mRNA. Translation: CAG30308.1.
CR456997 mRNA. Translation: CAG33278.1.
AY341246 Genomic DNA. Translation: AAP88929.1.
AC000080 Genomic DNA. No translation available.
AC000090 Genomic DNA. No translation available.
AC005663 Genomic DNA. No translation available.
CH471176 Genomic DNA. Translation: EAX03010.1.
BC011935 mRNA. Translation: AAH11935.1.
BC100018 mRNA. Translation: AAI00019.1.
CCDSCCDS13770.1. [P21964-1]
CCDS46663.1. [P21964-2]
PIRA38459. I37256.
RefSeqNP_000745.1. NM_000754.3. [P21964-1]
NP_001128633.1. NM_001135161.1. [P21964-1]
NP_001128634.1. NM_001135162.1. [P21964-1]
NP_009294.1. NM_007310.2. [P21964-2]
XP_005261286.1. XM_005261229.1. [P21964-1]
UniGeneHs.370408.
Hs.713616.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3A7EX-ray2.80A51-264[»]
3BWMX-ray1.98A52-265[»]
3BWYX-ray1.30A52-265[»]
ProteinModelPortalP21964.
SMRP21964. Positions 52-265.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107707. 10 interactions.
IntActP21964. 6 interactions.
MINTMINT-4529967.
STRING9606.ENSP00000354511.

Chemistry

BindingDBP21964.
ChEMBLCHEMBL2023.
DrugBankDB00190. Carbidopa.
DB00286. Conjugated Estrogens.
DB00255. Diethylstilbestrol.
DB00841. Dobutamine.
DB00988. Dopamine.
DB00494. Entacapone.
DB00158. Folic Acid.
DB00161. L-Valine.
DB01235. Levodopa.
DB00968. Methyldopa.
DB00745. Modafinil.
DB00295. Morphine.
DB00118. S-Adenosylmethionine.
DB00323. Tolcapone.
GuidetoPHARMACOLOGY2472.

PTM databases

PhosphoSiteP21964.

Polymorphism databases

DMDM116907.

2D gel databases

REPRODUCTION-2DPAGEIPI00375513.

Proteomic databases

MaxQBP21964.
PaxDbP21964.
PRIDEP21964.

Protocols and materials databases

DNASU1312.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361682; ENSP00000354511; ENSG00000093010. [P21964-1]
ENST00000403710; ENSP00000385917; ENSG00000093010. [P21964-1]
ENST00000406520; ENSP00000385150; ENSG00000093010. [P21964-1]
ENST00000407537; ENSP00000384654; ENSG00000093010. [P21964-2]
ENST00000449653; ENSP00000416778; ENSG00000093010. [P21964-2]
GeneID1312.
KEGGhsa:1312.
UCSCuc002zqu.3. human. [P21964-1]

Organism-specific databases

CTD1312.
GeneCardsGC22P019929.
HGNCHGNC:2228. COMT.
HPACAB011233.
HPA001169.
MIM103780. phenotype.
116790. gene+phenotype.
neXtProtNX_P21964.
Orphanet567. 22q11.2 deletion syndrome.
240863. Cisplatin toxicity.
3140. Schizophrenia.
240999. Susceptibility to deafness due to cisplatin treatment.
PharmGKBPA117.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4122.
HOGENOMHOG000046392.
HOVERGENHBG005376.
InParanoidP21964.
KOK00545.
OMACTHYSSY.
OrthoDBEOG7PZRZJ.
PhylomeDBP21964.
TreeFamTF329140.

Enzyme and pathway databases

BioCycMetaCyc:HS01791-MONOMER.
BRENDA2.1.1.6. 2681.
ReactomeREACT_111217. Metabolism.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpressP21964.
BgeeP21964.
CleanExHS_COMT.
GenevestigatorP21964.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR025782. Catechol_O-MeTrfase.
IPR017128. Catechol_O-MeTrfase_euk.
IPR002935. O-MeTrfase_3.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERPTHR10509. PTHR10509. 1 hit.
PfamPF01596. Methyltransf_3. 1 hit.
[Graphical view]
PIRSFPIRSF037177. Catechol_O-mtfrase_euk. 1 hit.
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS51682. SAM_OMT_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOMT. human.
EvolutionaryTraceP21964.
GeneWikiCatechol-O-methyl_transferase.
GenomeRNAi1312.
NextBio5365.
PROP21964.
SOURCESearch...

Entry information

Entry nameCOMT_HUMAN
AccessionPrimary (citable) accession number: P21964
Secondary accession number(s): A8MPV9, Q6IB07, Q6ICE6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: May 1, 1992
Last modified: July 9, 2014
This is version 167 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM