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Protein

Catechol O-methyltransferase

Gene

COMT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation1 Publication
Binding sitei114 – 1141S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei122 – 1221S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication
Binding sitei140 – 1401S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication
Binding sitei141 – 1411S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Binding sitei169 – 1691S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Metal bindingi191 – 1911Magnesium1 Publication
Binding sitei191 – 1911S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication
Binding sitei194 – 1941Substrate
Metal bindingi219 – 2191Magnesium1 Publication
Metal bindingi220 – 2201Magnesium1 Publication
Binding sitei220 – 2201Substrate
Binding sitei249 – 2491Substrate

GO - Molecular functioni

  • catechol O-methyltransferase activity Source: UniProtKB-EC
  • magnesium ion binding Source: InterPro
  • O-methyltransferase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Catecholamine metabolism, Neurotransmitter degradation

Keywords - Ligandi

Magnesium, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:HS01791-MONOMER.
BRENDAi2.1.1.6. 2681.
ReactomeiREACT_15511. Enzymatic degradation of Dopamine by monoamine oxidase.
REACT_15548. Enzymatic degradation of dopamine by COMT.
REACT_6946. Methylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Catechol O-methyltransferase (EC:2.1.1.6)
Gene namesi
Name:COMT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:2228. COMT.

Subcellular locationi

Isoform Membrane-bound :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2620Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini27 – 271245ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • axon Source: Ensembl
  • cell body Source: Ensembl
  • cytosol Source: Reactome
  • dendritic spine Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • mitochondrion Source: Ensembl
  • plasma membrane Source: Reactome
  • postsynaptic membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

MIMi103780. phenotype.
116790. gene+phenotype.
Orphaneti567. 22q11.2 deletion syndrome.
240863. Cisplatin toxicity.
3140. Schizophrenia.
PharmGKBiPA117.

Chemistry

DrugBankiDB00286. Conjugated Estrogens.
DB00255. Diethylstilbestrol.
DB00841. Dobutamine.
DB00988. Dopamine.
DB00494. Entacapone.
DB00968. Methyldopa.
DB01141. Micafungin.
DB00118. S-Adenosylmethionine.
DB01420. Testosterone Propionate.
DB00323. Tolcapone.

Polymorphism and mutation databases

BioMutaiCOMT.
DMDMi116907.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Catechol O-methyltransferasePRO_0000020971Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

MaxQBiP21964.
PaxDbiP21964.
PRIDEiP21964.

2D gel databases

REPRODUCTION-2DPAGEIPI00375513.

PTM databases

PhosphoSiteiP21964.

Expressioni

Tissue specificityi

Brain, liver, placenta, lymphocytes and erythrocytes.

Gene expression databases

BgeeiP21964.
CleanExiHS_COMT.
ExpressionAtlasiP21964. baseline and differential.
GenevisibleiP21964. HS.

Organism-specific databases

HPAiCAB011233.
HPA001169.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC27P302603EBI-10200977,EBI-994813
KRT31Q153233EBI-10200977,EBI-948001
KRT40Q6A1623EBI-10200977,EBI-10171697
KRTAP5-9P263713EBI-10200977,EBI-3958099
TRIP13Q156453EBI-10200977,EBI-358993

Protein-protein interaction databases

BioGridi107707. 14 interactions.
IntActiP21964. 11 interactions.
MINTiMINT-4529967.
STRINGi9606.ENSP00000354511.

Structurei

Secondary structure

1
271
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi55 – 6612Combined sources
Helixi72 – 8514Combined sources
Helixi93 – 10715Combined sources
Beta strandi110 – 1156Combined sources
Beta strandi118 – 1203Combined sources
Helixi121 – 1277Combined sources
Beta strandi135 – 1417Combined sources
Helixi143 – 15513Combined sources
Helixi159 – 1613Combined sources
Beta strandi162 – 1676Combined sources
Helixi169 – 1724Combined sources
Helixi173 – 1753Combined sources
Helixi176 – 1805Combined sources
Beta strandi185 – 1906Combined sources
Helixi194 – 1963Combined sources
Helixi197 – 20610Combined sources
Beta strandi210 – 21910Combined sources
Helixi221 – 2255Combined sources
Helixi227 – 2359Combined sources
Beta strandi239 – 2479Combined sources
Beta strandi251 – 26212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A7EX-ray2.80A51-264[»]
3BWMX-ray1.98A52-265[»]
3BWYX-ray1.30A52-265[»]
4PYIX-ray1.35A51-271[»]
4PYJX-ray1.90A51-271[»]
4PYKX-ray2.22A51-271[»]
4XUCX-ray1.80A48-265[»]
4XUDX-ray2.40A48-265[»]
4XUEX-ray2.30A/B52-265[»]
ProteinModelPortaliP21964.
SMRiP21964. Positions 52-265.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21964.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni167 – 1704S-adenosyl-L-methionine binding

Sequence similaritiesi

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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG4122.
GeneTreeiENSGT00390000011316.
HOGENOMiHOG000046392.
HOVERGENiHBG005376.
InParanoidiP21964.
KOiK00545.
OMAiCTHYSSY.
OrthoDBiEOG7PZRZJ.
PhylomeDBiP21964.
TreeFamiTF329140.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR017128. Catechol_O-MeTrfase_euk.
IPR002935. O-MeTrfase_3.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10509. PTHR10509. 1 hit.
PfamiPF01596. Methyltransf_3. 1 hit.
[Graphical view]
PIRSFiPIRSF037177. Catechol_O-mtfrase_euk. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51682. SAM_OMT_I. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform Membrane-bound (identifier: P21964-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPEAPPLLLA AVLLGLVLLV VLLLLLRHWG WGLCLIGWNE FILQPIHNLL
60 70 80 90 100
MGDTKEQRIL NHVLQHAEPG NAQSVLEAID TYCEQKEWAM NVGDKKGKIV
110 120 130 140 150
DAVIQEHQPS VLLELGAYCG YSAVRMARLL SPGARLITIE INPDCAAITQ
160 170 180 190 200
RMVDFAGVKD KVTLVVGASQ DIIPQLKKKY DVDTLDMVFL DHWKDRYLPD
210 220 230 240 250
TLLLEECGLL RKGTVLLADN VICPGAPDFL AHVRGSSCFE CTHYQSFLEY
260 270
REVVDGLEKA IYKGPGSEAG P
Length:271
Mass (Da):30,037
Last modified:May 1, 1992 - v2
Checksum:iD2547A1C399AC758
GO
Isoform Soluble (identifier: P21964-2) [UniParc]FASTAAdd to basket

Also known as: S-COMT

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

Show »
Length:221
Mass (Da):24,449
Checksum:iF17399A01E493B63
GO

Sequence cautioni

The sequence AAH00419.2 differs from that shown. Reason: Erroneous termination at position 85. Translated as Gln.Curated
The sequence AAH05867.1 differs from that shown. Reason: Erroneous termination at position 85. Translated as Gln.Curated
The sequence ACI46037.1 differs from that shown. Reason: Erroneous termination at position 85. Translated as Gln.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti245 – 2451Q → N AA sequence (PubMed:1993083).Curated

Mass spectrometryi

Molecular mass is 24352±2 Da from positions 52 - 271. Determined by ESI. 1 Publication

Polymorphismi

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 [MIMi:103780].

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti34 – 341C → S.2 Publications
Corresponds to variant rs6270 [ dbSNP | Ensembl ].
VAR_013925
Natural varianti72 – 721A → S Correlated with reduced enzyme activity; could be a risk allele for schizophrenia. 3 Publications
Corresponds to variant rs6267 [ dbSNP | Ensembl ].
VAR_013926
Natural varianti102 – 1021A → T.
Corresponds to variant rs5031015 [ dbSNP | Ensembl ].
VAR_020274
Natural varianti146 – 1461A → V.
Corresponds to variant rs4986871 [ dbSNP | Ensembl ].
VAR_020275
Natural varianti158 – 1581V → M in allele COMT*2; associated with low enzyme activity and thermolability; may increase the tendency to develop high blood pressure and abdominal obesity. 6 Publications
Corresponds to variant rs4680 [ dbSNP | Ensembl ].
VAR_005139

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5050Missing in isoform Soluble. CuratedVSP_018778Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65212 mRNA. Translation: AAA68927.1.
M65213 mRNA. Translation: AAA68928.1.
M58525 mRNA. Translation: AAA68929.1.
Z26491 Genomic DNA. Translation: CAA81263.1.
FJ224345 mRNA. Translation: ACI46037.1. Different termination.
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.
BC000419 mRNA. Translation: AAH00419.2. Different termination.
BC005867 mRNA. Translation: AAH05867.1. Different termination.
BC011935 mRNA. Translation: AAH11935.1.
BC100018 mRNA. Translation: AAI00019.1.
CCDSiCCDS13770.1. [P21964-1]
CCDS46663.1. [P21964-2]
PIRiI37256. A38459.
RefSeqiNP_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]
UniGeneiHs.370408.
Hs.713616.

Genome annotation databases

EnsembliENST00000361682; ENSP00000354511; ENSG00000093010. [P21964-1]
ENST00000403710; ENSP00000385917; ENSG00000093010. [P21964-1]
ENST00000406520; ENSP00000385150; ENSG00000093010. [P21964-1]
ENST00000407537; ENSP00000384654; ENSG00000093010. [P21964-1]
ENST00000449653; ENSP00000416778; ENSG00000093010. [P21964-2]
GeneIDi1312.
KEGGihsa:1312.
UCSCiuc002zqu.3. human. [P21964-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Catechol-O-methyl transferase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65212 mRNA. Translation: AAA68927.1.
M65213 mRNA. Translation: AAA68928.1.
M58525 mRNA. Translation: AAA68929.1.
Z26491 Genomic DNA. Translation: CAA81263.1.
FJ224345 mRNA. Translation: ACI46037.1. Different termination.
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.
BC000419 mRNA. Translation: AAH00419.2. Different termination.
BC005867 mRNA. Translation: AAH05867.1. Different termination.
BC011935 mRNA. Translation: AAH11935.1.
BC100018 mRNA. Translation: AAI00019.1.
CCDSiCCDS13770.1. [P21964-1]
CCDS46663.1. [P21964-2]
PIRiI37256. A38459.
RefSeqiNP_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]
UniGeneiHs.370408.
Hs.713616.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A7EX-ray2.80A51-264[»]
3BWMX-ray1.98A52-265[»]
3BWYX-ray1.30A52-265[»]
4PYIX-ray1.35A51-271[»]
4PYJX-ray1.90A51-271[»]
4PYKX-ray2.22A51-271[»]
4XUCX-ray1.80A48-265[»]
4XUDX-ray2.40A48-265[»]
4XUEX-ray2.30A/B52-265[»]
ProteinModelPortaliP21964.
SMRiP21964. Positions 52-265.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107707. 14 interactions.
IntActiP21964. 11 interactions.
MINTiMINT-4529967.
STRINGi9606.ENSP00000354511.

Chemistry

BindingDBiP21964.
ChEMBLiCHEMBL2023.
DrugBankiDB00286. Conjugated Estrogens.
DB00255. Diethylstilbestrol.
DB00841. Dobutamine.
DB00988. Dopamine.
DB00494. Entacapone.
DB00968. Methyldopa.
DB01141. Micafungin.
DB00118. S-Adenosylmethionine.
DB01420. Testosterone Propionate.
DB00323. Tolcapone.
GuidetoPHARMACOLOGYi2472.

PTM databases

PhosphoSiteiP21964.

Polymorphism and mutation databases

BioMutaiCOMT.
DMDMi116907.

2D gel databases

REPRODUCTION-2DPAGEIPI00375513.

Proteomic databases

MaxQBiP21964.
PaxDbiP21964.
PRIDEiP21964.

Protocols and materials databases

DNASUi1312.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361682; ENSP00000354511; ENSG00000093010. [P21964-1]
ENST00000403710; ENSP00000385917; ENSG00000093010. [P21964-1]
ENST00000406520; ENSP00000385150; ENSG00000093010. [P21964-1]
ENST00000407537; ENSP00000384654; ENSG00000093010. [P21964-1]
ENST00000449653; ENSP00000416778; ENSG00000093010. [P21964-2]
GeneIDi1312.
KEGGihsa:1312.
UCSCiuc002zqu.3. human. [P21964-1]

Organism-specific databases

CTDi1312.
GeneCardsiGC22P019929.
HGNCiHGNC:2228. COMT.
HPAiCAB011233.
HPA001169.
MIMi103780. phenotype.
116790. gene+phenotype.
neXtProtiNX_P21964.
Orphaneti567. 22q11.2 deletion syndrome.
240863. Cisplatin toxicity.
3140. Schizophrenia.
PharmGKBiPA117.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4122.
GeneTreeiENSGT00390000011316.
HOGENOMiHOG000046392.
HOVERGENiHBG005376.
InParanoidiP21964.
KOiK00545.
OMAiCTHYSSY.
OrthoDBiEOG7PZRZJ.
PhylomeDBiP21964.
TreeFamiTF329140.

Enzyme and pathway databases

BioCyciMetaCyc:HS01791-MONOMER.
BRENDAi2.1.1.6. 2681.
ReactomeiREACT_15511. Enzymatic degradation of Dopamine by monoamine oxidase.
REACT_15548. Enzymatic degradation of dopamine by COMT.
REACT_6946. Methylation.

Miscellaneous databases

ChiTaRSiCOMT. human.
EvolutionaryTraceiP21964.
GeneWikiiCatechol-O-methyl_transferase.
GenomeRNAii1312.
NextBioi5365.
PROiP21964.
SOURCEiSearch...

Gene expression databases

BgeeiP21964.
CleanExiHS_COMT.
ExpressionAtlasiP21964. baseline and differential.
GenevisibleiP21964. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR017128. Catechol_O-MeTrfase_euk.
IPR002935. O-MeTrfase_3.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10509. PTHR10509. 1 hit.
PfamiPF01596. Methyltransf_3. 1 hit.
[Graphical view]
PIRSFiPIRSF037177. Catechol_O-mtfrase_euk. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51682. SAM_OMT_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Li J.Y., Wang H.Y., Liu J., Liu F.J.
    Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "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.
    , 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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-158.
  7. "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].
  8. NIEHS SNPs program
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-72 AND MET-158.
  9. "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.
    , 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].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT MET-158.
  11. "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, Muscle and Skin.
  12. "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.
  13. "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.
  14. "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.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Orientation and cellular distribution of membrane-bound catechol-O-methyltransferase in cortical neurons: implications for drug development."
    Chen J., Song J., Yuan P., Tian Q., Ji Y., Ren-Patterson R., Liu G., Sei Y., Weinberger D.R.
    J. Biol. Chem. 286:34752-34760(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY.
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "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.
  19. "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.
  20. "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.
  21. Cited for: VARIANTS SER-34 AND SER-72.
  22. "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.
  23. "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.
  24. "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.

Entry informationi

Entry nameiCOMT_HUMAN
AccessioniPrimary (citable) accession number: P21964
Secondary accession number(s): A8MPV9
, Q6IB07, Q6ICE6, Q9BWC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: May 1, 1992
Last modified: June 24, 2015
This is version 177 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.