Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P21964

- COMT_HUMAN

UniProt

P21964 - COMT_HUMAN

Protein

Catechol O-methyltransferase

Gene

COMT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (01 May 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Binds 1 magnesium ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei92 – 921S-adenosyl-L-methionine; via amide nitrogen1 PublicationPROSITE-ProRule annotation
    Binding sitei114 – 1141S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei122 – 1221S-adenosyl-L-methionine1 PublicationPROSITE-ProRule annotation
    Binding sitei140 – 1401S-adenosyl-L-methionine1 PublicationPROSITE-ProRule annotation
    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-methionine1 PublicationPROSITE-ProRule annotation
    Binding sitei194 – 1941Substrate
    Metal bindingi219 – 2191Magnesium1 Publication
    Metal bindingi220 – 2201Magnesium1 Publication
    Binding sitei220 – 2201Substrate
    Binding sitei249 – 2491Substrate

    GO - Molecular functioni

    1. catechol O-methyltransferase activity Source: UniProtKB-EC
    2. magnesium ion binding Source: InterPro
    3. O-methyltransferase activity Source: ProtInc

    GO - Biological processi

    1. dopamine catabolic process Source: Ensembl
    2. estrogen metabolic process Source: Ensembl
    3. female pregnancy Source: Ensembl
    4. learning Source: Ensembl
    5. methylation Source: Reactome
    6. multicellular organismal reproductive process Source: Ensembl
    7. negative regulation of dopamine metabolic process Source: Ensembl
    8. negative regulation of smooth muscle cell proliferation Source: Ensembl
    9. neurotransmitter biosynthetic process Source: Reactome
    10. neurotransmitter catabolic process Source: UniProtKB-KW
    11. positive regulation of homocysteine metabolic process Source: Ensembl
    12. response to drug Source: Ensembl
    13. response to lipopolysaccharide Source: Ensembl
    14. response to organic cyclic compound Source: Ensembl
    15. response to pain Source: Ensembl
    16. small molecule metabolic process Source: Reactome
    17. synaptic transmission Source: Reactome
    18. xenobiotic metabolic process Source: Reactome

    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: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:2228. COMT.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane Source: UniProtKB
    5. mitochondrion Source: Ensembl
    6. plasma membrane Source: Reactome

    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.
    240999. Susceptibility to deafness due to cisplatin treatment.
    PharmGKBiPA117.

    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

    ArrayExpressiP21964.
    BgeeiP21964.
    CleanExiHS_COMT.
    GenevestigatoriP21964.

    Organism-specific databases

    HPAiCAB011233.
    HPA001169.

    Interactioni

    Protein-protein interaction databases

    BioGridi107707. 10 interactions.
    IntActiP21964. 6 interactions.
    MINTiMINT-4529967.
    STRINGi9606.ENSP00000354511.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    ProteinModelPortaliP21964.
    SMRiP21964. Positions 52-265.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21964.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2620Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

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

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025782. Catechol_O-MeTrfase.
    IPR017128. Catechol_O-MeTrfase_euk.
    IPR002935. O-MeTrfase_3.
    IPR029063. SAM-dependent_MTases-like.
    [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. Align

    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

    MPEAPPLLLA AVLLGLVLLV VLLLLLRHWG WGLCLIGWNE FILQPIHNLL    50
    MGDTKEQRIL NHVLQHAEPG NAQSVLEAID TYCEQKEWAM NVGDKKGKIV 100
    DAVIQEHQPS VLLELGAYCG YSAVRMARLL SPGARLITIE INPDCAAITQ 150
    RMVDFAGVKD KVTLVVGASQ DIIPQLKKKY DVDTLDMVFL DHWKDRYLPD 200
    TLLLEECGLL RKGTVLLADN VICPGAPDFL AHVRGSSCFE CTHYQSFLEY 250
    REVVDGLEKA IYKGPGSEAG P 271
    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.
    The sequence AAH05867.1 differs from that shown. Reason: Erroneous termination at position 85. Translated as Gln.
    The sequence ACI46037.1 differs from that shown. Reason: Erroneous termination at position 85. Translated as Gln.

    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. 2 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. 5 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:
    EMBL
    GenBank
    DDBJ
    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]
    XP_005261286.1. XM_005261229.1. [P21964-1]
    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. [P21964-2]
    ENST00000449653; ENSP00000416778; ENSG00000093010. [P21964-2]
    GeneIDi1312.
    KEGGihsa:1312.
    UCSCiuc002zqu.3. human. [P21964-1]

    Polymorphism databases

    DMDMi116907.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS13770.1. [P21964-1 ]
    CCDS46663.1. [P21964-2 ]
    PIRi I37256. A38459.
    RefSeqi NP_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 ]
    UniGenei Hs.370408.
    Hs.713616.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3A7E X-ray 2.80 A 51-264 [» ]
    3BWM X-ray 1.98 A 52-265 [» ]
    3BWY X-ray 1.30 A 52-265 [» ]
    4PYI X-ray 1.35 A 51-271 [» ]
    4PYJ X-ray 1.90 A 51-271 [» ]
    4PYK X-ray 2.22 A 51-271 [» ]
    ProteinModelPortali P21964.
    SMRi P21964. Positions 52-265.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107707. 10 interactions.
    IntActi P21964. 6 interactions.
    MINTi MINT-4529967.
    STRINGi 9606.ENSP00000354511.

    Chemistry

    BindingDBi P21964.
    ChEMBLi CHEMBL2023.
    DrugBanki DB00190. 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.
    GuidetoPHARMACOLOGYi 2472.

    PTM databases

    PhosphoSitei P21964.

    Polymorphism databases

    DMDMi 116907.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00375513.

    Proteomic databases

    MaxQBi P21964.
    PaxDbi P21964.
    PRIDEi P21964.

    Protocols and materials databases

    DNASUi 1312.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361682 ; ENSP00000354511 ; ENSG00000093010 . [P21964-1 ]
    ENST00000403710 ; ENSP00000385917 ; ENSG00000093010 . [P21964-1 ]
    ENST00000406520 ; ENSP00000385150 ; ENSG00000093010 . [P21964-1 ]
    ENST00000407537 ; ENSP00000384654 ; ENSG00000093010 . [P21964-2 ]
    ENST00000449653 ; ENSP00000416778 ; ENSG00000093010 . [P21964-2 ]
    GeneIDi 1312.
    KEGGi hsa:1312.
    UCSCi uc002zqu.3. human. [P21964-1 ]

    Organism-specific databases

    CTDi 1312.
    GeneCardsi GC22P019929.
    HGNCi HGNC:2228. COMT.
    HPAi CAB011233.
    HPA001169.
    MIMi 103780. phenotype.
    116790. gene+phenotype.
    neXtProti NX_P21964.
    Orphaneti 567. 22q11.2 deletion syndrome.
    240863. Cisplatin toxicity.
    3140. Schizophrenia.
    240999. Susceptibility to deafness due to cisplatin treatment.
    PharmGKBi PA117.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4122.
    HOGENOMi HOG000046392.
    HOVERGENi HBG005376.
    InParanoidi P21964.
    KOi K00545.
    OMAi CTHYSSY.
    OrthoDBi EOG7PZRZJ.
    PhylomeDBi P21964.
    TreeFami TF329140.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS01791-MONOMER.
    BRENDAi 2.1.1.6. 2681.
    Reactomei REACT_15511. Enzymatic degradation of Dopamine by monoamine oxidase.
    REACT_15548. Enzymatic degradation of dopamine by COMT.
    REACT_6946. Methylation.

    Miscellaneous databases

    ChiTaRSi COMT. human.
    EvolutionaryTracei P21964.
    GeneWikii Catechol-O-methyl_transferase.
    GenomeRNAii 1312.
    NextBioi 5365.
    PROi P21964.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21964.
    Bgeei P21964.
    CleanExi HS_COMT.
    Genevestigatori P21964.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR025782. Catechol_O-MeTrfase.
    IPR017128. Catechol_O-MeTrfase_euk.
    IPR002935. O-MeTrfase_3.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR10509. PTHR10509. 1 hit.
    Pfami PF01596. Methyltransf_3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037177. Catechol_O-mtfrase_euk. 1 hit.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51682. SAM_OMT_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    17. "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.
    18. "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.
    19. Cited for: VARIANTS SER-34 AND SER-72.
    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.

    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: October 1, 2014
    This is version 169 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