Genular: Defining Cellular Identity and Function

Details for: Comt

Gene ID: 24267

Symbol: Comt

Ensembl ID: ENSRNOG00000001889

Description: catechol-O-methyltransferase

Associated with

Biological oxidations
(R-RNO-211859)
Dopamine clearance from the synaptic cleft
(R-RNO-379401)
Enzymatic degradation of dopamine by comt
(R-RNO-379397)
Enzymatic degradation of dopamine by monoamine oxidase
(R-RNO-379398)
Metabolism
(R-RNO-1430728)
Neuronal system
(R-RNO-112316)
Neurotransmitter clearance
(R-RNO-112311)
Phase ii - conjugation of compounds
(R-RNO-156580)
Transmission across chemical synapses
(R-RNO-112315)
Artery development
(GO:0060840)
Axon
(GO:0030424)
Behavioral fear response
(GO:0001662)
Catechol-containing compound metabolic process
(GO:0009712)
Catecholamine catabolic process
(GO:0042424)
Catecholamine metabolic process
(GO:0006584)
Catechol o-methyltransferase activity
(GO:0016206)
Cell body
(GO:0044297)
Cellular response to cocaine
(GO:0071314)
Cellular response to phosphate starvation
(GO:0016036)
Cerebellar cortex morphogenesis
(GO:0021696)
Cholesterol efflux
(GO:0033344)
Cognition
(GO:0050890)
Cytosol
(GO:0005829)
Dendrite
(GO:0030425)
Dendritic spine
(GO:0043197)
Detection of temperature stimulus involved in sensory perception of pain
(GO:0050965)
Developmental process
(GO:0032502)
Dopamine catabolic process
(GO:0042420)
Dopamine metabolic process
(GO:0042417)
Dopamine secretion
(GO:0014046)
Estrogen metabolic process
(GO:0008210)
Exploration behavior
(GO:0035640)
Extracellular space
(GO:0005615)
Fear response
(GO:0042596)
Female pregnancy
(GO:0007565)
Gene expression
(GO:0010467)
Glomerulus development
(GO:0032835)
Glycogen metabolic process
(GO:0005977)
Habituation
(GO:0046959)
Intracellular membrane-bounded organelle
(GO:0043231)
Kidney development
(GO:0001822)
L-dopa o-methyltransferase activity
(GO:0102084)
Learning
(GO:0007612)
Learning or memory
(GO:0007611)
Magnesium ion binding
(GO:0000287)
Mastication
(GO:0071626)
Membrane
(GO:0016020)
Memory
(GO:0007613)
Methylation
(GO:0032259)
Multicellular organismal reproductive process
(GO:0048609)
Multicellular organismal response to stress
(GO:0033555)
Multicellular organism growth
(GO:0035264)
Negative regulation of dopamine metabolic process
(GO:0045963)
Negative regulation of smooth muscle cell proliferation
(GO:0048662)
Norepinephrine metabolic process
(GO:0042415)
Norepinephrine secretion
(GO:0048243)
Orcinol o-methyltransferase activity
(GO:0102938)
Plasma membrane
(GO:0005886)
Positive regulation of homocysteine metabolic process
(GO:0050668)
Positive regulation of lactation
(GO:1903489)
Postsynaptic membrane
(GO:0045211)
Prostaglandin metabolic process
(GO:0006693)
Regulation of blood pressure
(GO:0008217)
Renal albumin absorption
(GO:0097018)
Renal filtration
(GO:0097205)
Renal sodium excretion
(GO:0035812)
Renin secretion into blood stream
(GO:0002001)
Response to amphetamine
(GO:0001975)
Response to angiotensin
(GO:1990776)
Response to corticosterone
(GO:0051412)
Response to cytokine
(GO:0034097)
Response to dopamine
(GO:1903350)
Response to estrogen
(GO:0043627)
Response to food
(GO:0032094)
Response to hypoxia
(GO:0001666)
Response to inorganic substance
(GO:0010035)
Response to lipopolysaccharide
(GO:0032496)
Response to organic cyclic compound
(GO:0014070)
Response to organic substance
(GO:0010033)
Response to oxidative stress
(GO:0006979)
Response to pain
(GO:0048265)
Response to salt
(GO:1902074)
Response to temperature stimulus
(GO:0009266)
Response to toxic substance
(GO:0009636)
Response to wounding
(GO:0009611)
Response to xenobiotic stimulus
(GO:0009410)
S-adenosylhomocysteine metabolic process
(GO:0046498)
S-adenosylmethionine metabolic process
(GO:0046500)
Short-term memory
(GO:0007614)
Startle response
(GO:0001964)
Synaptic transmission, dopaminergic
(GO:0001963)
Vesicle
(GO:0031982)
Visual learning
(GO:0008542)

Other Information

Proteins

COMT_RAT
A0A8I6A1I0_RAT

Genular Protein ID: 2300524421

Symbol: COMT_RAT

Name: N/A

UniProtKB Accession Codes:

P22734

Database IDs:

Citations:

PubMed ID: 8280056

Title: Production of rat soluble and membrane-bound catechol O-methyltransferase forms from bifunctional mRNAs.

PubMed ID: 8280056

DOI: 10.1042/bj2960595

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 2227437

Title: Molecular cloning and characterization of rat liver catechol-O-methyltransferase.

PubMed ID: 2227437

DOI: 10.1016/0378-1119(90)90231-f

PubMed ID: 1765063

Title: Cell-free synthesis of rat and human catechol O-methyltransferase. Insertion of the membrane-bound form into microsomal membranes in vitro.

PubMed ID: 1765063

DOI: 10.1111/j.1432-1033.1991.tb16464.x

PubMed ID: 22673903

Title: Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues.

PubMed ID: 22673903

DOI: 10.1038/ncomms1871

PubMed ID: 8127373

Title: Crystal structure of catechol O-methyltransferase.

PubMed ID: 8127373

DOI: 10.1038/368354a0

PubMed ID: 10785817

Title: Structure-based design, synthesis, and in vitro evaluation of bisubstrate inhibitors for catechol O-methyltransferase (COMT).

PubMed ID: 10785817

DOI: 10.1002/(sici)1521-3765(20000317)6:6<971::aid-chem971>3.0.co;2-0

PubMed ID: 12237326

Title: Kinetics and crystal structure of catechol-O-methyltransferase complex with co-substrate and a novel inhibitor with potential therapeutic application.

PubMed ID: 12237326

DOI: 10.1124/mol.62.4.795

PubMed ID: 16618795

Title: Comparative study of ortho- and meta-nitrated inhibitors of catechol-O-methyltransferase: interactions with the active site and regioselectivity of O-methylation.

PubMed ID: 16618795

DOI: 10.1124/mol.106.023119

Sequence Information:

Length: 264
Mass: 29597
Checksum: F535DFF49C062854
Sequence:

MPLAAVSLGL LLLALLLLLR HLGWGLVTIF WFEYVLQPVH NLIMGDTKEQ RILRYVQQNA 
KPGDPQSVLE AIDTYCTQKE WAMNVGDAKG QIMDAVIREY SPSLVLELGA YCGYSAVRMA 
RLLQPGARLL TMEMNPDYAA ITQQMLNFAG LQDKVTILNG ASQDLIPQLK KKYDVDTLDM 
VFLDHWKDRY LPDTLLLEKC GLLRKGTVLL ADNVIVPGTP DFLAYVRGSS SFECTHYSSY 
LEYMKVVDGL EKAIYQGPSS PDKS

Genular Protein ID: 3786261145

Symbol: A0A8I6A1I0_RAT

Name: N/A

UniProtKB Accession Codes:

A0A8I6A1I0

Database IDs:

Citations:

PubMed ID: 15057822

Title: Genome sequence of the Brown Norway rat yields insights into mammalian evolution.

PubMed ID: 15057822

DOI: 10.1038/nature02426

Sequence Information:

Length: 265
Mass: 29729
Checksum: E3D842F4BD8E1854
Sequence:

MMPLAAVSLG LLLLALLLLL RHLGWGLVTI FWFEYVLQPV HNLIMGDTKE QRILRYVQQN 
AKPGDPQSVL EAIDTYCTQK EWAMNVGDAK GQIMDAVIRE YSPSLVLELG AYCGYSAVRM 
ARLLQPGARL LTMEMNPDYA AITQQMLNFA GLQDKVTILN GASQDLIPQL KKKYDVDTLD 
MVFLDHWKDR YLPDTLLLEK CGLLRKGTVL LADNVIVPGT PDFLAYVRGS SSFECTHYSS 
YLEYMKVVDG LEKAIYQGPS SPDKS

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: Comt

Associated with

Other Information

Production of rat soluble and membrane-bound catechol O-methyltransferase forms from bifunctional mRNAs. PubMed ID: 8280056

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Molecular cloning and characterization of rat liver catechol-O-methyltransferase. PubMed ID: 2227437

Cell-free synthesis of rat and human catechol O-methyltransferase. Insertion of the membrane-bound form into microsomal membranes in vitro. PubMed ID: 1765063

Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. PubMed ID: 22673903

Crystal structure of catechol O-methyltransferase. PubMed ID: 8127373

Structure-based design, synthesis, and in vitro evaluation of bisubstrate inhibitors for catechol O-methyltransferase (COMT). PubMed ID: 10785817

Kinetics and crystal structure of catechol-O-methyltransferase complex with co-substrate and a novel inhibitor with potential therapeutic application. PubMed ID: 12237326

Comparative study of ortho- and meta-nitrated inhibitors of catechol-O-methyltransferase: interactions with the active site and regioselectivity of O-methylation. PubMed ID: 16618795

Genome sequence of the Brown Norway rat yields insights into mammalian evolution. PubMed ID: 15057822