P21964 (COMT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catechol O-methyltransferase
EC=2.1.1.6

Gene names

Name:

COMT

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	271 AA.
Sequence status	Complete.
Protein existence	Evidence 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 mammalian catechol-O-methyltransferase family.
Mass spectrometry	Molecular mass is 24352±2 Da from positions 52 - 271. Determined by ESI. Ref.11

Ontologies

Keywords
Biological process	Catecholamine metabolism Neurotransmitter degradation
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative initiation Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Magnesium Metal-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	neurotransmitter biosynthetic process Traceable author statement. Source: Reactome neurotransmitter catabolic process Inferred from electronic annotation. Source: UniProtKB-KW xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Traceable author statement. Source: ProtInc plasma membrane Traceable author statement. Source: Reactome soluble fraction Traceable author statement. Source: ProtInc
Molecular function	catechol O-methyltransferase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
XRN2	Q9H0D6	1	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 271

271

Catechol O-methyltransferase

PRO_0000020971

Regions

Transmembrane

7 – 26

20

Helical; Signal-anchor for type II membrane protein; Potential

Region

167 – 170

4

S-adenosyl-L-methionine binding

Sites

Metal binding

191

1

Magnesium

Metal binding

219

1

Magnesium

Metal binding

220

1

Magnesium

Binding site

92

1

S-adenosyl-L-methionine; via amide nitrogen

Binding site

122

1

S-adenosyl-L-methionine

Binding site

140

1

S-adenosyl-L-methionine

Binding site

191

1

S-adenosyl-L-methionine

Binding site

194

1

Substrate

Binding site

220

1

Substrate

Binding site

249

1

Substrate

Amino acid modifications

Modified residue

267

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 50

50

Missing in isoform Soluble.

VSP_018778

Natural variant

34

1

C → S. Ref.2 Ref.18
Corresponds to variant rs6270 [ dbSNP | Ensembl ].

VAR_013925

Natural variant

72

1

A → 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 variant

102

1

A → T.
Corresponds to variant rs5031015 [ dbSNP | Ensembl ].

VAR_020274

Natural variant

146

1

A → V.
Corresponds to variant rs4986871 [ dbSNP | Ensembl ].

VAR_020275

Natural variant

158

1

V → 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 conflict

245

1

Q → N AA sequence Ref.12

Secondary structure

1

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271

Helix Strand Turn

Details...

Helix

55 – 66

12

Helix

72 – 85

14

Helix

93 – 107

15

Beta strand

110 – 115

6

Helix

121 – 127

7

Beta strand

135 – 141

7

Helix

143 – 155

13

Helix

159 – 161

3

Beta strand

162 – 167

6

Helix

169 – 172

4

Helix

173 – 175

3

Helix

176 – 180

5

Beta strand

185 – 190

6

Helix

194 – 196

3

Helix

197 – 206

10

Beta strand

210 – 219

10

Helix

221 – 225

5

Helix

227 – 235

9

Beta strand

239 – 247

9

Beta strand

251 – 262

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform Membrane-bound (MB-COMT) [UniParc]. Last modified May 1, 1992. Version 2. Checksum: D2547A1C399AC758	FASTA	271	30,037
	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
	Isoform Soluble (S-COMT) [UniParc]. Checksum: F17399A01E493B63	FASTA	221	24,449
	10 20 30 40 50 60 MGDTKEQRIL NHVLQHAEPG NAQSVLEAID TYCEQKEWAM NVGDKKGKIV DAVIQEHQPS 70 80 90 100 110 120 VLLELGAYCG YSAVRMARLL SPGARLITIE INPDCAAITQ RMVDFAGVKD KVTLVVGASQ 130 140 150 160 170 180 DIIPQLKKKY DVDTLDMVFL DHWKDRYLPD TLLLEECGLL RKGTVLLADN VICPGAPDFL 190 200 210 220 AHVRGSSCFE CTHYQSFLEY REVVDGLEKA IYKGPGSEAG P

References

	« Hide 'large scale' referencesShow '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: 1707278] [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: 1847521] [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: 8055944] [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. , 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: 14702039] [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: 15461802] [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. , 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: 10591208] [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. , 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: 15489334] [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: 8020475] [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: 1993083] [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: 1765063] [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: 21269460] [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: 18486144] [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: 8807664] [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: 10395222] [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: 10391209] [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: 15645182] [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: 18474266] [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: 18442637] [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.

IPI

IPI00011284.
IPI00375513.

PIR

A38459. I37256.

RefSeq

NP_000745.1. NM_000754.3.
NP_001128633.1. NM_001135161.1.
NP_001128634.1. NM_001135162.1.
NP_009294.1. NM_007310.2.

UniGene

Hs.370408.
Hs.704514.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P21964.

SMR

P21964. Positions 52-265.

ModBase

Search...

Protein-protein interaction databases

IntAct

P21964. 2 interactions.

MINT

MINT-4529967.

STRING

P21964.

PTM databases

PhosphoSite

P21964.

Polymorphism databases

DMDM

116907.

2D gel databases

Cornea-2DPAGE

P21964.

REPRODUCTION-2DPAGE

IPI00375513.

Proteomic databases

PRIDE

P21964.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361682; ENSP00000354511; ENSG00000093010.
ENST00000402871; ENSP00000385831; ENSG00000093010.
ENST00000403710; ENSP00000385917; ENSG00000093010.
ENST00000406520; ENSP00000385150; ENSG00000093010.
ENST00000407537; ENSP00000384654; ENSG00000093010.
ENST00000436217; ENSP00000410938; ENSG00000093010.

GeneID

1312.

KEGG

hsa:1312.

UCSC

uc002zqt.1. human.

Organism-specific databases

CTD

1312.

GeneCards

GC22P019929.

H-InvDB

HIX0016246.

HGNC

HGNC:2228. COMT.

HPA

CAB011233.
HPA001169.

MIM

103780. phenotype.
116790. gene+phenotype.

neXtProt

NX_P21964.

Orphanet

240863. Cisplatin toxicity.
240999. Susceptibility to deafness due to cisplatin treatment.

PharmGKB

PA117.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG565172.

HOVERGEN

HBG005376.

InParanoid

P21964.

OMA

SRFECTH.

OrthoDB

EOG4G1MH8.

PhylomeDB

P21964.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000093010-MONOMER.

BRENDA

2.1.1.6. 2681.

Reactome

REACT_111217. Metabolism.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpress

P21964.

Bgee

P21964.

CleanEx

HS_COMT.

Genevestigator

P21964.

GermOnline

ENSG00000093010. Homo sapiens.

Family and domain databases

InterPro

IPR017128. Catechol_O-MeTrfase_euk.
IPR002935. O-MeTrfase_3.
[Graphical view]

KO

K00545.

PANTHER

PTHR10509. Methyltransf_3. 1 hit.

Pfam

PF01596. Methyltransf_3. 1 hit.
[Graphical view]

PIRSF

PIRSF037177. Catechol_O-mtfrase_euk. 1 hit.

ProtoNet

Search...

Other

DrugBank

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.

NextBio

5365.

SOURCE

Search...

Entry information

Entry name

COMT_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 141 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.