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P46597 (ASMT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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:
Acetylserotonin O-methyltransferase

EC=2.1.1.4
Alternative name(s):
Hydroxyindole O-methyltransferase
Short name=HIOMT
Gene names
Name:ASMT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform 1 catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine). Isoform 2 and isoform 3 lack enzyme activity. Ref.9

Catalytic activity

S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin. Ref.9

Pathway

Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2.

Subunit structure

Homodimer. Ref.9

Tissue specificity

Expressed in the pineal gland (at protein level). In the retina, very low expression is found at the mRNA level (Ref.1), and not at the protein level (Ref.6). Ref.1 Ref.6 Ref.9

Induction

By all-trans-, 9-cis- and 13-cis-retinoic acid and by serum treatment, following starvation, in the retinoblastoma cell line Y79. Ref.7 Ref.8

Miscellaneous

The gene coding for this protein is located in the pseudoautosomal region 1 (PAR1) of X and Y chromosomes.

Sequence similarities

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-6502097,EBI-6502097

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P46597-1)

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 2 (identifier: P46597-2)

The sequence of this isoform differs from the canonical sequence as follows:
     189-235: Missing.
Isoform 3 (identifier: P46597-3)

The sequence of this isoform differs from the canonical sequence as follows:
     188-188: G → GTWIKLETIILSKLSQGQKTKHRVFSLIG
Note: Includes part of a LINE-1 element.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345Acetylserotonin O-methyltransferase
PRO_0000083982

Regions

Region235 – 2373S-adenosyl-L-methionine binding

Sites

Active site2551Proton donor/acceptor Probable
Binding site1471S-adenosyl-L-methionine
Binding site1641S-adenosyl-L-methionine
Binding site2101S-adenosyl-L-methionine
Binding site2521S-adenosyl-L-methionine
Binding site2561Substrate
Binding site3021Substrate
Binding site3061Substrate

Natural variations

Alternative sequence1881G → GTWIKLETIILSKLSQGQKT KHRVFSLIG in isoform 3.
VSP_004284
Alternative sequence189 – 23547Missing in isoform 2.
VSP_004285
Natural variant131N → H Polymorphism with no effect on enzyme activity. Ref.9 Ref.12
Corresponds to variant rs121918819 [ dbSNP | Ensembl ].
VAR_069111
Natural variant171N → K Functional polymorphism that nearly abolishes enzyme activity. Ref.9 Ref.11 Ref.12 Ref.15
Corresponds to variant rs17149149 [ dbSNP | Ensembl ].
VAR_045991
Natural variant611E → Q Functional polymorphism with reduced enzyme activity. Ref.9 Ref.12 Ref.14
Corresponds to variant rs121918823 [ dbSNP | Ensembl ].
VAR_069112
Natural variant811K → E Polymorphism with no effect on enzyme activity. Ref.9 Ref.11
Corresponds to variant rs117343570 [ dbSNP | Ensembl ].
VAR_069113
Natural variant1111R → K Polymorphism with no effect on enzyme activity. Ref.9 Ref.14
VAR_069114
Natural variant1151R → W. Ref.15
Corresponds to variant rs201053197 [ dbSNP | Ensembl ].
VAR_069115
Natural variant1511G → S. Ref.15
Corresponds to variant rs192710293 [ dbSNP | Ensembl ].
VAR_069116
Natural variant1661V → I. Ref.15
VAR_069117
Natural variant1711V → M Functional polymorphism that nearly abolishes enzyme activity. Ref.9 Ref.12
Corresponds to variant rs121918820 [ dbSNP | Ensembl ].
VAR_069118
Natural variant1791V → G. Ref.15
VAR_069119
Natural variant2101D → G Functional polymorphism that nearly abolishes enzyme activity. Ref.9 Ref.12 Ref.13
Corresponds to variant rs121918824 [ dbSNP | Ensembl ].
VAR_069120
Natural variant2111I → M. Ref.15
Corresponds to variant rs201316181 [ dbSNP | Ensembl ].
VAR_069121
Natural variant2171T → M. Ref.15
Corresponds to variant rs148036160 [ dbSNP | Ensembl ].
VAR_069122
Natural variant2191K → R Polymorphism with no effect on enzyme activity. Ref.9 Ref.12 Ref.14
Corresponds to variant rs121918825 [ dbSNP | Ensembl ].
VAR_069123
Natural variant2431P → L Functional polymorphism with reduced enzyme activity. Ref.9 Ref.12 Ref.14 Ref.15
Corresponds to variant rs121918826 [ dbSNP | Ensembl ].
VAR_069124
Natural variant2481Y → H Functional polymorphism that nearly abolishes enzyme activity. Ref.9 Ref.14
VAR_069125
Natural variant2691I → M Functional polymorphism with reduced enzyme activity. Ref.9
Corresponds to variant rs146121655 [ dbSNP | Ensembl ].
VAR_069126
Natural variant2731C → S Functional polymorphism with reduced enzyme activity. Ref.9 Ref.12 Ref.14
Corresponds to variant rs121918827 [ dbSNP | Ensembl ].
VAR_069127
Natural variant2781G → A Functional polymorphism with reduced enzyme activity. Ref.9 Ref.11
VAR_069128
Natural variant2881E → D Polymorphism with no effect on enzyme activity. Ref.9 Ref.10 Ref.12 Ref.14
Corresponds to variant rs121918821 [ dbSNP | Ensembl ].
VAR_069129
Natural variant2911R → Q Functional polymorphism that nearly abolishes enzyme activity. Ref.9 Ref.12 Ref.14
VAR_069130
Natural variant2981L → F Functional polymorphism that nearly abolishes enzyme activity. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Corresponds to variant rs121918822 [ dbSNP | Ensembl ].
VAR_069131
Natural variant3051V → M Functional polymorphism with reduced enzyme activity. Ref.9 Ref.14
VAR_069132

Experimental info

Mutagenesis111L → F: Reduced enzyme activity. Ref.9
Mutagenesis311L → H: No effect on enzyme activity.
Mutagenesis2961T → M: Nearly abolishes enzyme activity. Ref.9
Mutagenesis3181H → D: Reduced enzyme activity. Ref.9
Sequence conflict3021N → S in BAG37430. Ref.3
Isoform 3:
Sequence conflict1901W → R in AAA58582. Ref.1
Sequence conflict1901W → R in AAA58583. Ref.1
Sequence conflict1901W → R in AAA75290. Ref.1
Sequence conflict1901W → R in AAA17020. Ref.2
Sequence conflict1901W → R in BAG37430. Ref.3

Secondary structure

.............................................................. 345
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 187A375E1E2940B7

FASTA34538,453
        10         20         30         40         50         60 
MGSSEDQAYR LLNDYANGFM VSQVLFAACE LGVFDLLAEA PGPLDVAAVA AGVRASAHGT 

        70         80         90        100        110        120 
ELLLDICVSL KLLKVETRGG KAFYRNTELS SDYLTTVSPT SQCSMLKYMG RTSYRCWGHL 

       130        140        150        160        170        180 
ADAVREGRNQ YLETFGVPAE ELFTAIYRSE GERLQFMQAL QEVWSVNGRS VLTAFDLSVF 

       190        200        210        220        230        240 
PLMCDLGGGA GALAKECMSL YPGCKITVFD IPEVVWTAKQ HFSFQEEEQI DFQEGDFFKD 

       250        260        270        280        290        300 
PLPEADLYIL ARVLHDWADG KCSHLLERIY HTCKPGGGIL VIESLLDEDR RGPLLTQLYS 

       310        320        330        340 
LNMLVQTEGQ ERTPTHYHML LSSAGFRDFQ FKKTGAIYDA ILARK 

« Hide

Isoform 2 [UniParc].

Checksum: AAFC60D1F8D70E5A
Show »

FASTA29833,192
Isoform 3 [UniParc].

Checksum: 8CA134BD0BA50FDD
Show »

FASTA37341,661

References

« Hide 'large scale' references
[1]"Structural analysis of the human hydroxyindole-O-methyltransferase gene. Presence of two distinct promoters."
Rodriguez I.R., Mazuruk K., Schoen T.J., Chader G.J.
J. Biol. Chem. 269:31969-31977(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY.
[2]"Human hydroxyindole-O-methyltransferase: presence of LINE-1 fragment in a cDNA clone and pineal mRNA."
Donohue S.J., Roseboom P.H., Illnerova H., Weller J.L., Klein D.C.
DNA Cell Biol. 12:715-727(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Pineal gland.
[3]"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] (ISOFORM 3).
Tissue: Subthalamic nucleus.
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 2).
Tissue: Eye.
[6]"Human hydroxyindole-O-methyltransferase in pineal gland, retina and Y79 retinoblastoma cells."
Bernard M., Donohue S.J., Klein D.C.
Brain Res. 696:37-48(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Hydroxyindole-O-methyltransferase in Y-79 cells: regulation by serum."
Bernard M., Voisin P., Klein D.C.
Brain Res. 727:118-124(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY SERUM TREATMENT.
[8]"Retinoic acid increases hydroxyindole-O-methyltransferase activity and mRNA in human Y-79 retinoblastoma cells."
Bernard M., Klein D.C.
J. Neurochem. 67:1032-1038(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY RETINOIC ACID.
[9]"Crystal structure and functional mapping of human ASMT, the last enzyme of the melatonin synthesis pathway."
Botros H.G., Legrand P., Pagan C., Bondet V., Weber P., Ben-Abdallah M., Lemiere N., Huguet G., Bellalou J., Maronde E., Beguin P., Haouz A., Shepard W., Bourgeron T.
J. Pineal Res. 54:46-57(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEXES WITH S-ADENOSYL-L-METHIONINE; N-ACETYL SEROTONIN AND ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, CHARACTERIZATION OF ISOFORMS 1; 2 AND 3, SUBUNIT, TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANTS HIS-13; LYS-17; GLN-61; GLU-81; LYS-111; MET-171; GLY-210; ARG-219; LEU-243; HIS-248; MET-269; SER-273; ALA-278; ASP-288; GLN-291; PHE-298 AND MET-305, MUTAGENESIS OF LEU-11; THR-296 AND HIS-318.
[10]"Is ASMT a susceptibility gene for autism spectrum disorders? A replication study in European populations."
Toma C., Rossi M., Sousa I., Blasi F., Bacchelli E., Alen R., Vanhala R., Monaco A.P., Jarvela I., Maestrini E.
Mol. Psychiatry 12:977-979(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASP-288 AND PHE-298.
[11]"Abnormal melatonin synthesis in autism spectrum disorders."
Melke J., Goubran Botros H., Chaste P., Betancur C., Nygren G., Anckarsater H., Rastam M., Stahlberg O., Gillberg I.C., Delorme R., Chabane N., Mouren-Simeoni M.C., Fauchereau F., Durand C.M., Chevalier F., Drouot X., Collet C., Launay J.M. expand/collapse author list , Leboyer M., Gillberg C., Bourgeron T.
Mol. Psychiatry 13:90-98(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LYS-17; GLU-81; ALA-278 AND PHE-298.
[12]"Mutation screening of ASMT, the last enzyme of the melatonin pathway, in a large sample of patients with intellectual disability."
Pagan C., Botros H.G., Poirier K., Dumaine A., Jamain S., Moreno S., de Brouwer A., Van Esch H., Delorme R., Launay J.M., Tzschach A., Kalscheuer V., Lacombe D., Briault S., Laumonnier F., Raynaud M., van Bon B.W., Willemsen M.H. expand/collapse author list , Leboyer M., Chelly J., Bourgeron T.
BMC Med. Genet. 12:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HIS-13; LYS-17; GLN-61; MET-171; GLY-210; ARG-219; LEU-243; SER-273; ASP-288; GLN-291 AND PHE-298.
[13]"Genetic variations of the melatonin pathway in patients with attention-deficit and hyperactivity disorders."
Chaste P., Clement N., Botros H.G., Guillaume J.L., Konyukh M., Pagan C., Scheid I., Nygren G., Anckarsater H., Rastam M., Stahlberg O., Gillberg I.C., Melke J., Delorme R., Leblond C., Toro R., Huguet G., Fauchereau F. expand/collapse author list , Durand C., Boudarene L., Serrano E., Lemiere N., Launay J.M., Leboyer M., Jockers R., Gillberg C., Bourgeron T.
J. Pineal Res. 51:394-399(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLY-210 AND PHE-298.
[14]"Genetic and functional abnormalities of the melatonin biosynthesis pathway in patients with bipolar disorder."
Etain B., Dumaine A., Bellivier F., Pagan C., Francelle L., Goubran-Botros H., Moreno S., Deshommes J., Moustafa K., Le Dudal K., Mathieu F., Henry C., Kahn J.P., Launay J.M., Muhleisen T.W., Cichon S., Bourgeron T., Leboyer M., Jamain S.
Hum. Mol. Genet. 21:4030-4037(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLN-61; LYS-111; ARG-219; LEU-243; HIS-248; SER-273; ASP-288; GLN-291; PHE-298 AND MET-305.
[15]"Sequencing ASMT identifies rare mutations in Chinese Han patients with autism."
Wang L., Li J., Ruan Y., Lu T., Liu C., Jia M., Yue W., Liu J., Bourgeron T., Zhang D.
PLoS ONE 8:E53727-E53727(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LYS-17; TRP-115; SER-151; ILE-166; GLY-179; MET-211; MET-217 AND LEU-243.
+Additional computationally mapped references.

Web resources

Wikipedia

5-hydroxyindole-O-methyltransferase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U11098 expand/collapse EMBL AC list , U11089, U11093, U11094, U11095, U11096, U11092, U11097 Genomic DNA. Translation: AAA75291.1.
U11098 expand/collapse EMBL AC list , U11089, U11093, U11094, U11095, U11096, U11097 Genomic DNA. Translation: AAA75289.1.
U11098 expand/collapse EMBL AC list , U11089, U11093, U11094, U11095, U11096, U11092, U11097 Genomic DNA. Translation: AAA75290.1.
U11090 mRNA. Translation: AAA58582.1.
U11091 mRNA. Translation: AAA58583.1.
M83779 mRNA. Translation: AAA17020.1.
AK314922 mRNA. Translation: BAG37430.1.
AL683807 Genomic DNA. No translation available.
BC001620 mRNA. Translation: AAH01620.1.
CCDSCCDS14117.1. [P46597-3]
CCDS55364.1. [P46597-2]
PIRI37463.
RefSeqNP_001164509.1. NM_001171038.1. [P46597-3]
NP_001164510.1. NM_001171039.1. [P46597-2]
NP_004034.2. NM_004043.2. [P46597-3]
UniGeneHs.522572.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4A6DX-ray2.40A1-345[»]
4A6EX-ray2.70A1-345[»]
ProteinModelPortalP46597.
SMRP46597. Positions 1-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000370639.

Polymorphism databases

DMDM1170276.

Proteomic databases

MaxQBP46597.
PaxDbP46597.
PRIDEP46597.

Protocols and materials databases

DNASU438.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381229; ENSP00000370627; ENSG00000196433. [P46597-1]
ENST00000381233; ENSP00000370631; ENSG00000196433. [P46597-2]
ENST00000381241; ENSP00000370639; ENSG00000196433. [P46597-3]
GeneID438.
KEGGhsa:438.
UCSCuc004cqe.3. human. [P46597-2]

Organism-specific databases

CTD438.
GeneCardsGC0XP001674.
HGNCHGNC:750. ASMT.
MIM300015. gene.
402500. gene.
neXtProtNX_P46597.
PharmGKBPA25049.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0500.
HOGENOMHOG000247024.
HOVERGENHBG001526.
KOK00543.
OMAVSPTSQC.
OrthoDBEOG7W1557.
PhylomeDBP46597.
TreeFamTF314574.

Enzyme and pathway databases

BioCycMetaCyc:HS09884-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00837; UER00815.

Gene expression databases

ArrayExpressP46597.
BgeeP46597.
GenevestigatorP46597.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProIPR025781. AS_MeTrfase.
IPR016461. COMT.
IPR001077. O_MeTrfase_2.
IPR029063. SAM-dependent_MTases-like.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFPIRSF005739. O-mtase. 1 hit.
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS51683. SAM_OMT_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAcetylserotonin_O-methyltransferase.
GenomeRNAi438.
NextBio1835.
PROP46597.
SOURCESearch...

Entry information

Entry nameASMT_HUMAN
AccessionPrimary (citable) accession number: P46597
Secondary accession number(s): B2RC33 expand/collapse secondary AC list , Q16598, Q5JQ72, Q5JQ73
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 129 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 X

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