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Protein

Acetylserotonin O-methyltransferase

Gene

ASMT

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

Functioni

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.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin.1 Publication

Pathway: melatonin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes melatonin from serotonin.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Serotonin N-acetyltransferase (AANAT), Acetylserotonin O-methyltransferase (ASMT)
  2. no protein annotated in this organism
This subpathway is part of the pathway melatonin biosynthesis, which is itself part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes melatonin from serotonin, the pathway melatonin biosynthesis and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei147 – 1471S-adenosyl-L-methionine
Binding sitei164 – 1641S-adenosyl-L-methionine
Binding sitei210 – 2101S-adenosyl-L-methionine
Binding sitei252 – 2521S-adenosyl-L-methionine
Active sitei255 – 2551Proton donor/acceptor1 Publication
Binding sitei256 – 2561Substrate
Binding sitei302 – 3021Substrate
Binding sitei306 – 3061Substrate

GO - Molecular functioni

  • acetylserotonin O-methyltransferase activity Source: UniProtKB
  • identical protein binding Source: IntAct
  • O-methyltransferase activity Source: ProtInc
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Melatonin biosynthesis

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:HS09884-MONOMER.
BRENDAi2.1.1.4. 2681.
ReactomeiREACT_15439. Serotonin and melatonin biosynthesis.
UniPathwayiUPA00837; UER00815.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylserotonin O-methyltransferase (EC:2.1.1.4)
Alternative name(s):
Hydroxyindole O-methyltransferase
Short name:
HIOMT
Gene namesi
Name:ASMT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:750. ASMT.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111L → F: Reduced enzyme activity. 1 Publication
Mutagenesisi31 – 311L → H: No effect on enzyme activity.
Mutagenesisi296 – 2961T → M: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi318 – 3181H → D: Reduced enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA25049.

Chemistry

DrugBankiDB01065. Melatonin.

Polymorphism and mutation databases

BioMutaiASMT.
DMDMi1170276.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345Acetylserotonin O-methyltransferasePRO_0000083982Add
BLAST

Proteomic databases

MaxQBiP46597.
PaxDbiP46597.
PRIDEiP46597.

Expressioni

Tissue specificityi

Expressed in the pineal gland (at protein level). In the retina, very low expression is found at the mRNA level (PubMed:7989373), and not at the protein level (PubMed:8574683).3 Publications

Inductioni

By all-trans-, 9-cis- and 13-cis-retinoic acid and by serum treatment, following starvation, in the retinoblastoma cell line Y79.2 Publications

Gene expression databases

BgeeiP46597.
ExpressionAtlasiP46597. baseline.
GenevisibleiP46597. HS.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-6502097,EBI-6502097

Protein-protein interaction databases

STRINGi9606.ENSP00000370639.

Structurei

Secondary structure

1
345
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 3125Combined sources
Helixi33 – 397Combined sources
Beta strandi40 – 423Combined sources
Helixi46 – 538Combined sources
Helixi57 – 6913Combined sources
Beta strandi72 – 787Combined sources
Beta strandi81 – 866Combined sources
Helixi88 – 947Combined sources
Helixi103 – 1119Combined sources
Helixi113 – 1175Combined sources
Helixi120 – 1267Combined sources
Helixi131 – 1355Combined sources
Helixi142 – 1465Combined sources
Helixi150 – 16112Combined sources
Helixi164 – 17310Combined sources
Helixi177 – 1793Combined sources
Beta strandi181 – 1866Combined sources
Helixi192 – 2009Combined sources
Beta strandi205 – 2106Combined sources
Helixi212 – 22110Combined sources
Beta strandi229 – 2357Combined sources
Turni237 – 2393Combined sources
Beta strandi246 – 2538Combined sources
Helixi254 – 2563Combined sources
Helixi259 – 27214Combined sources
Beta strandi278 – 2836Combined sources
Helixi294 – 30512Combined sources
Beta strandi306 – 3083Combined sources
Helixi314 – 32411Combined sources
Beta strandi327 – 3326Combined sources
Beta strandi335 – 3373Combined sources
Beta strandi339 – 3446Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A6DX-ray2.40A1-345[»]
4A6EX-ray2.70A1-345[»]
ProteinModelPortaliP46597.
SMRiP46597. Positions 1-345.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni235 – 2373S-adenosyl-L-methionine binding

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0500.
GeneTreeiENSGT00530000064032.
HOGENOMiHOG000247024.
HOVERGENiHBG001526.
InParanoidiP46597.
KOiK00543.
OMAiVSPTSQC.
OrthoDBiEOG7W1557.
PhylomeDBiP46597.
TreeFamiTF314574.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR029063. SAM-dependent_MTases.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005739. O-mtase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P46597-1) [UniParc]FASTAAdd to basket

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
MGSSEDQAYR LLNDYANGFM VSQVLFAACE LGVFDLLAEA PGPLDVAAVA
60 70 80 90 100
AGVRASAHGT ELLLDICVSL KLLKVETRGG KAFYRNTELS SDYLTTVSPT
110 120 130 140 150
SQCSMLKYMG RTSYRCWGHL ADAVREGRNQ YLETFGVPAE ELFTAIYRSE
160 170 180 190 200
GERLQFMQAL QEVWSVNGRS VLTAFDLSVF PLMCDLGGGA GALAKECMSL
210 220 230 240 250
YPGCKITVFD IPEVVWTAKQ HFSFQEEEQI DFQEGDFFKD PLPEADLYIL
260 270 280 290 300
ARVLHDWADG KCSHLLERIY HTCKPGGGIL VIESLLDEDR RGPLLTQLYS
310 320 330 340
LNMLVQTEGQ ERTPTHYHML LSSAGFRDFQ FKKTGAIYDA ILARK
Length:345
Mass (Da):38,453
Last modified:November 1, 1995 - v1
Checksum:i187A375E1E2940B7
GO
Isoform 2 (identifier: P46597-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     189-235: Missing.

Show »
Length:298
Mass (Da):33,192
Checksum:iAAFC60D1F8D70E5A
GO
Isoform 3 (identifier: P46597-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     188-188: G → GTWIKLETIILSKLSQGQKTKHRVFSLIG

Note: Includes part of a LINE-1 element.Curated
Show »
Length:373
Mass (Da):41,661
Checksum:i8CA134BD0BA50FDD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti302 – 3021N → S in BAG37430 (PubMed:14702039).Curated
Isoform 3 (identifier: P46597-3)
Sequence conflicti190 – 1901W → R in AAA58582 (PubMed:7989373).Curated
Sequence conflicti190 – 1901W → R in AAA58583 (PubMed:7989373).Curated
Sequence conflicti190 – 1901W → R in AAA75290 (PubMed:7989373).Curated
Sequence conflicti190 – 1901W → R in AAA17020 (PubMed:8397829).Curated
Sequence conflicti190 – 1901W → R in BAG37430 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131N → H Polymorphism; no effect on enzyme activity. 2 Publications
Corresponds to variant rs121918819 [ dbSNP | Ensembl ].
VAR_069111
Natural varianti17 – 171N → K Functional polymorphism; nearly abolishes enzyme activity. 4 Publications
Corresponds to variant rs17149149 [ dbSNP | Ensembl ].
VAR_045991
Natural varianti61 – 611E → Q Functional polymorphism; reduced enzyme activity. 3 Publications
Corresponds to variant rs121918823 [ dbSNP | Ensembl ].
VAR_069112
Natural varianti81 – 811K → E Polymorphism; no effect on enzyme activity. 2 Publications
Corresponds to variant rs117343570 [ dbSNP | Ensembl ].
VAR_069113
Natural varianti111 – 1111R → K Polymorphism; no effect on enzyme activity. 2 Publications
VAR_069114
Natural varianti115 – 1151R → W.1 Publication
Corresponds to variant rs201053197 [ dbSNP | Ensembl ].
VAR_069115
Natural varianti151 – 1511G → S.1 Publication
Corresponds to variant rs192710293 [ dbSNP | Ensembl ].
VAR_069116
Natural varianti166 – 1661V → I.1 Publication
VAR_069117
Natural varianti171 – 1711V → M Functional polymorphism; nearly abolishes enzyme activity. 2 Publications
Corresponds to variant rs121918820 [ dbSNP | Ensembl ].
VAR_069118
Natural varianti179 – 1791V → G.1 Publication
VAR_069119
Natural varianti210 – 2101D → G Functional polymorphism; nearly abolishes enzyme activity. 3 Publications
Corresponds to variant rs121918824 [ dbSNP | Ensembl ].
VAR_069120
Natural varianti211 – 2111I → M.1 Publication
Corresponds to variant rs201316181 [ dbSNP | Ensembl ].
VAR_069121
Natural varianti217 – 2171T → M.1 Publication
Corresponds to variant rs148036160 [ dbSNP | Ensembl ].
VAR_069122
Natural varianti219 – 2191K → R Polymorphism; no effect on enzyme activity. 3 Publications
Corresponds to variant rs121918825 [ dbSNP | Ensembl ].
VAR_069123
Natural varianti243 – 2431P → L Functional polymorphism; reduced enzyme activity. 4 Publications
Corresponds to variant rs121918826 [ dbSNP | Ensembl ].
VAR_069124
Natural varianti248 – 2481Y → H Functional polymorphism; nearly abolishes enzyme activity. 2 Publications
VAR_069125
Natural varianti269 – 2691I → M Functional polymorphism; reduced enzyme activity. 1 Publication
Corresponds to variant rs146121655 [ dbSNP | Ensembl ].
VAR_069126
Natural varianti273 – 2731C → S Functional polymorphism; reduced enzyme activity. 3 Publications
Corresponds to variant rs121918827 [ dbSNP | Ensembl ].
VAR_069127
Natural varianti278 – 2781G → A Functional polymorphism; reduced enzyme activity. 2 Publications
VAR_069128
Natural varianti288 – 2881E → D Polymorphism; no effect on enzyme activity. 4 Publications
Corresponds to variant rs121918821 [ dbSNP | Ensembl ].
VAR_069129
Natural varianti291 – 2911R → Q Functional polymorphism; nearly abolishes enzyme activity. 3 Publications
VAR_069130
Natural varianti298 – 2981L → F Functional polymorphism; nearly abolishes enzyme activity. 6 Publications
Corresponds to variant rs121918822 [ dbSNP | Ensembl ].
VAR_069131
Natural varianti305 – 3051V → M Functional polymorphism; reduced enzyme activity. 2 Publications
VAR_069132

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei188 – 1881G → GTWIKLETIILSKLSQGQKT KHRVFSLIG in isoform 3. 2 PublicationsVSP_004284
Alternative sequencei189 – 23547Missing in isoform 2. 1 PublicationVSP_004285Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11098
, U11089, U11093, U11094, U11095, U11096, U11092, U11097 Genomic DNA. Translation: AAA75291.1.
U11098
, U11089, U11093, U11094, U11095, U11096, U11097 Genomic DNA. Translation: AAA75289.1.
U11098
, 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.
CCDSiCCDS14117.1. [P46597-3]
CCDS55364.1. [P46597-2]
PIRiI37463.
RefSeqiNP_001164509.1. NM_001171038.1. [P46597-3]
NP_001164510.1. NM_001171039.1. [P46597-2]
NP_004034.2. NM_004043.2. [P46597-3]
UniGeneiHs.522572.

Genome annotation databases

EnsembliENST00000381229; ENSP00000370627; ENSG00000196433. [P46597-1]
ENST00000381233; ENSP00000370631; ENSG00000196433. [P46597-2]
ENST00000381241; ENSP00000370639; ENSG00000196433. [P46597-3]
GeneIDi438.
KEGGihsa:438.
UCSCiuc004cqe.3. human. [P46597-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

5-hydroxyindole-O-methyltransferase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11098
, U11089, U11093, U11094, U11095, U11096, U11092, U11097 Genomic DNA. Translation: AAA75291.1.
U11098
, U11089, U11093, U11094, U11095, U11096, U11097 Genomic DNA. Translation: AAA75289.1.
U11098
, 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.
CCDSiCCDS14117.1. [P46597-3]
CCDS55364.1. [P46597-2]
PIRiI37463.
RefSeqiNP_001164509.1. NM_001171038.1. [P46597-3]
NP_001164510.1. NM_001171039.1. [P46597-2]
NP_004034.2. NM_004043.2. [P46597-3]
UniGeneiHs.522572.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A6DX-ray2.40A1-345[»]
4A6EX-ray2.70A1-345[»]
ProteinModelPortaliP46597.
SMRiP46597. Positions 1-345.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000370639.

Chemistry

DrugBankiDB01065. Melatonin.

Polymorphism and mutation databases

BioMutaiASMT.
DMDMi1170276.

Proteomic databases

MaxQBiP46597.
PaxDbiP46597.
PRIDEiP46597.

Protocols and materials databases

DNASUi438.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381229; ENSP00000370627; ENSG00000196433. [P46597-1]
ENST00000381233; ENSP00000370631; ENSG00000196433. [P46597-2]
ENST00000381241; ENSP00000370639; ENSG00000196433. [P46597-3]
GeneIDi438.
KEGGihsa:438.
UCSCiuc004cqe.3. human. [P46597-2]

Organism-specific databases

CTDi438.
GeneCardsiGC0XP001714.
HGNCiHGNC:750. ASMT.
MIMi300015. gene.
402500. gene.
neXtProtiNX_P46597.
PharmGKBiPA25049.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0500.
GeneTreeiENSGT00530000064032.
HOGENOMiHOG000247024.
HOVERGENiHBG001526.
InParanoidiP46597.
KOiK00543.
OMAiVSPTSQC.
OrthoDBiEOG7W1557.
PhylomeDBiP46597.
TreeFamiTF314574.

Enzyme and pathway databases

UniPathwayiUPA00837; UER00815.
BioCyciMetaCyc:HS09884-MONOMER.
BRENDAi2.1.1.4. 2681.
ReactomeiREACT_15439. Serotonin and melatonin biosynthesis.

Miscellaneous databases

GeneWikiiAcetylserotonin_O-methyltransferase.
GenomeRNAii438.
NextBioi1835.
PROiP46597.
SOURCEiSearch...

Gene expression databases

BgeeiP46597.
ExpressionAtlasiP46597. baseline.
GenevisibleiP46597. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR029063. SAM-dependent_MTases.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005739. O-mtase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. Cited for: VARIANTS LYS-17; GLU-81; ALA-278 AND PHE-298.
  12. 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. Cited for: VARIANTS GLY-210 AND PHE-298.
  14. 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.

Entry informationi

Entry nameiASMT_HUMAN
AccessioniPrimary (citable) accession number: P46597
Secondary accession number(s): B2RC33
, Q16598, Q5JQ72, Q5JQ73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 24, 2015
This is version 138 of the entry and version 1 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

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.