ASMT

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

Miscellaneous

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

Catalytic activityⁱ

N-acetylserotonin
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
S-adenosyl-L-methionine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
melatonin
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
S-adenosyl-L-homocysteine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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.
EC:2.1.1.4
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
N-acetylserotonin
zoom
+
S-adenosyl-L-methionine
zoom
=
H⁺
zoom
+
melatonin
zoom
+
S-adenosyl-L-homocysteine
zoom

Pathwayⁱ: 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:

Serotonin N-acetyltransferase (AANAT), Acetylserotonin O-methyltransferase (ASMT)
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 key	Position(s)	DescriptionActions	Length
Binding siteⁱ	147	S-adenosyl-L-methionine	1
Binding siteⁱ	164	S-adenosyl-L-methionine	1
Binding siteⁱ	210	S-adenosyl-L-methionine	1
Binding siteⁱ	252	S-adenosyl-L-methionine	1
Active siteⁱ	255	Proton donor/acceptor1 Publication	1
Binding siteⁱ	256	Substrate	1
Binding siteⁱ	302	Substrate	1
Binding siteⁱ	306	Substrate	1

GO - Molecular functionⁱ

acetylserotonin O-methyltransferase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 22775292
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 22775292
O-methyltransferase activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
protein homodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 22775292
S-adenosylmethionine-dependent methyltransferase activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
S-methyltransferase activity Source: Reactome

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

aromatic compound biosynthetic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
indolalkylamine biosynthetic process Source: Reactome
melatonin biosynthetic process
Source: UniProtKB
Inferred from direct assayⁱ
- 22775292
translation
Source: ProtInc
Traceable author statementⁱ
- 8397829

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Methyltransferase, Transferase
Biological process	Melatonin biosynthesis
Ligand	S-adenosyl-L-methionine

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS09884-MONOMER
BRENDAⁱ	2.1.1.4 2681
Reactomeⁱ	R-HSA-209931 Serotonin and melatonin biosynthesis
UniPathwayⁱ	UPA00837;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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome X

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000196433.12
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:750 ASMT
MIMⁱ	300015 gene 402500 gene
neXtProtⁱ	NX_P46597

Subcellular locationⁱ

GO - Cellular component

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	11	L → F: Reduced enzyme activity. 1 Publication	1
Mutagenesisⁱ	31	L → H: No effect on enzyme activity.	1
Mutagenesisⁱ	296	T → M: Nearly abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	318	H → D: Reduced enzyme activity. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	438
Open Targets More...OpenTargetsⁱ	ENSG00000196433
PharmGKBⁱ	PA25049

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB01065 Melatonin

DrugBankⁱ

DB01065 Melatonin

Polymorphism and mutation databases

BioMutaⁱ	ASMT
DMDMⁱ	1170276

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000083982	1 – 345	Acetylserotonin O-methyltransferaseAdd BLAST		345

Proteomic databases

PeptideAtlas More...PeptideAtlasⁱ	P46597
PRIDEⁱ	P46597
ProteomicsDBⁱ	55743 55744 [P46597-2] 55745 [P46597-3]

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

Bgeeⁱ	ENSG00000196433 Expressed in 76 organ(s), highest expression level in adenohypophysis
ExpressionAtlasⁱ	P46597 baseline and differential
Genevisibleⁱ	P46597 HS

Interactionⁱ

Subunit structureⁱ

Homodimer.1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-6502097,EBI-6502097

With

Entry

#Exp.

IntAct

Notes

itself

3

EBI-6502097,EBI-6502097

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 22775292
protein homodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 22775292

View the complete GO annotation on QuickGO ...

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	7 – 31	Combined sources	25
Helixⁱ	33 – 39	Combined sources	7
Beta strandⁱ	40 – 42	Combined sources	3
Helixⁱ	46 – 53	Combined sources	8
Helixⁱ	57 – 69	Combined sources	13
Beta strandⁱ	72 – 78	Combined sources	7
Beta strandⁱ	81 – 86	Combined sources	6
Helixⁱ	88 – 94	Combined sources	7
Helixⁱ	103 – 111	Combined sources	9
Helixⁱ	113 – 117	Combined sources	5
Helixⁱ	120 – 126	Combined sources	7
Helixⁱ	131 – 135	Combined sources	5
Helixⁱ	142 – 146	Combined sources	5
Helixⁱ	150 – 161	Combined sources	12
Helixⁱ	164 – 173	Combined sources	10
Helixⁱ	177 – 179	Combined sources	3
Beta strandⁱ	181 – 186	Combined sources	6
Helixⁱ	192 – 200	Combined sources	9
Beta strandⁱ	205 – 210	Combined sources	6
Helixⁱ	212 – 221	Combined sources	10
Beta strandⁱ	229 – 235	Combined sources	7
Turnⁱ	237 – 239	Combined sources	3
Beta strandⁱ	246 – 253	Combined sources	8
Helixⁱ	254 – 256	Combined sources	3
Helixⁱ	259 – 272	Combined sources	14
Beta strandⁱ	278 – 283	Combined sources	6
Helixⁱ	294 – 305	Combined sources	12
Beta strandⁱ	306 – 308	Combined sources	3
Helixⁱ	314 – 324	Combined sources	11
Beta strandⁱ	327 – 332	Combined sources	6
Beta strandⁱ	335 – 337	Combined sources	3
Beta strandⁱ	339 – 344	Combined sources	6

Show more details

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4A6D	X-ray	2.40	A	1-345	[»]
	4A6E	X-ray	2.70	A	1-345	[»]
ProteinModelPortalⁱ	P46597
SMRⁱ	P46597
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	235 – 237	S-adenosyl-L-methionine binding		3

Sequence similaritiesⁱ

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

Phylogenomic databases

Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000161561
HOGENOMⁱ	HOG000247024
HOVERGENⁱ	HBG001526
InParanoidⁱ	P46597
KEGG Orthology (KO) More...KOⁱ	K00543
OMAⁱ	WHYLTDA
Database of Orthologous Groups More...OrthoDBⁱ	817726at2759
PhylomeDBⁱ	P46597
TreeFamⁱ	TF314574

Family and domain databases

Gene3Dⁱ	1.10.10.10, 1 hit
InterProⁱ	View protein in InterPro IPR031725 ASMT_dimerisation IPR016461 O-MeTrfase_COMT IPR001077 O_MeTrfase_dom IPR029063 SAM-dependent_MTases IPR036388 WH-like_DNA-bd_sf IPR036390 WH_DNA-bd_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF16864 Dimerisation2, 1 hit PF00891 Methyltransf_2, 1 hit
PIRSFⁱ	PIRSF005739 O-mtase, 1 hit
SUPFAMⁱ	SSF46785 SSF46785, 1 hit SSF53335 SSF53335, 1 hit
PROSITEⁱ	View protein in PROSITE PS51683 SAM_OMT_II, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

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

This entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

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

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

« 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 PLMCDLGGDF FKDPLPEADL 
       210        220        230        240        250
YILARVLHDW ADGKCSHLLE RIYHTCKPGG GILVIESLLD EDRRGPLLTQ 
       260        270        280        290 
LYSLNMLVQT EGQERTPTHY HMLLSSAGFR DFQFKKTGAI YDAILARK

Show »

Length:298

Mass (Da):33,192

Checksum:ⁱAAFC60D1F8D70E5A

GO

Isoform 3 (identifier: P46597-3) [UniParc]FASTA Add to basket

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

« 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 PLMCDLGGTW IKLETIILSK 
       210        220        230        240        250
LSQGQKTKHR VFSLIGGAGA LAKECMSLYP GCKITVFDIP EVVWTAKQHF 
       260        270        280        290        300
SFQEEEQIDF QEGDFFKDPL PEADLYILAR VLHDWADGKC SHLLERIYHT 
       310        320        330        340        350
CKPGGGILVI ESLLDEDRRG PLLTQLYSLN MLVQTEGQER TPTHYHMLLS 
       360        370 
SAGFRDFQFK KTGAIYDAIL ARK

Note: Includes part of a LINE-1 element.Curated

Show »

Length:373

Mass (Da):41,661

Checksum:ⁱ8CA134BD0BA50FDD

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	I7HFW6	I7HFW6_HUMAN		Acetylserotonin O-methyltransferase Acetylserotonin O-methyltransferase	ASMT	124	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	302	N → S in BAG37430 (PubMed:14702039).Curated	1
Isoform 3 (identifier: P46597-3)
Sequence conflictⁱ	190	W → R in AAA58582 (PubMed:7989373).Curated	1
Sequence conflictⁱ	190	W → R in AAA58583 (PubMed:7989373).Curated	1
Sequence conflictⁱ	190	W → R in AAA75290 (PubMed:7989373).Curated	1
Sequence conflictⁱ	190	W → R in AAA17020 (PubMed:8397829).Curated	1
Sequence conflictⁱ	190	W → R in BAG37430 (PubMed:14702039).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_069111	13	N → H Polymorphism; no effect on enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs121918819Ensembl.	1
Natural variantⁱVAR_045991	17	N → K Functional polymorphism; nearly abolishes enzyme activity. 4 PublicationsCorresponds to variant dbSNP:rs17149149Ensembl.	1
Natural variantⁱVAR_069112	61	E → Q Functional polymorphism; reduced enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs121918823Ensembl.	1
Natural variantⁱVAR_069113	81	K → E Polymorphism; no effect on enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs117343570Ensembl.	1
Natural variantⁱVAR_069114	111	R → K Polymorphism; no effect on enzyme activity. 2 Publications	1
Natural variantⁱVAR_069115	115	R → W1 PublicationCorresponds to variant dbSNP:rs201053197Ensembl.	1
Natural variantⁱVAR_069116	151	G → S1 PublicationCorresponds to variant dbSNP:rs192710293Ensembl.	1
Natural variantⁱVAR_069117	166	V → I1 PublicationCorresponds to variant dbSNP:rs373339042Ensembl.	1
Natural variantⁱVAR_069118	171	V → M Functional polymorphism; nearly abolishes enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs121918820Ensembl.	1
Natural variantⁱVAR_069119	179	V → G1 Publication	1
Natural variantⁱVAR_069120	210	D → G Functional polymorphism; nearly abolishes enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs121918824Ensembl.	1
Natural variantⁱVAR_069121	211	I → M1 PublicationCorresponds to variant dbSNP:rs201316181Ensembl.	1
Natural variantⁱVAR_069122	217	T → M1 PublicationCorresponds to variant dbSNP:rs148036160Ensembl.	1
Natural variantⁱVAR_069123	219	K → R Polymorphism; no effect on enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs121918825Ensembl.	1
Natural variantⁱVAR_069124	243	P → L Functional polymorphism; reduced enzyme activity. 4 PublicationsCorresponds to variant dbSNP:rs121918826Ensembl.	1
Natural variantⁱVAR_069125	248	Y → H Functional polymorphism; nearly abolishes enzyme activity. 2 Publications	1
Natural variantⁱVAR_069126	269	I → M Functional polymorphism; reduced enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs146121655Ensembl.	1
Natural variantⁱVAR_069127	273	C → S Functional polymorphism; reduced enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs121918827Ensembl.	1
Natural variantⁱVAR_069128	278	G → A Functional polymorphism; reduced enzyme activity. 2 Publications	1
Natural variantⁱVAR_069129	288	E → D Polymorphism; no effect on enzyme activity. 4 PublicationsCorresponds to variant dbSNP:rs121918821Ensembl.	1
Natural variantⁱVAR_069130	291	R → Q Functional polymorphism; nearly abolishes enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs121918828Ensembl.	1
Natural variantⁱVAR_069131	298	L → F Functional polymorphism; nearly abolishes enzyme activity. 6 PublicationsCorresponds to variant dbSNP:rs121918822Ensembl.	1
Natural variantⁱVAR_069132	305	V → M Functional polymorphism; reduced enzyme activity. 2 Publications	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_004284	188	G → GTWIKLETIILSKLSQGQKT KHRVFSLIG in isoform 3. 2 Publications		1
Alternative sequenceⁱVSP_004285	189 – 235	Missing in isoform 2. 1 PublicationAdd BLAST		47

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U11098 U11097 Genomic DNA Translation: AAA75291.1 U11098 U11097 Genomic DNA Translation: AAA75289.1 U11098 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS14117.1 [P46597-3] CCDS55364.1 [P46597-2]
PIRⁱ	I37463
NCBI Reference Sequences More...RefSeqⁱ	NP_001164509.1, NM_001171038.1 [P46597-3] NP_001164510.1, NM_001171039.1 [P46597-2] NP_004034.2, NM_004043.2 [P46597-3]
UniGeneⁱ	Hs.522572

Genome annotation databases

Ensemblⁱ	ENST00000381229; ENSP00000370627; ENSG00000196433 [P46597-1] ENST00000381233; ENSP00000370631; ENSG00000196433 [P46597-2] ENST00000381241; ENSP00000370639; ENSG00000196433 [P46597-3]
GeneIDⁱ	438
KEGGⁱ	hsa:438
UCSC genome browser More...UCSCⁱ	uc010ncy.4 human [P46597-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Protein	Similar proteins		Species	Score	Length	Source
P46597	Acetylserotonin O-methyltransferase isoform B (Fragment)		HUMAN		345	UniRef100_P46597
UPI00029722F0		HUMAN		353
P46597-2	Acetylserotonin O-methyltransferase isoform C (Fragment)		HUMAN		298	UniRef100_P46597-2
P46597-3	HCG1981394, isoform CRA_b		HUMAN		373	UniRef100_A0A024RBT9

Protein	Similar proteins		Species	Score	Length	Source
P46597	Acetylserotonin O-methyltransferase isoform B (Fragment)		HUMAN		345	UniRef90_P46597
Acetylserotonin O-methyltransferase		PANTR		357
ASMT isoform 2		PONAB		345
Acetylserotonin O-methyltransferase		MACMU		345
Hydroxyindole O-methyltransferase (Fragment)		MACFA		129
+5
P46597-2	Acetylserotonin O-methyltransferase isoform C (Fragment)		HUMAN		298	UniRef90_P46597-2
ASMT isoform 2		PANTR		298
ASMT isoform 3		PONAB		298
Acetylserotonin O-methyltransferase		MANLE		298
Acetylserotonin O-methyltransferase		RHIBE		298
+2
P46597-3	HCG1981394, isoform CRA_b		HUMAN		373	UniRef90_A0A024RBT9
ASMT isoform 3		PANTR		373
ASMT isoform 1		PONAB		373

Protein	Similar proteins		Species	Score	Length	Source
P46597	Acetylserotonin O-methyltransferase isoform B (Fragment)		HUMAN		345	UniRef50_P46597
Acetylserotonin O-methyltransferase		PANTR		357
ASMT isoform 2		PONAB		345
Acetylserotonin O-methyltransferase		MACMU		345
Hydroxyindole O-methyltransferase (Fragment)		MACFA		129
+40
P46597-2	Acetylserotonin O-methyltransferase isoform C (Fragment)		HUMAN		298	UniRef50_P46597-2
Acetylserotonin O-methyltransferase		RHIBE		298
ASMT isoform 2		PANTR		298
Acetylserotonin O-methyltransferase		MANLE		298
ASMT isoform 3		PONAB		298
+18
P46597-3	HCG1981394, isoform CRA_b		HUMAN		373	UniRef50_A0A024RBT9
ASMT isoform 1		PONAB		373
ASMT isoform 3		PANTR		373
Hydroxyindole O-methyltransferase-like protein		CAMFR		453
Acetylserotonin O-methyltransferase		PIG		345
+14

Cross-referencesⁱ

Web resourcesⁱ

Wikipedia

5-hydroxyindole-O-methyltransferase entry

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U11098 U11097 Genomic DNA Translation: AAA75291.1 U11098 U11097 Genomic DNA Translation: AAA75289.1 U11098 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
CCDSⁱ	CCDS14117.1 [P46597-3] CCDS55364.1 [P46597-2]
PIRⁱ	I37463
RefSeqⁱ	NP_001164509.1, NM_001171038.1 [P46597-3] NP_001164510.1, NM_001171039.1 [P46597-2] NP_004034.2, NM_004043.2 [P46597-3]
UniGeneⁱ	Hs.522572

3D structure databases

Select the link destinations: PDBeⁱ RCSB PDBⁱ PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4A6D	X-ray	2.40	A	1-345	[»]
	4A6E	X-ray	2.70	A	1-345	[»]
ProteinModelPortalⁱ	P46597
SMRⁱ	P46597
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Chemistry databases

DrugBankⁱ	DB01065 Melatonin

DrugBankⁱ

DB01065 Melatonin

Polymorphism and mutation databases

BioMutaⁱ	ASMT
DMDMⁱ	1170276

Proteomic databases

PeptideAtlasⁱ	P46597
PRIDEⁱ	P46597
ProteomicsDBⁱ	55743 55744 [P46597-2] 55745 [P46597-3]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	438
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000381229; ENSP00000370627; ENSG00000196433 [P46597-1] ENST00000381233; ENSP00000370631; ENSG00000196433 [P46597-2] ENST00000381241; ENSP00000370639; ENSG00000196433 [P46597-3]
GeneIDⁱ	438
KEGGⁱ	hsa:438
UCSCⁱ	uc010ncy.4 human [P46597-1]

Organism-specific databases

CTDⁱ	438
DisGeNETⁱ	438
EuPathDBⁱ	HostDB:ENSG00000196433.12
GeneCardsⁱ	ASMT
HGNCⁱ	HGNC:750 ASMT
MIMⁱ	300015 gene 402500 gene
neXtProtⁱ	NX_P46597
OpenTargetsⁱ	ENSG00000196433
PharmGKBⁱ	PA25049
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

GeneTreeⁱ	ENSGT00940000161561
HOGENOMⁱ	HOG000247024
HOVERGENⁱ	HBG001526
InParanoidⁱ	P46597
KOⁱ	K00543
OMAⁱ	WHYLTDA
OrthoDBⁱ	817726at2759
PhylomeDBⁱ	P46597
TreeFamⁱ	TF314574

Enzyme and pathway databases

UniPathwayⁱ	UPA00837;UER00815
BioCycⁱ	MetaCyc:HS09884-MONOMER
BRENDAⁱ	2.1.1.4 2681
Reactomeⁱ	R-HSA-209931 Serotonin and melatonin biosynthesis

Miscellaneous databases

GeneWikiⁱ	Acetylserotonin_O-methyltransferase
GenomeRNAiⁱ	438
Protein Ontology More...PROⁱ	PR:P46597
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000196433 Expressed in 76 organ(s), highest expression level in adenohypophysis
ExpressionAtlasⁱ	P46597 baseline and differential
Genevisibleⁱ	P46597 HS

Family and domain databases

Gene3Dⁱ	1.10.10.10, 1 hit
InterProⁱ	View protein in InterPro IPR031725 ASMT_dimerisation IPR016461 O-MeTrfase_COMT IPR001077 O_MeTrfase_dom IPR029063 SAM-dependent_MTases IPR036388 WH-like_DNA-bd_sf IPR036390 WH_DNA-bd_sf
Pfamⁱ	View protein in Pfam PF16864 Dimerisation2, 1 hit PF00891 Methyltransf_2, 1 hit
PIRSFⁱ	PIRSF005739 O-mtase, 1 hit
SUPFAMⁱ	SSF46785 SSF46785, 1 hit SSF53335 SSF53335, 1 hit
PROSITEⁱ	View protein in PROSITE PS51683 SAM_OMT_II, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ASMT_HUMAN
Accessionⁱ	P46597Primary (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:	January 16, 2019
	This is version 162 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human chromosome X
Human chromosome X: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P46597 (ASMT_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Acetylserotonin O-methyltransferase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: melatonin biosynthesis

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytosol

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Chemistry databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

Catalytic activityⁱ

Pathwayⁱ: melatonin biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ