Reviewed, UniProtKB/Swiss-Prot P46597 (HIOM_HUMAN)

Names and origin

Protein names

Recommended name:
    Hydroxyindole O-methyltransferase
      Short name(s)=HIOMT
    EC=2.1.1.4
Alternative name(s):
    Acetylserotonin O-methyltransferase
      Short name(s)=ASMT

Gene names

Name:

ASMT

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	345 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine.
Pathway	Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2.
Tissue specificity	Most abundant in pineal gland, less in retina and brain, not in pigment epithelium.
Miscellaneous	The gene encoding for this protein is located in the pseudoautosomal region 1 (PAR1) of X and Y chromosomes.
Sequence similarities	Belongs to the methyltransferase superfamily.

Ontologies

Keywords
Biological process	Melatonin biosynthesis
Coding sequence diversity	Alternative splicing
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Gene Ontology (GO)
Biological process	translation Ref.2 Traceable author statement. Source: ProtInc
Molecular function	O-methyltransferase activity Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

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 → GTRIKLETIILSKLSQGQKTKHRVFSLIG

Notes: Includes part of a LINE-1 element.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 345	345	Hydroxyindole O-methyltransferase
Natural variations
	Alternative sequence	188	1	G → GTRIKLETIILSKLSQGQKT KHRVFSLIG in isoform 3.
	Alternative sequence	189 – 235	47	Missing in isoform 2.

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 187A375E1E2940B7	FASTA	345	38,453
	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
	Isoform 2 [UniParc]. Checksum: AAFC60D1F8D70E5A		298	33,192
	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 PLMCDLGGDF FKDPLPEADL YILARVLHDW ADGKCSHLLE RIYHTCKPGG GILVIESLLD 250 260 270 280 290 EDRRGPLLTQ LYSLNMLVQT EGQERTPTHY HMLLSSAGFR DFQFKKTGAI YDAILARK
	Isoform 3 [UniParc]. Checksum: 29A343CF7EA50ADE		373	41,631
	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 PLMCDLGGTR IKLETIILSK LSQGQKTKHR VFSLIGGAGA LAKECMSLYP GCKITVFDIP 250 260 270 280 290 300 EVVWTAKQHF SFQEEEQIDF QEGDFFKDPL PEADLYILAR VLHDWADGKC SHLLERIYHT 310 320 330 340 350 360 CKPGGGILVI ESLLDEDRRG PLLTQLYSLN MLVQTEGQER TPTHYHMLLS SAGFRDFQFK 370 KTGAIYDAIL ARK

References

	« Hide 'large scale' referencesShow '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: 7989373] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
[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: 8397829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Pineal gland.
[3]	"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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] (ISOFORM 2). Tissue: Eye.

Web resources

Wikipedia

5-hydroxyindole-O-methyltransferase entry

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. AL683807 Genomic DNA. Translation: CAI41503.1. AL683807 Genomic DNA. Translation: CAI41502.1. BC001620 mRNA. Translation: AAH01620.1.
PIR	I37463.
RefSeq	NP_004034.2.
UniGene	Hs.522572
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSG00000196433. Homo sapiens. [Contig view]
GeneID	438.
KEGG	hsa:438.
Organism-specific databases
H-InvDB	HIX0093577. HIX0093723.
HGNC	HGNC:750. ASMT.
MIM	300015. gene. 402500. gene.
PharmGKB	PA25049.
GenAtlas	Search...
GeneCards	Search...
GeneLynx	Search...
Phylogenomic databases
HOVERGEN	P46597.
Gene expression databases
ArrayExpress	P46597.
GermOnline	ENSG00000196433. Homo sapiens.
Family and domain databases
InterPro	IPR016461. O-MeTrfase_COMT_euk. IPR001077. O_MeTrfase_2. [Graphical view]
Pfam	PF00891. Methyltransf_2. 1 hit. [Graphical view]
PIRSF	PIRSF005739. O-mtase. 1 hit.
ProDom	P46597. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
LinkHub	P46597.
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

HIOM_HUMAN

Accession

Primary (citable) accession number: P46597
Secondary accession number(s): Q16598, Q5JQ72, Q5JQ73

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	July 22, 2008
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)