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P46597

- ASMT_HUMAN

UniProt

P46597 - ASMT_HUMAN

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Protein

Acetylserotonin O-methyltransferase

Gene
ASMT
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Pathwayi

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/acceptor Inferred
Binding sitei256 – 2561Substrate
Binding sitei302 – 3021Substrate
Binding sitei306 – 3061Substrate

GO - Molecular functioni

  1. acetylserotonin O-methyltransferase activity Source: UniProtKB
  2. identical protein binding Source: IntAct
  3. O-methyltransferase activity Source: ProtInc
  4. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. indolalkylamine biosynthetic process Source: Reactome
  3. melatonin biosynthetic process Source: UniProtKB
  4. negative regulation of male gonad development Source: Ensembl
  5. small molecule metabolic process Source: Reactome
  6. translation Source: ProtInc
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.
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: Chromosome X

Organism-specific databases

HGNCiHGNC:750. ASMT.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
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.

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 (1 Publication), and not at the protein level (1 Publication).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

ArrayExpressiP46597.
BgeeiP46597.
GenevestigatoriP46597.

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 – 3125
Helixi33 – 397
Beta strandi40 – 423
Helixi46 – 538
Helixi57 – 6913
Beta strandi72 – 787
Beta strandi81 – 866
Helixi88 – 947
Helixi103 – 1119
Helixi113 – 1175
Helixi120 – 1267
Helixi131 – 1355
Helixi142 – 1465
Helixi150 – 16112
Helixi164 – 17310
Helixi177 – 1793
Beta strandi181 – 1866
Helixi192 – 2009
Beta strandi205 – 2106
Helixi212 – 22110
Beta strandi229 – 2357
Turni237 – 2393
Beta strandi246 – 2538
Helixi254 – 2563
Helixi259 – 27214
Beta strandi278 – 2836
Helixi294 – 30512
Beta strandi306 – 3083
Helixi314 – 32411
Beta strandi327 – 3326
Beta strandi335 – 3373
Beta strandi339 – 3446

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A6DX-ray2.40A1-345[»]
4A6EX-ray2.70A1-345[»]
ProteinModelPortaliP46597.
SMRiP46597. Positions 1-345.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

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

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR025781. AS_MeTrfase.
IPR016461. COMT.
IPR001077. O_MeTrfase_2.
IPR029063. SAM-dependent_MTases-like.
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. Align

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

MGSSEDQAYR LLNDYANGFM VSQVLFAACE LGVFDLLAEA PGPLDVAAVA    50
AGVRASAHGT ELLLDICVSL KLLKVETRGG KAFYRNTELS SDYLTTVSPT 100
SQCSMLKYMG RTSYRCWGHL ADAVREGRNQ YLETFGVPAE ELFTAIYRSE 150
GERLQFMQAL QEVWSVNGRS VLTAFDLSVF PLMCDLGGGA GALAKECMSL 200
YPGCKITVFD IPEVVWTAKQ HFSFQEEEQI DFQEGDFFKD PLPEADLYIL 250
ARVLHDWADG KCSHLLERIY HTCKPGGGIL VIESLLDEDR RGPLLTQLYS 300
LNMLVQTEGQ ERTPTHYHML LSSAGFRDFQ FKKTGAIYDA ILARK 345
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.

Show »
Length:373
Mass (Da):41,661
Checksum:i8CA134BD0BA50FDD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131N → H Polymorphism with no effect on enzyme activity. 2 Publications
Corresponds to variant rs121918819 [ dbSNP | Ensembl ].
VAR_069111
Natural varianti17 – 171N → K Functional polymorphism that nearly abolishes enzyme activity. 4 Publications
Corresponds to variant rs17149149 [ dbSNP | Ensembl ].
VAR_045991
Natural varianti61 – 611E → Q Functional polymorphism with reduced enzyme activity. 3 Publications
Corresponds to variant rs121918823 [ dbSNP | Ensembl ].
VAR_069112
Natural varianti81 – 811K → E Polymorphism with no effect on enzyme activity. 2 Publications
Corresponds to variant rs117343570 [ dbSNP | Ensembl ].
VAR_069113
Natural varianti111 – 1111R → K Polymorphism with 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 that 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 that 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 with no effect on enzyme activity. 3 Publications
Corresponds to variant rs121918825 [ dbSNP | Ensembl ].
VAR_069123
Natural varianti243 – 2431P → L Functional polymorphism with reduced enzyme activity. 4 Publications
Corresponds to variant rs121918826 [ dbSNP | Ensembl ].
VAR_069124
Natural varianti248 – 2481Y → H Functional polymorphism that nearly abolishes enzyme activity. 2 Publications
VAR_069125
Natural varianti269 – 2691I → M Functional polymorphism with reduced enzyme activity. 1 Publication
Corresponds to variant rs146121655 [ dbSNP | Ensembl ].
VAR_069126
Natural varianti273 – 2731C → S Functional polymorphism with reduced enzyme activity. 3 Publications
Corresponds to variant rs121918827 [ dbSNP | Ensembl ].
VAR_069127
Natural varianti278 – 2781G → A Functional polymorphism with reduced enzyme activity. 2 Publications
VAR_069128
Natural varianti288 – 2881E → D Polymorphism with no effect on enzyme activity. 4 Publications
Corresponds to variant rs121918821 [ dbSNP | Ensembl ].
VAR_069129
Natural varianti291 – 2911R → Q Functional polymorphism that nearly abolishes enzyme activity. 3 Publications
VAR_069130
Natural varianti298 – 2981L → F Functional polymorphism that nearly abolishes enzyme activity. 6 Publications
Corresponds to variant rs121918822 [ dbSNP | Ensembl ].
VAR_069131
Natural varianti305 – 3051V → M Functional polymorphism with reduced enzyme activity. 2 Publications
VAR_069132

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei188 – 1881G → GTWIKLETIILSKLSQGQKT KHRVFSLIG in isoform 3. VSP_004284
Alternative sequencei189 – 23547Missing in isoform 2. VSP_004285Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti302 – 3021N → S in BAG37430. 1 Publication
Isoform 3 (identifier: P46597-3)
Sequence conflicti190 – 1901W → R in AAA58582. 1 Publication
Sequence conflicti190 – 1901W → R in AAA58583. 1 Publication
Sequence conflicti190 – 1901W → R in AAA75290. 1 Publication
Sequence conflicti190 – 1901W → R in AAA17020. 1 Publication
Sequence conflicti190 – 1901W → R in BAG37430. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]

Polymorphism databases

DMDMi1170276.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

5-hydroxyindole-O-methyltransferase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
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:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 1-345.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000370639.

Polymorphism databases

DMDMi 1170276.

Proteomic databases

MaxQBi P46597.
PaxDbi P46597.
PRIDEi P46597.

Protocols and materials databases

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 uc004cqe.3. human. [P46597-2 ]

Organism-specific databases

CTDi 438.
GeneCardsi GC0XP001674.
HGNCi HGNC:750. ASMT.
MIMi 300015. gene.
402500. gene.
neXtProti NX_P46597.
PharmGKBi PA25049.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0500.
HOGENOMi HOG000247024.
HOVERGENi HBG001526.
KOi K00543.
OMAi VSPTSQC.
OrthoDBi EOG7W1557.
PhylomeDBi P46597.
TreeFami TF314574.

Enzyme and pathway databases

UniPathwayi UPA00837 ; UER00815 .
BioCyci MetaCyc:HS09884-MONOMER.
Reactomei REACT_15439. Serotonin and melatonin biosynthesis.

Miscellaneous databases

GeneWikii Acetylserotonin_O-methyltransferase.
GenomeRNAii 438.
NextBioi 1835.
PROi P46597.
SOURCEi Search...

Gene expression databases

ArrayExpressi P46597.
Bgeei P46597.
Genevestigatori P46597.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProi IPR025781. AS_MeTrfase.
IPR016461. COMT.
IPR001077. O_MeTrfase_2.
IPR029063. SAM-dependent_MTases-like.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00891. Methyltransf_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF005739. O-mtase. 1 hit.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51683. SAM_OMT_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 130 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

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