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P46597

- ASMT_HUMAN

UniProt

P46597 - ASMT_HUMAN

Protein

Acetylserotonin O-methyltransferase

Gene

ASMT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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/acceptor1 Publication
    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

    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

    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 (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

    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.
    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.
    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.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 with no effect on enzyme activity. 1 Publication
    Corresponds to variant rs121918819 [ dbSNP | Ensembl ].
    VAR_069111
    Natural varianti17 – 171N → K Functional polymorphism that nearly abolishes enzyme activity. 3 Publications
    Corresponds to variant rs17149149 [ dbSNP | Ensembl ].
    VAR_045991
    Natural varianti61 – 611E → Q Functional polymorphism with reduced enzyme activity. 2 Publications
    Corresponds to variant rs121918823 [ dbSNP | Ensembl ].
    VAR_069112
    Natural varianti81 – 811K → E Polymorphism with no effect on enzyme activity. 1 Publication
    Corresponds to variant rs117343570 [ dbSNP | Ensembl ].
    VAR_069113
    Natural varianti111 – 1111R → K Polymorphism with no effect on enzyme activity. 1 Publication
    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. 1 Publication
    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. 2 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. 2 Publications
    Corresponds to variant rs121918825 [ dbSNP | Ensembl ].
    VAR_069123
    Natural varianti243 – 2431P → L Functional polymorphism with reduced enzyme activity. 3 Publications
    Corresponds to variant rs121918826 [ dbSNP | Ensembl ].
    VAR_069124
    Natural varianti248 – 2481Y → H Functional polymorphism that nearly abolishes enzyme activity. 1 Publication
    VAR_069125
    Natural varianti269 – 2691I → M Functional polymorphism with reduced enzyme activity.
    Corresponds to variant rs146121655 [ dbSNP | Ensembl ].
    VAR_069126
    Natural varianti273 – 2731C → S Functional polymorphism with reduced enzyme activity. 2 Publications
    Corresponds to variant rs121918827 [ dbSNP | Ensembl ].
    VAR_069127
    Natural varianti278 – 2781G → A Functional polymorphism with reduced enzyme activity. 1 Publication
    VAR_069128
    Natural varianti288 – 2881E → D Polymorphism with no effect on enzyme activity. 3 Publications
    Corresponds to variant rs121918821 [ dbSNP | Ensembl ].
    VAR_069129
    Natural varianti291 – 2911R → Q Functional polymorphism that nearly abolishes enzyme activity. 2 Publications
    VAR_069130
    Natural varianti298 – 2981L → F Functional polymorphism that nearly abolishes enzyme activity. 5 Publications
    Corresponds to variant rs121918822 [ dbSNP | Ensembl ].
    VAR_069131
    Natural varianti305 – 3051V → M Functional polymorphism with reduced enzyme activity. 1 Publication
    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:
    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

    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: October 1, 2014
    This is version 131 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