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Q16613

- SNAT_HUMAN

UniProt

Q16613 - SNAT_HUMAN

Protein

Serotonin N-acetyltransferase

Gene

AANAT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin.

    Catalytic activityi

    Acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine.

    Kineticsi

    1. KM=0.13 mM for tryptamine1 Publication
    2. KM=2.6 mM for 5-hydroxytryptamine1 Publication
    3. KM=0.55 mM for phenylethylamine1 Publication
    4. KM=10.6 mM for tyramine1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei120 – 1201Important for the catalytic mechanism; involved in substrate deprotonationBy similarity
    Sitei122 – 1221Important for the catalytic mechanism; involved in substrate deprotonationBy similarity
    Binding sitei124 – 1241Substrate; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. aralkylamine N-acetyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. cellular response to cAMP Source: UniProtKB
    3. circadian rhythm Source: UniProtKB
    4. indolalkylamine biosynthetic process Source: Reactome
    5. melatonin biosynthetic process Source: UniProtKB
    6. N-terminal protein amino acid acetylation Source: UniProtKB
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Biological rhythms, Melatonin biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05303-MONOMER.
    ReactomeiREACT_15439. Serotonin and melatonin biosynthesis.
    UniPathwayiUPA00837; UER00815.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serotonin N-acetyltransferase (EC:2.3.1.87)
    Short name:
    Serotonin acetylase
    Alternative name(s):
    Aralkylamine N-acetyltransferase
    Short name:
    AA-NAT
    Gene namesi
    Name:AANAT
    Synonyms:SNAT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:19. AANAT.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Delayed sleep phase syndrome (DSPS) [MIM:614163]: A circadian rhythm sleep disorder characterized by sleep-onset insomnia and difficulty in awakening at the desired time. Patients with DSPS have chronic difficulty in adjusting their sleep-onset and wake-up times to occupational, school, and social activities.1 Publication
    Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry. Susceptibility to delayed sleep phase syndrome can be conferred by variant Thr-129. Thr-129 shows a significantly higher frequency in affected individuals than in healthy controls.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti129 – 1291A → T in DSPS. 1 Publication
    Corresponds to variant rs28936679 [ dbSNP | Ensembl ].
    VAR_055086

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi31 – 311T → A: Loss of activation by cAMP. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614163. phenotype.
    PharmGKBiPA24366.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 207207Serotonin N-acetyltransferasePRO_0000074580Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei31 – 311Phosphothreonine; by PKABy similarity
    Modified residuei205 – 2051PhosphoserineBy similarity

    Post-translational modificationi

    cAMP-dependent phosphorylation on both N-terminal Thr-31 and C-terminal Ser-205 regulates AANAT activity by promoting interaction with 14-3-3 proteins.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ16613.
    PRIDEiQ16613.

    Miscellaneous databases

    PMAP-CutDBQ16613.

    Expressioni

    Tissue specificityi

    Highly expressed in pineal gland and at lower levels in the retina. Weak expression in several brain regions and in the pituitary gland.2 Publications

    Gene expression databases

    ArrayExpressiQ16613.
    BgeeiQ16613.
    CleanExiHS_AANAT.
    GenevestigatoriQ16613.

    Organism-specific databases

    HPAiHPA050784.

    Interactioni

    Subunit structurei

    Monomer By similarity. Interacts with several 14-3-3 proteins, including YWHAB, YWHAE, YWHAG and YWHAZ, preferentially when phosphorylated at Thr-31. Phosphorylation on Ser-205 also allows binding to YWHAZ, but with lower affinity. The interaction with YWHAZ considerably increases affinity for arylalkylamines and acetyl-CoA and protects the enzyme from dephosphorylation and proteasomal degradation By similarity. It may also prevent thiol-dependent inactivation By similarity.By similarity

    Protein-protein interaction databases

    BioGridi106533. 1 interaction.
    IntActiQ16613. 1 interaction.
    MINTiMINT-1559914.
    STRINGi9606.ENSP00000250615.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16613.
    SMRiQ16613. Positions 30-195.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 194160N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni124 – 1263Acetyl-CoA bindingBy similarity
    Regioni132 – 1376Acetyl-CoA bindingBy similarity
    Regioni168 – 1703Acetyl-CoA bindingBy similarity

    Sequence similaritiesi

    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG324206.
    HOGENOMiHOG000115812.
    HOVERGENiHBG016332.
    InParanoidiQ16613.
    KOiK00669.
    OMAiLRRNSGC.
    OrthoDBiEOG7C2R2B.
    PhylomeDBiQ16613.
    TreeFamiTF331622.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    [Graphical view]
    PfamiPF00583. Acetyltransf_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    PROSITEiPS51186. GNAT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q16613-1) [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

    MSTQSTHPLK PEAPRLPPGI PESPSCQRRH TLPASEFRCL TPEDAVSAFE    50
    IEREAFISVL GVCPLYLDEI RHFLTLCPEL SLGWFEEGCL VAFIIGSLWD 100
    KERLMQESLT LHRSGGHIAH LHVLAVHRAF RQQGRGPILL WRYLHHLGSQ 150
    PAVRRAALMC EDALVPFYER FSFHAVGPCA ITVGSLTFME LHCSLRGHPF 200
    LRRNSGC 207
    Length:207
    Mass (Da):23,344
    Last modified:November 1, 1996 - v1
    Checksum:i7476612F3661E0D5
    GO
    Isoform 2 (identifier: Q16613-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MEPQSMKGQKRPFGGPWRLKVLGGPPWLRRTLPKLGRPKEAPVARM

    Note: No experimental confirmation available.

    Show »
    Length:252
    Mass (Da):28,432
    Checksum:i112BEFE03782A3D8
    GO

    Sequence cautioni

    The sequence AAH69434.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151R → C.
    Corresponds to variant rs34470791 [ dbSNP | Ensembl ].
    VAR_048168
    Natural varianti129 – 1291A → T in DSPS. 1 Publication
    Corresponds to variant rs28936679 [ dbSNP | Ensembl ].
    VAR_055086

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MEPQSMKGQKRPFGGPWRLK VLGGPPWLRRTLPKLGRPKE APVARM in isoform 2. CuratedVSP_054108

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40347 mRNA. Translation: AAC50554.1.
    U40391 Genomic DNA. Translation: AAC50555.1.
    AC015802 Genomic DNA. No translation available.
    BC069434 mRNA. Translation: AAH69434.1. Different initiation.
    BC092430 mRNA. Translation: AAH92430.1.
    BC126332 mRNA. Translation: AAI26333.1.
    BC126334 mRNA. Translation: AAI26335.1.
    CCDSiCCDS11745.1. [Q16613-1]
    CCDS54169.1. [Q16613-2]
    RefSeqiNP_001079.1. NM_001088.2. [Q16613-1]
    NP_001160051.1. NM_001166579.1. [Q16613-2]
    UniGeneiHs.431417.

    Genome annotation databases

    EnsembliENST00000250615; ENSP00000250615; ENSG00000129673. [Q16613-2]
    ENST00000392492; ENSP00000376282; ENSG00000129673. [Q16613-1]
    GeneIDi15.
    KEGGihsa:15.
    UCSCiuc002jro.3. human. [Q16613-1]

    Polymorphism databases

    DMDMi11387096.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40347 mRNA. Translation: AAC50554.1 .
    U40391 Genomic DNA. Translation: AAC50555.1 .
    AC015802 Genomic DNA. No translation available.
    BC069434 mRNA. Translation: AAH69434.1 . Different initiation.
    BC092430 mRNA. Translation: AAH92430.1 .
    BC126332 mRNA. Translation: AAI26333.1 .
    BC126334 mRNA. Translation: AAI26335.1 .
    CCDSi CCDS11745.1. [Q16613-1 ]
    CCDS54169.1. [Q16613-2 ]
    RefSeqi NP_001079.1. NM_001088.2. [Q16613-1 ]
    NP_001160051.1. NM_001166579.1. [Q16613-2 ]
    UniGenei Hs.431417.

    3D structure databases

    ProteinModelPortali Q16613.
    SMRi Q16613. Positions 30-195.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106533. 1 interaction.
    IntActi Q16613. 1 interaction.
    MINTi MINT-1559914.
    STRINGi 9606.ENSP00000250615.

    Chemistry

    BindingDBi Q16613.

    Polymorphism databases

    DMDMi 11387096.

    Proteomic databases

    PaxDbi Q16613.
    PRIDEi Q16613.

    Protocols and materials databases

    DNASUi 15.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000250615 ; ENSP00000250615 ; ENSG00000129673 . [Q16613-2 ]
    ENST00000392492 ; ENSP00000376282 ; ENSG00000129673 . [Q16613-1 ]
    GeneIDi 15.
    KEGGi hsa:15.
    UCSCi uc002jro.3. human. [Q16613-1 ]

    Organism-specific databases

    CTDi 15.
    GeneCardsi GC17P074449.
    HGNCi HGNC:19. AANAT.
    HPAi HPA050784.
    MIMi 600950. gene.
    614163. phenotype.
    neXtProti NX_Q16613.
    PharmGKBi PA24366.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG324206.
    HOGENOMi HOG000115812.
    HOVERGENi HBG016332.
    InParanoidi Q16613.
    KOi K00669.
    OMAi LRRNSGC.
    OrthoDBi EOG7C2R2B.
    PhylomeDBi Q16613.
    TreeFami TF331622.

    Enzyme and pathway databases

    UniPathwayi UPA00837 ; UER00815 .
    BioCyci MetaCyc:HS05303-MONOMER.
    Reactomei REACT_15439. Serotonin and melatonin biosynthesis.

    Miscellaneous databases

    GenomeRNAii 15.
    NextBioi 35534776.
    PMAP-CutDB Q16613.
    PROi Q16613.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16613.
    Bgeei Q16613.
    CleanExi HS_AANAT.
    Genevestigatori Q16613.

    Family and domain databases

    Gene3Di 3.40.630.30. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    [Graphical view ]
    Pfami PF00583. Acetyltransf_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55729. SSF55729. 1 hit.
    PROSITEi PS51186. GNAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression."
      Coon S.L., Mazuruk K., Bernard M., Roseboom P., Klein D.C., Rodriguez I.R.
      Genomics 34:76-84(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY.
    2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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].
      Tissue: Brain and Testis.
    4. "cAMP regulation of arylalkylamine N-acetyltransferase (AANAT, EC 2.3.1.87): a new cell line (1E7) provides evidence of intracellular AANAT activation."
      Coon S.L., Weller J.L., Korf H.-W., Namboodiri M.A., Rollag M., Klein D.C.
      J. Biol. Chem. 276:24097-24107(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    5. "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis."
      Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H., Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T., Beauverger P., Ferry G., Boutin J.A., Klein D.C.
      Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH 14-3-3 PROTEINS, MUTAGENESIS OF THR-31.
    6. "Role of melatonin in upper gastrointestinal tract."
      Konturek S.J., Konturek P.C., Brzozowski T., Bubenik G.A.
      J. Physiol. Pharmacol. 58:23-52(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Significant association of the arylalkylamine N-acetyltransferase (AA-NAT) gene with delayed sleep phase syndrome."
      Hohjoh H., Takasu M., Shishikura K., Takahashi Y., Honda Y., Tokunaga K.
      Neurogenetics 4:151-153(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DSPS THR-129.

    Entry informationi

    Entry nameiSNAT_HUMAN
    AccessioniPrimary (citable) accession number: Q16613
    Secondary accession number(s): A0AVF2, J3KMZ5, Q562F4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 123 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3