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Q16613

- SNAT_HUMAN

UniProt

Q16613 - SNAT_HUMAN

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Protein

Serotonin N-acetyltransferase

Gene
AANAT, SNAT
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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-hydroxytryptamine
  3. KM=0.55 mM for phenylethylamine
  4. KM=10.6 mM for tyramine

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei120 – 1201Important for the catalytic mechanism; involved in substrate deprotonation By similarity
Sitei122 – 1221Important for the catalytic mechanism; involved in substrate deprotonation By similarity
Binding sitei124 – 1241Substrate; via carbonyl oxygen By 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
Complete GO annotation...

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
Complete GO annotation...

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.
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.1 Publication
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 PKA By similarity
Modified residuei205 – 2051Phosphoserine By 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.1 Publication

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ16613.
SMRiQ16613. Positions 30-195.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 194160N-acetyltransferaseAdd
BLAST

Region

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

Sequence similaritiesi

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. VSP_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.
ENST00000392492; ENSP00000376282; ENSG00000129673.
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 .
ENST00000392492 ; ENSP00000376282 ; ENSG00000129673 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 122 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

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