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Protein

Diamine acetyltransferase 1

Gene

SAT1

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

Functioni

Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)-acetylspermine > putrescine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. Also involved in the regulation of polyamine transport out of cells. Acts on 1,3-diaminopropane, 1,5-diaminopentane, putrescine, spermidine (forming N(1)- and N(8)-acetylspermidine), spermine, N(1)-acetylspermidine and N(8)-acetylspermidine.

Catalytic activityi

Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine.

Kineticsi

  1. KM=3.8 µM for acetyl-coenzyme A1 Publication
  2. KM=5.7 µM for spermine1 Publication
  3. KM=22 µM for spermidine1 Publication

    pH dependencei

    Optimum pH is 8.0.1 Publication

    Pathway: putrescine degradation

    This protein is involved in step 1 of the subpathway that synthesizes N-acetylputrescine from putrescine.
    Proteins known to be involved in this subpathway in this organism are:
    1. Diamine acetyltransferase 2 (SAT2), Diamine acetyltransferase 1 (SAT1)
    This subpathway is part of the pathway putrescine degradation, which is itself part of Amine and polyamine degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-acetylputrescine from putrescine, the pathway putrescine degradation and in Amine and polyamine degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei92 – 921Substrate; via carbonyl oxygen
    Binding sitei152 – 1521Substrate

    GO - Molecular functioni

    • diamine N-acetyltransferase activity Source: ProtInc
    • spermidine binding Source: Ensembl

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05339-MONOMER.
    BRENDAi2.3.1.57. 2681.
    ReactomeiREACT_14805. Interconversion of polyamines.
    UniPathwayiUPA00188; UER00363.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Diamine acetyltransferase 1 (EC:2.3.1.57)
    Alternative name(s):
    Polyamine N-acetyltransferase 1
    Putrescine acetyltransferase
    Spermidine/spermine N(1)-acetyltransferase 1
    Short name:
    SSAT
    Short name:
    SSAT-1
    Gene namesi
    Name:SAT1
    Synonyms:SAT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome X

    Organism-specific databases

    HGNCiHGNC:10540. SAT1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Keratosis follicularis spinulosa decalvans X-linked (KFSDX)2 Publications

    The disease may be caused by mutations affecting the gene represented in this entry.

    Disease descriptionA rare disorder affecting the skin and the eye. Affected men show thickening of the skin of the neck, ears, and extremities, especially the palms and soles, loss of eyebrows, eyelashes and beard, thickening of the eyelids with blepharitis and ectropion, and corneal degeneration.

    See also OMIM:308800

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi140 – 1401Y → F: Reduces activity by 95%. 1 Publication

    Organism-specific databases

    MIMi308800. phenotype.
    Orphaneti2340. Keratosis follicularis spinulosa decalvans.
    PharmGKBiPA162402389.

    Chemistry

    DrugBankiDB00127. Spermine.

    Polymorphism and mutation databases

    BioMutaiSAT1.
    DMDMi114322.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 171171Diamine acetyltransferase 1PRO_0000074591Add
    BLAST

    Proteomic databases

    MaxQBiP21673.
    PaxDbiP21673.
    PRIDEiP21673.

    PTM databases

    PhosphoSiteiP21673.

    Expressioni

    Gene expression databases

    BgeeiP21673.
    CleanExiHS_SAT1.
    ExpressionAtlasiP21673. baseline and differential.
    GenevisibleiP21673. HS.

    Organism-specific databases

    HPAiCAB047343.
    HPA055312.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HOXB9P174823EBI-711613,EBI-745290
    TCF25Q9BQ704EBI-711613,EBI-745182

    Protein-protein interaction databases

    BioGridi112210. 73 interactions.
    DIPiDIP-36801N.
    IntActiP21673. 59 interactions.
    MINTiMINT-1369180.
    STRINGi9606.ENSP00000368572.

    Structurei

    Secondary structure

    1
    171
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 84Combined sources
    Helixi11 – 133Combined sources
    Helixi14 – 2512Combined sources
    Beta strandi28 – 303Combined sources
    Helixi31 – 333Combined sources
    Helixi38 – 458Combined sources
    Beta strandi46 – 494Combined sources
    Beta strandi53 – 586Combined sources
    Helixi61 – 633Combined sources
    Beta strandi71 – 8212Combined sources
    Turni83 – 853Combined sources
    Beta strandi86 – 9611Combined sources
    Helixi98 – 1003Combined sources
    Beta strandi102 – 1043Combined sources
    Helixi105 – 12016Combined sources
    Beta strandi123 – 1308Combined sources
    Helixi134 – 1418Combined sources
    Turni142 – 1443Combined sources
    Helixi148 – 1525Combined sources
    Beta strandi154 – 1607Combined sources
    Helixi161 – 1688Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B3UX-ray1.85A/B1-171[»]
    2B3VX-ray1.95A1-171[»]
    2B4BX-ray2.00A/B1-171[»]
    2B4DX-ray2.00A/B1-171[»]
    2B58X-ray1.95A1-171[»]
    2B5GX-ray1.70A/B1-171[»]
    2F5IX-ray2.30A/B1-171[»]
    2FXFX-ray2.00A/B2-171[»]
    2G3TX-ray1.80A/B1-171[»]
    2JEVX-ray2.30A/B1-171[»]
    ProteinModelPortaliP21673.
    SMRiP21673. Positions 3-171.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21673.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 171168N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni27 – 282Substrate binding
    Regioni94 – 963Acetyl-CoA binding
    Regioni102 – 1076Acetyl-CoA binding
    Regioni126 – 1283Substrate binding
    Regioni133 – 1364Acetyl-CoA binding
    Regioni140 – 1434Acetyl-CoA binding

    Sequence similaritiesi

    Belongs to the acetyltransferase family.Curated
    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0454.
    HOGENOMiHOG000078521.
    HOVERGENiHBG063175.
    InParanoidiP21673.
    KOiK00657.
    OMAiFYESVGA.
    PhylomeDBiP21673.
    TreeFamiTF319736.

    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]

    Sequencei

    Sequence statusi: Complete.

    P21673-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAKFVIRPAT AADCSDILRL IKELAKYEYM EEQVILTEKD LLEDGFGEHP
    60 70 80 90 100
    FYHCLVAEVP KEHWTPEGHS IVGFAMYYFT YDPWIGKLLY LEDFFVMSDY
    110 120 130 140 150
    RGFGIGSEIL KNLSQVAMRC RCSSMHFLVA EWNEPSINFY KRRGASDLSS
    160 170
    EEGWRLFKID KEYLLKMATE E
    Length:171
    Mass (Da):20,024
    Last modified:May 1, 1991 - v1
    Checksum:i6A0578B88CD72F09
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261K → E in CAA78509 (PubMed:1417826).Curated
    Sequence conflicti26 – 261K → E in AAA98854 (PubMed:8573111).Curated
    Sequence conflicti69 – 691H → G AA sequence (PubMed:2241897).Curated
    Sequence conflicti84 – 841W → P AA sequence (PubMed:2241897).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M77693 mRNA. Translation: AAA60573.1.
    M55580 mRNA. Translation: AAA63260.1.
    Z14136 Genomic DNA. Translation: CAA78509.1.
    U40369 Genomic DNA. Translation: AAA98854.1.
    BT006825 mRNA. Translation: AAP35471.1.
    BC002503 mRNA. Translation: AAH02503.1.
    BC008424 mRNA. Translation: AAH08424.1.
    CCDSiCCDS14207.1.
    PIRiJH0783.
    RefSeqiNP_002961.1. NM_002970.3.
    UniGeneiHs.28491.

    Genome annotation databases

    EnsembliENST00000379270; ENSP00000368572; ENSG00000130066.
    GeneIDi6303.
    KEGGihsa:6303.
    UCSCiuc004dau.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M77693 mRNA. Translation: AAA60573.1.
    M55580 mRNA. Translation: AAA63260.1.
    Z14136 Genomic DNA. Translation: CAA78509.1.
    U40369 Genomic DNA. Translation: AAA98854.1.
    BT006825 mRNA. Translation: AAP35471.1.
    BC002503 mRNA. Translation: AAH02503.1.
    BC008424 mRNA. Translation: AAH08424.1.
    CCDSiCCDS14207.1.
    PIRiJH0783.
    RefSeqiNP_002961.1. NM_002970.3.
    UniGeneiHs.28491.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B3UX-ray1.85A/B1-171[»]
    2B3VX-ray1.95A1-171[»]
    2B4BX-ray2.00A/B1-171[»]
    2B4DX-ray2.00A/B1-171[»]
    2B58X-ray1.95A1-171[»]
    2B5GX-ray1.70A/B1-171[»]
    2F5IX-ray2.30A/B1-171[»]
    2FXFX-ray2.00A/B2-171[»]
    2G3TX-ray1.80A/B1-171[»]
    2JEVX-ray2.30A/B1-171[»]
    ProteinModelPortaliP21673.
    SMRiP21673. Positions 3-171.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi112210. 73 interactions.
    DIPiDIP-36801N.
    IntActiP21673. 59 interactions.
    MINTiMINT-1369180.
    STRINGi9606.ENSP00000368572.

    Chemistry

    BindingDBiP21673.
    ChEMBLiCHEMBL4286.
    DrugBankiDB00127. Spermine.

    PTM databases

    PhosphoSiteiP21673.

    Polymorphism and mutation databases

    BioMutaiSAT1.
    DMDMi114322.

    Proteomic databases

    MaxQBiP21673.
    PaxDbiP21673.
    PRIDEiP21673.

    Protocols and materials databases

    DNASUi6303.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000379270; ENSP00000368572; ENSG00000130066.
    GeneIDi6303.
    KEGGihsa:6303.
    UCSCiuc004dau.3. human.

    Organism-specific databases

    CTDi6303.
    GeneCardsiGC0XP023815.
    H-InvDBHIX0176797.
    HGNCiHGNC:10540. SAT1.
    HPAiCAB047343.
    HPA055312.
    MIMi308800. phenotype.
    313020. gene.
    neXtProtiNX_P21673.
    Orphaneti2340. Keratosis follicularis spinulosa decalvans.
    PharmGKBiPA162402389.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0454.
    HOGENOMiHOG000078521.
    HOVERGENiHBG063175.
    InParanoidiP21673.
    KOiK00657.
    OMAiFYESVGA.
    PhylomeDBiP21673.
    TreeFamiTF319736.

    Enzyme and pathway databases

    UniPathwayiUPA00188; UER00363.
    BioCyciMetaCyc:HS05339-MONOMER.
    BRENDAi2.3.1.57. 2681.
    ReactomeiREACT_14805. Interconversion of polyamines.

    Miscellaneous databases

    ChiTaRSiSAT1. human.
    EvolutionaryTraceiP21673.
    GeneWikiiSAT1_(gene).
    GenomeRNAii6303.
    NextBioi24471.
    PROiP21673.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP21673.
    CleanExiHS_SAT1.
    ExpressionAtlasiP21673. baseline and differential.
    GenevisibleiP21673. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Isolation and characterization of a cDNA clone that codes for human spermidine/spermine N1-acetyltransferase."
      Casero R.A. Jr., Celano P., Ervin S.J., Applegren N.B., Wiest L., Pegg A.E.
      J. Biol. Chem. 266:810-814(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Characterization of a full-length cDNA which codes for the human spermidine/spermine N1-acetyltransferase."
      Xiao L., Celano P., Mank A.R., Pegg A.E., Casero R.A. Jr.
      Biochem. Biophys. Res. Commun. 179:407-415(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    3. "Structure of the human spermidine/spermine N1-acetyltransferase gene (exon/intron gene organization and localization to Xp22.1)."
      Xiao L., Celano P., Mank A.R., Griffin C., Wang J.E., Casero R.A. Jr.
      Biochem. Biophys. Res. Commun. 187:1493-1502(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Differential transcription of the human spermidine/spermine N1-acetyltransferase (SSAT) gene in human lung carcinoma cells."
      Xiao L., Casero R.A. Jr.
      Biochem. J. 313:691-696(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "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: Bone marrow and Skin.
    7. "High specific induction of spermidine/spermine N1-acetyltransferase in a human large cell lung carcinoma."
      Casero R.A. Jr., Celano P., Ervin S.J., Wiest L., Pegg A.E.
      Biochem. J. 270:615-620(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    8. "Structures of wild-type and mutant human spermidine/spermine N1-acetyltransferase, a potential therapeutic drug target."
      Bewley M.C., Graziano V., Jiang J., Matz E., Studier F.W., Pegg A.E., Coleman C.S., Flanagan J.M.
      Proc. Natl. Acad. Sci. U.S.A. 103:2063-2068(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH ACETYL-COENZYME A; THE SUBSTRATES SPERMINE AND N1,N11-BIS-(ETHYL)-NORSPERMINE, MUTAGENESIS OF TYR-140, SUBUNIT.
    9. "Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase."
      Hegde S.S., Chandler J., Vetting M.W., Yu M., Blanchard J.S.
      Biochemistry 46:7187-7195(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH THE SUBSTRATE AND ACETYL-COA ANALOG N1-SPERMINE-ACETYL-COENZYME A, BIOPHYSICOCHEMICAL PROPERTIES.
    10. "Crystal structure of human spermidine/spermine N1-acetyltransferase (hSSAT): the first structure of a new sequence family of transferase homologous superfamily."
      Zhu Y.-Q., Zhu D.-Y., Yin L., Zhang Y., Vonrhein C., Wang D.-C.
      Proteins 63:1127-1131(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT.
    11. "Molecular genetic analysis of two families with keratosis follicularis spinulosa decalvans: refinement of gene localization and evidence for genetic heterogeneity."
      Oosterwijk J.C., Richard G., van der Wielen M.J.R., van de Vosse E., Harth W., Sandkuijl L.A., Bakker E., van Ommen G.-J.B.
      Hum. Genet. 100:520-524(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN KFSDX.
    12. "Gene dosage of the spermidine/spermine N(1)-acetyltransferase (SSAT) gene with putrescine accumulation in a patient with a Xp21.1p22.12 duplication and keratosis follicularis spinulosa decalvans (KFSD)."
      Gimelli G., Giglio S., Zuffardi O., Alhonen L., Suppola S., Cusano R., Lo Nigro C., Gatti R., Ravazzolo R., Seri M.
      Hum. Genet. 111:235-241(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN KFSDX.

    Entry informationi

    Entry nameiSAT1_HUMAN
    AccessioniPrimary (citable) accession number: P21673
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: June 24, 2015
    This is version 155 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.