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P21673

- SAT1_HUMAN

UniProt

P21673 - SAT1_HUMAN

Protein

Diamine acetyltransferase 1

Gene

SAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    Pathwayi

    Sites

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

    GO - Molecular functioni

    1. diamine N-acetyltransferase activity Source: ProtInc
    2. protein binding Source: IntAct
    3. spermidine binding Source: Ensembl

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. polyamine biosynthetic process Source: Reactome
    4. polyamine metabolic process Source: Reactome
    5. putrescine catabolic process Source: UniProtKB-UniPathway
    6. regulation of cell proliferation Source: Ensembl
    7. small molecule metabolic process Source: Reactome
    8. spermidine acetylation Source: Ensembl

    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: Chromosome X

    Organism-specific databases

    HGNCiHGNC:10540. SAT1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. intracellular Source: LIFEdb

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Keratosis follicularis spinulosa decalvans X-linked (KFSDX) [MIM:308800]: A 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.2 Publications
    Note: The disease may be caused by mutations affecting the gene represented in this entry.

    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.

    PTM / Processingi

    Molecule processing

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

    Proteomic databases

    PaxDbiP21673.
    PRIDEiP21673.

    PTM databases

    PhosphoSiteiP21673.

    Expressioni

    Gene expression databases

    ArrayExpressiP21673.
    BgeeiP21673.
    CleanExiHS_SAT1.
    GenevestigatoriP21673.

    Organism-specific databases

    HPAiCAB047343.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi112210. 62 interactions.
    IntActiP21673. 58 interactions.
    MINTiMINT-1369180.
    STRINGi9606.ENSP00000368572.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK00657.
    OMAiAARPEDC.
    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

    MAKFVIRPAT AADCSDILRL IKELAKYEYM EEQVILTEKD LLEDGFGEHP    50
    FYHCLVAEVP KEHWTPEGHS IVGFAMYYFT YDPWIGKLLY LEDFFVMSDY 100
    RGFGIGSEIL KNLSQVAMRC RCSSMHFLVA EWNEPSINFY KRRGASDLSS 150
    EEGWRLFKID KEYLLKMATE E 171
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi114322.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14207.1.
    PIRi JH0783.
    RefSeqi NP_002961.1. NM_002970.3.
    UniGenei Hs.28491.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2B3U X-ray 1.85 A/B 1-171 [» ]
    2B3V X-ray 1.95 A 1-171 [» ]
    2B4B X-ray 2.00 A/B 1-171 [» ]
    2B4D X-ray 2.00 A/B 1-171 [» ]
    2B58 X-ray 1.95 A 1-171 [» ]
    2B5G X-ray 1.70 A/B 1-171 [» ]
    2F5I X-ray 2.30 A/B 1-171 [» ]
    2FXF X-ray 2.00 A/B 2-171 [» ]
    2G3T X-ray 1.80 A/B 1-171 [» ]
    2JEV X-ray 2.30 A/B 1-171 [» ]
    ProteinModelPortali P21673.
    SMRi P21673. Positions 3-171.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112210. 62 interactions.
    IntActi P21673. 58 interactions.
    MINTi MINT-1369180.
    STRINGi 9606.ENSP00000368572.

    Chemistry

    BindingDBi P21673.
    ChEMBLi CHEMBL4286.
    DrugBanki DB00127. Spermine.

    PTM databases

    PhosphoSitei P21673.

    Polymorphism databases

    DMDMi 114322.

    Proteomic databases

    PaxDbi P21673.
    PRIDEi P21673.

    Protocols and materials databases

    DNASUi 6303.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379270 ; ENSP00000368572 ; ENSG00000130066 .
    GeneIDi 6303.
    KEGGi hsa:6303.
    UCSCi uc004dau.3. human.

    Organism-specific databases

    CTDi 6303.
    GeneCardsi GC0XP023807.
    H-InvDB HIX0176797.
    HGNCi HGNC:10540. SAT1.
    HPAi CAB047343.
    MIMi 308800. phenotype.
    313020. gene.
    neXtProti NX_P21673.
    Orphaneti 2340. Keratosis follicularis spinulosa decalvans.
    PharmGKBi PA162402389.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0454.
    HOGENOMi HOG000078521.
    HOVERGENi HBG063175.
    KOi K00657.
    OMAi AARPEDC.
    PhylomeDBi P21673.
    TreeFami TF319736.

    Enzyme and pathway databases

    UniPathwayi UPA00188 ; UER00363 .
    BioCyci MetaCyc:HS05339-MONOMER.
    BRENDAi 2.3.1.57. 2681.
    Reactomei REACT_14805. Interconversion of polyamines.

    Miscellaneous databases

    ChiTaRSi SAT1. human.
    EvolutionaryTracei P21673.
    GeneWikii SAT1_(gene).
    GenomeRNAii 6303.
    NextBioi 24471.
    PROi P21673.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21673.
    Bgeei P21673.
    CleanExi HS_SAT1.
    Genevestigatori P21673.

    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. "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: October 1, 2014
    This is version 148 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