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Reviewed, UniProtKB/Swiss-Prot P21673 (SAT1_HUMAN)

Last modified June 16, 2009. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Diamine acetyltransferase 1
    EC=2.3.1.57
Alternative name(s):
    Spermidine/spermine N(1)-acetyltransferase 1
      Short name=SSAT-1
      Short name=SSAT
    Putrescine acetyltransferase
    Polyamine N-acetyltransferase 1
Gene names
Name: SAT1
Synonyms: SAT
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length171 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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.

Catalytic activity

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

Pathway

Amine and polyamine degradation; putrescine degradation; N-acetylputrescine from putrescine: step 1/1.

Subunit structure

Homodimer. Ref.8 Ref.10

Subcellular location

Cytoplasm.

Involvement in disease

Defects in SAT1 may be the cause of keratosis follicularis spinulosa decalvans (KFSD) [MIM:308800]; also known as keratosis follicularis spinulosa decalvans cum ophiasi or Siemens-1 syndrome. KFSD is a rare X-linked 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. Although most affected families are compatible with X-linked inheritance, KFSD appears to be clinically and genetically heterogeneous. Ref.11 Ref.12

Miscellaneous

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.

Sequence similarities

Belongs to the acetyltransferase family.

Contains 1 N-acetyltransferase domain.

biophysicochemical properties

Kinetic parameters:

KM=3.8 µM for acetyl-coenzyme A

KM=5.7 µM for spermine

KM=22 µM for spermidine

pH dependence:

Optimum pH is 8.0.

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Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondiamine N-acetyltransferase activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 171171Diamine acetyltransferase 1
PRO_0000074591

Regions

Domain4 – 171168N-acetyltransferase
Region27 – 282Substrate binding
Region94 – 963Acetyl-CoA binding
Region102 – 1076Acetyl-CoA binding
Region126 – 1283Substrate binding
Region133 – 1364Acetyl-CoA binding
Region140 – 1434Acetyl-CoA binding

Sites

Binding site921Substrate; via carbonyl oxygen
Binding site1521Substrate

Experimental info

Mutagenesis1401Y → F: Reduces activity by 95%. Ref.8
Sequence conflict261K → E in CAA78509. Ref.3
Sequence conflict261K → E in AAA98854. Ref.4
Sequence conflict691H → G AA sequence Ref.7
Sequence conflict841W → P AA sequence Ref.7

Secondary structure

1 ................................ 171
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P21673-1 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 6A0578B88CD72F09

FASTA17120,024
        10         20         30         40         50         60 
MAKFVIRPAT AADCSDILRL IKELAKYEYM EEQVILTEKD LLEDGFGEHP FYHCLVAEVP 

        70         80         90        100        110        120 
KEHWTPEGHS IVGFAMYYFT YDPWIGKLLY LEDFFVMSDY RGFGIGSEIL KNLSQVAMRC 

       130        140        150        160        170 
RCSSMHFLVA EWNEPSINFY KRRGASDLSS EEGWRLFKID KEYLLKMATE E

« Hide

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References

« Hide 'large scale' references
[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: 1985966] [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: 1652956] [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: 1417826] [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: 8573111] [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: 15489334] [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: 2241897] [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: 16455797] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH ACETYL-COENZYME A; 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: 17516632] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH 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: 16544326] [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: 9341865] [Abstract]
Cited for: INVOLVEMENT IN KFSD.
[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: 12215835] [Abstract]
Cited for: INVOLVEMENT IN KFSD.
+Additional computationally mapped references.

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Cross-references

Sequence databases

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.
IPIIPI00009889.
PIRJH0783.
RefSeqNP_002961.1.
UniGeneHs.28491

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2B3UX-ray1.85A/B1-171[»]
2B3VX-ray1.95A1-171[»]
2B4BX-ray2.00A/B1-171[»]
2B4DX-ray2.00A1-171[»]
B1-171[»]
2B58X-ray1.95A1-171[»]
2B5GX-ray1.70A1-171[»]
B1-171[»]
2F5IX-ray2.30A/B1-171[»]
2FXFX-ray2.00A/B2-171[»]
2G3TX-ray1.80A/B1-171[»]
2JEVX-ray2.30A/B1-171[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP21673. 53 interactions.

PTM databases

PhosphoSiteP21673.

Genome annotation databases

EnsemblENSG00000130066. Homo sapiens. [Contig view]
GeneID6303.
KEGGhsa:6303.

Organism-specific databases

GeneCardsGC0XP023711.
H-InvDBHIX0016703.
HGNCHGNC:10540. SAT1.
MIM308800. phenotype.
313020. gene.
Orphanet2340. Keratosis follicularis spinulosa decalvans.
PharmGKBPA128395782.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP21673.
OMAP21673. SDYRGMV.

Enzyme and pathway databases

BRENDA2.3.1.57. 247.
ReactomeREACT_13. Metabolism of amino acids.

Gene expression databases

ArrayExpressP21673.
BgeeP21673.
CleanExHS_SAT1.
GermOnlineENSG00000130066. Homo sapiens.

Family and domain databases

InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GCN5-rel_AcTrfase.
[Graphical view]
Gene3DG3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00127. Spermine.
NextBio24471.
SOURCESearch...

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Entry information

Entry nameSAT1_HUMAN
AccessionPrimary (citable) accession number: P21673
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: June 16, 2009
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents