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P21673 (SAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SAT1
Synonyms:SAT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length171 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. 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 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

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.
Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12

Sequence similarities

Belongs to the acetyltransferase family.

Contains 1 N-acetyltransferase domain.

Biophysicochemical properties

Kinetic parameters:

KM=3.8 µM for acetyl-coenzyme A Ref.9

KM=5.7 µM for spermine

KM=22 µM for spermidine

pH dependence:

Optimum pH is 8.0.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HOXB9P174823EBI-711613,EBI-745290
TCF25Q9BQ704EBI-711613,EBI-745182

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

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P21673 [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

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] [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; 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 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJH0783.
RefSeqNP_002961.1. NM_002970.2.
UniGeneHs.28491.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP21673.
SMRP21673. Positions 3-171.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112210. 62 interactions.
IntActP21673. 58 interactions.
MINTMINT-1369180.
STRING9606.ENSP00000368572.

Chemistry

BindingDBP21673.
ChEMBLCHEMBL4286.
DrugBankDB00127. Spermine.

PTM databases

PhosphoSiteP21673.

Polymorphism databases

DMDM114322.

Proteomic databases

PaxDbP21673.
PRIDEP21673.

Protocols and materials databases

DNASU6303.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379270; ENSP00000368572; ENSG00000130066.
GeneID6303.
KEGGhsa:6303.
UCSCuc004dau.3. human.

Organism-specific databases

CTD6303.
GeneCardsGC0XP023807.
H-InvDBHIX0176797.
HGNCHGNC:10540. SAT1.
HPACAB047343.
MIM308800. phenotype.
313020. gene.
neXtProtNX_P21673.
Orphanet2340. Keratosis follicularis spinulosa decalvans.
PharmGKBPA162402389.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0454.
HOGENOMHOG000078521.
HOVERGENHBG063175.
KOK00657.
OMAFYESVGA.
PhylomeDBP21673.
TreeFamTF319736.

Enzyme and pathway databases

BioCycMetaCyc:HS05339-MONOMER.
BRENDA2.3.1.57. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00188; UER00363.

Gene expression databases

ArrayExpressP21673.
BgeeP21673.
CleanExHS_SAT1.
GenevestigatorP21673.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSAT1. human.
EvolutionaryTraceP21673.
GeneWikiSAT1_(gene).
GenomeRNAi6303.
NextBio24471.
PROP21673.
SOURCESearch...

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: April 16, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome X

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