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P21673

- SAT1_HUMAN

UniProt

P21673 - SAT1_HUMAN

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Protein

Diamine acetyltransferase 1

Gene

SAT1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

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. 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
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: Chromosome X

Organism-specific databases

HGNCiHGNC:10540. SAT1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. intracellular Source: LIFEdb
Complete GO annotation...

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

MaxQBiP21673.
PaxDbiP21673.
PRIDEiP21673.

PTM databases

PhosphoSiteiP21673.

Expressioni

Gene expression databases

BgeeiP21673.
CleanExiHS_SAT1.
ExpressionAtlasiP21673. baseline and differential.
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. 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.
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

        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.

Polymorphism databases

DMDMi114322.

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 .
CCDSi CCDS14207.1.
PIRi JH0783.
RefSeqi NP_002961.1. NM_002970.3.
UniGenei Hs.28491.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 59 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

MaxQBi P21673.
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 GC0XP023815.
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.
InParanoidi P21673.
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

Bgeei P21673.
CleanExi HS_SAT1.
ExpressionAtlasi P21673. baseline and differential.
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

« 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: November 26, 2014
This is version 150 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