Version 5.4
Mus musculus Protein: Sat2
Summary
InnateDB Protein IDBP-191217.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Sat2
Protein Name spermidine/spermine N1-acetyl transferase 2
Synonyms 2610016A03Rik; SSAT-2; SSAT2;
Species Mus musculus
Ensembl Protein ENSMUSP00000090647
InnateDB Gene IDBG-191215 (Sat2)
Protein Structure
UniProt Annotation
Function Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine > spermidine = spermine >> N(1)acetylspermine = putrescine (By similarity). {ECO:0000250}.
Subcellular Localization Cytoplasm {ECO:0000250}. Note=Intracellular organelles. {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 6 interaction(s) predicted by orthology.
Predicted by orthology
Total 6 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004145 diamine N-acetyltransferase activity
GO:0008080 N-acetyltransferase activity
Biological Process
GO:0008215 spermine metabolic process
GO:0008216 spermidine metabolic process
GO:0009447 putrescine catabolic process
Cellular Component
GO:0005737 cytoplasm
Protein Structure and Domains
PDB ID MGI:1916465
InterPro IPR000182 GNAT domain
IPR016181 Acyl-CoA N-acyltransferase
PFAM PF00583
PF13302
PF13508
PF13673
PF13718
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q6P8J2
PhosphoSite PhosphoSite-Q6P8J2
TrEMBL
UniProt Splice Variant
Entrez Gene 69215
UniGene Mm.340410
RefSeq XP_006534173
MGI ID
MGI Symbol Sat2
OMIM
CCDS CCDS36194
HPRD
IMGT
EMBL AL603707 AL731687 BC061227
GenPept AAH61227 CAI51952

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca