Version 5.4
Mus musculus Protein: Srm
Summary
InnateDB Protein IDBP-204693.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Srm
Protein Name spermidine synthase
Synonyms AA407669; SpdST; SpdSy;
Species Mus musculus
Ensembl Protein ENSMUSP00000006611
InnateDB Gene IDBG-204691 (Srm)
Protein Structure
UniProt Annotation
Function Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM). Has a strong preference for putrescine as substrate, and has very low activity towards 1,3-diaminopropane. Has extremely low activity towards spermidine (By similarity). {ECO:0000250}.
Subcellular Localization
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 10 interaction(s) predicted by orthology.
Predicted by orthology
Total 10 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003824 catalytic activity
GO:0004766 spermidine synthase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0008295 spermidine biosynthetic process
Cellular Component
Protein Structure and Domains
PDB ID MGI:102690
InterPro IPR001045 Spermidine/spermine synthases family
IPR029063 S-adenosyl-L-methionine-dependent methyltransferase-like
PFAM PF01564
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q64674
PhosphoSite PhosphoSite-Q64674
TrEMBL Q543H0
UniProt Splice Variant
Entrez Gene 20810
UniGene Mm.10
RefSeq NP_033298
MGI ID
MGI Symbol Srm
OMIM
CCDS CCDS18940
HPRD
IMGT
EMBL AK051101 BC005566 CH466594 L19311 Z67748
GenPept AAC37666 AAH05566 BAC34526 CAA91561 EDL14826

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