Spermine synthase

Details

Name

Spermine synthase

Synonyms

• 2.5.1.22
• Spermidine aminopropyltransferase
• SPMSY

Gene Name

SMS

Organism

Humans

Amino acid sequence

>lcl|BSEQ0001919|Spermine synthase
MAAARHSTLDFMLGAKADGETILKGLQSIFQEQGMAESVHTWQDHGYLATYTNKNGSFAN
LRIYPHGLVLLDLQSYDGDAQGKEEIDSILNKVEERMKELSQDSTGRVKRLPPIVRGGAI
DRYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRA
IMGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRKTCGDV
LDNLKGDCYQVLIEDCIPVLKRYAKEGREFDYVINDLTAVPISTSPEEDSTWEFLRLILD
LSMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTV
WKKAKP

Number of residues

366

Molecular Weight

41267.855

Theoretical pI

4.62

GO Classification

Functions

spermine synthase activity

Processes

cellular nitrogen compound metabolic process / methionine metabolic process / polyamine metabolic process / small molecule metabolic process / spermine biosynthetic process

Components

cytosol / extracellular exosome

General Function

Spermine synthase activity

Specific Function

Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM).

Pfam Domain Function

• Spermine_synth (PF01564)

Transmembrane Regions

Not Available

Cellular Location

Not Available

Gene sequence

>lcl|BSEQ0010676|Spermine synthase (SMS)
ATGGCAGCAGCACGGCACAGCACGCTCGACTTCATGCTCGGCGCCAAAGCTGATGGTGAG
ACCATTCTAAAAGGCCTCCAGTCCATTTTCCAGGAGCAGGGGATGGCGGAGTCGGTGCAC
ACCTGGCAGGACCATGGCTATTTAGCAACCTACACAAACAAGAACGGCAGATTACCACCC
ATAGTGCGAGGAGGAGCCATCGACAGATACTGGCCCACCGCCGACGGGCGCCTGGTTGAA
TATGACATAGATGAAGTGGTATATGACGAAGATTCACCTTATCAAAATATAAAAATTCTA
CACTCGAAGCAGTTTGGAAATATTCTCATCCTTAGTGGGGATGTTAATTTGGCAGAGAGT
GATTTGGCATATACCCGGGCCATCATGGGCAGTGGCAAAGAAGATTACACTGGCAAAGAT
GTACTCATTCTGGGAGGTGGAGACGGAGGCATATTGTGTGAAATAGTCAAACTAAAACCA
AAGATGGTCACTATGGTAGAGATTGACCAAATGGTGATTGATGGGTGTAAGAAATACATG
CGAAAAACGTGTGGCGATGTCTTAGACAATCTTAAAGGAGACTGCTATCAGGTTCTAATA
GAAGACTGTATCCCGGTACTGAAGAGGTACGCCAAAGAAGGGAGAGAATTTGATTATGTG
ATTAATGATTTGACAGCTGTTCCAATCTCCACGTCTCCAGAAGAAGATTCCACATGGGAG
TTTCTCAGACTGATTCTTGACCTCTCAATGAAAGTGTTGAAACAGGATGGGAAATATTTT
ACACAGGGGAACTGTGTCAATCTGACAGAAGCACTGTCGCTCTATGAAGAACAGCTGGGG
CGCCTGTATTGTCCTGTGGAATTTTCAAAGGAGATCGTCTGTGTCCCTTCATACTTGGAA
TTGTGGGTATTTTACACTGTTTGGAAGAAAGCTAAACCCTGA

Chromosome Location

X

Locus

Xp22.1

External Identifiers

Resource	Link
UniProtKB ID	P52788
UniProtKB Entry Name	SPSY_HUMAN
GenBank Protein ID	791051
GenBank Gene ID	Z49099
GenAtlas ID	SMS
HGNC ID	HGNC:11123

General References

1. Korhonen VP, Halmekyto M, Kauppinen L, Myohanen S, Wahlfors J, Keinanen T, Hyvonen T, Alhonen L, Eloranta T, Janne J: Molecular cloning of a cDNA encoding human spermine synthase. DNA Cell Biol. 1995 Oct;14(10):841-7. [Article]
2. Grieff M, Whyte MP, Thakker RV, Mazzarella R: Sequence analysis of 139 kb in Xp22.1 containing spermine synthase and the 5' region of PEX. Genomics. 1997 Sep 1;44(2):227-31. [Article]
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6. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [Article]
7. Cason AL, Ikeguchi Y, Skinner C, Wood TC, Holden KR, Lubs HA, Martinez F, Simensen RJ, Stevenson RE, Pegg AE, Schwartz CE: X-linked spermine synthase gene (SMS) defect: the first polyamine deficiency syndrome. Eur J Hum Genet. 2003 Dec;11(12):937-44. [Article]
8. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [Article]
9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
10. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
11. Wu H, Min J, Zeng H, McCloskey DE, Ikeguchi Y, Loppnau P, Michael AJ, Pegg AE, Plotnikov AN: Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. J Biol Chem. 2008 Jun 6;283(23):16135-46. doi: 10.1074/jbc.M710323200. Epub 2008 Mar 26. [Article]
12. Lemke JR, Riesch E, Scheurenbrand T, Schubach M, Wilhelm C, Steiner I, Hansen J, Courage C, Gallati S, Burki S, Strozzi S, Simonetti BG, Grunt S, Steinlin M, Alber M, Wolff M, Klopstock T, Prott EC, Lorenz R, Spaich C, Rona S, Lakshminarasimhan M, Kroll J, Dorn T, Kramer G, Synofzik M, Becker F, Weber YG, Lerche H, Bohm D, Biskup S: Targeted next generation sequencing as a diagnostic tool in epileptic disorders. Epilepsia. 2012 Aug;53(8):1387-98. doi: 10.1111/j.1528-1167.2012.03516.x. Epub 2012 May 21. [Article]
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Drug Relations

Drug Relations

DrugBank ID	Name	Drug group	Pharmacological action?	Actions	Details
DB00127	Spermine	experimental, nutraceutical	yes	ligand	Details