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P19623 (SPEE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Spermidine synthase
Short name=SPDSY
EC=2.5.1.16
Alternative name(s):
Putrescine aminopropyltransferase
Gene names
Name:SRM
Synonyms:SPS1, SRML1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.8

Catalytic activity

S-adenosylmethioninamine + putrescine = 5'-S-methyl-5'-thioadenosine + spermidine. Ref.8

Enzyme regulation

The activity is thought to be regulated mainly by the availability of decarboxylated S-adenosylmethionine.

Pathway

Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.

Subunit structure

Homodimer or homotetramer. Ref.8

Sequence similarities

Belongs to the spermidine/spermine synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=20 µM for putrescine Ref.8

KM=0.9 µM for S-adenosylmethioninamine

Ontologies

Keywords
   Biological processSpermidine biosynthesis
   Coding sequence diversityPolymorphism
   Molecular functionTransferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processspermidine biosynthetic process

Inferred from direct assay Ref.8. Source: UniProtKB

   Cellular componentcytosol

Traceable author statement. Source: Reactome

   Molecular functionprotein homodimerization activity

Inferred from direct assay Ref.8. Source: UniProtKB

spermidine synthase activity

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302Spermidine synthase
PRO_0000156445

Regions

Region155 – 1562S-adenosylmethioninamine binding
Region173 – 1764Putrescine binding

Sites

Active site1731Proton acceptor Probable
Binding site491S-adenosylmethioninamine
Binding site791Putrescine
Binding site801S-adenosylmethioninamine
Binding site1041S-adenosylmethioninamine
Binding site1241S-adenosylmethioninamine
Binding site1731S-adenosylmethioninamine
Binding site2411Putrescine

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6

Natural variations

Natural variant1491L → V.
Corresponds to variant rs1049932 [ dbSNP | Ensembl ].
VAR_011807

Experimental info

Sequence conflict2101Q → E in AAA36633. Ref.1

Secondary structure

1 ..................................................... 302
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19623 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 3EF454D886F6425D

FASTA30233,825
        10         20         30         40         50         60 
MEPGPDGPAA SGPAAIREGW FRETCSLWPG QALSLQVEQL LHHRRSRYQD ILVFRSKTYG 

        70         80         90        100        110        120 
NVLVLDGVIQ CTERDEFSYQ EMIANLPLCS HPNPRKVLII GGGDGGVLRE VVKHPSVESV 

       130        140        150        160        170        180 
VQCEIDEDVI QVSKKFLPGM AIGYSSSKLT LHVGDGFEFM KQNQDAFDVI ITDSSDPMGP 

       190        200        210        220        230        240 
AESLFKESYY QLMKTALKED GVLCCQGECQ WLHLDLIKEM RQFCQSLFPV VAYAYCTIPT 

       250        260        270        280        290        300 
YPSGQIGFML CSKNPSTNFQ EPVQPLTQQQ VAQMQLKYYN SDVHRAAFVL PEFARKALND 


VS

« Hide

References

« Hide 'large scale' references
[1]"Human spermidine synthase: cloning and primary structure."
Wahlfors J., Alhonen L., Kauppinen L., Hyvoenen T., Jaenne J., Eloranta T.
DNA Cell Biol. 9:103-110(1990) [PubMed: 2344393] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human spermidine synthase gene: structure and chromosomal localization."
Myoehaenen S., Kauppinen L., Wahlfors J., Alhonen L., Jaenne J.
DNA Cell Biol. 10:467-474(1991) [PubMed: 2069720] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Skin.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Structure and mechanism of spermidine synthases."
Wu H., Min J., Ikeguchi Y., Zeng H., Dong A., Loppnau P., Pegg A.E., Plotnikov A.N.
Biochemistry 46:8331-8339(2007) [PubMed: 17585781] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEXES WITH SPERMIDINE; PUTRESCINE; MTA AND S-ADENOSYLMETHIONINAMINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M34338 mRNA. Translation: AAA36633.1.
M64231 Genomic DNA. Translation: AAA60574.1.
AL109811 Genomic DNA. Translation: CAI22104.1.
CH471130 Genomic DNA. Translation: EAW71675.1.
BC000309 mRNA. Translation: AAH00309.1.
BC033106 mRNA. Translation: AAH33106.1.
IPIIPI00292020.
PIRA32610.
RefSeqNP_003123.2. NM_003132.2.
UniGeneHs.76244.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2O05X-ray2.00A/B1-302[»]
2O06X-ray2.00A/B1-302[»]
2O07X-ray1.89A/B1-302[»]
2O0LX-ray1.99A/B1-302[»]
3RW9X-ray2.00A/B1-302[»]
ProteinModelPortalP19623.
SMRP19623. Positions 15-299.
ModBaseSearch...

Protein-protein interaction databases

IntActP19623. 5 interactions.
STRINGP19623.

Polymorphism databases

DMDM134811.

Proteomic databases

PeptideAtlasP19623.
PRIDEP19623.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376957; ENSP00000366156; ENSG00000116649.
GeneID6723.
KEGGhsa:6723.
UCSCuc001arz.1. human.

Organism-specific databases

CTD6723.
GeneCardsGC01M011114.
H-InvDBHIX0199940.
HGNCHGNC:11296. SRM.
HPAHPA015746.
HPA029528.
MIM182891. gene.
neXtProtNX_P19623.
PharmGKBPA36120.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG04267.
GeneTreeENSGT00530000063329.
HOGENOMHBG635113.
HOVERGENHBG000834.
InParanoidP19623.
OMAELWYTEK.
OrthoDBEOG4H9XM0.
PhylomeDBP19623.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11578.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP19623.
BgeeP19623.
CleanExHS_SRM.
GenevestigatorP19623.
GermOnlineENSG00000116649. Homo sapiens.

Family and domain databases

InterProIPR001045. Sprmine_synthase.
[Graphical view]
KOK00797.
PANTHERPTHR11558. Sprmine_synthase. 1 hit.
PfamPF01564. Spermine_synth. 1 hit.
[Graphical view]
TIGRFAMsTIGR00417. SpeE. 1 hit.
PROSITEPS01330. SPERMIDINE_SYNTHASE_1. 1 hit.
PS51006. SPERMIDINE_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00118. S-Adenosylmethionine.
DB00127. Spermine.
NextBio26226.
SOURCESearch...

Entry information

Entry nameSPEE_HUMAN
AccessionPrimary (citable) accession number: P19623
Secondary accession number(s): B1AKP9, Q15511
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: January 25, 2012
This is version 126 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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents