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P97355

- SPSY_MOUSE

UniProt

P97355 - SPSY_MOUSE

Protein

Spermine synthase

Gene

Sms

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM) By similarity. Required for normal viability, growth and fertility.By similarity1 Publication

    Catalytic activityi

    S-adenosyl 3-(methylthio)propylamine + spermidine = S-methyl-5'-thioadenosine + spermine.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei148 – 1481S-adenosylmethioninamineBy similarity
    Binding sitei177 – 1771SpermidineBy similarity
    Binding sitei201 – 2011SpermidineBy similarity
    Binding sitei220 – 2201S-adenosylmethioninamineBy similarity
    Active sitei276 – 2761Proton acceptorPROSITE-ProRule annotation
    Binding sitei351 – 3511SpermidineBy similarity
    Binding sitei353 – 3531SpermidineBy similarity

    GO - Molecular functioni

    1. spermine synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. spermine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Polyamine biosynthesis

    Enzyme and pathway databases

    UniPathwayiUPA00249; UER00315.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Spermine synthase (EC:2.5.1.22)
    Short name:
    SPMSY
    Alternative name(s):
    Spermidine aminopropyltransferase
    Gene namesi
    Name:Sms
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:109490. Sms.

    Pathology & Biotechi

    Disruption phenotypei

    Mouse ES cells lacking Sms display normal growth rates but are sensitive to antiproliferative and DNA damage-inducing drugs.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 366365Spermine synthasePRO_0000156539Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP97355.
    PaxDbiP97355.
    PRIDEiP97355.

    PTM databases

    PhosphoSiteiP97355.

    Expressioni

    Gene expression databases

    ArrayExpressiP97355.
    BgeeiP97355.
    CleanExiMM_SMS.
    GenevestigatoriP97355.

    Interactioni

    Subunit structurei

    Homodimer. Dimerization is mediated through the N-terminal domain and seems to be required for activity as deletion of the N-terminal domain causes complete loss of activity By similarity.By similarity

    Protein-protein interaction databases

    IntActiP97355. 1 interaction.
    MINTiMINT-4135428.

    Structurei

    3D structure databases

    ProteinModelPortaliP97355.
    SMRiP97355. Positions 3-366.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini122 – 362241PABSPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni255 – 2562S-adenosylmethioninamine bindingBy similarity

    Domaini

    Composed of 3 domains: the N-terminal domain has structural similarity to S-adenosylmethionine decarboxylase, the central domain is made up of four beta strands and the C-terminal domain is similar in structure to spermidine synthase. The N- and C-terminal domains are both required for activity By similarity.By similarity

    Sequence similaritiesi

    Contains 1 PABS (polyamine biosynthesis) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG259013.
    GeneTreeiENSGT00620000088036.
    HOVERGENiHBG004512.
    InParanoidiP97355.
    KOiK00802.
    OMAiEGRMFDY.
    OrthoDBiEOG7G1V6F.
    PhylomeDBiP97355.
    TreeFamiTF324508.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR029063. SAM-dependent_MTases-like.
    IPR001045. Spermidine/spermine_synthase.
    IPR015576. Spermine_synthase_animal.
    [Graphical view]
    PANTHERiPTHR11558. PTHR11558. 1 hit.
    PTHR11558:SF27. PTHR11558:SF27. 1 hit.
    PfamiPF01564. Spermine_synth. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS01330. PABS_1. 1 hit.
    PS51006. PABS_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P97355-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAARHSTLD FKLGAKADGE AILKGLQSIF QEQGMTESVH TWQDHGYLAT    50
    YTNKNGSFAN LRIYPHGLVL LDLQSYDSDV QGKQETDSLL NKIEEKMKEL 100
    SQDSTGRVKR LPPIVRGGAI DRYWPTADGR LVEYDIDEVV YDEDSPYQNI 150
    KILHSKQFGN ILILSGDVNL AESDLAYTRA IMGSGKEDYT GKDVLILGGG 200
    DGGILCEIVK LKPKMVTMVE IDQMVIDGCK KYMRRTCGDV LDNLRGDCYQ 250
    VLIEDCIPVL KMYAKEGREF DYVINDLTAV PISTSPEEDS TWDFLRLILD 300
    LSMKVLKQDG KYFTQGNCVN LTEALSLYEE QLGRLYCPVE FSKEIVCVPS 350
    YLELWVFYTV WKKAKP 366
    Length:366
    Mass (Da):41,313
    Last modified:May 1, 1997 - v1
    Checksum:iD549F319F51C43C5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti188 – 1881D → H in BAC33920. (PubMed:16141072)Curated
    Sequence conflicti245 – 2451R → K in BAC33920. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09419 mRNA. Translation: CAA70573.1.
    AF031486 mRNA. Translation: AAB86631.1.
    AK049787 mRNA. Translation: BAC33920.1.
    AK011542 mRNA. Translation: BAB27685.1.
    AK017775 mRNA. Translation: BAB30923.1.
    AK149929 mRNA. Translation: BAE29173.1.
    AK160637 mRNA. Translation: BAE35931.1.
    AK160659 mRNA. Translation: BAE35947.1.
    AK166665 mRNA. Translation: BAE38927.1.
    AL663072 Genomic DNA. Translation: CAM18089.1.
    BC046623 mRNA. Translation: AAH46623.1.
    BC058688 mRNA. Translation: AAH58688.1.
    AF136179 Genomic DNA. Translation: AAD33057.1.
    AJ000093 Genomic DNA. Translation: CAA03919.1.
    AJ000087
    , AJ000088, AJ000089, AJ000090, AJ000091, AJ000092 Genomic DNA. Translation: CAA03918.1.
    CCDSiCCDS41189.1.
    RefSeqiNP_033240.3. NM_009214.3.
    XP_001473484.1. XM_001473434.4.
    XP_006544632.1. XM_006544569.1.
    UniGeneiMm.18652.

    Genome annotation databases

    EnsembliENSMUST00000112529; ENSMUSP00000108148; ENSMUSG00000071708.
    GeneIDi20603.
    671878.
    KEGGimmu:20603.
    mmu:671878.
    UCSCiuc009urz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09419 mRNA. Translation: CAA70573.1 .
    AF031486 mRNA. Translation: AAB86631.1 .
    AK049787 mRNA. Translation: BAC33920.1 .
    AK011542 mRNA. Translation: BAB27685.1 .
    AK017775 mRNA. Translation: BAB30923.1 .
    AK149929 mRNA. Translation: BAE29173.1 .
    AK160637 mRNA. Translation: BAE35931.1 .
    AK160659 mRNA. Translation: BAE35947.1 .
    AK166665 mRNA. Translation: BAE38927.1 .
    AL663072 Genomic DNA. Translation: CAM18089.1 .
    BC046623 mRNA. Translation: AAH46623.1 .
    BC058688 mRNA. Translation: AAH58688.1 .
    AF136179 Genomic DNA. Translation: AAD33057.1 .
    AJ000093 Genomic DNA. Translation: CAA03919.1 .
    AJ000087
    , AJ000088 , AJ000089 , AJ000090 , AJ000091 , AJ000092 Genomic DNA. Translation: CAA03918.1 .
    CCDSi CCDS41189.1.
    RefSeqi NP_033240.3. NM_009214.3.
    XP_001473484.1. XM_001473434.4.
    XP_006544632.1. XM_006544569.1.
    UniGenei Mm.18652.

    3D structure databases

    ProteinModelPortali P97355.
    SMRi P97355. Positions 3-366.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P97355. 1 interaction.
    MINTi MINT-4135428.

    PTM databases

    PhosphoSitei P97355.

    Proteomic databases

    MaxQBi P97355.
    PaxDbi P97355.
    PRIDEi P97355.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000112529 ; ENSMUSP00000108148 ; ENSMUSG00000071708 .
    GeneIDi 20603.
    671878.
    KEGGi mmu:20603.
    mmu:671878.
    UCSCi uc009urz.1. mouse.

    Organism-specific databases

    CTDi 6611.
    MGIi MGI:109490. Sms.

    Phylogenomic databases

    eggNOGi NOG259013.
    GeneTreei ENSGT00620000088036.
    HOVERGENi HBG004512.
    InParanoidi P97355.
    KOi K00802.
    OMAi EGRMFDY.
    OrthoDBi EOG7G1V6F.
    PhylomeDBi P97355.
    TreeFami TF324508.

    Enzyme and pathway databases

    UniPathwayi UPA00249 ; UER00315 .

    Miscellaneous databases

    NextBioi 298937.
    PROi P97355.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P97355.
    Bgeei P97355.
    CleanExi MM_SMS.
    Genevestigatori P97355.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR029063. SAM-dependent_MTases-like.
    IPR001045. Spermidine/spermine_synthase.
    IPR015576. Spermine_synthase_animal.
    [Graphical view ]
    PANTHERi PTHR11558. PTHR11558. 1 hit.
    PTHR11558:SF27. PTHR11558:SF27. 1 hit.
    Pfami PF01564. Spermine_synth. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS01330. PABS_1. 1 hit.
    PS51006. PABS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Pex gene deletions in Gy and Hyp mice provide mouse models for X-linked hypophosphatemia."
      Strom T.M., Francis F., Lorenz B., Boeddrich A., Econs M.J., Lehrach H., Meitinger T.
      Hum. Mol. Genet. 6:165-171(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Nucleotide sequence of mouse spermidine aminopropyltransferase cDNA."
      Niiranen K., Korhonen V., Janne J.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Diaphragm.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow macrophage, Embryo, Embryonic spinal cord and Morula.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain and Olfactory epithelium.
    6. "Spermine deficiency resulting from targeted disruption of the spermine synthase gene in embryonic stem cells leads to enhanced sensitivity to antiproliferative drugs."
      Korhonen V.-P., Niiranen K., Halmekyto M., Pietila M., Diegelman P., Parkkinen J.J., Eloranta T., Porter C.W., Alhonen L., Janne J.
      Mol. Pharmacol. 59:231-238(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-315.
      Strain: 129/SvJ.
    7. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 297-307, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    8. "Spermine deficiency in Gy mice caused by deletion of the spermine synthase gene."
      Lorenz B., Francis F., Gempel K., Boeddrich A., Josten M., Schmahl W., Schmidt J., Lehrach H., Meitinger T., Strom T.M.
      Hum. Mol. Genet. 7:541-547(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 316-366, DISRUPTION PHENOTYPE.
    9. "Spermine synthesis is required for normal viability, growth, and fertility in the mouse."
      Wang X., Ikeguchi Y., McCloskey D.E., Nelson P., Pegg A.E.
      J. Biol. Chem. 279:51370-51375(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiSPSY_MOUSE
    AccessioniPrimary (citable) accession number: P97355
    Secondary accession number(s): A2AC82
    , Q3TL65, Q3TUP0, Q3UDT8, Q8C7P4, Q9CT09, Q9R282
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3