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P52788

- SPSY_HUMAN

UniProt

P52788 - SPSY_HUMAN

Protein

Spermine synthase

Gene

SMS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Pathwayi

    Sites

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

    GO - Molecular functioni

    1. spermidine synthase activity Source: ProtInc
    2. spermine synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. methionine metabolic process Source: ProtInc
    3. polyamine metabolic process Source: Reactome
    4. small molecule metabolic process Source: Reactome
    5. spermine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Polyamine biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02362-MONOMER.
    ReactomeiREACT_14820. Metabolism of polyamines.
    SABIO-RKP52788.
    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:11123. SMS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Involvement in diseasei

    X-linked syndromic mental retardation Snyder-Robinson type (MRXSSR) [MIM:309583]: Characterized by moderate intellectual deficit, hypotonia, an unsteady gait, osteoporosis, kyphoscoliosis and facial asymmetry. Transmission is X-linked recessive.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi201 – 2011D → A or N: 100,000-fold decrease in catalytic efficiency. 1 Publication
    Mutagenesisi276 – 2761D → N: 200,000-fold decrease in catalytic efficiency. 1 Publication
    Mutagenesisi353 – 3531E → Q: 800-fold decrease in catalytic efficiency. 1 Publication

    Keywords - Diseasei

    Mental retardation

    Organism-specific databases

    MIMi309583. phenotype.
    Orphaneti3063. intellectual disability, X-linked, Snyder type.
    PharmGKBiPA35972.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 366365Spermine synthasePRO_0000156538Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP52788.
    PaxDbiP52788.
    PRIDEiP52788.

    2D gel databases

    OGPiP52788.

    PTM databases

    PhosphoSiteiP52788.

    Expressioni

    Gene expression databases

    BgeeiP52788.
    CleanExiHS_SMS.
    GenevestigatoriP52788.

    Organism-specific databases

    HPAiHPA029849.
    HPA029852.

    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.1 Publication

    Protein-protein interaction databases

    BioGridi112495. 29 interactions.
    IntActiP52788. 6 interactions.
    MINTiMINT-5002620.
    STRINGi9606.ENSP00000385746.

    Structurei

    Secondary structure

    1
    366
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 128
    Helixi21 – 3212
    Beta strandi36 – 427
    Turni43 – 453
    Beta strandi46 – 527
    Beta strandi58 – 636
    Beta strandi67 – 759
    Helixi85 – 9814
    Beta strandi114 – 1174
    Beta strandi136 – 1449
    Beta strandi149 – 1557
    Turni156 – 1583
    Beta strandi159 – 1646
    Beta strandi167 – 1715
    Helixi175 – 1817
    Turni182 – 1854
    Beta strandi193 – 1986
    Helixi203 – 2097
    Beta strandi214 – 2218
    Helixi223 – 23210
    Helixi234 – 2374
    Beta strandi242 – 2465
    Beta strandi249 – 2546
    Helixi256 – 26611
    Beta strandi270 – 2767
    Helixi291 – 30414
    Beta strandi306 – 31813
    Helixi322 – 33211
    Beta strandi335 – 3373
    Beta strandi339 – 3468
    Helixi349 – 3513
    Beta strandi355 – 3628

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3C6KX-ray1.95A/B/C/D5-366[»]
    3C6MX-ray2.45A/B/C/D5-366[»]
    ProteinModelPortaliP52788.
    SMRiP52788. Positions 3-365.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52788.

    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 binding

    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.

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG259013.
    HOGENOMiHOG000007053.
    HOVERGENiHBG004512.
    InParanoidiP52788.
    KOiK00802.
    OMAiEGRMFDY.
    OrthoDBiEOG7G1V6F.
    PhylomeDBiP52788.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P52788-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAARHSTLD FMLGAKADGE TILKGLQSIF QEQGMAESVH TWQDHGYLAT    50
    YTNKNGSFAN LRIYPHGLVL LDLQSYDGDA QGKEEIDSIL NKVEERMKEL 100
    SQDSTGRVKR LPPIVRGGAI DRYWPTADGR LVEYDIDEVV YDEDSPYQNI 150
    KILHSKQFGN ILILSGDVNL AESDLAYTRA IMGSGKEDYT GKDVLILGGG 200
    DGGILCEIVK LKPKMVTMVE IDQMVIDGCK KYMRKTCGDV LDNLKGDCYQ 250
    VLIEDCIPVL KRYAKEGREF DYVINDLTAV PISTSPEEDS TWEFLRLILD 300
    LSMKVLKQDG KYFTQGNCVN LTEALSLYEE QLGRLYCPVE FSKEIVCVPS 350
    YLELWVFYTV WKKAKP 366
    Length:366
    Mass (Da):41,268
    Last modified:May 30, 2000 - v2
    Checksum:iD5B23EF61DE66443
    GO
    Isoform 2 (identifier: P52788-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         57-109: Missing.

    Note: Gene prediction confirmed by EST data.

    Show »
    Length:313
    Mass (Da):35,278
    Checksum:i7D237FC4CD55D3E6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → MPG in CAA88921. (PubMed:7546290)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti60 – 601N → S.1 Publication
    VAR_071048

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei57 – 10953Missing in isoform 2. CuratedVSP_034406Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49099 mRNA. Translation: CAA88921.1.
    AD001528 mRNA. Translation: AAB61308.1.
    AK313834 mRNA. Translation: BAG36567.1.
    U53331 Genomic DNA. Translation: AAD08634.1.
    U73023 Genomic DNA. No translation available.
    CH471074 Genomic DNA. Translation: EAW98984.1.
    BC009898 mRNA. Translation: AAH09898.1.
    BC085621 mRNA. Translation: AAH85621.1.
    CCDSiCCDS14203.1. [P52788-1]
    CCDS59161.1. [P52788-2]
    PIRiS54160.
    RefSeqiNP_001245352.1. NM_001258423.1. [P52788-2]
    NP_004586.2. NM_004595.4. [P52788-1]
    UniGeneiHs.724874.

    Genome annotation databases

    EnsembliENST00000379404; ENSP00000368714; ENSG00000102172. [P52788-2]
    ENST00000404933; ENSP00000385746; ENSG00000102172. [P52788-1]
    GeneIDi6611.
    KEGGihsa:6611.
    UCSCiuc004dag.4. human. [P52788-1]
    uc031tgx.1. human. [P52788-2]

    Polymorphism databases

    DMDMi8247960.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49099 mRNA. Translation: CAA88921.1 .
    AD001528 mRNA. Translation: AAB61308.1 .
    AK313834 mRNA. Translation: BAG36567.1 .
    U53331 Genomic DNA. Translation: AAD08634.1 .
    U73023 Genomic DNA. No translation available.
    CH471074 Genomic DNA. Translation: EAW98984.1 .
    BC009898 mRNA. Translation: AAH09898.1 .
    BC085621 mRNA. Translation: AAH85621.1 .
    CCDSi CCDS14203.1. [P52788-1 ]
    CCDS59161.1. [P52788-2 ]
    PIRi S54160.
    RefSeqi NP_001245352.1. NM_001258423.1. [P52788-2 ]
    NP_004586.2. NM_004595.4. [P52788-1 ]
    UniGenei Hs.724874.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3C6K X-ray 1.95 A/B/C/D 5-366 [» ]
    3C6M X-ray 2.45 A/B/C/D 5-366 [» ]
    ProteinModelPortali P52788.
    SMRi P52788. Positions 3-365.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112495. 29 interactions.
    IntActi P52788. 6 interactions.
    MINTi MINT-5002620.
    STRINGi 9606.ENSP00000385746.

    Chemistry

    BindingDBi P52788.
    ChEMBLi CHEMBL4934.
    DrugBanki DB00127. Spermine.

    PTM databases

    PhosphoSitei P52788.

    Polymorphism databases

    DMDMi 8247960.

    2D gel databases

    OGPi P52788.

    Proteomic databases

    MaxQBi P52788.
    PaxDbi P52788.
    PRIDEi P52788.

    Protocols and materials databases

    DNASUi 6611.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379404 ; ENSP00000368714 ; ENSG00000102172 . [P52788-2 ]
    ENST00000404933 ; ENSP00000385746 ; ENSG00000102172 . [P52788-1 ]
    GeneIDi 6611.
    KEGGi hsa:6611.
    UCSCi uc004dag.4. human. [P52788-1 ]
    uc031tgx.1. human. [P52788-2 ]

    Organism-specific databases

    CTDi 6611.
    GeneCardsi GC0XP021958.
    GeneReviewsi SMS.
    HGNCi HGNC:11123. SMS.
    HPAi HPA029849.
    HPA029852.
    MIMi 300105. gene.
    309583. phenotype.
    neXtProti NX_P52788.
    Orphaneti 3063. intellectual disability, X-linked, Snyder type.
    PharmGKBi PA35972.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG259013.
    HOGENOMi HOG000007053.
    HOVERGENi HBG004512.
    InParanoidi P52788.
    KOi K00802.
    OMAi EGRMFDY.
    OrthoDBi EOG7G1V6F.
    PhylomeDBi P52788.
    TreeFami TF324508.

    Enzyme and pathway databases

    UniPathwayi UPA00249 ; UER00315 .
    BioCyci MetaCyc:HS02362-MONOMER.
    Reactomei REACT_14820. Metabolism of polyamines.
    SABIO-RK P52788.

    Miscellaneous databases

    EvolutionaryTracei P52788.
    GeneWikii SMS_(gene).
    GenomeRNAii 6611.
    NextBioi 25739.
    PROi P52788.
    SOURCEi Search...

    Gene expression databases

    Bgeei P52788.
    CleanExi HS_SMS.
    Genevestigatori P52788.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Sequence analysis of 139 kb in Xp22.1 containing spermine synthase and the 5' region of PEX."
      Grieff M., Whyte M.P., Thakker R.V., Mazzarella R.
      Genomics 44:227-231(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Colon.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Kidney and Skin.
    7. Eloranta T., Kajander O., Kauppinen L., Hyvoenen T., Linnala-Kankkunen A., Kalkkinen N., Kulomaa M., Alhonen L., Jaenne J.
      (In) Goldemberg S.H., Algranati I.D. (eds.); Proceedings of the international symposium on the biology and chemistry of polyamines, pp.91-98, ICSU Press, New York (1988)
      Cited for: PARTIAL PROTEIN SEQUENCE.
    8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 97-107 (ISOFORM 1).
      Tissue: Platelet.
    9. Cited for: INVOLVEMENT IN MRXSSR.
    10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism."
      Wu H., Min J., Zeng H., McCloskey D.E., Ikeguchi Y., Loppnau P., Michael A.J., Pegg A.E., Plotnikov A.N.
      J. Biol. Chem. 283:16135-16146(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 5-366 (ISOFORM 1) IN COMPLEX WITH SPERMIDINE AND 5-METHYLTHIOADENOSINE, SUBUNIT, MUTAGENESIS OF ASP-201; ASP-276 AND GLU-353.
    14. "De novo loss-of-function mutations in SETD5, encoding a methyltransferase in a 3p25 microdeletion syndrome critical region, cause intellectual disability."
      UK10K Consortium
      Grozeva D., Carss K., Spasic-Boskovic O., Parker M.J., Archer H., Firth H.V., Park S.M., Canham N., Holder S.E., Wilson M., Hackett A., Field M., Floyd J.A., Hurles M., Raymond F.L.
      Am. J. Hum. Genet. 94:618-624(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SER-60.

    Entry informationi

    Entry nameiSPSY_HUMAN
    AccessioniPrimary (citable) accession number: P52788
    Secondary accession number(s): A6NHA7
    , A6NI34, B2R9M0, O00544, Q9UQS1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3