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Protein

Spermine oxidase

Gene

SMOX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Flavoenzyme which catalyzes the oxidation of spermine to spermidine. Can also use N(1)-acetylspermine and spermidine as substrates, with different affinity depending on the isoform (isozyme) and on the experimental conditions. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs. May contribute to beta-alanine production via aldehyde dehydrogenase conversion of 3-amino-propanal.

Catalytic activityi

Spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Enzyme regulationi

Inhibited at more than 90% by SL-11144, SL-11150 and SL-11158, at concentrations less than 1 µM.

Kineticsi

Kcat is 27-fold higher with spermine than N1-acetylspermine as substrate for isoform 1 and isoform 6.

  1. KM=0.6 µM for spermine (isoform 1)3 Publications
  2. KM=0.5 µM for spermine (isoform 6)3 Publications
  3. KM=3.0 µM for N1-acetylspermine (Isoform 1 and isoform 6)3 Publications

    pH dependencei

    Optimum pH is 9.5 with spermine as substrate.3 Publications

    Pathwayi: spermine degradation

    This protein is involved in the pathway spermine degradation, which is part of Amine and polyamine degradation.
    View all proteins of this organism that are known to be involved in the pathway spermine degradation and in Amine and polyamine degradation.

    GO - Molecular functioni

    GO - Biological processi

    • oxidation-reduction process Source: GOC
    • polyamine biosynthetic process Source: Reactome
    • polyamine catabolic process Source: UniProtKB
    • spermine catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01609-MONOMER.
    BRENDAi1.5.3.16. 2681.
    ReactomeiR-HSA-141334. PAOs oxidise polyamines to amines.
    R-HSA-351200. Interconversion of polyamines.
    SABIO-RKQ9NWM0.
    UniPathwayiUPA00211.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Spermine oxidase (EC:1.5.3.16)
    Alternative name(s):
    Polyamine oxidase 1
    Short name:
    PAO-1
    Short name:
    PAOh1
    Gene namesi
    Name:SMOX
    Synonyms:C20orf16, SMO
    ORF Names:UNQ3039/PRO9854
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15862. SMOX.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • cytosol Source: Reactome
    • nucleus Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi320 – 3201C → R: No change in enzymatic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA25701.

    Chemistry

    ChEMBLiCHEMBL2176769.
    DrugBankiDB00127. Spermine.

    Polymorphism and mutation databases

    BioMutaiSMOX.
    DMDMi50401688.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 555555Spermine oxidasePRO_0000099877Add
    BLAST

    Proteomic databases

    MaxQBiQ9NWM0.
    PaxDbiQ9NWM0.
    PRIDEiQ9NWM0.

    PTM databases

    iPTMnetiQ9NWM0.
    PhosphoSiteiQ9NWM0.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed in human tumor cell lines. Isoform 4 is only found in an embryonal kidney cell line.1 Publication

    Inductioni

    By antitumor polyamine analogs.

    Gene expression databases

    BgeeiQ9NWM0.
    CleanExiHS_SMO.
    HS_SMOX.
    ExpressionAtlasiQ9NWM0. baseline and differential.
    GenevisibleiQ9NWM0. HS.

    Organism-specific databases

    HPAiHPA047117.

    Interactioni

    Protein-protein interaction databases

    BioGridi119994. 6 interactions.
    STRINGi9606.ENSP00000307252.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NWM0.
    SMRiQ9NWM0. Positions 18-547.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the flavin monoamine oxidase family.Curated

    Phylogenomic databases

    eggNOGiKOG0685. Eukaryota.
    ENOG410XQW0. LUCA.
    GeneTreeiENSGT00530000062888.
    HOVERGENiHBG053499.
    InParanoidiQ9NWM0.
    KOiK12259.
    OMAiQEFFRHG.
    OrthoDBiEOG751NFD.
    PhylomeDBiQ9NWM0.
    TreeFamiTF318348.

    Family and domain databases

    Gene3Di3.50.50.60. 1 hit.
    InterProiIPR002937. Amino_oxidase.
    IPR023753. FAD/NAD-binding_dom.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 2 hits.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 3 hits.

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

    Note: The resultant proteins have different biochemical characteristics and substrate specificity.

    Isoform 1 (identifier: Q9NWM0-1) [UniParc]FASTAAdd to basket

    Also known as: PAOh1, SMO

    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

            10         20         30         40         50
    MQSCESSGDS ADDPLSRGLR RRGQPRVVVI GAGLAGLAAA KALLEQGFTD
    60 70 80 90 100
    VTVLEASSHI GGRVQSVKLG HATFELGATW IHGSHGNPIY HLAEANGLLE
    110 120 130 140 150
    ETTDGERSVG RISLYSKNGV ACYLTNHGRR IPKDVVEEFS DLYNEVYNLT
    160 170 180 190 200
    QEFFRHDKPV NAESQNSVGV FTREEVRNRI RNDPDDPEAT KRLKLAMIQQ
    210 220 230 240 250
    YLKVESCESS SHSMDEVSLS AFGEWTEIPG AHHIIPSGFM RVVELLAEGI
    260 270 280 290 300
    PAHVIQLGKP VRCIHWDQAS ARPRGPEIEP RGEGDHNHDT GEGGQGGEEP
    310 320 330 340 350
    RGGRWDEDEQ WSVVVECEDC ELIPADHVIV TVSLGVLKRQ YTSFFRPGLP
    360 370 380 390 400
    TEKVAAIHRL GIGTTDKIFL EFEEPFWGPE CNSLQFVWED EAESHTLTYP
    410 420 430 440 450
    PELWYRKICG FDVLYPPERY GHVLSGWICG EEALVMEKCD DEAVAEICTE
    460 470 480 490 500
    MLRQFTGNPN IPKPRRILRS AWGSNPYFRG SYSYTQVGSS GADVEKLAKP
    510 520 530 540 550
    LPYTESSKTA PMQVLFSGEA THRKYYSTTH GALLSGQREA ARLIEMYRDL

    FQQGT
    Note: Low affinity for acetylated polyamine.
    Length:555
    Mass (Da):61,819
    Last modified:October 1, 2000 - v1
    Checksum:iBDBEA65ECE9F45BF
    GO
    Isoform 2 (identifier: Q9NWM0-2) [UniParc]FASTAAdd to basket

    Also known as: PAOh2

    The sequence of this isoform differs from the canonical sequence as follows:
         282-334: Missing.

    Note: Low affinity for acetylated polyamine.
    Show »
    Length:502
    Mass (Da):56,091
    Checksum:i45921536D1B92403
    GO
    Isoform 3 (identifier: Q9NWM0-3) [UniParc]FASTAAdd to basket

    Also known as: PAOh3

    The sequence of this isoform differs from the canonical sequence as follows:
         146-510: Missing.

    Note: Major isoform. Has the highest affinity for the 3 substrates. Has a greater affinity for spermidine and spermine than for N(1)-acetylspermine.
    Show »
    Length:190
    Mass (Da):20,630
    Checksum:iC6A51E1B71E3A56A
    GO
    Isoform 4 (identifier: Q9NWM0-4) [UniParc]FASTAAdd to basket

    Also known as: PAOh4

    The sequence of this isoform differs from the canonical sequence as follows:
         282-334: Missing.
         510-510: A → AHGSSTKQQPGHLFSSKCPEQPLDANRGAVK

    Note: Has the lowest Km values for the different substrates and has the highest affinity for spermidine.
    Show »
    Length:532
    Mass (Da):59,279
    Checksum:iB9AE5FCB9B7762B3
    GO
    Isoform 5 (identifier: Q9NWM0-5) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-196: Missing.
         510-510: A → AHGSSTKQQPGHLFSSKCPEQPLDANRGAVK

    Note: Does not seem to display oxidase activity towards spermidine or N(1)-acetyl-spermine, but this has to be confirmed. No experimental confirmation available.
    Show »
    Length:389
    Mass (Da):43,553
    Checksum:iF8AF920F5B10EBA9
    GO
    Isoform 6 (identifier: Q9NWM0-6) [UniParc]FASTAAdd to basket

    Also known as: SMO5, SMOX5

    The sequence of this isoform differs from the canonical sequence as follows:
         510-510: A → AHGSSTKQQPGHLFSSKCPEQPLDANRGAVK

    Note: Substrate specificities and affinities comparable to those of isoform 1.
    Show »
    Length:585
    Mass (Da):65,007
    Checksum:i7B1744F671906B9B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161S → R in AAK55764 (PubMed:12398765).Curated
    Sequence conflicti60 – 601I → V in AAK55765 (PubMed:12398765).Curated
    Sequence conflicti156 – 1561H → Y in AAK55764 (PubMed:12398765).Curated
    Sequence conflicti290 – 2901T → A in BAB15288 (PubMed:14702039).Curated
    Sequence conflicti320 – 3201C → R in AAK55763 (PubMed:11454677).Curated
    Sequence conflicti320 – 3201C → R in ABM01872 (PubMed:18422650).Curated
    Sequence conflicti372 – 3721F → L in AAN77119 (PubMed:12398765).Curated
    Sequence conflicti431 – 4311E → G in AAN77119 (PubMed:12398765).Curated
    Sequence conflicti431 – 4311E → G in ABM01872 (PubMed:18422650).Curated
    Sequence conflicti504 – 5041T → A in AAK55764 (PubMed:12398765).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti301 – 3011R → P.
    Corresponds to variant rs6084654 [ dbSNP | Ensembl ].
    VAR_059114
    Natural varianti340 – 3401Q → K in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036546
    Natural varianti522 – 5221H → Y.1 Publication
    VAR_019531

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 196196Missing in isoform 5. 1 PublicationVSP_011123Add
    BLAST
    Alternative sequencei146 – 510365Missing in isoform 3. 1 PublicationVSP_011124Add
    BLAST
    Alternative sequencei282 – 33453Missing in isoform 2 and isoform 4. 2 PublicationsVSP_011125Add
    BLAST
    Alternative sequencei510 – 5101A → AHGSSTKQQPGHLFSSKCPE QPLDANRGAVK in isoform 4, isoform 5 and isoform 6. 3 PublicationsVSP_011126

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY033889 mRNA. Translation: AAK55763.1.
    AY033890 mRNA. Translation: AAK55764.1.
    AY033891 mRNA. Translation: AAK55765.1.
    AF519179 mRNA. Translation: AAN77119.1.
    EF032141 mRNA. Translation: ABM01872.1.
    AY358104 mRNA. Translation: AAQ88471.1.
    AK000753 mRNA. Translation: BAA91360.1.
    AK025938 mRNA. Translation: BAB15288.1.
    AL121675 Genomic DNA. Translation: CAI22747.1.
    AL121675 Genomic DNA. Translation: CAI22748.1.
    AL121675 Genomic DNA. Translation: CAM28308.1.
    AL121675 Genomic DNA. Translation: CAM28309.1.
    CH471133 Genomic DNA. Translation: EAX10460.1.
    CH471133 Genomic DNA. Translation: EAX10461.1.
    CH471133 Genomic DNA. Translation: EAX10457.1.
    CH471133 Genomic DNA. Translation: EAX10458.1.
    CH471133 Genomic DNA. Translation: EAX10459.1.
    CH471133 Genomic DNA. Translation: EAX10462.1.
    BC000669 mRNA. Translation: AAH00669.1.
    AL162058 mRNA. Translation: CAB82396.1.
    CCDSiCCDS13075.1. [Q9NWM0-1]
    CCDS13076.1. [Q9NWM0-2]
    CCDS13077.1. [Q9NWM0-3]
    CCDS13078.1. [Q9NWM0-4]
    CCDS74702.1. [Q9NWM0-6]
    PIRiT47142.
    RefSeqiNP_001257620.1. NM_001270691.1. [Q9NWM0-6]
    NP_787033.1. NM_175839.2. [Q9NWM0-1]
    NP_787034.1. NM_175840.2. [Q9NWM0-2]
    NP_787035.1. NM_175841.2. [Q9NWM0-3]
    NP_787036.1. NM_175842.2. [Q9NWM0-4]
    XP_011527563.1. XM_011529261.1. [Q9NWM0-6]
    UniGeneiHs.433337.

    Genome annotation databases

    EnsembliENST00000278795; ENSP00000278795; ENSG00000088826. [Q9NWM0-4]
    ENST00000305958; ENSP00000307252; ENSG00000088826. [Q9NWM0-1]
    ENST00000339123; ENSP00000344595; ENSG00000088826. [Q9NWM0-2]
    ENST00000346595; ENSP00000341775; ENSG00000088826. [Q9NWM0-3]
    ENST00000379460; ENSP00000368773; ENSG00000088826. [Q9NWM0-1]
    ENST00000621355; ENSP00000478305; ENSG00000088826. [Q9NWM0-6]
    GeneIDi54498.
    KEGGihsa:54498.
    UCSCiuc002wkk.2. human. [Q9NWM0-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY033889 mRNA. Translation: AAK55763.1.
    AY033890 mRNA. Translation: AAK55764.1.
    AY033891 mRNA. Translation: AAK55765.1.
    AF519179 mRNA. Translation: AAN77119.1.
    EF032141 mRNA. Translation: ABM01872.1.
    AY358104 mRNA. Translation: AAQ88471.1.
    AK000753 mRNA. Translation: BAA91360.1.
    AK025938 mRNA. Translation: BAB15288.1.
    AL121675 Genomic DNA. Translation: CAI22747.1.
    AL121675 Genomic DNA. Translation: CAI22748.1.
    AL121675 Genomic DNA. Translation: CAM28308.1.
    AL121675 Genomic DNA. Translation: CAM28309.1.
    CH471133 Genomic DNA. Translation: EAX10460.1.
    CH471133 Genomic DNA. Translation: EAX10461.1.
    CH471133 Genomic DNA. Translation: EAX10457.1.
    CH471133 Genomic DNA. Translation: EAX10458.1.
    CH471133 Genomic DNA. Translation: EAX10459.1.
    CH471133 Genomic DNA. Translation: EAX10462.1.
    BC000669 mRNA. Translation: AAH00669.1.
    AL162058 mRNA. Translation: CAB82396.1.
    CCDSiCCDS13075.1. [Q9NWM0-1]
    CCDS13076.1. [Q9NWM0-2]
    CCDS13077.1. [Q9NWM0-3]
    CCDS13078.1. [Q9NWM0-4]
    CCDS74702.1. [Q9NWM0-6]
    PIRiT47142.
    RefSeqiNP_001257620.1. NM_001270691.1. [Q9NWM0-6]
    NP_787033.1. NM_175839.2. [Q9NWM0-1]
    NP_787034.1. NM_175840.2. [Q9NWM0-2]
    NP_787035.1. NM_175841.2. [Q9NWM0-3]
    NP_787036.1. NM_175842.2. [Q9NWM0-4]
    XP_011527563.1. XM_011529261.1. [Q9NWM0-6]
    UniGeneiHs.433337.

    3D structure databases

    ProteinModelPortaliQ9NWM0.
    SMRiQ9NWM0. Positions 18-547.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi119994. 6 interactions.
    STRINGi9606.ENSP00000307252.

    Chemistry

    ChEMBLiCHEMBL2176769.
    DrugBankiDB00127. Spermine.

    PTM databases

    iPTMnetiQ9NWM0.
    PhosphoSiteiQ9NWM0.

    Polymorphism and mutation databases

    BioMutaiSMOX.
    DMDMi50401688.

    Proteomic databases

    MaxQBiQ9NWM0.
    PaxDbiQ9NWM0.
    PRIDEiQ9NWM0.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000278795; ENSP00000278795; ENSG00000088826. [Q9NWM0-4]
    ENST00000305958; ENSP00000307252; ENSG00000088826. [Q9NWM0-1]
    ENST00000339123; ENSP00000344595; ENSG00000088826. [Q9NWM0-2]
    ENST00000346595; ENSP00000341775; ENSG00000088826. [Q9NWM0-3]
    ENST00000379460; ENSP00000368773; ENSG00000088826. [Q9NWM0-1]
    ENST00000621355; ENSP00000478305; ENSG00000088826. [Q9NWM0-6]
    GeneIDi54498.
    KEGGihsa:54498.
    UCSCiuc002wkk.2. human. [Q9NWM0-1]

    Organism-specific databases

    CTDi54498.
    GeneCardsiSMOX.
    HGNCiHGNC:15862. SMOX.
    HPAiHPA047117.
    MIMi615854. gene.
    neXtProtiNX_Q9NWM0.
    PharmGKBiPA25701.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0685. Eukaryota.
    ENOG410XQW0. LUCA.
    GeneTreeiENSGT00530000062888.
    HOVERGENiHBG053499.
    InParanoidiQ9NWM0.
    KOiK12259.
    OMAiQEFFRHG.
    OrthoDBiEOG751NFD.
    PhylomeDBiQ9NWM0.
    TreeFamiTF318348.

    Enzyme and pathway databases

    UniPathwayiUPA00211.
    BioCyciMetaCyc:HS01609-MONOMER.
    BRENDAi1.5.3.16. 2681.
    ReactomeiR-HSA-141334. PAOs oxidise polyamines to amines.
    R-HSA-351200. Interconversion of polyamines.
    SABIO-RKQ9NWM0.

    Miscellaneous databases

    ChiTaRSiSMOX. human.
    GeneWikiiSMOX.
    GenomeRNAii54498.
    PROiQ9NWM0.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9NWM0.
    CleanExiHS_SMO.
    HS_SMOX.
    ExpressionAtlasiQ9NWM0. baseline and differential.
    GenevisibleiQ9NWM0. HS.

    Family and domain databases

    Gene3Di3.50.50.60. 1 hit.
    InterProiIPR002937. Amino_oxidase.
    IPR023753. FAD/NAD-binding_dom.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 2 hits.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 3 hits.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure."
      Wang Y., Devereux W., Woster P.M., Murray-Stewart T., Hacker A., Casero R.A. Jr.
      Cancer Res. 61:5370-5373(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics."
      Murray-Stewart T., Wang Y., Devereux W., Casero R.A. Jr.
      Biochem. J. 368:673-677(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Lung carcinoma.
    3. "Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology."
      Murray-Stewart T., Wang Y., Goodwin A., Hacker A., Meeker A., Casero R.A. Jr.
      FEBS J. 275:2795-2806(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT TYR-522.
    5. "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] (ISOFORMS 1 AND 5).
      Tissue: Hepatoma and Kidney.
    6. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 2).
      Tissue: Kidney.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-555 (ISOFORM 1).
      Tissue: Amygdala.
    10. Cited for: CHARACTERIZATION (ISOFORM 1).
    11. "Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin."
      Vujcic S., Diegelman P., Bacchi C.J., Kramer D.L., Porter C.W.
      Biochem. J. 367:665-675(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-320.
    12. Cited for: REVIEW.
    13. Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-340.

    Entry informationi

    Entry nameiSMOX_HUMAN
    AccessioniPrimary (citable) accession number: Q9NWM0
    Secondary accession number(s): A2A2P5
    , A2A2P6, A8BE87, D3DVZ4, Q5TE26, Q5TE27, Q6UY28, Q8IX00, Q96LC3, Q96LC4, Q96QT3, Q9BW38, Q9H6H1, Q9NP51, Q9NPY1, Q9NPY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: October 1, 2000
    Last modified: June 8, 2016
    This is version 127 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.