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O00391

- QSOX1_HUMAN

UniProt

O00391 - QSOX1_HUMAN

Protein

Sulfhydryl oxidase 1

Gene

QSOX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins. In fibroblasts, it may have tumor-suppressing capabilities being involved in growth regulation.6 Publications

    Catalytic activityi

    2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2.1 Publication

    Cofactori

    Binds 1 FAD per subunit.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei70 – 701Nucleophile1 Publication
    Active sitei73 – 731Nucleophile1 Publication
    Binding sitei401 – 4011FAD1 Publication
    Binding sitei408 – 4081FAD1 Publication
    Binding sitei412 – 4121FAD1 Publication
    Binding sitei451 – 4511FAD1 Publication
    Binding sitei455 – 4551FAD1 Publication
    Binding sitei500 – 5001FAD1 Publication
    Binding sitei503 – 5031FAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi478 – 4858FAD1 Publication

    GO - Molecular functioni

    1. flavin-linked sulfhydryl oxidase activity Source: UniProtKB
    2. protein disulfide isomerase activity Source: UniProtKB

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. protein folding Source: GOC

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BRENDAi1.8.3.2. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sulfhydryl oxidase 1 (EC:1.8.3.2)
    Short name:
    hQSOX
    Alternative name(s):
    Quiescin Q6
    Gene namesi
    Name:QSOX1
    Synonyms:QSCN6
    ORF Names:UNQ2520/PRO6013
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9756. QSOX1.

    Subcellular locationi

    Isoform 2 : Secretedextracellular space
    Note: Found in the extracellular medium of quiescent cells but is not found in proliferating cells.

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProtKB
    3. integral component of Golgi membrane Source: UniProtKB

    Keywords - Cellular componenti

    Golgi apparatus, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi70 – 701C → S: Reduces activity by 93%. 1 Publication
    Mutagenesisi73 – 731C → S: Reduces activity by 93%. 1 Publication
    Mutagenesisi449 – 4491C → S: Reduces activity by 96%. 1 Publication
    Mutagenesisi452 – 4521C → S: Loss of activity. 1 Publication
    Mutagenesisi509 – 5091C → S: No effect. Reduces activity by 70%; when associated with S-512. 1 Publication
    Mutagenesisi512 – 5121C → S: Reduces activity by 40%. Reduces activity by 70%; when associated with S-509. 1 Publication

    Organism-specific databases

    PharmGKBiPA162400559.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 747718Sulfhydryl oxidase 1PRO_0000249533Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi70 ↔ 73Redox-active1 Publication
    Glycosylationi130 – 1301N-linked (GlcNAc...) (complex)2 Publications
    Glycosylationi243 – 2431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi393 ↔ 4051 PublicationPROSITE-ProRule annotation
    Disulfide bondi449 ↔ 4521 PublicationPROSITE-ProRule annotation
    Disulfide bondi509 ↔ 5121 PublicationPROSITE-ProRule annotation
    Glycosylationi575 – 5751N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiO00391.
    PaxDbiO00391.
    PeptideAtlasiO00391.
    PRIDEiO00391.

    PTM databases

    PhosphoSiteiO00391.

    Expressioni

    Tissue specificityi

    Expressed in heart, placenta, lung, liver, skeletal muscle, pancreas and very weakly in brain and kidney.2 Publications

    Inductioni

    Induced in quiescent cells just as fibroblasts begin to leave the proliferative cycle and enter quiescence.3 Publications

    Gene expression databases

    ArrayExpressiO00391.
    BgeeiO00391.
    CleanExiHS_QSOX1.
    GenevestigatoriO00391.

    Organism-specific databases

    HPAiHPA042127.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    BioGridi111734. 4 interactions.
    IntActiO00391. 1 interaction.
    MINTiMINT-2862351.
    STRINGi9606.ENSP00000356574.

    Structurei

    Secondary structure

    1
    747
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 456
    Turni47 – 493
    Helixi50 – 545
    Beta strandi58 – 669
    Helixi71 – 8616
    Helixi88 – 903
    Turni91 – 933
    Beta strandi94 – 1007
    Turni104 – 1063
    Helixi107 – 1126
    Beta strandi117 – 1248
    Beta strandi130 – 1323
    Beta strandi134 – 1363
    Helixi143 – 15513
    Helixi173 – 1775
    Helixi179 – 1824
    Beta strandi186 – 1938
    Helixi199 – 2068
    Turni207 – 2093
    Beta strandi213 – 2197
    Helixi223 – 2297
    Beta strandi234 – 2418
    Beta strandi246 – 2483
    Beta strandi252 – 2554
    Helixi256 – 2649
    Beta strandi298 – 3003
    Helixi301 – 31313
    Helixi316 – 3183
    Beta strandi320 – 3234
    Helixi324 – 34017
    Helixi345 – 36016
    Beta strandi363 – 3675
    Helixi368 – 37710
    Helixi380 – 3834
    Beta strandi400 – 4023
    Helixi403 – 41917
    Helixi426 – 4316
    Helixi432 – 4343
    Helixi435 – 44612
    Helixi450 – 46314
    Helixi464 – 4663
    Helixi470 – 48819
    Beta strandi502 – 5043
    Turni506 – 5083
    Helixi510 – 5123
    Beta strandi517 – 5193
    Helixi524 – 53411
    Helixi537 – 5393

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LLIX-ray2.05A286-546[»]
    3LLKX-ray2.00A/B/C286-546[»]
    3Q6OX-ray2.05A33-272[»]
    4IJ3X-ray2.70A33-272[»]
    ProteinModelPortaliO00391.
    SMRiO00391. Positions 33-544.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00391.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei710 – 73021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 156121ThioredoxinPROSITE-ProRule annotationAdd
    BLAST
    Domaini396 – 503108ERV/ALR sulfhydryl oxidasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ERV/ALR sulfhydryl oxidase domain.PROSITE-ProRule annotation
    Contains 1 thioredoxin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0526.
    HOGENOMiHOG000231631.
    HOVERGENiHBG080360.
    InParanoidiO00391.
    KOiK10758.
    OMAiSHNRVNA.
    OrthoDBiEOG73RB9X.
    PhylomeDBiO00391.
    TreeFamiTF316749.

    Family and domain databases

    Gene3Di1.20.120.310. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR017905. ERV/ALR_sulphydryl_oxidase.
    IPR012336. Thioredoxin-like_fold.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PfamiPF04777. Evr1_Alr. 1 hit.
    PF00085. Thioredoxin. 1 hit.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 1 hit.
    SSF69000. SSF69000. 1 hit.
    PROSITEiPS51324. ERV_ALR. 1 hit.
    PS51352. THIOREDOXIN_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: O00391-1) [UniParc]FASTAAdd to Basket

    Also known as: a, QSOX-L

    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

    MRRCNSGSGP PPSLLLLLLW LLAVPGANAA PRSALYSPSD PLTLLQADTV    50
    RGAVLGSRSA WAVEFFASWC GHCIAFAPTW KALAEDVKAW RPALYLAALD 100
    CAEETNSAVC RDFNIPGFPT VRFFKAFTKN GSGAVFPVAG ADVQTLRERL 150
    IDALESHHDT WPPACPPLEP AKLEEIDGFF ARNNEEYLAL IFEKGGSYLG 200
    REVALDLSQH KGVAVRRVLN TEANVVRKFG VTDFPSCYLL FRNGSVSRVP 250
    VLMESRSFYT AYLQRLSGLT REAAQTTVAP TTANKIAPTV WKLADRSKIY 300
    MADLESALHY ILRIEVGRFP VLEGQRLVAL KKFVAVLAKY FPGRPLVQNF 350
    LHSVNEWLKR QKRNKIPYSF FKTALDDRKE GAVLAKKVNW IGCQGSEPHF 400
    RGFPCSLWVL FHFLTVQAAR QNVDHSQEAA KAKEVLPAIR GYVHYFFGCR 450
    DCASHFEQMA AASMHRVGSP NAAVLWLWSS HNRVNARLAG APSEDPQFPK 500
    VQWPPRELCS ACHNERLDVP VWDVEATLNF LKAHFSPSNI ILDFPAAGSA 550
    ARRDVQNVAA APELAMGALE LESRNSTLDP GKPEMMKSPT NTTPHVPAEG 600
    PEASRPPKLH PGLRAAPGQE PPEHMAELQR NEQEQPLGQW HLSKRDTGAA 650
    LLAESRAEKN RLWGPLEVRR VGRSSKQLVD IPEGQLEARA GRGRGQWLQV 700
    LGGGFSYLDI SLCVGLYSLS FMGLLAMYTY FQAKIRALKG HAGHPAA 747
    Length:747
    Mass (Da):82,578
    Last modified:June 1, 2001 - v3
    Checksum:i52639D09A50E00C5
    GO
    Isoform 2 (identifier: O00391-2) [UniParc]FASTAAdd to Basket

    Also known as: b, QSOX-S

    The sequence of this isoform differs from the canonical sequence as follows:
         603-604: AS → LI
         605-747: Missing.

    Show »
    Length:604
    Mass (Da):66,861
    Checksum:iB557EE4D1525E7FB
    GO

    Sequence cautioni

    The sequence BAD92517.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti114 – 1141N → S.
    Corresponds to variant rs3894211 [ dbSNP | Ensembl ].
    VAR_027429
    Natural varianti200 – 2001G → A.3 Publications
    Corresponds to variant rs17855475 [ dbSNP | Ensembl ].
    VAR_027430
    Natural varianti256 – 2561R → M.
    Corresponds to variant rs4360492 [ dbSNP | Ensembl ].
    VAR_027431
    Natural varianti294 – 2941A → S.
    Corresponds to variant rs2278943 [ dbSNP | Ensembl ].
    VAR_027432
    Natural varianti444 – 4441H → R.1 Publication
    Corresponds to variant rs12371 [ dbSNP | Ensembl ].
    VAR_027433
    Natural varianti591 – 5911N → H.
    Corresponds to variant rs3738115 [ dbSNP | Ensembl ].
    VAR_027434
    Natural varianti605 – 6051R → P.
    Corresponds to variant rs16855466 [ dbSNP | Ensembl ].
    VAR_053652

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei603 – 6042AS → LI in isoform 2. 2 PublicationsVSP_020489
    Alternative sequencei605 – 747143Missing in isoform 2. 2 PublicationsVSP_020490Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U97276 mRNA. Translation: AAC09010.2.
    AF361868 mRNA. Translation: AAM00263.1.
    AY358941 mRNA. Translation: AAQ89300.1.
    AB209280 mRNA. Translation: BAD92517.1. Different initiation.
    AL390718 Genomic DNA. Translation: CAI14838.1.
    AL390718 Genomic DNA. Translation: CAI14839.1.
    BC017692 mRNA. Translation: AAH17692.1.
    BC100023 mRNA. Translation: AAI00024.1.
    CCDSiCCDS1337.1. [O00391-1]
    CCDS30950.1. [O00391-2]
    RefSeqiNP_001004128.1. NM_001004128.2. [O00391-2]
    NP_002817.2. NM_002826.4. [O00391-1]
    UniGeneiHs.744925.

    Genome annotation databases

    EnsembliENST00000367600; ENSP00000356572; ENSG00000116260. [O00391-2]
    ENST00000367602; ENSP00000356574; ENSG00000116260. [O00391-1]
    GeneIDi5768.
    KEGGihsa:5768.
    UCSCiuc001gny.3. human. [O00391-2]
    uc001gnz.3. human. [O00391-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U97276 mRNA. Translation: AAC09010.2 .
    AF361868 mRNA. Translation: AAM00263.1 .
    AY358941 mRNA. Translation: AAQ89300.1 .
    AB209280 mRNA. Translation: BAD92517.1 . Different initiation.
    AL390718 Genomic DNA. Translation: CAI14838.1 .
    AL390718 Genomic DNA. Translation: CAI14839.1 .
    BC017692 mRNA. Translation: AAH17692.1 .
    BC100023 mRNA. Translation: AAI00024.1 .
    CCDSi CCDS1337.1. [O00391-1 ]
    CCDS30950.1. [O00391-2 ]
    RefSeqi NP_001004128.1. NM_001004128.2. [O00391-2 ]
    NP_002817.2. NM_002826.4. [O00391-1 ]
    UniGenei Hs.744925.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3LLI X-ray 2.05 A 286-546 [» ]
    3LLK X-ray 2.00 A/B/C 286-546 [» ]
    3Q6O X-ray 2.05 A 33-272 [» ]
    4IJ3 X-ray 2.70 A 33-272 [» ]
    ProteinModelPortali O00391.
    SMRi O00391. Positions 33-544.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111734. 4 interactions.
    IntActi O00391. 1 interaction.
    MINTi MINT-2862351.
    STRINGi 9606.ENSP00000356574.

    PTM databases

    PhosphoSitei O00391.

    Proteomic databases

    MaxQBi O00391.
    PaxDbi O00391.
    PeptideAtlasi O00391.
    PRIDEi O00391.

    Protocols and materials databases

    DNASUi 5768.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367600 ; ENSP00000356572 ; ENSG00000116260 . [O00391-2 ]
    ENST00000367602 ; ENSP00000356574 ; ENSG00000116260 . [O00391-1 ]
    GeneIDi 5768.
    KEGGi hsa:5768.
    UCSCi uc001gny.3. human. [O00391-2 ]
    uc001gnz.3. human. [O00391-1 ]

    Organism-specific databases

    CTDi 5768.
    GeneCardsi GC01P180123.
    HGNCi HGNC:9756. QSOX1.
    HPAi HPA042127.
    MIMi 603120. gene.
    neXtProti NX_O00391.
    PharmGKBi PA162400559.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000231631.
    HOVERGENi HBG080360.
    InParanoidi O00391.
    KOi K10758.
    OMAi SHNRVNA.
    OrthoDBi EOG73RB9X.
    PhylomeDBi O00391.
    TreeFami TF316749.

    Enzyme and pathway databases

    BRENDAi 1.8.3.2. 2681.

    Miscellaneous databases

    ChiTaRSi QSOX1. human.
    EvolutionaryTracei O00391.
    GeneWikii QSOX1.
    GenomeRNAii 5768.
    NextBioi 22434.
    PROi O00391.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00391.
    Bgeei O00391.
    CleanExi HS_QSOX1.
    Genevestigatori O00391.

    Family and domain databases

    Gene3Di 1.20.120.310. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR017905. ERV/ALR_sulphydryl_oxidase.
    IPR012336. Thioredoxin-like_fold.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF04777. Evr1_Alr. 1 hit.
    PF00085. Thioredoxin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 1 hit.
    SSF69000. SSF69000. 1 hit.
    PROSITEi PS51324. ERV_ALR. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: thioredoxin and ERV1."
      Coppock D.L., Cina-Poppe D., Gilleran S.
      Genomics 54:460-468(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION.
      Tissue: Lung.
    2. "Identification and expression of a new splicing variant of FAD-sulfhydryl oxidase in adult rat brain."
      Radom J., Colin D., Thiebault F., Dognin-Bergeret M.J., Mairet-Coello G., Esnard-Feve A., Fellmann D., Jouvenot M.
      Biochim. Biophys. Acta 1759:225-233(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, VARIANTS ALA-200 AND ARG-444.
      Tissue: Placenta.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-200.
      Tissue: Brain.
    5. "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.
      , 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] [Europe PMC] [Abstract]
      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] (ISOFORMS 1 AND 2), VARIANT ALA-200.
      Tissue: Chondrosarcoma and Kidney.
    7. "Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases."
      Hoober K.L., Glynn N.M., Burnside J., Coppock D.L., Thorpe C.
      J. Biol. Chem. 274:31759-31762(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "Regulation of the quiescence-induced genes: quiescin Q6, decorin, and ribosomal protein S29."
      Coppock D.L., Kopman C., Gudas J., Cina-Poppe D.A.
      Biochem. Biophys. Res. Commun. 269:604-610(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    9. "The distribution and specificity of expression of quiescin Q6 (Q6) in Human tissues is associated with both endocrine and non-endocrine protein secretion."
      Turi G.K.
      Proc. Annu. Meet. Am. Assoc. Cancer Res. 42:397-397(2001)
      Cited for: TISSUE SPECIFICITY.
    10. "Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes."
      Thorpe C., Hoober K.L., Raje S., Glynn N.M., Burnside J., Turi G.K., Coppock D.L.
      Arch. Biochem. Biophys. 405:1-12(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, NOMENCLATURE, ALTERNATIVE SPLICING.
    11. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130.
      Tissue: Plasma.
    12. "Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1."
      Chakravarthi S., Jessop C.E., Willer M., Stirling C.J., Bulleid N.J.
      Biochem. J. 404:403-411(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesis."
      Heckler E.J., Alon A., Fass D., Thorpe C.
      Biochemistry 47:4955-4963(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, MUTAGENESIS OF CYS-70; CYS-73; CYS-449; CYS-452; CYS-509 AND CYS-512, ACTIVE SITE.
    14. Cited for: GLYCOSYLATION AT ASN-130.
    15. "QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains."
      Alon A., Heckler E.J., Thorpe C., Fass D.
      FEBS Lett. 584:1521-1525(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 286-546 IN COMPLEX WITH FAD, SUBUNIT, COFACTOR, DISULFIDE BONDS.

    Entry informationi

    Entry nameiQSOX1_HUMAN
    AccessioniPrimary (citable) accession number: O00391
    Secondary accession number(s): Q59G29
    , Q5T2X0, Q8TDL6, Q8WVP4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2006
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 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

    Miscellaneous

    'Quiescin Q6' means that it was the sixth clone to be found at a higher level of expression in quiescent fibroblasts.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3