Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q6ZRP7

- QSOX2_HUMAN

UniProt

Q6ZRP7 - QSOX2_HUMAN

Protein

Sulfhydryl oxidase 2

Gene

QSOX2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 3 (24 Jul 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. Also seems to play a role in regulating the sensitization of neuroblastoma cells for interferon-gamma-induced apoptosis.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 1 FAD per subunit.Curated

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei91 – 911NucleophileBy similarity
    Active sitei94 – 941NucleophileBy similarity
    Binding sitei426 – 4261FADBy similarity
    Binding sitei433 – 4331FADBy similarity
    Binding sitei437 – 4371FADBy similarity
    Binding sitei478 – 4781FADBy similarity
    Binding sitei482 – 4821FADBy similarity
    Binding sitei527 – 5271FADBy similarity
    Binding sitei530 – 5301FADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi505 – 5128FADBy similarity

    GO - Molecular functioni

    1. thiol oxidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sulfhydryl oxidase 2 (EC:1.8.3.2)
    Alternative name(s):
    Neuroblastoma-derived sulfhydryl oxidase
    Quiescin Q6-like protein 1
    Gene namesi
    Name:QSOX2
    Synonyms:QSCN6L1, SOXN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:30249. QSOX2.

    Subcellular locationi

    Membrane 1 Publication; Single-pass membrane protein 1 Publication. Secreted 1 Publication. Cell membrane Curated; Single-pass membrane protein Curated. Nucleus membrane Curated; Single-pass membrane protein Curated
    Note: Seems to be predominantly targeted to the nuclear and outer plasma membrane.

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. nuclear membrane Source: UniProtKB-SubCell
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane, Nucleus, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162400588.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 698677Sulfhydryl oxidase 2PRO_0000249538Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi91 ↔ 94Redox-activePROSITE-ProRule annotation
    Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi418 ↔ 430PROSITE-ProRule annotation
    Disulfide bondi476 ↔ 479PROSITE-ProRule annotation
    Disulfide bondi536 ↔ 539PROSITE-ProRule annotation
    Modified residuei579 – 5791Phosphoserine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ6ZRP7.
    PaxDbiQ6ZRP7.
    PRIDEiQ6ZRP7.

    PTM databases

    PhosphoSiteiQ6ZRP7.

    Expressioni

    Tissue specificityi

    Expressed in pancreas, brain, placenta, kidney, heart and fetal tissues. Weakly expressed in lung, liver and skeletal muscles.1 Publication

    Gene expression databases

    BgeeiQ6ZRP7.
    CleanExiHS_QSOX2.
    GenevestigatoriQ6ZRP7.

    Organism-specific databases

    HPAiHPA012716.

    Interactioni

    Protein-protein interaction databases

    BioGridi127987. 5 interactions.
    STRINGi9606.ENSP00000351536.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6ZRP7.
    SMRiQ6ZRP7. Positions 58-568.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei662 – 68221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 178145ThioredoxinPROSITE-ProRule annotationAdd
    BLAST
    Domaini421 – 530110ERV/ALR sulfhydryl oxidasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi41 – 444Poly-Ala
    Compositional biasi588 – 5914Poly-Glu

    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

    eggNOGiNOG237986.
    HOVERGENiHBG080360.
    InParanoidiQ6ZRP7.
    KOiK10758.
    OMAiHCIGYAP.
    PhylomeDBiQ6ZRP7.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    Q6ZRP7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAGAAVAR SPGIGAGPAL RARRSPPPRA ARLPRLLVLL AAAAVGPGAG    50
    GAARLYRAGE DAVWVLDSGS VRGATANSSA AWLVQFYSSW CGHCIGYAPT 100
    WRALAGDVRD WASAIRVAAL DCMEEKNQAV CHDYDIHFYP TFRYFKAFTK 150
    EFTTGENFKG PDRELRTVRQ TMIDFLQNHT EGSRPPACPR LDPIQPSDVL 200
    SLLDNRGSHY VAIVFESNSS YLGREVILDL IPYESIVVTR ALDGDKAFLE 250
    KLGVSSVPSC YLIYPNGSHG LINVVKPLRA FFSSYLKSLP DVRKKSLPLP 300
    EKPHKEENSE IVVWREFDKS KLYTVDLESG LHYLLRVELA AHKSLAGAEL 350
    KTLKDFVTVL AKLFPGRPPV KKLLEMLQEW LASLPLDRIP YNAVLDLVNN 400
    KMRISGIFLT NHIKWVGCQG SRSELRGYPC SLWKLFHTLT VEASTHPDAL 450
    VGTGFEDDPQ AVLQTMRRYV HTFFGCKECG EHFEEMAKES MDSVKTPDQA 500
    ILWLWKKHNM VNGRLAGHLS EDPRFPKLQW PTPDLCPACH EEIKGLASWD 550
    EGHVLTFLKQ HYGRDNLLDT YSADQGDSSE GGTLARGEEE EKRLTPPEVS 600
    HGDRDTQSVR PPGALGPRPA LPESLHHSLD GKLQSLDGPG AHKEVGGAAP 650
    FLGVDFSSLD MSLCVVLYVA SSLFLMVMYF FFRVRSRRWK VKHHHPAV 698
    Length:698
    Mass (Da):77,529
    Last modified:July 24, 2007 - v3
    Checksum:i7F2B3F890AE657CF
    GO

    Sequence cautioni

    The sequence CAC85331.1 differs from that shown. Reason: Frameshift at positions 354, 369, 616 and 618.
    The sequence BAC87262.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 961G → A in CAC85331. (PubMed:14633699)Curated
    Sequence conflicti205 – 2051N → K in BAC87262. (PubMed:14702039)Curated
    Sequence conflicti224 – 2241R → W in CAC85331. (PubMed:14633699)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti126 – 1261K → E.
    Corresponds to variant rs12380852 [ dbSNP | Ensembl ].
    VAR_027435

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ318051 mRNA. Translation: CAC85331.1. Frameshift.
    AL138781, CR392000 Genomic DNA. Translation: CAI16881.2.
    CR392000, AL138781 Genomic DNA. Translation: CAM28352.1.
    AK128077 mRNA. Translation: BAC87262.1. Different initiation.
    AL834369 mRNA. Translation: CAD39032.1.
    CCDSiCCDS35178.1.
    RefSeqiNP_859052.3. NM_181701.3.
    UniGeneiHs.144073.

    Genome annotation databases

    EnsembliENST00000358701; ENSP00000351536; ENSG00000165661.
    GeneIDi169714.
    KEGGihsa:169714.
    UCSCiuc010nbi.2. human.

    Polymorphism databases

    DMDMi158958335.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ318051 mRNA. Translation: CAC85331.1 . Frameshift.
    AL138781 , CR392000 Genomic DNA. Translation: CAI16881.2 .
    CR392000 , AL138781 Genomic DNA. Translation: CAM28352.1 .
    AK128077 mRNA. Translation: BAC87262.1 . Different initiation.
    AL834369 mRNA. Translation: CAD39032.1 .
    CCDSi CCDS35178.1.
    RefSeqi NP_859052.3. NM_181701.3.
    UniGenei Hs.144073.

    3D structure databases

    ProteinModelPortali Q6ZRP7.
    SMRi Q6ZRP7. Positions 58-568.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 127987. 5 interactions.
    STRINGi 9606.ENSP00000351536.

    PTM databases

    PhosphoSitei Q6ZRP7.

    Polymorphism databases

    DMDMi 158958335.

    Proteomic databases

    MaxQBi Q6ZRP7.
    PaxDbi Q6ZRP7.
    PRIDEi Q6ZRP7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358701 ; ENSP00000351536 ; ENSG00000165661 .
    GeneIDi 169714.
    KEGGi hsa:169714.
    UCSCi uc010nbi.2. human.

    Organism-specific databases

    CTDi 169714.
    GeneCardsi GC09M139098.
    H-InvDB HIX0008541.
    HGNCi HGNC:30249. QSOX2.
    HPAi HPA012716.
    MIMi 612860. gene.
    neXtProti NX_Q6ZRP7.
    PharmGKBi PA162400588.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG237986.
    HOVERGENi HBG080360.
    InParanoidi Q6ZRP7.
    KOi K10758.
    OMAi HCIGYAP.
    PhylomeDBi Q6ZRP7.
    TreeFami TF316749.

    Miscellaneous databases

    GenomeRNAii 169714.
    NextBioi 88829.
    PROi Q6ZRP7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q6ZRP7.
    CleanExi HS_QSOX2.
    Genevestigatori Q6ZRP7.

    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. "Neuroblastoma-derived sulfhydryl oxidase, a new member of the sulfhydryl oxidase/quiescin 6 family, regulates sensitization to interferon gamma-induced cell death in human neuroblastoma cells."
      Wittke I., Wiedemeyer R., Pillmann A., Savelyeva L., Westermann F., Schwab M.
      Cancer Res. 63:7742-7752(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] OF 100-698.
      Tissue: Testis.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 158-698.
      Tissue: Melanoma.
    5. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiQSOX2_HUMAN
    AccessioniPrimary (citable) accession number: Q6ZRP7
    Secondary accession number(s): A2CEE0
    , A6NLB0, Q5TB37, Q7Z7B6, Q86VV7, Q8N3G2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2006
    Last sequence update: July 24, 2007
    Last modified: October 1, 2014
    This is version 99 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3