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Q6ZRP7 (QSOX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sulfhydryl oxidase 2

EC=1.8.3.2
Alternative name(s):
Neuroblastoma-derived sulfhydryl oxidase
Quiescin Q6-like protein 1
Gene names
Name:QSOX2
Synonyms:QSCN6L1, SOXN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length698 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

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

Cofactor

Binds 1 FAD per subunit Potential.

Subcellular location

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

Tissue specificity

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

Sequence similarities

Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.

Contains 1 ERV/ALR sulfhydryl oxidase domain.

Contains 1 thioredoxin domain.

Sequence caution

The sequence BAC87262.1 differs from that shown. Reason: Erroneous initiation.

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

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Nucleus
Secreted
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionthiol oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 698677Sulfhydryl oxidase 2
PRO_0000249538

Regions

Transmembrane662 – 68221Helical; Potential
Domain34 – 178145Thioredoxin
Domain421 – 530110ERV/ALR sulfhydryl oxidase
Nucleotide binding505 – 5128FAD By similarity
Compositional bias41 – 444Poly-Ala
Compositional bias588 – 5914Poly-Glu

Sites

Active site911Nucleophile By similarity
Active site941Nucleophile By similarity
Binding site4261FAD By similarity
Binding site4331FAD By similarity
Binding site4371FAD By similarity
Binding site4781FAD By similarity
Binding site4821FAD By similarity
Binding site5271FAD By similarity
Binding site5301FAD By similarity

Amino acid modifications

Modified residue5791Phosphoserine Ref.8
Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation1781N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Glycosylation2661N-linked (GlcNAc...) Potential
Disulfide bond91 ↔ 94Redox-active By similarity
Disulfide bond418 ↔ 430 By similarity
Disulfide bond476 ↔ 479 By similarity
Disulfide bond536 ↔ 539 By similarity

Natural variations

Natural variant1261K → E.
Corresponds to variant rs12380852 [ dbSNP | Ensembl ].
VAR_027435

Experimental info

Sequence conflict961G → A in CAC85331. Ref.1
Sequence conflict2051N → K in BAC87262. Ref.3
Sequence conflict2241R → W in CAC85331. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6ZRP7 [UniParc].

Last modified July 24, 2007. Version 3.
Checksum: 7F2B3F890AE657CF

FASTA69877,529
        10         20         30         40         50         60 
MAAAGAAVAR SPGIGAGPAL RARRSPPPRA ARLPRLLVLL AAAAVGPGAG GAARLYRAGE 

        70         80         90        100        110        120 
DAVWVLDSGS VRGATANSSA AWLVQFYSSW CGHCIGYAPT WRALAGDVRD WASAIRVAAL 

       130        140        150        160        170        180 
DCMEEKNQAV CHDYDIHFYP TFRYFKAFTK EFTTGENFKG PDRELRTVRQ TMIDFLQNHT 

       190        200        210        220        230        240 
EGSRPPACPR LDPIQPSDVL SLLDNRGSHY VAIVFESNSS YLGREVILDL IPYESIVVTR 

       250        260        270        280        290        300 
ALDGDKAFLE KLGVSSVPSC YLIYPNGSHG LINVVKPLRA FFSSYLKSLP DVRKKSLPLP 

       310        320        330        340        350        360 
EKPHKEENSE IVVWREFDKS KLYTVDLESG LHYLLRVELA AHKSLAGAEL KTLKDFVTVL 

       370        380        390        400        410        420 
AKLFPGRPPV KKLLEMLQEW LASLPLDRIP YNAVLDLVNN KMRISGIFLT NHIKWVGCQG 

       430        440        450        460        470        480 
SRSELRGYPC SLWKLFHTLT VEASTHPDAL VGTGFEDDPQ AVLQTMRRYV HTFFGCKECG 

       490        500        510        520        530        540 
EHFEEMAKES MDSVKTPDQA ILWLWKKHNM VNGRLAGHLS EDPRFPKLQW PTPDLCPACH 

       550        560        570        580        590        600 
EEIKGLASWD EGHVLTFLKQ HYGRDNLLDT YSADQGDSSE GGTLARGEEE EKRLTPPEVS 

       610        620        630        640        650        660 
HGDRDTQSVR PPGALGPRPA LPESLHHSLD GKLQSLDGPG AHKEVGGAAP FLGVDFSSLD 

       670        680        690 
MSLCVVLYVA SSLFLMVMYF FFRVRSRRWK VKHHHPAV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_859052.3. NM_181701.3.
UniGeneHs.144073.

3D structure databases

ProteinModelPortalQ6ZRP7.
SMRQ6ZRP7. Positions 58-568.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127987. 5 interactions.
STRING9606.ENSP00000351536.

PTM databases

PhosphoSiteQ6ZRP7.

Polymorphism databases

DMDM158958335.

Proteomic databases

PaxDbQ6ZRP7.
PRIDEQ6ZRP7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358701; ENSP00000351536; ENSG00000165661.
ENST00000561576; ENSP00000455224; ENSG00000261074.
GeneID169714.
KEGGhsa:169714.
UCSCuc010nbi.2. human.

Organism-specific databases

CTD169714.
GeneCardsGC09M139098.
H-InvDBHIX0008541.
HGNCHGNC:30249. QSOX2.
HPAHPA012716.
MIM612860. gene.
neXtProtNX_Q6ZRP7.
PharmGKBPA162400588.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG237986.
HOVERGENHBG080360.
InParanoidQ6ZRP7.
KOK10758.
OMAHCIGYAP.
PhylomeDBQ6ZRP7.
TreeFamTF316749.

Gene expression databases

BgeeQ6ZRP7.
CleanExHS_QSOX2.
GenevestigatorQ6ZRP7.

Family and domain databases

Gene3D1.20.120.310. 1 hit.
3.40.30.10. 1 hit.
InterProIPR017905. ERV/ALR_sulphydryl_oxidase.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF04777. Evr1_Alr. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
SSF69000. SSF69000. 1 hit.
PROSITEPS51324. ERV_ALR. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi169714.
NextBio88829.
PROQ6ZRP7.
SOURCESearch...

Entry information

Entry nameQSOX2_HUMAN
AccessionPrimary (citable) accession number: Q6ZRP7
Secondary accession number(s): A2CEE0 expand/collapse secondary AC list , A6NLB0, Q5TB37, Q7Z7B6, Q86VV7, Q8N3G2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: July 24, 2007
Last modified: April 16, 2014
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM