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O00391

- QSOX1_HUMAN

UniProt

O00391 - QSOX1_HUMAN

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Protein

Sulfhydryl oxidase 1

Gene

QSOX1

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

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (2)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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

FAD2 PublicationsNote: 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
Complete GO annotation...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9756. QSOX1.

Subcellular locationi

Isoform 1 : Golgi apparatus membrane; Single-pass membrane protein
Isoform 2 : Secreted › extracellular space
Note: Found in the extracellular medium of quiescent cells but is not found in proliferating cells.

Topology

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

GO - Cellular componenti

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

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

BgeeiO00391.
CleanExiHS_QSOX1.
ExpressionAtlasiO00391. baseline and differential.
GenevestigatoriO00391.

Organism-specific databases

HPAiHPA042127.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

BioGridi111734. 9 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 – 456Combined sources
Turni47 – 493Combined sources
Helixi50 – 545Combined sources
Beta strandi58 – 669Combined sources
Helixi71 – 8616Combined sources
Helixi88 – 903Combined sources
Turni91 – 933Combined sources
Beta strandi94 – 1007Combined sources
Turni104 – 1063Combined sources
Helixi107 – 1126Combined sources
Beta strandi117 – 1248Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi134 – 1363Combined sources
Helixi143 – 15513Combined sources
Helixi173 – 1775Combined sources
Helixi179 – 1824Combined sources
Beta strandi186 – 1938Combined sources
Helixi199 – 2068Combined sources
Turni207 – 2093Combined sources
Beta strandi213 – 2197Combined sources
Helixi223 – 2297Combined sources
Beta strandi234 – 2418Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi252 – 2554Combined sources
Helixi256 – 2649Combined sources
Beta strandi298 – 3003Combined sources
Helixi301 – 31313Combined sources
Helixi316 – 3183Combined sources
Beta strandi320 – 3234Combined sources
Helixi324 – 34017Combined sources
Helixi345 – 36016Combined sources
Beta strandi363 – 3675Combined sources
Helixi368 – 37710Combined sources
Helixi380 – 3834Combined sources
Beta strandi400 – 4023Combined sources
Helixi403 – 41917Combined sources
Helixi426 – 4316Combined sources
Helixi432 – 4343Combined sources
Helixi435 – 44612Combined sources
Helixi450 – 46314Combined sources
Helixi464 – 4663Combined sources
Helixi470 – 48819Combined sources
Beta strandi502 – 5043Combined sources
Turni506 – 5083Combined sources
Helixi510 – 5123Combined sources
Beta strandi517 – 5193Combined sources
Helixi524 – 53411Combined sources
Helixi537 – 5393Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 35-544.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00391.

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

Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.Curated
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.
GeneTreeiENSGT00390000008045.
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

        10         20         30         40         50
MRRCNSGSGP PPSLLLLLLW LLAVPGANAA PRSALYSPSD PLTLLQADTV 
        60         70         80         90        100
RGAVLGSRSA WAVEFFASWC GHCIAFAPTW KALAEDVKAW RPALYLAALD 
       110        120        130        140        150
CAEETNSAVC RDFNIPGFPT VRFFKAFTKN GSGAVFPVAG ADVQTLRERL 
       160        170        180        190        200
IDALESHHDT WPPACPPLEP AKLEEIDGFF ARNNEEYLAL IFEKGGSYLG 
       210        220        230        240        250
REVALDLSQH KGVAVRRVLN TEANVVRKFG VTDFPSCYLL FRNGSVSRVP 
       260        270        280        290        300
VLMESRSFYT AYLQRLSGLT REAAQTTVAP TTANKIAPTV WKLADRSKIY 
       310        320        330        340        350
MADLESALHY ILRIEVGRFP VLEGQRLVAL KKFVAVLAKY FPGRPLVQNF 
       360        370        380        390        400
LHSVNEWLKR QKRNKIPYSF FKTALDDRKE GAVLAKKVNW IGCQGSEPHF 
       410        420        430        440        450
RGFPCSLWVL FHFLTVQAAR QNVDHSQEAA KAKEVLPAIR GYVHYFFGCR 
       460        470        480        490        500
DCASHFEQMA AASMHRVGSP NAAVLWLWSS HNRVNARLAG APSEDPQFPK 
       510        520        530        540        550
VQWPPRELCS ACHNERLDVP VWDVEATLNF LKAHFSPSNI ILDFPAAGSA 
       560        570        580        590        600
ARRDVQNVAA APELAMGALE LESRNSTLDP GKPEMMKSPT NTTPHVPAEG 
       610        620        630        640        650
PEASRPPKLH PGLRAAPGQE PPEHMAELQR NEQEQPLGQW HLSKRDTGAA 
       660        670        680        690        700
LLAESRAEKN RLWGPLEVRR VGRSSKQLVD IPEGQLEARA GRGRGQWLQV 
       710        720        730        740 
LGGGFSYLDI SLCVGLYSLS FMGLLAMYTY FQAKIRALKG HAGHPAA
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 35-544.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111734. 9 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.
GeneTreei ENSGT00390000008045.
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

Bgeei O00391.
CleanExi HS_QSOX1.
ExpressionAtlasi O00391. baseline and differential.
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

« Hide 'large scale' publications
  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.
+Additional computationally mapped references.

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: January 7, 2015
This is version 130 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

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 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.
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