O00391 (QSOX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sulfhydryl oxidase 1
Short name=hQSOX
EC=1.8.3.2

Alternative name(s):
Quiescin Q6

Gene names

Name:	QSOX1
Synonyms:	QSCN6
ORF Names:	UNQ2520/PRO6013

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	747 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. In fibroblasts, it may have tumor-suppressing capabilities being involved in growth regulation. Ref.2 Ref.7 Ref.8 Ref.10 Ref.12 Ref.13
Catalytic activity	2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2. Ref.13
Cofactor	Binds 1 FAD per subunit. Ref.13 Ref.14
Subunit structure	Monomer. Ref.13 Ref.14
Subcellular location	Isoform 1: Golgi apparatus membrane; Single-pass membrane protein Ref.8 Ref.12. Isoform 2: Secreted › extracellular space. Note: Found in the extracellular medium of quiescent cells but is not found in proliferating cells. Ref.8 Ref.12
Tissue specificity	Expressed in heart, placenta, lung, liver, skeletal muscle, pancreas and very weakly in brain and kidney. Ref.8 Ref.9
Induction	Induced in quiescent cells just as fibroblasts begin to leave the proliferative cycle and enter quiescence. Ref.1 Ref.7 Ref.8
Miscellaneous	'Quiescin Q6' means that it was the sixth clone to be found at a higher level of expression in quiescent fibroblasts.
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 BAD92517.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular space Inferred from direct assay Ref.8. Source: UniProtKB integral to Golgi membrane Inferred from direct assay Ref.12. Source: UniProtKB
Molecular_function	flavin-linked sulfhydryl oxidase activity Inferred from direct assay Ref.13. Source: UniProtKB protein disulfide isomerase activity Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O00391-1)

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.

Isoform 2 (identifier: O00391-2)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Potential

Chain

30 – 747

718

Sulfhydryl oxidase 1

PRO_0000249533

Regions

Transmembrane

710 – 730

21

Helical; Potential

Domain

36 – 156

121

Thioredoxin

Domain

396 – 503

108

ERV/ALR sulfhydryl oxidase

Nucleotide binding

478 – 485

8

FAD

Sites

Active site

70

1

Nucleophile Probable

Active site

73

1

Nucleophile Probable

Binding site

401

1

FAD

Binding site

408

1

FAD

Binding site

412

1

FAD

Binding site

451

1

FAD

Binding site

455

1

FAD

Binding site

500

1

FAD

Binding site

503

1

FAD

Amino acid modifications

Glycosylation

130

1

N-linked (GlcNAc...) Ref.11

Glycosylation

243

1

N-linked (GlcNAc...) Potential

Glycosylation

575

1

N-linked (GlcNAc...) Potential

Disulfide bond

70 ↔ 73

Redox-active Probable

Disulfide bond

393 ↔ 405

Ref.14

Disulfide bond

449 ↔ 452

Ref.14

Disulfide bond

509 ↔ 512

Ref.14

Natural variations

Alternative sequence

603 – 604

2

AS → LI in isoform 2.

VSP_020489

Alternative sequence

605 – 747

143

Missing in isoform 2.

VSP_020490

Natural variant

114

1

N → S.
Corresponds to variant rs3894211 [ dbSNP | Ensembl ].

VAR_027429

Natural variant

200

1

G → A. Ref.2 Ref.4 Ref.6
Corresponds to variant rs17855475 [ dbSNP | Ensembl ].

VAR_027430

Natural variant

256

1

R → M.
Corresponds to variant rs4360492 [ dbSNP | Ensembl ].

VAR_027431

Natural variant

294

1

A → S.
Corresponds to variant rs2278943 [ dbSNP | Ensembl ].

VAR_027432

Natural variant

444

1

H → R. Ref.2
Corresponds to variant rs12371 [ dbSNP | Ensembl ].

VAR_027433

Natural variant

591

1

N → H.
Corresponds to variant rs3738115 [ dbSNP | Ensembl ].

VAR_027434

Natural variant

605

1

R → P.
Corresponds to variant rs16855466 [ dbSNP | Ensembl ].

VAR_053652

Experimental info

Mutagenesis

70

1

C → S: Reduces activity by 93%. Ref.13

Mutagenesis

73

1

C → S: Reduces activity by 93%. Ref.13

Mutagenesis

449

1

C → S: Reduces activity by 96%. Ref.13

Mutagenesis

452

1

C → S: Loss of activity. Ref.13

Mutagenesis

509

1

C → S: No effect. Reduces activity by 70%; when associated with S-512. Ref.13

Mutagenesis

512

1

C → S: Reduces activity by 40%. Reduces activity by 70%; when associated with S-509. Ref.13

Secondary structure

1

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747

Helix Strand Turn

Details...

Beta strand

40 – 45

6

Turn

47 – 49

3

Helix

50 – 54

5

Beta strand

58 – 66

9

Helix

71 – 86

16

Helix

88 – 90

3

Turn

91 – 93

3

Beta strand

94 – 100

7

Turn

104 – 106

3

Helix

107 – 112

6

Beta strand

117 – 124

8

Beta strand

130 – 132

3

Helix

143 – 155

13

Helix

173 – 177

5

Helix

179 – 182

4

Beta strand

186 – 193

8

Helix

199 – 206

8

Turn

207 – 209

3

Beta strand

213 – 219

7

Helix

223 – 229

7

Beta strand

234 – 241

8

Beta strand

246 – 248

3

Beta strand

252 – 255

4

Helix

256 – 264

9

Beta strand

298 – 300

3

Helix

301 – 313

13

Helix

316 – 318

3

Beta strand

320 – 323

4

Helix

324 – 340

17

Helix

345 – 360

16

Beta strand

363 – 367

5

Helix

368 – 377

10

Helix

380 – 383

4

Beta strand

400 – 402

3

Helix

403 – 419

17

Helix

426 – 431

6

Helix

432 – 434

3

Helix

435 – 446

12

Helix

450 – 463

14

Helix

464 – 466

3

Helix

470 – 488

19

Beta strand

502 – 504

3

Turn

506 – 508

3

Helix

510 – 512

3

Beta strand

517 – 519

3

Helix

524 – 534

11

Helix

537 – 539

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (a) (QSOX-L) [UniParc]. Last modified June 1, 2001. Version 3. Checksum: 52639D09A50E00C5	FASTA	747	82,578
	10 20 30 40 50 60 MRRCNSGSGP PPSLLLLLLW LLAVPGANAA PRSALYSPSD PLTLLQADTV RGAVLGSRSA 70 80 90 100 110 120 WAVEFFASWC GHCIAFAPTW KALAEDVKAW RPALYLAALD CAEETNSAVC RDFNIPGFPT 130 140 150 160 170 180 VRFFKAFTKN GSGAVFPVAG ADVQTLRERL IDALESHHDT WPPACPPLEP AKLEEIDGFF 190 200 210 220 230 240 ARNNEEYLAL IFEKGGSYLG REVALDLSQH KGVAVRRVLN TEANVVRKFG VTDFPSCYLL 250 260 270 280 290 300 FRNGSVSRVP VLMESRSFYT AYLQRLSGLT REAAQTTVAP TTANKIAPTV WKLADRSKIY 310 320 330 340 350 360 MADLESALHY ILRIEVGRFP VLEGQRLVAL KKFVAVLAKY FPGRPLVQNF LHSVNEWLKR 370 380 390 400 410 420 QKRNKIPYSF FKTALDDRKE GAVLAKKVNW IGCQGSEPHF RGFPCSLWVL FHFLTVQAAR 430 440 450 460 470 480 QNVDHSQEAA KAKEVLPAIR GYVHYFFGCR DCASHFEQMA AASMHRVGSP NAAVLWLWSS 490 500 510 520 530 540 HNRVNARLAG APSEDPQFPK VQWPPRELCS ACHNERLDVP VWDVEATLNF LKAHFSPSNI 550 560 570 580 590 600 ILDFPAAGSA ARRDVQNVAA APELAMGALE LESRNSTLDP GKPEMMKSPT NTTPHVPAEG 610 620 630 640 650 660 PEASRPPKLH PGLRAAPGQE PPEHMAELQR NEQEQPLGQW HLSKRDTGAA LLAESRAEKN 670 680 690 700 710 720 RLWGPLEVRR VGRSSKQLVD IPEGQLEARA GRGRGQWLQV LGGGFSYLDI SLCVGLYSLS 730 740 FMGLLAMYTY FQAKIRALKG HAGHPAA
	Isoform 2 (b) (QSOX-S) [UniParc]. Checksum: B557EE4D1525E7FB	FASTA	604	66,861
	10 20 30 40 50 60 MRRCNSGSGP PPSLLLLLLW LLAVPGANAA PRSALYSPSD PLTLLQADTV RGAVLGSRSA 70 80 90 100 110 120 WAVEFFASWC GHCIAFAPTW KALAEDVKAW RPALYLAALD CAEETNSAVC RDFNIPGFPT 130 140 150 160 170 180 VRFFKAFTKN GSGAVFPVAG ADVQTLRERL IDALESHHDT WPPACPPLEP AKLEEIDGFF 190 200 210 220 230 240 ARNNEEYLAL IFEKGGSYLG REVALDLSQH KGVAVRRVLN TEANVVRKFG VTDFPSCYLL 250 260 270 280 290 300 FRNGSVSRVP VLMESRSFYT AYLQRLSGLT REAAQTTVAP TTANKIAPTV WKLADRSKIY 310 320 330 340 350 360 MADLESALHY ILRIEVGRFP VLEGQRLVAL KKFVAVLAKY FPGRPLVQNF LHSVNEWLKR 370 380 390 400 410 420 QKRNKIPYSF FKTALDDRKE GAVLAKKVNW IGCQGSEPHF RGFPCSLWVL FHFLTVQAAR 430 440 450 460 470 480 QNVDHSQEAA KAKEVLPAIR GYVHYFFGCR DCASHFEQMA AASMHRVGSP NAAVLWLWSS 490 500 510 520 530 540 HNRVNARLAG APSEDPQFPK VQWPPRELCS ACHNERLDVP VWDVEATLNF LKAHFSPSNI 550 560 570 580 590 600 ILDFPAAGSA ARRDVQNVAA APELAMGALE LESRNSTLDP GKPEMMKSPT NTTPHVPAEG PELI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] 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, 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, MASS SPECTROMETRY. 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]	"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00003590.
IPI00465016.

RefSeq

NP_001004128.1. NM_001004128.2.
NP_002817.2. NM_002826.4.

UniGene

Hs.702167.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O00391.

ModBase

Search...

Protein-protein interaction databases

IntAct

O00391. 1 interaction.

MINT

MINT-2862351.

STRING

9606.ENSP00000356574.

PTM databases

PhosphoSite

O00391.

Proteomic databases

PaxDb

O00391.

PeptideAtlas

O00391.

PRIDE

O00391.

Protocols and materials databases

DNASU

5768.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000367600; ENSP00000356572; ENSG00000116260.
ENST00000367602; ENSP00000356574; ENSG00000116260.

GeneID

5768.

KEGG

hsa:5768.

UCSC

uc001gny.3. human.
uc001gnz.3. human.

Organism-specific databases

CTD

5768.

GeneCards

GC01P180123.

HGNC

HGNC:9756. QSOX1.

HPA

HPA042127.

MIM

603120. gene.

neXtProt

NX_O00391.

PharmGKB

PA162400559.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0526.

HOGENOM

HOG000231631.

HOVERGEN

HBG080360.

InParanoid

O00391.

KO

K10758.

OMA

SHNRVNA.

OrthoDB

EOG4JT05B.

PhylomeDB

O00391.

Enzyme and pathway databases

BRENDA

1.8.3.2. 2681.

Gene expression databases

ArrayExpress

O00391.

Bgee

O00391.

CleanEx

HS_QSOX1.

Genevestigator

O00391.

GermOnline

ENSG00000116260. Homo sapiens.

Family and domain databases

Gene3D

1.20.120.310. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR017905. ERV/ALR_sulphydryl_oxidase.
IPR006863. Evr1_Alr.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]

Pfam

PF04777. Evr1_Alr. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]

SUPFAM

SSF69000. Evr1_Alr. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS51324. ERV_ALR. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

QSOX1. human.

EvolutionaryTrace

O00391.

GenomeRNAi

5768.

NextBio

22434.

SOURCE

Search...

Entry information

Entry name

QSOX1_HUMAN

Accession

Primary (citable) accession number: O00391
Secondary accession number(s): Q59G29 , Q5T2X0, Q8TDL6, Q8WVP4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2006
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.