Q6ZRP7 (QSOX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	698 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. 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 component	Cell membrane Membrane Nucleus Secreted
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to 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 function	thiol oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 698	677	Sulfhydryl oxidase 2		PRO_0000249538
Regions
	Transmembrane	662 – 682	21	Helical; Potential
	Domain	34 – 178	145	Thioredoxin
	Domain	421 – 530	110	ERV/ALR sulfhydryl oxidase
	Nucleotide binding	505 – 512	8	FAD By similarity
	Compositional bias	41 – 44	4	Poly-Ala
	Compositional bias	588 – 591	4	Poly-Glu
Sites
	Active site	91	1	Nucleophile By similarity
	Active site	94	1	Nucleophile By similarity
	Binding site	426	1	FAD By similarity
	Binding site	433	1	FAD By similarity
	Binding site	437	1	FAD By similarity
	Binding site	478	1	FAD By similarity
	Binding site	482	1	FAD By similarity
	Binding site	527	1	FAD By similarity
	Binding site	530	1	FAD By similarity
Amino acid modifications
	Modified residue	578	1	Phosphoserine Ref.5 Ref.6
	Glycosylation	77	1	N-linked (GlcNAc...) Potential
	Glycosylation	178	1	N-linked (GlcNAc...) Potential
	Glycosylation	218	1	N-linked (GlcNAc...) Potential
	Glycosylation	266	1	N-linked (GlcNAc...) Potential
	Disulfide bond	91 ↔ 94		Redox-active By similarity
	Disulfide bond	418 ↔ 430		By similarity
	Disulfide bond	476 ↔ 479		By similarity
	Disulfide bond	536 ↔ 539		By similarity
Natural variations
	Natural variant	126	1	K → E. Corresponds to variant rs12380852 [ dbSNP | Ensembl ].		VAR_027435
Experimental info
	Sequence conflict	96	1	G → A in CAC85331. Ref.1
	Sequence conflict	205	1	N → K in BAC87262. Ref.3
	Sequence conflict	224	1	R → W in CAC85331. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q6ZRP7 [UniParc]. Last modified July 24, 2007. Version 3. Checksum: 7F2B3F890AE657CF	FASTA	698	77,529
	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

References

	« Hide 'large scale' referencesShow '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: 14633699] [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: 15164053] [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: 14702039] [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: 17974005] [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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, MASS SPECTROMETRY.
+	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.
IPI	IPI00376394.
RefSeq	NP_859052.3. NM_181701.3.
UniGene	Hs.657864.
3D structure databases
ProteinModelPortal	Q6ZRP7.
SMR	Q6ZRP7. Positions 54-219, 317-571.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6ZRP7.
PTM databases
PhosphoSite	Q6ZRP7.
Polymorphism databases
DMDM	158958335.
Proteomic databases
PRIDE	Q6ZRP7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000358701; ENSP00000351536; ENSG00000165661.
GeneID	169714.
KEGG	hsa:169714.
UCSC	uc010nbi.1. human.
Organism-specific databases
CTD	169714.
GeneCards	GC09M139098.
H-InvDB	HIX0008541.
HGNC	HGNC:30249. QSOX2.
HPA	HPA012716.
MIM	612860. gene.
neXtProt	NX_Q6ZRP7.
PharmGKB	PA162400588.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000008045.
HOVERGEN	HBG080360.
InParanoid	Q6ZRP7.
OMA	ANSSAAW.
OrthoDB	EOG415GDC.
PhylomeDB	Q6ZRP7.
Gene expression databases
ArrayExpress	Q6ZRP7.
Bgee	Q6ZRP7.
CleanEx	HS_QSOX2.
Genevestigator	Q6ZRP7.
GermOnline	ENSG00000165661. Homo sapiens.
Family and domain databases
InterPro	IPR017905. ERV/ALR_sulphydryl_oxidase. IPR006863. Evr1_Alr. IPR012336. Thioredoxin-like_fold. IPR013766. Thioredoxin_domain. [Graphical view]
Gene3D	G3DSA:1.20.120.310. Evr1_Alr. 1 hit. G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KO	K10758.
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
NextBio	88829.
SOURCE	Search...

Entry information

Entry name

QSOX2_HUMAN

Accession

Primary (citable) accession number: Q6ZRP7
Secondary accession number(s): A2CEE0 , A6NLB0, Q5TB37, Q7Z7B6, Q86VV7, Q8N3G2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2006
Last sequence update:	July 24, 2007
Last modified:	January 25, 2012
This is version 77 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.