QSOX2_HUMAN - dbPTM
QSOX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID QSOX2_HUMAN
UniProt AC Q6ZRP7
Protein Name Sulfhydryl oxidase 2
Gene Name QSOX2
Organism Homo sapiens (Human).
Sequence Length 698
Subcellular Localization Membrane
Single-pass membrane protein . Secreted . Cell membrane
Single-pass membrane protein . Nucleus membrane
Single-pass membrane protein . Seems to be predominantly targeted to the nuclear and outer plasma membrane.
Protein Description 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..
Protein Sequence MAAAGAAVARSPGIGAGPALRARRSPPPRAARLPRLLVLLAAAAVGPGAGGAARLYRAGEDAVWVLDSGSVRGATANSSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMEEKNQAVCHDYDIHFYPTFRYFKAFTKEFTTGENFKGPDRELRTVRQTMIDFLQNHTEGSRPPACPRLDPIQPSDVLSLLDNRGSHYVAIVFESNSSYLGREVILDLIPYESIVVTRALDGDKAFLEKLGVSSVPSCYLIYPNGSHGLINVVKPLRAFFSSYLKSLPDVRKKSLPLPEKPHKEENSEIVVWREFDKSKLYTVDLESGLHYLLRVELAAHKSLAGAELKTLKDFVTVLAKLFPGRPPVKKLLEMLQEWLASLPLDRIPYNAVLDLVNNKMRISGIFLTNHIKWVGCQGSRSELRGYPCSLWKLFHTLTVEASTHPDALVGTGFEDDPQAVLQTMRRYVHTFFGCKECGEHFEEMAKESMDSVKTPDQAILWLWKKHNMVNGRLAGHLSEDPRFPKLQWPTPDLCPACHEEIKGLASWDEGHVLTFLKQHYGRDNLLDTYSADQGDSSEGGTLARGEEEEKRLTPPEVSHGDRDTQSVRPPGALGPRPALPESLHHSLDGKLQSLDGPGAHKEVGGAAPFLGVDFSSLDMSLCVVLYVASSLFLMVMYFFFRVRSRRWKVKHHHPAV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
11PhosphorylationAGAAVARSPGIGAGP
CCCCHHCCCCCCCCH		20.1027251275
25PhosphorylationPALRARRSPPPRAAR
HHHHHCCCCCCHHHH		35.8830266825
70PhosphorylationVWVLDSGSVRGATAN
EEEECCCCCCCCCCC		16.7630387612
77N-linked_GlycosylationSVRGATANSSAAWLV
CCCCCCCCCHHHHHH		31.94UniProtKB CARBOHYD
109MethylationRALAGDVRDWASAIR
HHHHHCHHHHHHHHH		38.19115489797
141O-linked_GlycosylationYDIHFYPTFRYFKAF
CEECCCCCHHHHHHH		14.90OGP
146UbiquitinationYPTFRYFKAFTKEFT
CCCHHHHHHHHCCCC		33.39-
149O-linked_GlycosylationFRYFKAFTKEFTTGE
HHHHHHHHCCCCCCC		34.2355832001
153O-linked_GlycosylationKAFTKEFTTGENFKG
HHHHCCCCCCCCCCC		34.6855826353
154O-linked_GlycosylationAFTKEFTTGENFKGP
HHHCCCCCCCCCCCC		48.0655826359
159UbiquitinationFTTGENFKGPDRELR
CCCCCCCCCCCHHHH		79.6429967540
178N-linked_GlycosylationTMIDFLQNHTEGSRP
HHHHHHHHCCCCCCC		46.31UniProtKB CARBOHYD
183O-linked_GlycosylationLQNHTEGSRPPACPR
HHHCCCCCCCCCCCC		35.07OGP
197O-linked_GlycosylationRLDPIQPSDVLSLLD
CCCCCCHHHHHHHHC		24.79OGP
197PhosphorylationRLDPIQPSDVLSLLD
CCCCCCHHHHHHHHC		24.7920068231
201PhosphorylationIQPSDVLSLLDNRGS
CCHHHHHHHHCCCCC		27.0820068231
208PhosphorylationSLLDNRGSHYVAIVF
HHHCCCCCCEEEEEE		14.3825907765
210PhosphorylationLDNRGSHYVAIVFES
HCCCCCCEEEEEEEC		8.0225907765
217PhosphorylationYVAIVFESNSSYLGR
EEEEEEECCCCCCCC		30.4625907765
218N-linked_GlycosylationVAIVFESNSSYLGRE
EEEEEECCCCCCCCE		27.98UniProtKB CARBOHYD
219PhosphorylationAIVFESNSSYLGREV
EEEEECCCCCCCCEE		29.6425907765
220PhosphorylationIVFESNSSYLGREVI
EEEECCCCCCCCEEH		28.7325907765
221PhosphorylationVFESNSSYLGREVIL
EEECCCCCCCCEEHH		17.0125907765
246UbiquitinationTRALDGDKAFLEKLG
EEECCCCHHHHHHHC		46.71-
2462-HydroxyisobutyrylationTRALDGDKAFLEKLG
EEECCCCHHHHHHHC		46.71-
266N-linked_GlycosylationSCYLIYPNGSHGLIN
EEEEECCCCCCCCHH		47.86UniProtKB CARBOHYD
296PhosphorylationLPDVRKKSLPLPEKP
CCCHHHHCCCCCCCC		37.9521406692
323PhosphorylationEFDKSKLYTVDLESG
ECCCCCCEEEECCCH		14.41-
324PhosphorylationFDKSKLYTVDLESGL
CCCCCCEEEECCCHH		20.27-
358PhosphorylationKTLKDFVTVLAKLFP
HHHHHHHHHHHHHCC		15.1420068231
445O-linked_GlycosylationTLTVEASTHPDALVG
EEEECCCCCCCCCCC		44.46OGP
453O-linked_GlycosylationHPDALVGTGFEDDPQ
CCCCCCCCCCCCCHH		31.08OGP
465PhosphorylationDPQAVLQTMRRYVHT
CHHHHHHHHHHHHHH		14.4224719451
520PhosphorylationGRLAGHLSEDPRFPK
CCCCCCCCCCCCCCC		33.9929978859
520O-linked_GlycosylationGRLAGHLSEDPRFPK
CCCCCCCCCCCCCCC		33.99OGP
532PhosphorylationFPKLQWPTPDLCPAC
CCCCCCCCCCCCHHH		26.8625690035
562PhosphorylationLTFLKQHYGRDNLLD
HHHHHHHHCCCCCCC		16.0321406692
570PhosphorylationGRDNLLDTYSADQGD
CCCCCCCCEECCCCC		21.2423403867
571PhosphorylationRDNLLDTYSADQGDS
CCCCCCCEECCCCCC		11.0923403867
572PhosphorylationDNLLDTYSADQGDSS
CCCCCCEECCCCCCC		27.7130266825
578PhosphorylationYSADQGDSSEGGTLA
EECCCCCCCCCCCCC		36.7922167270
579PhosphorylationSADQGDSSEGGTLAR
ECCCCCCCCCCCCCC		45.0325463755
579O-linked_GlycosylationSADQGDSSEGGTLAR
ECCCCCCCCCCCCCC		45.03OGP
583PhosphorylationGDSSEGGTLARGEEE
CCCCCCCCCCCCHHH		28.2730266825
595O-linked_GlycosylationEEEEKRLTPPEVSHG
HHHHHCCCCCCCCCC		40.61OGP
600O-linked_GlycosylationRLTPPEVSHGDRDTQ
CCCCCCCCCCCCCCC		21.79OGP
608O-linked_GlycosylationHGDRDTQSVRPPGAL
CCCCCCCCCCCCCCC		23.37OGP
624O-linked_GlycosylationPRPALPESLHHSLDG
CCCCCCHHHHHHCCC		30.94OGP
635O-linked_GlycosylationSLDGKLQSLDGPGAH
HCCCCCCCCCCCCCC		38.5755832717
657PhosphorylationPFLGVDFSSLDMSLC
CCCCCCHHHCCHHHH		26.0627251275
658PhosphorylationFLGVDFSSLDMSLCV
CCCCCHHHCCHHHHH		28.5127251275
662PhosphorylationDFSSLDMSLCVVLYV
CHHHCCHHHHHHHHH		20.4827251275
668PhosphorylationMSLCVVLYVASSLFL
HHHHHHHHHHHHHHH		5.1627251275
672PhosphorylationVVLYVASSLFLMVMY
HHHHHHHHHHHHHHH		17.2527251275
679PhosphorylationSLFLMVMYFFFRVRS
HHHHHHHHHHHHHHH		5.9427251275
692UbiquitinationRSRRWKVKHHHPAV-
HHHCCCCCCCCCCC-		33.2333845483
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of QSOX2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of QSOX2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of QSOX2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NP1L1_HUMANNAP1L1physical
26496610
SNF5_HUMANSMARCB1physical
26496610
TTC1_HUMANTTC1physical
26496610
C2CD5_HUMANC2CD5physical
26496610
CEPT1_HUMANCEPT1physical
26496610
NBEL2_HUMANNBEAL2physical
26496610
ORC3_HUMANORC3physical
26496610
XRN1_HUMANXRN1physical
26496610
IMPCT_HUMANIMPACTphysical
26496610
TUT7_HUMANZCCHC6physical
26496610
CEP44_HUMANCEP44physical
26496610
FBX30_HUMANFBXO30physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of QSOX2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, AND MASSSPECTROMETRY.

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