dbPTM

QSOX1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	QSOX1_HUMAN
UniProt AC	O00391
Protein Name	Sulfhydryl oxidase 1
Gene Name	QSOX1
Organism	Homo sapiens (Human).
Sequence Length	747
Subcellular Localization	Isoform 1: Golgi apparatus membrane Single-pass membrane protein. Isoform 2: Secreted, extracellular space. Found in the extracellular medium of quiescent cells but is not found in proliferating cells.
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. In fibroblasts, it may have tumor-suppressing capabilities being involved in growth regulation..
Protein Sequence	MRRCNSGSGPPPSLLLLLLWLLAVPGANAAPRSALYSPSDPLTLLQADTVRGAVLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETNSAVCRDFNIPGFPTVRFFKAFTKNGSGAVFPVAGADVQTLRERLIDALESHHDTWPPACPPLEPAKLEEIDGFFARNNEEYLALIFEKGGSYLGREVALDLSQHKGVAVRRVLNTEANVVRKFGVTDFPSCYLLFRNGSVSRVPVLMESRSFYTAYLQRLSGLTREAAQTTVAPTTANKIAPTVWKLADRSKIYMADLESALHYILRIEVGRFPVLEGQRLVALKKFVAVLAKYFPGRPLVQNFLHSVNEWLKRQKRNKIPYSFFKTALDDRKEGAVLAKKVNWIGCQGSEPHFRGFPCSLWVLFHFLTVQAARQNVDHSQEAAKAKEVLPAIRGYVHYFFGCRDCASHFEQMAAASMHRVGSPNAAVLWLWSSHNRVNARLAGAPSEDPQFPKVQWPPRELCSACHNERLDVPVWDVEATLNFLKAHFSPSNIILDFPAAGSAARRDVQNVAAAPELAMGALELESRNSTLDPGKPEMMKSPTNTTPHVPAEGPEASRPPKLHPGLRAAPGQEPPEHMAELQRNEQEQPLGQWHLSKRDTGAALLAESRAEKNRLWGPLEVRRVGRSSKQLVDIPEGQLEARAGRGRGQWLQVLGGGFSYLDISLCVGLYSLSFMGLLAMYTYFQAKIRALKGHAGHPAA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	Phosphorylation	GANAAPRSALYSPSD CCCCCCCHHCCCCCC	22.90	26091039
49	Phosphorylation	LTLLQADTVRGAVLG CHHHCCCCCCCCCCC	18.34	-
130	N-linked_Glycosylation	FFKAFTKNGSGAVFP EEEEECCCCCCCEEE	46.97	29757379
194 (in isoform 2)	Ubiquitination	-	58.80	21906983
194 (in isoform 1)	Ubiquitination	-	58.80	21906983
194	Ubiquitination	YLALIFEKGGSYLGR HEEEEEECCCCCCCC	58.80	21906983
243	N-linked_Glycosylation	SCYLLFRNGSVSRVP CEEEEEECCCCCCCE	39.49	29757379
255	Phosphorylation	RVPVLMESRSFYTAY CCEEEECCCHHHHHH	21.18	22817900
259	Phosphorylation	LMESRSFYTAYLQRL EECCCHHHHHHHHHH	7.54	29759185
260	Phosphorylation	MESRSFYTAYLQRLS ECCCHHHHHHHHHHH	13.55	29759185
267	Phosphorylation	TAYLQRLSGLTREAA HHHHHHHHCCCHHHH	33.67	29759185
270	Phosphorylation	LQRLSGLTREAAQTT HHHHHCCCHHHHHHC	29.95	29759185
276	O-linked_Glycosylation	LTREAAQTTVAPTTA CCHHHHHHCCCCCCH	20.64	55827049
277	O-linked_Glycosylation	TREAAQTTVAPTTAN CHHHHHHCCCCCCHH	11.55	55827055
281	O-linked_Glycosylation	AQTTVAPTTANKIAP HHHCCCCCCHHHHHH	28.89	55827061
282	O-linked_Glycosylation	QTTVAPTTANKIAPT HHCCCCCCHHHHHHH	27.46	55827065
285	Ubiquitination	VAPTTANKIAPTVWK CCCCCHHHHHHHHHH	37.47	-
289	O-linked_Glycosylation	TANKIAPTVWKLADR CHHHHHHHHHHHHCC	29.94	55828151
297	Phosphorylation	VWKLADRSKIYMADL HHHHHCCCCEEECCH	24.77	20068231
300	Phosphorylation	LADRSKIYMADLESA HHCCCCEEECCHHHH	7.03	20068231
306	Phosphorylation	IYMADLESALHYILR EEECCHHHHHHHHHH	43.35	20068231
310	Phosphorylation	DLESALHYILRIEVG CHHHHHHHHHHHCCC	11.51	20068231
426	Phosphorylation	ARQNVDHSQEAAKAK HHHCCCCHHHHHHHH	25.83	24972180
493	O-linked_Glycosylation	ARLAGAPSEDPQFPK HHHCCCCCCCCCCCC	54.84	55835703
549	O-linked_Glycosylation	LDFPAAGSAARRDVQ EECCCCCHHHHHHHH	17.65	55827985
575	N-linked_Glycosylation	ALELESRNSTLDPGK HHHHHHCCCCCCCCC	48.93	UniProtKB CARBOHYD
576	Phosphorylation	LELESRNSTLDPGKP HHHHHCCCCCCCCCH	29.27	-
576	O-linked_Glycosylation	LELESRNSTLDPGKP HHHHHCCCCCCCCCH	29.27	68736639
577	O-linked_Glycosylation	ELESRNSTLDPGKPE HHHHCCCCCCCCCHH	38.44	68736645
577	Phosphorylation	ELESRNSTLDPGKPE HHHHCCCCCCCCCHH	38.44	-
588	O-linked_Glycosylation	GKPEMMKSPTNTTPH CCHHHCCCCCCCCCC	21.04	11362185
588	Phosphorylation	GKPEMMKSPTNTTPH CCHHHCCCCCCCCCC	21.04	-
590	Phosphorylation	PEMMKSPTNTTPHVP HHHCCCCCCCCCCCC	52.90	-
590 (in isoform 2)	Phosphorylation	-	52.90	25159151
590	O-linked_Glycosylation	PEMMKSPTNTTPHVP HHHCCCCCCCCCCCC	52.90	55832267
592	Phosphorylation	MMKSPTNTTPHVPAE HCCCCCCCCCCCCCC	44.15	-
592	O-linked_Glycosylation	MMKSPTNTTPHVPAE HCCCCCCCCCCCCCC	44.15	11362193
593	Phosphorylation	MKSPTNTTPHVPAEG CCCCCCCCCCCCCCC	17.29	-
593	O-linked_Glycosylation	MKSPTNTTPHVPAEG CCCCCCCCCCCCCCC	17.29	68736651
604	O-linked_Glycosylation	PAEGPEASRPPKLHP CCCCCCCCCCCCCCC	43.59	55832281
643	O-linked_Glycosylation	PLGQWHLSKRDTGAA CCCCCCCCHHHHHHH	16.86	55824161
647	O-linked_Glycosylation	WHLSKRDTGAALLAE CCCCHHHHHHHHHHH	32.52	55830539
647	Phosphorylation	WHLSKRDTGAALLAE CCCCHHHHHHHHHHH	32.52	22210691
655	O-linked_Glycosylation	GAALLAESRAEKNRL HHHHHHHHHHHHCCC	31.05	55830545
655	Phosphorylation	GAALLAESRAEKNRL HHHHHHHHHHHHCCC	31.05	22210691
676	Ubiquitination	RRVGRSSKQLVDIPE HHCCCCCCCEEECCC	49.23	2190698
676 (in isoform 1)	Ubiquitination	-	49.23	21906983
739	Ubiquitination	QAKIRALKGHAGHPA HHHHHHHCCCCCCCC	47.90	-

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
426	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of QSOX1_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 QSOX1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
UB2D2_HUMAN	UBE2D2	physical	22582951

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 QSOX1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130, AND MASSSPECTROMETRY.	16335952 [Abstract]