SODE_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SODE_HUMAN
• UniProt AC: P08294
• Protein Name: Extracellular superoxide dismutase [Cu-Zn]
• Gene Name: SOD3
• Organism: Homo sapiens (Human).
• Sequence Length: 240
• Subcellular Localization: Secreted, extracellular space. 99% of EC-SOD is anchored to heparan sulfate proteoglycans in the tissue interstitium, and 1% is located in the vasculature in equilibrium between the plasma and the endothelium.
• Protein Description: Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen..
• Protein Sequence: MLALLCSCLLLAAGASDAWTGEDSAEPNSDSAEWIRDMYAKVTEIWQEVMQRRDDDGALHAACQVQPSATLDAAQPRVTGVVLFRQLAPRAKLDAFFALEGFPTEPNSSSRAIHVHQFGDLSQGCESTGPHYNPLAVPHPQHPGDFGNFAVRDGSLWRYRAGLAASLAGPHSIVGRAVVVHAGEDDLGRGGNQASVENGNAGRRLACCVVGVCGPGLWERQAREHSERKKRRRESECKAA

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
24	Phosphorylation	DAWTGEDSAEPNSDS CCCCCCCCCCCCCCH	30.17	26657352
29	Phosphorylation	EDSAEPNSDSAEWIR CCCCCCCCCHHHHHH	43.59	26657352
29	O-linked_Glycosylation	EDSAEPNSDSAEWIR CCCCCCCCCHHHHHH	43.59	OGP
31	Phosphorylation	SAEPNSDSAEWIRDM CCCCCCCHHHHHHHH	28.10	26657352
107	N-linked_Glycosylation	EGFPTEPNSSSRAIH CCCCCCCCCCCCEEE	48.57	16335952
155	Phosphorylation	NFAVRDGSLWRYRAG CEEEECCCCEEECHH	29.10	24719451
159	Phosphorylation	RDGSLWRYRAGLAAS ECCCCEEECHHHHHH	8.01	22617229
166	Phosphorylation	YRAGLAASLAGPHSI ECHHHHHHHCCCCCE	17.10	22617229
172	Phosphorylation	ASLAGPHSIVGRAVV HHHCCCCCEECEEEE	23.31	22617229
195	Phosphorylation	GRGGNQASVENGNAG CCCCCCHHHHCCCHH	21.87	29759185
229	Glycation	AREHSERKKRRRESE HHHHHHHHHHHHHHH	46.72	-
229	N-linked_Glycosylation	AREHSERKKRRRESE HHHHHHHHHHHHHHH	46.72	1505778
230	Glycation	REHSERKKRRRESEC HHHHHHHHHHHHHHH	58.31	-
230	N-linked_Glycosylation	REHSERKKRRRESEC HHHHHHHHHHHHHHH	58.31	1505778

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SODE_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SODE_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SODE_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of SODE_HUMAN !!

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"The site of nonenzymic glycation of human extracellular-superoxidedismutase in vitro.";
Adachi T., Ohta H., Hayashi K., Hirano K., Marklund S.L.;
Free Radic. Biol. Med. 13:205-210(1992).
Cited for: GLYCATION AT LYS-229 AND LYS-230.
PubMed: 1505778

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107, AND MASSSPECTROMETRY.
PubMed: 19159218

"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-107, AND MASSSPECTROMETRY.
PubMed: 16335952