SPON2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SPON2_HUMAN
• UniProt AC: Q9BUD6
• Protein Name: Spondin-2
• Gene Name: SPON2
• Organism: Homo sapiens (Human).
• Sequence Length: 331
• Subcellular Localization: Secreted, extracellular space, extracellular matrix.
• Protein Description: Cell adhesion protein that promotes adhesion and outgrowth of hippocampal embryonic neurons. Binds directly to bacteria and their components and functions as an opsonin for macrophage phagocytosis of bacteria. Essential in the initiation of the innate immune response and represents a unique pattern-recognition molecule in the ECM for microbial pathogens (By similarity). Binds bacterial lipopolysaccharide (LPS)..
• Protein Sequence: MENPSPAAALGKALCALLLATLGAAGQPLGGESICSARALAKYSITFTGKWSQTAFPKQYPLFRPPAQWSSLLGAAHSSDYSMWRKNQYVSNGLRDFAERGEAWALMKEIEAAGEALQSVHEVFSAPAVPSGTGQTSAELEVQRRHSLVSFVVRIVPSPDWFVGVDSLDLCDGDRWREQAALDLYPYDAGTDSGFTFSSPNFATIPQDTVTEITSSSPSHPANSFYYPRLKALPPIARVTLVRLRQSPRAFIPPAPVLPSRDNEIVDSASVPETPLDCEVSLWSSWGLCGGHCGRLGTKSRTRYVRVQPANNGSPCPELEEEAECVPDNCV

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
43	Phosphorylation	SARALAKYSITFTGK HHHHHEEEEEEEEEC	10.33	29083192
44	Phosphorylation	ARALAKYSITFTGKW HHHHEEEEEEEEECC	17.91	29083192
46	Phosphorylation	ALAKYSITFTGKWSQ HHEEEEEEEEECCCC	14.81	29083192
48	Phosphorylation	AKYSITFTGKWSQTA EEEEEEEEECCCCCC	29.24	29083192
52	Phosphorylation	ITFTGKWSQTAFPKQ EEEEECCCCCCCCCC	22.57	29083192
89	Phosphorylation	SMWRKNQYVSNGLRD HHHHHCHHHHHCHHH	18.42	-
147	Phosphorylation	LEVQRRHSLVSFVVR EEHHHHHCCEEEEEE	28.75	24719451
216	O-linked_Glycosylation	TVTEITSSSPSHPAN CEEEECCCCCCCCCH	37.30	OGP
260	Phosphorylation	PPAPVLPSRDNEIVD CCCCCCCCCCCCCCC	48.37	-
283	C-linked_Glycosylation	LDCEVSLWSSWGLCG CCCEEEEHHHCCCCC	5.25	19153605
304	Phosphorylation	GTKSRTRYVRVQPAN CCCCCCEEEEEEECC	7.62	-

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

Oops, there are no upstream regulatory protein records of SPON2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SPON2_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 SPON2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of SPON2_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

C-linked Glycosylation

"Structure of the F-spondin domain of mindin, an integrin ligand andpattern recognition molecule.";
Li Y., Cao C., Jia W., Yu L., Mo M., Wang Q., Huang Y., Lim J.-M.,Ishihara M., Wells L., Azadi P., Robinson H., He Y.-W., Zhang L.,Mariuzza R.A.;
EMBO J. 28:286-297(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-249 IN COMPLEX WITH METALIONS, PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, SUBUNIT,GLYCOSYLATION AT TRP-283, INTERACTION WITH INTEGRIN AND BACTERIALLIPOPOLYSACCHARIDE, MUTAGENESIS OF GLU-122 AND GLU-141, AND DISULFIDEBOND.
PubMed: 19153605