CCL11_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CCL11_HUMAN
• UniProt AC: P51671
• Protein Name: Eotaxin
• Gene Name: CCL11
• Organism: Homo sapiens (Human).
• Sequence Length: 97
• Subcellular Localization: Secreted.
• Protein Description: In response to the presence of allergens, this protein directly promotes the accumulation of eosinophils, a prominent feature of allergic inflammatory reactions. Binds to CCR3..
• Protein Sequence: MKVSAALLWLLLIAAAFSPQGLAGPASVPTTCCFNLANRKIPLQRLESYRRITSGKCPQKAVIFKTKLAKDICADPKKKWVQDSMKYLDQKSPTPKP

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
53	Phosphorylation	LESYRRITSGKCPQK HHHHHHHCCCCCCCE	29.61	-
54	Phosphorylation	ESYRRITSGKCPQKA HHHHHHCCCCCCCEE	33.61	-
94	O-linked_Glycosylation	YLDQKSPTPKP---- HHHHCCCCCCC----	51.54	9578468
94	O-linked_Glycosylation	YLDQKSPTPKP---- HHHHCCCCCCC----	51.54	9578468

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

Oops, there are no upstream regulatory protein records of CCL11_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CCL11_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 CCL11_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CCL11_HUMAN	CCL11	physical	9712872

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

O-linked Glycosylation

"Delayed production of biologically active O-glycosylated forms ofhuman eotaxin by tumor-necrosis-factor-alpha-stimulated dermalfibroblasts.";
Noso N., Bartels J., Mallet A.I., Mochizuki M., Christophers E.,Schroeder J.-M.;
Eur. J. Biochem. 253:114-122(1998).
Cited for: GLYCOSYLATION AT THR-94.
PubMed: 9578468