IL36A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IL36A_HUMAN
• UniProt AC: Q9UHA7
• Protein Name: Interleukin-36 alpha
• Gene Name: IL36A
• Organism: Homo sapiens (Human).
• Sequence Length: 158
• Subcellular Localization: Secreted .
• Protein Description: Cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP. Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. In cultured keratinocytes induces the expression of macrophage, T-cell, and neutrophil chemokines, such as CCL3, CCL4, CCL5, CCL2, CCL17, CCL22, CL20, CCL5, CCL2, CCL17, CCL22, CXCL8, CCL20 and CXCL1, and the production of proinflammatory cytokines such as TNF-alpha, IL-8 and IL-6. In cultured monocytes upregulates expression of IL-1A, IL-1B and IL-6. In myeloid dendritic cells involved in cell maturation by upregulating surface expression of CD83, CD86 and HLA-DR. In monocyte-derived dendritic cells facilitates dendritic cell maturation and drives T-cell proliferation. May play a role in proinflammatory effects in the lung..
• Protein Sequence: MEKALKIDTPQQGSIQDINHRVWVLQDQTLIAVPRKDRMSPVTIALISCRHVETLEKDRGNPIYLGLNGLNLCLMCAKVGDQPTLQLKEKDIMDLYNQPEPVKSFLFYHSQSGRNSTFESVAFPGWFIAVSSEGGCPLILTQELGKANTTDFGLTMLF

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
9	Phosphorylation	EKALKIDTPQQGSIQ CCCCCCCCCCCCCCE	26.86	21299198
40	Phosphorylation	VPRKDRMSPVTIALI EECCCCCCHHEEEEE	19.67	30257219
43	Phosphorylation	KDRMSPVTIALISCR CCCCCHHEEEEEECC	12.15	28634298
48	Phosphorylation	PVTIALISCRHVETL HHEEEEEECCCHHHH	13.12	26434552
54	Phosphorylation	ISCRHVETLEKDRGN EECCCHHHHHHHCCC	38.84	28634298
88	Ubiquitination	DQPTLQLKEKDIMDL CCCEEECCHHHHHHH	50.16	29967540
96	Nitrated tyrosine	EKDIMDLYNQPEPVK HHHHHHHHCCCCCCC	13.90	-
96	Phosphorylation	EKDIMDLYNQPEPVK HHHHHHHHCCCCCCC	13.90	19658100
96	Nitration	EKDIMDLYNQPEPVK HHHHHHHHCCCCCCC	13.90	16777052
96	Nitration	EKDIMDLYNQPEPVK HHHHHHHHCCCCCCC	13.90	16777052
104	Phosphorylation	NQPEPVKSFLFYHSQ CCCCCCCEEEEEECC	27.67	30206219

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

Oops, there are no upstream regulatory protein records of IL36A_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IL36A_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 IL36A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BRE1A_HUMAN	RNF20	physical	26186194
BRE1B_HUMAN	RNF40	physical	26186194
CARM1_HUMAN	CARM1	physical	26186194
CTF8_HUMAN	CHTF8	physical	26186194
BRE1A_HUMAN	RNF20	physical	28514442
CTF8_HUMAN	CHTF8	physical	28514442
BRE1B_HUMAN	RNF40	physical	28514442
EF1A2_HUMAN	EEF1A2	physical	28514442
ACTA_HUMAN	ACTA2	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
TLK2_HUMAN	TLK2	physical	28514442
CARM1_HUMAN	CARM1	physical	28514442

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

Nitration

"Nitroproteins from a human pituitary adenoma tissue discovered with anitrotyrosine affinity column and tandem mass spectrometry.";
Zhan X., Desiderio D.M.;
Anal. Biochem. 354:279-289(2006).
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-96, AND MASS SPECTROMETRY.
PubMed: 16777052