I22R1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: I22R1_HUMAN
• UniProt AC: Q8N6P7
• Protein Name: Interleukin-22 receptor subunit alpha-1
• Gene Name: IL22RA1
• Organism: Homo sapiens (Human).
• Sequence Length: 574
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: Component of the receptor for IL20, IL22 and IL24. Component of IL22 receptor formed by IL22RA1 and IL10RB enabling IL22 signaling via JAK/STAT pathways. IL22 also induces activation of MAPK1/MAPK3 and Akt kinases pathways. Component of one of the receptor for IL20 and IL24 formed by IL22RA1 and IL20RB also signaling through STATs activation. Mediates IL24 antiangiogenic activity as well as IL24 inhibitory effect on endothelial cell tube formation and differentiation..
• Protein Sequence: MRTLLTILTVGSLAAHAPEDPSDLLQHVKFQSSNFENILTWDSGPEGTPDTVYSIEYKTYGERDWVAKKGCQRITRKSCNLTVETGNLTELYYARVTAVSAGGRSATKMTDRFSSLQHTTLKPPDVTCISKVRSIQMIVHPTPTPIRAGDGHRLTLEDIFHDLFYHLELQVNRTYQMHLGGKQREYEFFGLTPDTEFLGTIMICVPTWAKESAPYMCRVKTLPDRTWTYSFSGAFLFSMGFLVAVLCYLSYRYVTKPPAPPNSLNVQRVLTFQPLRFIQEHVLIPVFDLSGPSSLAQPVQYSQIRVSGPREPAGAPQRHSLSEITYLGQPDISILQPSNVPPPQILSPLSYAPNAAPEVGPPSYAPQVTPEAQFPFYAPQAISKVQPSSYAPQATPDSWPPSYGVCMEGSGKDSPTGTLSSPKHLRPKGQLQKEPPAGSCMLGGLSLQEVTSLAMEESQEAKSLHQPLGICTDRTSDPNVLHSGEEGTPQYLKGQLPLLSSVQIEGHPMSLPLQPPSRPCSPSDQGPSPWGLLESLVCPKDEAKSPAPETSDLEQPTELDSLFRGLALTVQWES

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
3	Phosphorylation	-----MRTLLTILTV -----CCHHHHHHHH	25.48	-
40	Phosphorylation	SNFENILTWDSGPEG CCCCCEEEECCCCCC	24.35	22468782
43	Phosphorylation	ENILTWDSGPEGTPD CCEEEECCCCCCCCC	48.05	22468782
48	Phosphorylation	WDSGPEGTPDTVYSI ECCCCCCCCCCEEEE	19.14	22468782
51	Phosphorylation	GPEGTPDTVYSIEYK CCCCCCCCEEEEEEE	23.65	22468782
59	Phosphorylation	VYSIEYKTYGERDWV EEEEEEEECCCCHHH	35.54	22468782
80	N-linked_Glycosylation	RITRKSCNLTVETGN HCCCCCCCEEEECCC	45.93	UniProtKB CARBOHYD
134	Phosphorylation	TCISKVRSIQMIVHP EEEEECCEEEEEEEC	21.84	29083192
142	Phosphorylation	IQMIVHPTPTPIRAG EEEEEECCCCCCCCC	25.56	29083192
144	Phosphorylation	MIVHPTPTPIRAGDG EEEECCCCCCCCCCC	33.55	29083192
172	N-linked_Glycosylation	YHLELQVNRTYQMHL HHHHEEECCEEEEEE	20.02	UniProtKB CARBOHYD
186	Phosphorylation	LGGKQREYEFFGLTP ECCCCCEEEEECCCC	21.89	-
215	Phosphorylation	WAKESAPYMCRVKTL CHHHCCCEEEEEEEC	14.46	-
251	Phosphorylation	AVLCYLSYRYVTKPP HHHHHHHHHHCCCCC	11.90	22817900
301	Phosphorylation	SLAQPVQYSQIRVSG HHCCCCEEEEEEECC	11.63	22817900
410	Phosphorylation	YGVCMEGSGKDSPTG CCEEECCCCCCCCCC	29.39	-
414	Phosphorylation	MEGSGKDSPTGTLSS ECCCCCCCCCCCCCC	28.04	24275569
421	Phosphorylation	SPTGTLSSPKHLRPK CCCCCCCCCCCCCCC	40.87	19664994

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
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW12	Q6X9E4	PMID:26171402

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of I22R1_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 I22R1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IL22_HUMAN	IL22	physical	11035029
STAT3_HUMAN	STAT3	physical	21988832

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.