INLR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: INLR1_HUMAN
• UniProt AC: Q8IU57
• Protein Name: Interferon lambda receptor 1
• Gene Name: IFNLR1
• Organism: Homo sapiens (Human).
• Sequence Length: 520
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state. Determines the cell type specificity of the lambda interferon action. Shows a more restricted pattern of expression in the epithelial tissues thereby limiting responses to lambda interferons primarily to epithelial cells of the respiratory, gastrointestinal, and reproductive tracts. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium..
• Protein Sequence: MAGPERWGPLLLCLLQAAPGRPRLAPPQNVTLLSQNFSVYLTWLPGLGNPQDVTYFVAYQSSPTRRRWREVEECAGTKELLCSMMCLKKQDLYNKFKGRVRTVSPSSKSPWVESEYLDYLFEVEPAPPVLVLTQTEEILSANATYQLPPCMPPLDLKYEVAFWKEGAGNKTLFPVTPHGQPVQITLQPAASEHHCLSARTIYTFSVPKYSKFSKPTCFLLEVPEANWAFLVLPSLLILLLVIAAGGVIWKTLMGNPWFQRAKMPRALDFSGHTHPVATFQPSRPESVNDLFLCPQKELTRGVRPTPRVRAPATQQTRWKKDLAEDEEEEDEEDTEDGVSFQPYIEPPSFLGQEHQAPGHSEAGGVDSGRPRAPLVPSEGSSAWDSSDRSWASTVDSSWDRAGSSGYLAEKGPGQGPGGDGHQESLPPPEFSKDSGFLEELPEDNLSSWATWGTLPPEPNLVPGGPPVSLQTLTFCWESSPEEEEEARESEIEDSDAGSWGAESTQRTEDRGRTLGHYMAR

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
29	N-linked_Glycosylation	PRLAPPQNVTLLSQN CCCCCCCCEEEEECC		20934432
36	N-linked_Glycosylation	NVTLLSQNFSVYLTW CEEEEECCEEEEEEE		20934432
93	Phosphorylation	CLKKQDLYNKFKGRV HHHHHHHHHHHCCCE		24905233
104	Phosphorylation	KGRVRTVSPSSKSPW CCCEEECCCCCCCCC		26546556
106	Phosphorylation	RVRTVSPSSKSPWVE CEEECCCCCCCCCEE		26546556
107	Phosphorylation	VRTVSPSSKSPWVES EEECCCCCCCCCEEH		26546556
142	N-linked_Glycosylation	TEEILSANATYQLPP CHHHHHCCCEECCCC		20934432
169	N-linked_Glycosylation	FWKEGAGNKTLFPVT EEECCCCCCEEEEEC		UniProtKB CARBOHYD
205	Phosphorylation	ARTIYTFSVPKYSKF EEEEEEEECCCCCCC		23911959
209	Phosphorylation	YTFSVPKYSKFSKPT EEEECCCCCCCCCCE		23911959
210	Phosphorylation	TFSVPKYSKFSKPTC EEECCCCCCCCCCEE		23911959
334	Phosphorylation	EEEDEEDTEDGVSFQ CCCCCCCCCCCCCCC		28787133
343	Phosphorylation	DGVSFQPYIEPPSFL CCCCCCCCCCCCHHC		28787133
498	Phosphorylation	IEDSDAGSWGAESTQ CCCCCCCCCCCCCCC		26471730
517	Phosphorylation	RGRTLGHYMAR---- HCCCHHHHCCC----		27642862

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

Oops, there are no upstream regulatory protein records of INLR1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of INLR1_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 INLR1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of INLR1_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
• D10078: Peginterferon lambda-1a (USAN)
• DrugBank
• There are no disease associations of PTM sites.