I10R2_HUMAN - dbPTM
I10R2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID I10R2_HUMAN
UniProt AC Q08334
Protein Name Interleukin-10 receptor subunit beta
Gene Name IL10RB
Organism Homo sapiens (Human).
Sequence Length 325
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Shared cell surface receptor required for the activation of five class 2 cytokines: IL10, IL22, IL26, IL28, and IFNL1. 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..
Protein Sequence MAWSLGSWLGGCLLVSALGMVPPPENVRMNSVNFKNILQWESPAFAKGNLTFTAQYLSYRIFQDKCMNTTLTECDFSSLSKYGDHTLRVRAEFADEHSDWVNITFCPVDDTIIGPPGMQVEVLADSLHMRFLAPKIENEYETWTMKNVYNSWTYNVQYWKNGTDEKFQITPQYDFEVLRNLEPWTTYCVQVRGFLPDRNKAGEWSEPVCEQTTHDETVPSWMVAVILMASVFMVCLALLGCFALLWCVYKKTKYAFSPRNSLPQHLKEFLGHPHHNTLLFFSFPLSDENDVFDKLSVIAEDSESGKQNPGDSCSLGTPPGQGPQS
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 Orthologous
Protein Cluster
49N-linked_GlycosylationSPAFAKGNLTFTAQY
CCCHHCCCEEEEEEH
34.89UniProtKB CARBOHYD
68N-linked_GlycosylationIFQDKCMNTTLTECD
HHHHHHCCCCCCCCC
39.11UniProtKB CARBOHYD
69PhosphorylationFQDKCMNTTLTECDF
HHHHHCCCCCCCCCH
9.0426074081
70PhosphorylationQDKCMNTTLTECDFS
HHHHCCCCCCCCCHH
27.0326074081
72PhosphorylationKCMNTTLTECDFSSL
HHCCCCCCCCCHHHH
32.2626074081
77PhosphorylationTLTECDFSSLSKYGD
CCCCCCHHHHHHCCC
19.6726074081
78PhosphorylationLTECDFSSLSKYGDH
CCCCCHHHHHHCCCE
36.3326074081
80PhosphorylationECDFSSLSKYGDHTL
CCCHHHHHHCCCEEE
26.2726074081
82PhosphorylationDFSSLSKYGDHTLRV
CHHHHHHCCCEEEEE
25.1426074081
86PhosphorylationLSKYGDHTLRVRAEF
HHHCCCEEEEEEEEE
22.4726074081
102N-linked_GlycosylationDEHSDWVNITFCPVD
CCCCCCEEEEEECCC
24.27UniProtKB CARBOHYD
140PhosphorylationAPKIENEYETWTMKN
HHHCCCEEEEEEEEC
30.1827732954
142PhosphorylationKIENEYETWTMKNVY
HCCCEEEEEEEECCC
25.9027732954
144PhosphorylationENEYETWTMKNVYNS
CCEEEEEEEECCCCC
26.2027732954
161N-linked_GlycosylationYNVQYWKNGTDEKFQ
EEEEEEECCCCCCEE
44.44UniProtKB CARBOHYD
252PhosphorylationLWCVYKKTKYAFSPR
HHHHHHHHCCCCCCC
25.7421712546
253UbiquitinationWCVYKKTKYAFSPRN
HHHHHHHCCCCCCCC
43.3833845483
257PhosphorylationKKTKYAFSPRNSLPQ
HHHCCCCCCCCCCCH
18.1221712546
261PhosphorylationYAFSPRNSLPQHLKE
CCCCCCCCCCHHHHH
42.5825056879
296PhosphorylationNDVFDKLSVIAEDSE
CCHHHHHEEEEECCC
19.7426657352
302PhosphorylationLSVIAEDSESGKQNP
HEEEEECCCCCCCCC
25.7625159151
304PhosphorylationVIAEDSESGKQNPGD
EEEECCCCCCCCCCC
56.0721815630
306UbiquitinationAEDSESGKQNPGDSC
EECCCCCCCCCCCCC
57.0633845483
312PhosphorylationGKQNPGDSCSLGTPP
CCCCCCCCCCCCCCC
16.1229514088
314PhosphorylationQNPGDSCSLGTPPGQ
CCCCCCCCCCCCCCC
33.5129514088
317PhosphorylationGDSCSLGTPPGQGPQ
CCCCCCCCCCCCCCC
31.4423663014
325PhosphorylationPPGQGPQS-------
CCCCCCCC-------
45.3722115753

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

Oops, there are no upstream regulatory protein records of I10R2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of I10R2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of I10R2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
I10R1_HUMANIL10RAphysical
9312047

Drug and Disease Associations
Kegg Disease
H01227 Inflammatory bowel disease
OMIM Disease
612567Inflammatory bowel disease 25 (IBD25)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of I10R2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-317, AND MASSSPECTROMETRY.

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