IL21R_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IL21R_HUMAN
• UniProt AC: Q9HBE5
• Protein Name: Interleukin-21 receptor
• Gene Name: IL21R
• Organism: Homo sapiens (Human).
• Sequence Length: 538
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: This is a receptor for interleukin-21..
• Protein Sequence: MPRGWAAPLLLLLLQGGWGCPDLVCYTDYLQTVICILEMWNLHPSTLTLTWQDQYEELKDEATSCSLHRSAHNATHATYTCHMDVFHFMADDIFSVNITDQSGNYSQECGSFLLAESIKPAPPFNVTVTFSGQYNISWRSDYEDPAFYMLKGKLQYELQYRNRGDPWAVSPRRKLISVDSRSVSLLPLEFRKDSSYELQVRAGPMPGSSYQGTWSEWSDPVIFQTQSEELKEGWNPHLLLLLLLVIVFIPAFWSLKTHPLWRLWKKIWAVPSPERFFMPLYKGCSGDFKKWVGAPFTGSSLELGPWSPEVPSTLEVYSCHPPRSPAKRLQLTELQEPAELVESDGVPKPSFWPTAQNSGGSAYSEERDRPYGLVSIDTVTVLDAEGPCTWPCSCEDDGYPALDLDAGLEPSPGLEDPLLDAGTTVLSCGCVSAGSPGLGGPLGSLLDRLKPPLADGEDWAGGLPWGGRSPGGVSESEAGSPLAGLDMDTFDSGFVGSDCSSPVECDFTSPGDEGPPRSYLRQWVVIPPPLSSPGPQAS

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
73	N-linked_Glycosylation	SLHRSAHNATHATYT HHHHHHCCCCCCEEE	46.37	22235133
95	N-linked_Glycosylation	FMADDIFSVNITDQS HHHCCEEEEECCCCC	18.00	22235133
97	N-linked_Glycosylation	ADDIFSVNITDQSGN HCCEEEEECCCCCCC	30.19	UniProtKB CARBOHYD
104	N-linked_Glycosylation	NITDQSGNYSQECGS ECCCCCCCCCCCCCC	38.23	UniProtKB CARBOHYD
125	N-linked_Glycosylation	IKPAPPFNVTVTFSG CCCCCCEEEEEEECC	34.03	UniProtKB CARBOHYD
135	N-linked_Glycosylation	VTFSGQYNISWRSDY EEECCEEEEEECCCC	17.58	UniProtKB CARBOHYD
137	Phosphorylation	FSGQYNISWRSDYED ECCEEEEEECCCCCC	16.88	24719451
170	Phosphorylation	RGDPWAVSPRRKLIS CCCCCCCCCCCEEEE	12.63	24719451
174	Malonylation	WAVSPRRKLISVDSR CCCCCCCEEEEECCC	51.99	30639696
201	Methylation	SSYELQVRAGPMPGS CCEEEEEEECCCCCC	22.36	115480237
214	C-linked_Glycosylation	GSSYQGTWSEWSDPV CCCCCCCCHHCCCCE	10.90	22235133
223	Methylation	EWSDPVIFQTQSEEL HCCCCEEEECCCHHH	7.00	-
236	C-linked_Glycosylation	ELKEGWNPHLLLLLL HHHCCCCHHHHHHHH	17.00	22235133
297	Phosphorylation	KWVGAPFTGSSLELG HHCCCCCCCCCCCCC	34.79	28270605
299	Phosphorylation	VGAPFTGSSLELGPW CCCCCCCCCCCCCCC	28.79	28270605
300	Phosphorylation	GAPFTGSSLELGPWS CCCCCCCCCCCCCCC	27.49	28270605
332	Phosphorylation	PAKRLQLTELQEPAE HHHHCCCEECCCCHH	22.99	24719451
354	Phosphorylation	PKPSFWPTAQNSGGS CCCCCCCCCCCCCCC	31.32	24719451

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

Oops, there are no upstream regulatory protein records of IL21R_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IL21R_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 IL21R_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WSB2_HUMAN	WSB2	physical	20059963

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 615207: IL21R immunodeficiency (IL21RID)
• Kegg Drug
• D09332: Denenicokin (USAN/INN)
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

C-linked Glycosylation

"Crystal structure of interleukin-21 receptor (IL-21R) bound to IL-21reveals that sugar chain interacting with WSXWS motif is integral partof IL-21R.";
Hamming O.J., Kang L., Svensson A., Karlsen J.L., Rahbek-Nielsen H.,Paludan S.R., Hjorth S.A., Bondensgaard K., Hartmann R.;
J. Biol. Chem. 287:9454-9460(2012).
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-232 IN COMPLEX WITH IL21,WSXWS MOTIF, GLYCOSYLATION AT ASN-73 AND TRP-214, FIBRONECTIN DOMAINS,AND DISULFIDE BONDS.
PubMed: 22235133

N-linked Glycosylation

"Crystal structure of interleukin-21 receptor (IL-21R) bound to IL-21reveals that sugar chain interacting with WSXWS motif is integral partof IL-21R.";
Hamming O.J., Kang L., Svensson A., Karlsen J.L., Rahbek-Nielsen H.,Paludan S.R., Hjorth S.A., Bondensgaard K., Hartmann R.;
J. Biol. Chem. 287:9454-9460(2012).
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-232 IN COMPLEX WITH IL21,WSXWS MOTIF, GLYCOSYLATION AT ASN-73 AND TRP-214, FIBRONECTIN DOMAINS,AND DISULFIDE BONDS.
PubMed: 22235133