IL6RA_HUMAN - dbPTM
IL6RA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IL6RA_HUMAN
UniProt AC P08887
Protein Name Interleukin-6 receptor subunit alpha
Gene Name IL6R
Organism Homo sapiens (Human).
Sequence Length 468
Subcellular Localization Isoform 1: Basolateral cell membrane
Single-pass type I membrane protein.
Isoform 2: Secreted.
Protein Description Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation may lead to the regulation of the immune response, acute-phase reactions and hematopoiesis.; Low concentration of a soluble form of IL6 receptor acts as an agonist of IL6 activity..
Protein Sequence MLAVGCALLAALLAAPGAALAPRRCPAQEVARGVLTSLPGDSVTLTCPGVEPEDNATVHWVLRKPAAGSHPSRWAGMGRRLLLRSVQLHDSGNYSCYRAGRPAGTVHLLVDVPPEEPQLSCFRKSPLSNVVCEWGPRSTPSLTTKAVLLVRKFQNSPAEDFQEPCQYSQESQKFSCQLAVPEGDSSFYIVSMCVASSVGSKFSKTQTFQGCGILQPDPPANITVTAVARNPRWLSVTWQDPHSWNSSFYRLRFELRYRAERSKTFTTWMVKDLQHHCVIHDAWSGLRHVVQLRAQEEFGQGEWSEWSPEAMGTPWTESRSPPAENEVSTPMQALTTNKDDDNILFRDSANATSLPVQDSSSVPLPTFLVAGGSLAFGTLLCIAIVLRFKKTWKLRALKEGKTSMHPPYSLGQLVPERPRPTPVLVPLISPPVSPSSLGSDNTSSHNRPDARDPRSPYDISNTDYFFPR
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
55N-linked_GlycosylationPGVEPEDNATVHWVL
CCCCCCCCCEEEEEE		35.5310066782
55N-linked_GlycosylationPGVEPEDNATVHWVL
CCCCCCCCCEEEEEE		35.5328060820
91PhosphorylationRSVQLHDSGNYSCYR
HEEECCCCCCCCEEE		20.42-
93N-linked_GlycosylationVQLHDSGNYSCYRAG
EECCCCCCCCEEECC		29.5110066782
93N-linked_GlycosylationVQLHDSGNYSCYRAG
EECCCCCCCCEEECC		29.5128060820
139PhosphorylationCEWGPRSTPSLTTKA
ECCCCCCCCCCCHHH		20.41-
141PhosphorylationWGPRSTPSLTTKAVL
CCCCCCCCCCHHHHH		38.14-
144PhosphorylationRSTPSLTTKAVLLVR
CCCCCCCHHHHHHHH		23.4622817900
221N-linked_GlycosylationLQPDPPANITVTAVA
CCCCCCCCEEEEEEE		35.9210066782
221N-linked_GlycosylationLQPDPPANITVTAVA
CCCCCCCCEEEEEEE		35.9228060820
243PhosphorylationVTWQDPHSWNSSFYR
EEECCCCCCCCCEEH		33.08-
245N-linked_GlycosylationWQDPHSWNSSFYRLR
ECCCCCCCCCEEHHH		30.6928060820
329O-linked_GlycosylationPAENEVSTPMQALTT
CCCCCCCCCCHHHCC		28.14OGP
335O-linked_GlycosylationSTPMQALTTNKDDDN
CCCCHHHCCCCCCCC		31.19OGP
350N-linked_GlycosylationILFRDSANATSLPVQ
EEECCCCCCCCCCCC		47.9428060820
352O-linked_GlycosylationFRDSANATSLPVQDS
ECCCCCCCCCCCCCC		30.5128060820
353PhosphorylationRDSANATSLPVQDSS
CCCCCCCCCCCCCCC		28.4130257219
403PhosphorylationALKEGKTSMHPPYSL
HHHCCCCCCCCCCCH		20.6922210691
408PhosphorylationKTSMHPPYSLGQLVP
CCCCCCCCCHHHCCC		22.4522210691
409PhosphorylationTSMHPPYSLGQLVPE
CCCCCCCCHHHCCCC		31.6222210691
455PhosphorylationPDARDPRSPYDISNT
CCCCCCCCCCCCCCC		32.9523401153
457PhosphorylationARDPRSPYDISNTDY
CCCCCCCCCCCCCCC		27.4428450419
460PhosphorylationPRSPYDISNTDYFFP
CCCCCCCCCCCCCCC		30.6823312004
462PhosphorylationSPYDISNTDYFFPR-
CCCCCCCCCCCCCC-		25.8628152594
464PhosphorylationYDISNTDYFFPR---
CCCCCCCCCCCC---		12.7028152594
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 IL6RA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
55NGlycosylation

10066782
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 IL6RA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IL6_HUMANIL6physical
12643274
CNTF_HUMANCNTFphysical
12643274
IL6_HUMANIL6physical
2788034
IL6RB_HUMANIL6STphysical
2788034
STAT3_HUMANSTAT3physical
10982829
TBCK_HUMANTBCKphysical
28514442
PPR21_HUMANPPP1R21physical
28514442
TRI18_HUMANMID1physical
28514442
CL004_HUMANC12orf4physical
28514442
QORL1_HUMANCRYZL1physical
28514442
FANCB_HUMANFANCBphysical
28514442
FANCL_HUMANFANCLphysical
28514442
FP100_HUMANC17orf70physical
28514442
CETN2_HUMANCETN2physical
28514442
COPRS_HUMANCOPRSphysical
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
D02596 Tocilizumab (genetical recombination) (JAN); Tocilizumab (USAN/INN); Actemra (TN)
D10161 Sarilumab (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IL6RA_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Disulfide bond structure and N-glycosylation sites of theextracellular domain of the human interleukin-6 receptor.";
Cole A.R., Hall N.E., Treutlein H.R., Eddes J.S., Reid G.E.,Moritz R.L., Simpson R.J.;
J. Biol. Chem. 274:7207-7215(1999).
Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-55; ASN-93 AND ASN-221,LACK OF GLYCOSYLATION AT ASN-245, AND DISULFIDE BONDS.

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