dbPTM

IL6RB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IL6RB_HUMAN
UniProt AC	P40189
Protein Name	Interleukin-6 receptor subunit beta
Gene Name	IL6ST
Organism	Homo sapiens (Human).
Sequence Length	918
Subcellular Localization	Isoform 1: Cell membrane Single-pass type I membrane protein . Isoform 2: Secreted .
Protein Description	Signal-transducing molecule. The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize IL6ST for initiating signal transmission. Binding of IL6 to IL6R induces IL6ST homodimerization and formation of a high-affinity receptor complex, which activates Janus kinases. [PubMed: 2261637 That causes phosphorylation of IL6ST tyrosine residues which in turn activates STAT3]
Protein Sequence	MLTLQTWLVQALFIFLTTESTGELLDPCGYISPESPVVQLHSNFTAVCVLKEKCMDYFHVNANYIVWKTNHFTIPKEQYTIINRTASSVTFTDIASLNIQLTCNILTFGQLEQNVYGITIISGLPPEKPKNLSCIVNEGKKMRCEWDGGRETHLETNFTLKSEWATHKFADCKAKRDTPTSCTVDYSTVYFVNIEVWVEAENALGKVTSDHINFDPVYKVKPNPPHNLSVINSEELSSILKLTWTNPSIKSVIILKYNIQYRTKDASTWSQIPPEDTASTRSSFTVQDLKPFTEYVFRIRCMKEDGKGYWSDWSEEASGITYEDRPSKAPSFWYKIDPSHTQGYRTVQLVWKTLPPFEANGKILDYEVTLTRWKSHLQNYTVNATKLTVNLTNDRYLATLTVRNLVGKSDAAVLTIPACDFQATHPVMDLKAFPKDNMLWVEWTTPRESVKKYILEWCVLSDKAPCITDWQQEDGTVHRTYLRGNLAESKCYLITVTPVYADGPGSPESIKAYLKQAPPSKGPTVRTKKVGKNEAVLEWDQLPVDVQNGFIRNYTIFYRTIIGNETAVNVDSSHTEYTLSSLTSDTLYMVRMAAYTDEGGKDGPEFTFTTPKFAQGEIEAIVVPVCLAFLLTTLLGVLFCFNKRDLIKKHIWPNVPDPSKSHIAQWSPHTPPRHNFNSKDQMYSDGNFTDVSVVEIEANDKKPFPEDLKSLDLFKKEKINTEGHSSGIGGSSCMSSSRPSISSSDENESSQNTSSTVQYSTVVHSGYRHQVPSVQVFSRSESTQPLLDSEERPEDLQLVDHVDGGDGILPRQQYFKQNCSQHESSPDISHFERSKQVSSVNEEDFVRLKQQISDHISQSCGSGQMKMFQEVSAADAFGPGTEGQVERFETVGMEAATDEGMPKSYLPQTVRQGGYMPQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
43	N-linked_Glycosylation	PVVQLHSNFTAVCVL CEEEEECCCEEEEEE	27.78	20489211
43	N-linked_Glycosylation	PVVQLHSNFTAVCVL CEEEEECCCEEEEEE	27.78	11098061
83	N-linked_Glycosylation	KEQYTIINRTASSVT HHHEEEEECCCCCEE	31.25	20489211
83	N-linked_Glycosylation	KEQYTIINRTASSVT HHHEEEEECCCCCEE	31.25	11098061
119	Phosphorylation	EQNVYGITIISGLPP HHEEEEEEEEECCCC	14.11	26074081
122	Phosphorylation	VYGITIISGLPPEKP EEEEEEEECCCCCCC	30.35	26074081
128	Acetylation	ISGLPPEKPKNLSCI EECCCCCCCCCCEEE	68.04	25953088
131	N-linked_Glycosylation	LPPEKPKNLSCIVNE CCCCCCCCCEEEEEC	45.79	11098061
131	N-linked_Glycosylation	LPPEKPKNLSCIVNE CCCCCCCCCEEEEEC	45.79	11098061
140	Ubiquitination	SCIVNEGKKMRCEWD EEEEECCCCEEEEEC	36.90	-
157	N-linked_Glycosylation	RETHLETNFTLKSEW CEEEEEECEEECHHH	20.66	11098061
157	N-linked_Glycosylation	RETHLETNFTLKSEW CEEEEEECEEECHHH	20.66	11098061
168	Ubiquitination	KSEWATHKFADCKAK CHHHHCCCCCCCCCC	37.58	-
227	N-linked_Glycosylation	VKPNPPHNLSVINSE CCCCCCCCEEECCHH	39.52	11098061
227	N-linked_Glycosylation	VKPNPPHNLSVINSE CCCCCCCCEEECCHH	39.52	20489211
238	Phosphorylation	INSEELSSILKLTWT CCHHHHHHHHHHEEC	44.56	24719451
282	Phosphorylation	EDTASTRSSFTVQDL CCCCCCCCCEECCCC	29.86	30266825
283	Phosphorylation	DTASTRSSFTVQDLK CCCCCCCCEECCCCC	22.96	30266825
285	Phosphorylation	ASTRSSFTVQDLKPF CCCCCCEECCCCCCC	21.14	30266825
309	Phosphorylation	MKEDGKGYWSDWSEE EECCCCCCCCCCCHH	12.77	30576142
311	Phosphorylation	EDGKGYWSDWSEEAS CCCCCCCCCCCHHHC	22.25	30576142
318	Phosphorylation	SDWSEEASGITYEDR CCCCHHHCCCCCCCC	33.73	30576142
322	Phosphorylation	EEASGITYEDRPSKA HHHCCCCCCCCCCCC	17.57	-
379	N-linked_Glycosylation	RWKSHLQNYTVNATK HHHHHHHCEEECEEE	40.58	11098061
379	N-linked_Glycosylation	RWKSHLQNYTVNATK HHHHHHHCEEECEEE	40.58	11098061
383	N-linked_Glycosylation	HLQNYTVNATKLTVN HHHCEEECEEEEEEE	33.81	20489211
383	N-linked_Glycosylation	HLQNYTVNATKLTVN HHHCEEECEEEEEEE	33.81	11098061
390	N-linked_Glycosylation	NATKLTVNLTNDRYL CEEEEEEECCCCCEE	35.59	17660510
392	Phosphorylation	TKLTVNLTNDRYLAT EEEEEECCCCCEEEE	29.84	23403867
396	Phosphorylation	VNLTNDRYLATLTVR EECCCCCEEEEEEEH	11.98	22817900
409	Phosphorylation	VRNLVGKSDAAVLTI EHHHCCCCCEEEEEE	26.93	22210691
415	Phosphorylation	KSDAAVLTIPACDFQ CCCEEEEEEECCCCC	20.51	22210691
453	Phosphorylation	PRESVKKYILEWCVL CHHHHHHHHHHHHHH	12.67	28258704
461	Phosphorylation	ILEWCVLSDKAPCIT HHHHHHHCCCCCCCC	19.37	29083192
553	N-linked_Glycosylation	VQNGFIRNYTIFYRT CCCCEECEEEEEEEE	33.22	20489211
553	N-linked_Glycosylation	VQNGFIRNYTIFYRT CCCCEECEEEEEEEE	33.22	11098061
564	N-linked_Glycosylation	FYRTIIGNETAVNVD EEEEEECCCEEEECC	32.79	11098061
564	N-linked_Glycosylation	FYRTIIGNETAVNVD EEEEEECCCEEEECC	32.79	11098061
649	Ubiquitination	NKRDLIKKHIWPNVP CHHHHHHHCCCCCCC	33.07	-
659	Phosphorylation	WPNVPDPSKSHIAQW CCCCCCCCHHCCCCC	54.92	29507054
661	Phosphorylation	NVPDPSKSHIAQWSP CCCCCCHHCCCCCCC	25.18	23403867
667	Phosphorylation	KSHIAQWSPHTPPRH HHCCCCCCCCCCCCC	8.50	23927012
670	Phosphorylation	IAQWSPHTPPRHNFN CCCCCCCCCCCCCCC	38.07	30266825
678	Phosphorylation	PPRHNFNSKDQMYSD CCCCCCCCCCCCCCC	33.21	20363803
683	Phosphorylation	FNSKDQMYSDGNFTD CCCCCCCCCCCCCCE	9.66	10661409
702	Ubiquitination	EIEANDKKPFPEDLK EEECCCCCCCCHHHH	55.54	-
710	Phosphorylation	PFPEDLKSLDLFKKE CCCHHHHHCCCHHHH	34.12	30266825
715	Ubiquitination	LKSLDLFKKEKINTE HHHCCCHHHHHCCCC	68.28	-
718	Ubiquitination	LDLFKKEKINTEGHS CCCHHHHHCCCCCCC	50.57	-
740	Phosphorylation	CMSSSRPSISSSDEN CCCCCCCCCCCCCCC	33.71	28348404
742	Phosphorylation	SSSRPSISSSDENES CCCCCCCCCCCCCCC	28.29	28348404
743	Phosphorylation	SSRPSISSSDENESS CCCCCCCCCCCCCCC	39.89	28348404
744	Phosphorylation	SRPSISSSDENESSQ CCCCCCCCCCCCCCC	42.00	28348404
749	Phosphorylation	SSSDENESSQNTSST CCCCCCCCCCCCCCC	49.13	28348404
759	Dephosphorylation	NTSSTVQYSTVVHSG CCCCCEEEEEEEECC	11.28	12403768
759	Phosphorylation	NTSSTVQYSTVVHSG CCCCCEEEEEEEECC	11.28	9505191
761	Phosphorylation	SSTVQYSTVVHSGYR CCCEEEEEEEECCCC	22.93	25884760
767	Phosphorylation	STVVHSGYRHQVPSV EEEEECCCCCCCCEE	14.13	8612579
780	Phosphorylation	SVQVFSRSESTQPLL EEEEEECCCCCCCCC	34.40	27794612
782	Phosphorylation	QVFSRSESTQPLLDS EEEECCCCCCCCCCC	33.32	27794612
783	Phosphorylation	VFSRSESTQPLLDSE EEECCCCCCCCCCCC	30.10	30576142
789	Phosphorylation	STQPLLDSEERPEDL CCCCCCCCCCCHHHC	41.13	26699800
814	Phosphorylation	GILPRQQYFKQNCSQ CCCCHHHHHHHHCCC	12.38	8612579
820	Phosphorylation	QYFKQNCSQHESSPD HHHHHHCCCCCCCCC	41.96	30266825
824	Phosphorylation	QNCSQHESSPDISHF HHCCCCCCCCCHHHH	45.08	30266825
825	Phosphorylation	NCSQHESSPDISHFE HCCCCCCCCCHHHHH	24.49	30266825
829	Phosphorylation	HESSPDISHFERSKQ CCCCCCHHHHHHHHC	29.51	23403867
835	Ubiquitination	ISHFERSKQVSSVNE HHHHHHHHCCCCCCH	62.02	-
838	Phosphorylation	FERSKQVSSVNEEDF HHHHHCCCCCCHHHH	26.52	22167270
839	Phosphorylation	ERSKQVSSVNEEDFV HHHHCCCCCCHHHHH	30.06	19664994
849	Ubiquitination	EEDFVRLKQQISDHI HHHHHHHHHHHHHHH	29.59	-
849	Methylation	EEDFVRLKQQISDHI HHHHHHHHHHHHHHH	29.59	-
853	Phosphorylation	VRLKQQISDHISQSC HHHHHHHHHHHHHHC	20.85	28555341
859	Phosphorylation	ISDHISQSCGSGQMK HHHHHHHHCCCCHHH	17.41	28555341
862	Phosphorylation	HISQSCGSGQMKMFQ HHHHHCCCCHHHEEE	30.13	24961811
872	Phosphorylation	MKMFQEVSAADAFGP HHEEEEEHHHHHCCC	19.58	23532336
881	Phosphorylation	ADAFGPGTEGQVERF HHHCCCCCCCCEEEE	39.82	23532336
890	Phosphorylation	GQVERFETVGMEAAT CCEEEEEECCCCCCC	21.46	12361954
897	Phosphorylation	TVGMEAATDEGMPKS ECCCCCCCCCCCCHH	41.45	-
904	Phosphorylation	TDEGMPKSYLPQTVR CCCCCCHHHCCCCHH	26.49	28152594
905	Phosphorylation	DEGMPKSYLPQTVRQ CCCCCHHHCCCCHHC	28.64	25159151
909	Phosphorylation	PKSYLPQTVRQGGYM CHHHCCCCHHCCCCC	18.73	12361954
915	Phosphorylation	QTVRQGGYMPQ---- CCHHCCCCCCC----	16.67	8612579

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
782	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
782	S	Phosphorylation	Kinase	MAPKAPK2	P49137	GPS
890	T	Phosphorylation	Kinase	PRKCD	Q05655	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	SOCS3	O14543	PMID:24438103
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:18519587

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
782	S	Phosphorylation		10811661
Phosphorylation of Ser-782 down-regulates cell surface expression.

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 IL6RB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TLE1_HUMAN	TLE1	physical	12030375
CNTFR_HUMAN	CNTFR	physical	12707266
PTN11_HUMAN	PTPN11	physical	12403768
SOCS3_HUMAN	SOCS3	physical	12403768
ERBB2_HUMAN	ERBB2	physical	11821958
ERBB3_HUMAN	ERBB3	physical	11821958
VAV_HUMAN	VAV1	physical	9013873
GRB2_HUMAN	GRB2	physical	9013873
LIFR_HUMAN	LIFR	physical	8999038
OSMR_HUMAN	OSMR	physical	8999038
PTN11_HUMAN	PTPN11	physical	10946280
JAK1_HUMAN	JAK1	physical	9388212
JAK2_HUMAN	JAK2	physical	9388212
TYK2_HUMAN	TYK2	physical	9388212
PTN11_HUMAN	PTPN11	physical	9388212
KPCD_HUMAN	PRKCD	physical	12361954
STAT3_HUMAN	STAT3	physical	12361954
P85A_HUMAN	PIK3R1	physical	10579793
PTN6_HUMAN	PTPN6	physical	10800945
JAK1_HUMAN	JAK1	physical	11742534
SOCS3_HUMAN	SOCS3	physical	10777583
PTN11_HUMAN	PTPN11	physical	10777583
MAGAB_HUMAN	MAGEA11	physical	25416956
UBQL1_HUMAN	UBQLN1	physical	25416956
CSEN_HUMAN	KCNIP3	physical	25416956
SGTB_HUMAN	SGTB	physical	25416956

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.

Regulatory Network of IL6RB_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-227 AND ASN-390, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-379 AND ASN-383, AND MASSSPECTROMETRY.	16335952 [Abstract]
"Determination of the disulfide structure and N-glycosylation sites ofthe extracellular domain of the human signal transducer gp130."; Moritz R.L., Hall N.E., Connolly L.M., Simpson R.J.; J. Biol. Chem. 276:8244-8253(2001). Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND GLYCOSYLATION ATASN-43; ASN-83; ASN-131; ASN-157; ASN-227; ASN-379; ASN-383; ASN-553AND ASN-564.	11098061 [Abstract]
Phosphorylation
Reference	PubMed
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667; SER-820 ANDSER-829, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Phosphorylation of human gp130 at Ser-782 adjacent to the di-leucineinternalization motif. Effects on expression and signaling."; Gibson R.M., Schiemann W.P., Prichard L.B., Reno J.M., Ericsson L.H.,Nathanson N.M.; J. Biol. Chem. 275:22574-22582(2000). Cited for: PHOSPHORYLATION AT SER-782, MUTAGENESIS OF SER-782, AND MASSSPECTROMETRY.	10811661 [Abstract]

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