dbPTM

IL6RB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IL6RB_MOUSE
UniProt AC	Q00560
Protein Name	Interleukin-6 receptor subunit beta
Gene Name	Il6st
Organism	Mus musculus (Mouse).
Sequence Length	917
Subcellular Localization	Cell membrane Single-pass type I membrane protein .
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: 1602143 That causes phosphorylation of IL6ST tyrosine residues which in turn activates STAT3]
Protein Sequence	MSAPRIWLAQALLFFLTTESIGQLLEPCGYIYPEFPVVQRGSNFTAICVLKEACLQHYYVNASYIVWKTNHAAVPREQVTVINRTTSSVTFTDVVLPSVQLTCNILSFGQIEQNVYGVTMLSGFPPDKPTNLTCIVNEGKNMLCQWDPGRETYLETNYTLKSEWATEKFPDCQSKHGTSCMVSYMPTYYVNIEVWVEAENALGKVSSESINFDPVDKVKPTPPYNLSVTNSEELSSILKLSWVSSGLGGLLDLKSDIQYRTKDASTWIQVPLEDTMSPRTSFTVQDLKPFTEYVFRIRSIKDSGKGYWSDWSEEASGTTYEDRPSRPPSFWYKTNPSHGQEYRSVRLIWKALPLSEANGKILDYEVILTQSKSVSQTYTVTGTELTVNLTNDRYVASLAARNKVGKSAAAVLTIPSPHVTAAYSVVNLKAFPKDNLLWVEWTPPPKPVSKYILEWCVLSENAPCVEDWQQEDATVNRTHLRGRLLESKCYQITVTPVFATGPGGSESLKAYLKQAAPARGPTVRTKKVGKNEAVLAWDQIPVDDQNGFIRNYSISYRTSVGKEMVVHVDSSHTEYTLSSLSSDTLYMVRMAAYTDEGGKDGPEFTFTTPKFAQGEIEAIVVPVCLAFLLTTLLGVLFCFNKRDLIKKHIWPNVPDPSKSHIAQWSPHTPPRHNFNSKDQMYSDGNFTDVSVVEIEANNKKPCPDDLKSVDLFKKEKVSTEGHSSGIGGSSCMSSSRPSISSNEENESAQSTASTVQYSTVVHSGYRHQVPSVQVFSRSESTQPLLDSEERPEDLQLVDSVDGGDEILPRQPYFKQNCSQPEACPEISHFERSNQVLSGNEEDFVRLKQQQVSDHISQPYGSEQRRLFQEGSTADALGTGADGQMERFESVGMETTIDEEIPKSYLPQTVRQGGYMPQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
43	N-linked_Glycosylation	PVVQRGSNFTAICVL CEEECCCCCEEEECH	40.90	-
61	N-linked_Glycosylation	CLQHYYVNASYIVWK HHHHEEECCEEEEEE	13.67	-
69	Phosphorylation	ASYIVWKTNHAAVPR CEEEEEECCCCCCCH	19.27	24719451
83	N-linked_Glycosylation	REQVTVINRTTSSVT HHHEEEEECCCCCEE	30.80	-
131	N-linked_Glycosylation	FPPDKPTNLTCIVNE CCCCCCCCEEEEEEC	41.71	-
157	N-linked_Glycosylation	RETYLETNYTLKSEW CCEEEEEEEEECCHH	20.58	-
225	N-linked_Glycosylation	VKPTPPYNLSVTNSE CCCCCCCCCCCCCHH	31.45	19349973
229	Phosphorylation	PPYNLSVTNSEELSS CCCCCCCCCHHHHHH	29.65	21183079
231	Phosphorylation	YNLSVTNSEELSSIL CCCCCCCHHHHHHHH	24.07	22817900
235	Phosphorylation	VTNSEELSSILKLSW CCCHHHHHHHHHHHH	20.72	22817900
236	Phosphorylation	TNSEELSSILKLSWV CCHHHHHHHHHHHHH	44.56	22817900
388	N-linked_Glycosylation	TGTELTVNLTNDRYV ECCEEEEECCCHHHH	35.59	-
476	N-linked_Glycosylation	QQEDATVNRTHLRGR HHCCCCCCHHHHHHH	38.49	-
490	Phosphorylation	RLLESKCYQITVTPV HHHHCCCEEEEEEEE	13.49	25777480
493	Phosphorylation	ESKCYQITVTPVFAT HCCCEEEEEEEEEEC	11.64	25777480
495	Phosphorylation	KCYQITVTPVFATGP CCEEEEEEEEEECCC	12.70	25777480
500	Phosphorylation	TVTPVFATGPGGSES EEEEEEECCCCCHHH	32.23	25777480
505	Phosphorylation	FATGPGGSESLKAYL EECCCCCHHHHHHHH	29.90	25777480
507	Phosphorylation	TGPGGSESLKAYLKQ CCCCCHHHHHHHHHH	36.55	25777480
551	N-linked_Glycosylation	DQNGFIRNYSISYRT CCCCEEEEEEEEEEC	30.04	-
647	Ubiquitination	NKRDLIKKHIWPNVP CHHHHHHHCCCCCCC	33.07	22790023
647	Ubiquitination	NKRDLIKKHIWPNVP CHHHHHHHCCCCCCC	33.07	22790023
657	Phosphorylation	WPNVPDPSKSHIAQW CCCCCCCCHHCCCCC	54.92	25338131
659	Phosphorylation	NVPDPSKSHIAQWSP CCCCCCHHCCCCCCC	25.18	23140645
665	Phosphorylation	KSHIAQWSPHTPPRH HHCCCCCCCCCCCCC	8.50	26824392
668	Phosphorylation	IAQWSPHTPPRHNFN CCCCCCCCCCCCCCC	38.07	23684622
708	Phosphorylation	PCPDDLKSVDLFKKE CCCCCHHHCCCHHCC	28.32	25338131
757	Phosphorylation	STASTVQYSTVVHSG HHHHCEEEEEEEECC	12.81	12370259
778	Phosphorylation	SVQVFSRSESTQPLL EEEEEECCCCCCCCC	34.40	26239621
780	Phosphorylation	QVFSRSESTQPLLDS EEEECCCCCCCCCCC	33.32	25521595
781	Phosphorylation	VFSRSESTQPLLDSE EEECCCCCCCCCCCC	30.10	26239621
787	Phosphorylation	STQPLLDSEERPEDL CCCCCCCCCCCHHHC	41.13	22817900
799	Phosphorylation	EDLQLVDSVDGGDEI HHCCEEECCCCCCCC	18.03	23984901
812	Phosphorylation	EILPRQPYFKQNCSQ CCCCCCCCCCCCCCC	18.31	26643407
818	Phosphorylation	PYFKQNCSQPEACPE CCCCCCCCCCCCCCC	57.21	23684622
827	Phosphorylation	PEACPEISHFERSNQ CCCCCCCCCCHHHCC	22.06	-
832	Phosphorylation	EISHFERSNQVLSGN CCCCCHHHCCCCCCC	25.15	28833060
837	Phosphorylation	ERSNQVLSGNEEDFV HHHCCCCCCCHHHHH	40.49	28833060
856	Phosphorylation	QQVSDHISQPYGSEQ HHHHHHCCCCCCHHH	22.98	25338131
859	Phosphorylation	SDHISQPYGSEQRRL HHHCCCCCCHHHHHH	26.16	29514104
861	Phosphorylation	HISQPYGSEQRRLFQ HCCCCCCHHHHHHHH	25.39	29514104
889	Phosphorylation	GQMERFESVGMETTI CCCEEHHHCCCCCCC	22.66	25338131
904	Phosphorylation	DEEIPKSYLPQTVRQ CCCCCHHHCCHHHHC	28.64	29514104
914	Phosphorylation	QTVRQGGYMPQ---- HHHHCCCCCCC----	16.67	29514104

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
780	S	Phosphorylation	Kinase	KCC2A	P11798	PhosphoELM
780	S	Phosphorylation	Kinase	CAMK4	P08414	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	Cbl	P22682	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
780	S	Phosphorylation		-
Phosphorylation of Ser-780 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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PTN11_HUMAN	PTPN11	physical	18519587
CBL_HUMAN	CBL	physical	18519587
HGS_MOUSE	Hgs	physical	18519587
LIFR_MOUSE	Lifr	physical	16452727

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of IL6RB_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225, AND MASSSPECTROMETRY.	19349973 [Abstract]

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