IL2RG_HUMAN - dbPTM
IL2RG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IL2RG_HUMAN
UniProt AC P31785
Protein Name Cytokine receptor common subunit gamma
Gene Name IL2RG
Organism Homo sapiens (Human).
Sequence Length 369
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Common subunit for the receptors for a variety of interleukins..
Protein Sequence MLKPSLPFTSLLFLQLPLLGVGLNTTILTPNGNEDTTADFFLTTMPTDSLSVSTLPLPEVQCFVFNVEYMNCTWNSSSEPQPTNLTLHYWYKNSDNDKVQKCSHYLFSEEITSGCQLQKKEIHLYQTFVVQLQDPREPRRQATQMLKLQNLVIPWAPENLTLHKLSESQLELNWNNRFLNHCLEHLVQYRTDWDHSWTEQSVDYRHKFSLPSVDGQKRYTFRVRSRFNPLCGSAQHWSEWSHPIHWGSNTSKENPFLFALEAVVISVGSMGLIISLLCVYFWLERTMPRIPTLKNLEDLVTEYHGNFSAWSGVSKGLAESLQPDYSERLCLVSEIPPKGGALGEGPGASPCNQHSPYWAPPCYTLKPET
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
24N-linked_GlycosylationPLLGVGLNTTILTPN
HHHCCEECCEEECCC		29.28UniProtKB CARBOHYD
71N-linked_GlycosylationVFNVEYMNCTWNSSS
EEEEEEEECEECCCC		21.1116293754
75N-linked_GlycosylationEYMNCTWNSSSEPQP
EEEECEECCCCCCCC		17.54UniProtKB CARBOHYD
84N-linked_GlycosylationSSEPQPTNLTLHYWY
CCCCCCCEEEEEEEE		37.4016293754
98UbiquitinationYKNSDNDKVQKCSHY
EECCCCHHHEEEHHH		53.47-
101UbiquitinationSDNDKVQKCSHYLFS
CCCHHHEEEHHHHHC		40.4629967540
119UbiquitinationTSGCQLQKKEIHLYQ
CCCCCCCCCEEEEEE		62.0529967540
120UbiquitinationSGCQLQKKEIHLYQT
CCCCCCCCEEEEEEE		49.27-
127O-linked_GlycosylationKEIHLYQTFVVQLQD
CEEEEEEEEEEECCC		12.58OGP
147UbiquitinationRQATQMLKLQNLVIP
HHHHHHHHHHCCCCC		42.56-
159N-linked_GlycosylationVIPWAPENLTLHKLS
CCCCCCCCCEEEECC		36.9516293754
164UbiquitinationPENLTLHKLSESQLE
CCCCEEEECCHHHHH		57.74-
198O-linked_GlycosylationTDWDHSWTEQSVDYR
CCCCCCCCCHHCCEE		27.45OGP
204PhosphorylationWTEQSVDYRHKFSLP
CCCHHCCEEECCCCC		16.6826267517
207UbiquitinationQSVDYRHKFSLPSVD
HHCCEEECCCCCCCC		27.8722505724
217UbiquitinationLPSVDGQKRYTFRVR
CCCCCCCCEEEEEEE		53.56-
249N-linked_GlycosylationHPIHWGSNTSKENPF
CCCCCCCCCCCCCCC		44.42UniProtKB CARBOHYD
292PhosphorylationRTMPRIPTLKNLEDL
HHCCCCCCCCCHHHH		48.259049783
294UbiquitinationMPRIPTLKNLEDLVT
CCCCCCCCCHHHHHH		63.0622817900
301PhosphorylationKNLEDLVTEYHGNFS
CCHHHHHHHHCCCHH		37.82-
303PhosphorylationLEDLVTEYHGNFSAW
HHHHHHHHCCCHHHH		12.9819901323
308PhosphorylationTEYHGNFSAWSGVSK
HHHCCCHHHHCCCCH		32.59-
315UbiquitinationSAWSGVSKGLAESLQ
HHHCCCCHHHHHHHC		56.3822817900
320PhosphorylationVSKGLAESLQPDYSE
CCHHHHHHHCCCCCC		27.0523401153
325PhosphorylationAESLQPDYSERLCLV
HHHHCCCCCCCEEEE		21.0828796482
326PhosphorylationESLQPDYSERLCLVS
HHHCCCCCCCEEEEE		24.5023401153
349PhosphorylationLGEGPGASPCNQHSP
CCCCCCCCCCCCCCC		35.5827080861
355PhosphorylationASPCNQHSPYWAPPC
CCCCCCCCCCCCCCC		15.2127080861
357PhosphorylationPCNQHSPYWAPPCYT
CCCCCCCCCCCCCCC		19.7427259358
363PhosphorylationPYWAPPCYTLKPET-
CCCCCCCCCCCCCC-		22.3819901323
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
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:16004964
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IL2RG_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 IL2RG_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CPNS1_HUMANCAPNS1physical
9326644
IL4RA_HUMANIL4Rphysical
12242343
JAK1_HUMANJAK1physical
8041779
JAK2_HUMANJAK2physical
8041779
I13R1_HUMANIL13RA1physical
12207328
STK4_HUMANSTK4physical
21988832
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
NFIP2_HUMANNDFIP2physical
26186194
FLVC1_HUMANFLVCR1physical
26186194
PTPRD_HUMANPTPRDphysical
26186194
REEP6_HUMANREEP6physical
26186194
IL2_HUMANIL2physical
11418623
IL21_HUMANIL21physical
11418623
REEP6_HUMANREEP6physical
28514442
CD320_HUMANCD320physical
28514442
PTPRD_HUMANPTPRDphysical
28514442
FLVC1_HUMANFLVCR1physical
28514442
JAK3_HUMANJAK3physical
27742835
GRB10_HUMANGRB10physical
27742835
NED4L_HUMANNEDD4Lphysical
27742835
Drug and Disease Associations
Kegg Disease
H00080 Systemic lupus erythematosus
H00091 T-B+Severe combined immunodeficiencies (SCIDs), including the following eight diseases: X-linked SCI
H00093 Combined immunodeficiencies (CIDs), including the following nine diseases: X-linked hyper IgM syndro
OMIM Disease
300400Severe combined immunodeficiency X-linked T-cell-negative/B-cell-positive/NK-cell-negative (XSCID)
312863X-linked combined immunodeficiency (XCID)
Kegg Drug
D00748 Aldesleukin (USAN/INN); Interleukin-2; Proleukin (TN)
D02743 Celmoleukin (genetical recombination) (JP16); Celmoleukin (INN); Celeuk (TN)
D02749 Teceleukin (genetical recombination) (JP16); Teceleukin (USAN); Imunace (TN)
D03682 Denileukin diftitox (USAN/INN); Ontak (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IL2RG_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Crystal structure of the IL-2 signaling complex: paradigm for aheterotrimeric cytokine receptor.";
Stauber D.J., Debler E.W., Horton P.A., Smith K.A., Wilson I.A.;
Proc. Natl. Acad. Sci. U.S.A. 103:2788-2793(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 23-255 IN COMPLEX WITH IL2;IL2RA AND IL2RB, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-71; ASN-84AND ASN-159.
"Structure of the quaternary complex of interleukin-2 with its alpha,beta, and gammac receptors.";
Wang X., Rickert M., Garcia K.C.;
Science 310:1159-1163(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 56-254 IN COMPLEX WITH IL2;IL2RA AND IL2RB, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-71; ASN-84AND ASN-159.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-292, AND MASSSPECTROMETRY.

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