IL2RB_HUMAN - dbPTM
IL2RB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IL2RB_HUMAN
UniProt AC P14784
Protein Name Interleukin-2 receptor subunit beta
Gene Name IL2RB {ECO:0000312|HGNC:HGNC:6009}
Organism Homo sapiens (Human).
Sequence Length 551
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2..
Protein Sequence MAAPALSWRLPLLILLLPLATSWASAAVNGTSQFTCFYNSRANISCVWSQDGALQDTSCQVHAWPDRRRWNQTCELLPVSQASWACNLILGAPDSQKLTTVDIVTLRVLCREGVRWRVMAIQDFKPFENLRLMAPISLQVVHVETHRCNISWEISQASHYFERHLEFEARTLSPGHTWEEAPLLTLKQKQEWICLETLTPDTQYEFQVRVKPLQGEFTTWSPWSQPLAFRTKPAALGKDTIPWLGHLLVGLSGAFGFIILVYLLINCRNTGPWLKKVLKCNTPDPSKFFSQLSSEHGGDVQKWLSSPFPSSSFSPGGLAPEISPLEVLERDKVTQLLLQQDKVPEPASLSSNHSLTSCFTNQGYFFFHLPDALEIEACQVYFTYDPYSEEDPDEGVAGAPTGSSPQPLQPLSGEDDAYCTFPSRDDLLLFSPSLLGGPSPPSTAPGGSGAGEERMPPSLQERVPRDWDPQPLGPPTPGVPDLVDFQPPPELVLREAGEEVPDAGPREGVSFPWSRPPGQGEFRALNARLPLNTDAYLSLQELQGQDPTHLV
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
7Phosphorylation-MAAPALSWRLPLLI
-CCCCHHCCHHHHHH		16.5624719451
29N-linked_GlycosylationSWASAAVNGTSQFTC
HHHHHHHCCCCEEEE		43.21UniProtKB CARBOHYD
43N-linked_GlycosylationCFYNSRANISCVWSQ
EEECCCCCEEEEEEC		26.1216477002
71N-linked_GlycosylationWPDRRRWNQTCELLP
CCCCHHHHCCEEEEE		26.0216477002
105PhosphorylationLTTVDIVTLRVLCRE
CCEEEEEEHHHHHHC		14.80-
149N-linked_GlycosylationHVETHRCNISWEISQ
EEEEECCEEEEEEHH		31.1416293754
282PhosphorylationKKVLKCNTPDPSKFF
HHHHCCCCCCHHHHH		38.2419581576
290PhosphorylationPDPSKFFSQLSSEHG
CCHHHHHHHHHHHCC		33.0927080861
293PhosphorylationSKFFSQLSSEHGGDV
HHHHHHHHHHCCCCH		26.5021722762
294PhosphorylationKFFSQLSSEHGGDVQ
HHHHHHHHHCCCCHH		42.0530108239
364PhosphorylationSCFTNQGYFFFHLPD
ECEECCCEEEEECCC		6.358643566
381PhosphorylationEIEACQVYFTYDPYS
EEEEEEEEEEECCCC		2.432047859
384PhosphorylationACQVYFTYDPYSEED
EEEEEEEECCCCCCC		12.672047859
387PhosphorylationVYFTYDPYSEEDPDE
EEEEECCCCCCCCCC		26.302047859
418PhosphorylationLSGEDDAYCTFPSRD
CCCCCCCCCCCCCCC		10.0612200137
431PhosphorylationRDDLLLFSPSLLGGP
CCCEEEECHHHHCCC		17.3521722762
433PhosphorylationDLLLFSPSLLGGPSP
CEEEECHHHHCCCCC		34.7221722762
458PhosphorylationGEERMPPSLQERVPR
CCCCCCCCHHHCCCC		36.4921722762
476PhosphorylationPQPLGPPTPGVPDLV
CCCCCCCCCCCCCCC		35.49-
533PhosphorylationNARLPLNTDAYLSLQ
EEECCCCCCCEEEHH		29.6821722762
536PhosphorylationLPLNTDAYLSLQELQ
CCCCCCCEEEHHHHC		10.3012200137
538PhosphorylationLNTDAYLSLQELQGQ
CCCCCEEEHHHHCCC		18.4821722762
548PhosphorylationELQGQDPTHLV----
HHCCCCCCCCC----		35.8121722762
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
381YPhosphorylationKinaseLCKP06239
PSP
384YPhosphorylationKinaseLCKP06239
PSP
387YPhosphorylationKinaseLCKP06239
PSP
418YPhosphorylationKinaseLCKP06239
PSP
476TPhosphorylationKinaseMAPK1P28482
GPS
476TPhosphorylationKinaseMAPK3P27361
GPS
536YPhosphorylationKinaseLCKP06239
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IL2RB_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 IL2RB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SHC1_HUMANSHC1physical
10602027
GRB2_HUMANGRB2physical
10602027
STA5B_HUMANSTAT5Bphysical
10602027
STAT1_HUMANSTAT1physical
10602027
STAT3_HUMANSTAT3physical
10602027
STA5A_HUMANSTAT5Aphysical
10602027
CISH_HUMANCISHphysical
10514520
SOCS1_HUMANSOCS1physical
11133764
JAK1_HUMANJAK1physical
12133952
JAK1_HUMANJAK1physical
9553136
JAK2_HUMANJAK2physical
9553136
JAK1_HUMANJAK1physical
9774657
HGS_HUMANHGSphysical
18445679
HGS_HUMANHGSphysical
21362618
JAK1_HUMANJAK1physical
8041779
ECM1_HUMANECM1physical
21217760
Drug and Disease Associations
Kegg Disease
H00080 Systemic lupus erythematosus
OMIM Disease
There are no disease associations of PTM sites.
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 IL2RB_HUMAN

loading...

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 25-232 IN COMPLEX WITH IL2;IL2RA AND IL2RC, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-43; ASN-71AND ASN-149.
"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 27-240 IN COMPLEX WITH IL2;IL2RA AND IL2RC, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-149.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory