IL3RB_HUMAN - dbPTM
IL3RB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IL3RB_HUMAN
UniProt AC P32927
Protein Name Cytokine receptor common subunit beta
Gene Name CSF2RB
Organism Homo sapiens (Human).
Sequence Length 897
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description High affinity receptor for interleukin-3, interleukin-5 and granulocyte-macrophage colony-stimulating factor..
Protein Sequence MVLAQGLLSMALLALCWERSLAGAEETIPLQTLRCYNDYTSHITCRWADTQDAQRLVNVTLIRRVNEDLLEPVSCDLSDDMPWSACPHPRCVPRRCVIPCQSFVVTDVDYFSFQPDRPLGTRLTVTLTQHVQPPEPRDLQISTDQDHFLLTWSVALGSPQSHWLSPGDLEFEVVYKRLQDSWEDAAILLSNTSQATLGPEHLMPSSTYVARVRTRLAPGSRLSGRPSKWSPEVCWDSQPGDEAQPQNLECFFDGAAVLSCSWEVRKEVASSVSFGLFYKPSPDAGEEECSPVLREGLGSLHTRHHCQIPVPDPATHGQYIVSVQPRRAEKHIKSSVNIQMAPPSLNVTKDGDSYSLRWETMKMRYEHIDHTFEIQYRKDTATWKDSKTETLQNAHSMALPALEPSTRYWARVRVRTSRTGYNGIWSEWSEARSWDTESVLPMWVLALIVIFLTIAVLLALRFCGIYGYRLRRKWEEKIPNPSKSHLFQNGSAELWPPGSMSAFTSGSPPHQGPWGSRFPELEGVFPVGFGDSEVSPLTIEDPKHVCDPPSGPDTTPAASDLPTEQPPSPQPGPPAASHTPEKQASSFDFNGPYLGPPHSRSLPDILGQPEPPQEGGSQKSPPPGSLEYLCLPAGGQVQLVPLAQAMGPGQAVEVERRPSQGAAGSPSLESGGGPAPPALGPRVGGQDQKDSPVAIPMSSGDTEDPGVASGYVSSADLVFTPNSGASSVSLVPSLGLPSDQTPSLCPGLASGPPGAPGPVKSGFEGYVELPPIEGRSPRSPRNNPVPPEAKSPVLNPGERPADVSPTSPQPEGLLVLQQVGDYCFLPGLGPGPLSLRSKPSSPGPGPEIKNLDQAFQVKKPPGQAVPQVPVIQLFKALKQQDYLSLPPWEVNKPGEVC
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
58N-linked_GlycosylationQDAQRLVNVTLIRRV
HHHHHHHHHHHEECC		26.1618692472
191N-linked_GlycosylationDAAILLSNTSQATLG
HHHHHHCCCCCCCCC		43.6618692472
220PhosphorylationRTRLAPGSRLSGRPS
HCCCCCCCCCCCCCC		29.0523312004
223PhosphorylationLAPGSRLSGRPSKWS
CCCCCCCCCCCCCCC		31.4823312004
346N-linked_GlycosylationQMAPPSLNVTKDGDS
EECCCCCEECCCCCC		43.69UniProtKB CARBOHYD
355PhosphorylationTKDGDSYSLRWETMK
CCCCCCEEEEEEEEE		18.5324719451
390PhosphorylationWKDSKTETLQNAHSM
CCCCHHHHHHHHHHC		38.5824667141
396PhosphorylationETLQNAHSMALPALE
HHHHHHHHCHHCCCC		11.8924667141
466PhosphorylationALRFCGIYGYRLRRK
HHHHHHHHHHHHHHH		8.0610672044
468PhosphorylationRFCGIYGYRLRRKWE
HHHHHHHHHHHHHHH		6.9010672044
473UbiquitinationYGYRLRRKWEEKIPN
HHHHHHHHHHHCCCC		53.15-
477UbiquitinationLRRKWEEKIPNPSKS
HHHHHHHCCCCCCHH		52.53-
482PhosphorylationEEKIPNPSKSHLFQN
HHCCCCCCHHHCCCC		54.1325954137
483UbiquitinationEKIPNPSKSHLFQNG
HCCCCCCHHHCCCCC		43.05-
491PhosphorylationSHLFQNGSAELWPPG
HHCCCCCCCCCCCCC		26.56-
554PhosphorylationDPPSGPDTTPAASDL
CCCCCCCCCCCHHHC		37.5030108239
555PhosphorylationPPSGPDTTPAASDLP
CCCCCCCCCCHHHCC		20.5030108239
559PhosphorylationPDTTPAASDLPTEQP
CCCCCCHHHCCCCCC		41.6130108239
563PhosphorylationPAASDLPTEQPPSPQ
CCHHHCCCCCCCCCC		55.3330108239
568PhosphorylationLPTEQPPSPQPGPPA
CCCCCCCCCCCCCCC		42.7330108239
577PhosphorylationQPGPPAASHTPEKQA
CCCCCCCCCCCCCCC		29.9630108239
579PhosphorylationGPPAASHTPEKQASS
CCCCCCCCCCCCCCC		30.5530108239
585PhosphorylationHTPEKQASSFDFNGP
CCCCCCCCCCCCCCC		29.1010477722
593PhosphorylationSFDFNGPYLGPPHSR
CCCCCCCCCCCCCCC		26.2010704825
601PhosphorylationLGPPHSRSLPDILGQ
CCCCCCCCCCHHCCC		47.4723401153
628PhosphorylationPPPGSLEYLCLPAGG
CCCCCEEEEEECCCC		14.1710329850
628DephosphorylationPPPGSLEYLCLPAGG
CCCCCEEEEEECCCC		14.179162089
659PhosphorylationVEVERRPSQGAAGSP
EEEEECCCCCCCCCC		39.1623401153
665PhosphorylationPSQGAAGSPSLESGG
CCCCCCCCCCCCCCC		13.4423312004
667PhosphorylationQGAAGSPSLESGGGP
CCCCCCCCCCCCCCC		46.6023312004
711PhosphorylationDPGVASGYVSSADLV
CCCCCCCEECCCEEE		8.4810329850
766PhosphorylationVKSGFEGYVELPPIE
CCCCCCCEEECCCCC		5.4210329850
776PhosphorylationLPPIEGRSPRSPRNN
CCCCCCCCCCCCCCC		35.2123401153
822PhosphorylationVLQQVGDYCFLPGLG
EEEEECCEECCCCCC		4.5210329850
837PhosphorylationPGPLSLRSKPSSPGP
CCCCCCCCCCCCCCC		54.9623312004
840PhosphorylationLSLRSKPSSPGPGPE
CCCCCCCCCCCCCHH		53.5628450419
841PhosphorylationSLRSKPSSPGPGPEI
CCCCCCCCCCCCHHH		42.2626657352
882PhosphorylationKALKQQDYLSLPPWE
HHHHCCCCCCCCCCC		8.2110329850
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
466YPhosphorylationKinaseLYNP07948
PSP
468YPhosphorylationKinaseLYNP07948
PSP
601SPhosphorylationKinasePRKACAP05132
GPS
601SPhosphorylationKinasePKA-FAMILY-GPS
601SPhosphorylationKinasePKA_GROUP-PhosphoELM
822YPhosphorylationKinaseLYNP07948
PSP
882YPhosphorylationKinaseLYNP07948
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IL3RB_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 IL3RB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTN11_HUMANPTPN11physical
9162089
PTN6_HUMANPTPN6physical
9162089
IL3RB_HUMANCSF2RBphysical
11207369
JAK2_HUMANJAK2physical
7775438
RACK1_HUMANGNB2L1physical
10490850
KPCB_HUMANPRKCBphysical
10490850
PTN6_HUMANPTPN6physical
8246974
SHC1_HUMANSHC1physical
10704825
JAK2_HUMANJAK2physical
7527392
1433Z_HUMANYWHAZphysical
10477722
MD2L1_HUMANMAD2L1physical
11551900
JAK2_HUMANJAK2physical
21965659
JAK1_HUMANJAK1physical
21965659
IKKB_HUMANIKBKBphysical
12637324
SOCS1_HUMANSOCS1physical
24086733
VGFR2_HUMANKDRphysical
16007196
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614370Pulmonary surfactant metabolism dysfunction 5 (SMDP5)
Kegg Drug
D05066 Molgramostim (USAN/INN)
D05712 Regramostim (USAN/INN)
D05803 Sargramostim (USAN/INN); 1438 (genetical recombination) (JAN); Leukine (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IL3RB_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"The structure of the GM-CSF receptor complex reveals a distinct modeof cytokine receptor activation.";
Hansen G., Hercus T.R., McClure B.J., Stomski F.C., Dottore M.,Powell J., Ramshaw H., Woodcock J.M., Xu Y., Guthridge M.,McKinstry W.J., Lopez A.F., Parker M.W.;
Cell 134:496-507(2008).
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-438 IN COMPLEX WITH CSF2RAAND CSF2, SUBUNIT, GLYCOSYLATION AT ASN-58 AND ASN-191, AND DISULFIDEBONDS.
"An improved resolution structure of the human beta common receptorinvolved in IL-3, IL-5 and GM-CSF signalling which gives betterdefinition of the high-affinity binding epitope.";
Carr P.D., Conlan F., Ford S., Ollis D.L., Young I.G.;
Acta Crystallogr. F 62:509-513(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 25-443, DISULFIDE BONDS,SUBUNIT, AND GLYCOSYLATION AT ASN-58 AND ASN-191.

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