CBLB_MOUSE - dbPTM
CBLB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CBLB_MOUSE
UniProt AC Q3TTA7
Protein Name E3 ubiquitin-protein ligase CBL-B
Gene Name Cblb
Organism Mus musculus (Mouse).
Sequence Length 982
Subcellular Localization Cytoplasm . In adipocytes, translocates to the plasma membrane upon insulin stimulation.
Protein Description E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T-cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. Slightly promotes SRC ubiquitination. May be involved in EGFR ubiquitination and internalization. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3..
Protein Sequence MANSMNGRNPGGRGGNPRKGRILGIIDAIQDAVGPPKQAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFDPRDEGSRCCSIIDPFSIPMLDLDDDDDREESLMMNRLASVRKCTDRQNSPVTSPGSSPLAQRRKPQPDPLQIPHLSLPPVPPRLDLIQKGIVRSPCGSPTGSPKSSPCMVRKQDKPLPAPPPPLRDPPPPPERPPPIPPDNRLSRHFHHGESVPSRDQPMPLEAWCPRDAFGTNQVMGCRILGDGSPKPGVTANSSLNGRHSRMGSEQVLMRKHRRHDLPSEGAKVFSNGHLATEEYDVPPRLSPPPPVTTLLPSIKCTGPLANCLSEKTRDTVEDDDDEYKIPSSHPVSLNSQPSHCHNVKAPVRSCDNGHCILNGTHGAPSEMKKSNIPDLGIYLKGGGSDSASDPVPLPPARPPPRDSPKHGSSVNRTPSDYDLLIPPLGEDAFDALPPSLPPPPPPARHSLIEHSKPPGSSSRPSSGQDLFLLPSDPFFDPTSGQVPLPPARRAAGDSGKANRASQDYDQLPSSSDGSQAPARPPKPRPRRTAPEIHHRKPHGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFPPPVSPRLNL
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
4Phosphorylation----MANSMNGRNPG
----CCCCCCCCCCC		12.2329514104
48AcetylationADRRTVEKTWKLMDK
HHHHHHHHHHHHHHH		56.1823864654
48MalonylationADRRTVEKTWKLMDK
HHHHHHHHHHHHHHH		56.1826320211
282PhosphorylationKYSTKPGSYIFRLSC
HHCCCCCCEEEEEEC		24.47-
356PhosphorylationPHDHIKVTQEQYELY
CCCCCEECHHHHHHH		22.7625266776
363PhosphorylationTQEQYELYCEMGSTF
CHHHHHHHHHCCCHH		3.7126026062
466PhosphorylationLMMNRLASVRKCTDR
HHHHHHHHHHHCCCC		27.3524719451
471PhosphorylationLASVRKCTDRQNSPV
HHHHHHCCCCCCCCC		36.9324759943
476PhosphorylationKCTDRQNSPVTSPGS
HCCCCCCCCCCCCCC		16.6521082442
479PhosphorylationDRQNSPVTSPGSSPL
CCCCCCCCCCCCCCC		32.3721082442
480PhosphorylationRQNSPVTSPGSSPLA
CCCCCCCCCCCCCCH		27.7421082442
483PhosphorylationSPVTSPGSSPLAQRR
CCCCCCCCCCCHHCC		31.9721082442
484PhosphorylationPVTSPGSSPLAQRRK
CCCCCCCCCCHHCCC		29.8221082442
520DimethylationLIQKGIVRSPCGSPT
HHHCCCCCCCCCCCC		32.72-
521PhosphorylationIQKGIVRSPCGSPTG
HHCCCCCCCCCCCCC		17.4127087446
525PhosphorylationIVRSPCGSPTGSPKS
CCCCCCCCCCCCCCC		26.4625521595
527PhosphorylationRSPCGSPTGSPKSSP
CCCCCCCCCCCCCCC		52.5725619855
529PhosphorylationPCGSPTGSPKSSPCM
CCCCCCCCCCCCCCE		31.4723684622
532PhosphorylationSPTGSPKSSPCMVRK
CCCCCCCCCCCEEEC		42.7824759943
533PhosphorylationPTGSPKSSPCMVRKQ
CCCCCCCCCCEEECC		28.3925521595
613PhosphorylationCRILGDGSPKPGVTA
EEECCCCCCCCCCCC		34.1926643407
622PhosphorylationKPGVTANSSLNGRHS
CCCCCCCHHCCCCCC		33.4728285833
623PhosphorylationPGVTANSSLNGRHSR
CCCCCCHHCCCCCCC		26.1725266776
629PhosphorylationSSLNGRHSRMGSEQV
HHCCCCCCCCCCHHH		23.7025266776
633PhosphorylationGRHSRMGSEQVLMRK
CCCCCCCCHHHHHHH		18.6029176673
655PhosphorylationSEGAKVFSNGHLATE
CCCCEEECCCCCCCC		44.9126745281
661PhosphorylationFSNGHLATEEYDVPP
ECCCCCCCCCCCCCC		35.3926745281
664PhosphorylationGHLATEEYDVPPRLS
CCCCCCCCCCCCCCC		18.9312842890
671PhosphorylationYDVPPRLSPPPPVTT
CCCCCCCCCCCCCCC		36.3227180971
677PhosphorylationLSPPPPVTTLLPSIK
CCCCCCCCCCCCCCC		19.9426745281
678PhosphorylationSPPPPVTTLLPSIKC
CCCCCCCCCCCCCCC		26.9126745281
697PhosphorylationANCLSEKTRDTVEDD
HHHCCHHHCCCCCCC		29.7126643407
700PhosphorylationLSEKTRDTVEDDDDE
CCHHHCCCCCCCCCC		23.6226643407
708PhosphorylationVEDDDDEYKIPSSHP
CCCCCCCCCCCCCCC		22.6312842890
712PhosphorylationDDEYKIPSSHPVSLN
CCCCCCCCCCCCCCC		44.7626643407
713PhosphorylationDEYKIPSSHPVSLNS
CCCCCCCCCCCCCCC		26.8426643407
717PhosphorylationIPSSHPVSLNSQPSH
CCCCCCCCCCCCCCC		26.7026643407
720PhosphorylationSHPVSLNSQPSHCHN
CCCCCCCCCCCCCCC		49.0826643407
763PhosphorylationNIPDLGIYLKGGGSD
CCCCCEEEECCCCCC		10.6818515860
788PhosphorylationARPPPRDSPKHGSSV
CCCCCCCCCCCCCCC		36.8125619855
886PhosphorylationSGKANRASQDYDQLP
CCCCCCCCCCHHHCC		21.9822499769
889PhosphorylationANRASQDYDQLPSSS
CCCCCCCHHHCCCCC		9.6518515860
894PhosphorylationQDYDQLPSSSDGSQA
CCHHHCCCCCCCCCC		51.5828066266
895PhosphorylationDYDQLPSSSDGSQAP
CHHHCCCCCCCCCCC		30.4325777480
896PhosphorylationYDQLPSSSDGSQAPA
HHHCCCCCCCCCCCC		50.7825777480
899PhosphorylationLPSSSDGSQAPARPP
CCCCCCCCCCCCCCC		28.3225777480
965PhosphorylationNNVEVARSILREFAF
HHHHHHHHHHHHHCC		19.0830387612
977PhosphorylationFAFPPPVSPRLNL--
HCCCCCCCCCCCC--		15.2927180971
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
282SPhosphorylationKinasePRKCQQ02111
Uniprot
476SPhosphorylationKinaseGSK3AQ2NL51
PSP
476SPhosphorylationKinaseGSK3BQ9WV60
PSP
480SPhosphorylationKinaseGSK3AQ2NL51
PSP
480SPhosphorylationKinaseGSK3BQ9WV60
PSP
-KUbiquitinationE3 ubiquitin ligaseCblbQ3TTA7
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseNedd4P46935
PMID:18931680:12907674
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CBLB_MOUSE !!
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 CBLB_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TLR4_MOUSETlr4physical
17618294
ARHG7_MOUSEArhgef7physical
16892055
MYD88_MOUSEMyd88physical
20639876
TCAM1_MOUSETicam1physical
20639876
CRKL_MOUSECrklphysical
12697763
PSMD1_MOUSEPsmd1physical
17182860
PSMD6_MOUSEPsmd6physical
17182860
CRK_MOUSECrkphysical
12842890
SRBS1_MOUSESorbs1physical
12842890
CBLB_MOUSECblbphysical
12842890
CBL_MOUSECblphysical
12102152
SMAD7_MOUSESmad7physical
23709694
UBE2C_MOUSEUbe2cphysical
23709694
UBC_MOUSEUbcphysical
17182860
ITK_MOUSEItkgenetic
19009524
PTN6_MOUSEPtpn6physical
26416283
PTN11_MOUSEPtpn11physical
26416283
CBLB_MOUSECblbphysical
26416283
UB2D1_MOUSEUbe2d1physical
26416283
KSYK_MOUSESykphysical
27428901
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CBLB_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-889, AND MASSSPECTROMETRY.
"The roles of Cbl-b and c-Cbl in insulin-stimulated glucosetransport.";
Liu J., DeYoung S.M., Hwang J.B., O'Leary E.E., Saltiel A.R.;
J. Biol. Chem. 278:36754-36762(2003).
Cited for: PHOSPHORYLATION AT TYR-664 AND TYR-708, INTERACTION WITH CBL; CRK ANDSORBS1, AND SUBCELLULAR LOCATION.

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