IBTK_HUMAN - dbPTM
IBTK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IBTK_HUMAN
UniProt AC Q9P2D0
Protein Name Inhibitor of Bruton tyrosine kinase
Gene Name IBTK
Organism Homo sapiens (Human).
Sequence Length 1353
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Translocates to the plasma membrane upon IgM stimulation.
Isoform 2: Nucleus.
Protein Description Acts as an inhibitor of BTK tyrosine kinase activity, thereby playing a role in B-cell development. Down-regulates BTK kinase activity, leading to interference with BTK-mediated calcium mobilization and NF-kappa-B-driven transcription..
Protein Sequence MSSPMPDCTSKCRSLKHALDVLSVVTKGSENQIKAFLSSHCYNAATIKDVFGRNALHLVSSCGKKGVLDWLIQKGVDLLVKDKESGWTALHRSIFYGHIDCVWSLLKHGVSLYIQDKEGLSALDLVMKDRPTHVVFKNTDPTDVYTWGDNTNFTLGHGSQNSKHHPELVDLFSRSGIYIKQVVLCKFHSVFLSQKGQVYTCGHGPGGRLGHGDEQTCLVPRLVEGLNGHNCSQVAAAKDHTVVLTEDGCVYTFGLNIFHQLGIIPPPSSCNVPRQIQAKYLKGRTIIGVAAGRFHTVLWTREAVYTMGLNGGQLGCLLDPNGEKCVTAPRQVSALHHKDIALSLVAASDGATVCVTTRGDIYLLADYQCKKMASKQLNLKKVLVSGGHMEYKVDPEHLKENGGQKICILAMDGAGRVFCWRSVNSSLKQCRWAYPRQVFISDIALNRNEILFVTQDGEGFRGRWFEEKRKSSEKKEILSNLHNSSSDVSYVSDINSVYERIRLEKLTFAHRAVSVSTDPSGCNFAILQSDPKTSLYEIPAVSSSSFFEEFGKLLREADEMDSIHDVTFQVGNRLFPAHKYILAVHSDFFQKLFLSDGNTSEFTDIYQKDEDSAGCHLFVVEKVHPDMFEYLLQFIYTDTCDFLTHGFKPRIHLNKNPEEYQGTLNSHLNKVNFHEDDNQKSAFEVYKSNQAQTVSERQKSKPKSCKKGKNIREDDPVRMLQTVAKKFDFSNLSSRLDGVRFENEKINVIAKNTGNKLKLSQKKCSFLCDVTMKSVDGKEFPCHKCVLCARLEYFHSMLSSSWIEASSCAALEMPIHSDILKVILDYLYTDEAVVIKESQNVDFICSVLVVADQLLITRLKEICEVALTEKLTLKNAAMLLEFAAMYSAKQLKLSCLQFIGLNMAALLEARSLDVLSDGVLKDLSEFYRKMIPAMDRRVITPYQDGPDISYLEVEDGDIFLKEEINMEQNHSETMFKKAKTKAKKKPRKRSDSSGGYNLSDIIQSPSSTGLLKSGKTNSVESLPELLTSDSEGSYAGVGSPRDLQSPDFTTGFHSDKIEAKVKPYVNGTSPVYSREDLKPWEKSPILKISAPQPIPSNRIDTTSSASWVAGSFSPVSPPVVDLRTIMEIEESRQKCGATPKSHLGKTVSHGVKLSQKQRKMIALTTKENNSGMNSMETVLFTPSKAPKPVNAWASSLHSVSSKSFRDFLLEEKKSVTSHSSGDHVKKVSFKGIENSQAPKIVRCSTHGTPGPEGNHISDLPLLDSPNPWLSSSVTAPSMVAPVTFASIVEEELQQEAALIRSREKPLALIQIEEHAIQDLLVFYEAFGNPEEFVIVERTPQGPLAVPMWNKHGC
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
2Phosphorylation------MSSPMPDCT
------CCCCCCCCH
55.2224719451
3Phosphorylation-----MSSPMPDCTS
-----CCCCCCCCHH
36.7625627689
11UbiquitinationPMPDCTSKCRSLKHA
CCCCCHHHHHHHHHH
18.60-
27UbiquitinationDVLSVVTKGSENQIK
HHHHHHCCCCHHHHH
49.15-
64UbiquitinationHLVSSCGKKGVLDWL
HHHHHCCCCCHHHHH
51.16-
81UbiquitinationKGVDLLVKDKESGWT
CCCCEEEECCCCCCC
64.15-
96PhosphorylationALHRSIFYGHIDCVW
HHHHHHHCCHHHHHH
13.21-
104PhosphorylationGHIDCVWSLLKHGVS
CHHHHHHHHHHCCCE
11.9222817900
113PhosphorylationLKHGVSLYIQDKEGL
HHCCCEEEEECCCCC
6.77-
128UbiquitinationSALDLVMKDRPTHVV
CHHHHHCCCCCCEEE
43.01-
137UbiquitinationRPTHVVFKNTDPTDV
CCCEEEECCCCCCCC
47.53-
285PhosphorylationAKYLKGRTIIGVAAG
HHHHCCCEEEEEEEC
26.14-
296PhosphorylationVAAGRFHTVLWTREA
EEECCCEEEEEECHH
18.00-
300PhosphorylationRFHTVLWTREAVYTM
CCEEEEEECHHHEEC
17.92-
305PhosphorylationLWTREAVYTMGLNGG
EEECHHHEECCCCCC
9.6922210691
306PhosphorylationWTREAVYTMGLNGGQ
EECHHHEECCCCCCC
9.7322210691
375UbiquitinationQCKKMASKQLNLKKV
HHHHHHHCCCCCCEE
49.63-
381UbiquitinationSKQLNLKKVLVSGGH
HCCCCCCEEEEECCC
43.92-
475UbiquitinationKRKSSEKKEILSNLH
HCCCHHHHHHHHHHC
46.03-
479PhosphorylationSEKKEILSNLHNSSS
HHHHHHHHHHCCCCC
42.9023879269
484PhosphorylationILSNLHNSSSDVSYV
HHHHHCCCCCCCCHH
22.0723879269
485PhosphorylationLSNLHNSSSDVSYVS
HHHHCCCCCCCCHHH
35.5627251275
486PhosphorylationSNLHNSSSDVSYVSD
HHHCCCCCCCCHHHC
41.6827251275
490PhosphorylationNSSSDVSYVSDINSV
CCCCCCCHHHCHHHH
12.1127642862
505UbiquitinationYERIRLEKLTFAHRA
HHHHHHHHCCCCEEE
58.37-
514PhosphorylationTFAHRAVSVSTDPSG
CCCEEEEEECCCCCC
14.9030576142
516PhosphorylationAHRAVSVSTDPSGCN
CEEEEEECCCCCCCC
21.4230576142
520PhosphorylationVSVSTDPSGCNFAIL
EEECCCCCCCCEEEE
59.8130576142
599PhosphorylationLFLSDGNTSEFTDIY
HHCCCCCHHHCEEHH
34.85-
608UbiquitinationEFTDIYQKDEDSAGC
HCEEHHHCCCCCCCC
46.22-
630PhosphorylationVHPDMFEYLLQFIYT
CCHHHHHHHHHHHHH
11.0517053785
655UbiquitinationKPRIHLNKNPEEYQG
CCCEECCCCHHHHCH
79.02-
660PhosphorylationLNKNPEEYQGTLNSH
CCCCHHHHCHHHHHH
15.5825627689
663PhosphorylationNPEEYQGTLNSHLNK
CHHHHCHHHHHHHHC
13.7728555341
670UbiquitinationTLNSHLNKVNFHEDD
HHHHHHHCCCCCCCC
44.94-
680UbiquitinationFHEDDNQKSAFEVYK
CCCCCCCCCHHHHHH
50.43-
687MethylationKSAFEVYKSNQAQTV
CCHHHHHHHHHHCCH
48.3742353373
687UbiquitinationKSAFEVYKSNQAQTV
CCHHHHHHHHHHCCH
48.372190698
687 (in isoform 1)Ubiquitination-48.3721906983
687 (in isoform 2)Ubiquitination-48.3721906983
688PhosphorylationSAFEVYKSNQAQTVS
CHHHHHHHHHHCCHH
19.2523403867
695PhosphorylationSNQAQTVSERQKSKP
HHHHCCHHHHHHCCC
30.3723403867
725UbiquitinationRMLQTVAKKFDFSNL
HHHHHHHHHCCCCCH
50.03-
726UbiquitinationMLQTVAKKFDFSNLS
HHHHHHHHCCCCCHH
40.19-
745UbiquitinationGVRFENEKINVIAKN
CEEECCCEEEEEEEC
51.68-
751UbiquitinationEKINVIAKNTGNKLK
CEEEEEEECCCCCEE
43.87-
765PhosphorylationKLSQKKCSFLCDVTM
ECCCCCHHHEECCEE
30.0829449344
771PhosphorylationCSFLCDVTMKSVDGK
HHHEECCEEEECCCC
12.9629449344
774PhosphorylationLCDVTMKSVDGKEFP
EECCEEEECCCCCCC
18.0229449344
872PhosphorylationVALTEKLTLKNAAML
HHCCCCCCHHHHHHH
46.9124719451
886PhosphorylationLLEFAAMYSAKQLKL
HHHHHHHHCHHHHHH
10.7626670566
887PhosphorylationLEFAAMYSAKQLKLS
HHHHHHHCHHHHHHH
18.8626670566
949PhosphorylationYQDGPDISYLEVEDG
CCCCCCCEEEEEECC
30.92-
950PhosphorylationQDGPDISYLEVEDGD
CCCCCCEEEEEECCC
13.76-
981AcetylationMFKKAKTKAKKKPRK
HHHHHHHHCCCCCCC
58.4669567
984AcetylationKAKTKAKKKPRKRSD
HHHHHCCCCCCCCCC
73.2488605
990PhosphorylationKKKPRKRSDSSGGYN
CCCCCCCCCCCCCCC
44.9030278072
992PhosphorylationKPRKRSDSSGGYNLS
CCCCCCCCCCCCCHH
31.9330278072
993PhosphorylationPRKRSDSSGGYNLSD
CCCCCCCCCCCCHHH
41.0230278072
996PhosphorylationRSDSSGGYNLSDIIQ
CCCCCCCCCHHHHHC
19.2230278072
999PhosphorylationSSGGYNLSDIIQSPS
CCCCCCHHHHHCCCC
24.1123927012
1004PhosphorylationNLSDIIQSPSSTGLL
CHHHHHCCCCCCCCC
19.1523927012
1006PhosphorylationSDIIQSPSSTGLLKS
HHHHCCCCCCCCCCC
45.8623927012
1007PhosphorylationDIIQSPSSTGLLKSG
HHHCCCCCCCCCCCC
29.8523927012
1008PhosphorylationIIQSPSSTGLLKSGK
HHCCCCCCCCCCCCC
35.8723927012
1013PhosphorylationSSTGLLKSGKTNSVE
CCCCCCCCCCCCCCH
45.5522617229
1016PhosphorylationGLLKSGKTNSVESLP
CCCCCCCCCCCHHHH
35.9320873877
1018PhosphorylationLKSGKTNSVESLPEL
CCCCCCCCCHHHHHH
32.2829116813
1021PhosphorylationGKTNSVESLPELLTS
CCCCCCHHHHHHHHC
47.2530175587
1027PhosphorylationESLPELLTSDSEGSY
HHHHHHHHCCCCCCC
43.0120873877
1028PhosphorylationSLPELLTSDSEGSYA
HHHHHHHCCCCCCCC
38.8225159151
1030PhosphorylationPELLTSDSEGSYAGV
HHHHHCCCCCCCCCC
43.5627732954
1033PhosphorylationLTSDSEGSYAGVGSP
HHCCCCCCCCCCCCC
14.0427732954
1034PhosphorylationTSDSEGSYAGVGSPR
HCCCCCCCCCCCCCC
20.4522115753
1039PhosphorylationGSYAGVGSPRDLQSP
CCCCCCCCCCCCCCC
17.8526074081
1045PhosphorylationGSPRDLQSPDFTTGF
CCCCCCCCCCCCCCC
33.4629255136
1049PhosphorylationDLQSPDFTTGFHSDK
CCCCCCCCCCCCCCC
33.1323927012
1050PhosphorylationLQSPDFTTGFHSDKI
CCCCCCCCCCCCCCC
37.5323927012
1054PhosphorylationDFTTGFHSDKIEAKV
CCCCCCCCCCCEEEE
38.0323927012
1064PhosphorylationIEAKVKPYVNGTSPV
CEEEEECCCCCCCCC
10.7928450419
1068PhosphorylationVKPYVNGTSPVYSRE
EECCCCCCCCCCCHH
25.3425159151
1069PhosphorylationKPYVNGTSPVYSRED
ECCCCCCCCCCCHHH
17.4825159151
1072PhosphorylationVNGTSPVYSREDLKP
CCCCCCCCCHHHCCC
12.8528450419
1073PhosphorylationNGTSPVYSREDLKPW
CCCCCCCCHHHCCCC
29.4528450419
1078UbiquitinationVYSREDLKPWEKSPI
CCCHHHCCCCCCCCC
61.48-
1082UbiquitinationEDLKPWEKSPILKIS
HHCCCCCCCCCEEEE
58.63-
1083PhosphorylationDLKPWEKSPILKISA
HCCCCCCCCCEEEEC
12.9823401153
1087UbiquitinationWEKSPILKISAPQPI
CCCCCCEEEECCCCC
35.02-
1096PhosphorylationSAPQPIPSNRIDTTS
ECCCCCCCCCCCCCC
39.19-
1101PhosphorylationIPSNRIDTTSSASWV
CCCCCCCCCCCCCCC
26.6328176443
1102PhosphorylationPSNRIDTTSSASWVA
CCCCCCCCCCCCCCC
19.5528176443
1103PhosphorylationSNRIDTTSSASWVAG
CCCCCCCCCCCCCCC
26.4630576142
1104PhosphorylationNRIDTTSSASWVAGS
CCCCCCCCCCCCCCC
24.9930576142
1106PhosphorylationIDTTSSASWVAGSFS
CCCCCCCCCCCCCCC
24.8320873877
1111PhosphorylationSASWVAGSFSPVSPP
CCCCCCCCCCCCCCC
16.8922496350
1113PhosphorylationSWVAGSFSPVSPPVV
CCCCCCCCCCCCCEE
26.5328176443
1116PhosphorylationAGSFSPVSPPVVDLR
CCCCCCCCCCEECHH
27.2028176443
1138PhosphorylationSRQKCGATPKSHLGK
HHHHHCCCCHHHHCC
19.28-
1140MethylationQKCGATPKSHLGKTV
HHHCCCCHHHHCCHH
46.26115971303
1141PhosphorylationKCGATPKSHLGKTVS
HHCCCCHHHHCCHHH
25.75-
1145MethylationTPKSHLGKTVSHGVK
CCHHHHCCHHHHCCC
52.71115971311
1145UbiquitinationTPKSHLGKTVSHGVK
CCHHHHCCHHHHCCC
52.71-
1152UbiquitinationKTVSHGVKLSQKQRK
CHHHHCCCCCHHHHH
47.19-
1154PhosphorylationVSHGVKLSQKQRKMI
HHHCCCCCHHHHHHE
29.6128555341
1181PhosphorylationSMETVLFTPSKAPKP
CCCEEEECCCCCCCC
23.6121815630
1183PhosphorylationETVLFTPSKAPKPVN
CEEEECCCCCCCCCC
38.0927050516
1195PhosphorylationPVNAWASSLHSVSSK
CCCHHHHHCHHCCCH
23.5025627689
1198PhosphorylationAWASSLHSVSSKSFR
HHHHHCHHCCCHHHH
29.0525159151
1200PhosphorylationASSLHSVSSKSFRDF
HHHCHHCCCHHHHHH
34.7521482705
1202UbiquitinationSLHSVSSKSFRDFLL
HCHHCCCHHHHHHHH
46.22-
1203PhosphorylationLHSVSSKSFRDFLLE
CHHCCCHHHHHHHHH
27.7121482705
1212UbiquitinationRDFLLEEKKSVTSHS
HHHHHHHHHCCCCCC
40.76-
1213UbiquitinationDFLLEEKKSVTSHSS
HHHHHHHHCCCCCCC
54.13-
12252-HydroxyisobutyrylationHSSGDHVKKVSFKGI
CCCCCCCEEEEECCC
44.00-
1230MethylationHVKKVSFKGIENSQA
CCEEEEECCCCCCCC
52.01115971319
1230AcetylationHVKKVSFKGIENSQA
CCEEEEECCCCCCCC
52.0126051181
1239UbiquitinationIENSQAPKIVRCSTH
CCCCCCCCEEEEECC
57.77-
1350UbiquitinationLAVPMWNKHGC----
CCCCCCCCCCC----
26.34-

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
1200SPhosphorylationKinasePRKCBP05771
GPS
1203SPhosphorylationKinasePRKCBP05771
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IBTK_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 IBTK_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BTK_HUMANBTKphysical
11577348
BTK_HUMANBTKphysical
21482705
LTOR3_HUMANLAMTOR3physical
21988832
CUL3_HUMANCUL3physical
25882842
RBX1_HUMANRBX1physical
25882842
IBTK_HUMANIBTKphysical
25882842
CAND1_HUMANCAND1physical
25882842
CSN2_HUMANCOPS2physical
25882842
CSN4_HUMANCOPS4physical
25882842
UBA1_HUMANUBA1physical
25882842
UBC_HUMANUBCphysical
25882842
CSN3_HUMANCOPS3physical
25882842
PDCD4_HUMANPDCD4physical
25882842
IF4A1_HUMANEIF4A1physical
26496610
RFC1_HUMANRFC1physical
26496610
RFC3_HUMANRFC3physical
26496610
RFC4_HUMANRFC4physical
26496610
RL6_HUMANRPL6physical
26496610
RLA0_HUMANRPLP0physical
26496610
RLA1_HUMANRPLP1physical
26496610
RS3_HUMANRPS3physical
26496610
RS8_HUMANRPS8physical
26496610
RS9_HUMANRPS9physical
26496610
RS27_HUMANRPS27physical
26496610
SRP72_HUMANSRP72physical
26496610
UBP10_HUMANUSP10physical
26496610
DDX21_HUMANDDX21physical
26496610
ESPL1_HUMANESPL1physical
26496610
POP7_HUMANPOP7physical
26496610
DHX30_HUMANDHX30physical
26496610
WDR74_HUMANWDR74physical
26496610
NAT10_HUMANNAT10physical
26496610
TSR1_HUMANTSR1physical
26496610
LACTB_HUMANLACTBphysical
26496610
RP25L_HUMANRPP25Lphysical
26496610
MSL1_HUMANMSL1physical
26496610

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IBTK_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-990; SER-992; SER-993;SER-1004; SER-1045 AND SER-1054, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1045, AND MASSSPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-630, AND MASSSPECTROMETRY.

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