TBKB1_HUMAN - dbPTM
TBKB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBKB1_HUMAN
UniProt AC A7MCY6
Protein Name TANK-binding kinase 1-binding protein 1
Gene Name TBKBP1 {ECO:0000312|EMBL:AAI11419.1}
Organism Homo sapiens (Human).
Sequence Length 615
Subcellular Localization
Protein Description Adapter protein which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity..
Protein Sequence MESMFEDDISILTQEALGPSEVWLDSPGDPSLGGDMCSASHFALITAYGDIKERLGGLERENATLRRRLKVYEIKYPLISDFGEEHGFSLYEIKDGSLLEVEKVSLQQRLNQFQHELQKNKEQEEQLGEMIQAYEKLCVEKSDLETELREMRALVETHLRQICGLEQQLRQQQGLQDAAFSNLSPPPAPAPPCTDLDLHYLALRGGSGLSHAGWPGSTPSVSDLERRRLEEALEAAQGEARGAQLREEQLQAECERLQGELKQLQETRAQDLASNQSERDMAWVKRVGDDQVNLALAYTELTEELGRLRELSSLQGRILRTLLQEQARSGGQRHSPLSQRHSPAPQCPSPSPPARAAPPCPPCQSPVPQRRSPVPPCPSPQQRRSPASPSCPSPVPQRRSPVPPSCQSPSPQRRSPVPPSCPAPQPRPPPPPPPGERTLAERAYAKPPSHHVKAGFQGRRSYSELAEGAAYAGASPPWLQAEAATLPKPRAYGSELYGPGRPLSPRRAFEGIRLRFEKQPSEEDEWAVPTSPPSPEVGTIRCASFCAGFPIPESPAATAYAHAEHAQSWPSINLLMETVGSDIRSCPLCQLGFPVGYPDDALIKHIDSHLENSKI
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
10PhosphorylationSMFEDDISILTQEAL
CCCCCHHHHHHHHHH		20.66-
13PhosphorylationEDDISILTQEALGPS
CCHHHHHHHHHHCCC		23.77-
48PhosphorylationHFALITAYGDIKERL
HHHHHHHHHCHHHHH		13.49-
70UbiquitinationATLRRRLKVYEIKYP
HHHHHHHEEEEECCC		40.7429967540
91PhosphorylationEEHGFSLYEIKDGSL
HHHCEEEEEECCCCE		17.8927642862
94UbiquitinationGFSLYEIKDGSLLEV
CEEEEEECCCCEEEE		44.06-
97PhosphorylationLYEIKDGSLLEVEKV
EEEECCCCEEEEEEC		39.6622617229
103UbiquitinationGSLLEVEKVSLQQRL
CCEEEEEECCHHHHH		42.1529967540
105PhosphorylationLLEVEKVSLQQRLNQ
EEEEEECCHHHHHHH		31.3727251275
119UbiquitinationQFQHELQKNKEQEEQ
HHHHHHHHCHHHHHH		80.6729967540
121UbiquitinationQHELQKNKEQEEQLG
HHHHHHCHHHHHHHH		68.74-
157PhosphorylationEMRALVETHLRQICG
HHHHHHHHHHHHHHC		20.8028857561
181PhosphorylationGLQDAAFSNLSPPPA
CCCHHHHCCCCCCCC		31.9419369195
184PhosphorylationDAAFSNLSPPPAPAP
HHHHCCCCCCCCCCC		39.3419369195
262 (in isoform 1)Ubiquitination-44.6621906983
262UbiquitinationERLQGELKQLQETRA
HHHHHHHHHHHHHHH		44.662190698
285UbiquitinationERDMAWVKRVGDDQV
HHHHHHHHHHCHHHH		30.57-
329PhosphorylationLLQEQARSGGQRHSP
HHHHHHHHCCCCCCC		50.7430377224
335PhosphorylationRSGGQRHSPLSQRHS
HHCCCCCCCCHHCCC		29.7127422710
338PhosphorylationGQRHSPLSQRHSPAP
CCCCCCCHHCCCCCC		28.6627732954
342PhosphorylationSPLSQRHSPAPQCPS
CCCHHCCCCCCCCCC		25.5827732954
349PhosphorylationSPAPQCPSPSPPARA
CCCCCCCCCCCCCCC		45.7128450419
351PhosphorylationAPQCPSPSPPARAAP
CCCCCCCCCCCCCCC		48.1028450419
365PhosphorylationPPCPPCQSPVPQRRS
CCCCCCCCCCCCCCC		34.2830266825
372PhosphorylationSPVPQRRSPVPPCPS
CCCCCCCCCCCCCCC		32.2230266825
379PhosphorylationSPVPPCPSPQQRRSP
CCCCCCCCHHHCCCC		41.9030266825
385PhosphorylationPSPQQRRSPASPSCP
CCHHHCCCCCCCCCC		27.3222617229
388PhosphorylationQQRRSPASPSCPSPV
HHCCCCCCCCCCCCC		22.2621712546
390PhosphorylationRRSPASPSCPSPVPQ
CCCCCCCCCCCCCCC		35.8427732954
393PhosphorylationPASPSCPSPVPQRRS
CCCCCCCCCCCCCCC		42.7428985074
400PhosphorylationSPVPQRRSPVPPSCQ
CCCCCCCCCCCCCCC		32.2230266825
405PhosphorylationRRSPVPPSCQSPSPQ
CCCCCCCCCCCCCCC		20.7927732954
408PhosphorylationPVPPSCQSPSPQRRS
CCCCCCCCCCCCCCC		31.5027251275
410PhosphorylationPPSCQSPSPQRRSPV
CCCCCCCCCCCCCCC		38.6227732954
415PhosphorylationSPSPQRRSPVPPSCP
CCCCCCCCCCCCCCC		32.2230266825
420PhosphorylationRRSPVPPSCPAPQPR
CCCCCCCCCCCCCCC		27.0226552605
461PhosphorylationAGFQGRRSYSELAEG
CCCCCCCCHHHHHHH		31.4828348404
462PhosphorylationGFQGRRSYSELAEGA
CCCCCCCHHHHHHHH		12.3527251275
463PhosphorylationFQGRRSYSELAEGAA
CCCCCCHHHHHHHHH		27.6428348404
485PhosphorylationWLQAEAATLPKPRAY
HHHHHHHCCCCCCCC		51.1224719451
492PhosphorylationTLPKPRAYGSELYGP
CCCCCCCCCCCCCCC		23.5923186163
494PhosphorylationPKPRAYGSELYGPGR
CCCCCCCCCCCCCCC		16.2623186163
497PhosphorylationRAYGSELYGPGRPLS
CCCCCCCCCCCCCCC		19.7523186163
504PhosphorylationYGPGRPLSPRRAFEG
CCCCCCCCHHHHHCC		21.0230266825
513MethylationRRAFEGIRLRFEKQP
HHHHCCEEEEEECCC		30.57115918285
521PhosphorylationLRFEKQPSEEDEWAV
EEEECCCCCCCCCCC		51.6427251275
531PhosphorylationDEWAVPTSPPSPEVG
CCCCCCCCCCCCCCC		28.8325921289
534PhosphorylationAVPTSPPSPEVGTIR
CCCCCCCCCCCCCEE		36.7625921289
539PhosphorylationPPSPEVGTIRCASFC
CCCCCCCCEEEHHHH		15.4922468782
613PhosphorylationIDSHLENSKI-----
HHHHHHHCCC-----		23.5028555341
614UbiquitinationDSHLENSKI------
HHHHHHCCC------		65.11-
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

Oops, there are no upstream regulatory protein records of TBKB1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBKB1_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 TBKB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACD11_HUMANACAD11physical
21903422
AGO2_HUMANAGO2physical
21903422
APBA3_HUMANAPBA3physical
21903422
FMR1_HUMANFMR1physical
21903422
FXR2_HUMANFXR2physical
21903422
IKKE_HUMANIKBKEphysical
21903422
OBSL1_HUMANOBSL1physical
21903422
RBCC1_HUMANRB1CC1physical
21903422
TBK1_HUMANTBK1physical
21903422
IKKE_HUMANIKBKEphysical
17568778
TBK1_HUMANTBK1physical
17568778
AZI2_HUMANAZI2physical
17568778
TBKB1_HUMANTBKBP1physical
17568778
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 TBKB1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-184; SER-335;SER-349; SER-351; SER-365; SER-372; SER-379; SER-385; SER-388;SER-390; SER-400; SER-405; SER-415; SER-504; SER-521 AND SER-534, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372; SER-379 ANDSER-400, AND MASS SPECTROMETRY.

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