dbPTM

TBK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBK1_HUMAN
UniProt AC	Q9UHD2
Protein Name	Serine/threonine-protein kinase TBK1
Gene Name	TBK1
Organism	Homo sapiens (Human).
Sequence Length	729
Subcellular Localization	Cytoplasm . Upon mitogen stimulation or triggering of the immune system, TBK1 is recruited to the exocyst by EXOC2.
Protein Description	Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents. Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB. In order to establish such an antiviral state, TBK1 form several different complexes whose composition depends on the type of cell and cellular stimuli. Thus, several scaffolding molecules including FADD, TRADD, MAVS, AZI2, TANK or TBKBP1/SINTBAD can be recruited to the TBK1-containing-complexes. Under particular conditions, functions as a NF-kappa-B effector by phosphorylating NF-kappa-B inhibitor alpha/NFKBIA, IKBKB or RELA to translocate NF-Kappa-B to the nucleus. Restricts bacterial proliferation by phosphorylating the autophagy receptor OPTN/Optineurin on 'Ser-177', thus enhancing LC3 binding affinity and antibacterial autophagy. [PubMed: 21617041 Phosphorylates SMCR8 component of the C9orf72-SMCR8 complex, promoting autophagosome maturation]
Protein Sequence	MQSTSNHLWLLSDILGQGATANVFRGRHKKTGDLFAIKVFNNISFLRPVDVQMREFEVLKKLNHKNIVKLFAIEEETTTRHKVLIMEFCPCGSLYTVLEEPSNAYGLPESEFLIVLRDVVGGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVYKLTDFGAARELEDDEQFVSLYGTEEYLHPDMYERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFRPFEGPRRNKEVMYKIITGKPSGAISGVQKAENGPIDWSGDMPVSCSLSRGLQVLLTPVLANILEADQEKCWGFDQFFAETSDILHRMVIHVFSLQQMTAHKIYIHSYNTATIFHELVYKQTKIISSNQELIYEGRRLVLEPGRLAQHFPKTTEENPIFVVSREPLNTIGLIYEKISLPKVHPRYDLDGDASMAKAITGVVCYACRIASTLLLYQELMRKGIRWLIELIKDDYNETVHKKTEVVITLDFCIRNIEKTVKVYEKLMKINLEAAELGEISDIHTKLLRLSSSQGTIETSLQDIDSRLSPGGSLADAWAHQEGTHPKDRNVEKLQVLLNCMTEIYYQFKKDKAERRLAYNEEQIHKFDKQKLYYHATKAMTHFTDECVKKYEAFLNKSEEWIRKMLHLRKQLLSLTNQCFDIEEEVSKYQEYTNELQETLPQKMFTASSGIKHTMTPIYPSSNTLVEMTLGMKKLKEEMEGVVKELAENNHILERFGSLTMDGGLRNVDCL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MQSTSNHLWL -----CCCCCHHHHH	32.29	24043423
4	Phosphorylation	----MQSTSNHLWLL ----CCCCCHHHHHH	19.36	24043423
5	Phosphorylation	---MQSTSNHLWLLS ---CCCCCHHHHHHH	27.74	24043423
12	Phosphorylation	SNHLWLLSDILGQGA CHHHHHHHHHHCCCC	22.04	24043423
20	Phosphorylation	DILGQGATANVFRGR HHHCCCCCEEECCCC	26.11	24043423
30	Ubiquitination	VFRGRHKKTGDLFAI ECCCCCCCCCCEEEE	52.17	PubMed
30	Malonylation	VFRGRHKKTGDLFAI ECCCCCCCCCCEEEE	52.17	30639696
60	Ubiquitination	MREFEVLKKLNHKNI HHHHHHHHHCCCCCC	61.46	27667366
65	Ubiquitination	VLKKLNHKNIVKLFA HHHHCCCCCCEEEEE	47.50	29967540
69	Ubiquitination	LNHKNIVKLFAIEEE CCCCCCEEEEEEECC	33.81	29967540
77	Phosphorylation	LFAIEEETTTRHKVL EEEEECCCCCCCEEE	36.43	27307780
78	Phosphorylation	FAIEEETTTRHKVLI EEEECCCCCCCEEEE	25.72	27307780
79	Phosphorylation	AIEEETTTRHKVLIM EEECCCCCCCEEEEE	37.89	27307780
137	Ubiquitination	GIVHRDIKPGNIMRV CCCCCCCCCCCEEEE	51.68	22817900
151	Phosphorylation	VIGEDGQSVYKLTDF EECCCCCEEEEECCC	32.70	20071362
153	Phosphorylation	GEDGQSVYKLTDFGA CCCCCEEEEECCCCC	12.91	22817900
154	Ubiquitination	EDGQSVYKLTDFGAA CCCCEEEEECCCCCC	42.63	21906983
172	Phosphorylation	EDDEQFVSLYGTEEY CCHHHHHHHHCCHHH	19.70	22322096
174	Phosphorylation	DEQFVSLYGTEEYLH HHHHHHHHCCHHHCC	17.94	29978859
176	Phosphorylation	QFVSLYGTEEYLHPD HHHHHHCCHHHCCCH	16.46	29978859
179	Phosphorylation	SLYGTEEYLHPDMYE HHHCCHHHCCCHHHH	12.22	29978859
185	Phosphorylation	EYLHPDMYERAVLRK HHCCCHHHHHHHHCH	15.05	29978859
231	Ubiquitination	FEGPRRNKEVMYKII CCCCCCCCEEEEEHH	50.29	27667366
236	Ubiquitination	RNKEVMYKIITGKPS CCCEEEEEHHCCCCC	14.99	22817900
241	Ubiquitination	MYKIITGKPSGAISG EEEHHCCCCCCCCCC	27.62	21906983
247	Phosphorylation	GKPSGAISGVQKAEN CCCCCCCCCEEECCC	32.17	-
251	Ubiquitination	GAISGVQKAENGPID CCCCCEEECCCCCCC	56.09	29967540
278	Phosphorylation	RGLQVLLTPVLANIL HCHHHHHHHHHHHHH	13.74	-
291	Ubiquitination	ILEADQEKCWGFDQF HHHHHHHHHHCCCHH	29.65	-
325	Phosphorylation	QMTAHKIYIHSYNTA HHCCCEEEEEECCHH	9.44	23663014
328	Phosphorylation	AHKIYIHSYNTATIF CCEEEEEECCHHHHH	15.54	23663014
329	Phosphorylation	HKIYIHSYNTATIFH CEEEEEECCHHHHHH	11.45	23663014
331	Phosphorylation	IYIHSYNTATIFHEL EEEEECCHHHHHHHH	19.56	23663014
333	Phosphorylation	IHSYNTATIFHELVY EEECCHHHHHHHHHH	23.33	23663014
340	Phosphorylation	TIFHELVYKQTKIIS HHHHHHHHHHHEEEC	15.25	23663014
341	Ubiquitination	IFHELVYKQTKIISS HHHHHHHHHHEEECC	43.97	22817900
344	Ubiquitination	ELVYKQTKIISSNQE HHHHHHHEEECCCCE	35.23	22817900
347	Phosphorylation	YKQTKIISSNQELIY HHHHEEECCCCEEEE	27.06	20071362
354	Phosphorylation	SSNQELIYEGRRLVL CCCCEEEEECCEEEE	25.59	20090780
372	Ubiquitination	RLAQHFPKTTEENPI HHHHHCCCCCCCCCE	68.11	29967540
394	Phosphorylation	LNTIGLIYEKISLPK CCHHHHEEEECCCCC	19.06	-
396	Ubiquitination	TIGLIYEKISLPKVH HHHHEEEECCCCCCC	22.18	21906983
398	Phosphorylation	GLIYEKISLPKVHPR HHEEEECCCCCCCCC	50.08	24719451
401	Ubiquitination	YEKISLPKVHPRYDL EEECCCCCCCCCCCC	59.47	27667366
416	Ubiquitination	DGDASMAKAITGVVC CCCHHHHHHHHHHHH	31.51	-
435	Phosphorylation	IASTLLLYQELMRKG HHHHHHHHHHHHHCC	10.42	-
484	Ubiquitination	KTVKVYEKLMKINLE HHHHHHHHHHCCCHH	35.87	29967540
503	Phosphorylation	GEISDIHTKLLRLSS CCCCHHHHHHHHHHC	24.58	-
504	Ubiquitination	EISDIHTKLLRLSSS CCCHHHHHHHHHHCC	31.21	21906983
509	Phosphorylation	HTKLLRLSSSQGTIE HHHHHHHHCCCCCEE	22.85	18691976
510	Phosphorylation	TKLLRLSSSQGTIET HHHHHHHCCCCCEEE	31.13	20873877
511	Phosphorylation	KLLRLSSSQGTIETS HHHHHHCCCCCEEEE	29.29	20873877
514	Phosphorylation	RLSSSQGTIETSLQD HHHCCCCCEEEEHHH	14.17	29083192
527	Phosphorylation	QDIDSRLSPGGSLAD HHHHHCCCCCCCHHH	22.01	20873877
531	Phosphorylation	SRLSPGGSLADAWAH HCCCCCCCHHHHHHH	26.71	28348404
545	Ubiquitination	HQEGTHPKDRNVEKL HCCCCCCCCCCHHHH	62.81	29967540
577	Phosphorylation	KAERRLAYNEEQIHK HHHHHHCCCHHHHHH	27.91	22817900
584	Acetylation	YNEEQIHKFDKQKLY CCHHHHHHHCHHHHH	57.81	19608861
584	Ubiquitination	YNEEQIHKFDKQKLY CCHHHHHHHCHHHHH	57.81	21906983
587	Ubiquitination	EQIHKFDKQKLYYHA HHHHHHCHHHHHHHH	53.09	22817900
589	Ubiquitination	IHKFDKQKLYYHATK HHHHCHHHHHHHHHH	44.17	22817900
591	Phosphorylation	KFDKQKLYYHATKAM HHCHHHHHHHHHHHH	10.55	-
592	Phosphorylation	FDKQKLYYHATKAMT HCHHHHHHHHHHHHH	8.73	-
596	Ubiquitination	KLYYHATKAMTHFTD HHHHHHHHHHHHCCH	36.62	29967540
608	Ubiquitination	FTDECVKKYEAFLNK CCHHHHHHHHHHHCC	28.11	29967540
615	Ubiquitination	KYEAFLNKSEEWIRK HHHHHHCCCHHHHHH	62.48	29967540
646	Ubiquitination	DIEEEVSKYQEYTNE CHHHHHHHHHHHHHH	57.01	29967540
647	Phosphorylation	IEEEVSKYQEYTNEL HHHHHHHHHHHHHHH	10.08	-
650	Phosphorylation	EVSKYQEYTNELQET HHHHHHHHHHHHHHH	10.19	-
661	Ubiquitination	LQETLPQKMFTASSG HHHHCCHHHEECCCC	33.76	21906983
664	Phosphorylation	TLPQKMFTASSGIKH HCCHHHEECCCCCCC	23.33	-
670	Ubiquitination	FTASSGIKHTMTPIY EECCCCCCCCCCCCC	36.23	2238803
672	Phosphorylation	ASSGIKHTMTPIYPS CCCCCCCCCCCCCCC	20.10	18691976
674	Phosphorylation	SGIKHTMTPIYPSSN CCCCCCCCCCCCCCC	14.00	28555341
677	Phosphorylation	KHTMTPIYPSSNTLV CCCCCCCCCCCCCHH	9.77	-
687	Phosphorylation	SNTLVEMTLGMKKLK CCCHHHHHHCCHHHH	13.47	29116813
692	Ubiquitination	EMTLGMKKLKEEMEG HHHHCCHHHHHHHHH	56.77	-
697	Sulfoxidation	MKKLKEEMEGVVKEL CHHHHHHHHHHHHHH	5.95	21406390
702	Ubiquitination	EEMEGVVKELAENNH HHHHHHHHHHHHCCC	44.60	29967540
716	Phosphorylation	HILERFGSLTMDGGL CHHHHHCCEECCCCC	20.25	22617229
718	Phosphorylation	LERFGSLTMDGGLRN HHHHCCEECCCCCCC	18.21	28450419

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
172	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
172	S	Phosphorylation	Kinase	TBK1	Q9UHD2	PSP
172	S	Phosphorylation	Kinase	MAP2K-FAMILY	-	GPS
179	Y	Phosphorylation	Kinase	SRC	P05480	PSP
354	Y	Phosphorylation	Kinase	FGR	P09769	PSP
354	Y	Phosphorylation	Kinase	HCK	P08631	PSP
354	Y	Phosphorylation	Kinase	LCK	P06239	PSP
394	Y	Phosphorylation	Kinase	FGR	P09769	PSP
394	Y	Phosphorylation	Kinase	HCK	P08631	PSP
394	Y	Phosphorylation	Kinase	LCK	P06239	PSP
527	S	Phosphorylation	Kinase	DYRK2	Q92630	PSP
716	S	Phosphorylation	Kinase	PKCT	Q04759	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	MIB1	Q86YT6	PMID:21903422
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:20804422
-	K	Ubiquitination	E3 ubiquitin ligase	RNF41	Q9H4P4	PMID:19483718
-	K	Ubiquitination	E3 ubiquitin ligase	DTX4	Q9Y2E6	PMID:22388039
-	K	Ubiquitination	E3 ubiquitin ligase	TRAF3	Q13114	PMID:23308279
-	K	Ubiquitination	E3 ubiquitin ligase	MIB2	Q96AX9	PMID:21903422

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
30	K	Phosphorylation	23453971
Phosphorylation requires homodimerization and ubiquitination at Lys-30 and Lys-401.
30	K	ubiquitylation	23453971
'Lys-63'-linked polyubiquitination by MIB1 after RNA virus infection, or by NRDP1 after LPS stimulation at Lys-30 and Lys-401, participates in kinase activation.
30	K	ubiquitylation	23453971
'Lys-63'-linked polyubiquitination by RNF128 at Lys-30 and Lys-401 leads to the activation of antiviral responses.
30	K	ubiquitylation	23453971
Phosphorylation requires homodimerization and ubiquitination at Lys-30 and Lys-401.
172	S	Phosphorylation	11839743
Autophosphorylation at Ser-172 activates the kinase, and is an essential step for virus-triggered signaling.
172	S	Phosphorylation	11839743
Dephosphorylated at Ser-172 by PPM1B and this negatively regulates its role in mediating antiviral response.
172	S	Phosphorylation	11839743
Phosphorylated by IKBKB/IKKB at Ser-172.
401	K	Phosphorylation	23453971
Phosphorylation requires homodimerization and ubiquitination at Lys-30 and Lys-401.
401	K	ubiquitylation	23453971
'Lys-63'-linked polyubiquitination by MIB1 after RNA virus infection, or by NRDP1 after LPS stimulation at Lys-30 and Lys-401, participates in kinase activation.
401	K	ubiquitylation	23453971
'Lys-63'-linked polyubiquitination by RNF128 at Lys-30 and Lys-401 leads to the activation of antiviral responses.
401	K	ubiquitylation	23453971
Phosphorylation requires homodimerization and ubiquitination at Lys-30 and Lys-401.
670	K	ubiquitylation	22388039
'Lys-48'-linked polyubiquitination at Lys-670 by DTX4 leads to proteasomal degradation.

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 TBK1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDC37_HUMAN	CDC37	physical	14743216
TANK_HUMAN	TANK	physical	14743216
TBKB1_HUMAN	TBKBP1	physical	14743216
TRAF2_HUMAN	TRAF2	physical	14743216
FBW1A_HUMAN	BTRC	physical	14743216
REL_HUMAN	REL	physical	14743216
CUL1_HUMAN	CUL1	physical	14743216
ANR28_HUMAN	ANKRD28	physical	14743216
PP6R2_HUMAN	PPP6R2	physical	14743216
PP6R1_HUMAN	PPP6R1	physical	14743216
NFKB2_HUMAN	NFKB2	physical	14743216
PPP6_HUMAN	PPP6C	physical	14743216
TF65_HUMAN	RELA	physical	14743216
SKP1_HUMAN	SKP1	physical	14743216
CYLD_HUMAN	CYLD	physical	18636086
IRF3_HUMAN	IRF3	physical	18636086
TF65_HUMAN	RELA	physical	15489227
STING_HUMAN	TMEM173	physical	21074459
CACO2_HUMAN	CALCOCO2	physical	19820708
NCOA2_HUMAN	NCOA2	physical	16051665
ATG9A_HUMAN	ATG9A	physical	21903422
MRCKG_HUMAN	CDC42BPG	physical	21903422
FMR1_HUMAN	FMR1	physical	21903422
FXR2_HUMAN	FXR2	physical	21903422
IRF3_HUMAN	IRF3	physical	21903422
MIB1_HUMAN	MIB1	physical	21903422
MAVS_HUMAN	MAVS	physical	21903422
TRAF2_HUMAN	TRAF2	physical	21903422
OPTN_HUMAN	OPTN	physical	21903422
AGO2_HUMAN	AGO2	physical	21903422
CACO2_HUMAN	CALCOCO2	physical	21903422
HMMR_HUMAN	HMMR	physical	21903422
IKKE_HUMAN	IKBKE	physical	21903422
LETM1_HUMAN	LETM1	physical	21903422
PAPD1_HUMAN	MTPAP	physical	21903422
AZI2_HUMAN	AZI2	physical	21903422
RBBP5_HUMAN	RBBP5	physical	21903422
TBKB1_HUMAN	TBKBP1	physical	21903422
TANK_HUMAN	TANK	physical	21903422
TXLNA_HUMAN	TXLNA	physical	21903422
TXLNG_HUMAN	TXLNG	physical	21903422
NALP4_HUMAN	NLRP4	physical	22388039
TNIP1_HUMAN	TNIP1	physical	21885437
IRF3_HUMAN	IRF3	physical	19656901
TBK1_HUMAN	TBK1	physical	19656901
TNAP3_HUMAN	TNFAIP3	physical	15661910
STING_HUMAN	TMEM173	physical	22745133
MBP_HUMAN	MBP	physical	17599067
XIAP_HUMAN	XIAP	physical	22072751
IRF3_HUMAN	IRF3	physical	22072751
OPTN_HUMAN	OPTN	physical	20174559
TRAF3_HUMAN	TRAF3	physical	20174559
PELI1_HUMAN	PELI1	physical	21204785
TBK1_HUMAN	TBK1	physical	17599067
IKKE_HUMAN	IKBKE	physical	17599067
IRF3_HUMAN	IRF3	physical	17599067
IRF7_HUMAN	IRF7	physical	17599067
TRI27_HUMAN	TRIM27	physical	16393995
AZI2_HUMAN	AZI2	physical	14560022
TF65_HUMAN	RELA	physical	14560022
TCAM1_HUMAN	TICAM1	physical	14530355
TRAF3_HUMAN	TRAF3	physical	22079989
IRF3_HUMAN	IRF3	physical	22079989
SRC_HUMAN	SRC	physical	19419966
MAVS_HUMAN	MAVS	physical	16153868
IRF3_HUMAN	IRF3	physical	23028469
NEMO_HUMAN	IKBKG	physical	23028469
IKBA_HUMAN	NFKBIA	physical	20449947
IRF3_HUMAN	IRF3	physical	16394098
A4_HUMAN	APP	physical	21832049
RNF11_HUMAN	RNF11	physical	23308279
TRAF3_HUMAN	TRAF3	physical	23308279
XIAP_HUMAN	XIAP	physical	16887178
IRF3_HUMAN	IRF3	physical	20628368
HS90A_HUMAN	HSP90AA1	physical	20628368
CIKS_HUMAN	TRAF3IP2	physical	22851696
TRAF3_HUMAN	TRAF3	physical	23717208
TBK1_HUMAN	TBK1	physical	23453972
TANK_HUMAN	TANK	physical	23286385
AZI2_HUMAN	AZI2	physical	23286385
TBKB1_HUMAN	TBKBP1	physical	23286385
TBK1_HUMAN	TBK1	physical	23286385
TRI11_MOUSE	Trim11	physical	23675467
AKT1_HUMAN	AKT1	physical	21106850
TRAF3_HUMAN	TRAF3	physical	24763515
TBK1_HUMAN	TBK1	physical	25939384
SOCS3_HUMAN	SOCS3	physical	25939384
IKKE_HUMAN	IKBKE	physical	25939384
SQSTM_HUMAN	SQSTM1	physical	25972374
IFIT3_HUMAN	IFIT3	physical	21813773
MAVS_HUMAN	MAVS	physical	25636800
OPTN_HUMAN	OPTN	physical	25803835
TRI26_HUMAN	TRIM26	physical	26611359
OPTN_HUMAN	OPTN	physical	26365381
DYRK2_HUMAN	DYRK2	physical	26407194
NALP4_HUMAN	NLRP4	physical	26407194
OPTN_HUMAN	OPTN	physical	25923723
CYLD_HUMAN	CYLD	physical	25923723
TRI14_HUMAN	TRIM14	physical	24379373
OPTN_HUMAN	OPTN	physical	27035970
SQSTM_HUMAN	SQSTM1	physical	27035970
TANK_HUMAN	TANK	physical	27035970
TBKB1_HUMAN	TBKBP1	physical	27035970
CTBL1_HUMAN	CTNNBL1	physical	27035970
TANK_HUMAN	TANK	physical	24488098
PBIP1_HUMAN	PBXIP1	physical	24488098
TRIM9_HUMAN	TRIM9	physical	26915459
GSK3B_HUMAN	GSK3B	physical	26915459
TBK1_HUMAN	TBK1	physical	26915459
RN128_HUMAN	RNF128	physical	27776110
TRI23_HUMAN	TRIM23	physical	28871090
TBK1_HUMAN	TBK1	physical	28871090
YAP1_HUMAN	YAP1	physical	28346439
IRF3_HUMAN	IRF3	physical	28346439

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
177700	Glaucoma 1, open angle, P (GLC1P)
616439	Frontotemporal dementia and/or amyotrophic lateral sclerosis 4 (FTDALS4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TBK1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-172; SER-509; SER-510AND SER-716, AND MASS SPECTROMETRY.	19369195 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716, AND MASSSPECTROMETRY.	18691976 [Abstract]
"IKK-i and TBK-1 are enzymatically distinct from the homologous enzymeIKK-2: comparative analysis of recombinant human IKK-i, TBK-1, andIKK-2."; Kishore N., Huynh Q.K., Mathialagan S., Hall T., Rouw S., Creely D.,Lange G., Caroll J., Reitz B., Donnelly A., Boddupalli H., Combs R.G.,Kretzmer K., Tripp C.S.; J. Biol. Chem. 277:13840-13847(2002). Cited for: FUNCTION, MUTAGENESIS OF SER-172, AND PHOSPHORYLATION AT SER-172.	11839743 [Abstract]
Ubiquitylation
Reference	PubMed
"NLRP4 negatively regulates type I interferon signaling by targetingthe kinase TBK1 for degradation via the ubiquitin ligase DTX4."; Cui J., Li Y., Zhu L., Liu D., Songyang Z., Wang H.Y., Wang R.F.; Nat. Immunol. 13:387-395(2012). Cited for: UBIQUITINATION AT LYS-670 BY DTX4.	22388039 [Abstract]

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