TANK_HUMAN - dbPTM
TANK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TANK_HUMAN
UniProt AC Q92844
Protein Name TRAF family member-associated NF-kappa-B activator
Gene Name TANK
Organism Homo sapiens (Human).
Sequence Length 425
Subcellular Localization Cytoplasm.
Protein Description Adapter protein involved in I-kappa-B-kinase (IKK) regulation which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity. Acts as a regulator of TRAF function by maintaining them in a latent state. Blocks TRAF2 binding to LMP1 and inhibits LMP1-mediated NF-kappa-B activation. Negatively regulates NF-kappaB signaling and cell survival upon DNA damage. [PubMed: 25861989 Plays a role as an adapter to assemble ZC3H12A, USP10 in a deubiquitination complex which plays a negative feedback response to attenuate NF-kappaB activation through the deubiquitination of IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage]
Protein Sequence MDKNIGEQLNKAYEAFRQACMDRDSAVKELQQKTENYEQRIREQQEQLSLQQTIIDKLKSQLLLVNSTQDNNYGCVPLLEDSETRKNNLTLDQPQDKVISGIAREKLPKVRRQEVSSPRKETSARSLGSPLLHERGNIEKTFWDLKEEFHKICMLAKAQKDHLSKLNIPDTATETQCSVPIQCTDKTDKQEALFKPQAKDDINRGAPSITSVTPRGLCRDEEDTSFESLSKFNVKFPPMDNDSTFLHSTPERPGILSPATSEAVCQEKFNMEFRDNPGNFVKTEETLFEIQGIDPIASAIQNLKTTDKTKPSNLVNTCIRTTLDRAACLPPGDHNALYVNSFPLLDPSDAPFPSLDSPGKAIRGPQQPIWKPFPNQDSDSVVLSGTDSELHIPRVCEFCQAVFPPSITSRGDFLRHLNSHFNGET
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
1Acetylation-------MDKNIGEQ
-------CCCHHHHH		17.4522814378
49PhosphorylationREQQEQLSLQQTIID
HHHHHHHHHHHHHHH		24.6730108239
53PhosphorylationEQLSLQQTIIDKLKS
HHHHHHHHHHHHHHH		13.6230108239
57UbiquitinationLQQTIIDKLKSQLLL
HHHHHHHHHHHCEEE		47.62-
60PhosphorylationTIIDKLKSQLLLVNS
HHHHHHHHCEEEEEC		36.1826552605
67PhosphorylationSQLLLVNSTQDNNYG
HCEEEEECCCCCCCC		21.7029978859
68PhosphorylationQLLLVNSTQDNNYGC
CEEEEECCCCCCCCE		34.4425159151
73PhosphorylationNSTQDNNYGCVPLLE
ECCCCCCCCEEEECC		20.3920090780
82PhosphorylationCVPLLEDSETRKNNL
EEEECCCCCHHHCCC		31.3428348404
84PhosphorylationPLLEDSETRKNNLTL
EECCCCCHHHCCCCC		51.3928348404
86 (in isoform 2)Ubiquitination-58.5721906983
86 (in isoform 1)Ubiquitination-58.5721890473
86UbiquitinationLEDSETRKNNLTLDQ
CCCCCHHHCCCCCCC		58.5720972266
90PhosphorylationETRKNNLTLDQPQDK
CHHHCCCCCCCCHHH		30.34-
97UbiquitinationTLDQPQDKVISGIAR
CCCCCHHHHHHHHHH		35.90-
100PhosphorylationQPQDKVISGIAREKL
CCHHHHHHHHHHHHC		27.4328857561
116PhosphorylationKVRRQEVSSPRKETS
HHHHHHCCCCCHHHH		33.5918691976
117PhosphorylationVRRQEVSSPRKETSA
HHHHHCCCCCHHHHH		33.6227794612
122PhosphorylationVSSPRKETSARSLGS
CCCCCHHHHHHHHCC		30.6229514088
123PhosphorylationSSPRKETSARSLGSP
CCCCHHHHHHHHCCH		23.8329514088
126PhosphorylationRKETSARSLGSPLLH
CHHHHHHHHCCHHHH		36.4823401153
129PhosphorylationTSARSLGSPLLHERG
HHHHHHCCHHHHCCC		20.0529255136
157AcetylationHKICMLAKAQKDHLS
HHHHHHHHHHHHHHH		47.6025953088
165UbiquitinationAQKDHLSKLNIPDTA
HHHHHHHHCCCCCCC		52.49-
171PhosphorylationSKLNIPDTATETQCS
HHCCCCCCCCCCCCC		30.08-
175PhosphorylationIPDTATETQCSVPIQ
CCCCCCCCCCCCCEE		30.4419060867
178PhosphorylationTATETQCSVPIQCTD
CCCCCCCCCCEEECC		22.5527251275
186UbiquitinationVPIQCTDKTDKQEAL
CCEEECCCCCHHHHH		40.23-
189UbiquitinationQCTDKTDKQEALFKP
EECCCCCHHHHHHCC		56.1021906983
189 (in isoform 1)Ubiquitination-56.1021890473
195UbiquitinationDKQEALFKPQAKDDI
CHHHHHHCCCCCCCC		36.7521890473
195 (in isoform 1)Ubiquitination-36.7521890473
199UbiquitinationALFKPQAKDDINRGA
HHHCCCCCCCCCCCC		51.1621890473
199 (in isoform 1)Ubiquitination-51.1621890473
208PhosphorylationDINRGAPSITSVTPR
CCCCCCCCCCEECCC		37.6525159151
210PhosphorylationNRGAPSITSVTPRGL
CCCCCCCCEECCCCC		22.8323663014
211PhosphorylationRGAPSITSVTPRGLC
CCCCCCCEECCCCCC		23.4823663014
213PhosphorylationAPSITSVTPRGLCRD
CCCCCEECCCCCCCC		13.6729255136
224PhosphorylationLCRDEEDTSFESLSK
CCCCCCCCCCCHHHH		38.3023401153
225PhosphorylationCRDEEDTSFESLSKF
CCCCCCCCCCHHHHC		39.0623401153
228PhosphorylationEEDTSFESLSKFNVK
CCCCCCCHHHHCCCC		35.6129255136
230PhosphorylationDTSFESLSKFNVKFP
CCCCCHHHHCCCCCC		44.4723401153
231UbiquitinationTSFESLSKFNVKFPP
CCCCHHHHCCCCCCC		46.3721890473
231 (in isoform 1)Ubiquitination-46.3721890473
235UbiquitinationSLSKFNVKFPPMDND
HHHHCCCCCCCCCCC		53.94-
243PhosphorylationFPPMDNDSTFLHSTP
CCCCCCCCCCCCCCC		27.5818691976
244PhosphorylationPPMDNDSTFLHSTPE
CCCCCCCCCCCCCCC		32.8319369195
248PhosphorylationNDSTFLHSTPERPGI
CCCCCCCCCCCCCCC		48.0529978859
249PhosphorylationDSTFLHSTPERPGIL
CCCCCCCCCCCCCCC		20.5817192257
257PhosphorylationPERPGILSPATSEAV
CCCCCCCCCCCCHHH		15.5718691976
260PhosphorylationPGILSPATSEAVCQE
CCCCCCCCCHHHHHH		30.4029978859
261PhosphorylationGILSPATSEAVCQEK
CCCCCCCCHHHHHHH		26.1829978859
282SumoylationDNPGNFVKTEETLFE
CCCCCCEECHHHHEE		46.19-
282UbiquitinationDNPGNFVKTEETLFE
CCCCCCEECHHHHEE		46.19-
283O-linked_GlycosylationNPGNFVKTEETLFEI
CCCCCEECHHHHEEE		33.4823301498
286O-linked_GlycosylationNFVKTEETLFEIQGI
CCEECHHHHEEECCC		30.4323301498
304UbiquitinationASAIQNLKTTDKTKP
HHHHHHHCCCCCCCC		57.86-
308UbiquitinationQNLKTTDKTKPSNLV
HHHCCCCCCCCCHHH		57.25-
310UbiquitinationLKTTDKTKPSNLVNT
HCCCCCCCCCHHHHH		52.79-
312PhosphorylationTTDKTKPSNLVNTCI
CCCCCCCCHHHHHHH		44.3328555341
317PhosphorylationKPSNLVNTCIRTTLD
CCCHHHHHHHHHHHH		11.2228555341
338PhosphorylationPGDHNALYVNSFPLL
CCCCCCEEEECCCCC		8.6520090780
341PhosphorylationHNALYVNSFPLLDPS
CCCEEEECCCCCCCC		20.4226552605
348PhosphorylationSFPLLDPSDAPFPSL
CCCCCCCCCCCCCCC		46.1827080861
354PhosphorylationPSDAPFPSLDSPGKA
CCCCCCCCCCCCCCC		45.2318691976
357PhosphorylationAPFPSLDSPGKAIRG
CCCCCCCCCCCCCCC		40.6221712546
360UbiquitinationPSLDSPGKAIRGPQQ
CCCCCCCCCCCCCCC		43.98-
371UbiquitinationGPQQPIWKPFPNQDS
CCCCCCCCCCCCCCC		37.1821890473
371 (in isoform 1)Ubiquitination-37.1821890473
378PhosphorylationKPFPNQDSDSVVLSG
CCCCCCCCCCEEEEC		23.2528122231
380PhosphorylationFPNQDSDSVVLSGTD
CCCCCCCCEEEECCC		20.3429978859
384PhosphorylationDSDSVVLSGTDSELH
CCCCEEEECCCCCCC		28.2125849741
386PhosphorylationDSVVLSGTDSELHIP
CCEEEECCCCCCCHH		32.7329978859
388PhosphorylationVVLSGTDSELHIPRV
EEEECCCCCCCHHHH		41.7329978859
406PhosphorylationCQAVFPPSITSRGDF
HHHHCCCCCCCHHHH		38.4427251275
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
-KUbiquitinationE3 ubiquitin ligaseMARCHF5Q9NX47
PMID:32296023
-KUbiquitinationE3 ubiquitin ligaseBIRC3Q13489
PMID:23007157
-KUbiquitinationE3 ubiquitin ligaseBIRC2Q13490
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseSIAH2O43255
PMID:22199232
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:31558697
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TANK_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 TANK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZC12A_HUMANZC3H12Aphysical
16189514
TRAF3_HUMANTRAF3physical
14743216
TRAF2_HUMANTRAF2physical
14743216
NEMO_HUMANIKBKGphysical
12133833
IKKA_HUMANCHUKphysical
12133833
IKKE_HUMANIKBKEphysical
10759890
TRAF2_HUMANTRAF2physical
10759890
TBK1_HUMANTBK1physical
10581243
TRAF2_HUMANTRAF2physical
10581243
IRF7_HUMANIRF7physical
17823124
IRF3_HUMANIRF3physical
17823124
IKKE_HUMANIKBKEphysical
17823124
TBK1_HUMANTBK1physical
17823124
TRAF3_HUMANTRAF3physical
17823124
PLK1_HUMANPLK1physical
20484576
NEMO_HUMANIKBKGphysical
20484576
MARH5_HUMANMARCH5physical
21625535
APBA3_HUMANAPBA3physical
21903422
BIRC2_HUMANBIRC2physical
21903422
TBK1_HUMANTBK1physical
21903422
TRAF2_HUMANTRAF2physical
21903422
TRAF3_HUMANTRAF3physical
21903422
IKKE_HUMANIKBKEphysical
21212807
CBLB_HUMANCBLBphysical
17878343
TNR5_HUMANCD40physical
17878343
TRAF3_HUMANTRAF3physical
14517219
TRAF2_HUMANTRAF2physical
12005438
TRAF3_HUMANTRAF3physical
12005438
TRAF3_HUMANTRAF3physical
22079989
IKKE_HUMANIKBKEphysical
23007157
TRAF2_HUMANTRAF2physical
23007157
TBK1_HUMANTBK1physical
23007157
TANK_HUMANTANKphysical
10490605
A4_HUMANAPPphysical
21832049
IKKE_HUMANIKBKEphysical
17568778
TBK1_HUMANTBK1physical
17568778
TANK_HUMANTANKphysical
17568778
TRAF1_HUMANTRAF1physical
21988832
TRAF2_HUMANTRAF2physical
21988832
TBK1_HUMANTBK1physical
21988832
CEP63_HUMANCEP63physical
25416956
TBK1_HUMANTBK1physical
25409927
NEMO_HUMANIKBKGphysical
25861989
ZC12A_HUMANZC3H12Aphysical
25861989
UBP10_HUMANUSP10physical
25861989
TRAF6_HUMANTRAF6physical
25861989
PBIP1_HUMANPBXIP1physical
24488098
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 TANK_HUMAN

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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-116; SER-117; SER-126;SER-129; THR-175; THR-213; THR-224; SER-225; SER-228; SER-230;THR-244; SER-341; SER-354; SER-357 AND SER-380, AND MASS SPECTROMETRY.
"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-129, AND MASSSPECTROMETRY.
"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-117; SER-129; SER-208;THR-213; SER-225 AND SER-228, 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-225 AND SER-228, ANDMASS SPECTROMETRY.

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