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Protein Page:
TANK (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
TANK Acts as a regulator of TRAF function by maintaining them in a latent state. Overexpression inhibits TRAF2-mediated NF- kappa-B activation signaled by CD40, TNFR1 and TNFR2. Blocks TRAF2 binding to LMP1 and inhibits LMP1-mediated NF-kappa-B activation. May be involved in I-kappa-B-kinase (IKK) regulation; may function as an adapter for kinases such as TBK1 or IKBKE that can modulate IKK activity. Interacts with TBK1 (via TRAF-C domain). Interacts with TRAF1 (via TRAF-C domain). Interacts with TRAF2 (via TRAF-C domain); the interaction is disrupted by the phosphorylation of TANK by IKBKE. Interacts with TRAF3 (via TRAF-C domain); the interaction with TRAF3 is weaker than the interactions with TRAF1 and TRAF3. Interacts with IKBKG; the interaction is enhanced by IKBKE and TBK1. Part of a ternary complex consisting of TANK, IKBKB and IKBKG. Ubiquitous. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: C2H2-type zinc finger protein; Adaptor/scaffold
Cellular Component: cytosol
Molecular Function: protein binding; ubiquitin protein ligase binding; metal ion binding
Biological Process: I-kappaB kinase/NF-kappaB cascade; innate immune response; signal transduction
Reference #:  Q92844 (UniProtKB)
Alt. Names/Synonyms: I-TRAF; ITRAF; TANK; TRAF family member-associated NF-kappa-B activator; TRAF family member-associated NFKB activator; TRAF-interacting protein; TRAF2
Gene Symbols: TANK
Molecular weight: 47,816 Da
Basal Isoelectric point: 5.46  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

TANK
Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

► Hide Isoforms 		 
0 1 N72 VNSTQDNNyGCVPLL
0 8 Y73-p NSTQDNNyGCVPLLE
0 2 K86-u LEDSETRkNNLtLDQ
0 1 T90-p ETRkNNLtLDQPQDK
0 2 S117-p VRRQEVSsPRKETSA
0 1 S126-p RKETSARsLGsPLLH
0 4 S129-p TSARsLGsPLLHERG
0 1 T171-p SKLNIPDtATEtQCS
0 1 T175-p IPDtATEtQCSVPIQ
0 1 K186-u VPIQCTDkTDkQEAL
0 4 K189-u QCTDkTDkQEALFkP
0 14 K195-u DkQEALFkPQAkDDI
0 8 K199-u ALFkPQAkDDINRGA
0 1 S208-p DINRGAPsITSVtPR
0 16 T213-p APsITSVtPRGLCRD
0 7 S225-p CRDEEDTsFEsLskF
0 4 S228-p EEDTsFEsLskFNVk
0 1 S230-p DTsFEsLskFNVkFP
0 7 K231-u TsFEsLskFNVkFPP
0 1 K235-u sLskFNVkFPPMDND
0 2 S243-p FPPMDNDstFLHstP
0 1 T244-p PPMDNDstFLHstPE
0 1 S248-p NDstFLHstPERPGI
0 4 T249-p DstFLHstPERPGIL
0 4 S257-p PERPGILsPATsEAV
0 3 S261-p GILsPATsEAVCQEK
0 4 K282-u DNPGNFVkTEETLFE
0 11 K304-u ASAIQNLkTTDkTKP
0 1 K308-u QNLkTTDkTKPSNLV
0 3 Y338-p PGDHNALyVNsFPLL
0 1 S341-p HNALyVNsFPLLDPS
0 4 S354-p PSDAPFPsLDsPGKA
0 3 S357-p APFPsLDsPGKAIRG
0 2 K371-u GPQQPIWkPFPNQDS
0 1 S380-p FPNQDSDsVVLSGTD
  TANK iso3  
N72 VNSTQDNNYGCVPLL
Y73 NSTQDNNYGCVPLLE
K86 LEDSDTRKNTLTLAQ
T90 DTRKNTLTLAQPQDK
S117 VRRQEVSSPRKETSA
S126 RKETSARSLGSPLLH
S129 TSARSLGSPLLHERG
T171 SKLNIPDTATETQCS
T175 IPDTATETQCSVPIQ
K186 VPIQCTDKTDKQEAL
K189 QCTDKTDKQEALFTP
T195 DKQEALFTPQAKDDI
K199 ALFTPQAKDDINRGA
S208 DINRGAPSITSVTPR
T213 APSITSVTPRGLCRD
S225 CRDEEDTSLESLSKF
S228 EEDTSLESLSKFNVK
S230 DTSLESLSKFNVKFP
K231 TSLESLSKFNVKFPP
K235 SLSKFNVKFPPMDND
S243 FPPMDNDSTFLHSTP
T244 PPMDNDSTFLHSTPE
S248 NDSTFLHSTPERPGI
T249 DSTFLHSTPERPGIL
S257 PERPGILSPATSEAV
S261 GILSPATSEAVCQEK
K282 DNPGNFVKTEETLFE
K304 ASAIQNLKTTDKTKP
K308 QNLKTTDKTKPSNLV
Y338 PGDHNALYVNSFPLL
S341 HNALYVNSFPLLDPS
S354 PSDAPFPSLDSPGKA
S357 APFPSLDSPGKAIRG
K371 GPQQPIWKPFPNQDS
S380 FPNQDSDSVVLSGTD
  mouse

 
S107-p VDSSRDNsYGYVPLL
Y108 DSSRDNsYGYVPLLE
K121 LEDSDRRKNNLTLDE
T125 DRRKNNLTLDEPHDK
S152 VRRQEVSSGKESAKG
G159 SGKESAKGLNIPLHH
I162 ESAKGLNIPLHHERD
I204 SKLNIPDIATDTQCS
T208 IPDIATDTQCSVPIQ
K219 VPIQCTDKTEKQEAL
K222 QCTDKTEKQEALFKP
K228 EKQEALFKPQAkDDI
K232-u ALFKPQAkDDINRGM
C241 DINRGMSCVTAVTPR
T246 MSCVTAVTPRGLGRD
S258-p GRDEEDTsFEsLSKF
S261-p EEDTsFEsLSKFNVK
S263 DTsFEsLSKFNVKFP
K264 TsFEsLSKFNVKFPP
K268 sLSKFNVKFPPMDND
S276 FPPMDNDSIFLHSTP
I277 PPMDNDSIFLHSTPE
S281 NDSIFLHSTPEAPSI
T282 DSIFLHSTPEAPSIL
A290 PEAPSILAPATPETV
P294 SILAPATPETVCQDR
K315 DNPGNFVKTEETLFE
K337 TSAIQNLKTTDKTNP
K341 QNLKTTDKTNPSNLR
Y361 AGDHNVFYVNTFPLQ
T364 HNVFYVNTFPLQDPP
S377 PPDAPFPSLDsPGKA
S380-p APFPSLDsPGKAVRG
K394 GPQQPFWKPFLNQDT
L403 FLNQDTDLVVPSDSD
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