SIKE1_HUMAN - dbPTM
SIKE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIKE1_HUMAN
UniProt AC Q9BRV8
Protein Name Suppressor of IKBKE 1
Gene Name SIKE1
Organism Homo sapiens (Human).
Sequence Length 207
Subcellular Localization Cytoplasm .
Protein Description Physiological suppressor of IKK-epsilon and TBK1 that plays an inhibitory role in virus- and TLR3-triggered IRF3. Inhibits TLR3-mediated activation of interferon-stimulated response elements (ISRE) and the IFN-beta promoter. May act by disrupting the interactions of IKBKE or TBK1 with TICAM1/TRIF, IRF3 and DDX58/RIG-I. Does not inhibit NF-kappa-B activation pathways..
Protein Sequence MSCTIEKILTDAKTLLERLREHDAAAESLVDQSAALHRRVAAMREAGTALPDQYQEDASDMKDMSKYKPHILLSQENTQIRDLQQENRELWISLEEHQDALELIMSKYRKQMLQLMVAKKAVDAEPVLKAHQSHSAEIESQIDRICEMGEVMRKAVQVDDDQFCKIQEKLAQLELENKELRELLSISSESLQARKENSMDTASQAIK
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
7Acetylation-MSCTIEKILTDAKT
-CCCHHHHHHHHHHH		38.8825953088
13UbiquitinationEKILTDAKTLLERLR
HHHHHHHHHHHHHHH		42.3829967540
59PhosphorylationDQYQEDASDMKDMSK
HHHHHCCCCCHHHHH		51.0329038488
62UbiquitinationQEDASDMKDMSKYKP
HHCCCCCHHHHHHCC		56.1029967540
65PhosphorylationASDMKDMSKYKPHIL
CCCCHHHHHHCCEEE		42.8629038488
67PhosphorylationDMKDMSKYKPHILLS
CCHHHHHHCCEEEEC		23.5729214152
68UbiquitinationMKDMSKYKPHILLSQ
CHHHHHHCCEEEECC		33.5829967540
74PhosphorylationYKPHILLSQENTQIR
HCCEEEECCCCHHHH		31.8117525332
78PhosphorylationILLSQENTQIRDLQQ
EEECCCCHHHHHHHH		25.3127251275
120UbiquitinationLQLMVAKKAVDAEPV
HHHHHHHHCCCCHHH		43.8629967540
124UbiquitinationVAKKAVDAEPVLKAH
HHHHCCCCHHHHHHH		19.1829967540
129UbiquitinationVDAEPVLKAHQSHSA
CCCHHHHHHHHHCHH		44.0229967540
133PhosphorylationPVLKAHQSHSAEIES
HHHHHHHHCHHHHHH		15.00-
133UbiquitinationPVLKAHQSHSAEIES
HHHHHHHHCHHHHHH		15.0029967540
154UbiquitinationEMGEVMRKAVQVDDD
HHHHHHHHHHCCCHH		34.5129967540
158UbiquitinationVMRKAVQVDDDQFCK
HHHHHHCCCHHHHHH		7.5729967540
165UbiquitinationVDDDQFCKIQEKLAQ
CCHHHHHHHHHHHHH		49.0322817900
169UbiquitinationQFCKIQEKLAQLELE
HHHHHHHHHHHHHHC		32.5222817900
169 (in isoform 1)Ubiquitination-32.5221906983
173 (in isoform 2)Ubiquitination-7.2521906983
173UbiquitinationIQEKLAQLELENKEL
HHHHHHHHHHCCHHH		7.2522817900
178UbiquitinationAQLELENKELRELLS
HHHHHCCHHHHHHHC		49.0729967540
182UbiquitinationLENKELRELLSISSE
HCCHHHHHHHCCCHH		67.6929967540
185PhosphorylationKELRELLSISSESLQ
HHHHHHHCCCHHHHH		32.8026471730
187PhosphorylationLRELLSISSESLQAR
HHHHHCCCHHHHHHH		25.3626471730
188PhosphorylationRELLSISSESLQARK
HHHHCCCHHHHHHHH		29.5426471730
190PhosphorylationLLSISSESLQARKEN
HHCCCHHHHHHHHHC		27.9426471730
191PhosphorylationLSISSESLQARKENS
HCCCHHHHHHHHHCC		3.9724719451
195UbiquitinationSESLQARKENSMDTA
HHHHHHHHHCCHHHH		65.3529967540
198PhosphorylationLQARKENSMDTASQA
HHHHHHCCHHHHHHH		21.0823403867
199UbiquitinationQARKENSMDTASQAI
HHHHHCCHHHHHHHH		8.8329967540
201PhosphorylationRKENSMDTASQAIK-
HHHCCHHHHHHHHC-		21.4023403867
202PhosphorylationKENSMDTASQAIK--
HHCCHHHHHHHHC--		8.7227251275
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
133SPhosphorylationKinaseTBK1Q9UHD2
PSP
185SPhosphorylationKinaseTBK1Q9UHD2
PSP
187SPhosphorylationKinaseTBK1Q9UHD2
PSP
188SPhosphorylationKinaseTBK1Q9UHD2
PSP
190SPhosphorylationKinaseTBK1Q9UHD2
PSP
198SPhosphorylationKinaseTBK1Q9UHD2
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SIKE1_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 SIKE1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
2AAA_HUMANPPP2R1Aphysical
18782753
PP2AA_HUMANPPP2CAphysical
18782753
STRN_HUMANSTRNphysical
18782753
STRP1_HUMANSTRIP1physical
18782753
STRN3_HUMANSTRN3physical
18782753
STRN4_HUMANSTRN4physical
18782753
STK24_HUMANSTK24physical
18782753
PHOCN_HUMANMOB4physical
18782753
PDC10_HUMANPDCD10physical
18782753
STRP2_HUMANSTRIP2physical
18782753
SLMAP_HUMANSLMAPphysical
18782753
FGOP2_HUMANFGFR1OP2physical
18782753
BTD_HUMANBTDphysical
26496610
ICT1_HUMANICT1physical
26496610
PP2AA_HUMANPPP2CAphysical
26496610
2AAA_HUMANPPP2R1Aphysical
26496610
2AAB_HUMANPPP2R1Bphysical
26496610
STRN_HUMANSTRNphysical
26496610
TTC1_HUMANTTC1physical
26496610
SLMAP_HUMANSLMAPphysical
26496610
ELL_HUMANELLphysical
26496610
STK24_HUMANSTK24physical
26496610
PHOCN_HUMANMOB4physical
26496610
FGOP2_HUMANFGFR1OP2physical
26496610
STRN4_HUMANSTRN4physical
26496610
STRN3_HUMANSTRN3physical
26496610
RAIN_HUMANRASIP1physical
26496610
AGGF1_HUMANAGGF1physical
26496610
ASH1L_HUMANASH1Lphysical
26496610
STRP2_HUMANSTRIP2physical
26496610
ICE2_HUMANICE2physical
26496610
STRP1_HUMANSTRIP1physical
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 SIKE1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASSSPECTROMETRY.

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