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Protein

Suppressor of IKBKE 1

Gene

Sike1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Names & Taxonomyi

Protein namesi
Recommended name:
Suppressor of IKBKE 1
Alternative name(s):
Suppressor of IKK-epsilon
Gene namesi
Name:Sike1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1913891. Sike1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 207207Suppressor of IKBKE 1PRO_0000299051Add
BLAST

Proteomic databases

EPDiQ9CPR7.
MaxQBiQ9CPR7.
PaxDbiQ9CPR7.
PRIDEiQ9CPR7.

PTM databases

iPTMnetiQ9CPR7.
PhosphoSiteiQ9CPR7.

Expressioni

Gene expression databases

BgeeiQ9CPR7.
CleanExiMM_5730470L24RIK.
ExpressionAtlasiQ9CPR7. baseline and differential.
GenevisibleiQ9CPR7. MM.

Interactioni

Subunit structurei

Interacts with IKBKE and TBK1 via its coiled coil region. Interaction with TBK1 is disrupted upon viral infection or TLR3 stimulation. Interacts with CDC42BPB.By similarity

Protein-protein interaction databases

IntActiQ9CPR7. 2 interactions.
MINTiMINT-4114952.
STRINGi10090.ENSMUSP00000029447.

Structurei

3D structure databases

ProteinModelPortaliQ9CPR7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili70 – 10233Sequence analysisAdd
BLAST
Coiled coili164 – 19229Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the SIKE family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410II2X. Eukaryota.
ENOG4111HSR. LUCA.
GeneTreeiENSGT00390000018003.
HOGENOMiHOG000294110.
HOVERGENiHBG055808.
InParanoidiQ9CPR7.
KOiK12656.
OMAiICEMGQV.
OrthoDBiEOG7BGHMV.
PhylomeDBiQ9CPR7.
TreeFamiTF324337.

Family and domain databases

InterProiIPR008555. SIKE.
[Graphical view]
PANTHERiPTHR12186. PTHR12186. 1 hit.
PfamiPF05769. DUF837. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CPR7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSCTIEKILT DAKTLLERLR EHDAAAESLV DQSAALHRRV AAMREAGAVL
60 70 80 90 100
PEQYQEDASD VKDMSKYKPH ILLSQENTQI RDLQQENREL WVSLEEHQDA
110 120 130 140 150
LELIMSKYRK QMLQLMVAKK AVDAEPVLKA HQSHSAEIES QIDRICEMGA
160 170 180 190 200
VMRRAVQVDD NQFCKVQERL AQLELENKEL RELLSISSES LQVGKESSVA

PASQTIK
Length:207
Mass (Da):23,522
Last modified:June 1, 2001 - v1
Checksum:iFF12E0F36B948437
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641M → V in BAC29116 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014113 mRNA. Translation: BAB29165.1.
AK014247 mRNA. Translation: BAB29223.1.
AK017694 mRNA. Translation: BAB30879.1.
AK019264 mRNA. Translation: BAB31636.1.
AK033553 mRNA. Translation: BAC28353.1.
AK035590 mRNA. Translation: BAC29116.1.
BC004090 mRNA. Translation: AAH04090.1.
CCDSiCCDS17690.1.
RefSeqiNP_079955.1. NM_025679.3.
UniGeneiMm.208619.
Mm.33937.

Genome annotation databases

EnsembliENSMUST00000029447; ENSMUSP00000029447; ENSMUSG00000027854.
GeneIDi66641.
KEGGimmu:66641.
UCSCiuc008qsf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014113 mRNA. Translation: BAB29165.1.
AK014247 mRNA. Translation: BAB29223.1.
AK017694 mRNA. Translation: BAB30879.1.
AK019264 mRNA. Translation: BAB31636.1.
AK033553 mRNA. Translation: BAC28353.1.
AK035590 mRNA. Translation: BAC29116.1.
BC004090 mRNA. Translation: AAH04090.1.
CCDSiCCDS17690.1.
RefSeqiNP_079955.1. NM_025679.3.
UniGeneiMm.208619.
Mm.33937.

3D structure databases

ProteinModelPortaliQ9CPR7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CPR7. 2 interactions.
MINTiMINT-4114952.
STRINGi10090.ENSMUSP00000029447.

PTM databases

iPTMnetiQ9CPR7.
PhosphoSiteiQ9CPR7.

Proteomic databases

EPDiQ9CPR7.
MaxQBiQ9CPR7.
PaxDbiQ9CPR7.
PRIDEiQ9CPR7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029447; ENSMUSP00000029447; ENSMUSG00000027854.
GeneIDi66641.
KEGGimmu:66641.
UCSCiuc008qsf.1. mouse.

Organism-specific databases

CTDi80143.
MGIiMGI:1913891. Sike1.

Phylogenomic databases

eggNOGiENOG410II2X. Eukaryota.
ENOG4111HSR. LUCA.
GeneTreeiENSGT00390000018003.
HOGENOMiHOG000294110.
HOVERGENiHBG055808.
InParanoidiQ9CPR7.
KOiK12656.
OMAiICEMGQV.
OrthoDBiEOG7BGHMV.
PhylomeDBiQ9CPR7.
TreeFamiTF324337.

Miscellaneous databases

PROiQ9CPR7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CPR7.
CleanExiMM_5730470L24RIK.
ExpressionAtlasiQ9CPR7. baseline and differential.
GenevisibleiQ9CPR7. MM.

Family and domain databases

InterProiIPR008555. SIKE.
[Graphical view]
PANTHERiPTHR12186. PTHR12186. 1 hit.
PfamiPF05769. DUF837. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Colon, Head and Urinary bladder.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiSIKE1_MOUSE
AccessioniPrimary (citable) accession number: Q9CPR7
Secondary accession number(s): Q8CBP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.