ID TBKB1_MOUSE Reviewed; 611 AA.
AC A2A9T0; A2A9S9; Q6PFF1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 101.
DE RecName: Full=TANK-binding kinase 1-binding protein 1;
DE Short=TBK1-binding protein 1;
DE AltName: Full=Similar to NAP1 TBK1 adapter;
GN Name=Tbkbp1 {ECO:0000312|MGI:MGI:1920424};
GN Synonyms=Sintbad {ECO:0000303|PubMed:17568778};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH57590.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH57590.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH57590.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH TBK1 AND IKBKE, AND HOMODIMER.
RX PubMed=17568778; DOI=10.1038/sj.emboj.7601743;
RA Ryzhakov G., Randow F.;
RT "SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-
RT binding domain with NAP1 and TANK.";
RL EMBO J. 26:3180-3190(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Adapter protein which constitutively binds TBK1 and IKBKE
CC playing a role in antiviral innate immunity. Essential for the
CC efficient induction of IRF-dependent transcription following infection
CC with Sendai virus. {ECO:0000269|PubMed:17568778}.
CC -!- SUBUNIT: Homodimer (PubMed:17568778). May form a heterodimer with NAP1.
CC Interacts with TKB1 and IKBKE (PubMed:17568778). Weakly interacts with
CC DDX3X (By similarity). {ECO:0000250|UniProtKB:A7MCY6,
CC ECO:0000269|PubMed:17568778}.
CC -!- INTERACTION:
CC A2A9T0; Q9WUN2: Tbk1; NbExp=2; IntAct=EBI-7987134, EBI-764193;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2A9T0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=A2A9T0-2; Sequence=VSP_032344, VSP_052716;
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DR EMBL; AL627445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057590; AAH57590.1; -; mRNA.
DR CCDS; CCDS88239.1; -. [A2A9T0-1]
DR RefSeq; NP_932768.2; NM_198100.2.
DR RefSeq; XP_006534398.1; XM_006534335.1.
DR RefSeq; XP_006534399.1; XM_006534336.2.
DR RefSeq; XP_006534400.1; XM_006534337.2.
DR AlphaFoldDB; A2A9T0; -.
DR SMR; A2A9T0; -.
DR BioGRID; 215817; 4.
DR IntAct; A2A9T0; 1.
DR MINT; A2A9T0; -.
DR STRING; 10090.ENSMUSP00000103240; -.
DR iPTMnet; A2A9T0; -.
DR PhosphoSitePlus; A2A9T0; -.
DR EPD; A2A9T0; -.
DR MaxQB; A2A9T0; -.
DR PaxDb; 10090-ENSMUSP00000103240; -.
DR ProteomicsDB; 254830; -. [A2A9T0-1]
DR ProteomicsDB; 254831; -. [A2A9T0-2]
DR Antibodypedia; 30174; 169 antibodies from 27 providers.
DR DNASU; 73174; -.
DR Ensembl; ENSMUST00000066078.12; ENSMUSP00000065461.6; ENSMUSG00000038517.16. [A2A9T0-1]
DR Ensembl; ENSMUST00000107614.8; ENSMUSP00000103239.2; ENSMUSG00000038517.16. [A2A9T0-1]
DR GeneID; 73174; -.
DR KEGG; mmu:73174; -.
DR AGR; MGI:1920424; -.
DR CTD; 9755; -.
DR MGI; MGI:1920424; Tbkbp1.
DR VEuPathDB; HostDB:ENSMUSG00000038517; -.
DR eggNOG; ENOG502QVP4; Eukaryota.
DR GeneTree; ENSGT00940000153704; -.
DR InParanoid; A2A9T0; -.
DR OMA; QRHSPIQ; -.
DR OrthoDB; 4174931at2759; -.
DR PhylomeDB; A2A9T0; -.
DR TreeFam; TF331289; -.
DR BioGRID-ORCS; 73174; 5 hits in 77 CRISPR screens.
DR PRO; PR:A2A9T0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; A2A9T0; Protein.
DR Bgee; ENSMUSG00000038517; Expressed in granulocyte and 185 other cell types or tissues.
DR ExpressionAtlas; A2A9T0; baseline and differential.
DR Genevisible; A2A9T0; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR InterPro; IPR041641; CALCOCO1/2_Zn_UBZ1.
DR InterPro; IPR024581; TBD.
DR PANTHER; PTHR14432; PROSAPIP2 PROTEIN/5-AZACYTIDINE INDUCED GENE 2; 1.
DR PANTHER; PTHR14432:SF2; TANK-BINDING KINASE 1-BINDING PROTEIN 1; 1.
DR Pfam; PF12845; TBD; 1.
DR PROSITE; PS51905; ZF_UBZ1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Immunity; Innate immunity;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..611
FT /note="TANK-binding kinase 1-binding protein 1"
FT /id="PRO_0000324655"
FT ZN_FING 579..605
FT /note="UBZ1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT REGION 1..280
FT /note="Homodimerization"
FT REGION 281..330
FT /note="Interaction with TBK1 and IKBKE"
FT /evidence="ECO:0000269|PubMed:17568778"
FT REGION 328..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 48..162
FT /evidence="ECO:0000255"
FT COILED 218..277
FT /evidence="ECO:0000255"
FT COMPBIAS 328..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..435
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 582
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 585
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 601
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 605
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT VAR_SEQ 212
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032344"
FT VAR_SEQ 364..377
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052716"
SQ SEQUENCE 611 AA; 67001 MW; B2AF8DF98F1C6EF9 CRC64;
MESMFEDDIS ILTQEALGPS EVWLDGPGDP SLGGDMCSAS HFALITAYGD IKERLGGLER
ENATLRRRLK VYEIKYPLIT DFGEEHGFPL YELKDGSLLE VEKVSLQQRL NQFQHELQKS
KEQEEQLGEM IQAYEKLCVE KSDLETELGE MRALVETHLR QICGLEKQLQ QQQGLRDAAF
SSLSPPAVPA SACPDLDLHY LALRGGPALG HAGWPGPTSV SVSELERRRL EEALEAAQGE
ARGAQLREEQ LQAECERLQG ELKQLQETRA QDLASNQSEC DMAWVKRVGD DQVNLALAYT
ELTEELGRLR ELSSLQGRIL RTLLQEQARN AGQRHSPLSQ RHSPAPACPS PSPPARPPPC
APCQSPAAQR RSPVPPCPSP QQRRSPASPS CPSPVPQRRS PVPPSCQSPS PQRRSPVPPS
CPAPQPRPPP PPGERTLAER VYAKPPSHHA KAGFQGRRSY SELAEGAAYA GASPAWLQAE
AATLPKPRAY GGELYGRPLS PRRAFEGIRL RFEKQPSEEE EWAMPASPPS PEAGTIRCAS
FCAGFPIPES PAATAYAHAE HAQSWPSINL LMETVGSDIR SCPLCQLGFP VGYPDDALIK
HIDSHLENSK I
//
