TAXB1_MOUSE
ID TAXB1_MOUSE Reviewed; 814 AA.
AC Q3UKC1; Q91YT6; Q9CVF0; Q9DC45;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Tax1-binding protein 1 homolog;
GN Name=Tax1bp1;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung, Placenta, and Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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]
RP INTERACTION WITH TNFAIP3.
RX PubMed=10435631; DOI=10.1038/sj.onc.1202787;
RA de Valck D., Jin D.-Y., Heyninck K., van de Craen M., Contreras R.,
RA Fiers W., Jeang K.-T., Beyaert R.;
RT "The zinc finger protein A20 interacts with a novel anti-apoptotic protein
RT which is cleaved by specific caspases.";
RL Oncogene 18:4182-4190(1999).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=15509224; DOI=10.1111/j.1525-142x.2004.04050.x;
RA Lehoczky J.A., Williams M.E., Innis J.W.;
RT "Conserved expression domains for genes upstream and within the HoxA and
RT HoxD clusters suggests a long-range enhancer existed before cluster
RT duplication.";
RL Evol. Dev. 6:423-430(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-693, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-632 AND SER-693, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Pancreas, Spleen, and Testis;
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: Inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-
CC apoptotic activity. Degraded by caspase-3-like family proteins upon
CC TNF-induced apoptosis. May also play a role in the pro-inflammatory
CC cytokine IL-1 signaling cascade (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. Interacts with TRAF6 in a IL-1-dependent manner.
CC Interacts with STARD13 (By similarity). Interacts with TNFAIP3.
CC {ECO:0000250, ECO:0000269|PubMed:10435631}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 11.5 dpc and 12.5 dpc in distal limb
CC and genital bud. {ECO:0000269|PubMed:15509224}.
CC -!- DOMAIN: The C-terminal UBZ-type zinc fingers function as ubiquitin-
CC binding domains. {ECO:0000250|UniProtKB:Q86VP1}.
CC -!- PTM: Phosphorylated in the C-terminal region by CHUK/IKKA leading to
CC NF-kappa-B signaling down-regulation. {ECO:0000250}.
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DR EMBL; AK004574; BAB23383.1; -; mRNA.
DR EMBL; AK008528; BAB25721.1; -; mRNA.
DR EMBL; AK146076; BAE26880.1; -; mRNA.
DR EMBL; BC014798; AAH14798.1; -; mRNA.
DR CCDS; CCDS39490.1; -.
DR RefSeq; NP_080092.2; NM_025816.3.
DR RefSeq; XP_006506432.1; XM_006506369.3.
DR AlphaFoldDB; Q3UKC1; -.
DR BMRB; Q3UKC1; -.
DR SMR; Q3UKC1; -.
DR BioGRID; 206586; 19.
DR IntAct; Q3UKC1; 6.
DR MINT; Q3UKC1; -.
DR STRING; 10090.ENSMUSP00000079548; -.
DR iPTMnet; Q3UKC1; -.
DR PhosphoSitePlus; Q3UKC1; -.
DR EPD; Q3UKC1; -.
DR jPOST; Q3UKC1; -.
DR MaxQB; Q3UKC1; -.
DR PaxDb; Q3UKC1; -.
DR PeptideAtlas; Q3UKC1; -.
DR PRIDE; Q3UKC1; -.
DR ProteomicsDB; 254648; -.
DR Antibodypedia; 12449; 246 antibodies from 28 providers.
DR DNASU; 52440; -.
DR Ensembl; ENSMUST00000080723; ENSMUSP00000079548; ENSMUSG00000004535.
DR GeneID; 52440; -.
DR KEGG; mmu:52440; -.
DR UCSC; uc009byz.2; mouse.
DR CTD; 8887; -.
DR MGI; MGI:1289308; Tax1bp1.
DR VEuPathDB; HostDB:ENSMUSG00000004535; -.
DR eggNOG; ENOG502QQ1D; Eukaryota.
DR GeneTree; ENSGT00950000183025; -.
DR HOGENOM; CLU_021315_1_0_1; -.
DR InParanoid; Q3UKC1; -.
DR OMA; DANIQRW; -.
DR OrthoDB; 179838at2759; -.
DR PhylomeDB; Q3UKC1; -.
DR TreeFam; TF329501; -.
DR Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-MMU-936440; Negative regulators of DDX58/IFIH1 signaling.
DR BioGRID-ORCS; 52440; 17 hits in 74 CRISPR screens.
DR ChiTaRS; Tax1bp1; mouse.
DR PRO; PR:Q3UKC1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q3UKC1; protein.
DR Bgee; ENSMUSG00000004535; Expressed in ileal epithelium and 263 other tissues.
DR ExpressionAtlas; Q3UKC1; baseline and differential.
DR Genevisible; Q3UKC1; MM.
DR GO; GO:0019900; F:kinase binding; IPI:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; NAS:BHF-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
DR InterPro; IPR012852; CALCOCO1-like.
DR InterPro; IPR041641; CALCOCO1/2_Zn_UBZ1.
DR InterPro; IPR041611; SKICH.
DR Pfam; PF07888; CALCOCO1; 1.
DR Pfam; PF17751; SKICH; 1.
DR Pfam; PF18112; Zn-C2H2_12; 2.
DR PROSITE; PS51905; ZF_UBZ1; 2.
PE 1: Evidence at protein level;
KW Apoptosis; Coiled coil; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Zinc; Zinc-finger.
FT CHAIN 1..814
FT /note="Tax1-binding protein 1 homolog"
FT /id="PRO_0000234555"
FT ZN_FING 752..778
FT /note="UBZ1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT ZN_FING 779..805
FT /note="UBZ1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT REGION 320..420
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT REGION 701..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 144..623
FT /evidence="ECO:0000255"
FT BINDING 755
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 758
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 774
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 778
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 782
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 785
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 801
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 805
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VP1"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VP1"
FT MOD_RES 619
FT /note="Phosphoserine; by IKKA"
FT /evidence="ECO:0000250|UniProtKB:Q86VP1, ECO:0000305"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 693
FT /note="Phosphoserine; by IKKA"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 328
FT /note="C -> S (in Ref. 1; BAB23383)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="Q -> P (in Ref. 1; BAB23383)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="H -> Y (in Ref. 1; BAE26880)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="P -> T (in Ref. 1; BAB23383)"
FT /evidence="ECO:0000305"
FT CONFLICT 751
FT /note="V -> A (in Ref. 2; AAH14798)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="P -> H (in Ref. 1; BAB25721)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 814 AA; 93630 MW; 828A1FC7D61A06B7 CRC64;
MTSFQEVQLQ TSNFAHVIFQ NVAKSYLPNA HLECHYTLTP YIHPHSKDWV GIFKVGWSTA
RDYYTFLWSP MPEHYVEGST VNCVLAFQGY YLPNDDGEFY QFCYVTHKGE IRGASTPFQF
RAASPVEELL TMEDEGNSDM LVVTTKAGLL ELKIEKTLKE KEELLKLIAV LEKETAQLRE
QVGRMERELS QEKGRCEQLQ AEQKGLLEVS QSLRVENEEF MKRYSDATAK VQQLEEDIVS
VTHKAIEKET DLDSLKDKLR KAQHEREQLE CQLQTEKDEK ELYKVHLKNT EIENTKLVSE
IQTLKNLDGN KESMITHFKE EISKLQSCLA DKENLYRALL LTTSNKEDTL FLKEQLRKAE
EQVQATRQEL IFLTKELSDA VNVRDKTMAD LHTARLENER VKKQLADTLA ELQLHAVKKD
QEKTDTLEHE LRREVEDLKL RLQMAADHYR EKFKECQRLQ KQINKLSDQA ASTNSVFTKK
MGSQQKVNDA SINTDPAAST SASAVDVKPA ASCAETGFDM STKDHVCEMT KEIAEKIEKY
NKCKQLLQDE KTKCNKYAEE LAKMELKWKE QVKIAENVKL ELAEVEDNYK VQLAEKEKEI
NGLASYLENL SREKELTKSL EDQKGRKLEG QSPQQVSRCL NTCSEQNGLL PPLSSAQPVL
QYGNPYSAQE TRDGADGAFY PDEIQRPPVR VPSWEDNVVC SQPARNLSRP DGLEDPEDSR
EDENVPIPPD PANQHLRSHG AGFCFDSSFD VHKKCPLCEL MFPPNYDQTK FEEHVESHWK
VCPMCSEQFP PDYDQQGFER HVQTHFDQNV LNFD
