TAXB1_RAT
ID TAXB1_RAT Reviewed; 813 AA.
AC Q66HA4; Q7TQ13;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Tax1-binding protein 1 homolog;
DE AltName: Full=Liver regeneration-related protein LRRG004;
GN Name=Tax1bp1; ORFNames=Aa1076;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Xu C.S., Li W.Q., Li Y.C., Chai L.Q., Yuan J.Y., Yang K.J., Yan H.M.,
RA Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F., Han H.P., Wang G.P.,
RA Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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).
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 TNFAIP3. Interacts with STARD13 (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q66HA4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q66HA4-2; Sequence=VSP_018357, VSP_018358;
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; AY318959; AAP85370.1; -; mRNA.
DR EMBL; BC081949; AAH81949.1; -; mRNA.
DR RefSeq; NP_001004199.1; NM_001004199.1. [Q66HA4-1]
DR AlphaFoldDB; Q66HA4; -.
DR BMRB; Q66HA4; -.
DR SMR; Q66HA4; -.
DR IntAct; Q66HA4; 1.
DR STRING; 10116.ENSRNOP00000046052; -.
DR PaxDb; Q66HA4; -.
DR PRIDE; Q66HA4; -.
DR Ensembl; ENSRNOT00000011371; ENSRNOP00000011371; ENSRNOG00000008393. [Q66HA4-1]
DR Ensembl; ENSRNOT00000041988; ENSRNOP00000046052; ENSRNOG00000008393. [Q66HA4-2]
DR GeneID; 246244; -.
DR KEGG; rno:246244; -.
DR UCSC; RGD:708579; rat. [Q66HA4-1]
DR CTD; 8887; -.
DR RGD; 708579; Tax1bp1.
DR eggNOG; ENOG502QQ1D; Eukaryota.
DR GeneTree; ENSGT00950000183025; -.
DR HOGENOM; CLU_021315_1_0_1; -.
DR InParanoid; Q66HA4; -.
DR OMA; LHTARVE; -.
DR OrthoDB; 179838at2759; -.
DR PhylomeDB; Q66HA4; -.
DR TreeFam; TF329501; -.
DR Reactome; R-RNO-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-RNO-936440; Negative regulators of DDX58/IFIH1 signaling.
DR PRO; PR:Q66HA4; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000008393; Expressed in colon and 20 other tissues.
DR Genevisible; Q66HA4; RN.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:RGD.
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 2: Evidence at transcript level;
KW Alternative splicing; Apoptosis; Coiled coil; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..813
FT /note="Tax1-binding protein 1 homolog"
FT /id="PRO_0000234557"
FT ZN_FING 751..777
FT /note="UBZ1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT ZN_FING 778..804
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 667..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 144..596
FT /evidence="ECO:0000255"
FT BINDING 754
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 757
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 773
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 777
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 781
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 784
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 800
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 804
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:0000250|UniProtKB:Q3UKC1"
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 618
FT /note="Phosphoserine; by IKKA"
FT /evidence="ECO:0000250|UniProtKB:Q86VP1"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UKC1"
FT MOD_RES 692
FT /note="Phosphoserine; by IKKA"
FT /evidence="ECO:0000250|UniProtKB:Q86VP1"
FT VAR_SEQ 590..613
FT /note="LQLAEKDKEINCLASFLENLSREK -> VSSENVRLELAELEDSYS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018357"
FT VAR_SEQ 780..813
FT /note="VCPMCSEQFPPDYDQQGFERHVQTHFDQNVLNFD -> LPGEFFIEYPWATY
FT APHETLGPWRRLGKVLAVLSSDTQLWCEKPDISLGRQKQKILGMCWSESRQISDLQVQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018358"
SQ SEQUENCE 813 AA; 93197 MW; 82073C220E017AD3 CRC64;
MTSFQEVPLQ TSNFAHVIFQ NVAKSYLPNA HLECHYTLTP YIHPHSKDWV GIFKVGWSTA
RDYYTFLWSP MPEQYVEGST VNCVLAFQGY YLPNDDGEFY QFCYVTHKGE IRGASTPFQF
RAASPVEELL TMEDEGNSDM LVVTTKAGLL ELKIEKTLKE KEELLKLVSV LEKETAQLRE
QVGRMERELS HEKSRCEQLQ AEQKGLLEVS QSLRVENEEF MKRYSDATSK AHQLEEDIVS
VTHKAVEKET ELDSLKDKLR KAQQEKEQLE CQLKTEKDEK ELYKVHLKNT EIENTKLVSE
IQTLKNVDGN KESMITHFKE EIGKLQSCLA DKENLHRALL LTTSNKEDTL LLKEQLRKAE
EQVQATRQEL IFLAKELSDA VNVRDKTMAD LHTARLENER VKKQLADTLA ELQLHAVKTD
QEKTDTLEHE LRREVEDLKL RLQMAADHYK EKFKECQRLQ KQINKLSDQS ASSNGVFTKR
MGSQQKVNDA SINTDPAASA SAVDVKPAAS CAAETDFDMS AKDHVCEVTK EMAEKVEKYN
KCKQLLQDEK AKCNKYADEL AQMELKWKEQ VRIAENVKLE LAELEDSYSL QLAEKDKEIN
CLASFLENLS REKELTKSLE DQKGRKMEGQ SPQQVSRCLN TCSEQSGLLP TLPAAQPVLQ
YGNPYTAHET RDGADGAFYP DEIQRPPVRG PSWEDNVVCS QPARNLSRPD GLEDPEDSRE
DENVPIPPDP ANQHLRGHGA GFCFDSSFDV HKKCPLCELM FPPNYDQIKF EEHVESHWKV
CPMCSEQFPP DYDQQGFERH VQTHFDQNVL NFD
