TAXB1_BOVIN
ID TAXB1_BOVIN Reviewed; 817 AA.
AC Q2KJE0;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Tax1-binding protein 1 homolog;
GN Name=TAX1BP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Rumen reticulum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; BC105389; AAI05390.1; -; mRNA.
DR RefSeq; NP_001039874.1; NM_001046409.2.
DR RefSeq; XP_005205596.1; XM_005205539.3.
DR AlphaFoldDB; Q2KJE0; -.
DR SMR; Q2KJE0; -.
DR STRING; 9913.ENSBTAP00000033573; -.
DR PaxDb; Q2KJE0; -.
DR PRIDE; Q2KJE0; -.
DR Ensembl; ENSBTAT00000033663; ENSBTAP00000033573; ENSBTAG00000019020.
DR GeneID; 535589; -.
DR KEGG; bta:535589; -.
DR CTD; 8887; -.
DR VEuPathDB; HostDB:ENSBTAG00000019020; -.
DR VGNC; VGNC:35619; TAX1BP1.
DR eggNOG; ENOG502QQ1D; Eukaryota.
DR GeneTree; ENSGT00950000183025; -.
DR HOGENOM; CLU_021315_1_0_1; -.
DR InParanoid; Q2KJE0; -.
DR OMA; LHTARVE; -.
DR OrthoDB; 179838at2759; -.
DR TreeFam; TF329501; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000019020; Expressed in prostate gland and 107 other tissues.
DR ExpressionAtlas; Q2KJE0; baseline and differential.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
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 Apoptosis; Coiled coil; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Zinc; Zinc-finger.
FT CHAIN 1..817
FT /note="Tax1-binding protein 1 homolog"
FT /id="PRO_0000234553"
FT ZN_FING 755..781
FT /note="UBZ1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT ZN_FING 782..808
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 609..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 144..628
FT /evidence="ECO:0000255"
FT COMPBIAS 609..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 761
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="1"
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 788
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 BINDING 808
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 617
FT /note="Phosphoserine; by IKKA"
FT /evidence="ECO:0000250|UniProtKB:Q86VP1"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UKC1"
FT MOD_RES 694
FT /note="Phosphoserine; by IKKA"
FT /evidence="ECO:0000250|UniProtKB:Q86VP1"
SQ SEQUENCE 817 AA; 94059 MW; 5293ED0CB703F092 CRC64;
MTSFQEVPLQ TSNFAHVIFQ NVAKSYLPNA HLECHYTLTP YIHPHPKDWV GIFKVGWSTA
RDYYTFLWSP MPEHYVEGSA VNCELAFQGY YLPNDDGEFY QFCYVTHKGE IRGASTPFQF
RAASPVEELL TMEDEGNSDM LVVTTKAGLL ELKIEKTMKE KEELLKLIAV LEKETTQLRE
QVGRMERELN HEKERGDQLQ AEQKALTKVS QSLKMENEEF KKRYNDVTSK ALQLEEDIVS
VTHKAIEKET ELDSLKDKLK KAQCEREQLE CQLKTEKDEK ELYKVHLKNT EIENTKLVSE
VQTLKNLDGN KENMITHFKE EISRLQFSLA EKENLQRTFL LTTSSKEDTF ILKEQLRKAE
EQIQATRQEA VFLAKELSDA VNVRDKTMAD LHTAHLENEK VKKQLTDALA ELKLSAVNKD
QEKTDTLEHE LRREVEDLKL RLQMAADHYK EKFKECQRLQ KQINKLSDQS ANSNSVFTKK
IGSQQKVNDA SINTDPAATA STVDVKPLPS TAETDFDNLT KGQVSEMTKE IADKTEKYNK
CKQLLQDEKT KCNKYADELA KMELKWKEQV KIAENIKLEL AEVVDNYKLQ LAEKEKEISG
LTSYWENLSR EKEHKRSVEN QAERKLEGQN SQSPHQISQC LKTSSEKSGH VPAVSNTQPV
LQYGNPYATP ETRDGADGAF YPDEIQRPPV RVPSWGLEDN VVCSQPARNL SRPDGLEDPE
DSKEDEKVPT APDPPSQHLR GHGTGFCFDP SFDVQKKCPL CELMFPPNYD QSKFEEHVES
HWKVCPMCSE QFPPDYDQQV FERHVQTHFD QNVLNFD
