TAXB1_PONAB
ID TAXB1_PONAB Reviewed; 813 AA.
AC Q5R4U3; Q5R566;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Tax1-binding protein 1 homolog;
GN Name=TAX1BP1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R4U3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R4U3-2; Sequence=VSP_018356;
CC -!- DOMAIN: The C-terminal UBZ-type zinc fingers function as ubiquitin-
CC binding domains. {ECO:0000250|UniProtKB:Q86VP1}.
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DR EMBL; CR861000; CAH93100.1; -; mRNA.
DR EMBL; CR861148; CAH93223.1; -; mRNA.
DR RefSeq; NP_001126895.1; NM_001133423.1. [Q5R4U3-2]
DR RefSeq; NP_001128892.1; NM_001135420.1.
DR AlphaFoldDB; Q5R4U3; -.
DR BMRB; Q5R4U3; -.
DR SMR; Q5R4U3; -.
DR STRING; 9601.ENSPPYP00000019830; -.
DR PRIDE; Q5R4U3; -.
DR GeneID; 100173910; -.
DR GeneID; 100189828; -.
DR KEGG; pon:100189828; -.
DR CTD; 8887; -.
DR eggNOG; ENOG502QQ1D; Eukaryota.
DR InParanoid; Q5R4U3; -.
DR OrthoDB; 179838at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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_0000234556"
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 489..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 144..627
FT /evidence="ECO:0000255"
FT COMPBIAS 489..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 617
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VP1"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UKC1"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VP1"
FT VAR_SEQ 589..612
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_018356"
FT CONFLICT 295
FT /note="T -> I (in Ref. 1; CAH93100)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="M -> I (in Ref. 1; CAH93100)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 813 AA; 93607 MW; BC2681AE952764F8 CRC64;
MTSFQEVPLQ TSNFAHVIFQ NVAKSYLPNA HLECHYTLTP YIHPHPKDWV GIFKVGWSTA
RDYYTFLWSP MPEHYVEGST VNCVLAFQGY YLPNDDGEFY QFCYVTHKGE IRGASTPFQF
RASSPVEELL TMEDEGNSDM LVVTTKAGLL ELKIEKTMKE KEELLKLIAV LEKETAQLRE
QVGRMERELN HEKERCDQLQ AEQKGLTEVT QSLKMENEEF KKRFSDATSK AHQLEEDIVS
VTHKAIEKET ELDSLKDKLK KAQHEREQLE CQLKTEKDEK ELYKVHLKNT EIENTKLMSE
VQTLKNLDGN KESVITHFKE EIGRLQLCLA EKENLQRTFL LTTSSKEDTF FLKEQLRKAE
EQVQATRQEV VFLAKELSDA VNVRDRTMAD LHTARLENEK VKKQLADAVA ELKLNAMKKD
QDKTDTLEHE LRREVEDLKL RLQMAADHYK EKFKECQRLQ KQINKLSDQS ANNNNVFTKK
MGNQQKVNDA SVNTDPATSA STVDVKPSPS AAEADFDIVT KGQVCEMTKE IADKTEKYNK
CKQLLQDEKA KCNKYADELA KMELKWKEQV KIAENVKLEL AEVQDNYKLQ LAEKDKEISG
LTSHLENLSR EKELKRSLEN QAERKMEGQN SQSPQCLKTC SEQNGYVLTL SNAQPVLQYG
NPYASQETRD GADGAFYPDE IQRPPVRVPS WGLEDNVVCS QPARNLSRPD GLEDSEDSKE
DENAPTAPDP PSQHLRGHGT GFCFDSSFDV HKKCPLCELM FPPNYDQSKF EEHVESHWKV
CPMCSEQFPP DYDQQVFERH VQTHFDQNVL NFD
