TX1B3_HUMAN
ID TX1B3_HUMAN Reviewed; 124 AA.
AC O14907; B2RD53; D3DTJ6; Q7LCQ4;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Tax1-binding protein 3;
DE AltName: Full=Glutaminase-interacting protein 3;
DE AltName: Full=Tax interaction protein 1;
DE Short=TIP-1;
DE AltName: Full=Tax-interacting protein 1;
GN Name=TAX1BP3 {ECO:0000312|HGNC:HGNC:30684};
GN Synonyms=TIP1 {ECO:0000312|EMBL:AAF43104.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB84248.2}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH HTLV-1 TAX.
RC TISSUE=Peripheral blood lymphocyte {ECO:0000312|EMBL:AAB84248.2};
RX PubMed=9482110; DOI=10.1038/sj.onc.1201567;
RA Rousset R., Fabre S., Desbois C., Bantignies F., Jalinot P.;
RT "The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the
RT PDZ domain of cellular proteins.";
RL Oncogene 16:643-654(1998).
RN [2] {ECO:0000312|EMBL:AAF43104.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10673275; DOI=10.1101/gr.10.2.165;
RA Touchman J.W., Anikster Y., Dietrich N.L., Maduro V.V.B., McDowell G.,
RA Shotelersuk V., Bouffard G.G., Beckstrom-Sternberg S.M., Gahl W.A.,
RA Green E.D.;
RT "The genomic region encompassing the nephropathic cystinosis gene (CTNS):
RT complete sequencing of a 200-kb segment and discovery of a novel gene
RT within the common cystinosis-causing deletion.";
RL Genome Res. 10:165-173(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAG44368.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH GLS2.
RC TISSUE=Brain {ECO:0000312|EMBL:AAG44368.1};
RX PubMed=11163757; DOI=10.1016/s0014-5793(00)02373-5;
RA Olalla L., Aledo J.C., Bannenberg G., Marquez J.;
RT "The C-terminus of human glutaminase L mediates association with PDZ
RT domain-containing proteins.";
RL FEBS Lett. 488:116-122(2001).
RN [4] {ECO:0000312|EMBL:AAK69111.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary {ECO:0000312|EMBL:AAK69111.1};
RA Honore B.;
RT "hPWP1-interacting proteins 2 and 11 (Tax-interacting protein 1).";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6] {ECO:0000312|EMBL:AAK69111.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000312|EMBL:AAH23980.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH23980.1};
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 [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RTKN, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10940294; DOI=10.1074/jbc.m000465200;
RA Reynaud C., Fabre S., Jalinot P.;
RT "The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is
RT involved in Rho signaling to the serum response element.";
RL J. Biol. Chem. 275:33962-33968(2000).
RN [9]
RP FUNCTION, INTERACTION WITH KCNJ4, MUTAGENESIS OF LYS-20 AND HIS-90,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16855024; DOI=10.1091/mbc.e06-02-0129;
RA Alewine C., Olsen O., Wade J.B., Welling P.A.;
RT "TIP-1 has PDZ scaffold antagonist activity.";
RL Mol. Biol. Cell 17:4200-4211(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION, AND INTERACTION WITH ARHGEF16.
RX PubMed=21139582; DOI=10.1038/sj.bjc.6606026;
RA Oliver A.W., He X., Borthwick K., Donne A.J., Hampson L., Hampson I.N.;
RT "The HPV16 E6 binding protein Tip-1 interacts with ARHGEF16, which
RT activates Cdc42.";
RL Br. J. Cancer 104:324-331(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP STRUCTURE BY NMR, AND INTERACTION WITH KCNJ4.
RX PubMed=19685007; DOI=10.1007/s10858-009-9361-8;
RA Durney M.A., Birrane G., Anklin C., Soni A., Ladias J.A.;
RT "Solution structure of the human Tax-interacting protein-1.";
RL J. Biomol. NMR 45:329-334(2009).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), AND INTERACTION WITH KCNJ4.
RX PubMed=19635485; DOI=10.1016/j.jmb.2009.07.060;
RA Yan X., Zhou H., Zhang J., Shi C., Xie X., Wu Y., Tian C., Shen Y.,
RA Long J.;
RT "Molecular mechanism of inward rectifier potassium channel 2.3 regulation
RT by tax-interacting protein-1.";
RL J. Mol. Biol. 392:967-976(2009).
RN [19] {ECO:0000312|EMBL:AAK69111.1}
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 13-124.
RG Structural genomics consortium (SGC);
RT "The structure of the PDZ domain of TAX1BP.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [20]
RP STRUCTURE BY NMR IN COMPLEX WITH GLS2, AND INTERACTION WITH GLS2.
RX PubMed=21417405; DOI=10.1021/bi102055y;
RA Zoetewey D.L., Ovee M., Banerjee M., Bhaskaran R., Mohanty S.;
RT "Promiscuous binding at the crossroads of numerous cancer pathways: insight
RT from the binding of glutaminase interacting protein with glutaminase L.";
RL Biochemistry 50:3528-3539(2011).
RN [21]
RP STRUCTURE BY NMR IN COMPLEX WITH ADGRB2, AND INTERACTION WITH ADGRB2.
RX PubMed=21787750; DOI=10.1016/j.bbrc.2011.07.029;
RA Zencir S., Ovee M., Dobson M.J., Banerjee M., Topcu Z., Mohanty S.;
RT "Identification of brain-specific angiogenesis inhibitor 2 as an
RT interaction partner of glutaminase interacting protein.";
RL Biochem. Biophys. Res. Commun. 411:792-797(2011).
RN [22]
RP VARIANT THR-33, AND TISSUE SPECIFICITY.
RX PubMed=25645515; DOI=10.1002/humu.22759;
RA Reinstein E., Orvin K., Tayeb-Fligelman E., Stiebel-Kalish H., Tzur S.,
RA Pimienta A.L., Bazak L., Bengal T., Cohen L., Gaton D.D., Bormans C.,
RA Landau M., Kornowski R., Shohat M., Behar D.M.;
RT "Mutations in TAX1BP3 cause dilated cardiomyopathy with septo-optic
RT dysplasia.";
RL Hum. Mutat. 36:439-442(2015).
CC -!- FUNCTION: May regulate a number of protein-protein interactions by
CC competing for PDZ domain binding sites. Binds CTNNB1 and may thereby
CC act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A
CC for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play
CC a role in the Rho signaling pathway. May play a role in activation of
CC CDC42 by the viral protein HPV16 E6. {ECO:0000269|PubMed:10940294,
CC ECO:0000269|PubMed:16855024, ECO:0000269|PubMed:21139582}.
CC -!- SUBUNIT: Interacts (via its PDZ domain) with GLS2. Interacts (via its
CC PDZ domain) with RTKN (via the C-terminal region); this interaction
CC facilitates Rho-mediated activation of the FOS serum response element
CC (SRE). Interacts (via its PDZ domain) with CTNNB1; this interaction
CC inhibits the transcriptional activity of CTNNB1. Interacts with HTLV-1
CC TAX protein. Interacts (via PDZ domain) with ARHGEF16. Interacts (via
CC PDZ domain) with KCNJ4 (via C-terminus). Competes with LIN7A for KCNJ4
CC binding. Interacts with ADGRB2 (PubMed:21787750).
CC {ECO:0000269|PubMed:10940294, ECO:0000269|PubMed:11163757,
CC ECO:0000269|PubMed:16855024, ECO:0000269|PubMed:19635485,
CC ECO:0000269|PubMed:19685007, ECO:0000269|PubMed:21139582,
CC ECO:0000269|PubMed:21417405, ECO:0000269|PubMed:21787750,
CC ECO:0000269|PubMed:9482110}.
CC -!- INTERACTION:
CC O14907; Q96D59: RNF183; NbExp=3; IntAct=EBI-723259, EBI-743938;
CC O14907; P03126: E6; Xeno; NbExp=2; IntAct=EBI-723259, EBI-1177242;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane; Peripheral
CC membrane protein; Cytoplasmic side. Note=Recruited to the cell membrane
CC by interaction with membrane proteins.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in brain, heart, kidney, lung,
CC small intestine and skeletal muscle. Detected in various cell lines
CC including HeLa. Weakly expressed in peripheral blood leukocytes.
CC {ECO:0000269|PubMed:10940294, ECO:0000269|PubMed:16855024,
CC ECO:0000269|PubMed:25645515}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF43104.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF028823; AAB84248.2; -; mRNA.
DR EMBL; AF168787; AAF43104.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF234997; AAG44368.1; -; mRNA.
DR EMBL; AF277318; AAK69111.1; -; mRNA.
DR EMBL; AK315408; BAG37800.1; -; mRNA.
DR EMBL; CH471108; EAW90491.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90492.1; -; Genomic_DNA.
DR EMBL; BC023980; AAH23980.1; -; mRNA.
DR CCDS; CCDS11032.1; -.
DR RefSeq; NP_001191627.1; NM_001204698.1.
DR RefSeq; NP_055419.1; NM_014604.3.
DR PDB; 2KG2; NMR; -; A=2-124.
DR PDB; 2L4S; NMR; -; A=1-124.
DR PDB; 2L4T; NMR; -; A=1-124.
DR PDB; 2VZ5; X-ray; 1.74 A; A=13-124.
DR PDB; 3GJ9; X-ray; 2.80 A; A/B=1-124.
DR PDB; 3SFJ; X-ray; 1.24 A; A/C=10-112.
DR PDB; 4E3B; X-ray; 1.50 A; A/B=11-112.
DR PDB; 4NNL; X-ray; 1.50 A; A/B=10-112.
DR PDB; 4NNM; X-ray; 1.60 A; A/B=10-120.
DR PDBsum; 2KG2; -.
DR PDBsum; 2L4S; -.
DR PDBsum; 2L4T; -.
DR PDBsum; 2VZ5; -.
DR PDBsum; 3GJ9; -.
DR PDBsum; 3SFJ; -.
DR PDBsum; 4E3B; -.
DR PDBsum; 4NNL; -.
DR PDBsum; 4NNM; -.
DR AlphaFoldDB; O14907; -.
DR BMRB; O14907; -.
DR SMR; O14907; -.
DR BioGRID; 119061; 62.
DR ELM; O14907; -.
DR IntAct; O14907; 21.
DR MINT; O14907; -.
DR STRING; 9606.ENSP00000225525; -.
DR iPTMnet; O14907; -.
DR PhosphoSitePlus; O14907; -.
DR BioMuta; TAX1BP3; -.
DR UCD-2DPAGE; O14907; -.
DR EPD; O14907; -.
DR jPOST; O14907; -.
DR MassIVE; O14907; -.
DR MaxQB; O14907; -.
DR PaxDb; O14907; -.
DR PeptideAtlas; O14907; -.
DR PRIDE; O14907; -.
DR ProteomicsDB; 48291; -.
DR TopDownProteomics; O14907; -.
DR ABCD; O14907; 1 sequenced antibody.
DR Antibodypedia; 23095; 133 antibodies from 26 providers.
DR DNASU; 30851; -.
DR Ensembl; ENST00000225525.4; ENSP00000225525.3; ENSG00000213977.8.
DR GeneID; 30851; -.
DR KEGG; hsa:30851; -.
DR MANE-Select; ENST00000225525.4; ENSP00000225525.3; NM_014604.4; NP_055419.1.
DR UCSC; uc002fwc.4; human.
DR CTD; 30851; -.
DR DisGeNET; 30851; -.
DR GeneCards; TAX1BP3; -.
DR HGNC; HGNC:30684; TAX1BP3.
DR HPA; ENSG00000213977; Low tissue specificity.
DR MIM; 616476; gene.
DR neXtProt; NX_O14907; -.
DR OpenTargets; ENSG00000213977; -.
DR PharmGKB; PA134950693; -.
DR VEuPathDB; HostDB:ENSG00000213977; -.
DR eggNOG; KOG3553; Eukaryota.
DR GeneTree; ENSGT00390000002877; -.
DR HOGENOM; CLU_130477_0_0_1; -.
DR InParanoid; O14907; -.
DR OMA; LHMLVAR; -.
DR OrthoDB; 1471323at2759; -.
DR PhylomeDB; O14907; -.
DR TreeFam; TF318964; -.
DR BRENDA; 3.5.1.2; 2681.
DR PathwayCommons; O14907; -.
DR Reactome; R-HSA-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR SignaLink; O14907; -.
DR BioGRID-ORCS; 30851; 45 hits in 1084 CRISPR screens.
DR EvolutionaryTrace; O14907; -.
DR GeneWiki; TAX1BP3; -.
DR GenomeRNAi; 30851; -.
DR Pharos; O14907; Tbio.
DR PRO; PR:O14907; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O14907; protein.
DR Bgee; ENSG00000213977; Expressed in tibial nerve and 92 other tissues.
DR ExpressionAtlas; O14907; baseline and differential.
DR Genevisible; O14907; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IDA:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR017268; Tax1-binding_p3.
DR Pfam; PF00595; PDZ; 1.
DR PIRSF; PIRSF037712; Tax1-binding_p3; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Cytoplasm; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..124
FT /note="Tax1-binding protein 3"
FT /id="PRO_0000233943"
FT DOMAIN 15..112
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 33
FT /note="I -> T (found in a patient with dilated
FT cardiomyopathy and septo-optic dysplasia; unknown
FT pathological significance; dbSNP:rs1057517690)"
FT /evidence="ECO:0000269|PubMed:25645515"
FT /id="VAR_073966"
FT MUTAGEN 20
FT /note="K->A: Abolishes interaction with KCNJ4."
FT /evidence="ECO:0000269|PubMed:16855024"
FT MUTAGEN 90
FT /note="H->A: Abolishes interaction with KCNJ4."
FT /evidence="ECO:0000269|PubMed:16855024"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2KG2"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:3SFJ"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3SFJ"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:3SFJ"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3SFJ"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2L4S"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3SFJ"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:2KG2"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2L4S"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:3SFJ"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2KG2"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:3SFJ"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:3SFJ"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2L4T"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:3SFJ"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2L4T"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:3SFJ"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:2KG2"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:2KG2"
SQ SEQUENCE 124 AA; 13735 MW; FF0BCDF475F682CD CRC64;
MSYIPGQPVT AVVQRVEIHK LRQGENLILG FSIGGGIDQD PSQNPFSEDK TDKGIYVTRV
SEGGPAEIAG LQIGDKIMQV NGWDMTMVTH DQARKRLTKR SEEVVRLLVT RQSLQKAVQQ
SMLS
