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TAX_HTL1A
ID   TAX_HTL1A               Reviewed;         353 AA.
AC   P03409;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Protein Tax-1;
DE   AltName: Full=Protein X-LOR;
DE            Short=Protein PX;
DE   AltName: Full=Trans-activating transcriptional regulatory protein of HTLV-1;
GN   Name=Tax;
OS   Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX   NCBI_TaxID=11926;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6304725; DOI=10.1073/pnas.80.12.3618;
RA   Seiki M., Hattori S., Hirayama Y., Yoshida M.C.;
RT   "Human adult T-cell leukemia virus: complete nucleotide sequence of the
RT   provirus genome integrated in leukemia cell DNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:3618-3622(1983).
RN   [2]
RP   FUNCTION.
RX   PubMed=2990037; DOI=10.1126/science.2990037;
RA   Chen I.S.Y., Slamon D.J., Rosenblatt J.D., Shah N.P., Quan S.G.,
RA   Wachsman W.;
RT   "The x gene is essential for HTLV replication.";
RL   Science 229:54-58(1985).
RN   [3]
RP   FUNCTION.
RX   PubMed=2768259; DOI=10.1016/s0021-9258(19)84815-9;
RA   Giam C.-Z., Xu Y.L.;
RT   "HTLV-I tax gene product activates transcription via pre-existing cellular
RT   factors and cAMP responsive element.";
RL   J. Biol. Chem. 264:15236-15241(1989).
RN   [4]
RP   DOMAIN ZINC-FINGER.
RX   PubMed=1585646; DOI=10.1016/0042-6822(92)90530-3;
RA   Semmes O.J., Jeang K.T.;
RT   "HTLV-I Tax is a zinc-binding protein: role of zinc in Tax structure and
RT   function.";
RL   Virology 188:754-764(1992).
RN   [5]
RP   INTERACTION WITH RAT CREB1.
RX   PubMed=1386673; DOI=10.1073/pnas.89.15.7070;
RA   Zhao L.J., Giam C.-Z.;
RT   "Human T-cell lymphotropic virus type I (HTLV-I) transcriptional activator,
RT   Tax, enhances CREB binding to HTLV-I 21-base-pair repeats by protein-
RT   protein interaction.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:7070-7074(1992).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH HOST CREB1.
RX   PubMed=8970957; DOI=10.1128/jvi.70.12.8368-8374.1996;
RA   Tie F., Adya N., Greene W.C., Giam C.Z.;
RT   "Interaction of the human T-lymphotropic virus type 1 Tax dimer with CREB
RT   and the viral 21-base-pair repeat.";
RL   J. Virol. 70:8368-8374(1996).
RN   [7]
RP   SUBUNIT.
RX   PubMed=9016568; DOI=10.1093/nar/25.2.379;
RA   Jin D.Y., Jeang K.T.;
RT   "HTLV-I Tax self-association in optimal trans-activation function.";
RL   Nucleic Acids Res. 25:379-387(1997).
RN   [8]
RP   DOMAIN PDZ-BINDING.
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   [9]
RP   INTERACTION WITH HOST CREBBP AND EP300.
RX   PubMed=9528808; DOI=10.1128/mcb.18.4.2392;
RA   Bex F., Yin M.-J., Burny A., Gaynor R.B.;
RT   "Differential transcriptional activation by human T-cell leukemia virus
RT   type 1 Tax mutants is mediated by distinct interactions with CREB binding
RT   protein and p300.";
RL   Mol. Cell. Biol. 18:2392-2405(1998).
RN   [10]
RP   DNA-BINDING.
RX   PubMed=9447968; DOI=10.1128/mcb.18.2.721;
RA   Lenzmeier B.A., Giebler H.A., Nyborg J.K.;
RT   "Human T-cell leukemia virus type 1 Tax requires direct access to DNA for
RT   recruitment of CREB binding protein to the viral promoter.";
RL   Mol. Cell. Biol. 18:721-731(1998).
RN   [11]
RP   PHOSPHORYLATION AT SER-300 AND SER-301.
RX   PubMed=9847380; DOI=10.1128/jvi.73.1.738-745.1999;
RA   Bex F., Murphy K., Wattiez R., Burny A., Gaynor R.B.;
RT   "Phosphorylation of the human T-cell leukemia virus type 1 transactivator
RT   tax on adjacent serine residues is critical for tax activation.";
RL   J. Virol. 73:738-745(1999).
RN   [12]
RP   INTERACTION WITH HUMAN DLG1.
RX   PubMed=10557085; DOI=10.1038/sj.onc.1203008;
RA   Suzuki T., Ohsugi Y., Uchida-Toita M., Akiyama T., Yoshida M.;
RT   "Tax oncoprotein of HTLV-1 binds to the human homologue of Drosophila discs
RT   large tumor suppressor protein, hDLG, and perturbs its function in cell
RT   growth control.";
RL   Oncogene 18:5967-5972(1999).
RN   [13]
RP   INTERACTION WITH HUMAN PCAF.
RX   PubMed=10766811; DOI=10.1074/jbc.275.16.11852;
RA   Harrod R., Kuo Y.-L., Tang Y., Yao Y., Vassilev A., Nakatani Y.,
RA   Giam C.-Z.;
RT   "p300 and p300/cAMP-responsive element-binding protein associated factor
RT   interact with human T-cell lymphotropic virus type-1 Tax in a multi-histone
RT   acetyltransferase/activator-enhancer complex.";
RL   J. Biol. Chem. 275:11852-11857(2000).
RN   [14]
RP   INTERACTION WITH HUMAN IKBKG.
RX   PubMed=11064457; DOI=10.1038/sj.onc.1203894;
RA   Xiao G., Sun S.C.;
RT   "Activation of IKKalpha and IKKbeta through their fusion with HTLV-I tax
RT   protein.";
RL   Oncogene 19:5198-5203(2000).
RN   [15]
RP   INTERACTION WITH HOST CREBBP AND EP300.
RX   PubMed=11463834; DOI=10.1128/mcb.21.16.5520-5530.2001;
RA   Scoggin K.E.S., Ulloa A., Nyborg J.K.;
RT   "The oncoprotein Tax binds the SRC-1-interacting domain of CBP/p300 to
RT   mediate transcriptional activation.";
RL   Mol. Cell. Biol. 21:5520-5530(2001).
RN   [16]
RP   FUNCTION.
RX   PubMed=12052856; DOI=10.1128/mcb.22.13.4450-4462.2002;
RA   Lu H., Pise-Masison C.A., Fletcher T.M., Schiltz R.L., Nagaich A.K.,
RA   Radonovich M., Hager G., Cole P.A., Brady J.N.;
RT   "Acetylation of nucleosomal histones by p300 facilitates transcription from
RT   tax-responsive human T-cell leukemia virus type 1 chromatin template.";
RL   Mol. Cell. Biol. 22:4450-4462(2002).
RN   [17]
RP   NUCLEAR EXPORT SIGNAL, AND MUTAGENESIS OF LEU-200.
RX   PubMed=12670929; DOI=10.1074/jbc.m211576200;
RA   Alefantis T., Barmak K., Harhaj E.W., Grant C., Wigdahl B.;
RT   "Characterization of a nuclear export signal within the human T cell
RT   leukemia virus type I transactivator protein Tax.";
RL   J. Biol. Chem. 278:21814-21822(2003).
RN   [18]
RP   INTERACTION WITH HUMAN TAX1BP1.
RX   PubMed=14530271; DOI=10.1074/jbc.m310069200;
RA   Wu K., Bottazzi M.E., de la Fuente C., Deng L., Gitlin S.D., Maddukuri A.,
RA   Dadgar S., Li H., Vertes A., Pumfery A., Kashanchi F.;
RT   "Protein profile of tax-associated complexes.";
RL   J. Biol. Chem. 279:495-508(2004).
RN   [19]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15269214; DOI=10.1074/jbc.m400497200;
RA   Meertens L., Chevalier S., Weil R., Gessain A., Mahieux R.;
RT   "A 10-amino acid domain within human T-cell leukemia virus type 1 and type
RT   2 tax protein sequences is responsible for their divergent subcellular
RT   distribution.";
RL   J. Biol. Chem. 279:43307-43320(2004).
RN   [20]
RP   INTERACTION WITH HUMAN CRTC3, AND FUNCTION.
RX   PubMed=15466468; DOI=10.1074/jbc.m409021200;
RA   Koga H., Ohshima T., Shimotohno K.;
RT   "Enhanced activation of tax-dependent transcription of human T-cell
RT   leukemia virus type I (HTLV-I) long terminal repeat by TORC3.";
RL   J. Biol. Chem. 279:52978-52983(2004).
RN   [21]
RP   DOWN-REGULATION BY P30II.
RX   PubMed=14730358; DOI=10.1038/nm984;
RA   Nicot C., Dundr M., Johnson J.M., Fullen J.R., Alonzo N., Fukumoto R.,
RA   Princler G.L., Derse D., Misteli T., Franchini G.;
RT   "HTLV-1-encoded p30II is a post-transcriptional negative regulator of viral
RT   replication.";
RL   Nat. Med. 10:197-201(2004).
RN   [22]
RP   INTERACTION WITH HUMAN MAGI3.
RX   PubMed=15003862; DOI=10.1016/j.virol.2003.11.014;
RA   Ohashi M., Sakurai M., Higuchi M., Mori N., Fukushi M., Oie M.,
RA   Coffey R.J., Yoshiura K., Tanaka Y., Uchiyama M., Hatanaka M., Fujii M.;
RT   "Human T-cell leukemia virus type 1 Tax oncoprotein induces and interacts
RT   with a multi-PDZ domain protein, MAGI-3.";
RL   Virology 320:52-62(2004).
RN   [23]
RP   INTERACTION WITH HUMAN KDM4A.
RX   PubMed=15927959; DOI=10.1074/jbc.m413687200;
RA   Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H.,
RA   Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.;
RT   "Functional characterization of JMJD2A, a histone deacetylase- and
RT   retinoblastoma-binding protein.";
RL   J. Biol. Chem. 280:28507-28518(2005).
RN   [24]
RP   REVIEW.
RX   PubMed=16155604; DOI=10.1038/sj.onc.1208978;
RA   Grassmann R., Aboud M., Jeang K.T.;
RT   "Molecular mechanisms of cellular transformation by HTLV-1 Tax.";
RL   Oncogene 24:5976-5985(2005).
RN   [25]
RP   REVIEW.
RX   PubMed=16155601; DOI=10.1038/sj.onc.1208973;
RA   Kashanchi F., Brady J.N.;
RT   "Transcriptional and post-transcriptional gene regulation of HTLV-1.";
RL   Oncogene 24:5938-5951(2005).
RN   [26]
RP   DOMAIN PDZ-BINDING.
RX   PubMed=16042787; DOI=10.1186/1742-4690-2-46;
RA   Tsubata C., Higuchi M., Takahashi M., Oie M., Tanaka Y., Gejyo F.,
RA   Fujii M.;
RT   "PDZ domain-binding motif of human T-cell leukemia virus type 1 Tax
RT   oncoprotein is essential for the interleukin 2 independent growth induction
RT   of a T-cell line.";
RL   Retrovirology 2:46-46(2005).
RN   [27]
RP   INTERACTION WITH HUMAN CRTC1; CRTC2 AND CRTC3, AND FUNCTION.
RX   PubMed=16809310; DOI=10.1128/jvi.00103-06;
RA   Siu Y.-T., Chin K.-T., Siu K.-L., Yee Wai Choy E., Jeang K.-T., Jin D.-Y.;
RT   "TORC1 and TORC2 coactivators are required for tax activation of the human
RT   T-cell leukemia virus type 1 long terminal repeats.";
RL   J. Virol. 80:7052-7059(2006).
RN   [28]
RP   INTERACTION WITH HUMAN CARM1.
RX   PubMed=17005681; DOI=10.1128/jvi.00186-06;
RA   Jeong S.J., Lu H., Cho W.K., Park H.U., Pise-Masison C., Brady J.N.;
RT   "Coactivator-associated arginine methyltransferase 1 enhances
RT   transcriptional activity of the human T-cell lymphotropic virus type 1 long
RT   terminal repeat through direct interaction with Tax.";
RL   J. Virol. 80:10036-10044(2006).
RN   [29]
RP   PHOSPHORYLATION AT THR-48; THR-184; THR-215 AND SER-336, AND MUTAGENESIS OF
RP   THR-48; THR-184; THR-215; 300-SER-SER-301 AND SER-336.
RX   PubMed=16923801; DOI=10.1074/jbc.m607011200;
RA   Durkin S.S., Ward M.D., Fryrear K.A., Semmes O.J.;
RT   "Site-specific phosphorylation differentiates active from inactive forms of
RT   the HTLV-1 tax oncoprotein.";
RL   J. Biol. Chem. 281:31705-31712(2006).
RN   [30]
RP   INTERACTION WITH HUMAN SUV39H1.
RX   PubMed=16409643; DOI=10.1186/1742-4690-3-5;
RA   Kamoi K., Yamamoto K., Misawa A., Miyake A., Ishida T., Tanaka Y.,
RA   Mochizuki M., Watanabe T.;
RT   "SUV39H1 interacts with HTLV-1 Tax and abrogates Tax transactivation of
RT   HTLV-1 LTR.";
RL   Retrovirology 3:5-5(2006).
RN   [31]
RP   FUNCTION.
RX   PubMed=27082114; DOI=10.1371/journal.ppat.1005584;
RA   Wang C., Long W., Peng C., Hu L., Zhang Q., Wu A., Zhang X., Duan X.,
RA   Wong C.C., Tanaka Y., Xia Z.;
RT   "HTLV-1 Tax Functions as a Ubiquitin E3 Ligase for Direct IKK Activation
RT   via Synthesis of Mixed-Linkage Polyubiquitin Chains.";
RL   PLoS Pathog. 12:E1005584-E1005584(2016).
RN   [32]
RP   FUNCTION.
RX   PubMed=28103322; DOI=10.1371/journal.ppat.1006162;
RA   Shibata Y., Tokunaga F., Goto E., Komatsu G., Gohda J., Saeki Y.,
RA   Tanaka K., Takahashi H., Sawasaki T., Inoue S., Oshiumi H., Seya T.,
RA   Nakano H., Tanaka Y., Iwai K., Inoue J.I.;
RT   "HTLV-1 Tax Induces Formation of the Active Macromolecular IKK Complex by
RT   Generating Lys63- and Met1-Linked Hybrid Polyubiquitin Chains.";
RL   PLoS Pathog. 13:E1006162-E1006162(2017).
RN   [33]
RP   FUNCTION, AND INTERACTION WITH HOST OGT AND OGA.
RX   PubMed=28742148; DOI=10.1371/journal.ppat.1006518;
RA   Groussaud D., Khair M., Tollenaere A.I., Waast L., Kuo M.S., Mangeney M.,
RA   Martella C., Fardini Y., Coste S., Souidi M., Benit L., Pique C., Issad T.;
RT   "Hijacking of the O-GlcNAcZYME complex by the HTLV-1 Tax oncoprotein
RT   facilitates viral transcription.";
RL   PLoS Pathog. 13:E1006518-E1006518(2017).
RN   [34]
RP   FUNCTION, AND INTERACTION WITH HOST UPF1.
RX   PubMed=29382845; DOI=10.1038/s41467-017-02793-6;
RA   Fiorini F., Robin J.P., Kanaan J., Borowiak M., Croquette V., Le Hir H.,
RA   Jalinot P., Mocquet V.;
RT   "HTLV-1 Tax plugs and freezes UPF1 helicase leading to nonsense-mediated
RT   mRNA decay inhibition.";
RL   Nat. Commun. 9:431-431(2018).
RN   [35]
RP   MODIFICATION BY URMYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=29665857; DOI=10.1186/s12977-018-0415-4;
RA   Hleihel R., Khoshnood B., Dacklin I., Omran H., Mouawad C., Dassouki Z.,
RA   El-Sabban M., Shirinian M., Grabbe C., Bazarbachi A.;
RT   "The HTLV-1 oncoprotein Tax is modified by the ubiquitin related modifier 1
RT   (Urm1).";
RL   Retrovirology 15:33-33(2018).
CC   -!- FUNCTION: Transcriptional activator that governs the viral
CC       transcription from the 5'LTR via the recruitment of dimers of host
CC       phosphorylated CREB1. Together they bind cAMP response elements within
CC       the viral promoter and mediate high-level viral transcription
CC       (PubMed:8970957). Increases host CREB1 O-GlcNAcylation to further
CC       increase 5'LTR transactivation (PubMed:28742148). Modulates also the
CC       expression of cellular genes leading to the deregulation of T-cell
CC       proliferation, perturbing the integrity of cell cycle checkpoints, the
CC       DNA damage response and apopototic pathways. Acts as an ubiquitin E3
CC       ligase and stimulates host IKK complex by catalyzing the assembly of
CC       free mixed-linkage polyubiquitin chains, resulting in constitutive
CC       activation of the transcription factor NF-kappa-B (PubMed:28103322,
CC       PubMed:27082114). Inhibits the host nonsense-mediated mRNA decay (NMD),
CC       a cellular process that can actively degrade mRNAs by interacting with
CC       host UPF1 (PubMed:27082114). {ECO:0000269|PubMed:12052856,
CC       ECO:0000269|PubMed:15466468, ECO:0000269|PubMed:16809310,
CC       ECO:0000269|PubMed:27082114, ECO:0000269|PubMed:2768259,
CC       ECO:0000269|PubMed:28103322, ECO:0000269|PubMed:28742148,
CC       ECO:0000269|PubMed:29382845, ECO:0000269|PubMed:2990037,
CC       ECO:0000269|PubMed:8970957}.
CC   -!- SUBUNIT: Homodimer. Interacts with host CREB1 (PubMed:8970957).
CC       Interacts with host DLG1, IKBKG, KDM4A, MAGII3 and TAX1BP1. Recruits
CC       the coactivators CREBBP, EP300 and PCAF (PubMed:10766811). Interaction
CC       with human CARM1 enhances Tax transactivation and promotes methylation
CC       of histone H3 (PubMed:17005681). Interacts with host SUV39H1 protein,
CC       leading to abrogate Tax transactivation of HTLV-1 LTR
CC       (PubMed:16409643). Interaction with human CREB coactivators,
CC       CRTC1/TORC1, CRTC2/TORC2 and CRTC3/TORC3 enhances Tax transactivation
CC       (PubMed:15466468, PubMed:16809310). Interacts with host UPF1; this
CC       interaction inhibits the host nonsense-mediated mRNA decay (NMD).
CC       {ECO:0000269|PubMed:10557085, ECO:0000269|PubMed:10766811,
CC       ECO:0000269|PubMed:11064457, ECO:0000269|PubMed:11463834,
CC       ECO:0000269|PubMed:1386673, ECO:0000269|PubMed:14530271,
CC       ECO:0000269|PubMed:15003862, ECO:0000269|PubMed:15466468,
CC       ECO:0000269|PubMed:15927959, ECO:0000269|PubMed:16409643,
CC       ECO:0000269|PubMed:16809310, ECO:0000269|PubMed:17005681,
CC       ECO:0000269|PubMed:29382845, ECO:0000269|PubMed:8970957,
CC       ECO:0000269|PubMed:9016568, ECO:0000269|PubMed:9528808}.
CC   -!- INTERACTION:
CC       P03409; Q9UBN7: HDAC6; Xeno; NbExp=4; IntAct=EBI-5236464, EBI-301697;
CC       P03409; O14920: IKBKB; Xeno; NbExp=3; IntAct=EBI-5236464, EBI-81266;
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:15269214}. Host
CC       cytoplasm {ECO:0000269|PubMed:15269214, ECO:0000269|PubMed:29665857}.
CC       Note=Shuttles from the host nucleus to the cytoplasm. Found
CC       predominantly in the nucleus, where it is equally distributed between
CC       the nucleoplasm and the nuclear matrix.
CC   -!- INDUCTION: Down-regulated by P30II.
CC   -!- DOMAIN: The 48 N-terminal residues contain a non-canonical functional
CC       nuclear localization signal (NLS).
CC   -!- DOMAIN: The PDZ-binding domain mediates binding to human DLG1 and
CC       MAGI3. Interaction with other PDZ domain-containing protein induces
CC       IL2-independent growth.
CC   -!- PTM: Phosphorylation at Thr-48 results in the loss of NF-kappa-B
CC       activation function. Phosphorylation at Thr-215 results in loss of CREB
CC       and NF-B responsive promoters activation. Phosphorylation at Thr-184
CC       and Ser-336 have no effect on these Tax functions. Phosphorylation of
CC       either Ser-300 or Ser-301 is necessary for localization to nuclear
CC       bodies. Thr-48, Thr-184, Thr-215 and Ser-336 are highly phosphorylated,
CC       whereas Ser-300 or Ser-301 are only rarely phosphorylated.
CC       {ECO:0000269|PubMed:16923801, ECO:0000269|PubMed:9847380}.
CC   -!- PTM: Modified by host ubiquitin related modifier 1/URM1, resulting in a
CC       redistribution of Tax to the cytoplasm. {ECO:0000269|PubMed:29665857}.
CC   -!- MISCELLANEOUS: HTLV-1 lineages are divided in four clades, A
CC       (Cosmopolitan), B (Central African group), C (Melanesian group) and D
CC       (New Central African group).
CC   -!- SIMILARITY: Belongs to the deltaretrovirus Tax protein family.
CC       {ECO:0000305}.
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DR   EMBL; J02029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A93954; TNLJH1.
DR   ELM; P03409; -.
DR   IntAct; P03409; 4.
DR   MINT; P03409; -.
DR   BindingDB; P03409; -.
DR   iPTMnet; P03409; -.
DR   ABCD; P03409; 2 sequenced antibodies.
DR   Proteomes; UP000007683; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0039652; P:induction by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR   GO; GO:0039646; P:modulation by virus of host G0/G1 transition checkpoint; IEA:UniProtKB-KW.
DR   GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039593; P:suppression by virus of host exit from mitosis; IEA:UniProtKB-KW.
DR   InterPro; IPR004120; Tax.
DR   Pfam; PF02959; Tax; 1.
PE   1: Evidence at protein level;
KW   Activation of host NF-kappa-B by virus; Activator; DNA-binding;
KW   G0/G1 host cell cycle checkpoint dysregulation by virus;
KW   G1/S host cell cycle checkpoint dysregulation by virus; Host cytoplasm;
KW   Host nucleus; Host-virus interaction;
KW   Inhibition of host mitotic exit by virus; Metal-binding;
KW   Modulation of host cell cycle by virus; Oncogene; Phosphoprotein;
KW   Reference proteome; SH3-binding; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..353
FT                   /note="Protein Tax-1"
FT                   /id="PRO_0000085494"
FT   ZN_FING         23..49
FT                   /evidence="ECO:0000255"
FT   REGION          2..58
FT                   /note="Interaction with CREB1"
FT   REGION          81..95
FT                   /note="Interaction with CREBBP/P300"
FT   REGION          106..111
FT                   /note="Interaction with IKBKG"
FT   REGION          116..145
FT                   /note="Homodimerization"
FT   REGION          213..248
FT                   /note="Homodimerization"
FT   REGION          289..322
FT                   /note="Transactivation"
FT   REGION          312..319
FT                   /note="Interaction with CREBBP C-terminus"
FT   REGION          326..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           73..80
FT                   /note="SH3-binding"
FT                   /evidence="ECO:0000255"
FT   MOTIF           188..202
FT                   /note="Nuclear export signal"
FT   MOTIF           350..353
FT                   /note="PDZ-binding"
FT   MOD_RES         48
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000269|PubMed:16923801"
FT   MOD_RES         184
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000269|PubMed:16923801"
FT   MOD_RES         215
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000269|PubMed:16923801"
FT   MOD_RES         300
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000269|PubMed:9847380"
FT   MOD_RES         301
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000269|PubMed:9847380"
FT   MOD_RES         336
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000269|PubMed:16923801"
FT   MUTAGEN         48
FT                   /note="T->A: 30% loss of CREB activation. 70% loss of NF-
FT                   kappa-B activation."
FT                   /evidence="ECO:0000269|PubMed:16923801"
FT   MUTAGEN         48
FT                   /note="T->D: 50% loss of CREB activation. Almost complete
FT                   loss of NF-kappa-B activation."
FT                   /evidence="ECO:0000269|PubMed:16923801"
FT   MUTAGEN         184
FT                   /note="T->A: Slightly reduced CREB and NF-kappa-B
FT                   activation."
FT                   /evidence="ECO:0000269|PubMed:16923801"
FT   MUTAGEN         184
FT                   /note="T->D: Slightly reduced CREB and NF-kappa-B
FT                   activation."
FT                   /evidence="ECO:0000269|PubMed:16923801"
FT   MUTAGEN         200
FT                   /note="L->A: Complete loss of Tax-1 nuclear export."
FT                   /evidence="ECO:0000269|PubMed:12670929"
FT   MUTAGEN         215
FT                   /note="T->A: 30% loss of CREB activation. Slightly reduced
FT                   NF-kappa-B activation."
FT                   /evidence="ECO:0000269|PubMed:16923801"
FT   MUTAGEN         215
FT                   /note="T->D: Almost complete loss of CREB and NF-kappa-B
FT                   activation."
FT                   /evidence="ECO:0000269|PubMed:16923801"
FT   MUTAGEN         300..301
FT                   /note="SS->AA: Almost complete loss of CREB and NF-kappa-B
FT                   activation."
FT                   /evidence="ECO:0000269|PubMed:16923801"
FT   MUTAGEN         300..301
FT                   /note="SS->DD: 30% loss of CREB activation. 80% loss of NF-
FT                   kappa-B activation."
FT                   /evidence="ECO:0000269|PubMed:16923801"
FT   MUTAGEN         336
FT                   /note="S->A: Slightly reduced CREB and NF-kappa-B
FT                   activation."
FT                   /evidence="ECO:0000269|PubMed:16923801"
FT   MUTAGEN         336
FT                   /note="S->D: Slightly reduced CREB and NF-kappa-B
FT                   activation."
FT                   /evidence="ECO:0000269|PubMed:16923801"
SQ   SEQUENCE   353 AA;  39471 MW;  B3D2C05C26926D56 CRC64;
     MAHFPGFGQS LLFGYPVYVF GDCVQGDWCP ISGGLCSARL HRHALLATCP EHQITWDPID
     GRVIGSALQF LIPRLPSFPT QRTSKTLKVL TPPITHTTPN IPPSFLQAMR KYSPFRNGYM
     EPTLGQHLPT LSFPDPGLRP QNLYTLWGGS VVCMYLYQLS PPITWPLLPH VIFCHPGQLG
     AFLTNVPYKR IEELLYKISL TTGALIILPE DCLPTTLFQP ARAPVTLTAW QNGLLPFHST
     LTTPGLIWTF TDGTPMISGP CPKDGQPSLV LQSSSFIFHK FQTKAYHPSF LLSHGLIQYS
     SFHSLHLLFE EYTNIPISLL FNEKEADDND HEPQISPGGL EPPSEKHFRE TEV
 
 
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