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TOX3_MOUSE
ID   TOX3_MOUSE              Reviewed;         575 AA.
AC   Q80W03; Q8BIV8;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=TOX high mobility group box family member 3;
DE   AltName: Full=Trinucleotide repeat-containing gene 9 protein;
GN   Name=Tox3; Synonyms=Tnrc9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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: Transcriptional coactivator of the p300/CBP-mediated
CC       transcription complex. Activates transactivation through cAMP response
CC       element (CRE) sites. Protects against cell death by inducing
CC       antiapoptotic and repressing pro-apoptotic transcripts. Stimulates
CC       transcription from the estrogen-responsive or BCL-2 promoters. Required
CC       for depolarization-induced transcription activation of the C-FOS
CC       promoter in neurons. Associates with chromatin to the estrogen-
CC       responsive C3 promoter region (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts (via HGM box) with CITED1 (via C-
CC       terminus); the interaction increases estrogen-response element (ERE)-
CC       dependent transcription and protection against cell death. Interacts
CC       with CREB1 (phosphorylated form). Interacts with CREB1; the interaction
CC       is not depolarization dependent. Interacts with CREBBP (via C-terminus)
CC       (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q80W03; Q8VHS6: Asb15; NbExp=2; IntAct=EBI-26675915, EBI-26675998;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DOMAIN: the C-terminus is required for calcium responsiveness but not
CC       for transactivation activity. {ECO:0000250}.
CC   -!- DOMAIN: The N-terminus is absolutely necessary for transactivation
CC       activity. {ECO:0000250}.
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DR   EMBL; AK082602; BAC38545.1; -; mRNA.
DR   EMBL; BC052044; AAH52044.1; -; mRNA.
DR   CCDS; CCDS22516.1; -.
DR   RefSeq; NP_766501.2; NM_172913.3.
DR   AlphaFoldDB; Q80W03; -.
DR   SMR; Q80W03; -.
DR   BioGRID; 232663; 9.
DR   IntAct; Q80W03; 8.
DR   STRING; 10090.ENSMUSP00000105250; -.
DR   iPTMnet; Q80W03; -.
DR   PhosphoSitePlus; Q80W03; -.
DR   MaxQB; Q80W03; -.
DR   PaxDb; Q80W03; -.
DR   PRIDE; Q80W03; -.
DR   ProteomicsDB; 258954; -.
DR   Antibodypedia; 28333; 345 antibodies from 24 providers.
DR   DNASU; 244579; -.
DR   Ensembl; ENSMUST00000109621; ENSMUSP00000105250; ENSMUSG00000043668.
DR   GeneID; 244579; -.
DR   KEGG; mmu:244579; -.
DR   UCSC; uc009msb.2; mouse.
DR   CTD; 27324; -.
DR   MGI; MGI:3039593; Tox3.
DR   VEuPathDB; HostDB:ENSMUSG00000043668; -.
DR   eggNOG; KOG0381; Eukaryota.
DR   GeneTree; ENSGT00940000158043; -.
DR   HOGENOM; CLU_030650_1_0_1; -.
DR   InParanoid; Q80W03; -.
DR   OMA; QQHHMQL; -.
DR   OrthoDB; 1465513at2759; -.
DR   PhylomeDB; Q80W03; -.
DR   TreeFam; TF106481; -.
DR   BioGRID-ORCS; 244579; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; Tox3; mouse.
DR   PRO; PR:Q80W03; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q80W03; protein.
DR   Bgee; ENSMUSG00000043668; Expressed in rostral migratory stream and 200 other tissues.
DR   ExpressionAtlas; Q80W03; baseline and differential.
DR   Genevisible; Q80W03; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR   GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.30.10; -; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Apoptosis; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..575
FT                   /note="TOX high mobility group box family member 3"
FT                   /id="PRO_0000286354"
FT   DNA_BIND        254..322
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          189..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        10
FT                   /note="A -> G (in Ref. 1; BAC38545)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        14
FT                   /note="A -> S (in Ref. 1; BAC38545)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   575 AA;  63174 MW;  E1B95AD9F3BCFC91 CRC64;
     MDVRFYPAAA GDPAGLDFAQ CLGYYGYSKL GNNNYMNMAE ANNAFFAASE QTFHTPSLGD
     EEFEIPPITP PPESDPTLGM PDALLPFQTL SDPLPSQGTE FTPQFPPQSL DLPSITISRN
     LVEQDGVLHS NGLHMDQSHT QVSQYRQDPS LVMRSIVHMT DGARSGIMPP AQLTTINQSQ
     LSAQLGLNLG GANVSHTSPS PPASKSATPS PSSSINEEDA DDANRAIGEK RTAPDSGKKP
     KTPKKKKKKD PNEPQKPVSA YALFFRDTQA AIKGQNPNAT FGEVSKIVAS MWDSLGEEQK
     QVYKRKTEAA KKEYLKALAA YRASLVSKAA AESAEAQTIR SVQQTLASTN LTSSLLLNTS
     LSQHGTVPAS PQTLPQSLPR SIAPKPLTMR LPMSQIVTSV TIAANMPSNI GAPLISSMGT
     TMVGSATSTQ VSPSVQTQQH QMQLQQQQQQ QQQMQQMQQQ QLQQHQMHQQ IQQQMQQQHF
     QHHMQQHLQQ QQQQHLQQQL SQQQLQQQLQ QHLQLQQLQH MQHQSQPSPR QHSPVTSQIT
     SPIPAIGSPQ PASQQHQPQI QSQTQTQVLP QVSIF
 
 
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