UXT_MOUSE
ID UXT_MOUSE Reviewed; 157 AA.
AC Q9WTZ0; Q8CEJ2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein UXT;
DE AltName: Full=Ubiquitously expressed transcript protein;
GN Name=Uxt;
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 [MRNA] (ISOFORM 2).
RX PubMed=10087202; DOI=10.1006/geno.1998.5712;
RA Schroer A., Schneider S., Ropers H.-H., Nothwang H.G.;
RT "Cloning and characterization of UXT, a novel gene in human Xp11, which is
RT widely and abundantly expressed in tumor tissue.";
RL Genomics 56:340-343(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC25665.1};
RC TISSUE=Spleen {ECO:0000312|EMBL:BAC25665.1};
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Jaw {ECO:0000312|EMBL:AAH82294.1}, and
RC Limb {ECO:0000312|EMBL:AAH82294.1};
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION (ISOFORMS 1 AND 2), IDENTIFICATION IN APOPTOTIC COMPLEX I,
RP INTERACTION WITH TRAF2, SUBCELLULAR LOCATION, AND IDENTIFICATION OF ISOFORM
RP 1.
RX PubMed=21307340; DOI=10.1091/mbc.e10-10-0827;
RA Huang Y., Chen L., Zhou Y., Liu H., Yang J., Liu Z., Wang C.;
RT "UXT-V1 protects cells against TNF-induced apoptosis through modulating
RT complex II formation.";
RL Mol. Biol. Cell 22:1389-1397(2011).
CC -!- FUNCTION: Involved in gene transcription regulation. Acts in concert
CC with the corepressor URI1 to regulate androgen receptor AR-mediated
CC transcription. Together with URI1, associates with chromatin to the
CC NKX3-1 promoter region. Negatively regulates the transcriptional
CC activity of the estrogen receptor ESR1 by inducing its translocation
CC into the cytoplasm. May act as nuclear chaperone that facilitates the
CC formation of the NF-kappa-B enhanceosome and thus positively regulates
CC NF-kappa-B transcription activity. Potential component of
CC mitochondrial-associated LRPPRC, a multidomain organizer that
CC potentially integrates mitochondria and the microtubular cytoskeleton
CC with chromosome remodeling. Increasing concentrations of UXT
CC contributes to progressive aggregation of mitochondria and cell death
CC potentially through its association with LRPPRC. Suppresses cell
CC transformation and it might mediate this function by interaction and
CC inhibition of the biological activity of cell proliferation and
CC survival stimulatory factors like MECOM.
CC {ECO:0000250|UniProtKB:Q9UBK9}.
CC -!- FUNCTION: [Isoform 1]: Plays a role in protecting cells against TNF-
CC alpha-induced apoptosis by preventing the recruitment of FADD and
CC caspase 8 to the apoptotic complex I, composed of TRADD, TRAF2 and
CC RIPK1/RIP. {ECO:0000269|PubMed:21307340}.
CC -!- SUBUNIT: Homohexamer (By similarity). Component of the PAQosome complex
CC which is responsible for the biogenesis of several protein complexes
CC and which consists of R2TP complex members RUVBL1, RUVBL2, RPAP3 and
CC PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT and URI1 as well
CC as ASDURF, POLR2E and DNAAF10/WDR92 (By similarity). Interacts with
CC LRPPRC (By similarity). Interacts with androgen receptor AR (via N-
CC terminus) (By similarity). Interacts with estrogen receptor ESR1; the
CC interaction relocalizes ESR1 to the cytoplasm (By similarity). In the
CC nucleus, interacts specifically with RELA (via RHD domain) and forms a
CC dynamic complex with NF-kappa-B and is recruited to the NF-kappa-B
CC enhanceosome upon stimulation (By similarity). Interacts with MECOM (By
CC similarity). Interacts with URI1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UBK9, ECO:0000269|PubMed:21307340}.
CC -!- SUBUNIT: [Isoform 1]: Part of complex I composed of TNF-alpha receptor,
CC TRADD, TRAF2 and RIPK1 (By similarity). Within the complex, interacts
CC (via TPQE motif) with TRAF2; the interaction prevents the recruitment
CC of FADD and CASP8/caspase 8 to complex I (PubMed:21307340).
CC {ECO:0000250|UniProtKB:Q9UBK9, ECO:0000269|PubMed:21307340}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000250|UniProtKB:Q9UBK9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UBK9}. Nucleus
CC {ECO:0000250|UniProtKB:Q9UBK9}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q9UBK9}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9UBK9}.
CC Note=Predominantly localizes to the nucleus. Localizes to spindle pole
CC during mitosis. {ECO:0000250|UniProtKB:Q9UBK9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=UXT-V2 {ECO:0000303|PubMed:21307340};
CC IsoId=Q9WTZ0-1; Sequence=Displayed;
CC Name=1; Synonyms=UXT-V1 {ECO:0000303|PubMed:21307340};
CC IsoId=Q9WTZ0-2; Sequence=Not described;
CC -!- MISCELLANEOUS: [Isoform 1]: No initiation Met is found in the EST
CC sequence upstream the Met for isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the UXT family. {ECO:0000305}.
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DR EMBL; AF092738; AAD28699.1; -; mRNA.
DR EMBL; AK027917; BAC25665.1; -; mRNA.
DR EMBL; AK163983; BAE37569.1; -; mRNA.
DR EMBL; AL671853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466625; EDL00731.1; -; Genomic_DNA.
DR EMBL; BC082294; AAH82294.1; -; mRNA.
DR CCDS; CCDS30049.1; -. [Q9WTZ0-1]
DR RefSeq; NP_038868.2; NM_013840.3. [Q9WTZ0-1]
DR AlphaFoldDB; Q9WTZ0; -.
DR SMR; Q9WTZ0; -.
DR IntAct; Q9WTZ0; 2.
DR MINT; Q9WTZ0; -.
DR STRING; 10090.ENSMUSP00000115342; -.
DR iPTMnet; Q9WTZ0; -.
DR PhosphoSitePlus; Q9WTZ0; -.
DR EPD; Q9WTZ0; -.
DR MaxQB; Q9WTZ0; -.
DR PaxDb; Q9WTZ0; -.
DR PeptideAtlas; Q9WTZ0; -.
DR PRIDE; Q9WTZ0; -.
DR ProteomicsDB; 298260; -. [Q9WTZ0-1]
DR Antibodypedia; 25507; 240 antibodies from 29 providers.
DR DNASU; 22294; -.
DR Ensembl; ENSMUST00000123836; ENSMUSP00000115342; ENSMUSG00000001134. [Q9WTZ0-1]
DR GeneID; 22294; -.
DR KEGG; mmu:22294; -.
DR UCSC; uc009sue.1; mouse.
DR UCSC; uc009suf.1; mouse. [Q9WTZ0-1]
DR CTD; 8409; -.
DR MGI; MGI:1277988; Uxt.
DR VEuPathDB; HostDB:ENSMUSG00000001134; -.
DR eggNOG; KOG3047; Eukaryota.
DR GeneTree; ENSGT00390000018078; -.
DR InParanoid; Q9WTZ0; -.
DR OMA; NIFMQAR; -.
DR OrthoDB; 1559312at2759; -.
DR PhylomeDB; Q9WTZ0; -.
DR TreeFam; TF323827; -.
DR BioGRID-ORCS; 22294; 25 hits in 72 CRISPR screens.
DR ChiTaRS; Uxt; mouse.
DR PRO; PR:Q9WTZ0; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9WTZ0; protein.
DR Bgee; ENSMUSG00000001134; Expressed in quadriceps femoris and 69 other tissues.
DR GO; GO:0005813; C:centrosome; ISS:HGNC-UCL.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:HGNC-UCL.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:HGNC-UCL.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; ISS:HGNC-UCL.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:HGNC-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR009053; Prefoldin.
DR InterPro; IPR004127; Prefoldin_subunit_alpha.
DR InterPro; IPR003994; UXT.
DR Pfam; PF02996; Prefoldin; 1.
DR PRINTS; PR01502; UXTPROTEIN.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Apoptosis; Chaperone; Cytoplasm;
KW Cytoskeleton; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..157
FT /note="Protein UXT"
FT /id="PRO_0000065752"
FT CONFLICT 156
FT /note="P -> T (in Ref. 1; AAD28699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 157 AA; 18187 MW; FDBE1EF32730BA87 CRC64;
MATPPKRRAL DTVGEKVLRY ETFISDVLQR DLQKVLDHRD KVYEQLSVYL QLRNVIERLQ
ETNHSELYMQ VDLGCNFFVD TVVPDTSRIY VALGYGFFLE LTLAEALKFI DRKSSLLTEL
SDSLTKDSMN IKAHIHMMLE GLRELQGLQN FPEPSPH
