ID UXT_HUMAN Reviewed; 157 AA. AC Q9UBK9; A0A0C4DFR8; B2R561; Q5JZG3; Q9Y6E5; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 182. DE RecName: Full=Protein UXT; DE AltName: Full=Androgen receptor trapped clone 27 protein {ECO:0000303|PubMed:11854421}; DE Short=ART-27 {ECO:0000303|PubMed:11854421}; DE AltName: Full=Ubiquitously expressed transcript protein; GN Name=UXT; ORFNames=HSPC024; 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] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY. 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 [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND INTERACTION WITH AR. RX PubMed=11854421; DOI=10.1091/mbc.01-10-0513; RA Markus S.M., Taneja S.S., Logan S.K., Li W., Ha S., Hittelman A.B., RA Rogatsky I., Garabedian M.J.; RT "Identification and characterization of ART-27, a novel coactivator for the RT androgen receptor N terminus."; RL Mol. Biol. Cell 13:670-682(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, AND RP INTERACTION WITH MECOM. RX PubMed=17635584; DOI=10.1111/j.1742-4658.2007.05928.x; RA McGilvray R., Walker M., Bartholomew C.; RT "UXT interacts with the transcriptional repressor protein EVI1 and RT suppresses cell transformation."; RL FEBS J. 274:3960-3971(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION (ISOFORMS 1 AND 2), RP IDENTIFICATION IN COMPLEX I, INTERACTION WITH TRAF2, SUBCELLULAR LOCATION, RP AND IDENTIFICATION OF ISOFORM 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). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Mammary gland; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [8] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; 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 [10] RP FUNCTION, INTERACTION WITH LRPPRC, AND TISSUE SPECIFICITY. RX PubMed=11827465; DOI=10.1006/geno.2001.6679; RA Liu L., McKeehan W.L.; RT "Sequence analysis of LRPPRC and its SEC1 domain interaction partners RT suggests roles in cytoskeletal organization, vesicular trafficking, RT nucleocytosolic shuttling, and chromosome activity."; RL Genomics 79:124-136(2002). RN [11] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP MUTAGENESIS OF LEU-50 AND LEU-59. RX PubMed=16221885; DOI=10.1091/mbc.e05-08-0705; RA Zhao H., Wang Q., Zhang H., Liu Q., Du X., Richter M., Greene M.I.; RT "UXT is a novel centrosomal protein essential for cell viability."; RL Mol. Biol. Cell 16:5857-5865(2005). RN [12] RP FUNCTION, AND INTERACTION WITH LRPPRC. RX PubMed=17554592; DOI=10.1007/s11626-007-9016-6; RA Moss T.N., Vo A., McKeehan W.L., Liu L.; RT "UXT (Ubiquitously Expressed Transcript) causes mitochondrial RT aggregation."; RL In Vitro Cell. Dev. Biol. Anim. 43:139-146(2007). RN [13] RP FUNCTION, INTERACTION WITH RELA, AND SUBCELLULAR LOCATION. RX PubMed=17620405; DOI=10.1083/jcb.200611081; RA Sun S., Tang Y., Lou X., Zhu L., Yang K., Zhang B., Shi H., Wang C.; RT "UXT is a novel and essential cofactor in the NF-kappaB transcriptional RT enhanceosome."; RL J. Cell Biol. 178:231-244(2007). RN [14] 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 [15] RP FUNCTION, INTERACTION WITH URI1, AND TISSUE SPECIFICITY. RX PubMed=21730289; DOI=10.1128/mcb.05429-11; RA Mita P., Savas J.N., Djouder N., Yates J.R. III, Ha S., Ruoff R., RA Schafler E.D., Nwachukwu J.C., Tanese N., Cowan N.J., Zavadil J., RA Garabedian M.J., Logan S.K.; RT "Regulation of androgen receptor-mediated transcription by RPB5 binding RT protein URI/RMP."; RL Mol. Cell. Biol. 31:3639-3652(2011). RN [16] RP FUNCTION, INTERACTION WITH ESR1, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=28106301; DOI=10.1002/jcb.25893; RA Sanchez-Morgan N., Kirsch K.H., Trackman P.C., Sonenshein G.E.; RT "UXT is a LOX-PP interacting protein that modulates estrogen receptor alpha RT activity in breast cancer Cells."; RL J. Cell. Biochem. 118:2347-2356(2017). RN [17] RP IDENTIFICATION IN THE PAQOSOME COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=31738558; DOI=10.1021/acs.jproteome.9b00599; RA Cloutier P., Poitras C., Faubert D., Bouchard A., Blanchette M., RA Gauthier M.S., Coulombe B.; RT "Upstream ORF-Encoded ASDURF Is a Novel Prefoldin-like Subunit of the RT PAQosome."; RL J. Proteome Res. 19:18-27(2020). RN [18] RP UBIQUITINATION (ISOFORM 2), AND SUBCELLULAR LOCATION (ISOFORM 2). RX PubMed=33010352; DOI=10.1016/j.bbagen.2020.129754; RA Spagnol V., Oliveira C.A.B., Randle S.J., Passos P.M.S., RA Correia C.R.S.T.B., Simaroli N.B., Oliveira J.S., Mevissen T.E.T., RA Medeiros A.C., Gomes M.D., Komander D., Laman H., Teixeira F.R.; RT "The E3 ubiquitin ligase SCF(Fbxo7) mediates proteasomal degradation of UXT RT isoform 2 (UXT-V2) to inhibit the NF-kappaB signaling pathway."; RL Biochim. Biophys. Acta 1865:129754-129754(2021). CC -!- FUNCTION: Involved in gene transcription regulation (PubMed:28106301, CC PubMed:21730289). Acts in concert with the corepressor URI1 to regulate CC androgen receptor AR-mediated transcription (PubMed:11854421, CC PubMed:21730289). Together with URI1, associates with chromatin to the CC NKX3-1 promoter region (PubMed:21730289). Negatively regulates the CC transcriptional activity of the estrogen receptor ESR1 by inducing its CC translocation into the cytoplasm (PubMed:28106301). May act as nuclear CC chaperone that facilitates the formation of the NF-kappa-B enhanceosome CC and thus positively regulates NF-kappa-B transcription activity CC (PubMed:17620405, PubMed:21307340). Potential component of CC mitochondrial-associated LRPPRC, a multidomain organizer that CC potentially integrates mitochondria and the microtubular cytoskeleton CC with chromosome remodeling (PubMed:17554592). Increasing concentrations CC of UXT contributes to progressive aggregation of mitochondria and cell CC death potentially through its association with LRPPRC CC (PubMed:17554592). Suppresses cell transformation and it might mediate CC this function by interaction and inhibition of the biological activity CC of cell proliferation and survival stimulatory factors like MECOM CC (PubMed:17635584). {ECO:0000269|PubMed:11827465, CC ECO:0000269|PubMed:11854421, ECO:0000269|PubMed:16221885, CC ECO:0000269|PubMed:17554592, ECO:0000269|PubMed:17620405, CC ECO:0000269|PubMed:17635584, ECO:0000269|PubMed:21307340, CC ECO:0000269|PubMed:21730289, ECO:0000269|PubMed:28106301}. 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 (PubMed:16221885). Component of the PAQosome CC complex which is responsible for the biogenesis of several protein CC complexes and which consists of R2TP complex members RUVBL1, RUVBL2, CC RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT and URI1 CC as well as ASDURF, POLR2E and DNAAF10/WDR92 (PubMed:31738558). CC Interacts with LRPPRC (PubMed:11827465, PubMed:17554592). Interacts CC with androgen receptor AR (via N-terminus) (PubMed:11854421). Interacts CC with estrogen receptor ESR1; the interaction relocalizes ESR1 from the CC nucleus to the cytoplasm (PubMed:28106301). In the nucleus, interacts CC specifically with RELA (via RHD domain) and forms a dynamic complex CC with NF-kappa-B and is recruited to the NF-kappa-B enhanceosome upon CC stimulation (PubMed:17620405). Interacts with MECOM (PubMed:17635584). CC Interacts with URI1 (PubMed:21730289). {ECO:0000269|PubMed:11827465, CC ECO:0000269|PubMed:11854421, ECO:0000269|PubMed:16221885, CC ECO:0000269|PubMed:17554592, ECO:0000269|PubMed:17620405, CC ECO:0000269|PubMed:17635584, ECO:0000269|PubMed:21730289, CC ECO:0000269|PubMed:28106301, ECO:0000269|PubMed:31738558}. CC -!- SUBUNIT: [Isoform 1]: Part of complex I composed of TNF-alpha receptor CC TNFRSF1A, TRADD, TRAF2 and RIPK1 formed in response to TNF-alpha CC stimulation. Within the complex, interacts (via TPQE motif) with TRAF2; CC the interaction prevents the recruitment of FADD and CASP8/caspase 8 to CC complex I. {ECO:0000269|PubMed:21307340}. CC -!- INTERACTION: CC Q9UBK9; P63172: DYNLT1; NbExp=3; IntAct=EBI-357355, EBI-1176455; CC Q9UBK9; P03372: ESR1; NbExp=2; IntAct=EBI-357355, EBI-78473; CC Q9UBK9; Q15323: KRT31; NbExp=6; IntAct=EBI-357355, EBI-948001; CC Q9UBK9; Q6A162: KRT40; NbExp=3; IntAct=EBI-357355, EBI-10171697; CC Q9UBK9; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-357355, EBI-11749135; CC Q9UBK9; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-357355, EBI-10172290; CC Q9UBK9; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-357355, EBI-10171774; CC Q9UBK9; P60328: KRTAP12-3; NbExp=4; IntAct=EBI-357355, EBI-11953334; CC Q9UBK9; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-357355, EBI-11987425; CC Q9UBK9; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-357355, EBI-3958099; CC Q9UBK9; Q03112: MECOM; NbExp=5; IntAct=EBI-357355, EBI-1384862; CC Q9UBK9; Q00013: MPP1; NbExp=3; IntAct=EBI-357355, EBI-711788; CC Q9UBK9; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-357355, EBI-945833; CC Q9UBK9; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-357355, EBI-22310682; CC Q9UBK9; Q9P286: PAK5; NbExp=4; IntAct=EBI-357355, EBI-741896; CC Q9UBK9; Q9UHV9: PFDN2; NbExp=2; IntAct=EBI-357355, EBI-359873; CC Q9UBK9; Q04206: RELA; NbExp=5; IntAct=EBI-357355, EBI-73886; CC Q9UBK9; Q9H6T3: RPAP3; NbExp=2; IntAct=EBI-357355, EBI-356928; CC Q9UBK9; Q0D2N8: SARM1; NbExp=2; IntAct=EBI-357355, EBI-8716526; CC Q9UBK9; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-357355, EBI-747107; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm CC {ECO:0000269|PubMed:21307340}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus CC {ECO:0000269|PubMed:33010352}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21307340, CC ECO:0000305|PubMed:28106301}. Nucleus {ECO:0000269|PubMed:11854421, CC ECO:0000269|PubMed:17620405, ECO:0000269|PubMed:21307340, CC ECO:0000305|PubMed:28106301}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:16221885}. Cytoplasm, CC cytoskeleton, spindle pole {ECO:0000269|PubMed:16221885}. CC Note=Predominantly localizes to the nucleus (PubMed:16221885). CC Localizes to spindle pole during mitosis (PubMed:16221885). CC {ECO:0000269|PubMed:16221885, ECO:0000269|PubMed:21307340}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=2; Synonyms=UXT-V2 {ECO:0000303|PubMed:21307340}; CC IsoId=Q9UBK9-1; Sequence=Displayed; CC Name=1; Synonyms=UXT-V1 {ECO:0000303|PubMed:21307340}; CC IsoId=Q9UBK9-2; Sequence=VSP_059081; CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:10087202, PubMed:11854421, CC PubMed:17635584, PubMed:11827465). Expressed in prostate epithelial CC cells (PubMed:21730289). Expressed in mammary epithelial cells CC (PubMed:28106301). Highest levels in the heart, skeletal muscle, CC pancreas, kidney, liver, adrenal gland, peripheral blood leukocytes, CC lymph node, prostate, and thyroid and the lowest levels in bladder and CC uterus (PubMed:11854421, PubMed:17635584, PubMed:11827465). CC Overexpressed in a number of tumor tissues (PubMed:11854421, CC PubMed:16221885, PubMed:28106301). {ECO:0000269|PubMed:10087202, CC ECO:0000269|PubMed:11827465, ECO:0000269|PubMed:11854421, CC ECO:0000269|PubMed:16221885, ECO:0000269|PubMed:17635584, CC ECO:0000269|PubMed:21730289, ECO:0000269|PubMed:28106301}. CC -!- PTM: [Isoform 2]: Ubiquitinated by E3 ubiquitin-protein ligase complex CC containing FBXO7; leading to proteasomal degradation. CC {ECO:0000269|PubMed:33010352}. CC -!- SIMILARITY: Belongs to the UXT family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF092737; AAD28698.1; -; mRNA. DR EMBL; AF083241; AAD39839.1; -; mRNA. DR EMBL; AF083242; AAD39840.1; -; mRNA. DR EMBL; AK312072; BAG35008.1; -; mRNA. DR EMBL; AL009172; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471164; EAW59325.1; -; Genomic_DNA. DR EMBL; CH471164; EAW59326.1; -; Genomic_DNA. DR EMBL; BC000720; AAH00720.1; -; mRNA. DR EMBL; BC008890; AAH08890.1; -; mRNA. DR CCDS; CCDS14284.1; -. [Q9UBK9-2] DR CCDS; CCDS14285.1; -. [Q9UBK9-1] DR RefSeq; NP_004173.1; NM_004182.3. [Q9UBK9-1] DR RefSeq; NP_705582.1; NM_153477.2. [Q9UBK9-2] DR AlphaFoldDB; Q9UBK9; -. DR SMR; Q9UBK9; -. DR BioGRID; 113997; 127. DR ComplexPortal; CPX-6144; URI1 prefoldin co-chaperone complex. DR IntAct; Q9UBK9; 84. DR MINT; Q9UBK9; -. DR STRING; 9606.ENSP00000337393; -. DR iPTMnet; Q9UBK9; -. DR PhosphoSitePlus; Q9UBK9; -. DR BioMuta; UXT; -. DR DMDM; 8928445; -. DR EPD; Q9UBK9; -. DR jPOST; Q9UBK9; -. DR MassIVE; Q9UBK9; -. DR MaxQB; Q9UBK9; -. DR PaxDb; 9606-ENSP00000337393; -. DR PeptideAtlas; Q9UBK9; -. DR ProteomicsDB; 83987; -. DR Pumba; Q9UBK9; -. DR Antibodypedia; 25507; 257 antibodies from 29 providers. DR DNASU; 8409; -. DR Ensembl; ENST00000333119.8; ENSP00000327797.3; ENSG00000126756.12. [Q9UBK9-1] DR Ensembl; ENST00000335890.3; ENSP00000337393.2; ENSG00000126756.12. [Q9UBK9-2] DR GeneID; 8409; -. DR KEGG; hsa:8409; -. DR MANE-Select; ENST00000333119.8; ENSP00000327797.3; NM_004182.4; NP_004173.1. DR UCSC; uc004dim.4; human. [Q9UBK9-1] DR AGR; HGNC:12641; -. DR CTD; 8409; -. DR DisGeNET; 8409; -. DR GeneCards; UXT; -. DR HGNC; HGNC:12641; UXT. DR HPA; ENSG00000126756; Low tissue specificity. DR MIM; 300234; gene. DR neXtProt; NX_Q9UBK9; -. DR OpenTargets; ENSG00000126756; -. DR PharmGKB; PA37265; -. DR VEuPathDB; HostDB:ENSG00000126756; -. DR eggNOG; KOG3047; Eukaryota. DR GeneTree; ENSGT00390000018078; -. DR HOGENOM; CLU_121199_1_0_1; -. DR InParanoid; Q9UBK9; -. DR OMA; IPQEPIM; -. DR OrthoDB; 73521at2759; -. DR PhylomeDB; Q9UBK9; -. DR TreeFam; TF323827; -. DR PathwayCommons; Q9UBK9; -. DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6. DR SignaLink; Q9UBK9; -. DR SIGNOR; Q9UBK9; -. DR BioGRID-ORCS; 8409; 418 hits in 803 CRISPR screens. DR ChiTaRS; UXT; human. DR GeneWiki; UXT; -. DR GenomeRNAi; 8409; -. DR Pharos; Q9UBK9; Tbio. DR PRO; PR:Q9UBK9; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q9UBK9; Protein. DR Bgee; ENSG00000126756; Expressed in left ovary and 203 other cell types or tissues. DR ExpressionAtlas; Q9UBK9; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:HGNC-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IDA:HGNC-UCL. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0101031; C:protein folding chaperone complex; NAS:ComplexPortal. DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; IPI:ComplexPortal. DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell. DR GO; GO:0048487; F:beta-tubulin binding; IDA:HGNC-UCL. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0008017; F:microtubule binding; TAS:HGNC-UCL. DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0007098; P:centrosome cycle; IMP:HGNC-UCL. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:HGNC-UCL. DR GO; GO:0047497; P:mitochondrion transport along microtubule; TAS:HGNC-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0050821; P:protein stabilization; NAS:ComplexPortal. DR CDD; cd00584; Prefoldin_alpha; 1. DR Gene3D; 1.10.287.370; -; 1. DR InterPro; IPR009053; Prefoldin. DR InterPro; IPR004127; Prefoldin_subunit_alpha. DR InterPro; IPR003994; UXT. DR PANTHER; PTHR13345; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 10; 1. DR PANTHER; PTHR13345:SF12; PROTEIN UXT; 1. DR Pfam; PF02996; Prefoldin; 1. DR PRINTS; PR01502; UXTPROTEIN. DR SUPFAM; SSF46579; Prefoldin; 1. DR Genevisible; Q9UBK9; HS. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Apoptosis; Chaperone; Cytoplasm; KW Cytoskeleton; Nucleus; Reference proteome; Repressor; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..157 FT /note="Protein UXT" FT /id="PRO_0000065751" FT VAR_SEQ 1 FT /note="M -> MVFPLPTPQEPIM (in isoform 1)" FT /evidence="ECO:0000305" FT /id="VSP_059081" FT MUTAGEN 50 FT /note="L->P: Causes dislocation from the centrosome; when FT associated with L-59." FT /evidence="ECO:0000269|PubMed:16221885" FT MUTAGEN 59 FT /note="L->P: Causes dislocation from the centrosome; when FT associated with L-50." FT /evidence="ECO:0000269|PubMed:16221885" SQ SEQUENCE 157 AA; 18246 MW; 94CE14C462DEE308 CRC64; MATPPKRRAV EATGEKVLRY ETFISDVLQR DLRKVLDHRD KVYEQLAKYL QLRNVIERLQ EAKHSELYMQ VDLGCNFFVD TVVPDTSRIY VALGYGFFLE LTLAEALKFI DRKSSLLTEL SNSLTKDSMN IKAHIHMLLE GLRELQGLQN FPEKPHH //