UXT_HUMAN
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 03-AUG-2022, entry version 174.
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).
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: 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 -!- SIMILARITY: Belongs to the UXT family. {ECO:0000305}.
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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; 123.
DR ComplexPortal; CPX-6144; URI1 prefoldin co-chaperone complex.
DR IntAct; Q9UBK9; 83.
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; Q9UBK9; -.
DR PeptideAtlas; Q9UBK9; -.
DR PRIDE; Q9UBK9; -.
DR ProteomicsDB; 83987; -.
DR Antibodypedia; 25507; 240 antibodies from 29 providers.
DR DNASU; 8409; -.
DR Ensembl; ENST00000333119.7; 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; ENST00000335890.3; ENSP00000337393.2; NM_153477.3; NP_705582.1. [Q9UBK9-2]
DR UCSC; uc004dim.4; human. [Q9UBK9-1]
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; NIFMQAR; -.
DR OrthoDB; 1559312at2759; -.
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; 383 hits in 717 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 201 other tissues.
DR ExpressionAtlas; Q9UBK9; baseline and differential.
DR Genevisible; Q9UBK9; HS.
DR GO; GO:0005813; C:centrosome; IDA:HGNC-UCL.
DR GO; GO:0101031; C:chaperone complex; IC:ComplexPortal.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
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: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:0003712; F:transcription coregulator activity; IBA:GO_Central.
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; IC:ComplexPortal.
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_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
