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Protein UXT (Androgen receptor trapped clone 27 protein) (ART-27) (Ubiquitously expressed transcript protein)

 UXT_HUMAN               Reviewed;         157 AA.
Q9UBK9; A0A0C4DFR8; B2R561; Q5JZG3; Q9Y6E5;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
12-SEP-2018, entry version 152.
RecName: Full=Protein UXT;
AltName: Full=Androgen receptor trapped clone 27 protein {ECO:0000303|PubMed:11854421};
Short=ART-27 {ECO:0000303|PubMed:11854421};
AltName: Full=Ubiquitously expressed transcript protein;
Name=UXT; ORFNames=HSPC024;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=10087202; DOI=10.1006/geno.1998.5712;
Schroer A., Schneider S., Ropers H.-H., Nothwang H.G.;
"Cloning and characterization of UXT, a novel gene in human Xp11,
which is widely and abundantly expressed in tumor tissue.";
Genomics 56:340-343(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH AR.
PubMed=11854421; DOI=10.1091/mbc.01-10-0513;
Markus S.M., Taneja S.S., Logan S.K., Li W., Ha S., Hittelman A.B.,
Rogatsky I., Garabedian M.J.;
"Identification and characterization of ART-27, a novel coactivator
for the androgen receptor N terminus.";
Mol. Biol. Cell 13:670-682(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
AND INTERACTION WITH MECOM.
PubMed=17635584; DOI=10.1111/j.1742-4658.2007.05928.x;
McGilvray R., Walker M., Bartholomew C.;
"UXT interacts with the transcriptional repressor protein EVI1 and
suppresses cell transformation.";
FEBS J. 274:3960-3971(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION (ISOFORMS 1 AND 2),
IDENTIFICATION IN COMPLEX I, INTERACTION WITH TRAF2, SUBCELLULAR
LOCATION, AND IDENTIFICATION OF ISOFORM 1.
PubMed=21307340; DOI=10.1091/mbc.E10-10-0827;
Huang Y., Chen L., Zhou Y., Liu H., Yang J., Liu Z., Wang C.;
"UXT-V1 protects cells against TNF-induced apoptosis through
modulating complex II formation.";
Mol. Biol. Cell 22:1389-1397(2011).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Mammary gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
FUNCTION, INTERACTION WITH LRPPRC, AND TISSUE SPECIFICITY.
PubMed=11827465; DOI=10.1006/geno.2001.6679;
Liu L., McKeehan W.L.;
"Sequence analysis of LRPPRC and its SEC1 domain interaction partners
suggests roles in cytoskeletal organization, vesicular trafficking,
nucleocytosolic shuttling, and chromosome activity.";
Genomics 79:124-136(2002).
[11]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
MUTAGENESIS OF LEU-50 AND LEU-59.
PubMed=16221885; DOI=10.1091/mbc.E05-08-0705;
Zhao H., Wang Q., Zhang H., Liu Q., Du X., Richter M., Greene M.I.;
"UXT is a novel centrosomal protein essential for cell viability.";
Mol. Biol. Cell 16:5857-5865(2005).
[12]
FUNCTION, AND INTERACTION WITH LRPPRC.
PubMed=17554592; DOI=10.1007/s11626-007-9016-6;
Moss T.N., Vo A., McKeehan W.L., Liu L.;
"UXT (Ubiquitously Expressed Transcript) causes mitochondrial
aggregation.";
In Vitro Cell. Dev. Biol. Anim. 43:139-146(2007).
[13]
FUNCTION, INTERACTION WITH RELA, AND SUBCELLULAR LOCATION.
PubMed=17620405; DOI=10.1083/jcb.200611081;
Sun S., Tang Y., Lou X., Zhu L., Yang K., Zhang B., Shi H., Wang C.;
"UXT is a novel and essential cofactor in the NF-kappaB
transcriptional enhanceosome.";
J. Cell Biol. 178:231-244(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
FUNCTION, INTERACTION WITH URI1, AND TISSUE SPECIFICITY.
PubMed=21730289; DOI=10.1128/MCB.05429-11;
Mita P., Savas J.N., Djouder N., Yates J.R. III, Ha S., Ruoff R.,
Schafler E.D., Nwachukwu J.C., Tanese N., Cowan N.J., Zavadil J.,
Garabedian M.J., Logan S.K.;
"Regulation of androgen receptor-mediated transcription by RPB5
binding protein URI/RMP.";
Mol. Cell. Biol. 31:3639-3652(2011).
[16]
FUNCTION, INTERACTION WITH ESR1, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=28106301; DOI=10.1002/jcb.25893;
Sanchez-Morgan N., Kirsch K.H., Trackman P.C., Sonenshein G.E.;
"UXT is a LOX-PP interacting protein that modulates estrogen receptor
alpha activity in breast cancer Cells.";
J. Cell. Biochem. 118:2347-2356(2017).
-!- FUNCTION: Involved in gene transcription regulation
(PubMed:28106301, PubMed:21730289). Acts in concert with the
corepressor URI1 to regulate androgen receptor AR-mediated
transcription (PubMed:11854421, PubMed:21730289). Together with
URI1, associates with chromatin to the NKX3-1 promoter region
(PubMed:21730289). Negatively regulates the transcriptional
activity of the estrogen receptor ESR1 by inducing its
translocation into the cytoplasm (PubMed:28106301). May act as
nuclear chaperone that facilitates the formation of the NF-kappa-B
enhanceosome and thus positively regulates NF-kappa-B
transcription activity (PubMed:17620405, PubMed:21307340).
Potential component of mitochondrial-associated LRPPRC, a
multidomain organizer that potentially integrates mitochondria and
the microtubular cytoskeleton with chromosome remodeling
(PubMed:17554592). Increasing concentrations of UXT contributes to
progressive aggregation of mitochondria and cell death potentially
through its association with LRPPRC (PubMed:17554592). Suppresses
cell transformation and it might mediate this function by
interaction and inhibition of the biological activity of cell
proliferation and survival stimulatory factors like MECOM
(PubMed:17635584). {ECO:0000269|PubMed:11827465,
ECO:0000269|PubMed:11854421, ECO:0000269|PubMed:16221885,
ECO:0000269|PubMed:17554592, ECO:0000269|PubMed:17620405,
ECO:0000269|PubMed:17635584, ECO:0000269|PubMed:21307340,
ECO:0000269|PubMed:21730289, ECO:0000269|PubMed:28106301}.
-!- FUNCTION: Isoform 1: Plays a role in protecting cells against TNF-
alpha-induced apoptosis by preventing the recruitment of FADD and
caspase 8 to the apoptotic complex I, composed of TRADD, TRAF2 and
RIPK1/RIP. {ECO:0000269|PubMed:21307340}.
-!- SUBUNIT: Homohexamer (PubMed:16221885). Interacts with LRPPRC
(PubMed:11827465, PubMed:17554592). Interacts with androgen
receptor AR (via N-terminus) (PubMed:11854421). Interacts with
estrogen receptor ESR1; the interaction relocalizes ESR1 from the
nucleus to the cytoplasm (PubMed:28106301). In the nucleus,
interacts specifically with RELA (via RHD domain) and forms a
dynamic complex with NF-kappa-B and is recruited to the NF-kappa-B
enhanceosome upon stimulation (PubMed:17620405). Interacts with
MECOM (PubMed:17635584). Interacts with URI1 (PubMed:21730289).
Isoform 1 is part of complex I composed of TNF-alpha receptor
TNFRSF1A, TRADD, TRAF2 and RIPK1 formed in response to TNF-alpha
stimulation. Within the complex, interacts (via TPQE motif) with
TRAF2; the interaction prevents the recruitment of FADD and
CASP8/caspase 8 to complex I (PubMed:21307340).
{ECO:0000269|PubMed:11827465, ECO:0000269|PubMed:11854421,
ECO:0000269|PubMed:16221885, ECO:0000269|PubMed:17554592,
ECO:0000269|PubMed:17620405, ECO:0000269|PubMed:17635584,
ECO:0000269|PubMed:21307340, ECO:0000269|PubMed:21730289,
ECO:0000269|PubMed:28106301}.
-!- INTERACTION:
P03372:ESR1; NbExp=2; IntAct=EBI-357355, EBI-78473;
Q15323:KRT31; NbExp=5; IntAct=EBI-357355, EBI-948001;
Q6A162:KRT40; NbExp=3; IntAct=EBI-357355, EBI-10171697;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-357355, EBI-10172290;
P60410:KRTAP10-8; NbExp=5; IntAct=EBI-357355, EBI-10171774;
Q03112:MECOM; NbExp=5; IntAct=EBI-357355, EBI-1384862;
Q7Z3S9:NOTCH2NL; NbExp=5; IntAct=EBI-357355, EBI-945833;
Q9P286:PAK5; NbExp=3; IntAct=EBI-357355, EBI-741896;
Q04206:RELA; NbExp=5; IntAct=EBI-357355, EBI-73886;
Q9H6T3:RPAP3; NbExp=2; IntAct=EBI-357355, EBI-356928;
Q0D2N8:SARM1; NbExp=2; IntAct=EBI-357355, EBI-8716526;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-357355, EBI-747107;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm
{ECO:0000269|PubMed:21307340}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21307340,
ECO:0000305|PubMed:28106301}. Nucleus
{ECO:0000269|PubMed:11854421, ECO:0000269|PubMed:17620405,
ECO:0000269|PubMed:21307340, ECO:0000305|PubMed:28106301}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:16221885}. Cytoplasm, cytoskeleton, spindle
pole {ECO:0000269|PubMed:16221885}. Note=Predominantly localizes
to the nucleus (PubMed:16221885). Localizes to spindle pole during
mitosis (PubMed:16221885). {ECO:0000269|PubMed:16221885,
ECO:0000269|PubMed:21307340}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2; Synonyms=UXT-V2 {ECO:0000303|PubMed:21307340};
IsoId=Q9UBK9-1; Sequence=Displayed;
Name=1; Synonyms=UXT-V1 {ECO:0000303|PubMed:21307340};
IsoId=Q9UBK9-2; Sequence=VSP_059081;
-!- TISSUE SPECIFICITY: Ubiquitous (PubMed:10087202, PubMed:11854421,
PubMed:17635584, PubMed:11827465). Expressed in prostate
epithelial cells (PubMed:21730289). Expressed in mammary
epithelial cells (PubMed:28106301). Highest levels in the heart,
skeletal muscle, pancreas, kidney, liver, adrenal gland,
peripheral blood leukocytes, lymph node, prostate, and thyroid and
the lowest levels in bladder and uterus (PubMed:11854421,
PubMed:17635584, PubMed:11827465). Overexpressed in a number of
tumor tissues (PubMed:11854421, PubMed:16221885, PubMed:28106301).
{ECO:0000269|PubMed:10087202, ECO:0000269|PubMed:11827465,
ECO:0000269|PubMed:11854421, ECO:0000269|PubMed:16221885,
ECO:0000269|PubMed:17635584, ECO:0000269|PubMed:21730289,
ECO:0000269|PubMed:28106301}.
-!- SIMILARITY: Belongs to the UXT family. {ECO:0000305}.
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EMBL; AF092737; AAD28698.1; -; mRNA.
EMBL; AF083241; AAD39839.1; -; mRNA.
EMBL; AF083242; AAD39840.1; -; mRNA.
EMBL; AK312072; BAG35008.1; -; mRNA.
EMBL; AL009172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471164; EAW59325.1; -; Genomic_DNA.
EMBL; CH471164; EAW59326.1; -; Genomic_DNA.
EMBL; BC000720; AAH00720.1; -; mRNA.
EMBL; BC008890; AAH08890.1; -; mRNA.
CCDS; CCDS14284.1; -. [Q9UBK9-2]
CCDS; CCDS14285.1; -. [Q9UBK9-1]
RefSeq; NP_004173.1; NM_004182.3. [Q9UBK9-1]
RefSeq; NP_705582.1; NM_153477.2. [Q9UBK9-2]
UniGene; Hs.172791; -.
UniGene; Hs.735566; -.
ProteinModelPortal; Q9UBK9; -.
SMR; Q9UBK9; -.
BioGrid; 113997; 62.
IntAct; Q9UBK9; 57.
MINT; Q9UBK9; -.
STRING; 9606.ENSP00000337393; -.
iPTMnet; Q9UBK9; -.
PhosphoSitePlus; Q9UBK9; -.
BioMuta; UXT; -.
DMDM; 8928445; -.
EPD; Q9UBK9; -.
MaxQB; Q9UBK9; -.
PaxDb; Q9UBK9; -.
PeptideAtlas; Q9UBK9; -.
PRIDE; Q9UBK9; -.
ProteomicsDB; 83987; -.
Ensembl; ENST00000333119; ENSP00000327797; ENSG00000126756. [Q9UBK9-1]
Ensembl; ENST00000335890; ENSP00000337393; ENSG00000126756. [Q9UBK9-2]
GeneID; 8409; -.
KEGG; hsa:8409; -.
UCSC; uc004dim.4; human. [Q9UBK9-1]
CTD; 8409; -.
DisGeNET; 8409; -.
EuPathDB; HostDB:ENSG00000126756.11; -.
GeneCards; UXT; -.
HGNC; HGNC:12641; UXT.
HPA; HPA050499; -.
HPA; HPA058400; -.
MIM; 300234; gene.
neXtProt; NX_Q9UBK9; -.
OpenTargets; ENSG00000126756; -.
PharmGKB; PA37265; -.
eggNOG; KOG3047; Eukaryota.
eggNOG; ENOG4111Q3P; LUCA.
GeneTree; ENSGT00390000018078; -.
HOGENOM; HOG000005748; -.
HOVERGEN; HBG001087; -.
InParanoid; Q9UBK9; -.
OMA; QVNIGSN; -.
PhylomeDB; Q9UBK9; -.
TreeFam; TF323827; -.
Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
SIGNOR; Q9UBK9; -.
ChiTaRS; UXT; human.
GeneWiki; UXT; -.
GenomeRNAi; 8409; -.
PRO; PR:Q9UBK9; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000126756; Expressed in 228 organ(s), highest expression level in right ovary.
CleanEx; HS_UXT; -.
ExpressionAtlas; Q9UBK9; baseline and differential.
Genevisible; Q9UBK9; HS.
GO; GO:0005813; C:centrosome; IDA:HGNC.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IDA:HGNC.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0048487; F:beta-tubulin binding; IDA:HGNC.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0008017; F:microtubule binding; TAS:HGNC.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007098; P:centrosome cycle; IMP:HGNC.
GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:HGNC.
GO; GO:0047497; P:mitochondrion transport along microtubule; TAS:HGNC.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.287.370; -; 1.
InterPro; IPR009053; Prefoldin.
InterPro; IPR004127; Prefoldin_subunit_alpha.
InterPro; IPR003994; UXT.
Pfam; PF02996; Prefoldin; 1.
PRINTS; PR01502; UXTPROTEIN.
1: Evidence at protein level;
Activator; Alternative splicing; Apoptosis; Chaperone;
Complete proteome; Cytoplasm; Cytoskeleton; Nucleus;
Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 157 Protein UXT.
/FTId=PRO_0000065751.
VAR_SEQ 1 1 M -> MVFPLPTPQEPIM (in isoform 1).
{ECO:0000305}.
/FTId=VSP_059081.
MUTAGEN 50 50 L->P: Causes dislocation from the
centrosome; when associated with L-59.
{ECO:0000269|PubMed:16221885}.
MUTAGEN 59 59 L->P: Causes dislocation from the
centrosome; when associated with L-50.
{ECO:0000269|PubMed:16221885}.
SEQUENCE 157 AA; 18246 MW; 94CE14C462DEE308 CRC64;
MATPPKRRAV EATGEKVLRY ETFISDVLQR DLRKVLDHRD KVYEQLAKYL QLRNVIERLQ
EAKHSELYMQ VDLGCNFFVD TVVPDTSRIY VALGYGFFLE LTLAEALKFI DRKSSLLTEL
SNSLTKDSMN IKAHIHMLLE GLRELQGLQN FPEKPHH


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