Q9UBK9 (UXT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein UXT

Alternative name(s):
Androgen receptor trapped clone 27 protein
Short name=ART-27
Ubiquitously expressed transcript protein

Gene names

Name:	UXT
ORF Names:	HSPC024

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	157 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in gene transcription regulation. Acts in concert with the corepressor URI1 to regulate androgen receptor transcription (AR). AR N-terminus-associated coactivator which may play a role in facilitating receptor-induced transcriptional activation (Ref.2). Potential component of mitochondrial-associated LRPPRC, a multidomain organizer that potentially integrates mitochondria and the microtubular cytoskeleton with chromosome remodeling (Ref.10). Increasing concentrations of UXT contributes to progressive aggregation of mitochondria and cell death potentially through its association with LRPPRC (Ref.12). May be a nuclear chaperone that promotes formation of the NF-kappa-B enhanceosome and which is essential for its nuclear function (Ref.13). 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 (Ref.3). Together with URI1, associates with chromatin to the NKX3-1 promoter region. Ref.2 Ref.3 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15
Subunit structure	Homohexamer. Interacts with LRPPRC. Interacts with AR N-terminus. In the nucleus interacts specifically with RELA and forms a dynamic complex with NF-kappa-B and is recruited to the NF-kappa-B enhanceosome upon stimulation. Interacts with MECOM and URI1. Ref.2 Ref.3 Ref.10 Ref.11 Ref.13 Ref.15
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Nucleus Ref.2 Ref.11.
Tissue specificity	Ubiquitous. Expressed in prostate epithelial cells. Overexpressed in a number of tumor tissues (Ref.11). 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. Ref.2 Ref.3 Ref.15
Sequence similarities	Belongs to the UXT family.
Sequence caution	The sequence AAD39840.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAI42447.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Cytoskeleton Nucleus
Molecular function	Activator Chaperone Repressor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	centrosome organization Inferred from mutant phenotype Ref.11. Source: HGNC mitochondrion transport along microtubule Traceable author statement PubMed 12762840. Source: HGNC protein folding Inferred from electronic annotation. Source: InterPro
Cellular_component	centrosome Inferred from direct assay Ref.11. Source: HGNC cytoplasm Inferred from direct assay Ref.15. Source: UniProtKB nucleus Inferred from direct assay Ref.15. Source: UniProtKB prefoldin complex Inferred from electronic annotation. Source: InterPro
Molecular_function	RNA polymerase II transcription corepressor activity Inferred from direct assay Ref.15. Source: UniProtKB beta-tubulin binding Inferred from direct assay PubMed 12762840. Source: HGNC chromatin binding Inferred from direct assay Ref.15. Source: UniProtKB microtubule binding Traceable author statement PubMed 12762840. Source: HGNC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MECOM	Q03112	5	EBI-357355,EBI-1384862
RELA	Q04206	5	EBI-357355,EBI-73886

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 157	157	Protein UXT		PRO_0000065751
Experimental info
	Mutagenesis	50	1	L → P: Causes dislocation from the centrosome; when associated with L-59. Ref.11
	Mutagenesis	59	1	L → P: Causes dislocation from the centrosome; when associated with L-50. Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Q9UBK9 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 94CE14C462DEE308	FASTA	157	18,246
	10 20 30 40 50 60 MATPPKRRAV EATGEKVLRY ETFISDVLQR DLRKVLDHRD KVYEQLAKYL QLRNVIERLQ 70 80 90 100 110 120 EAKHSELYMQ VDLGCNFFVD TVVPDTSRIY VALGYGFFLE LTLAEALKFI DRKSSLLTEL 130 140 150 SNSLTKDSMN IKAHIHMLLE GLRELQGLQN FPEKPHH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of UXT, a novel gene in human Xp11, which is widely and abundantly expressed in tumor tissue." Schroer A., Schneider S., Ropers H.-H., Nothwang H.G. Genomics 56:340-343(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Identification and characterization of ART-27, a novel coactivator for the androgen receptor N terminus." Markus S.M., Taneja S.S., Logan S.K., Li W., Ha S., Hittelman A.B., Rogatsky I., Garabedian M.J. Mol. Biol. Cell 13:670-682(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH AR.
[3]	"UXT interacts with the transcriptional repressor protein EVI1 and suppresses cell transformation." McGilvray R., Walker M., Bartholomew C. FEBS J. 274:3960-3971(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH MECOM.
[4]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." 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. Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[5]	Zhou J., Ye M., Fu G., Zhang Q., Shen Y., Huang Q., Xu S., He K., Chen S., Mao M., Chen Z. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary gland.
[7]	"The DNA sequence of the human X chromosome." 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. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[10]	"Sequence analysis of LRPPRC and its SEC1 domain interaction partners suggests roles in cytoskeletal organization, vesicular trafficking, nucleocytosolic shuttling, and chromosome activity." Liu L., McKeehan W.L. Genomics 79:124-136(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH LRPPRC.
[11]	"UXT is a novel centrosomal protein essential for cell viability." Zhao H., Wang Q., Zhang H., Liu Q., Du X., Richter M., Greene M.I. Mol. Biol. Cell 16:5857-5865(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, HOMOHEXAMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-50 AND LEU-59.
[12]	"UXT (Ubiquitously Expressed Transcript) causes mitochondrial aggregation." Moss T.N., Vo A., McKeehan W.L., Liu L. In Vitro Cell. Dev. Biol. Anim. 43:139-146(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"UXT is a novel and essential cofactor in the NF-kappaB transcriptional enhanceosome." Sun S., Tang Y., Lou X., Zhu L., Yang K., Zhang B., Shi H., Wang C. J. Cell Biol. 178:231-244(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RELA.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"Regulation of androgen receptor-mediated transcription by RPB5 binding protein URI/RMP." 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. Mol. Cell. Biol. 31:3639-3652(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH URI1, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF092737 mRNA. Translation: AAD28698.1. AF083241 mRNA. Translation: AAD39839.1. AF083242 mRNA. Translation: AAD39840.1. Different initiation. AL009172 Genomic DNA. Translation: CAI42447.1. Different initiation. AL009172 Genomic DNA. Translation: CAI42448.1. AK312072 mRNA. Translation: BAG35008.1. CH471164 Genomic DNA. Translation: EAW59326.1. BC000720 mRNA. Translation: AAH00720.1. BC008890 mRNA. Translation: AAH08890.1.
IPI	IPI00002646.
RefSeq	NP_004173.1. NM_004182.3. NP_705582.1. NM_153477.2.
UniGene	Hs.172791. Hs.735566.
3D structure databases
ProteinModelPortal	Q9UBK9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UBK9. 19 interactions.
MINT	MINT-1143575.
STRING	9606.ENSP00000337393.
PTM databases
PhosphoSite	Q9UBK9.
Polymorphism databases
DMDM	8928445.
Proteomic databases
PaxDb	Q9UBK9.
PRIDE	Q9UBK9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000333119; ENSP00000327797; ENSG00000126756. ENST00000335890; ENSP00000337393; ENSG00000126756.
GeneID	8409.
KEGG	hsa:8409.
UCSC	uc004dim.3. human.
Organism-specific databases
CTD	8409.
GeneCards	GC0XM047511.
HGNC	HGNC:12641. UXT.
MIM	300234. gene.
neXtProt	NX_Q9UBK9.
PharmGKB	PA37265.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG263764.
HOGENOM	HOG000005748.
HOVERGEN	HBG001087.
InParanoid	Q9UBK9.
OrthoDB	EOG4Z36G3.
Gene expression databases
Bgee	Q9UBK9.
CleanEx	HS_UXT.
Genevestigator	Q9UBK9.
GermOnline	ENSG00000126756. Homo sapiens.
Family and domain databases
InterPro	IPR003994. PFD_UXT. IPR009053. Prefoldin. IPR004127. Prefoldin_subunit. [Graphical view]
Pfam	PF02996. Prefoldin. 1 hit. [Graphical view]
PRINTS	PR01502. UXTPROTEIN.
SUPFAM	SSF46579. Prefoldin. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	8409.
NextBio	31482.
SOURCE	Search...

Entry information

Entry name

UXT_HUMAN

Accession

Primary (citable) accession number: Q9UBK9
Secondary accession number(s): B2R561, Q5JZG3, Q9Y6E5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.