Q9BZK7 (TBL1R_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
F-box-like/WD repeat-containing protein TBL1XR1

Alternative name(s):
Nuclear receptor corepressor/HDAC3 complex subunit TBLR1
TBL1-related protein 1
Transducin beta-like 1X-related protein 1

Gene names

Name:	TBL1XR1
Synonyms:	IRA1, TBLR1

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 › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	F-box-like protein involved in the recruitment of the ubiquitin/19S proteasome complex to nuclear receptor-regulated transcription units. Plays an essential role in transcription activation mediated by nuclear receptors. Probably acts as integral component of the N-Cor corepressor complex that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of N-Cor complex, thereby allowing cofactor exchange, and transcription activation. Ref.7
Subunit structure	Component of the N-Cor repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1XR1, CORO2A and GPS2. Probable component of some E3 ubiquitin ligase complex. Interacts with histones H2B and H4.
Subcellular location	Nucleus Probable.
Tissue specificity	Ubiquitous.
Domain	The F-box-like domain is related to the F-box domain, and apparently displays the same function as component of ubiquitin E3 ligase complexes By similarity.
Sequence similarities	Belongs to the WD repeat EBI family. Contains 1 F-box-like domain. Contains 1 LisH domain. Contains 8 WD repeats.
Sequence caution	The sequence AAH60320.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Domain	Repeat WD repeat
Molecular function	Activator Chromatin regulator Repressor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling pathway Traceable author statement. Source: Reactome canonical Wnt signaling pathway Inferred from mutant phenotype PubMed 18193033. Source: UniProtKB cellular lipid metabolic process Traceable author statement. Source: Reactome chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.6. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 18193033. Source: UniProtKB positive regulation of transcription, DNA-templated Inferred from direct assay PubMed 18193033. Source: UniProtKB proteasome-mediated ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB small molecule metabolic process Traceable author statement. Source: Reactome transcription, DNA-templated Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome nucleus Inferred from direct assay PubMed 18193033. Source: UniProtKB spindle microtubule Inferred from direct assay PubMed 18326024. Source: UniProtKB transcriptional repressor complex Inferred from direct assay Ref.6PubMed 15601853. Source: UniProtKB
Molecular_function	beta-catenin binding Inferred from physical interaction PubMed 18193033. Source: UniProtKB histone binding Inferred from direct assay PubMed 15601853. Source: UniProtKB protein N-terminus binding Inferred from physical interaction PubMed 16893456. Source: UniProtKB transcription corepressor activity Inferred from direct assay Ref.6. Source: UniProtKB transcription regulatory region DNA binding Inferred from direct assay PubMed 18193033. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.11
	Chain	2 – 514	513	F-box-like/WD repeat-containing protein TBL1XR1		PRO_0000051266
Regions
	Domain	4 – 36	33	LisH
	Domain	41 – 86	46	F-box-like
	Repeat	167 – 206	40	WD 1
	Repeat	223 – 262	40	WD 2
	Repeat	264 – 303	40	WD 3
	Repeat	306 – 344	39	WD 4
	Repeat	347 – 386	40	WD 5
	Repeat	389 – 437	49	WD 6
	Repeat	440 – 479	40	WD 7
	Repeat	481 – 513	33	WD 8
	Compositional bias	108 – 118	11	Poly-Ala
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.11 Ref.12
	Modified residue	102	1	N6-acetyllysine By similarity
	Modified residue	119	1	Phosphoserine Ref.9
Experimental info
	Sequence conflict	31	1	E → K in AAG44736. Ref.2
	Sequence conflict	59	1	Y → H in BAB14331. Ref.3
	Sequence conflict	389	1	A → Q in AAG44736. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9BZK7 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 0B556D2EE4BA796D	FASTA	514	55,595
	10 20 30 40 50 60 MSISSDEVNF LVYRYLQESG FSHSAFTFGI ESHISQSNIN GALVPPAALI SIIQKGLQYV 70 80 90 100 110 120 EAEVSINEDG TLFDGRPIES LSLIDAVMPD VVQTRQQAYR DKLAQQQAAA AAAAAAAASQ 130 140 150 160 170 180 QGSAKNGENT ANGEENGAHT IANNHTDMME VDGDVEIPPN KAVVLRGHES EVFICAWNPV 190 200 210 220 230 240 SDLLASGSGD STARIWNLSE NSTSGSTQLV LRHCIREGGQ DVPSNKDVTS LDWNSEGTLL 250 260 270 280 290 300 ATGSYDGFAR IWTKDGNLAS TLGQHKGPIF ALKWNKKGNF ILSAGVDKTT IIWDAHTGEA 310 320 330 340 350 360 KQQFPFHSAP ALDVDWQSNN TFASCSTDMC IHVCKLGQDR PIKTFQGHTN EVNAIKWDPT 370 380 390 400 410 420 GNLLASCSDD MTLKIWSMKQ DNCVHDLQAH NKEIYTIKWS PTGPGTNNPN ANLMLASASF 430 440 450 460 470 480 DSTVRLWDVD RGICIHTLTK HQEPVYSVAF SPDGRYLASG SFDKCVHIWN TQTGALVHSY 490 500 510 RGTGGIFEVC WNAAGDKVGA SASDGSVCVL DLRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2." Zhang J., Kalkum M., Chait B.T., Roeder R.G. Mol. Cell 9:611-623(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, COMPONENT OF THE N-COR COMPLEX WITH NCOR1; NCOR2; GPS2; TBL1X AND HDAC3.
[2]	"Identification of four human cDNAs that are differentially expressed by early hematopoietic progenitors." Zhang X., Dormady S.P., Basch R.S. Exp. Hematol. 28:1286-1296(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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].
[4]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: Adrenal cortex and Liver.
[6]	"Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1." Yoon H.-G., Chan D.W., Huang Z.-Q., Li J., Fondell J.D., Qin J., Wong J. EMBO J. 22:1336-1346(2003) [PubMed] [Europe PMC] [Abstract] Cited for: COMPONENT OF THE N-COR COMPLEX WITH TBL1X; CORO2A AND HDAC3, HISTONE-BINDING.
[7]	"A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors." Perissi V., Aggarwal A., Glass C.K., Rose D.W., Rosenfeld M.G. Cell 116:511-526(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, RECRUITMENT OF 19S PROTEASOME COMPLEX.
[8]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[9]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"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].
[11]	"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features." Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C. Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]	"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB." Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R. Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF314544 mRNA. Translation: AAK00301.1. AF268193 mRNA. Translation: AAG44736.1. AK022956 mRNA. Translation: BAB14331.1. CH471052 Genomic DNA. Translation: EAW78438.1. BC060320 mRNA. Translation: AAH60320.1. Sequence problems. BC113421 mRNA. Translation: AAI13422.1.
RefSeq	NP_078941.2. NM_024665.4. XP_005247829.1. XM_005247772.1. XP_005247832.1. XM_005247775.1.
UniGene	Hs.715026.
3D structure databases
ProteinModelPortal	Q9BZK7.
SMR	Q9BZK7. Positions 1-68, 124-512.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	122834. 32 interactions.
IntAct	Q9BZK7. 16 interactions.
MINT	MINT-2816883.
STRING	9606.ENSP00000405574.
PTM databases
PhosphoSite	Q9BZK7.
Polymorphism databases
DMDM	23396874.
Proteomic databases
PaxDb	Q9BZK7.
PRIDE	Q9BZK7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000430069; ENSP00000405574; ENSG00000177565. ENST00000457928; ENSP00000413251; ENSG00000177565.
GeneID	79718.
KEGG	hsa:79718.
UCSC	uc003fiw.4. human.
Organism-specific databases
CTD	79718.
GeneCards	GC03M176737.
H-InvDB	HIX0147994.
HGNC	HGNC:29529. TBL1XR1.
HPA	HPA019182.
MIM	608628. gene.
neXtProt	NX_Q9BZK7.
PharmGKB	PA134928556.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2319.
HOGENOM	HOG000220902.
HOVERGEN	HBG050240.
InParanoid	Q9BZK7.
KO	K04508.
OMA	LANNHAD.
OrthoDB	EOG79CXZ3.
PhylomeDB	Q9BZK7.
TreeFam	TF323190.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_116125. Disease.
SignaLink	Q9BZK7.
Gene expression databases
ArrayExpress	Q9BZK7.
Bgee	Q9BZK7.
CleanEx	HS_TBL1XR1.
Genevestigator	Q9BZK7.
Family and domain databases
Gene3D	2.130.10.10. 2 hits.
InterPro	IPR020472. G-protein_beta_WD-40_rep. IPR006594. LisH_dimerisation. IPR013720. LisH_dimerisation_subgr. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_dom. [Graphical view]
Pfam	PF08513. LisH. 1 hit. PF00400. WD40. 7 hits. [Graphical view]
PRINTS	PR00320. GPROTEINBRPT.
SMART	SM00667. LisH. 1 hit. SM00320. WD40. 8 hits. [Graphical view]
SUPFAM	SSF50978. SSF50978. 2 hits.
PROSITE	PS50896. LISH. 1 hit. PS00678. WD_REPEATS_1. 4 hits. PS50082. WD_REPEATS_2. 6 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TBL1XR1. human.
GeneWiki	TBL1XR1.
GenomeRNAi	79718.
NextBio	69065.
PMAP-CutDB	Q9BZK7.
PRO	Q9BZK7.
SOURCE	Search...

Entry information

Entry name

TBL1R_HUMAN

Accession

Primary (citable) accession number: Q9BZK7
Secondary accession number(s): D3DNQ9 , Q14DC3, Q9H2I1, Q9H9A1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	June 1, 2001
Last modified:	April 16, 2014
This is version 126 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.