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	3D-structure 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 protein binding Inferred from physical interaction Ref.6. 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

Secondary structure

1

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514

Helix Strand Turn

Details...

Helix

159 – 161

3

Beta strand

162 – 165

4

Beta strand

172 – 177

6

Beta strand

179 – 188

10

Beta strand

191 – 197

7

Beta strand

208 – 212

5

Beta strand

228 – 233

6

Beta strand

237 – 244

8

Beta strand

247 – 253

7

Beta strand

258 – 264

7

Beta strand

269 – 274

6

Beta strand

276 – 285

10

Beta strand

290 – 294

5

Turn

295 – 298

4

Beta strand

299 – 304

6

Beta strand

311 – 326

16

Beta strand

331 – 335

5

Beta strand

342 – 345

4

Beta strand

352 – 357

6

Beta strand

361 – 368

8

Beta strand

371 – 377

7

Beta strand

384 – 388

5

Beta strand

394 – 399

6

Beta strand

406 – 408

3

Beta strand

415 – 419

5

Beta strand

424 – 428

5

Turn

429 – 432

4

Beta strand

433 – 438

6

Beta strand

445 – 450

6

Beta strand

454 – 461

8

Beta strand

464 – 470

7

Turn

471 – 473

3

Beta strand

476 – 481

6

Beta strand

486 – 491

6

Beta strand

495 – 502

8

Beta strand

507 – 511

5

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.

CCDS

CCDS46961.1.

RefSeq

NP_078941.2. NM_024665.4.
XP_005247829.1. XM_005247772.1.
XP_005247832.1. XM_005247775.1.
XP_006713808.1. XM_006713745.1.
XP_006713809.1. XM_006713746.1.

UniGene

Hs.715026.

3D structure databases

PDBe
RCSB-PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4LG9	X-ray	2.28	A	134-514	[»]

ProteinModelPortal

Q9BZK7.

SMR

Q9BZK7. Positions 1-68, 124-514.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

122834. 33 interactions.

IntAct

Q9BZK7. 16 interactions.

MINT

MINT-2816883.

STRING

9606.ENSP00000405574.

PTM databases

PhosphoSite

Q9BZK7.

Polymorphism databases

DMDM

23396874.

Proteomic databases

MaxQB

Q9BZK7.

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:	July 9, 2014
This is version 129 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.