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Q9BZK7 (TBL1R_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   DomainRepeat
WD repeat
   Molecular functionActivator
Chromatin regulator
Repressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch 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_componentnucleoplasm

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_functionbeta-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 514513F-box-like/WD repeat-containing protein TBL1XR1
PRO_0000051266

Regions

Domain4 – 3633LisH
Domain41 – 8646F-box-like
Repeat167 – 20640WD 1
Repeat223 – 26240WD 2
Repeat264 – 30340WD 3
Repeat306 – 34439WD 4
Repeat347 – 38640WD 5
Repeat389 – 43749WD 6
Repeat440 – 47940WD 7
Repeat481 – 51333WD 8
Compositional bias108 – 11811Poly-Ala

Amino acid modifications

Modified residue21N-acetylserine Ref.11 Ref.12
Modified residue1021N6-acetyllysine By similarity
Modified residue1191Phosphoserine Ref.9

Experimental info

Sequence conflict311E → K in AAG44736. Ref.2
Sequence conflict591Y → H in BAB14331. Ref.3
Sequence conflict3891A → Q in AAG44736. Ref.2

Secondary structure

................................................................... 514
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BZK7 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 0B556D2EE4BA796D

FASTA51455,595
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
CCDSCCDS46961.1.
RefSeqNP_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.
UniGeneHs.715026.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4LG9X-ray2.28A134-514[»]
ProteinModelPortalQ9BZK7.
SMRQ9BZK7. Positions 1-68, 124-514.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122834. 33 interactions.
IntActQ9BZK7. 16 interactions.
MINTMINT-2816883.
STRING9606.ENSP00000405574.

PTM databases

PhosphoSiteQ9BZK7.

Polymorphism databases

DMDM23396874.

Proteomic databases

MaxQBQ9BZK7.
PaxDbQ9BZK7.
PRIDEQ9BZK7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000430069; ENSP00000405574; ENSG00000177565.
ENST00000457928; ENSP00000413251; ENSG00000177565.
GeneID79718.
KEGGhsa:79718.
UCSCuc003fiw.4. human.

Organism-specific databases

CTD79718.
GeneCardsGC03M176737.
H-InvDBHIX0147994.
HGNCHGNC:29529. TBL1XR1.
HPAHPA019182.
MIM608628. gene.
neXtProtNX_Q9BZK7.
PharmGKBPA134928556.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000220902.
HOVERGENHBG050240.
InParanoidQ9BZK7.
KOK04508.
OMALANNHAD.
OrthoDBEOG79CXZ3.
PhylomeDBQ9BZK7.
TreeFamTF323190.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
SignaLinkQ9BZK7.

Gene expression databases

ArrayExpressQ9BZK7.
BgeeQ9BZK7.
CleanExHS_TBL1XR1.
GenevestigatorQ9BZK7.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR020472. 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]
PfamPF08513. LisH. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00667. LisH. 1 hit.
SM00320. WD40. 8 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 2 hits.
PROSITEPS50896. LISH. 1 hit.
PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTBL1XR1. human.
GeneWikiTBL1XR1.
GenomeRNAi79718.
NextBio69065.
PMAP-CutDBQ9BZK7.
PROQ9BZK7.
SOURCESearch...

Entry information

Entry nameTBL1R_HUMAN
AccessionPrimary (citable) accession number: Q9BZK7
Secondary accession number(s): D3DNQ9 expand/collapse secondary AC list , 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM