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O60907

- TBL1X_HUMAN

UniProt

O60907 - TBL1X_HUMAN

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Protein

F-box-like/WD repeat-containing protein TBL1X

Gene

TBL1X

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 corepressor complexes that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of transcription repressor complexes, thereby allowing cofactor exchange.1 Publication

GO - Molecular functioni

  1. beta-catenin binding Source: UniProtKB
  2. histone binding Source: UniProtKB
  3. protein C-terminus binding Source: UniProtKB
  4. protein domain specific binding Source: UniProtKB
  5. transcription corepressor activity Source: UniProtKB
  6. transcription factor binding Source: UniProtKB
  7. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. canonical Wnt signaling pathway Source: UniProtKB
  2. cellular lipid metabolic process Source: Reactome
  3. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  4. Notch signaling pathway Source: Reactome
  5. positive regulation of transcription, DNA-templated Source: UniProtKB
  6. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  7. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  8. proteolysis Source: UniProtKB
  9. sensory perception of sound Source: UniProtKB
  10. small molecule metabolic process Source: Reactome
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates circadian gene expression.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_118789. REV-ERBA represses gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_228222. HDACs deacetylate histones.
REACT_24941. Circadian Clock.
REACT_267716. Orphan transporters.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiO60907.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box-like/WD repeat-containing protein TBL1X
Alternative name(s):
SMAP55
Transducin beta-like protein 1X
Transducin-beta-like protein 1, X-linked
Gene namesi
Name:TBL1X
Synonyms:TBL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:11585. TBL1X.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: UniProtKB
  3. spindle microtubule Source: UniProtKB
  4. transcriptional repressor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Deafness

Organism-specific databases

PharmGKBiPA36349.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 577577F-box-like/WD repeat-containing protein TBL1XPRO_0000051263Add
BLAST

Proteomic databases

MaxQBiO60907.
PaxDbiO60907.
PRIDEiO60907.

PTM databases

PhosphoSiteiO60907.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiO60907.
CleanExiHS_TBL1X.
ExpressionAtlasiO60907. baseline and differential.
GenevestigatoriO60907.

Organism-specific databases

HPAiCAB005363.

Interactioni

Subunit structurei

Component of the N-Cor repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1R, CORO2A and GPS2. Component of a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Probably part of other corepressor complexes, that do not contain NCOR1 and NCOR2. Interacts with histones H2B, H3a and H4.1 Publication

Protein-protein interaction databases

BioGridi112770. 42 interactions.
DIPiDIP-60532N.
IntActiO60907. 10 interactions.
STRINGi9606.ENSP00000217964.

Structurei

Secondary structure

1
577
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 6914Combined sources
Helixi73 – 8210Combined sources
Helixi85 – 873Combined sources
Helixi92 – 943Combined sources
Helixi99 – 11618Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XTCX-ray2.22A/B52-141[»]
2XTDX-ray3.20A/B52-122[»]
2XTEX-ray3.90A/B/C/D/E/F/G/H/I/J/K/L52-141[»]
ProteinModelPortaliO60907.
SMRiO60907. Positions 53-126, 215-576.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60907.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 8733LisHPROSITE-ProRule annotationAdd
BLAST
Domaini92 – 13746F-box-likeAdd
BLAST
Repeati230 – 26940WD 1Add
BLAST
Repeati286 – 32540WD 2Add
BLAST
Repeati327 – 36640WD 3Add
BLAST
Repeati369 – 40941WD 4Add
BLAST
Repeati410 – 44940WD 5Add
BLAST
Repeati452 – 50049WD 6Add
BLAST
Repeati503 – 54240WD 7Add
BLAST
Repeati544 – 57633WD 8Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi159 – 17517Poly-AlaAdd
BLAST

Domaini

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 similaritiesi

Belongs to the WD repeat EBI family.Curated
Contains 1 F-box-like domain.Curated
Contains 1 LisH domain.PROSITE-ProRule annotation
Contains 8 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00750000117536.
HOGENOMiHOG000220902.
HOVERGENiHBG050240.
InParanoidiO60907.
KOiK04508.
OMAiSMKQEVC.
OrthoDBiEOG79CXZ3.
PhylomeDBiO60907.
TreeFamiTF323190.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR006594. LisH_dimerisation.
IPR013720. LisH_dimerisation_subgr.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08513. LisH. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00667. LisH. 1 hit.
SM00320. WD40. 8 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
SSF50998. SSF50998. 1 hit.
PROSITEiPS50896. LISH. 1 hit.
PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60907-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTELAGASSS CCHRPAGRGA MQSVLHHFQR LRGREGGSHF INTSSPRGEA
60 70 80 90 100
KMSITSDEVN FLVYRYLQES GFSHSAFTFG IESHISQSNI NGTLVPPAAL
110 120 130 140 150
ISILQKGLQY VEAEISINED GTVFDGRPIE SLSLIDAVMP DVVQTRQQAF
160 170 180 190 200
REKLAQQQAS AAAAAAAATA AATAATTTSA GVSHQNPSKN REATVNGEEN
210 220 230 240 250
RAHSVNNHAK PMEIDGEVEI PSSKATVLRG HESEVFICAW NPVSDLLASG
260 270 280 290 300
SGDSTARIWN LNENSNGGST QLVLRHCIRE GGHDVPSNKD VTSLDWNTNG
310 320 330 340 350
TLLATGSYDG FARIWTEDGN LASTLGQHKG PIFALKWNRK GNYILSAGVD
360 370 380 390 400
KTTIIWDAHT GEAKQQFPFH SAPALDVDWQ NNTTFASCST DMCIHVCRLG
410 420 430 440 450
CDRPVKTFQG HTNEVNAIKW DPSGMLLASC SDDMTLKIWS MKQEVCIHDL
460 470 480 490 500
QAHNKEIYTI KWSPTGPATS NPNSNIMLAS ASFDSTVRLW DIERGVCTHT
510 520 530 540 550
LTKHQEPVYS VAFSPDGKYL ASGSFDKCVH IWNTQSGNLV HSYRGTGGIF
560 570
EVCWNARGDK VGASASDGSV CVLDLRK
Length:577
Mass (Da):62,496
Last modified:April 14, 2009 - v3
Checksum:iD830A37781E2A15C
GO
Isoform 2 (identifier: O60907-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.

Show »
Length:526
Mass (Da):57,049
Checksum:i98922F88EC42F6E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti316 – 3161T → A in BAF82098. (PubMed:14702039)Curated
Sequence conflicti390 – 3901T → A in BAF83651. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5151Missing in isoform 2. 2 PublicationsVSP_036905Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12781 mRNA. Translation: CAA73319.1.
AK289409 mRNA. Translation: BAF82098.1.
AK290962 mRNA. Translation: BAF83651.1.
AC003036 Genomic DNA. No translation available.
BC032708 mRNA. Translation: AAH32708.1.
BC052304 mRNA. Translation: AAH52304.1.
CCDSiCCDS14133.1. [O60907-1]
CCDS48078.1. [O60907-2]
RefSeqiNP_001132938.1. NM_001139466.1. [O60907-1]
NP_001132939.1. NM_001139467.1. [O60907-2]
NP_001132940.1. NM_001139468.1. [O60907-2]
NP_005638.1. NM_005647.3. [O60907-1]
UniGeneiHs.495656.

Genome annotation databases

EnsembliENST00000217964; ENSP00000217964; ENSG00000101849. [O60907-1]
ENST00000380961; ENSP00000370348; ENSG00000101849. [O60907-2]
ENST00000407597; ENSP00000385988; ENSG00000101849. [O60907-1]
ENST00000424279; ENSP00000394097; ENSG00000101849. [O60907-2]
GeneIDi6907.
KEGGihsa:6907.
UCSCiuc004csq.4. human. [O60907-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12781 mRNA. Translation: CAA73319.1 .
AK289409 mRNA. Translation: BAF82098.1 .
AK290962 mRNA. Translation: BAF83651.1 .
AC003036 Genomic DNA. No translation available.
BC032708 mRNA. Translation: AAH32708.1 .
BC052304 mRNA. Translation: AAH52304.1 .
CCDSi CCDS14133.1. [O60907-1 ]
CCDS48078.1. [O60907-2 ]
RefSeqi NP_001132938.1. NM_001139466.1. [O60907-1 ]
NP_001132939.1. NM_001139467.1. [O60907-2 ]
NP_001132940.1. NM_001139468.1. [O60907-2 ]
NP_005638.1. NM_005647.3. [O60907-1 ]
UniGenei Hs.495656.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XTC X-ray 2.22 A/B 52-141 [» ]
2XTD X-ray 3.20 A/B 52-122 [» ]
2XTE X-ray 3.90 A/B/C/D/E/F/G/H/I/J/K/L 52-141 [» ]
ProteinModelPortali O60907.
SMRi O60907. Positions 53-126, 215-576.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112770. 42 interactions.
DIPi DIP-60532N.
IntActi O60907. 10 interactions.
STRINGi 9606.ENSP00000217964.

PTM databases

PhosphoSitei O60907.

Proteomic databases

MaxQBi O60907.
PaxDbi O60907.
PRIDEi O60907.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000217964 ; ENSP00000217964 ; ENSG00000101849 . [O60907-1 ]
ENST00000380961 ; ENSP00000370348 ; ENSG00000101849 . [O60907-2 ]
ENST00000407597 ; ENSP00000385988 ; ENSG00000101849 . [O60907-1 ]
ENST00000424279 ; ENSP00000394097 ; ENSG00000101849 . [O60907-2 ]
GeneIDi 6907.
KEGGi hsa:6907.
UCSCi uc004csq.4. human. [O60907-1 ]

Organism-specific databases

CTDi 6907.
GeneCardsi GC0XP009431.
HGNCi HGNC:11585. TBL1X.
HPAi CAB005363.
MIMi 300196. gene.
neXtProti NX_O60907.
PharmGKBi PA36349.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00750000117536.
HOGENOMi HOG000220902.
HOVERGENi HBG050240.
InParanoidi O60907.
KOi K04508.
OMAi SMKQEVC.
OrthoDBi EOG79CXZ3.
PhylomeDBi O60907.
TreeFami TF323190.

Enzyme and pathway databases

Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates circadian gene expression.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_118789. REV-ERBA represses gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_228222. HDACs deacetylate histones.
REACT_24941. Circadian Clock.
REACT_267716. Orphan transporters.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinki O60907.

Miscellaneous databases

ChiTaRSi TBL1X. human.
EvolutionaryTracei O60907.
GeneWikii TBL1X.
GenomeRNAii 6907.
NextBioi 27011.
PROi O60907.
SOURCEi Search...

Gene expression databases

Bgeei O60907.
CleanExi HS_TBL1X.
ExpressionAtlasi O60907. baseline and differential.
Genevestigatori O60907.

Family and domain databases

Gene3Di 2.130.10.10. 2 hits.
InterProi IPR020472. G-protein_beta_WD-40_rep.
IPR006594. LisH_dimerisation.
IPR013720. LisH_dimerisation_subgr.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF08513. LisH. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view ]
PRINTSi PR00320. GPROTEINBRPT.
SMARTi SM00667. LisH. 1 hit.
SM00320. WD40. 8 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 1 hit.
SSF50998. SSF50998. 1 hit.
PROSITEi PS50896. LISH. 1 hit.
PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "X-linked late-onset sensorineural deafness caused by a deletion involving OA1 and a novel gene containing WD-40 repeats."
    Bassi M.T., Ramesar R.S., Caciotti B., Winship I.M., De Grandi A., Riboni M., Townes P.L., Beighton P., Ballabio A., Borsani G.
    Am. J. Hum. Genet. 64:1604-1616(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. "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] (ISOFORMS 1 AND 2).
  3. "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].
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Lymph and Pancreas.
  5. "A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness."
    Guenther M.G., Lane W.S., Fischle W., Verdin E., Lazar M.A., Shiekhattar R.
    Genes Dev. 14:1048-1057(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, COMPONENT OF THE N-COR COMPLEX WITH NCOR2 AND HDAC3.
  6. "Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3."
    Li J., Wang J., Wang J., Nawaz Z., Liu J.M., Qin J., Wong J.
    EMBO J. 19:4342-4350(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF THE N-COR COMPLEX WITH NCOR2 AND HDAC3.
  7. "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses."
    Matsuzawa S., Reed J.C.
    Mol. Cell 7:915-926(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT OF A COMPLEX WITH UBE2D1; CACYBP; SIAH1 AND APC.
  8. "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: COMPONENT OF THE N-COR COMPLEX WITH NCOR1; NCOR2; GPS2; TBL1R AND HDAC3.
  9. "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 TBL1R; CORO2A AND HDAC3, HISTONE-BINDING.
  10. "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.

Entry informationi

Entry nameiTBL1X_HUMAN
AccessioniPrimary (citable) accession number: O60907
Secondary accession number(s): A8K044, A8K4J7, Q86UY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: April 14, 2009
Last modified: November 26, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3