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F-box-like/WD repeat-containing protein TBL1XR1 (Nuclear receptor corepressor/HDAC3 complex subunit TBLR1) (TBL1-related protein 1) (Transducin beta-like 1X-related protein 1)

 TBL1R_HUMAN             Reviewed;         514 AA.
Q9BZK7; D3DNQ9; Q14DC3; Q9H2I1; Q9H9A1;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
22-NOV-2017, entry version 163.
RecName: Full=F-box-like/WD repeat-containing protein TBL1XR1;
AltName: Full=Nuclear receptor corepressor/HDAC3 complex subunit TBLR1;
AltName: Full=TBL1-related protein 1;
AltName: Full=Transducin beta-like 1X-related protein 1;
Name=TBL1XR1; Synonyms=IRA1, TBLR1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
COMPONENT OF THE N-COR COMPLEX WITH NCOR1; NCOR2; GPS2; TBL1X AND
HDAC3.
PubMed=11931768; DOI=10.1016/S1097-2765(02)00468-9;
Zhang J., Kalkum M., Chait B.T., Roeder R.G.;
"The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK
pathway through the integral subunit GPS2.";
Mol. Cell 9:611-623(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11063877; DOI=10.1016/S0301-472X(00)00539-7;
Zhang X., Dormady S.P., Basch R.S.;
"Identification of four human cDNAs that are differentially expressed
by early hematopoietic progenitors.";
Exp. Hematol. 28:1286-1296(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Adrenal cortex, and Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
COMPONENT OF THE N-COR COMPLEX WITH TBL1X; CORO2A AND HDAC3, AND
HISTONE-BINDING.
PubMed=12628926; DOI=10.1093/emboj/cdg120;
Yoon H.-G., Chan D.W., Huang Z.-Q., Li J., Fondell J.D., Qin J.,
Wong J.;
"Purification and functional characterization of the human N-CoR
complex: the roles of HDAC3, TBL1 and TBLR1.";
EMBO J. 22:1336-1346(2003).
[7]
FUNCTION, AND RECRUITMENT OF 19S PROTEASOME COMPLEX.
PubMed=14980219; DOI=10.1016/S0092-8674(04)00133-3;
Perissi V., Aggarwal A., Glass C.K., Rose D.W., Rosenfeld M.G.;
"A corepressor/coactivator exchange complex required for
transcriptional activation by nuclear receptors and other regulated
transcription factors.";
Cell 116:511-526(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
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.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
INVOLVEMENT IN MRD41, AND VARIANT MRD41 PRO-282.
PubMed=22495309; DOI=10.1038/nature10989;
O'Roak B.J., Vives L., Girirajan S., Karakoc E., Krumm N., Coe B.P.,
Levy R., Ko A., Lee C., Smith J.D., Turner E.H., Stanaway I.B.,
Vernot B., Malig M., Baker C., Reilly B., Akey J.M., Borenstein E.,
Rieder M.J., Nickerson D.A., Bernier R., Shendure J., Eichler E.E.;
"Sporadic autism exomes reveal a highly interconnected protein network
of de novo mutations.";
Nature 485:246-250(2012).
[15]
INVOLVEMENT IN MRD41.
PubMed=23160955; DOI=10.1126/science.1227764;
O'Roak B.J., Vives L., Fu W., Egertson J.D., Stanaway I.B.,
Phelps I.G., Carvill G., Kumar A., Lee C., Ankenman K., Munson J.,
Hiatt J.B., Turner E.H., Levy R., O'Day D.R., Krumm N., Coe B.P.,
Martin B.K., Borenstein E., Nickerson D.A., Mefford H.C., Doherty D.,
Akey J.M., Bernier R., Eichler E.E., Shendure J.;
"Multiplex targeted sequencing identifies recurrently mutated genes in
autism spectrum disorders.";
Science 338:1619-1622(2012).
[16]
INVOLVEMENT IN MRD41, VARIANT MRD41 ASP-70, AND VARIANTS SER-116;
GLU-405 AND SER-407.
PubMed=25102098; DOI=10.1038/jhg.2014.71;
Saitsu H., Tohyama J., Walsh T., Kato M., Kobayashi Y., Lee M.,
Tsurusaki Y., Miyake N., Goto Y., Nishino I., Ohtake A., King M.C.,
Matsumoto N.;
"A girl with West syndrome and autistic features harboring a de novo
TBL1XR1 mutation.";
J. Hum. Genet. 59:581-583(2014).
[17]
INVOLVEMENT IN MRD41, AND VARIANT MRD41 CYS-245.
PubMed=27133561; DOI=10.1002/ajmg.a.37684;
FORGE Canada Consortium;
Armour C.M., Smith A., Hartley T., Chardon J.W., Sawyer S.,
Schwartzentruber J., Hennekam R., Majewski J., Bulman D.E., Suri M.,
Boycott K.M.;
"Syndrome disintegration: Exome sequencing reveals that Fitzsimmons
syndrome is a co-occurrence of multiple events.";
Am. J. Med. Genet. A 170:1820-1825(2016).
[18]
TISSUE SPECIFICITY, INVOLVEMENT IN PRPTS, VARIANT PRPTS CYS-446, AND
CHARACTERIZATION OF VARIANT PRPTS CYS-446.
PubMed=26769062; DOI=10.1136/jmedgenet-2015-103233;
Heinen C.A., Jongejan A., Watson P.J., Redeker B., Boelen A.,
Boudzovitch-Surovtseva O., Forzano F., Hordijk R., Kelley R.,
Olney A.H., Pierpont M.E., Schaefer G.B., Stewart F.,
van Trotsenburg A.S., Fliers E., Schwabe J.W., Hennekam R.C.;
"A specific mutation in TBL1XR1 causes Pierpont syndrome.";
J. Med. Genet. 53:330-337(2016).
[19]
ERRATUM.
PubMed=27221108; DOI=10.1136/jmedgenet-2015-103233corr1;
Heinen C.A., Jongejan A., Watson P.J., Redeker B., Boelen A.,
Boudzovitch-Surovtseva O., Forzano F., Hordijk R., Kelley R.,
Olney A.H., Pierpont M.E., Schaefer G.B., Stewart F.,
van Trotsenburg A.S., Fliers E., Schwabe J.W., Hennekam R.C.;
J. Med. Genet. 53:430-430(2016).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-277, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- 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.
{ECO:0000269|PubMed:14980219}.
-!- SUBUNIT: Component of the N-Cor repressor complex, at least
composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1XR1, CORO2A and GPS2
(PubMed:11931768). Probable component of some E3 ubiquitin ligase
complex. Interacts with histones H2B and H4 (PubMed:12628926).
Interacts with MECP2; bridges interaction between MECP2 and NCOR1
(By similarity). {ECO:0000250|UniProtKB:Q8BHJ5,
ECO:0000269|PubMed:11931768, ECO:0000269|PubMed:12628926}.
-!- INTERACTION:
P36404:ARL2; NbExp=3; IntAct=EBI-765729, EBI-752365;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- TISSUE SPECIFICITY: Widely expressed including the pituitary,
hypothalamus, white and brown adipose tissue, muscle and liver.
{ECO:0000269|PubMed:26769062}.
-!- 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. {ECO:0000250}.
-!- DISEASE: Pierpont syndrome (PRPTS) [MIM:602342]: An autosomal
dominant syndrome characterized by multiple congenital anomalies,
global developmental delay, learning disability, palmar and
plantar fat pads, and distinctive facial characteristics,
especially when smiling. {ECO:0000269|PubMed:26769062}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Mental retardation, autosomal dominant 41 (MRD41)
[MIM:616944]: A form of mental retardation, a disorder
characterized by significantly below average general intellectual
functioning associated with impairments in adaptive behavior and
manifested during the developmental period. MRD41 patients
manifest delayed psychomotor development, variable severity of
intellectual disability, and delayed language. Non-specific
dysmorphic features and autistic behavior is observed in some
patients. {ECO:0000269|PubMed:22495309,
ECO:0000269|PubMed:23160955, ECO:0000269|PubMed:25102098,
ECO:0000269|PubMed:27133561}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the WD repeat EBI family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH60320.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AF314544; AAK00301.1; -; mRNA.
EMBL; AF268193; AAG44736.1; -; mRNA.
EMBL; AK022956; BAB14331.1; -; mRNA.
EMBL; CH471052; EAW78438.1; -; Genomic_DNA.
EMBL; BC060320; AAH60320.1; ALT_SEQ; mRNA.
EMBL; BC113421; AAI13422.1; -; mRNA.
CCDS; CCDS46961.1; -.
RefSeq; NP_001308122.1; NM_001321193.1.
RefSeq; NP_001308123.1; NM_001321194.1.
RefSeq; NP_001308124.1; NM_001321195.1.
RefSeq; NP_078941.2; NM_024665.5.
RefSeq; XP_005247832.1; XM_005247775.2.
RefSeq; XP_006713809.1; XM_006713746.1.
RefSeq; XP_011511443.1; XM_011513141.1.
RefSeq; XP_011511444.1; XM_011513142.2.
RefSeq; XP_011511445.1; XM_011513143.2.
RefSeq; XP_016862674.1; XM_017007185.1.
UniGene; Hs.714201; -.
UniGene; Hs.715026; -.
PDB; 4LG9; X-ray; 2.28 A; A=134-514.
PDBsum; 4LG9; -.
ProteinModelPortal; Q9BZK7; -.
SMR; Q9BZK7; -.
BioGrid; 122834; 72.
CORUM; Q9BZK7; -.
DIP; DIP-34582N; -.
IntAct; Q9BZK7; 32.
MINT; MINT-2816883; -.
STRING; 9606.ENSP00000405574; -.
iPTMnet; Q9BZK7; -.
PhosphoSitePlus; Q9BZK7; -.
BioMuta; TBL1XR1; -.
DMDM; 23396874; -.
EPD; Q9BZK7; -.
MaxQB; Q9BZK7; -.
PaxDb; Q9BZK7; -.
PeptideAtlas; Q9BZK7; -.
PRIDE; Q9BZK7; -.
Ensembl; ENST00000430069; ENSP00000405574; ENSG00000177565.
Ensembl; ENST00000457928; ENSP00000413251; ENSG00000177565.
GeneID; 79718; -.
KEGG; hsa:79718; -.
UCSC; uc003fiw.5; human.
CTD; 79718; -.
DisGeNET; 79718; -.
EuPathDB; HostDB:ENSG00000177565.15; -.
GeneCards; TBL1XR1; -.
H-InvDB; HIX0147994; -.
HGNC; HGNC:29529; TBL1XR1.
HPA; HPA019182; -.
MalaCards; TBL1XR1; -.
MIM; 602342; phenotype.
MIM; 608628; gene.
MIM; 616944; phenotype.
neXtProt; NX_Q9BZK7; -.
OpenTargets; ENSG00000177565; -.
Orphanet; 520; Acute promyelocytic leukemia.
PharmGKB; PA134928556; -.
eggNOG; ENOG410IQU2; Eukaryota.
eggNOG; COG2319; LUCA.
GeneTree; ENSGT00890000139430; -.
HOGENOM; HOG000220902; -.
HOVERGEN; HBG050240; -.
InParanoid; Q9BZK7; -.
KO; K04508; -.
OMA; KWDPQGQ; -.
OrthoDB; EOG091G04MW; -.
PhylomeDB; Q9BZK7; -.
TreeFam; TF323190; -.
Reactome; R-HSA-1368082; RORA activates gene expression.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-8951671; RUNX3 regulates YAP1-mediated transcription.
SignaLink; Q9BZK7; -.
SIGNOR; Q9BZK7; -.
ChiTaRS; TBL1XR1; human.
GeneWiki; TBL1XR1; -.
GenomeRNAi; 79718; -.
PMAP-CutDB; Q9BZK7; -.
PRO; PR:Q9BZK7; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000177565; -.
CleanEx; HS_TBL1XR1; -.
ExpressionAtlas; Q9BZK7; baseline and differential.
Genevisible; Q9BZK7; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
GO; GO:0017053; C:transcriptional repressor complex; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0060613; P:fat pad development; IEA:Ensembl.
GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
GO; GO:0016042; P:lipid catabolic process; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0030814; P:regulation of cAMP metabolic process; IEA:Ensembl.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0090207; P:regulation of triglyceride metabolic process; IEA:Ensembl.
GO; GO:0002021; P:response to dietary excess; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0050872; P:white fat cell differentiation; IEA:Ensembl.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR006594; LisH.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF08513; LisH; 1.
Pfam; PF00400; WD40; 6.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00667; LisH; 1.
SMART; SM00320; WD40; 8.
SUPFAM; SSF50978; SSF50978; 2.
PROSITE; PS50896; LISH; 1.
PROSITE; PS00678; WD_REPEATS_1; 4.
PROSITE; PS50082; WD_REPEATS_2; 6.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Chromatin regulator;
Complete proteome; Disease mutation; Isopeptide bond;
Mental retardation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Ubl conjugation pathway;
WD repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 514 F-box-like/WD repeat-containing protein
TBL1XR1.
/FTId=PRO_0000051266.
DOMAIN 4 36 LisH. {ECO:0000255|PROSITE-
ProRule:PRU00126}.
DOMAIN 41 86 F-box-like.
REPEAT 167 206 WD 1.
REPEAT 223 262 WD 2.
REPEAT 264 303 WD 3.
REPEAT 306 344 WD 4.
REPEAT 347 386 WD 5.
REPEAT 389 437 WD 6.
REPEAT 440 479 WD 7.
REPEAT 481 513 WD 8.
COMPBIAS 108 118 Poly-Ala.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 102 102 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BHJ5}.
MOD_RES 119 119 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 277 277 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 70 70 G -> D (in MRD41; dbSNP:rs786205859).
{ECO:0000269|PubMed:25102098}.
/FTId=VAR_076753.
VARIANT 116 116 A -> S (in dbSNP:rs372813783).
{ECO:0000269|PubMed:25102098}.
/FTId=VAR_076754.
VARIANT 245 245 Y -> C (in MRD41; dbSNP:rs878854401).
{ECO:0000269|PubMed:27133561}.
/FTId=VAR_076755.
VARIANT 282 282 L -> P (in MRD41).
{ECO:0000269|PubMed:22495309}.
/FTId=VAR_076756.
VARIANT 405 405 G -> E (found in a patient with epilepsy;
unknown pathological significance;
dbSNP:rs747932785).
{ECO:0000269|PubMed:25102098}.
/FTId=VAR_076757.
VARIANT 407 407 N -> S (found in a patient with epilepsy;
unknown pathological significance;
dbSNP:rs781011308).
{ECO:0000269|PubMed:25102098}.
/FTId=VAR_076758.
VARIANT 446 446 Y -> C (in PRPTS; does not affect
assembly into the N-Cor repressor
complex; dbSNP:rs878854402).
{ECO:0000269|PubMed:26769062}.
/FTId=VAR_076759.
CONFLICT 31 31 E -> K (in Ref. 2; AAG44736).
{ECO:0000305}.
CONFLICT 59 59 Y -> H (in Ref. 3; BAB14331).
{ECO:0000305}.
CONFLICT 389 389 A -> Q (in Ref. 2; AAG44736).
{ECO:0000305}.
HELIX 159 161 {ECO:0000244|PDB:4LG9}.
STRAND 162 165 {ECO:0000244|PDB:4LG9}.
STRAND 172 177 {ECO:0000244|PDB:4LG9}.
STRAND 179 188 {ECO:0000244|PDB:4LG9}.
STRAND 191 197 {ECO:0000244|PDB:4LG9}.
STRAND 208 212 {ECO:0000244|PDB:4LG9}.
STRAND 228 233 {ECO:0000244|PDB:4LG9}.
STRAND 237 244 {ECO:0000244|PDB:4LG9}.
STRAND 247 253 {ECO:0000244|PDB:4LG9}.
STRAND 258 264 {ECO:0000244|PDB:4LG9}.
STRAND 269 274 {ECO:0000244|PDB:4LG9}.
STRAND 276 285 {ECO:0000244|PDB:4LG9}.
STRAND 290 294 {ECO:0000244|PDB:4LG9}.
TURN 295 298 {ECO:0000244|PDB:4LG9}.
STRAND 299 304 {ECO:0000244|PDB:4LG9}.
STRAND 311 326 {ECO:0000244|PDB:4LG9}.
STRAND 331 335 {ECO:0000244|PDB:4LG9}.
STRAND 342 345 {ECO:0000244|PDB:4LG9}.
STRAND 352 357 {ECO:0000244|PDB:4LG9}.
STRAND 361 368 {ECO:0000244|PDB:4LG9}.
STRAND 371 377 {ECO:0000244|PDB:4LG9}.
STRAND 384 388 {ECO:0000244|PDB:4LG9}.
STRAND 394 399 {ECO:0000244|PDB:4LG9}.
STRAND 406 408 {ECO:0000244|PDB:4LG9}.
STRAND 415 419 {ECO:0000244|PDB:4LG9}.
STRAND 424 428 {ECO:0000244|PDB:4LG9}.
TURN 429 432 {ECO:0000244|PDB:4LG9}.
STRAND 433 438 {ECO:0000244|PDB:4LG9}.
STRAND 445 450 {ECO:0000244|PDB:4LG9}.
STRAND 454 461 {ECO:0000244|PDB:4LG9}.
STRAND 464 470 {ECO:0000244|PDB:4LG9}.
TURN 471 473 {ECO:0000244|PDB:4LG9}.
STRAND 476 481 {ECO:0000244|PDB:4LG9}.
STRAND 486 491 {ECO:0000244|PDB:4LG9}.
STRAND 495 502 {ECO:0000244|PDB:4LG9}.
STRAND 507 511 {ECO:0000244|PDB:4LG9}.
SEQUENCE 514 AA; 55595 MW; 0B556D2EE4BA796D CRC64;
MSISSDEVNF LVYRYLQESG FSHSAFTFGI ESHISQSNIN GALVPPAALI SIIQKGLQYV
EAEVSINEDG TLFDGRPIES LSLIDAVMPD VVQTRQQAYR DKLAQQQAAA AAAAAAAASQ
QGSAKNGENT ANGEENGAHT IANNHTDMME VDGDVEIPPN KAVVLRGHES EVFICAWNPV
SDLLASGSGD STARIWNLSE NSTSGSTQLV LRHCIREGGQ DVPSNKDVTS LDWNSEGTLL
ATGSYDGFAR IWTKDGNLAS TLGQHKGPIF ALKWNKKGNF ILSAGVDKTT IIWDAHTGEA
KQQFPFHSAP ALDVDWQSNN TFASCSTDMC IHVCKLGQDR PIKTFQGHTN EVNAIKWDPT
GNLLASCSDD MTLKIWSMKQ DNCVHDLQAH NKEIYTIKWS PTGPGTNNPN ANLMLASASF
DSTVRLWDVD RGICIHTLTK HQEPVYSVAF SPDGRYLASG SFDKCVHIWN TQTGALVHSY
RGTGGIFEVC WNAAGDKVGA SASDGSVCVL DLRK


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