ID   TBL1R_HUMAN             Reviewed;         514 AA.
AC   Q9BZK7; D3DNQ9; Q14DC3; Q9H2I1; Q9H9A1;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 202.
DE   RecName: Full=F-box-like/WD repeat-containing protein TBL1XR1;
DE   AltName: Full=Nuclear receptor corepressor/HDAC3 complex subunit TBLR1;
DE   AltName: Full=TBL1-related protein 1;
DE   AltName: Full=Transducin beta-like 1X-related protein 1;
GN   Name=TBL1XR1; Synonyms=IRA1, TBLR1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   COMPONENT OF THE N-COR COMPLEX WITH NCOR1; NCOR2; GPS2; TBL1X AND HDAC3.
RX   PubMed=11931768; DOI=10.1016/s1097-2765(02)00468-9;
RA   Zhang J., Kalkum M., Chait B.T., Roeder R.G.;
RT   "The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK
RT   pathway through the integral subunit GPS2.";
RL   Mol. Cell 9:611-623(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11063877; DOI=10.1016/s0301-472x(00)00539-7;
RA   Zhang X., Dormady S.P., Basch R.S.;
RT   "Identification of four human cDNAs that are differentially expressed by
RT   early hematopoietic progenitors.";
RL   Exp. Hematol. 28:1286-1296(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Adrenal cortex, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   COMPONENT OF THE N-COR COMPLEX WITH TBL1X; CORO2A AND HDAC3, AND
RP   HISTONE-BINDING.
RX   PubMed=12628926; DOI=10.1093/emboj/cdg120;
RA   Yoon H.-G., Chan D.W., Huang Z.-Q., Li J., Fondell J.D., Qin J., Wong J.;
RT   "Purification and functional characterization of the human N-CoR complex:
RT   the roles of HDAC3, TBL1 and TBLR1.";
RL   EMBO J. 22:1336-1346(2003).
RN   [7]
RP   FUNCTION, AND RECRUITMENT OF 19S PROTEASOME COMPLEX.
RX   PubMed=14980219; DOI=10.1016/s0092-8674(04)00133-3;
RA   Perissi V., Aggarwal A., Glass C.K., Rose D.W., Rosenfeld M.G.;
RT   "A corepressor/coactivator exchange complex required for transcriptional
RT   activation by nuclear receptors and other regulated transcription
RT   factors.";
RL   Cell 116:511-526(2004).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [12]
RP   INVOLVEMENT IN MRD41, AND VARIANT MRD41 PRO-282.
RX   PubMed=22495309; DOI=10.1038/nature10989;
RA   O'Roak B.J., Vives L., Girirajan S., Karakoc E., Krumm N., Coe B.P.,
RA   Levy R., Ko A., Lee C., Smith J.D., Turner E.H., Stanaway I.B., Vernot B.,
RA   Malig M., Baker C., Reilly B., Akey J.M., Borenstein E., Rieder M.J.,
RA   Nickerson D.A., Bernier R., Shendure J., Eichler E.E.;
RT   "Sporadic autism exomes reveal a highly interconnected protein network of
RT   de novo mutations.";
RL   Nature 485:246-250(2012).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [14]
RP   INVOLVEMENT IN MRD41.
RX   PubMed=23160955; DOI=10.1126/science.1227764;
RA   O'Roak B.J., Vives L., Fu W., Egertson J.D., Stanaway I.B., Phelps I.G.,
RA   Carvill G., Kumar A., Lee C., Ankenman K., Munson J., Hiatt J.B.,
RA   Turner E.H., Levy R., O'Day D.R., Krumm N., Coe B.P., Martin B.K.,
RA   Borenstein E., Nickerson D.A., Mefford H.C., Doherty D., Akey J.M.,
RA   Bernier R., Eichler E.E., Shendure J.;
RT   "Multiplex targeted sequencing identifies recurrently mutated genes in
RT   autism spectrum disorders.";
RL   Science 338:1619-1622(2012).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [16]
RP   INVOLVEMENT IN MRD41, VARIANT MRD41 ASP-70, AND VARIANTS SER-116; GLU-405
RP   AND SER-407.
RX   PubMed=25102098; DOI=10.1038/jhg.2014.71;
RA   Saitsu H., Tohyama J., Walsh T., Kato M., Kobayashi Y., Lee M.,
RA   Tsurusaki Y., Miyake N., Goto Y., Nishino I., Ohtake A., King M.C.,
RA   Matsumoto N.;
RT   "A girl with West syndrome and autistic features harboring a de novo
RT   TBL1XR1 mutation.";
RL   J. Hum. Genet. 59:581-583(2014).
RN   [17]
RP   INVOLVEMENT IN MRD41, AND VARIANT MRD41 CYS-245.
RX   PubMed=27133561; DOI=10.1002/ajmg.a.37684;
RG   FORGE Canada Consortium;
RA   Armour C.M., Smith A., Hartley T., Chardon J.W., Sawyer S.,
RA   Schwartzentruber J., Hennekam R., Majewski J., Bulman D.E., Suri M.,
RA   Boycott K.M.;
RT   "Syndrome disintegration: Exome sequencing reveals that Fitzsimmons
RT   syndrome is a co-occurrence of multiple events.";
RL   Am. J. Med. Genet. A 170:1820-1825(2016).
RN   [18]
RP   INTERACTION WITH USP44.
RX   PubMed=27880911; DOI=10.1016/j.celrep.2016.10.076;
RA   Lan X., Atanassov B.S., Li W., Zhang Y., Florens L., Mohan R.D.,
RA   Galardy P.J., Washburn M.P., Workman J.L., Dent S.Y.R.;
RT   "USP44 Is an Integral Component of N-CoR that Contributes to Gene
RT   Repression by Deubiquitinating Histone H2B.";
RL   Cell Rep. 17:2382-2393(2016).
RN   [19]
RP   TISSUE SPECIFICITY, INVOLVEMENT IN PRPTS, VARIANT PRPTS CYS-446, AND
RP   CHARACTERIZATION OF VARIANT PRPTS CYS-446.
RX   PubMed=26769062; DOI=10.1136/jmedgenet-2015-103233;
RA   Heinen C.A., Jongejan A., Watson P.J., Redeker B., Boelen A.,
RA   Boudzovitch-Surovtseva O., Forzano F., Hordijk R., Kelley R., Olney A.H.,
RA   Pierpont M.E., Schaefer G.B., Stewart F., van Trotsenburg A.S., Fliers E.,
RA   Schwabe J.W., Hennekam R.C.;
RT   "A specific mutation in TBL1XR1 causes Pierpont syndrome.";
RL   J. Med. Genet. 53:330-337(2016).
RN   [20]
RP   ERRATUM OF PUBMED:26769062.
RX   PubMed=27221108; DOI=10.1136/jmedgenet-2015-103233corr1;
RA   Heinen C.A., Jongejan A., Watson P.J., Redeker B., Boelen A.,
RA   Boudzovitch-Surovtseva O., Forzano F., Hordijk R., Kelley R., Olney A.H.,
RA   Pierpont M.E., Schaefer G.B., Stewart F., van Trotsenburg A.S., Fliers E.,
RA   Schwabe J.W., Hennekam R.C.;
RL   J. Med. Genet. 53:430-430(2016).
RN   [21]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-277, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: F-box-like protein involved in the recruitment of the
CC       ubiquitin/19S proteasome complex to nuclear receptor-regulated
CC       transcription units. Plays an essential role in transcription
CC       activation mediated by nuclear receptors. Probably acts as integral
CC       component of the N-Cor corepressor complex that mediates the
CC       recruitment of the 19S proteasome complex, leading to the subsequent
CC       proteasomal degradation of N-Cor complex, thereby allowing cofactor
CC       exchange, and transcription activation. {ECO:0000269|PubMed:14980219}.
CC   -!- SUBUNIT: Component of the N-Cor repressor complex, at least composed of
CC       NCOR1, NCOR2, HDAC3, TBL1X, TBL1XR1, CORO2A and GPS2 (PubMed:11931768).
CC       Probable component of some E3 ubiquitin ligase complex. Interacts with
CC       histones H2B and H4 (PubMed:12628926). Interacts with MECP2; bridges
CC       interaction between MECP2 and NCOR1 (By similarity). Interacts with
CC       USP44 (PubMed:27880911). {ECO:0000250|UniProtKB:Q8BHJ5,
CC       ECO:0000269|PubMed:11931768, ECO:0000269|PubMed:12628926,
CC       ECO:0000269|PubMed:27880911}.
CC   -!- INTERACTION:
CC       Q9BZK7; P36404: ARL2; NbExp=4; IntAct=EBI-765729, EBI-752365;
CC       Q9BZK7; P54253: ATXN1; NbExp=6; IntAct=EBI-765729, EBI-930964;
CC       Q9BZK7; O14645: DNALI1; NbExp=3; IntAct=EBI-765729, EBI-395638;
CC       Q9BZK7; O14901: KLF11; NbExp=3; IntAct=EBI-765729, EBI-948266;
CC       Q9BZK7; P00441: SOD1; NbExp=3; IntAct=EBI-765729, EBI-990792;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Widely expressed including the pituitary,
CC       hypothalamus, white and brown adipose tissue, muscle and liver.
CC       {ECO:0000269|PubMed:26769062}.
CC   -!- DOMAIN: The F-box-like domain is related to the F-box domain, and
CC       apparently displays the same function as component of ubiquitin E3
CC       ligase complexes. {ECO:0000250}.
CC   -!- DISEASE: Pierpont syndrome (PRPTS) [MIM:602342]: An autosomal dominant
CC       syndrome characterized by multiple congenital anomalies, global
CC       developmental delay, learning disability, palmar and plantar fat pads,
CC       and distinctive facial characteristics, especially when smiling.
CC       {ECO:0000269|PubMed:26769062}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Intellectual developmental disorder, autosomal dominant 41
CC       (MRD41) [MIM:616944]: A disorder characterized by significantly below
CC       average general intellectual functioning associated with impairments in
CC       adaptive behavior and manifested during the developmental period. MRD41
CC       patients manifest delayed psychomotor development, variable severity of
CC       intellectual disability, and delayed language. Non-specific dysmorphic
CC       features and autistic behavior is observed in some patients.
CC       {ECO:0000269|PubMed:22495309, ECO:0000269|PubMed:23160955,
CC       ECO:0000269|PubMed:25102098, ECO:0000269|PubMed:27133561}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the WD repeat EBI family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH60320.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AF314544; AAK00301.1; -; mRNA.
DR   EMBL; AF268193; AAG44736.1; -; mRNA.
DR   EMBL; AK022956; BAB14331.1; -; mRNA.
DR   EMBL; CH471052; EAW78438.1; -; Genomic_DNA.
DR   EMBL; BC060320; AAH60320.1; ALT_SEQ; mRNA.
DR   EMBL; BC113421; AAI13422.1; -; mRNA.
DR   CCDS; CCDS46961.1; -.
DR   RefSeq; NP_001308122.1; NM_001321193.1.
DR   RefSeq; NP_001308123.1; NM_001321194.1.
DR   RefSeq; NP_001308124.1; NM_001321195.1.
DR   RefSeq; NP_078941.2; NM_024665.5.
DR   RefSeq; XP_005247832.1; XM_005247775.2.
DR   RefSeq; XP_006713809.1; XM_006713746.1.
DR   RefSeq; XP_011511443.1; XM_011513141.1.
DR   RefSeq; XP_011511444.1; XM_011513142.2.
DR   RefSeq; XP_011511445.1; XM_011513143.2.
DR   RefSeq; XP_016862674.1; XM_017007185.1.
DR   PDB; 4LG9; X-ray; 2.28 A; A=134-514.
DR   PDBsum; 4LG9; -.
DR   AlphaFoldDB; Q9BZK7; -.
DR   SMR; Q9BZK7; -.
DR   BioGRID; 122834; 199.
DR   CORUM; Q9BZK7; -.
DR   DIP; DIP-34582N; -.
DR   IntAct; Q9BZK7; 58.
DR   MINT; Q9BZK7; -.
DR   STRING; 9606.ENSP00000405574; -.
DR   GlyGen; Q9BZK7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BZK7; -.
DR   PhosphoSitePlus; Q9BZK7; -.
DR   BioMuta; TBL1XR1; -.
DR   DMDM; 23396874; -.
DR   EPD; Q9BZK7; -.
DR   jPOST; Q9BZK7; -.
DR   MassIVE; Q9BZK7; -.
DR   MaxQB; Q9BZK7; -.
DR   PaxDb; 9606-ENSP00000405574; -.
DR   PeptideAtlas; Q9BZK7; -.
DR   ProteomicsDB; 79864; -.
DR   Pumba; Q9BZK7; -.
DR   Antibodypedia; 9317; 410 antibodies from 33 providers.
DR   DNASU; 79718; -.
DR   Ensembl; ENST00000352800.10; ENSP00000263964.11; ENSG00000177565.19.
DR   Ensembl; ENST00000422066.6; ENSP00000398477.2; ENSG00000177565.19.
DR   Ensembl; ENST00000422442.6; ENSP00000387849.3; ENSG00000177565.19.
DR   Ensembl; ENST00000430069.5; ENSP00000405574.1; ENSG00000177565.19.
DR   Ensembl; ENST00000457928.7; ENSP00000413251.3; ENSG00000177565.19.
DR   Ensembl; ENST00000673974.1; ENSP00000501274.1; ENSG00000177565.19.
DR   Ensembl; ENST00000704383.1; ENSP00000515885.1; ENSG00000177565.19.
DR   Ensembl; ENST00000704384.1; ENSP00000515886.1; ENSG00000177565.19.
DR   Ensembl; ENST00000704385.1; ENSP00000515887.1; ENSG00000177565.19.
DR   GeneID; 79718; -.
DR   KEGG; hsa:79718; -.
DR   MANE-Select; ENST00000457928.7; ENSP00000413251.3; NM_024665.7; NP_078941.2.
DR   UCSC; uc003fiw.5; human.
DR   AGR; HGNC:29529; -.
DR   CTD; 79718; -.
DR   DisGeNET; 79718; -.
DR   GeneCards; TBL1XR1; -.
DR   HGNC; HGNC:29529; TBL1XR1.
DR   HPA; ENSG00000177565; Low tissue specificity.
DR   MalaCards; TBL1XR1; -.
DR   MIM; 602342; phenotype.
DR   MIM; 608628; gene.
DR   MIM; 616944; phenotype.
DR   neXtProt; NX_Q9BZK7; -.
DR   OpenTargets; ENSG00000177565; -.
DR   Orphanet; 520; Acute promyelocytic leukemia.
DR   Orphanet; 487825; Pierpont syndrome.
DR   PharmGKB; PA134928556; -.
DR   VEuPathDB; HostDB:ENSG00000177565; -.
DR   eggNOG; KOG0273; Eukaryota.
DR   GeneTree; ENSGT00940000153421; -.
DR   HOGENOM; CLU_007609_2_0_1; -.
DR   InParanoid; Q9BZK7; -.
DR   OMA; ANLMLAX; -.
DR   OrthoDB; 5481136at2759; -.
DR   PhylomeDB; Q9BZK7; -.
DR   TreeFam; TF323190; -.
DR   PathwayCommons; Q9BZK7; -.
DR   Reactome; R-HSA-1368082; RORA activates gene expression.
DR   Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR   Reactome; R-HSA-1989781; PPARA activates gene expression.
DR   Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR   Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR   Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR   Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR   Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR   Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR   Reactome; R-HSA-350054; Notch-HLH transcription pathway.
DR   Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR   Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha.
DR   Reactome; R-HSA-400253; Circadian Clock.
DR   Reactome; R-HSA-9022537; Loss of MECP2 binding ability to the NCoR/SMRT complex.
DR   Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity.
DR   Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR   Reactome; R-HSA-9609690; HCMV Early Events.
DR   Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR   Reactome; R-HSA-9707616; Heme signaling.
DR   SignaLink; Q9BZK7; -.
DR   SIGNOR; Q9BZK7; -.
DR   BioGRID-ORCS; 79718; 227 hits in 1173 CRISPR screens.
DR   ChiTaRS; TBL1XR1; human.
DR   GeneWiki; TBL1XR1; -.
DR   GenomeRNAi; 79718; -.
DR   Pharos; Q9BZK7; Tbio.
DR   PRO; PR:Q9BZK7; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9BZK7; Protein.
DR   Bgee; ENSG00000177565; Expressed in calcaneal tendon and 205 other cell types or tissues.
DR   ExpressionAtlas; Q9BZK7; baseline and differential.
DR   GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR   GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR   GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR   GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR   GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0060613; P:fat pad development; IEA:Ensembl.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0090207; P:regulation of triglyceride metabolic process; IEA:Ensembl.
DR   GO; GO:0002021; P:response to dietary excess; IEA:Ensembl.
DR   GO; GO:0050872; P:white fat cell differentiation; IEA:Ensembl.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 1.20.960.30; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR045183; Ebi-like.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR22846:SF40; F-BOX-LIKE_WD REPEAT-CONTAINING PROTEIN TBL1XR1; 1.
DR   PANTHER; PTHR22846; WD40 REPEAT PROTEIN; 1.
DR   Pfam; PF08513; LisH; 1.
DR   Pfam; PF00400; WD40; 7.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00667; LisH; 1.
DR   SMART; SM00320; WD40; 8.
DR   SUPFAM; SSF50978; WD40 repeat-like; 2.
DR   PROSITE; PS50896; LISH; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 4.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   Genevisible; Q9BZK7; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Chromatin regulator; Disease variant;
KW   Intellectual disability; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Ubl conjugation pathway;
KW   WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..514
FT                   /note="F-box-like/WD repeat-containing protein TBL1XR1"
FT                   /id="PRO_0000051266"
FT   DOMAIN          4..36
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   DOMAIN          41..86
FT                   /note="F-box-like"
FT   REPEAT          167..206
FT                   /note="WD 1"
FT   REPEAT          223..262
FT                   /note="WD 2"
FT   REPEAT          264..303
FT                   /note="WD 3"
FT   REPEAT          306..344
FT                   /note="WD 4"
FT   REPEAT          347..386
FT                   /note="WD 5"
FT   REPEAT          389..437
FT                   /note="WD 6"
FT   REPEAT          440..479
FT                   /note="WD 7"
FT   REPEAT          481..513
FT                   /note="WD 8"
FT   REGION          120..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         102
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BHJ5"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   CROSSLNK        277
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         70
FT                   /note="G -> D (in MRD41; dbSNP:rs786205859)"
FT                   /evidence="ECO:0000269|PubMed:25102098"
FT                   /id="VAR_076753"
FT   VARIANT         116
FT                   /note="A -> S (in dbSNP:rs372813783)"
FT                   /evidence="ECO:0000269|PubMed:25102098"
FT                   /id="VAR_076754"
FT   VARIANT         245
FT                   /note="Y -> C (in MRD41; dbSNP:rs878854401)"
FT                   /evidence="ECO:0000269|PubMed:27133561"
FT                   /id="VAR_076755"
FT   VARIANT         282
FT                   /note="L -> P (in MRD41)"
FT                   /evidence="ECO:0000269|PubMed:22495309"
FT                   /id="VAR_076756"
FT   VARIANT         405
FT                   /note="G -> E (found in a patient with epilepsy; uncertain
FT                   significance; dbSNP:rs747932785)"
FT                   /evidence="ECO:0000269|PubMed:25102098"
FT                   /id="VAR_076757"
FT   VARIANT         407
FT                   /note="N -> S (found in a patient with epilepsy; uncertain
FT                   significance; dbSNP:rs781011308)"
FT                   /evidence="ECO:0000269|PubMed:25102098"
FT                   /id="VAR_076758"
FT   VARIANT         446
FT                   /note="Y -> C (in PRPTS; does not affect assembly into the
FT                   N-Cor repressor complex; dbSNP:rs878854402)"
FT                   /evidence="ECO:0000269|PubMed:26769062"
FT                   /id="VAR_076759"
FT   CONFLICT        31
FT                   /note="E -> K (in Ref. 2; AAG44736)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        59
FT                   /note="Y -> H (in Ref. 3; BAB14331)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        389
FT                   /note="A -> Q (in Ref. 2; AAG44736)"
FT                   /evidence="ECO:0000305"
FT   HELIX           159..161
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          162..165
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          172..177
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          179..188
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          191..197
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          208..212
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          228..233
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          237..244
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          247..253
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          258..264
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          269..274
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          276..285
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          290..294
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   TURN            295..298
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          299..304
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          311..326
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          331..335
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          342..345
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          352..357
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          361..368
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          371..377
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          384..388
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          394..399
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          406..408
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          415..419
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          424..428
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   TURN            429..432
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          433..438
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          445..450
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          454..461
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          464..470
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   TURN            471..473
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          476..481
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          486..491
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          495..502
FT                   /evidence="ECO:0007829|PDB:4LG9"
FT   STRAND          507..511
FT                   /evidence="ECO:0007829|PDB:4LG9"
SQ   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
//