TBL1X_MACFA
ID TBL1X_MACFA Reviewed; 569 AA.
AC Q4R8H1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=F-box-like/WD repeat-containing protein TBL1X;
GN Name=TBL1X; ORFNames=QtsA-12504;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 corepressor complexes that mediates the recruitment of the
CC 19S proteasome complex, leading to the subsequent proteasomal
CC degradation of transcription repressor complexes, thereby allowing
CC cofactor exchange. {ECO:0000250|UniProtKB:O60907}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. Component of the N-Cor
CC repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X,
CC TBL1R, CORO2A and GPS2. Interacts with GPS2 (when sumoylated); leading
CC to protect GPS2 against degradation by the proteasome. Component of a
CC E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1,
CC APC and TBL1X (By similarity). Probably part of other corepressor
CC complexes, that do not contain NCOR1 and NCOR2. Interacts with histones
CC H2B, H3a and H4. Interacts with MECP2; recruits TBL1X to the
CC heterochromatin foci (By similarity). {ECO:0000250|UniProtKB:O60907,
CC ECO:0000250|UniProtKB:Q9QXE7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalized with
CC MECP2 to the heterochromatin foci. {ECO:0000250|UniProtKB:Q9QXE7}.
CC -!- SIMILARITY: Belongs to the WD repeat EBI family. {ECO:0000305}.
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DR EMBL; AB168481; BAE00601.1; -; mRNA.
DR RefSeq; NP_001270300.1; NM_001283371.1.
DR AlphaFoldDB; Q4R8H1; -.
DR SMR; Q4R8H1; -.
DR STRING; 9541.XP_005592988.1; -.
DR GeneID; 101866537; -.
DR CTD; 6907; -.
DR eggNOG; KOG0273; Eukaryota.
DR OrthoDB; 1463197at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045183; Ebi-like.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR22846; PTHR22846; 1.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
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.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..569
FT /note="F-box-like/WD repeat-containing protein TBL1X"
FT /id="PRO_0000370190"
FT DOMAIN 55..87
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 92..137
FT /note="F-box-like"
FT REPEAT 222..261
FT /note="WD 1"
FT REPEAT 278..317
FT /note="WD 2"
FT REPEAT 319..358
FT /note="WD 3"
FT REPEAT 361..401
FT /note="WD 4"
FT REPEAT 402..441
FT /note="WD 5"
FT REPEAT 444..492
FT /note="WD 6"
FT REPEAT 495..534
FT /note="WD 7"
FT REPEAT 536..568
FT /note="WD 8"
FT REGION 170..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 153
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHJ5"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZK7"
FT CROSSLNK 332
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BZK7"
SQ SEQUENCE 569 AA; 61930 MW; 62D0C2FBA24EEB9B CRC64;
MTELAGASSS CCHRPAGRGA MQSVLHHFQR LRGREGGSHF INTSSPRGEA KMSITSDEVN
FLVYRYLQES GFSHSAFTFG IESHISQSNI NGTLVPPAAL ISILQKGLQY VEAEISINED
GTVFDGRPIE SLSLIDAVMP DVVQTRQRAF REKLAQQQAS AAAAAAAATT SASVSQQNPS
KNREATVNGE ENRAHSVNNH AKPMEIDGEV DIPSSKATVL RGHESEVFIC AWNPVSDLLA
SGSGDSTARI WNLNENSNGG STQLVLRHCI REGGHDVPSN KDVTSLDWNT NGTLLATGSY
DGFARIWTED GNLASTLGQH KGPIFALKWN RKGNYILSAG VDKTTIIWDA HTGEAKQQFP
FHSAPALDVD WQNNMTFASC STDMCIHVCR LGCDRPVKTF QGHTNEVNAI KWDPSGMLLA
SCSDDMTLKI WSMKQEVCIH DLQAHNKEIY TIKWSPTGPA TSNPNSNIML ASASFDSTVR
LWDIERGVCT HTLTKHQEPV YSVAFSPDGR YLASGSFDKC VHIWNTQSGN LVHSYRGTGG
IFEVCWNARG DKVGASASDG SVCVLDLRK
