BCORL_MOUSE
ID BCORL_MOUSE Reviewed; 1781 AA.
AC A2AQH4; Q8BMH7; Q8BV26; Q8BW58;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=BCL-6 corepressor-like protein 1;
DE Short=BCoR-L1;
DE Short=BCoR-like protein 1;
GN Name=Bcorl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-1781.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Fetal forelimb, and Ovary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Transcriptional corepressor. May specifically inhibit gene
CC expression when recruited to promoter regions by sequence specific DNA-
CC binding proteins such as BCL6. This repression may be mediated at least
CC in part by histone deacetylase activities which can associate with this
CC corepressor (By similarity). {ECO:0000250|UniProtKB:Q5H9F3}.
CC -!- SUBUNIT: Interacts with PCGF1, forming heterodimers (By similarity).
CC The PCGF1-BCORL1 heterodimeric complex interacts with the KDM2B-SKP1
CC heterodimeric complex to form a homotetrameric polycomb repression
CC complex 1 (PRC1.1) (By similarity). Interacts with CTBP1, HDAC4, HDAC5
CC and HDAC7 (By similarity). {ECO:0000250|UniProtKB:Q5H9F3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5H9F3}.
CC -!- SIMILARITY: Belongs to the BCOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27262.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC27262.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC35708.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC38112.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL844594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK031119; BAC27262.1; ALT_SEQ; mRNA.
DR EMBL; AK054259; BAC35708.1; ALT_INIT; mRNA.
DR EMBL; AK081004; BAC38112.1; ALT_INIT; mRNA.
DR CCDS; CCDS40961.1; -.
DR RefSeq; NP_848897.3; NM_178782.4.
DR RefSeq; XP_006541560.1; XM_006541497.3.
DR RefSeq; XP_006541561.1; XM_006541498.3.
DR RefSeq; XP_006541562.1; XM_006541499.3.
DR RefSeq; XP_006541563.1; XM_006541500.3.
DR AlphaFoldDB; A2AQH4; -.
DR SMR; A2AQH4; -.
DR BioGRID; 235973; 1.
DR STRING; 10090.ENSMUSP00000122000; -.
DR iPTMnet; A2AQH4; -.
DR PhosphoSitePlus; A2AQH4; -.
DR EPD; A2AQH4; -.
DR PaxDb; A2AQH4; -.
DR PeptideAtlas; A2AQH4; -.
DR PRIDE; A2AQH4; -.
DR ProteomicsDB; 273599; -.
DR Antibodypedia; 30129; 78 antibodies from 16 providers.
DR DNASU; 320376; -.
DR Ensembl; ENSMUST00000037596; ENSMUSP00000039898; ENSMUSG00000036959.
DR Ensembl; ENSMUST00000136348; ENSMUSP00000122000; ENSMUSG00000036959.
DR GeneID; 320376; -.
DR KEGG; mmu:320376; -.
DR UCSC; uc009tcc.1; mouse.
DR CTD; 63035; -.
DR MGI; MGI:2443910; Bcorl1.
DR VEuPathDB; HostDB:ENSMUSG00000036959; -.
DR eggNOG; ENOG502QSMY; Eukaryota.
DR GeneTree; ENSGT00940000153737; -.
DR HOGENOM; CLU_003920_0_0_1; -.
DR InParanoid; A2AQH4; -.
DR OMA; EVEFQSW; -.
DR OrthoDB; 85469at2759; -.
DR PhylomeDB; A2AQH4; -.
DR TreeFam; TF333317; -.
DR BioGRID-ORCS; 320376; 3 hits in 75 CRISPR screens.
DR PRO; PR:A2AQH4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; A2AQH4; protein.
DR Bgee; ENSMUSG00000036959; Expressed in animal zygote and 111 other tissues.
DR ExpressionAtlas; A2AQH4; baseline and differential.
DR Genevisible; A2AQH4; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.10.260.40; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR032365; PUFD.
DR InterPro; IPR038227; PUFD_som_sf.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF16553; PUFD; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 2: Evidence at transcript level;
KW ANK repeat; Chromatin regulator; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1781
FT /note="BCL-6 corepressor-like protein 1"
FT /id="PRO_0000312269"
FT REPEAT 1493..1523
FT /note="ANK 1"
FT REPEAT 1527..1556
FT /note="ANK 2"
FT REPEAT 1560..1589
FT /note="ANK 3"
FT REGION 64..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1664..1781
FT /note="PCGF Ub-like fold domain (PUFD); required for the
FT interaction with the KDM2B-SKP1 heterodimeric complex"
FT /evidence="ECO:0000250|UniProtKB:Q5H9F3"
FT COMPBIAS 64..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1371..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5H9F3"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5H9F3"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5H9F3"
FT MOD_RES 1024
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5H9F3"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5H9F3"
FT CROSSLNK 741
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5H9F3"
FT CROSSLNK 1087
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5H9F3"
FT CONFLICT 1209
FT /note="A -> V (in Ref. 2; BAC27262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1781 AA; 190487 MW; C7A689F5D0A76A9F CRC64;
MISTAPLYSG VHNWTSSDRI RMCGINEERR APLSDEESTT GGCQHFGSQE FCVSSSFSKV
ELTAVGSGSN ARGTNPDGNT TEKLGHRSED QSDDPQPKMD YVGNPAEAEG LLVPLSSPGD
GLKLPTPDST EASHSRANCS WTPLSTQMSK QVDCSPAGVK ALDSRHGVGE KNTFILATLG
TGVPVEGTLP LVTTNFSQLP APICPPAPGS ASGTPSVPDP FQVPLSVPAP VPHSGLVPVQ
VATSASAPSP PLAPAAPSVP TLISDSNPLS VSASVLVPVP VSAPHSVPVP LSAPAPTPLT
VSVSAPPLAL IQAPVPPSAP TLVLASVPTP VLAPMPASTP PAAPAPPSVP MPTPTPSSGP
PSTPTLIPAF APTPVPAPTP APIFTPAPTP MPAATPAAIP TSAPIPASFS LSRVCFPAAQ
APAMQKVPLS FQPGTVLTPN QPLVYIPPPS CGQPLSVATL PTTLGVSSTL TLPVLPSYLQ
DRCLPGVLAS PDLRSYPCAF SVARPLASDS KLVSLEVNRL SCTSPSSSTN SQPAPDGVPG
PLADTSLTTA SAKVLPTSQL LLPAPSGSSV PPHPSKMPGG TDQQTEGTSV TFSPLKSPPQ
LEREMASPPE CSEMPLDLSA KSNRQKLPLP NQRKTPPMPV LTPVHTSSKA LLSTVLSRSQ
RTTQAAGSNV TSCLGSTSSP FVIFPEMVRN GDPSTWVKNS TALISTIPGT YVGVANPVPA
SLLLNKDPNL GLNRDPRHLP KQEPISIIDQ GEPKSTSATC GKKGSQAGAE GQPSTVKSRY
TPARIAPGLP GCQTKELSLW KPTGLTNMYP RCSINGKPTS TQVLPVGWSP YHQASLLSIG
ISSAGQLTPS QGVPIRPTSI VSEFSGVSPL GSSETVHGLP EGQPRPGGPF APEQDAVTKN
KNCRIAAKPY EEQVNPVLLT LSPQSGTLAL SVQPSSGDMG VNQGSEESES HLCSDSTPKM
EGPQAACGLK LAGDTKPKNQ VLATYMSHEL VLANPQNLCK MPELPLLPHD SHSKELILDV
VPSSERGPST DLSQLGSQVD LGRVKMEKAD GDVVFNLANC FRADGLPAVP QRGQAEARAN
AGQARVKRES IGVFTCKNSW QPDEETESLP PKKVKCNKEK EIEEEPRQQP PPQPHDKPMV
RSSLGSKCRK LPGDPQEPTK KSPRGALDSG KEHNGVRGKH KHRKPTKPES QPPGKRTDGH
EEGSLEKKAK NSFRDFIPVV LSTRTRSQSG SICSSFAGMA DSDMGSQEVF PTEEEEEVAP
TPAKRRKVRK TQRDTQYRSH HAQDKTLLSQ GRRHLWRARE MPWRTEAARQ MWDTNEEEED
DEEEGLVKRK KRRRQKSRKY QTGEYLIEQE EQRRKGRADS KARKQKTSSQ SSEHCLRNRN
LLLSSKAQGI SDSPNGFLPD NLEEPACLEN PEKPSGKRKC KTKHMANASE EARSKGRWSQ
QKTRSSKSPT PVKPTEPCTP SKYRSAGPEE ASESPTARQI PPEARRLIVN KNAGETLLQR
AARLGYKDVV LYCLQKHSED VNHRDNAGYT ALHEACSRGW TDILNILLQH GANVNCSSQD
GTRPVHDAVV NDNLETIWLL LSYGADPTLA TYSGQTAMKL ASSDNMKRFL SDHLSDLQGR
AEGDPRASWD FYSSSVLEKK DGFACDLLHN PPGSAEQGDD SEQDDFMFEL SDKPLLPCYN
LQVSVSRGPC NWFLFSDVLK RLKLSSRIFQ ARFPHLEITT LPKAEFYRQV ASSQLLSPAE
RPGSLEDRSP PGSSETVELV QYEPELLRLL GSEVEYQSWS S
