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Database: UniProt
Entry: BCORL_MOUSE
LinkDB: BCORL_MOUSE
Original site: 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   24-JAN-2024, entry version 120.
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   GlyGen; A2AQH4; 5 sites, 1 O-linked glycan (5 sites).
DR   iPTMnet; A2AQH4; -.
DR   PhosphoSitePlus; A2AQH4; -.
DR   EPD; A2AQH4; -.
DR   PaxDb; 10090-ENSMUSP00000122000; -.
DR   PeptideAtlas; A2AQH4; -.
DR   ProteomicsDB; 273599; -.
DR   Antibodypedia; 30129; 80 antibodies from 16 providers.
DR   DNASU; 320376; -.
DR   Ensembl; ENSMUST00000037596.13; ENSMUSP00000039898.7; ENSMUSG00000036959.16.
DR   Ensembl; ENSMUST00000136348.8; ENSMUSP00000122000.2; ENSMUSG00000036959.16.
DR   GeneID; 320376; -.
DR   KEGG; mmu:320376; -.
DR   UCSC; uc009tcc.1; mouse.
DR   AGR; MGI:2443910; -.
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; EFQSWNS; -.
DR   OrthoDB; 296979at2759; -.
DR   PhylomeDB; A2AQH4; -.
DR   TreeFam; TF333317; -.
DR   BioGRID-ORCS; 320376; 3 hits in 81 CRISPR screens.
DR   PRO; PR:A2AQH4; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; A2AQH4; Protein.
DR   Bgee; ENSMUSG00000036959; Expressed in animal zygote and 113 other cell types or 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   CDD; cd14260; PUFD_like_1; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.10.260.40; BCL-6 corepressor, PCGF1 binding domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR047144; BCOR-like.
DR   InterPro; IPR032365; PUFD.
DR   InterPro; IPR038227; PUFD_som_sf.
DR   PANTHER; PTHR24117; AGAP007537-PB; 1.
DR   PANTHER; PTHR24117:SF6; BCL-6 COREPRESSOR-LIKE PROTEIN 1; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF16553; PUFD; 1.
DR   SMART; SM00248; ANK; 3.
DR   SUPFAM; SSF48403; Ankyrin repeat; 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
//
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