ID BCORL_HUMAN Reviewed; 1785 AA.
AC Q5H9F3; B5MDQ8; Q5H9F2; Q5H9F4; Q6ZVE0; Q8TEN3; Q9Y528;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 27-MAR-2024, entry version 162.
DE RecName: Full=BCL-6 corepressor-like protein 1 {ECO:0000305};
DE Short=BCoR-L1;
DE Short=BCoR-like protein 1;
GN Name=BCORL1 {ECO:0000312|HGNC:HGNC:25657};
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-1785 (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 566-1435 (ISOFORM 4).
RA Rhodes S.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1265-1785 (ISOFORM 3).
RC TISSUE=Amygdala;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTBP1; HDAC4; HDAC5 AND
RP HDAC7, MUTAGENESIS OF 623-ASP-LEU-624, AND TISSUE SPECIFICITY.
RX PubMed=17379597; DOI=10.1074/jbc.m700246200;
RA Pagan J.K., Arnold J., Hanchard K.J., Kumar R., Bruno T., Jones M.J.,
RA Richard D.J., Forrest A., Spurdle A., Verdin E., Crossley M., Fanciulli M.,
RA Chenevix-Trench G., Young D.B., Khanna K.K.;
RT "A novel corepressor, BCoR-L1, represses transcription through an
RT interaction with CtBP.";
RL J. Biol. Chem. 282:15248-15257(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-1033; SER-1162 AND
RP SER-1476, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496; SER-599; SER-1029;
RP SER-1033 AND SER-1162, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1092, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1092, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-747 AND LYS-1092, AND
RP IDENTIFICATION BY MASS 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).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1708-1822 IN COMPLEX WITH PCGF1,
RP INTERACTION WITH PCGF1, AND MUTAGENESIS OF LEU-1739.
RX PubMed=23523425; DOI=10.1016/j.str.2013.02.013;
RA Junco S.E., Wang R., Gaipa J.C., Taylor A.B., Schirf V., Gearhart M.D.,
RA Bardwell V.J., Demeler B., Hart P.J., Kim C.A.;
RT "Structure of the polycomb group protein PCGF1 in complex with BCOR reveals
RT basis for binding selectivity of PCGF homologs.";
RL Structure 21:665-671(2013).
RN [13] {ECO:0007744|PDB:5JH5}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1668-1785, AND SUBUNIT.
RX PubMed=27568929; DOI=10.1016/j.str.2016.07.011;
RA Wong S.J., Gearhart M.D., Taylor A.B., Nanyes D.R., Ha D.J., Robinson A.K.,
RA Artigas J.A., Lee O.J., Demeler B., Hart P.J., Bardwell V.J., Kim C.A.;
RT "KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires
RT Cooperation between PCGF1 and BCORL1.";
RL Structure 24:1795-1801(2016).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-832.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [15]
RP VARIANT SHUVER SER-820, AND INVOLVEMENT IN SHUVER.
RX PubMed=24123876; DOI=10.1136/jmedgenet-2013-101644;
RA Schuurs-Hoeijmakers J.H., Vulto-van Silfhout A.T., Vissers L.E.,
RA van de Vondervoort I.I., van Bon B.W., de Ligt J., Gilissen C.,
RA Hehir-Kwa J.Y., Neveling K., del Rosario M., Hira G., Reitano S.,
RA Vitello A., Failla P., Greco D., Fichera M., Galesi O., Kleefstra T.,
RA Greally M.T., Ockeloen C.W., Willemsen M.H., Bongers E.M., Janssen I.M.,
RA Pfundt R., Veltman J.A., Romano C., Willemsen M.A., van Bokhoven H.,
RA Brunner H.G., de Vries B.B., de Brouwer A.P.;
RT "Identification of pathogenic gene variants in small families with
RT intellectually disabled siblings by exome sequencing.";
RL J. Med. Genet. 50:802-811(2013).
RN [16]
RP VARIANT ILE-327.
RX PubMed=26933038; DOI=10.1161/circgenetics.115.001193;
RA Xue Y., Schoser B., Rao A.R., Quadrelli R., Vaglio A., Rupp V.,
RA Beichler C., Nelson S.F., Schapacher-Tilp G., Windpassinger C.,
RA Wilcox W.R.;
RT "Exome sequencing identified a splice site mutation in FHL1 that causes
RT Uruguay Syndrome, an X-linked disorder with skeletal muscle hypertrophy and
RT premature cardiac death.";
RL Circ. Cardiovasc. Genet. 9:130-135(2016).
RN [17]
RP VARIANTS SHUVER LEU-32; PHE-496 AND GLU-782, AND INVOLVEMENT IN SHUVER.
RX PubMed=30941876; DOI=10.1002/ajmg.a.61118;
RA Shukla A., Girisha K.M., Somashekar P.H., Nampoothiri S., McClellan R.,
RA Vernon H.J.;
RT "Variants in the transcriptional corepressor BCORL1 are associated with an
RT X-linked disorder of intellectual disability, dysmorphic features, and
RT behavioral abnormalities.";
RL Am. J. Med. Genet. A 179:870-874(2019).
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. {ECO:0000269|PubMed:17379597}.
CC -!- SUBUNIT: Interacts with PCGF1, forming heterodimers (PubMed:23523425,
CC PubMed:27568929). The PCGF1-BCORL1 heterodimeric complex interacts with
CC the KDM2B-SKP1 heterodimeric complex to form a homotetrameric polycomb
CC repression complex 1 (PRC1.1) (PubMed:27568929). Interacts with CTBP1,
CC HDAC4, HDAC5 and HDAC7 (PubMed:17379597). {ECO:0000269|PubMed:17379597,
CC ECO:0000269|PubMed:23523425, ECO:0000269|PubMed:27568929}.
CC -!- INTERACTION:
CC Q5H9F3-1; Q9BSM1-1: PCGF1; NbExp=6; IntAct=EBI-16041827, EBI-16041863;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17379597}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=Q5H9F3-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q5H9F3-1; Sequence=VSP_061440;
CC Name=4;
CC IsoId=Q5H9F3-4; Sequence=VSP_061439;
CC -!- TISSUE SPECIFICITY: Detected in testis and prostate. Detected at lower
CC levels in peripheral blood leukocytes and spleen.
CC {ECO:0000269|PubMed:17379597}.
CC -!- DISEASE: Shukla-Vernon syndrome (SHUVER) [MIM:301029]: An X-linked
CC neurodevelopmental disorder manifesting in affected males with
CC intellectual and learning disability, motor and language delay, autism
CC spectrum disorder, attention deficit and hyperactivity disorder, and
CC dysmorphic features. Some patients may have seizures and/or cerebellar
CC atrophy on brain imaging. Carrier females may have mild disease
CC manifestations. {ECO:0000269|PubMed:24123876,
CC ECO:0000269|PubMed:30941876}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the BCOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC85922.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB46626.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL034405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF459398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF459400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF510634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z82208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK074089; BAB84915.1; -; mRNA.
DR EMBL; AL096777; CAB46626.1; ALT_INIT; mRNA.
DR EMBL; AK124676; BAC85922.1; ALT_INIT; mRNA.
DR CCDS; CCDS14616.1; -. [Q5H9F3-1]
DR CCDS; CCDS94663.1; -. [Q5H9F3-3]
DR RefSeq; NP_001171701.1; NM_001184772.2. [Q5H9F3-3]
DR RefSeq; NP_068765.3; NM_021946.4. [Q5H9F3-1]
DR RefSeq; XP_005262509.2; XM_005262452.4.
DR RefSeq; XP_005262510.2; XM_005262453.4. [Q5H9F3-3]
DR RefSeq; XP_005262511.2; XM_005262454.3.
DR RefSeq; XP_005262512.2; XM_005262455.4. [Q5H9F3-3]
DR RefSeq; XP_005262513.2; XM_005262456.4. [Q5H9F3-4]
DR RefSeq; XP_006724839.1; XM_006724776.3. [Q5H9F3-3]
DR RefSeq; XP_006724840.1; XM_006724777.3. [Q5H9F3-3]
DR RefSeq; XP_016885210.1; XM_017029721.1. [Q5H9F3-3]
DR RefSeq; XP_016885211.1; XM_017029722.1. [Q5H9F3-3]
DR PDB; 4HPM; X-ray; 1.85 A; A/C=1668-1785.
DR PDB; 5JH5; X-ray; 2.55 A; D=1668-1785.
DR PDBsum; 4HPM; -.
DR PDBsum; 5JH5; -.
DR AlphaFoldDB; Q5H9F3; -.
DR SMR; Q5H9F3; -.
DR BioGRID; 121961; 77.
DR ComplexPortal; CPX-2627; Non-canonical polycomb repressive complex 1.1, RING2-PCGF1-RYBP variant.
DR DIP; DIP-60148N; -.
DR IntAct; Q5H9F3; 27.
DR MINT; Q5H9F3; -.
DR STRING; 9606.ENSP00000437775; -.
DR GlyCosmos; Q5H9F3; 5 sites, 1 glycan.
DR GlyGen; Q5H9F3; 9 sites, 1 O-linked glycan (9 sites).
DR iPTMnet; Q5H9F3; -.
DR PhosphoSitePlus; Q5H9F3; -.
DR BioMuta; BCORL1; -.
DR DMDM; 74762178; -.
DR EPD; Q5H9F3; -.
DR jPOST; Q5H9F3; -.
DR MassIVE; Q5H9F3; -.
DR MaxQB; Q5H9F3; -.
DR PaxDb; 9606-ENSP00000437775; -.
DR PeptideAtlas; Q5H9F3; -.
DR ProteomicsDB; 62886; -. [Q5H9F3-1]
DR ProteomicsDB; 62888; -. [Q5H9F3-3]
DR Pumba; Q5H9F3; -.
DR Antibodypedia; 30129; 80 antibodies from 16 providers.
DR DNASU; 63035; -.
DR Ensembl; ENST00000218147.11; ENSP00000218147.7; ENSG00000085185.16. [Q5H9F3-1]
DR Ensembl; ENST00000540052.6; ENSP00000437775.2; ENSG00000085185.16. [Q5H9F3-3]
DR GeneID; 63035; -.
DR KEGG; hsa:63035; -.
DR MANE-Select; ENST00000540052.6; ENSP00000437775.2; NM_001379451.1; NP_001366380.1.
DR UCSC; uc022cdu.1; human. [Q5H9F3-3]
DR AGR; HGNC:25657; -.
DR CTD; 63035; -.
DR DisGeNET; 63035; -.
DR GeneCards; BCORL1; -.
DR HGNC; HGNC:25657; BCORL1.
DR HPA; ENSG00000085185; Low tissue specificity.
DR MalaCards; BCORL1; -.
DR MIM; 300688; gene.
DR MIM; 301029; phenotype.
DR neXtProt; NX_Q5H9F3; -.
DR OpenTargets; ENSG00000085185; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR VEuPathDB; HostDB:ENSG00000085185; -.
DR eggNOG; ENOG502QSMY; Eukaryota.
DR GeneTree; ENSGT00940000153737; -.
DR InParanoid; Q5H9F3; -.
DR OMA; EFQSWNS; -.
DR OrthoDB; 296979at2759; -.
DR PhylomeDB; Q5H9F3; -.
DR TreeFam; TF333317; -.
DR PathwayCommons; Q5H9F3; -.
DR SignaLink; Q5H9F3; -.
DR SIGNOR; Q5H9F3; -.
DR BioGRID-ORCS; 63035; 21 hits in 794 CRISPR screens.
DR ChiTaRS; BCORL1; human.
DR GenomeRNAi; 63035; -.
DR Pharos; Q5H9F3; Tbio.
DR PRO; PR:Q5H9F3; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q5H9F3; Protein.
DR Bgee; ENSG00000085185; Expressed in cervix squamous epithelium and 191 other cell types or tissues.
DR ExpressionAtlas; Q5H9F3; baseline and differential.
DR Genevisible; Q5H9F3; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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 IDEAL; IID00623; -.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Autism spectrum disorder;
KW Chromatin regulator; Disease variant; Intellectual disability;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1785
FT /note="BCL-6 corepressor-like protein 1"
FT /id="PRO_0000312268"
FT REPEAT 1529..1558
FT /note="ANK 1"
FT REPEAT 1562..1591
FT /note="ANK 2"
FT REPEAT 1595..1623
FT /note="ANK 3"
FT REGION 65..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1668..1785
FT /note="PCGF Ub-like fold domain (PUFD); required for the
FT interaction with the KDM2B-SKP1 heterodimeric complex"
FT /evidence="ECO:0000269|PubMed:27568929"
FT MOTIF 1328..1336
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 79..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..578
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..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..1293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1459..1477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1033
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 747
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1092
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1230..1359
FT /note="Missing (in isoform 4)"
FT /id="VSP_061439"
FT VAR_SEQ 1436..1509
FT /note="Missing (in isoform 1)"
FT /id="VSP_061440"
FT VARIANT 32
FT /note="P -> L (in SHUVER; uncertain significance;
FT dbSNP:rs1603105985)"
FT /evidence="ECO:0000269|PubMed:30941876"
FT /id="VAR_082288"
FT VARIANT 111
FT /note="L -> F (in dbSNP:rs4830173)"
FT /id="VAR_061020"
FT VARIANT 209
FT /note="G -> S (in dbSNP:rs5932715)"
FT /id="VAR_037467"
FT VARIANT 327
FT /note="T -> I (found in a patient with Uruguay
FT faciocardiomusculoskeletal syndrome; uncertain
FT significance)"
FT /evidence="ECO:0000269|PubMed:26933038"
FT /id="VAR_080909"
FT VARIANT 496
FT /note="S -> F (in SHUVER; uncertain significance;
FT dbSNP:rs1057521638)"
FT /evidence="ECO:0000269|PubMed:30941876"
FT /id="VAR_082289"
FT VARIANT 782
FT /note="V -> E (in SHUVER; uncertain significance;
FT dbSNP:rs1488781894)"
FT /evidence="ECO:0000269|PubMed:30941876"
FT /id="VAR_082290"
FT VARIANT 820
FT /note="N -> S (in SHUVER; uncertain significance;
FT dbSNP:rs398123004)"
FT /evidence="ECO:0000269|PubMed:24123876"
FT /id="VAR_070559"
FT VARIANT 832
FT /note="G -> D (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_037468"
FT MUTAGEN 623..624
FT /note="DL->AS: Strongly reduced repressor activity.
FT Interferes with CTBP1 binding."
FT /evidence="ECO:0000269|PubMed:17379597"
FT MUTAGEN 1739
FT /note="L->D,R: Slightly inhibits interaction with PCGF1."
FT /evidence="ECO:0000269|PubMed:23523425"
FT CONFLICT 1638
FT /note="V -> A (in Ref. 4; BAC85922)"
FT /evidence="ECO:0000305"
FT STRAND 1670..1677
FT /evidence="ECO:0007829|PDB:4HPM"
FT STRAND 1683..1685
FT /evidence="ECO:0007829|PDB:4HPM"
FT STRAND 1694..1698
FT /evidence="ECO:0007829|PDB:4HPM"
FT HELIX 1699..1706
FT /evidence="ECO:0007829|PDB:4HPM"
FT HELIX 1710..1716
FT /evidence="ECO:0007829|PDB:4HPM"
FT STRAND 1722..1726
FT /evidence="ECO:0007829|PDB:4HPM"
FT HELIX 1727..1734
FT /evidence="ECO:0007829|PDB:4HPM"
FT STRAND 1738..1740
FT /evidence="ECO:0007829|PDB:4HPM"
FT TURN 1742..1744
FT /evidence="ECO:0007829|PDB:4HPM"
FT STRAND 1760..1765
FT /evidence="ECO:0007829|PDB:4HPM"
FT HELIX 1768..1773
FT /evidence="ECO:0007829|PDB:4HPM"
FT STRAND 1777..1781
FT /evidence="ECO:0007829|PDB:4HPM"
SQ SEQUENCE 1785 AA; 190561 MW; DD62FFFEC2DE1E9C CRC64;
MISTAPLYSG VHNWTSSDRI RMCGINEERR APLSDEESTT GDCQHFGSQE FCVSSSFSKV
ELTAVGSGSN ARGADPDGSA TEKLGHKSED KPDDPQPKMD YAGNVAEAEG LLVPLSSPGD
GLKLPASDSA EASNSRADCS WTPLNTQMSK QVDCSPAGVK ALDSRQGVGE KNTFILATLG
TGVPVEGTLP LVTTNFSPLP APICPPAPGS ASVPHSVPDA FQVPLSVPAP VPHSGLVPVQ
VATSVPAPSP PLAPVPALAP APPSVPTLIS DSNPLSVSAS VLVPVPASAP PSGPVPLSAP
APAPLSVPVS APPLALIQAP VPPSAPTLVL APVPTPVLAP MPASTPPAAP APPSVPMPTP
TPSSGPPSTP TLIPAFAPTP VPAPTPAPIF TPAPTPMPAA TPAAIPTSAP IPASFSLSRV
CFPAAQAPAM QKVPLSFQPG TVLTPSQPLV YIPPPSCGQP LSVATLPTTL GVSSTLTLPV
LPSYLQDRCL PGVLASPELR SYPYAFSVAR PLTSDSKLVS LEVNRLPCTS PSGSTTTQPA
PDGVPGPLAD TSLVTASAKV LPTPQPLLPA PSGSSAPPHP AKMPSGTEQQ TEGTSVTFSP
LKSPPQLERE MASPPECSEM PLDLSSKSNR QKLPLPNQRK TPPMPVLTPV HTSSKALLST
VLSRSQRTTQ AAGGNVTSCL GSTSSPFVIF PEIVRNGDPS TWVKNSTALI STIPGTYVGV
ANPVPASLLL NKDPNLGLNR DPRHLPKQEP ISIIDQGEPK GTGATCGKKG SQAGAEGQPS
TVKRYTPARI APGLPGCQTK ELSLWKPTGP ANIYPRCSVN GKPTSTQVLP VGWSPYHQAS
LLSIGISSAG QLTPSQGAPI RPTSVVSEFS GVPSLSSSEA VHGLPEGQPR PGGSFVPEQD
PVTKNKTCRI AAKPYEEQVN PVLLTLSPQT GTLALSVQPS GGDIRMNQGP EESESHLCSD
STPKMEGPQG ACGLKLAGDT KPKNQVLATY MSHELVLATP QNLPKMPELP LLPHDSHPKE
LILDVVPSSR RGSSTERPQL GSQVDLGRVK MEKVDGDVVF NLATCFRADG LPVAPQRGQA
EVRAKAGQAR VKQESVGVFA CKNKWQPDDV TESLPPKKMK CGKEKDSEEQ QLQPQAKAVV
RSSHRPKCRK LPSDPQESTK KSPRGASDSG KEHNGVRGKH KHRKPTKPES QSPGKRADSH
EEGSLEKKAK SSFRDFIPVV LSTRTRSQSG SICSSFAGMA DSDMGSQEVF PTEEEEEVTP
TPAKRRKVRK TQRDTQYRSH HAQDKSLLSQ GRRHLWRARE MPWRTEAARQ MWDTNEEEEE
EEEEGLLKRK KRRRQKSRKY QTGEYLTEQE DEQRRKGRAD LKARKQKTSS SQSLEHRLRN
RNLLLPNKVQ GISDSPNGFL PNNLEEPACL ENSEKPSGKR KCKTKHMATV SEEAKGKGRW
SQQKTRSPKS PTPVKPTEPC TPSKSRSASS EEASESPTAR QIPPEARRLI VNKNAGETLL
QRAARLGYKD VVLYCLQKDS EDVNHRDNAG YTALHEACSR GWTDILNILL EHGANVNCSA
QDGTRPVHDA VVNDNLETIW LLLSYGADPT LATYSGQTAM KLASSDTMKR FLSDHLSDLQ
GRAEGDPGVS WDFYSSSVLE EKDGFACDLL HNPPGSSDQE GDDPMEEDDF MFELSDKPLL
PCYNLQVSVS RGPCNWFLFS DVLKRLKLSS RIFQARFPHF EITTMPKAEF YRQVASSQLL
TPAERPGGLD DRSPPGSSET VELVRYEPDL LRLLGSEVEF QSCNS
//
