位置:首页 > 蛋白库 > BCORL_HUMAN
BCORL_HUMAN
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   03-AUG-2022, entry version 153.
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   RefSeq; NP_068765.3; NM_021946.4.
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   BioGRID; 121961; 66.
DR   DIP; DIP-60148N; -.
DR   IntAct; Q5H9F3; 30.
DR   MINT; Q5H9F3; -.
DR   STRING; 9606.ENSP00000437775; -.
DR   GlyGen; Q5H9F3; 5 sites, 1 O-linked glycan (5 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; Q5H9F3; -.
DR   PeptideAtlas; Q5H9F3; -.
DR   PRIDE; Q5H9F3; -.
DR   ProteomicsDB; 62886; -. [Q5H9F3-1]
DR   ProteomicsDB; 62888; -. [Q5H9F3-3]
DR   Antibodypedia; 30129; 78 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   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   OrthoDB; 85469at2759; -.
DR   PhylomeDB; Q5H9F3; -.
DR   TreeFam; TF333317; -.
DR   PathwayCommons; Q5H9F3; -.
DR   SignaLink; Q5H9F3; -.
DR   SIGNOR; Q5H9F3; -.
DR   BioGRID-ORCS; 63035; 18 hits in 711 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 189 other 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   Gene3D; 1.25.40.20; -; 1.
DR   Gene3D; 3.10.260.40; -; 1.
DR   IDEAL; IID00623; -.
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   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; unknown pathological
FT                   significance)"
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; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:26933038"
FT                   /id="VAR_080909"
FT   VARIANT         496
FT                   /note="S -> F (in SHUVER; unknown pathological
FT                   significance; dbSNP:rs1057521638)"
FT                   /evidence="ECO:0000269|PubMed:30941876"
FT                   /id="VAR_082289"
FT   VARIANT         782
FT                   /note="V -> E (in SHUVER; unknown pathological
FT                   significance; dbSNP:rs1488781894)"
FT                   /evidence="ECO:0000269|PubMed:30941876"
FT                   /id="VAR_082290"
FT   VARIANT         820
FT                   /note="N -> S (in SHUVER; unknown pathological
FT                   significance; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024