BICRL_HUMAN
ID BICRL_HUMAN Reviewed; 1079 AA.
AC Q6AI39; A1L3W2; Q5TFZ3; Q92514;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=BRD4-interacting chromatin-remodeling complex-associated protein-like {ECO:0000305};
DE AltName: Full=Glioma tumor suppressor candidate region gene 1 protein-like {ECO:0000312|HGNC:HGNC:21111};
GN Name=BICRAL {ECO:0000312|HGNC:HGNC:21111};
GN Synonyms=GLTSCR1L {ECO:0000312|HGNC:HGNC:21111},
GN KIAA0240 {ECO:0000312|EMBL:BAA13246.2};
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 MRNA].
RC TISSUE=Brain;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623 AND SER-980, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [9]
RP FUNCTION, AND IDENTIFICATION IN THE GBAF COMPLEX.
RX PubMed=29374058; DOI=10.1074/jbc.ra117.001065;
RA Alpsoy A., Dykhuizen E.C.;
RT "Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog
RT GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.";
RL J. Biol. Chem. 293:3892-3903(2018).
CC -!- FUNCTION: Component of SWI/SNF chromatin remodeling subcomplex GBAF
CC that carries out key enzymatic activities, changing chromatin structure
CC by altering DNA-histone contacts within a nucleosome in an ATP-
CC dependent manner. {ECO:0000269|PubMed:29374058}.
CC -!- SUBUNIT: Component of the multiprotein chromatin-remodeling complexes
CC SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The
CC canonical complex contains a catalytic subunit (either
CC SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1,
CC ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47.
CC Other subunits specific to each of the complexes may also be present
CC permitting several possible combinations developmentally and tissue
CC specific. Component of the SWI/SNF (GBAF) subcomplex, which includes at
CC least BICRA or BICRAL (mutually exclusive), BRD9, SS18, the core BAF
CC subunits, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53,
CC SMARCC1/BAF155, and SMARCD1/BAF60A. {ECO:0000269|PubMed:29374058}.
CC -!- INTERACTION:
CC Q6AI39; Q99819: ARHGDIG; NbExp=3; IntAct=EBI-1012434, EBI-10295284;
CC Q6AI39; P54253: ATXN1; NbExp=3; IntAct=EBI-1012434, EBI-930964;
CC Q6AI39; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-1012434, EBI-11524452;
CC Q6AI39; Q13515: BFSP2; NbExp=3; IntAct=EBI-1012434, EBI-10229433;
CC Q6AI39; Q86UW9: DTX2; NbExp=3; IntAct=EBI-1012434, EBI-740376;
CC Q6AI39; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-1012434, EBI-742102;
CC Q6AI39; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-1012434, EBI-10242151;
CC Q6AI39; O14964: HGS; NbExp=3; IntAct=EBI-1012434, EBI-740220;
CC Q6AI39; Q16082: HSPB2; NbExp=3; IntAct=EBI-1012434, EBI-739395;
CC Q6AI39; Q96IV0: NGLY1; NbExp=3; IntAct=EBI-1012434, EBI-6165879;
CC Q6AI39; Q16656-4: NRF1; NbExp=3; IntAct=EBI-1012434, EBI-11742836;
CC Q6AI39; P86480: PRR20D; NbExp=3; IntAct=EBI-1012434, EBI-12754095;
CC Q6AI39; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-1012434, EBI-2798044;
CC Q6AI39; O75177-5: SS18L1; NbExp=3; IntAct=EBI-1012434, EBI-12035119;
CC Q6AI39; P36406: TRIM23; NbExp=3; IntAct=EBI-1012434, EBI-740098;
CC Q6AI39; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-1012434, EBI-739895;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13246.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D87077; BAA13246.2; ALT_INIT; mRNA.
DR EMBL; CR627378; CAH10475.1; -; mRNA.
DR EMBL; AL035587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04102.1; -; Genomic_DNA.
DR EMBL; BC130302; AAI30303.1; -; mRNA.
DR CCDS; CCDS34451.1; -.
DR RefSeq; NP_001305748.1; NM_001318819.1.
DR RefSeq; NP_056164.1; NM_015349.2.
DR AlphaFoldDB; Q6AI39; -.
DR BioGRID; 117053; 41.
DR ComplexPortal; CPX-4203; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4207; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-4224; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4226; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant.
DR IntAct; Q6AI39; 36.
DR STRING; 9606.ENSP00000313933; -.
DR GlyGen; Q6AI39; 7 sites, 2 O-linked glycans (7 sites).
DR iPTMnet; Q6AI39; -.
DR PhosphoSitePlus; Q6AI39; -.
DR BioMuta; BICRAL; -.
DR DMDM; 114149731; -.
DR EPD; Q6AI39; -.
DR jPOST; Q6AI39; -.
DR MassIVE; Q6AI39; -.
DR MaxQB; Q6AI39; -.
DR PaxDb; Q6AI39; -.
DR PeptideAtlas; Q6AI39; -.
DR PRIDE; Q6AI39; -.
DR ProteomicsDB; 66188; -.
DR Antibodypedia; 30175; 23 antibodies from 8 providers.
DR DNASU; 23506; -.
DR Ensembl; ENST00000314073.10; ENSP00000313933.4; ENSG00000112624.13.
DR Ensembl; ENST00000394168.1; ENSP00000377723.1; ENSG00000112624.13.
DR Ensembl; ENST00000614467.4; ENSP00000482211.1; ENSG00000112624.13.
DR GeneID; 23506; -.
DR KEGG; hsa:23506; -.
DR MANE-Select; ENST00000314073.10; ENSP00000313933.4; NM_001393499.1; NP_001380428.1.
DR UCSC; uc003osn.2; human.
DR CTD; 23506; -.
DR GeneCards; BICRAL; -.
DR HGNC; HGNC:21111; BICRAL.
DR HPA; ENSG00000112624; Low tissue specificity.
DR MIM; 618502; gene.
DR neXtProt; NX_Q6AI39; -.
DR OpenTargets; ENSG00000112624; -.
DR PharmGKB; PA134964468; -.
DR VEuPathDB; HostDB:ENSG00000112624; -.
DR eggNOG; ENOG502QPQ9; Eukaryota.
DR GeneTree; ENSGT00940000159766; -.
DR HOGENOM; CLU_011632_0_0_1; -.
DR InParanoid; Q6AI39; -.
DR OMA; DQFHPVP; -.
DR OrthoDB; 352636at2759; -.
DR PhylomeDB; Q6AI39; -.
DR TreeFam; TF335495; -.
DR PathwayCommons; Q6AI39; -.
DR SignaLink; Q6AI39; -.
DR BioGRID-ORCS; 23506; 8 hits in 1076 CRISPR screens.
DR ChiTaRS; GLTSCR1L; human.
DR GenomeRNAi; 23506; -.
DR Pharos; Q6AI39; Tdark.
DR PRO; PR:Q6AI39; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q6AI39; protein.
DR Bgee; ENSG00000112624; Expressed in cerebellar vermis and 212 other tissues.
DR Genevisible; Q6AI39; HS.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR InterPro; IPR038842; BICRA.
DR InterPro; IPR015671; GSCR1_dom.
DR PANTHER; PTHR15572:SF2; PTHR15572:SF2; 1.
DR Pfam; PF15249; GLTSCR1; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1079
FT /note="BRD4-interacting chromatin-remodeling complex-
FT associated protein-like"
FT /id="PRO_0000248602"
FT REGION 51..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 980
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 446
FT /note="R -> G (in Ref. 3; CAH10475)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="I -> V (in Ref. 3; CAH10475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1079 AA; 115084 MW; 92357E9993343A76 CRC64;
MDDDDDSCLL DLIGDPQALN YFLHGPSNKS SNDDLTNAGY SAANSNSIFA NSSNADPKSS
LKGVSNQLGE GPSDGLPLSS SLQFLEDELE SSPLPDLTED QPFDILQKSL QEANITEQTL
AEEAYLDASI GSSQQFAQAQ LHPSSSASFT QASNVSNYSG QTLQPIGVTH VPVGASFASN
TVGVQHGFMQ HVGISVPSQH LSNSSQISGS GQIQLIGSFG NHPSMMTINN LDGSQIILKG
SGQQAPSNVS GGLLVHRQTP NGNSLFGNSS SSPVAQPVTV PFNSTNFQTS LPVHNIIIQR
GLAPNSNKVP INIQPKPIQM GQQNTYNVNN LGIQQHHVQQ GISFASASSP QGSVVGPHMS
VNIVNQQNTR KPVTSQAVSS TGGSIVIHSP MGQPHAPQSQ FLIPTSLSVS SNSVHHVQTI
NGQLLQTQPS QLISGQVASE HVMLNRNSSN MLRTNQPYTG PMLNNQNTAV HLVSGQTFAA
SGSPVIANHA SPQLVGGQMP LQQASPTVLH LSPGQSSVSQ GRPGFATMPS VTSMSGPSRF
PAVSSASTAH PSLGSAVQSG SSGSNFTGDQ LTQPNRTPVP VSVSHRLPVS SSKSTSTFSN
TPGTGTQQQF FCQAQKKCLN QTSPISAPKT TDGLRQAQIP GLLSTTLPGQ DSGSKVISAS
LGTAQPQQEK VVGSSPGHPA VQVESHSGGQ KRPAAKQLTK GAFILQQLQR DQAHTVTPDK
SHFRSLSDAV QRLLSYHVCQ GSMPTEEDLR KVDNEFETVA TQLLKRTQAM LNKYRCLLLE
DAMRINPSAE MVMIDRMFNQ EERASLSRDK RLALVDPEGF QADFCCSFKL DKAAHETQFG
RSDQHGSKAS SSLQPPAKAQ GRDRAKTGVT EPMNHDQFHL VPNHIVVSAE GNISKKTECL
GRALKFDKVG LVQYQSTSEE KASRREPLKA SQCSPGPEGH RKTSSRSDHG TESKLSSILA
DSHLEMTCNN SFQDKSLRNS PKNEVLHTDI MKGSGEPQPD LQLTKSLETT FKNILELKKA
GRQPQSDPTV SGSVELDFPN FSPMASQENC LEKFIPDHSE GVVETDSILE AAVNSILEC
