Q5H9F3 · BCORL_HUMAN

  • Protein
    BCL-6 corepressor-like protein 1
  • Gene
    BCORL1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Transcriptional corepressor. May specifically inhibit gene expression when recruited to promoter regions by sequence-specific DNA-binding proteins such as BCL6. This repression may be mediated at least in part by histone deacetylase activities which can associate with this corepressor.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentplasma membrane
Molecular Functiontranscription corepressor activity
Biological Processchromatin organization
Biological Processnegative regulation of transcription by RNA polymerase II

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    BCL-6 corepressor-like protein 1
  • Short names
    BCoR-L1; BCoR-like protein 1

Gene names

    • Name
      BCORL1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q5H9F3
  • Secondary accessions
    • B5MDQ8
    • Q5H9F2
    • Q5H9F4
    • Q6ZVE0
    • Q8TEN3
    • Q9Y528

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Involvement in disease

Shukla-Vernon syndrome (SHUVER)

  • Note
    • The disease may be caused by variants affecting the gene represented in this entry
  • Description
    An X-linked neurodevelopmental disorder manifesting in affected males with intellectual and learning disability, motor and language delay, autism spectrum disorder, attention deficit and hyperactivity disorder, and dysmorphic features. Some patients may have seizures and/or cerebellar atrophy on brain imaging. Carrier females may have mild disease manifestations.
  • See also
    MIM:301029
Natural variants in SHUVER
Variant IDPosition(s)ChangeDescription
VAR_08228832P>Lin SHUVER; uncertain significance; dbSNP:rs1603105985
VAR_082289496S>Fin SHUVER; uncertain significance; dbSNP:rs1057521638
VAR_082290782V>Ein SHUVER; uncertain significance; dbSNP:rs1488781894
VAR_070559820N>Sin SHUVER; uncertain significance; dbSNP:rs398123004

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variantVAR_08228832in SHUVER; uncertain significance; dbSNP:rs1603105985
Natural variantVAR_061020111in dbSNP:rs4830173
Natural variantVAR_037467209in dbSNP:rs5932715
Natural variantVAR_080909327found in a patient with Uruguay faciocardiomusculoskeletal syndrome; uncertain significance
Natural variantVAR_082289496in SHUVER; uncertain significance; dbSNP:rs1057521638
Mutagenesis623-624Strongly reduced repressor activity. Interferes with CTBP1 binding.
Natural variantVAR_082290782in SHUVER; uncertain significance; dbSNP:rs1488781894
Natural variantVAR_070559820in SHUVER; uncertain significance; dbSNP:rs398123004
Natural variantVAR_037468832in a breast cancer sample; somatic mutation
Mutagenesis1739Slightly inhibits interaction with PCGF1.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,211 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue, cross-link.

TypeIDPosition(s)SourceDescription
ChainPRO_00003122681-1785UniProtBCL-6 corepressor-like protein 1
Modified residue (large scale data)155PRIDEPhosphoserine
Modified residue496UniProtPhosphoserine
Modified residue (large scale data)496PRIDEPhosphoserine
Modified residue599UniProtPhosphoserine
Modified residue (large scale data)599PRIDEPhosphoserine
Modified residue (large scale data)603PRIDEPhosphoserine
Modified residue613UniProtPhosphoserine
Modified residue (large scale data)613PRIDEPhosphoserine
Modified residue (large scale data)641PRIDEPhosphothreonine
Cross-link747UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)927PRIDEPhosphoserine
Modified residue (large scale data)961PRIDEPhosphoserine
Modified residue (large scale data)962PRIDEPhosphothreonine
Modified residue (large scale data)1016PRIDEPhosphoserine
Modified residue (large scale data)1028PRIDEPhosphoserine
Modified residue1029UniProtPhosphoserine
Modified residue (large scale data)1029PRIDEPhosphoserine
Modified residue1033UniProtPhosphoserine
Modified residue (large scale data)1033PRIDEPhosphoserine
Modified residue (large scale data)1034PRIDEPhosphoserine
Cross-link1092UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue1162UniProtPhosphoserine
Modified residue (large scale data)1199PRIDEPhosphoserine
Modified residue (large scale data)1204PRIDEPhosphoserine
Modified residue (large scale data)1417PRIDEPhosphoserine
Modified residue (large scale data)1450PRIDEPhosphoserine
Modified residue (large scale data)1452PRIDEPhosphothreonine
Modified residue (large scale data)1461PRIDEPhosphothreonine
Modified residue (large scale data)1467PRIDEPhosphoserine
Modified residue (large scale data)1469PRIDEPhosphoserine
Modified residue (large scale data)1474PRIDEPhosphoserine
Modified residue1476UniProtPhosphoserine
Modified residue (large scale data)1476PRIDEPhosphoserine
Modified residue (large scale data)1478PRIDEPhosphothreonine
Modified residue (large scale data)1753PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Detected in testis and prostate. Detected at lower levels in peripheral blood leukocytes and spleen.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with PCGF1, forming heterodimers (PubMed:23523425, PubMed:27568929).
The PCGF1-BCORL1 heterodimeric complex interacts with the KDM2B-SKP1 heterodimeric complex to form a homotetrameric polycomb repression complex 1 (PRC1.1) (PubMed:27568929).
Interacts with CTBP1, HDAC4, HDAC5 and HDAC7 (PubMed:17379597).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q5H9F3-1PCGF1 Q9BSM1-16EBI-16041827, EBI-16041863
View interactors in UniProtKB
View CPX-2627 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, motif, repeat.

TypeIDPosition(s)Description
Region65-101Disordered
Compositional bias79-97Basic and acidic residues
Region113-137Disordered
Region343-368Disordered
Compositional bias527-541Polar residues
Region527-550Disordered
Region562-646Disordered
Compositional bias564-578Pro residues
Compositional bias584-602Polar residues
Compositional bias622-636Polar residues
Region753-781Disordered
Region876-901Disordered
Region937-977Disordered
Region1107-1293Disordered
Compositional bias1111-1131Basic and acidic residues
Compositional bias1187-1213Basic and acidic residues
Compositional bias1221-1236Polar residues
Compositional bias1275-1293Basic and acidic residues
Region1312-1487Disordered
Motif1328-1336Nuclear localization signal
Compositional bias1339-1374Basic and acidic residues
Compositional bias1386-1400Polar residues
Compositional bias1425-1440Basic and acidic residues
Compositional bias1459-1477Polar residues
Repeat1529-1558ANK 1
Repeat1562-1591ANK 2
Repeat1595-1623ANK 3
Region1668-1785PCGF Ub-like fold domain (PUFD); required for the interaction with the KDM2B-SKP1 heterodimeric complex

Sequence similarities

Belongs to the BCOR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q5H9F3-3

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    1,785
  • Mass (Da)
    190,561
  • Last updated
    2022-02-23 v2
  • Checksum
    DD62FFFEC2DE1E9C
MISTAPLYSGVHNWTSSDRIRMCGINEERRAPLSDEESTTGDCQHFGSQEFCVSSSFSKVELTAVGSGSNARGADPDGSATEKLGHKSEDKPDDPQPKMDYAGNVAEAEGLLVPLSSPGDGLKLPASDSAEASNSRADCSWTPLNTQMSKQVDCSPAGVKALDSRQGVGEKNTFILATLGTGVPVEGTLPLVTTNFSPLPAPICPPAPGSASVPHSVPDAFQVPLSVPAPVPHSGLVPVQVATSVPAPSPPLAPVPALAPAPPSVPTLISDSNPLSVSASVLVPVPASAPPSGPVPLSAPAPAPLSVPVSAPPLALIQAPVPPSAPTLVLAPVPTPVLAPMPASTPPAAPAPPSVPMPTPTPSSGPPSTPTLIPAFAPTPVPAPTPAPIFTPAPTPMPAATPAAIPTSAPIPASFSLSRVCFPAAQAPAMQKVPLSFQPGTVLTPSQPLVYIPPPSCGQPLSVATLPTTLGVSSTLTLPVLPSYLQDRCLPGVLASPELRSYPYAFSVARPLTSDSKLVSLEVNRLPCTSPSGSTTTQPAPDGVPGPLADTSLVTASAKVLPTPQPLLPAPSGSSAPPHPAKMPSGTEQQTEGTSVTFSPLKSPPQLEREMASPPECSEMPLDLSSKSNRQKLPLPNQRKTPPMPVLTPVHTSSKALLSTVLSRSQRTTQAAGGNVTSCLGSTSSPFVIFPEIVRNGDPSTWVKNSTALISTIPGTYVGVANPVPASLLLNKDPNLGLNRDPRHLPKQEPISIIDQGEPKGTGATCGKKGSQAGAEGQPSTVKRYTPARIAPGLPGCQTKELSLWKPTGPANIYPRCSVNGKPTSTQVLPVGWSPYHQASLLSIGISSAGQLTPSQGAPIRPTSVVSEFSGVPSLSSSEAVHGLPEGQPRPGGSFVPEQDPVTKNKTCRIAAKPYEEQVNPVLLTLSPQTGTLALSVQPSGGDIRMNQGPEESESHLCSDSTPKMEGPQGACGLKLAGDTKPKNQVLATYMSHELVLATPQNLPKMPELPLLPHDSHPKELILDVVPSSRRGSSTERPQLGSQVDLGRVKMEKVDGDVVFNLATCFRADGLPVAPQRGQAEVRAKAGQARVKQESVGVFACKNKWQPDDVTESLPPKKMKCGKEKDSEEQQLQPQAKAVVRSSHRPKCRKLPSDPQESTKKSPRGASDSGKEHNGVRGKHKHRKPTKPESQSPGKRADSHEEGSLEKKAKSSFRDFIPVVLSTRTRSQSGSICSSFAGMADSDMGSQEVFPTEEEEEVTPTPAKRRKVRKTQRDTQYRSHHAQDKSLLSQGRRHLWRAREMPWRTEAARQMWDTNEEEEEEEEEGLLKRKKRRRQKSRKYQTGEYLTEQEDEQRRKGRADLKARKQKTSSSQSLEHRLRNRNLLLPNKVQGISDSPNGFLPNNLEEPACLENSEKPSGKRKCKTKHMATVSEEAKGKGRWSQQKTRSPKSPTPVKPTEPCTPSKSRSASSEEASESPTARQIPPEARRLIVNKNAGETLLQRAARLGYKDVVLYCLQKDSEDVNHRDNAGYTALHEACSRGWTDILNILLEHGANVNCSAQDGTRPVHDAVVNDNLETIWLLLSYGADPTLATYSGQTAMKLASSDTMKRFLSDHLSDLQGRAEGDPGVSWDFYSSSVLEEKDGFACDLLHNPPGSSDQEGDDPMEEDDFMFELSDKPLLPCYNLQVSVSRGPCNWFLFSDVLKRLKLSSRIFQARFPHFEITTMPKAEFYRQVASSQLLTPAERPGGLDDRSPPGSSETVELVRYEPDLLRLLGSEVEFQSCNS

Q5H9F3-1

Q5H9F3-4

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
V9GYD4V9GYD4_HUMANBCORL145
H7C4B2H7C4B2_HUMANBCORL1741
A0A087X1F0A0A087X1F0_HUMANBCORL128

Sequence caution

The sequence BAC85922.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence CAB46626.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Compositional bias79-97Basic and acidic residues
Compositional bias527-541Polar residues
Compositional bias564-578Pro residues
Compositional bias584-602Polar residues
Compositional bias622-636Polar residues
Compositional bias1111-1131Basic and acidic residues
Compositional bias1187-1213Basic and acidic residues
Compositional bias1221-1236Polar residues
Alternative sequenceVSP_0614391230-1359in isoform 4
Compositional bias1275-1293Basic and acidic residues
Compositional bias1339-1374Basic and acidic residues
Compositional bias1386-1400Polar residues
Compositional bias1425-1440Basic and acidic residues
Alternative sequenceVSP_0614401436-1509in isoform 1
Compositional bias1459-1477Polar residues
Sequence conflict1638in Ref. 4; BAC85922

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL034405
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL136450
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
KF459398
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
KF459400
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
KF510634
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
Z82208
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AK074089
EMBL· GenBank· DDBJ
BAB84915.1
EMBL· GenBank· DDBJ
mRNA
AL096777
EMBL· GenBank· DDBJ
CAB46626.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK124676
EMBL· GenBank· DDBJ
BAC85922.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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