Q9C0K0 · BC11B_HUMAN
- ProteinB-cell lymphoma/leukemia 11B
- GeneBCL11B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids894 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Key regulator of both differentiation and survival of T-lymphocytes during thymocyte development in mammals. Essential in controlling the responsiveness of hematopoietic stem cells to chemotactic signals by modulating the expression of the receptors CCR7 and CCR9, which direct the movement of progenitor cells from the bone marrow to the thymus (PubMed:27959755).
Is a regulator of IL2 promoter and enhances IL2 expression in activated CD4+ T-lymphocytes (PubMed:16809611).
Tumor-suppressor that represses transcription through direct, TFCOUP2-independent binding to a GC-rich response element (By similarity).
May also function in the P53-signaling pathway (By similarity).
Is a regulator of IL2 promoter and enhances IL2 expression in activated CD4+ T-lymphocytes (PubMed:16809611).
Tumor-suppressor that represses transcription through direct, TFCOUP2-independent binding to a GC-rich response element (By similarity).
May also function in the P53-signaling pathway (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameB-cell lymphoma/leukemia 11B
- Short namesBCL-11B
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9C0K0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Immunodeficiency 49 (IMD49)
- Note
- DescriptionA form of severe combined immunodeficiency characterized by severe T-cell lymphopenia, no detectable T-cell receptor excision circles, no naive helper CD4+ T-cells, and impaired T-cell proliferative response. In addition to primary immunodeficiency, affected individuals manifest multiple abnormal systemic features, including severe delayed psychomotor development, intellectual disability, spastic quadriplegia, and craniofacial abnormalities.
- See alsoMIM:617237
Natural variants in IMD49
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_078423 | 441 | N>K | in IMD49; loss of stimulation of T-lymphocyte development; dominant negative loss of activation of IL2 expression; results in reduced binding to known canonical promoters and abnormal binding to novel DNA sites not recognized by the wild-type protein; no effect on interaction with EP300; dbSNP:rs750610248 | |
VAR_081175 | 807 | N>K | in IMD49; dbSNP:rs888230251 |
Intellectual developmental disorder with speech delay, dysmorphic facies, and T-cell abnormalities (IDDSFTA)
- Note
- DescriptionAn autosomal dominant developmental disorder with onset in first months of life, and characterized by delayed psychomotor development with intellectual disability and speech delay. Additional features include autistic features, attention deficit-hyperactivity disorder, anxiety, and other behavioral abnormalities. Some patients suffer from recurrent infections, asthma and allergies.
- See alsoMIM:618092
Natural variants in IDDSFTA
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_081174 | 499-894 | missing | in IDDSFTA |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_065741 | 32 | in a patient with amyotrophic lateral sclerosis | |||
Sequence: E → V | ||||||
Natural variant | VAR_065742 | 229 | in a patient with amyotrophic lateral sclerosis; dbSNP:rs749837100 | |||
Sequence: P → S | ||||||
Natural variant | VAR_035554 | 331 | in a colorectal cancer sample; somatic mutation | |||
Sequence: S → P | ||||||
Natural variant | VAR_078423 | 441 | in IMD49; loss of stimulation of T-lymphocyte development; dominant negative loss of activation of IL2 expression; results in reduced binding to known canonical promoters and abnormal binding to novel DNA sites not recognized by the wild-type protein; no effect on interaction with EP300; dbSNP:rs750610248 | |||
Sequence: N → K | ||||||
Natural variant | VAR_081174 | 499-894 | in IDDSFTA | |||
Sequence: Missing | ||||||
Natural variant | VAR_081175 | 807 | in IMD49; dbSNP:rs888230251 | |||
Sequence: N → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,046 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000047104 | 1-894 | UniProt | B-cell lymphoma/leukemia 11B | |||
Sequence: MSRRKQGNPQHLSQRELITPEADHVEAAILEEDEGLEIEEPSGLGLMVGGPDPDLLTCGQCQMNFPLGDILVFIEHKRKQCGGSLGACYDKALDKDSPPPSSRSELRKVSEPVEIGIQVTPDEDDHLLSPTKGICPKQENIAGPCRPAQLPAVAPIAASSHPHSSVITSPLRALGALPPCLPLPCCSARPVSGDGTQGEGQTEAPFGCQCQLSGKDEPSSYICTTCKQPFNSAWFLLQHAQNTHGFRIYLEPGPASSSLTPRLTIPPPLGPEAVAQSPLMNFLGDSNPFNLLRMTGPILRDHPGFGEGRLPGTPPLFSPPPRHHLDPHRLSAEEMGLVAQHPSAFDRVMRLNPMAIDSPAMDFSRRLRELAGNSSTPPPVSPGRGNPMHRLLNPFQPSPKSPFLSTPPLPPMPPGGTPPPQPPAKSKSCEFCGKTFKFQSNLIVHRRSHTGEKPYKCQLCDHACSQASKLKRHMKTHMHKAGSLAGRSDDGLSAASSPEPGTSELAGEGLKAADGDFRHHESDPSLGHEPEEEDEEEEEEEEELLLENESRPESSFSMDSELSRNRENGGGGVPGVPGAGGGAAKALADEKALVLGKVMENVGLGALPQYGELLADKQKRGAFLKRAAGGGDAGDDDDAGGCGDAGAGGAVNGRGGGFAPGTEPFPGLFPRKPAPLPSPGLNSAAKRIKVEKDLELPPAALIPSENVYSQWLVGYAASRHFMKDPFLGFTDARQSPFATSSEHSSENGSLRFSTPPGDLLDGGLSGRSGTASGGSTPHLGGPGPGRPSSKEGRRSDTCEYCGKVFKNCSNLTVHRRSHTGERPYKCELCNYACAQSSKLTRHMKTHGQIGKEVYRCDICQMPFSVYSTLEKHMKKWHGEHLLTNDVKIEQAERS | |||||||
Modified residue | 97 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 97 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 101 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 110 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 110 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 120 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 120 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 129 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 129 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 131 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 137 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 137 | UniProt | In isoform Q9C0K0-2; Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 256 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 258 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 260 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 260 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 264 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 277 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 293 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 313 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 318 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 322 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 358 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 358 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 374 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 375 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 376 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 376 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 381 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 381 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 398 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 398 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 401 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 401 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 406 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 406 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 417 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 417 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 483 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 483 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 488 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 488 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 493 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 496 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 496 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 497 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 497 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 591 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 617 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 678 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 678 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 683 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 686 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 723 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 753 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 754 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 754 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 765 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 768 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 770 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 772 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 772 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 775 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 776 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 788 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 789 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 851 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 887 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Post-translational modification
Sumoylated with SUMO1.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in brain and in malignant T-cell lines derived from patients with adult T-cell leukemia/lymphoma.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with TFCOUP1, SIRT1, ARP1 and EAR2 (By similarity).
Interacts with EP300; the interaction is detected in activated T-lymphocytes, but not under resting conditions (PubMed:27959755).
Interacts with EP300; the interaction is detected in activated T-lymphocytes, but not under resting conditions (PubMed:27959755).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9C0K0 | HDAC1 Q13547 | 5 | EBI-6597578, EBI-301834 | |
BINARY | Q9C0K0 | HDAC2 Q92769 | 5 | EBI-6597578, EBI-301821 | |
BINARY | Q9C0K0 | SUV39H1 O43463 | 3 | EBI-6597578, EBI-349968 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 221-251 | C2H2-type 1 | ||||
Sequence: YICTTCKQPFNSAWFLLQHAQNTHGFRIYLE | ||||||
Region | 370-428 | Disordered | ||||
Sequence: LAGNSSTPPPVSPGRGNPMHRLLNPFQPSPKSPFLSTPPLPPMPPGGTPPPQPPAKSKS | ||||||
Compositional bias | 400-425 | Pro residues | ||||
Sequence: KSPFLSTPPLPPMPPGGTPPPQPPAK | ||||||
Zinc finger | 427-454 | C2H2-type 2 | ||||
Sequence: KSCEFCGKTFKFQSNLIVHRRSHTGEKP | ||||||
Zinc finger | 455-482 | C2H2-type 3 | ||||
Sequence: YKCQLCDHACSQASKLKRHMKTHMHKAG | ||||||
Region | 471-583 | Disordered | ||||
Sequence: KRHMKTHMHKAGSLAGRSDDGLSAASSPEPGTSELAGEGLKAADGDFRHHESDPSLGHEPEEEDEEEEEEEEELLLENESRPESSFSMDSELSRNRENGGGGVPGVPGAGGGA | ||||||
Compositional bias | 511-527 | Basic and acidic residues | ||||
Sequence: KAADGDFRHHESDPSLG | ||||||
Compositional bias | 528-547 | Acidic residues | ||||
Sequence: HEPEEEDEEEEEEEEELLLE | ||||||
Compositional bias | 550-564 | Polar residues | ||||
Sequence: SRPESSFSMDSELSR | ||||||
Region | 653-680 | Disordered | ||||
Sequence: GRGGGFAPGTEPFPGLFPRKPAPLPSPG | ||||||
Compositional bias | 737-752 | Polar residues | ||||
Sequence: FATSSEHSSENGSLRF | ||||||
Region | 737-794 | Disordered | ||||
Sequence: FATSSEHSSENGSLRFSTPPGDLLDGGLSGRSGTASGGSTPHLGGPGPGRPSSKEGRR | ||||||
Zinc finger | 796-823 | C2H2-type 4 | ||||
Sequence: DTCEYCGKVFKNCSNLTVHRRSHTGERP | ||||||
Zinc finger | 824-853 | C2H2-type 5 | ||||
Sequence: YKCELCNYACAQSSKLTRHMKTHGQIGKEV | ||||||
Zinc finger | 854-884 | C2H2-type 6 | ||||
Sequence: YRCDICQMPFSVYSTLEKHMKKWHGEHLLTN |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9C0K0-1
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.
- Name1
- SynonymsAlpha
- Length894
- Mass (Da)95,519
- Last updated2001-06-01 v1
- ChecksumDF6C467AE2EEC122
Q9C0K0-2
- Name2
- NoteMay be due to exon skipping.
- Differences from canonical
- 143-213: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D3YTK1 | D3YTK1_HUMAN | BCL11B | 700 |
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_009565 | 143-213 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 400-425 | Pro residues | ||||
Sequence: KSPFLSTPPLPPMPPGGTPPPQPPAK | ||||||
Compositional bias | 511-527 | Basic and acidic residues | ||||
Sequence: KAADGDFRHHESDPSLG | ||||||
Compositional bias | 528-547 | Acidic residues | ||||
Sequence: HEPEEEDEEEEEEEEELLLE | ||||||
Compositional bias | 550-564 | Polar residues | ||||
Sequence: SRPESSFSMDSELSR | ||||||
Compositional bias | 737-752 | Polar residues | ||||
Sequence: FATSSEHSSENGSLRF |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ404614 EMBL· GenBank· DDBJ | CAC17726.1 EMBL· GenBank· DDBJ | mRNA | ||
AB043584 EMBL· GenBank· DDBJ | BAB32731.1 EMBL· GenBank· DDBJ | mRNA |