CBFB
entrez
865
canonical
uniprot
Q13951
canonical
ensembl
ENSG00000067955
resolver
ensp
ENSP00000290858
resolver
ensp
ENSP00000415151
resolver
ensp
ENSP00000532149
resolver
ensp
ENSP00000663014
resolver
genesymbol
CBFB
resolver
hgnc
HGNC:1539
resolver
uniprot
A8K347
resolver
uniprot
Q13124
resolver
uniprot
Q9HCT2
resolver
uniprot_entry
PEBB_HUMAN
resolver
uniprot_sec
A8K347
resolver
uniprot_sec
Q13124
resolver
uniprot_sec
Q9HCT2
resolver
amino_acid_sequence
MPRVVPDQRSKFENEEFFRKLSRECEIKYTGFRDRPHEERQARFQNACRDGRSEIAFVATGTNLSLQFFPASWQGEQRQTPSREYVDLEREAGKVYLKAPMILNGVCVIWKGWIDLQRLDGMGCLEFDEERAQQEDALAQQAFEEARRRTREFEDRDRSHREEMEVRVSQLLAVTGKKTTRP
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving CBFB is associated with acute myeloid leukemia of M4EO subtype. Pericentric inversion inv(16)(p13;q22). The inversion produces a fusion protein that consists of the 165 N-terminal residues of CBF-beta (PEPB2) with the tail region of MYH11. {ECO:0000269|PubMed:8351518}.; DISEASE: Cleidocranial dysplasia 2 (CLCD2) [MIM:620099]: A form of cleidocranial dysplasia, a rare skeletal disorder with significant clinical variability, even within families. Patients typically present with delayed closure of cranial sutures and fontanels with multiple Wormian bones, retarded ossification of the skull, shortening of the distal phalanges, dental anomalies including supernumerary teeth and eruption failure, clavicular hypoplasia or aplasia, wide pubic symphysis, vertebral anomalies, and short stature. Craniofacial features are subtle and characterized by prominent parietal and frontal bones, widely spaced eyes, depressed nasal bridge and small maxilla. Some CLCD2 patients present mild to moderate developmental delay. CLCD2 inheritance is autosomal dominant. {ECO:0000269|PubMed:36241386}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Forms the heterodimeric complex core-binding factor (CBF) with RUNX family proteins (RUNX1, RUNX2, and RUNX3). RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters. CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation. {ECO:0000250|UniProtKB:Q08024}.; FUNCTION: (Microbial infection) Following infection, hijacked by the HIV-1 Vif protein, leading to the formation a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex) that catalyzes ubiquitination and degradation of APOBEC3F and APOBEC3G (PubMed:22190037, PubMed:31792451, PubMed:36598981, PubMed:36754086, PubMed:37419875). The complex can also ubiquitinate APOBEC3H to some extent (PubMed:37640699). Association with HIV-1 Vif protein also inhibits the transcription coactivator activity of CBFB/CBF-beta (PubMed:22190037). {ECO:0000269|PubMed:22190037, ECO:0000269|PubMed:31792451, ECO:0000269|PubMed:36598981, ECO:0000269|PubMed:36754086, ECO:0000269|PubMed:37419875, ECO:0000269|PubMed:37640699}.
uniprot
proteins
mass_dalton
21508
uniprot
proteins
mutagenesis
MUTAGEN 35..43; /note="RPHEERQAR->EPHEERQAE: Abolished ability to promote ubiquitination and degradation of APOBEC3F following interaction with HIV-1 Vif. Does not affect ability to promote ubiquitination and degradation of APOBEC3G following interaction with HIV-1 Vif."; MUTAGEN 54; /note="E->K: Abolished ability to promote ubiquitination and degradation of APOBEC3F following interaction with HIV-1 Vif. Does not affect ability to promote ubiquitination and degradation of APOBEC3G following interaction with HIV-1 Vif."; /evidence="ECO:0000269|PubMed:31792451
uniprot
proteins
protein_family
CBF-beta family
uniprot
proteins
pubmed
10404215
uniprot
proteins
pubmed
10856244
uniprot
proteins
pubmed
11276260
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22190037
uniprot
proteins
pubmed
24402281
uniprot
proteins
pubmed
31792451
uniprot
proteins
pubmed
36241386
uniprot
proteins
pubmed
36598981
uniprot
proteins
pubmed
36754086
uniprot
proteins
pubmed
37419875
uniprot
proteins
pubmed
37640699
uniprot
proteins
pubmed
7607682
uniprot
proteins
pubmed
8351518
uniprot
proteins
pubmed
9064279
uniprot
proteins
sequence_length
182
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q08024}.
uniprot
proteins