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Protein

Core-binding factor subunit beta

Gene

CBFB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters. CBFB enhances DNA binding by RUNX1.

GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-HSA-8877330 RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs)
R-HSA-8878166 Transcriptional regulation by RUNX2
R-HSA-8931987 RUNX1 regulates estrogen receptor mediated transcription
R-HSA-8934593 Regulation of RUNX1 Expression and Activity
R-HSA-8935964 RUNX1 regulates expression of components of tight junctions
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939242 RUNX1 regulates transcription of genes involved in differentiation of keratinocytes
R-HSA-8939243 RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-HSA-8939245 RUNX1 regulates transcription of genes involved in BCR signaling
R-HSA-8939246 RUNX1 regulates transcription of genes involved in differentiation of myeloid cells
R-HSA-8939247 RUNX1 regulates transcription of genes involved in interleukin signaling
R-HSA-8939256 RUNX1 regulates transcription of genes involved in WNT signaling
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8940973 RUNX2 regulates osteoblast differentiation
R-HSA-8941284 RUNX2 regulates chondrocyte maturation
R-HSA-8941326 RUNX2 regulates bone development
R-HSA-8941332 RUNX2 regulates genes involved in cell migration
R-HSA-8941333 RUNX2 regulates genes involved in differentiation of myeloid cells
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8949275 RUNX3 Regulates Immune Response and Cell Migration
R-HSA-8951430 RUNX3 regulates WNT signaling
R-HSA-8951911 RUNX3 regulates RUNX1-mediated transcription
R-HSA-8951936 RUNX3 regulates p14-ARF
SIGNORiQ13951

Names & Taxonomyi

Protein namesi
Recommended name:
Core-binding factor subunit beta
Short name:
CBF-beta
Alternative name(s):
Polyomavirus enhancer-binding protein 2 beta subunit
Short name:
PEA2-beta
Short name:
PEBP2-beta
SL3-3 enhancer factor 1 subunit beta
SL3/AKV core-binding factor beta subunit
Gene namesi
Name:CBFB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000067955.13
HGNCiHGNC:1539 CBFB
MIMi121360 gene
neXtProtiNX_Q13951

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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 MYH11.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei165 – 166Breakpoint for translocation to form CBF-beta-MYH11 oncogene in AML, subtype M4EO2

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi865
MalaCardsiCBFB
OpenTargetsiENSG00000067955
Orphaneti98829 'Acute myeloid leukemia with abnormal bone marrow eosinophils inv(16)(p13q22) or t(16;16)(p13;q22)'
PharmGKBiPA26114

Chemistry databases

ChEMBLiCHEMBL1615386

Polymorphism and mutation databases

BioMutaiCBFB
DMDMi2498753

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000583011 – 182Core-binding factor subunit betaAdd BLAST182

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform 2 (identifier: Q13951-2)
Modified residuei173PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ13951
MaxQBiQ13951
PaxDbiQ13951
PeptideAtlasiQ13951
PRIDEiQ13951

PTM databases

iPTMnetiQ13951
PhosphoSitePlusiQ13951

Expressioni

Gene expression databases

BgeeiENSG00000067955
CleanExiHS_CBFB
ExpressionAtlasiQ13951 baseline and differential
GenevisibleiQ13951 HS

Organism-specific databases

HPAiHPA038852

Interactioni

Subunit structurei

Heterodimer with RUNX1. Interacts with COPRS (By similarity). Found in a complex with PRMT5, RUNX1 and CBFB (By similarity).By similarity

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi107313, 29 interactors
CORUMiQ13951
DIPiDIP-36772N
IntActiQ13951, 26 interactors
MINTiQ13951
STRINGi9606.ENSP00000415151

Chemistry databases

BindingDBiQ13951

Structurei

Secondary structure

1182
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 14Combined sources7
Helixi16 – 19Combined sources4
Beta strandi25 – 29Combined sources5
Beta strandi33 – 35Combined sources3
Helixi37 – 49Combined sources13
Beta strandi52 – 57Combined sources6
Turni58 – 61Combined sources4
Beta strandi65 – 67Combined sources3
Helixi71 – 73Combined sources3
Turni83 – 85Combined sources3
Beta strandi86 – 91Combined sources6
Beta strandi94 – 103Combined sources10
Beta strandi106 – 115Combined sources10
Turni116 – 118Combined sources3
Beta strandi119 – 127Combined sources9
Helixi129 – 134Combined sources6
Helixi137 – 148Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CL3NMR-A4-141[»]
1E50X-ray2.60B/D/F/H2-135[»]
1H9DX-ray2.60B/D2-135[»]
4N9FX-ray3.300/6/F/L/N/R/a/c/i/k/o/u1-170[»]
ProteinModelPortaliQ13951
SMRiQ13951
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13951

Family & Domainsi

Sequence similaritiesi

Belongs to the CBF-beta family.Curated

Phylogenomic databases

eggNOGiKOG4785 Eukaryota
ENOG410Z04Q LUCA
GeneTreeiENSGT00390000018132
HOGENOMiHOG000008040
HOVERGENiHBG000541
InParanoidiQ13951
OMAiPGKVHIK
OrthoDBiEOG091G0VFL
PhylomeDBiQ13951
TreeFamiTF314675

Family and domain databases

Gene3Di2.40.250.10, 1 hit
InterProiView protein in InterPro
IPR003417 CBF_beta
IPR036552 CBF_bsu_sf
PANTHERiPTHR10276 PTHR10276, 1 hit
PfamiView protein in Pfam
PF02312 CBF_beta, 1 hit
SUPFAMiSSF50723 SSF50723, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13951-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPRVVPDQRS KFENEEFFRK LSRECEIKYT GFRDRPHEER QARFQNACRD
60 70 80 90 100
GRSEIAFVAT GTNLSLQFFP ASWQGEQRQT PSREYVDLER EAGKVYLKAP
110 120 130 140 150
MILNGVCVIW KGWIDLQRLD GMGCLEFDEE RAQQEDALAQ QAFEEARRRT
160 170 180
REFEDRDRSH REEMEVRVSQ LLAVTGKKTT RP
Length:182
Mass (Da):21,508
Last modified:November 1, 1997 - v2
Checksum:i20FB1CC05FBFE4FB
GO
Isoform 2 (identifier: Q13951-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     166-182: VRVSQLLAVTGKKTTRP → ARRQQDPSPGSNLGGGDDLKLR

Show »
Length:187
Mass (Da):21,991
Checksum:i277B13D2A2ED18E4
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036226100P → A in a breast cancer sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_036044166 – 182VRVSQ…KTTRP → ARRQQDPSPGSNLGGGDDLK LR in isoform 2. 1 PublicationAdd BLAST17

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF294326 mRNA Translation: AAG01553.1
BT006862 mRNA Translation: AAP35508.1
AK290462 mRNA Translation: BAF83151.1
CH471092 Genomic DNA Translation: EAW83067.1
CH471092 Genomic DNA Translation: EAW83068.1
BC018509 mRNA Translation: AAH18509.1
L20298 mRNA Translation: AAA02868.1
CCDSiCCDS10827.1 [Q13951-1]
CCDS45508.1 [Q13951-2]
PIRiA56840
I59579
RefSeqiNP_001746.1, NM_001755.2 [Q13951-1]
NP_074036.1, NM_022845.2 [Q13951-2]
UniGeneiHs.460988

Genome annotation databases

EnsembliENST00000290858; ENSP00000290858; ENSG00000067955 [Q13951-1]
ENST00000412916; ENSP00000415151; ENSG00000067955 [Q13951-2]
GeneIDi865
KEGGihsa:865
UCSCiuc002era.4 human [Q13951-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPEBB_HUMAN
AccessioniPrimary (citable) accession number: Q13951
Secondary accession number(s): A8K347, Q13124, Q9HCT2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 169 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health