PEBB_HUMAN
ID PEBB_HUMAN Reviewed; 182 AA.
AC Q13951; A8K347; Q13124; Q9HCT2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Core-binding factor subunit beta;
DE Short=CBF-beta;
DE AltName: Full=Polyomavirus enhancer-binding protein 2 beta subunit;
DE Short=PEA2-beta;
DE Short=PEBP2-beta;
DE AltName: Full=SL3-3 enhancer factor 1 subunit beta;
DE AltName: Full=SL3/AKV core-binding factor beta subunit;
GN Name=CBFB;
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 [MRNA] (ISOFORM 2).
RA Liu P.P.;
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-182 (ISOFORM 1), AND CHROMOSOMAL INVERSION.
RC TISSUE=Brain;
RX PubMed=8351518; DOI=10.1126/science.8351518;
RA Liu P., Tarle S.A., Hajra A., Claxton D.F., Marlton P., Freedman M.,
RA Siciliano M.J., Collins F.S.;
RT "Fusion between transcription factor CBF beta/PEBP2 beta and a myosin heavy
RT chain in acute myeloid leukemia.";
RL Science 261:1041-1044(1993).
RN [7]
RP RETRACTED PAPER.
RX PubMed=7607682; DOI=10.1016/0888-7543(95)80177-n;
RA Hajra A., Collins F.S.;
RT "Structure of the leukemia-associated human CBFB gene.";
RL Genomics 26:571-579(1995).
RN [8]
RP RETRACTION NOTICE OF PUBMED:7607682.
RX PubMed=9064279; DOI=10.1006/geno.1996.0603;
RA Hajra A., Collins F.S.;
RL Genomics 38:107-107(1996).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-135 IN COMPLEX WITH RUNX1.
RX PubMed=10856244; DOI=10.1093/emboj/19.12.3004;
RA Warren A.J., Bravo J., Williams R.L., Rabbitts T.H.;
RT "Structural basis for the heterodimeric interaction between the acute
RT leukaemia-associated transcription factors AML1 and CBFbeta.";
RL EMBO J. 19:3004-3015(2000).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-135 IN COMPLEX WITH RUNX1 AND
RP DNA.
RX PubMed=11276260; DOI=10.1038/86264;
RA Bravo J., Li Z., Speck N.A., Warren A.J.;
RT "The leukemia-associated AML1 (Runx1) -- CBF beta complex functions as a
RT DNA-induced molecular clamp.";
RL Nat. Struct. Biol. 8:371-378(2001).
RN [15]
RP STRUCTURE BY NMR OF 4-141.
RX PubMed=10404215; DOI=10.1038/10664;
RA Goger M., Gupta V., Kim W.Y., Shigesada K., Ito Y., Werner M.H.;
RT "Molecular insights into PEBP2/CBF beta-SMMHC associated acute leukemia
RT revealed from the structure of PEBP2/CBF beta.";
RL Nat. Struct. Biol. 6:620-623(1999).
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-100.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Forms the heterodimeric complex core-binding factor (CBF)
CC with RUNX family proteins (RUNX1, RUNX2, and RUNX3). RUNX members
CC modulate the transcription of their target genes through recognizing
CC the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-
CC TGCGGT-3', within their regulatory regions via their runt domain, while
CC CBFB is a non-DNA-binding regulatory subunit that allosterically
CC enhances the sequence-specific DNA-binding capacity of RUNX. The
CC heterodimers bind to the core site of a number of enhancers and
CC promoters, including murine leukemia virus, polyomavirus enhancer, T-
CC cell receptor enhancers, LCK, IL3 and GM-CSF promoters. CBF complexes
CC repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell
CC development. They bind to RUNX-binding sequence within the ZBTB7B locus
CC acting as transcriptional silencer and allowing for cytotoxic T cell
CC differentiation. {ECO:0000250|UniProtKB:Q08024}.
CC -!- SUBUNIT: Heterodimer with RUNX1, RUNX2 and RUNX3. Interacts with COPRS.
CC Found in a complex with PRMT5 and RUNX1.
CC {ECO:0000250|UniProtKB:Q08024}.
CC -!- INTERACTION:
CC Q13951; Q9NVM9: INTS13; NbExp=2; IntAct=EBI-718750, EBI-741429;
CC Q13951; P11137: MAP2; NbExp=2; IntAct=EBI-718750, EBI-2682460;
CC Q13951; Q01196: RUNX1; NbExp=3; IntAct=EBI-718750, EBI-925904;
CC Q13951; Q01196-8: RUNX1; NbExp=3; IntAct=EBI-718750, EBI-12001422;
CC Q13951; Q13761-2: RUNX3; NbExp=3; IntAct=EBI-718750, EBI-12145465;
CC Q13951; P12504: vif; Xeno; NbExp=10; IntAct=EBI-718750, EBI-779991;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13951-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13951-2; Sequence=VSP_036044;
CC -!- DISEASE: Note=A chromosomal aberration involving CBFB is associated
CC with acute myeloid leukemia of M4EO subtype. Pericentric inversion
CC inv(16)(p13;q22). The inversion produces a fusion protein that consists
CC of the 165 N-terminal residues of CBF-beta (PEPB2) with the tail region
CC of MYH11. {ECO:0000269|PubMed:8351518}.
CC -!- SIMILARITY: Belongs to the CBF-beta family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CBFbID45.html";
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DR EMBL; AF294326; AAG01553.1; -; mRNA.
DR EMBL; BT006862; AAP35508.1; -; mRNA.
DR EMBL; AK290462; BAF83151.1; -; mRNA.
DR EMBL; CH471092; EAW83067.1; -; Genomic_DNA.
DR EMBL; CH471092; EAW83068.1; -; Genomic_DNA.
DR EMBL; BC018509; AAH18509.1; -; mRNA.
DR EMBL; L20298; AAA02868.1; -; mRNA.
DR CCDS; CCDS10827.1; -. [Q13951-1]
DR CCDS; CCDS45508.1; -. [Q13951-2]
DR PIR; A56840; A56840.
DR PIR; I59579; I59579.
DR RefSeq; NP_001746.1; NM_001755.2. [Q13951-1]
DR RefSeq; NP_074036.1; NM_022845.2. [Q13951-2]
DR PDB; 1CL3; NMR; -; A=4-141.
DR PDB; 1E50; X-ray; 2.60 A; B/D/F/H=2-135.
DR PDB; 1H9D; X-ray; 2.60 A; B/D=2-135.
DR PDB; 4N9F; X-ray; 3.30 A; 0/6/F/L/N/R/a/c/i/k/o/u=1-170.
DR PDB; 6NIL; EM; 3.90 A; B/E/H/K=1-151.
DR PDB; 6P59; X-ray; 2.94 A; A/C=1-165.
DR PDB; 6VGD; X-ray; 4.20 A; G=1-142.
DR PDB; 6VGE; X-ray; 4.25 A; G=1-142.
DR PDB; 6VGG; X-ray; 4.31 A; G=1-142.
DR PDBsum; 1CL3; -.
DR PDBsum; 1E50; -.
DR PDBsum; 1H9D; -.
DR PDBsum; 4N9F; -.
DR PDBsum; 6NIL; -.
DR PDBsum; 6P59; -.
DR PDBsum; 6VGD; -.
DR PDBsum; 6VGE; -.
DR PDBsum; 6VGG; -.
DR AlphaFoldDB; Q13951; -.
DR BMRB; Q13951; -.
DR SMR; Q13951; -.
DR BioGRID; 107313; 90.
DR CORUM; Q13951; -.
DR DIP; DIP-36772N; -.
DR IntAct; Q13951; 36.
DR MINT; Q13951; -.
DR STRING; 9606.ENSP00000415151; -.
DR BindingDB; Q13951; -.
DR ChEMBL; CHEMBL1615386; -.
DR GlyGen; Q13951; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13951; -.
DR MetOSite; Q13951; -.
DR PhosphoSitePlus; Q13951; -.
DR BioMuta; CBFB; -.
DR DMDM; 2498753; -.
DR EPD; Q13951; -.
DR jPOST; Q13951; -.
DR MassIVE; Q13951; -.
DR MaxQB; Q13951; -.
DR PaxDb; Q13951; -.
DR PeptideAtlas; Q13951; -.
DR PRIDE; Q13951; -.
DR ProteomicsDB; 59770; -. [Q13951-1]
DR ProteomicsDB; 59771; -. [Q13951-2]
DR Antibodypedia; 15619; 427 antibodies from 40 providers.
DR DNASU; 865; -.
DR Ensembl; ENST00000290858.11; ENSP00000290858.6; ENSG00000067955.15. [Q13951-1]
DR Ensembl; ENST00000412916.7; ENSP00000415151.2; ENSG00000067955.15. [Q13951-2]
DR GeneID; 865; -.
DR KEGG; hsa:865; -.
DR MANE-Select; ENST00000412916.7; ENSP00000415151.2; NM_022845.3; NP_074036.1. [Q13951-2]
DR UCSC; uc002era.4; human. [Q13951-1]
DR CTD; 865; -.
DR DisGeNET; 865; -.
DR GeneCards; CBFB; -.
DR HGNC; HGNC:1539; CBFB.
DR HPA; ENSG00000067955; Low tissue specificity.
DR MalaCards; CBFB; -.
DR MIM; 121360; gene.
DR neXtProt; NX_Q13951; -.
DR OpenTargets; ENSG00000067955; -.
DR Orphanet; 98829; Acute myeloid leukemia with abnormal bone marrow eosinophils inv(16)(p13q22) or t(16;16)(p13;q22).
DR PharmGKB; PA26114; -.
DR VEuPathDB; HostDB:ENSG00000067955; -.
DR eggNOG; KOG4785; Eukaryota.
DR GeneTree; ENSGT00390000018132; -.
DR HOGENOM; CLU_074992_1_0_1; -.
DR InParanoid; Q13951; -.
DR OMA; CCEGHTE; -.
DR OrthoDB; 1254153at2759; -.
DR PhylomeDB; Q13951; -.
DR TreeFam; TF314675; -.
DR PathwayCommons; Q13951; -.
DR Reactome; R-HSA-8877330; RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs).
DR Reactome; R-HSA-8878166; Transcriptional regulation by RUNX2.
DR Reactome; R-HSA-8931987; RUNX1 regulates estrogen receptor mediated transcription.
DR Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
DR Reactome; R-HSA-8935964; RUNX1 regulates expression of components of tight junctions.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-HSA-8939245; RUNX1 regulates transcription of genes involved in BCR signaling.
DR Reactome; R-HSA-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
DR Reactome; R-HSA-8939247; RUNX1 regulates transcription of genes involved in interleukin signaling.
DR Reactome; R-HSA-8939256; RUNX1 regulates transcription of genes involved in WNT signaling.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
DR Reactome; R-HSA-8941284; RUNX2 regulates chondrocyte maturation.
DR Reactome; R-HSA-8941326; RUNX2 regulates bone development.
DR Reactome; R-HSA-8941332; RUNX2 regulates genes involved in cell migration.
DR Reactome; R-HSA-8941333; RUNX2 regulates genes involved in differentiation of myeloid cells.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8949275; RUNX3 Regulates Immune Response and Cell Migration.
DR Reactome; R-HSA-8951911; RUNX3 regulates RUNX1-mediated transcription.
DR Reactome; R-HSA-8951936; RUNX3 regulates p14-ARF.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR SignaLink; Q13951; -.
DR SIGNOR; Q13951; -.
DR BioGRID-ORCS; 865; 116 hits in 1102 CRISPR screens.
DR ChiTaRS; CBFB; human.
DR EvolutionaryTrace; Q13951; -.
DR GeneWiki; CBFB; -.
DR GenomeRNAi; 865; -.
DR Pharos; Q13951; Tchem.
DR PRO; PR:Q13951; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q13951; protein.
DR Bgee; ENSG00000067955; Expressed in secondary oocyte and 200 other tissues.
DR ExpressionAtlas; Q13951; baseline and differential.
DR Genevisible; Q13951; HS.
DR GO; GO:0016513; C:core-binding factor complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0048469; P:cell maturation; IEA:Ensembl.
DR GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
DR GO; GO:0030098; P:lymphocyte differentiation; IEA:Ensembl.
DR GO; GO:0030099; P:myeloid cell differentiation; IEA:Ensembl.
DR GO; GO:0043371; P:negative regulation of CD4-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0043378; P:positive regulation of CD8-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IMP:CACAO.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR Gene3D; 2.40.250.10; -; 1.
DR InterPro; IPR003417; CBF_beta.
DR InterPro; IPR036552; CBF_bsu_sf.
DR PANTHER; PTHR10276; PTHR10276; 1.
DR Pfam; PF02312; CBF_beta; 1.
DR SUPFAM; SSF50723; SSF50723; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosomal rearrangement; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome.
FT CHAIN 1..182
FT /note="Core-binding factor subunit beta"
FT /id="PRO_0000058301"
FT SITE 165..166
FT /note="Breakpoint for translocation to form CBF-beta-MYH11
FT oncogene in AML, subtype M4EO"
FT VAR_SEQ 166..182
FT /note="VRVSQLLAVTGKKTTRP -> ARRQQDPSPGSNLGGGDDLKLR (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_036044"
FT VARIANT 100
FT /note="P -> A (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1280921900)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036226"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:1E50"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:1E50"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1E50"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1E50"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:1E50"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:1E50"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:1E50"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1E50"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:6P59"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1E50"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:1E50"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:1E50"
FT STRAND 106..115
FT /evidence="ECO:0007829|PDB:1E50"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1E50"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:1E50"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:1E50"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:6P59"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:6P59"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:6P59"
FT MOD_RES Q13951-2:173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
SQ SEQUENCE 182 AA; 21508 MW; 20FB1CC05FBFE4FB CRC64;
MPRVVPDQRS KFENEEFFRK LSRECEIKYT GFRDRPHEER QARFQNACRD GRSEIAFVAT
GTNLSLQFFP ASWQGEQRQT PSREYVDLER EAGKVYLKAP MILNGVCVIW KGWIDLQRLD
GMGCLEFDEE RAQQEDALAQ QAFEEARRRT REFEDRDRSH REEMEVRVSQ LLAVTGKKTT
RP
