Q13951 (PEBB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

CBFB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	182 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Heterodimer with RUNX1. Interacts with COPRS By similarity. Found in a complex with PRMT5, RUNX1 and CBFB By similarity.
Subcellular location	Nucleus Potential.
Involvement in disease	A chromosomal aberration involving CBFB is associated with acute myeloid leukemia of M4EO subtype. Pericentric inversion inv16(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.
Sequence similarities	Belongs to the CBF-beta family.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell maturation Inferred from electronic annotation. Source: Compara definitive hemopoiesis Inferred from electronic annotation. Source: Compara lymphocyte differentiation Inferred from electronic annotation. Source: Compara myeloid cell differentiation Inferred from electronic annotation. Source: Compara osteoblast differentiation Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara transcription from RNA polymerase II promoter Traceable author statement Ref.8. Source: ProtInc
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding transcription factor activity Traceable author statement Ref.8PubMed 9751756. Source: ProtInc transcription coactivator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Asun	Q9NVM9	2	EBI-718750,EBI-741429
MAP2	P11137	2	EBI-718750,EBI-2682460
vif	P12504	5	EBI-718750,EBI-779991	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13951-1)

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.

Isoform 2 (identifier: Q13951-2)

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

Note: Contains a phosphoserine at position 173.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 182

182

Core-binding factor subunit beta

PRO_0000058301

Sites

Site

165 – 166

2

Breakpoint for translocation to form CBF-beta-MYH11 oncogene in AML, subtype M4EO

Natural variations

Alternative sequence

166 – 182

17

VRVSQ…KTTRP → ARRQQDPSPGSNLGGGDDLK LR in isoform 2.

VSP_036044

Natural variant

100

1

P → A in a breast cancer sample; somatic mutation. Ref.16

VAR_036226

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

182

Helix Strand Turn

Details...

Helix

8 – 14

7

Helix

16 – 19

4

Beta strand

25 – 29

5

Beta strand

33 – 35

3

Helix

37 – 49

13

Beta strand

52 – 57

6

Turn

58 – 61

4

Beta strand

65 – 67

3

Turn

83 – 85

3

Beta strand

86 – 91

6

Beta strand

94 – 103

10

Beta strand

106 – 115

10

Turn

116 – 118

3

Beta strand

119 – 127

9

Helix

129 – 134

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 20FB1CC05FBFE4FB	FASTA	182	21,508
	10 20 30 40 50 60 MPRVVPDQRS KFENEEFFRK LSRECEIKYT GFRDRPHEER QARFQNACRD GRSEIAFVAT 70 80 90 100 110 120 GTNLSLQFFP ASWQGEQRQT PSREYVDLER EAGKVYLKAP MILNGVCVIW KGWIDLQRLD 130 140 150 160 170 180 GMGCLEFDEE RAQQEDALAQ QAFEEARRRT REFEDRDRSH REEMEVRVSQ LLAVTGKKTT RP
	Isoform 2 [UniParc]. Checksum: 277B13D2A2ED18E4	FASTA	187	21,991
	10 20 30 40 50 60 MPRVVPDQRS KFENEEFFRK LSRECEIKYT GFRDRPHEER QARFQNACRD GRSEIAFVAT 70 80 90 100 110 120 GTNLSLQFFP ASWQGEQRQT PSREYVDLER EAGKVYLKAP MILNGVCVIW KGWIDLQRLD 130 140 150 160 170 180 GMGCLEFDEE RAQQEDALAQ QAFEEARRRT REFEDRDRSH REEMEARRQQ DPSPGSNLGG GDDLKLR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Liu P.P. Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Eye.
[6]	"Structure of the leukemia-associated human CBFB gene." Hajra A., Collins F.S. Genomics 26:571-579(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-26 (ISOFORMS 1/2).
[7]	Erratum Hajra A., Collins F.S. Genomics 38:107-107(1996) [PubMed] [Europe PMC] [Abstract]
[8]	"Fusion between transcription factor CBF beta/PEBP2 beta and a myosin heavy chain in acute myeloid leukemia." Liu P., Tarle S.A., Hajra A., Claxton D.F., Marlton P., Freedman M., Siciliano M.J., Collins F.S. Science 261:1041-1044(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-182 (ISOFORM 1). Tissue: Brain.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Structural basis for the heterodimeric interaction between the acute leukaemia-associated transcription factors AML1 and CBFbeta." Warren A.J., Bravo J., Williams R.L., Rabbitts T.H. EMBO J. 19:3004-3015(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-135 IN COMPLEX WITH RUNX1.
[14]	"The leukemia-associated AML1 (Runx1) -- CBF beta complex functions as a DNA-induced molecular clamp." Bravo J., Li Z., Speck N.A., Warren A.J. Nat. Struct. Biol. 8:371-378(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-135 IN COMPLEX WITH RUNX1 AND DNA.
[15]	"Molecular insights into PEBP2/CBF beta-SMMHC associated acute leukemia revealed from the structure of PEBP2/CBF beta." Goger M., Gupta V., Kim W.Y., Shigesada K., Ito Y., Werner M.H. Nat. Struct. Biol. 6:620-623(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 4-141.
[16]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-100.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00016746.
IPI00024871.

PIR

A56840.
I59579.

RefSeq

NP_001746.1. NM_001755.2.
NP_074036.1. NM_022845.2.

UniGene

Hs.460988.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CL3	NMR	-	A	4-141	[»]
1E50	X-ray	2.60	B/D/F/H	2-135	[»]
1H9D	X-ray	2.60	B/D	2-135	[»]

ProteinModelPortal

Q13951.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13951. 21 interactions.

MINT

MINT-1414765.

STRING

9606.ENSP00000415151.

PTM databases

PhosphoSite

Q13951.

Polymorphism databases

DMDM

2498753.

Proteomic databases

PaxDb

Q13951.

PeptideAtlas

Q13951.

PRIDE

Q13951.

Protocols and materials databases

DNASU

865.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000290858; ENSP00000290858; ENSG00000067955.
ENST00000412916; ENSP00000415151; ENSG00000067955.

GeneID

865.

KEGG

hsa:865.

UCSC

uc002era.3. human.
uc002erb.3. human.

Organism-specific databases

CTD

865.

GeneCards

GC16P067063.

HGNC

HGNC:1539. CBFB.

HPA

HPA038852.

MIM

121360. gene.

neXtProt

NX_Q13951.

Orphanet

98829. Acute myeloid leukemia with abnormal bone marrow eosinophils inv(16)(p13q22) or t(16;16)(p13;q22).

PharmGKB

PA26114.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG245525.

HOGENOM

HOG000008040.

HOVERGEN

HBG000541.

InParanoid

Q13951.

OMA

KECDFDK.

OrthoDB

EOG4933K1.

PhylomeDB

Q13951.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Gene expression databases

ArrayExpress

Q13951.

Bgee

Q13951.

CleanEx

HS_CBFB.

Genevestigator

Q13951.

GermOnline

ENSG00000067955. Homo sapiens.

Family and domain databases

Gene3D

2.40.250.10. 1 hit.

InterPro

IPR003417. CBF_beta.
[Graphical view]

PANTHER

PTHR10276. PTHR10276. 1 hit.

Pfam

PF02312. CBF_beta. 1 hit.
[Graphical view]

SUPFAM

SSF50723. CBF_beta. 1 hit.

ProtoNet

Search...

Other

ChEMBL

CHEMBL1615386.

ChiTaRS

CBFB. human.

EvolutionaryTrace

Q13951.

GenomeRNAi

865.

NextBio

3608.

SOURCE

Search...

Entry information

Entry name

PEBB_HUMAN

Accession

Primary (citable) accession number: Q13951
Secondary accession number(s): A8K347, Q13124, Q9HCT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.