CEBPB

Functionⁱ

Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:1741402, PubMed:9374525, PubMed:12048245, PubMed:18647749). Plays also a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant functions with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Plays also a role in intracellular bacteria killing (By similarity). During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation (PubMed:20829347). Essential for female reproduction because of a critical role in ovarian follicle development (By similarity). Restricts osteoclastogenesis: together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity).1 PublicationBy similarity4 Publications

Isoform 2: Essential for gene expression induction in activated macrophages. Plays a major role in immune responses such as CD4⁺ T-cell response, granuloma formation and endotoxin shock. Not essential for intracellular bacteria killing.By similarity

Isoform 3: Acts as a dominant negative through heterodimerization with isoform 2 (PubMed:11741938). Promotes osteoblast differentiation and osteoclastogenesis (By similarity).By similarity1 Publication

GO - Molecular functionⁱ

chromatin binding Source: Ensembl
DNA binding
Source: ProtInc
Traceable author statementⁱ
- 10821850
DNA-binding transcription factor activity
Source: ProtInc
Non-traceable author statementⁱ
- 10821850
DNA-binding transcription factor activity, RNA polymerase II-specific Source: NTNU_SB
glucocorticoid receptor binding Source: Ensembl
histone acetyltransferase binding Source: Ensembl
histone deacetylase binding Source: Ensembl
kinase binding Source: Ensembl
protein heterodimerization activity
Source: ParkinsonsUK-UCL
Non-traceable author statementⁱ
- 15775988
protein homodimerization activity Source: UniProtKB
proximal promoter DNA-binding transcription activator activity, RNA polymerase II-specific Source: Ensembl
proximal promoter DNA-binding transcription repressor activity, RNA polymerase II-specific
Source: UniProtKB
Inferred from sequence or structural similarityⁱ
- 15308669
RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
RNA polymerase II proximal promoter sequence-specific DNA binding Source: Ensembl
RNA polymerase II regulatory region sequence-specific DNA binding
Source: MGI
Inferred from direct assayⁱ
- 7959007
transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding Source: UniProtKB
ubiquitin-like protein ligase binding Source: Ensembl

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

acute-phase response
Source: ProtInc
Traceable author statementⁱ
- 2112087
brown fat cell differentiation Source: Ensembl
cellular response to amino acid stimulus Source: Ensembl
cellular response to interleukin-1 Source: Ensembl
cellular response to lipopolysaccharide Source: Ensembl
cellular response to organic cyclic compound Source: Ensembl
defense response to bacterium Source: UniProtKB
embryonic placenta development Source: Ensembl
granuloma formation Source: UniProtKB
hepatocyte proliferation Source: UniProtKB
immune response
Source: ProtInc
Traceable author statementⁱ
- 2112087
inflammatory response
Source: ProtInc
Traceable author statementⁱ
- 2112087
intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
Source: ParkinsonsUK-UCL
Traceable author statementⁱ
- 14685163
liver regeneration Source: UniProtKB
mammary gland epithelial cell differentiation Source: Ensembl
mammary gland epithelial cell proliferation Source: Ensembl
memory Source: Ensembl
negative regulation of neuron apoptotic process Source: Ensembl
negative regulation of T cell proliferation Source: UniProtKB
negative regulation of transcription by RNA polymerase II
Source: UniProtKB
Inferred from sequence or structural similarityⁱ
- 15308669
neuron differentiation Source: Ensembl
ovarian follicle development Source: UniProtKB
positive regulation of biomineral tissue development
Source: MGI
Inferred from direct assayⁱ
- 27812542
positive regulation of cold-induced thermogenesis
Source: YuBioLab
Inferred from sequence or structural similarityⁱ
- 15762841
positive regulation of fat cell differentiation Source: UniProtKB
positive regulation of interleukin-4 production Source: UniProtKB
positive regulation of osteoblast differentiation Source: Ensembl
positive regulation of sodium-dependent phosphate transport
Source: MGI
Inferred from direct assayⁱ
- 27812542
positive regulation of transcription, DNA-templated
Source: MGI
Inferred from direct assayⁱ
- 27812542
positive regulation of transcription by RNA polymerase II
Source: MGI
Inferred from direct assayⁱ
- 7959007
positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress
Source: ParkinsonsUK-UCL
Inferred from direct assayⁱ
- 15775988
regulation of interleukin-6 biosynthetic process Source: Ensembl
regulation of odontoblast differentiation
Source: UniProtKB
Inferred from sequence or structural similarityⁱ
- 15308669
regulation of osteoclast differentiation Source: UniProtKB
regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from direct assayⁱ
- 20829347
regulation of transcription involved in cell fate commitment Source: UniProtKB
response to endoplasmic reticulum stress
Source: UniProtKB
Inferred from direct assayⁱ
- 20829347
T-helper 1 cell activation Source: UniProtKB
transcription by RNA polymerase II
Source: ProtInc
Traceable author statementⁱ
- 10821850

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Activator, DNA-binding
Biological process	Differentiation, Transcription, Transcription regulation

Enzyme and pathway databases

Reactomeⁱ	R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP) R-HSA-381340 Transcriptional regulation of white adipocyte differentiation
SignaLinkⁱ	P17676
SIGNORⁱ	P17676

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: CCAAT/enhancer-binding protein betaImported Short name: C/EBP betaImported Alternative name(s): Liver activator protein Short name: LAP Liver-enriched inhibitory protein Short name: LIP Nuclear factor NF-IL61 Publication Transcription factor 5 Short name: TCF-5
Gene namesⁱ	Name:CEBPBImported Synonyms:TCF5 ORF Names:PP9092
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 20

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000172216.5
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:1834 CEBPB
MIMⁱ	189965 gene
neXtProtⁱ	NX_P17676

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	235	T → S: Loss of transactivation activity in response to IFNG. 1 Publication		1
Mutagenesisⁱ	288	S → A: Loss of nuclear translocation. 1 Publication		1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	1051
Open Targets More...OpenTargetsⁱ	ENSG00000172216
PharmGKBⁱ	PA26377

Polymorphism and mutation databases

BioMutaⁱ	CEBPB
DMDMⁱ	34223718

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000076617	1 – 345	CCAAT/enhancer-binding protein betaAdd BLAST		345

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	3	Omega-N-methylated arginine; by CARM11 Publication	1
Modified residueⁱ	43	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	43	N6-methylated lysine; alternateBy similarity	1
Modified residueⁱ	129	N6-acetyllysine; by KAT2A and KAT2BBy similarity	1
Modified residueⁱ	132	N6-acetyllysine; by KAT2A and KAT2BBy similarity	1
Modified residueⁱ	133	N6-acetyllysine; by KAT2A and KAT2B; alternateBy similarity	1
Cross-linkⁱ	133	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linkⁱ	174	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linkⁱ	174	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linkⁱ	185	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	187	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	226	Phosphothreonine; by GSK3-betaBy similarity	1
Glycosylationⁱ	227	O-linked (GlcNAc) serineBy similarity	1
Glycosylationⁱ	228	O-linked (GlcNAc) serineBy similarity	1
Modified residueⁱ	231	Phosphoserine; by GSK3-betaBy similarity	1
Modified residueⁱ	235	Phosphothreonine; by RPS6KA1, CDK2 and MAPK2 Publications	1
Cross-linkⁱ	260	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	262	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	266	Phosphothreonine; by RPS6KA1 and PKC/PRKCABy similarity	1
Modified residueⁱ	288	Phosphoserine; by PKC/PRKCA1 Publication	1
Modified residueⁱ	325	Phosphoserine; by CaMK2By similarity	1
Cross-linkⁱ	332	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationⁱ

Methylated. Methylation at Arg-3 by CARM1 and at Lys-43 by EHMT2 inhibit transactivation activity. Methylation is probably inhibited by phosphorylation at Thr-235.2 Publications

Sumoylated by polymeric chains of SUMO2 or SUMO3 (PubMed:12810706). Sumoylation at Lys-174 is required for inhibition of T-cells proliferation. In adipocytes, sumoylation at Lys-174 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation. Desumoylated by SENP2, which abolishes ubiquitination and stabilizes protein levels (By similarity).By similarity1 Publication

Ubiquitinated, leading to proteasomal degradation.By similarity

Phosphorylated at Thr-235 by MAPK and CDK2, serves to prime phosphorylation at Thr-226 and Ser-231 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis. MAPK and CDK2 act sequentially to maintain Thr-235 in the primed phosphorylated state during mitotical cloning expansion and thereby progression of terminal differentiation. Phosphorylation at Thr-266 enhances transactivation activity. Phosphorylation at Ser-325 in response to calcium increases transactivation activity. Phosphorylated at Thr-235 by RPS6KA1 (PubMed:11684016).By similarity1 Publication

O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding activity which delays the adipocyte differentiation program.By similarity

Acetylated. Acetylation at Lys-43 is an important and dynamic regulatory event that contributes to its ability to transactivate target genes, including those associated with adipogenesis and adipocyte function. Deacetylation by HDAC1 represses its transactivation activity. Acetylated by KAT2A and KAT2B within a cluster of lysine residues between amino acids 129-133, this acetylation is strongly induced by glucocorticoid treatment and enhances transactivation activity.By similarity

Keywords - PTMⁱ

Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	P17676
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P17676
PaxDbⁱ	P17676
PeptideAtlas More...PeptideAtlasⁱ	P17676
PRIDEⁱ	P17676
ProteomicsDBⁱ	53503

PTM databases

iPTMnetⁱ	P17676
PhosphoSitePlusⁱ	P17676

Expressionⁱ

Tissue specificityⁱ

Expressed at low levels in the lung, kidney and spleen.

Inductionⁱ

By ER stress.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000172216 Expressed in 240 organ(s), highest expression level in layer of synovial tissue
CleanExⁱ	HS_CEBPB
Genevisibleⁱ	P17676 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB004213 HPA061355 HPA062267

HPAⁱ

CAB004213
HPA061355
HPA062267

Interactionⁱ

Subunit structureⁱ

Binds DNA as a homodimer and as a heterodimer (PubMed:11018027, PubMed:11257229, PubMed:11792321). Interacts with ATF4. Binds DNA as a heterodimer with ATF4 (PubMed:11018027). Interacts with MYB; within the complex, MYB and CEBPB bind to different promoter regions (PubMed:11792321). Can form stable heterodimers with CEBPD (PubMed:1741402). Can form stable heterodimers with CEBPA and CEBPE (By similarity). Isoform 2 and isoform 3 also form heterodimers. Interacts with TRIM28 and PTGES2. Interacts with PRDM16. Interacts with CCDC85B. Forms a complex with THOC5. Interacts with ZNF638; this interaction increases transcriptional activation. Interacts with CIDEA and CIDEC; these interactions increase transcriptional activation of a subset of CEBPB downstream target genes (By similarity). Interacts with DDIT3/CHOP (PubMed:20829347). Interacts with EP300; recruits EP300 to chromatin. Interacts with RORA; the interaction disrupts interaction with EP300. Interacts (not methylated) with MED23, MED26, SMARCA2, SMARCB1 and SMARCC1 (PubMed:20111005). Interacts with KAT2A and KAT2B (By similarity). Interacts with ATF5; EP300 is required for ATF5 and CEBPB interaction and DNA binding (By similarity). Interacts with NFE2L1; the heterodimer represses expression of DSPP during odontoblast differentiation (By similarity).By similarity5 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
ATF4	P18848	2	EBI-969696,EBI-492498
BATF	Q16520	2	EBI-969696,EBI-749503
CARM1	Q86X55	2	EBI-969696,EBI-2339854
CEBPA	P49715	2	EBI-969696,EBI-1172054
CEBPG	P53567	2	EBI-969696,EBI-740209
DDIT3	P35638	2	EBI-969696,EBI-742651
E2	P03120	2	EBI-969696,EBI-1779322	From Human papillomavirus type 16.
E2	P03122	3	EBI-969696,EBI-7028618	From Bovine papillomavirus type 1.
E2	P06422	4	EBI-969696,EBI-7136851	From Human papillomavirus type 8.
E2	P06790	4	EBI-969696,EBI-7010629	From Human papillomavirus type 18.
MUC1	P15941	8	EBI-969696,EBI-10053698
TP53	P04637	4	EBI-969696,EBI-366083

GO - Molecular functionⁱ

glucocorticoid receptor binding Source: Ensembl
histone acetyltransferase binding Source: Ensembl
histone deacetylase binding Source: Ensembl
kinase binding Source: Ensembl
protein heterodimerization activity
Source: ParkinsonsUK-UCL
Non-traceable author statementⁱ
- 15775988
protein homodimerization activity Source: UniProtKB
ubiquitin-like protein ligase binding Source: Ensembl

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	107480, 69 interactors
ComplexPortalⁱ	CPX-3361 C/EBPbeta complex CPX-504 c-Myb-C/EBPbeta complex CPX-70 CHOP-C/EBPbeta complex
CORUMⁱ	P17676
Database of interacting proteins More...DIPⁱ	DIP-35345N
ELMⁱ	P17676
IntActⁱ	P17676, 25 interactors
Molecular INTeraction database More...MINTⁱ	P17676
STRINGⁱ	9606.ENSP00000305422

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	269 – 271	Combined sources	3
Helixⁱ	272 – 328	Combined sources	57
Turnⁱ	329 – 331	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P17676
SMRⁱ	P17676
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P17676

EvolutionaryTraceⁱ

P17676

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	271 – 334	bZIPPROSITE-ProRule annotationAdd BLAST		64

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 24	Required for Lys-174 sumoylationAdd BLAST	24
Regionⁱ	24 – 135	Required for MYC transcriptional repressionBy similarityAdd BLAST	112
Regionⁱ	275 – 295	Basic motifPROSITE-ProRule annotationAdd BLAST	21
Regionⁱ	297 – 304	Leucine-zipperPROSITE-ProRule annotation	8

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	116 – 124	9aaTAD		9

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	162 – 170	Poly-Pro		9

Domainⁱ

the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.1 Publication

Sequence similaritiesⁱ

Belongs to the bZIP family. C/EBP subfamily.Curated

Phylogenomic databases

eggNOGⁱ	ENOG410ISXW Eukaryota ENOG410XX4P LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000063192
HOGENOMⁱ	HOG000013112
HOVERGENⁱ	HBG050879
InParanoidⁱ	P17676
KEGG Orthology (KO) More...KOⁱ	K10048
OMAⁱ	CKKPAEY
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G11FC
PhylomeDBⁱ	P17676
TreeFamⁱ	TF105008

Family and domain databases

InterProⁱ	View protein in InterPro IPR004827 bZIP IPR016468 C/EBP_chordates
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF07716 bZIP_2, 1 hit
PIRSFⁱ	PIRSF005879 CCAAT/enhancer-binding, 1 hit
SMARTⁱ	View protein in SMART SM00338 BRLZ, 1 hit
PROSITEⁱ	View protein in PROSITE PS50217 BZIP, 1 hit

Sequences (3)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative initiation. Align Add to basket

Isoform 1 (identifier: P17676-1) [UniParc]FASTA Add to basket

Also known as: C/EBPbeta-FL

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
MQRLVAWDPA CLPLPPPPPA FKSMEVANFY YEADCLAAAY GGKAAPAAPP 
        60         70         80         90        100
AARPGPRPPA GELGSIGDHE RAIDFSPYLE PLGAPQAPAP ATATDTFEAA 
       110        120        130        140        150
PPAPAPAPAS SGQHHDFLSD LFSDDYGGKN CKKPAEYGYV SLGRLGAAKG 
       160        170        180        190        200
ALHPGCFAPL HPPPPPPPPP AELKAEPGFE PADCKRKEEA GAPGGGAGMA 
       210        220        230        240        250
AGFPYALRAY LGYQAVPSGS SGSLSTSSSS SPPGTPSPAD AKAPPTACYA 
       260        270        280        290        300
GAAPAPSQVK SKAKKTVDKH SDEYKIRRER NNIAVRKSRD KAKMRNLETQ 
       310        320        330        340 
HKVLELTAEN ERLQKKVEQL SRELSTLRNL FKQLPEPLLA SSGHC

Length:345

Mass (Da):36,106

Last modified:August 22, 2003 - v2

Checksum:ⁱ9B725BD6CCAA771D

GO

Isoform 2 (identifier: P17676-2) [UniParc]FASTA Add to basket

Also known as: C/EBPbeta-LAP

The sequence of this isoform differs from the canonical sequence as follows:
1-23: Missing.

« Hide

        10         20         30         40         50
MEVANFYYEA DCLAAAYGGK AAPAAPPAAR PGPRPPAGEL GSIGDHERAI 
        60         70         80         90        100
DFSPYLEPLG APQAPAPATA TDTFEAAPPA PAPAPASSGQ HHDFLSDLFS 
       110        120        130        140        150
DDYGGKNCKK PAEYGYVSLG RLGAAKGALH PGCFAPLHPP PPPPPPPAEL 
       160        170        180        190        200
KAEPGFEPAD CKRKEEAGAP GGGAGMAAGF PYALRAYLGY QAVPSGSSGS 
       210        220        230        240        250
LSTSSSSSPP GTPSPADAKA PPTACYAGAA PAPSQVKSKA KKTVDKHSDE 
       260        270        280        290        300
YKIRRERNNI AVRKSRDKAK MRNLETQHKV LELTAENERL QKKVEQLSRE 
       310        320 
LSTLRNLFKQ LPEPLLASSG HC

Show »

Length:322

Mass (Da):33,592

Checksum:ⁱ842B381C36DFA8CE

GO

Isoform 3 (identifier: P17676-3) [UniParc]FASTA Add to basket

Also known as: C/EBPbeta-LIP

The sequence of this isoform differs from the canonical sequence as follows:
1-198: Missing.

« Hide

        10         20         30         40         50
MAAGFPYALR AYLGYQAVPS GSSGSLSTSS SSSPPGTPSP ADAKAPPTAC 
        60         70         80         90        100
YAGAAPAPSQ VKSKAKKTVD KHSDEYKIRR ERNNIAVRKS RDKAKMRNLE 
       110        120        130        140 
TQHKVLELTA ENERLQKKVE QLSRELSTLR NLFKQLPEPL LASSGHC

Show »

Length:147

Mass (Da):15,938

Checksum:ⁱ3D75D9D752E47B88

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	241	A → P no nucleotide entry (PubMed:7635140).Curated		1
Sequence conflictⁱ	253	A → G in CAA36794 (PubMed:2112087).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_016300	195	G → S1 PublicationCorresponds to variant dbSNP:rs4253440Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_053313	1 – 198	Missing in isoform 3. CuratedAdd BLAST		198
Alternative sequenceⁱVSP_053314	1 – 23	Missing in isoform 2. CuratedAdd BLAST		23

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X52560 Genomic DNA Translation: CAA36794.1 AF289608 mRNA Translation: AAL55792.1 AY193834 Genomic DNA Translation: AAN86350.1 AK291536 mRNA Translation: BAF84225.1 AL161937 Genomic DNA No translation available. CH471077 Genomic DNA Translation: EAW75629.1 BC007538 mRNA Translation: AAH07538.1 BC021931 mRNA Translation: AAH21931.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS13429.1 [P17676-1]
PIRⁱ	S12788 S66246
NCBI Reference Sequences More...RefSeqⁱ	NP_001272807.1, NM_001285878.1 [P17676-2] NP_001272808.1, NM_001285879.1 [P17676-3] NP_005185.2, NM_005194.3 [P17676-1]
UniGeneⁱ	Hs.517106 Hs.719041 Hs.720603

Genome annotation databases

Ensemblⁱ	ENST00000303004; ENSP00000305422; ENSG00000172216 [P17676-1]
GeneIDⁱ	1051
KEGGⁱ	hsa:1051
UCSC genome browser More...UCSCⁱ	uc002xvi.4 human [P17676-1]

Keywords - Coding sequence diversityⁱ

Alternative initiation, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P17676	CCAAT/enhancer binding protein (C/EBP), beta		PANTR		345	UniRef100_P17676
Isoform 2 of CCAAT/enhancer-binding protein beta		HUMAN		322
P17676-3	CCAAT/enhancer binding protein (C/EBP), beta		PANTR		347	UniRef100_K7D2A9
CEBPB protein (Fragment)		HUMAN		137
Transcription factor C/EBP beta (Fragment)		HUMAN		92

Protein	Similar proteins		Species	Score	Length	Source
P17676	CCAAT/enhancer-binding protein beta		BOVIN		348	UniRef90_P17676
CCAAT/enhancer binding protein (C/EBP), beta		PANTR		345
Isoform 2 of CCAAT/enhancer-binding protein beta		HUMAN		322
CCAAT/enhancer-binding protein beta		ERIEU		369
CCAAT/enhancer-binding protein beta		ODORO		348
+63

Protein	Similar proteins		Species	Score	Length	Source
P17676	CCAAT/enhancer-binding protein beta		BOVIN		348	UniRef50_P17676
CCAAT/enhancer-binding protein beta		CHICK		328
CCAAT/enhancer binding protein (C/EBP), beta		PANTR		345
Isoform 2 of CCAAT/enhancer-binding protein beta		HUMAN		322
CCAAT/enhancer-binding protein beta		ERIEU		369
+88

Cross-referencesⁱ

Web resourcesⁱ

SeattleSNPs

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X52560 Genomic DNA Translation: CAA36794.1 AF289608 mRNA Translation: AAL55792.1 AY193834 Genomic DNA Translation: AAN86350.1 AK291536 mRNA Translation: BAF84225.1 AL161937 Genomic DNA No translation available. CH471077 Genomic DNA Translation: EAW75629.1 BC007538 mRNA Translation: AAH07538.1 BC021931 mRNA Translation: AAH21931.1
CCDSⁱ	CCDS13429.1 [P17676-1]
PIRⁱ	S12788 S66246
RefSeqⁱ	NP_001272807.1, NM_001285878.1 [P17676-2] NP_001272808.1, NM_001285879.1 [P17676-3] NP_005185.2, NM_005194.3 [P17676-1]
UniGeneⁱ	Hs.517106 Hs.719041 Hs.720603

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1GTW	X-ray	1.85	A/B	259-336	[»]
	1GU4	X-ray	1.80	A/B	259-336	[»]
	1GU5	X-ray	2.10	A/B	259-336	[»]
	1H88	X-ray	2.80	A/B	259-336	[»]
	1H89	X-ray	2.45	A/B	273-336	[»]
	1H8A	X-ray	2.23	A/B	259-336	[»]
	1HJB	X-ray	3.00	A/B/D/E	259-345	[»]
	1IO4	X-ray	3.00	A/B	259-336	[»]
	2E42	X-ray	1.80	A/B	259-336	[»]
	2E43	X-ray	2.10	A/B	259-336	[»]
ProteinModelPortalⁱ	P17676
SMRⁱ	P17676
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	107480, 69 interactors
ComplexPortalⁱ	CPX-3361 C/EBPbeta complex CPX-504 c-Myb-C/EBPbeta complex CPX-70 CHOP-C/EBPbeta complex
CORUMⁱ	P17676
DIPⁱ	DIP-35345N
ELMⁱ	P17676
IntActⁱ	P17676, 25 interactors
MINTⁱ	P17676
STRINGⁱ	9606.ENSP00000305422

PTM databases

iPTMnetⁱ	P17676
PhosphoSitePlusⁱ	P17676

Polymorphism and mutation databases

BioMutaⁱ	CEBPB
DMDMⁱ	34223718

Proteomic databases

EPDⁱ	P17676
MaxQBⁱ	P17676
PaxDbⁱ	P17676
PeptideAtlasⁱ	P17676
PRIDEⁱ	P17676
ProteomicsDBⁱ	53503

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	1051
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000303004; ENSP00000305422; ENSG00000172216 [P17676-1]
GeneIDⁱ	1051
KEGGⁱ	hsa:1051
UCSCⁱ	uc002xvi.4 human [P17676-1]

Organism-specific databases

CTDⁱ	1051
DisGeNETⁱ	1051
EuPathDBⁱ	HostDB:ENSG00000172216.5
GeneCardsⁱ	CEBPB
H-InvDBⁱ	HIX0174729
HGNCⁱ	HGNC:1834 CEBPB
HPAⁱ	CAB004213 HPA061355 HPA062267
MIMⁱ	189965 gene
neXtProtⁱ	NX_P17676
OpenTargetsⁱ	ENSG00000172216
PharmGKBⁱ	PA26377
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410ISXW Eukaryota ENOG410XX4P LUCA
GeneTreeⁱ	ENSGT00530000063192
HOGENOMⁱ	HOG000013112
HOVERGENⁱ	HBG050879
InParanoidⁱ	P17676
KOⁱ	K10048
OMAⁱ	CKKPAEY
OrthoDBⁱ	EOG091G11FC
PhylomeDBⁱ	P17676
TreeFamⁱ	TF105008

Enzyme and pathway databases

Reactomeⁱ	R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP) R-HSA-381340 Transcriptional regulation of white adipocyte differentiation
SignaLinkⁱ	P17676
SIGNORⁱ	P17676

Miscellaneous databases

ChiTaRSⁱ	CEBPB human
EvolutionaryTraceⁱ	P17676
GeneWikiⁱ	CEBPB
GenomeRNAiⁱ	1051
Protein Ontology More...PROⁱ	PR:P17676
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000172216 Expressed in 240 organ(s), highest expression level in layer of synovial tissue
CleanExⁱ	HS_CEBPB
Genevisibleⁱ	P17676 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR004827 bZIP IPR016468 C/EBP_chordates
Pfamⁱ	View protein in Pfam PF07716 bZIP_2, 1 hit
PIRSFⁱ	PIRSF005879 CCAAT/enhancer-binding, 1 hit
SMARTⁱ	View protein in SMART SM00338 BRLZ, 1 hit
PROSITEⁱ	View protein in PROSITE PS50217 BZIP, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CEBPB_HUMAN
Accessionⁱ	P17676Primary (citable) accession number: P17676 Secondary accession number(s): A8K671, Q96IH2, Q9H4Z5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
	Last sequence update:	August 22, 2003
	Last modified:	November 7, 2018
	This is version 202 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Human chromosome 20
Human chromosome 20: entries, gene names and cross-references to MIM
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

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UniProtKB - P17676 (CEBPB_HUMAN)

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CCAAT/enhancer-binding protein beta

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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Keywords - PTMi

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<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

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<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ