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Protein

CCAAT/enhancer-binding protein beta

Gene

CEBPB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (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 (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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiP17676.

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-IL6
Transcription factor 5
Short name:
TCF-5
Gene namesi
Name:CEBPBImported
Synonyms:TCF5
ORF Names:PP9092
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:1834. CEBPB.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication

  • Note: Translocates to the nucleus when phosphorylated at Ser-288. In T-cells when sumoylated drawn to pericentric heterochromatin thereby allowing proliferation (By similarity).By similarity1 Publication

GO - Cellular componenti

  • CHOP-C/EBP complex Source: ParkinsonsUK-UCL
  • condensed chromosome, centromeric region Source: Ensembl
  • cytoplasm Source: UniProtKB-SubCell
  • nuclear chromatin Source: Ensembl
  • nuclear matrix Source: Ensembl
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi235 – 2351T → S: Loss of transactivation activity in response to IFNG. 1 Publication
Mutagenesisi288 – 2881S → A: Loss of nuclear translocation. 1 Publication

Organism-specific databases

PharmGKBiPA26377.

Polymorphism and mutation databases

BioMutaiCEBPB.
DMDMi34223718.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345CCAAT/enhancer-binding protein betaPRO_0000076617Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31Omega-N-methylated arginine; by CARM11 Publication
Modified residuei43 – 431N6-acetyllysineBy similarity
Modified residuei43 – 431N6-methylated lysineBy similarity
Modified residuei129 – 1291N6-acetyllysine; by KAT2A and KAT2BBy similarity
Modified residuei132 – 1321N6-acetyllysine; by KAT2A and KAT2BBy similarity
Modified residuei133 – 1331N6-acetyllysine; by KAT2A and KAT2BBy similarity
Cross-linki174 – 174Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity1 Publication
Modified residuei226 – 2261Phosphothreonine; by GSK3-betaBy similarity
Glycosylationi227 – 2271O-linked (GlcNAc)By similarity
Glycosylationi228 – 2281O-linked (GlcNAc)By similarity
Modified residuei231 – 2311Phosphoserine; by GSK3-betaBy similarity
Modified residuei235 – 2351Phosphothreonine; by RPS6KA1, CDK2 and MAPKBy similarity2 Publications
Modified residuei266 – 2661Phosphothreonine; by RPS6KA1 and PKC/PRKCABy similarity
Modified residuei288 – 2881Phosphoserine; by PKC/PRKCA1 Publication
Modified residuei325 – 3251Phosphoserine; by CaMK2By similarity

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

MaxQBiP17676.
PaxDbiP17676.
PeptideAtlasiP17676.
PRIDEiP17676.

PTM databases

PhosphoSiteiP17676.

Expressioni

Tissue specificityi

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

Inductioni

By ER stress.1 Publication

Gene expression databases

BgeeiP17676.
CleanExiHS_CEBPB.
GenevisibleiP17676. HS.

Organism-specific databases

HPAiCAB004213.

Interactioni

Subunit structurei

Binds DNA as a dimer and can form stable heterodimers with CEBPA, CEBPD and CEBPG. 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. Interacts with DDIT3/CHOP.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).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CARM1Q86X552EBI-969696,EBI-2339854
E2P031202EBI-969696,EBI-1779322From a different organism.
E2P031223EBI-969696,EBI-7028618From a different organism.
E2P064224EBI-969696,EBI-7136851From a different organism.
E2P067904EBI-969696,EBI-7010629From a different organism.
MUC1P159418EBI-969696,EBI-10053698
TP53P046374EBI-969696,EBI-366083

Protein-protein interaction databases

BioGridi107480. 65 interactions.
DIPiDIP-35345N.
IntActiP17676. 15 interactions.
MINTiMINT-230873.
STRINGi9606.ENSP00000305422.

Structurei

Secondary structure

1
345
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi269 – 2713Combined sources
Helixi272 – 32857Combined sources
Turni329 – 3313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GTWX-ray1.85A/B259-336[»]
1GU4X-ray1.80A/B259-336[»]
1GU5X-ray2.10A/B259-336[»]
1H88X-ray2.80A/B259-336[»]
1H89X-ray2.45A/B273-336[»]
1H8AX-ray2.23A/B259-336[»]
1HJBX-ray3.00A/B/D/E259-345[»]
1IO4X-ray3.00A/B259-336[»]
2E42X-ray1.80A/B259-336[»]
2E43X-ray2.10A/B259-336[»]
ProteinModelPortaliP17676.
SMRiP17676. Positions 268-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17676.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini271 – 33464bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2424Required for Lys-174 sumoylationAdd
BLAST
Regioni24 – 135112Required for MYC transcriptional repressionBy similarityAdd
BLAST
Regioni275 – 29521Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni297 – 3048Leucine-zipperPROSITE-ProRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi116 – 12499aaTAD

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi162 – 1709Poly-Pro

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
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG299311.
GeneTreeiENSGT00530000063192.
HOGENOMiHOG000013112.
HOVERGENiHBG050879.
InParanoidiP17676.
KOiK10048.
OMAiCKKPAEY.
OrthoDBiEOG7R56TQ.
PhylomeDBiP17676.
TreeFamiTF105008.

Family and domain databases

InterProiIPR004827. bZIP.
IPR031106. C/EBP.
IPR016468. C/EBP_chordates.
[Graphical view]
PANTHERiPTHR23334. PTHR23334. 1 hit.
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005879. CCAAT/enhancer-binding. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

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

Also known as: C/EBPbeta-LAP

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

Show »
Length:322
Mass (Da):33,592
Checksum:i842B381C36DFA8CE
GO
Isoform 3 (identifier: P17676-3) [UniParc]FASTAAdd to basket

Also known as: C/EBPbeta-LIP

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

Show »
Length:147
Mass (Da):15,938
Checksum:i3D75D9D752E47B88
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti241 – 2411A → P no nucleotide entry (PubMed:7635140).Curated
Sequence conflicti253 – 2531A → G in CAA36794 (PubMed:2112087).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti195 – 1951G → S.1 Publication
Corresponds to variant rs4253440 [ dbSNP | Ensembl ].
VAR_016300

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 198198Missing in isoform 3. CuratedVSP_053313Add
BLAST
Alternative sequencei1 – 2323Missing in isoform 2. CuratedVSP_053314Add
BLAST

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. Translation: CAC14276.1.
CH471077 Genomic DNA. Translation: EAW75629.1.
BC007538 mRNA. Translation: AAH07538.1.
BC021931 mRNA. Translation: AAH21931.1.
CCDSiCCDS13429.1. [P17676-1]
PIRiS12788.
S66246.
RefSeqiNP_001272807.1. NM_001285878.1. [P17676-2]
NP_001272808.1. NM_001285879.1. [P17676-3]
NP_005185.2. NM_005194.3. [P17676-1]
UniGeneiHs.517106.
Hs.719041.
Hs.720603.

Genome annotation databases

EnsembliENST00000303004; ENSP00000305422; ENSG00000172216.
GeneIDi1051.
KEGGihsa:1051.
UCSCiuc002xvi.2. human. [P17676-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

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. Translation: CAC14276.1.
CH471077 Genomic DNA. Translation: EAW75629.1.
BC007538 mRNA. Translation: AAH07538.1.
BC021931 mRNA. Translation: AAH21931.1.
CCDSiCCDS13429.1. [P17676-1]
PIRiS12788.
S66246.
RefSeqiNP_001272807.1. NM_001285878.1. [P17676-2]
NP_001272808.1. NM_001285879.1. [P17676-3]
NP_005185.2. NM_005194.3. [P17676-1]
UniGeneiHs.517106.
Hs.719041.
Hs.720603.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GTWX-ray1.85A/B259-336[»]
1GU4X-ray1.80A/B259-336[»]
1GU5X-ray2.10A/B259-336[»]
1H88X-ray2.80A/B259-336[»]
1H89X-ray2.45A/B273-336[»]
1H8AX-ray2.23A/B259-336[»]
1HJBX-ray3.00A/B/D/E259-345[»]
1IO4X-ray3.00A/B259-336[»]
2E42X-ray1.80A/B259-336[»]
2E43X-ray2.10A/B259-336[»]
ProteinModelPortaliP17676.
SMRiP17676. Positions 268-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107480. 65 interactions.
DIPiDIP-35345N.
IntActiP17676. 15 interactions.
MINTiMINT-230873.
STRINGi9606.ENSP00000305422.

PTM databases

PhosphoSiteiP17676.

Polymorphism and mutation databases

BioMutaiCEBPB.
DMDMi34223718.

Proteomic databases

MaxQBiP17676.
PaxDbiP17676.
PeptideAtlasiP17676.
PRIDEiP17676.

Protocols and materials databases

DNASUi1051.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303004; ENSP00000305422; ENSG00000172216.
GeneIDi1051.
KEGGihsa:1051.
UCSCiuc002xvi.2. human. [P17676-1]

Organism-specific databases

CTDi1051.
GeneCardsiGC20P048807.
H-InvDBHIX0174729.
HGNCiHGNC:1834. CEBPB.
HPAiCAB004213.
MIMi189965. gene.
neXtProtiNX_P17676.
PharmGKBiPA26377.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG299311.
GeneTreeiENSGT00530000063192.
HOGENOMiHOG000013112.
HOVERGENiHBG050879.
InParanoidiP17676.
KOiK10048.
OMAiCKKPAEY.
OrthoDBiEOG7R56TQ.
PhylomeDBiP17676.
TreeFamiTF105008.

Enzyme and pathway databases

ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiP17676.

Miscellaneous databases

EvolutionaryTraceiP17676.
GeneWikiiCEBPB.
GenomeRNAii1051.
NextBioi4401.
PROiP17676.
SOURCEiSearch...

Gene expression databases

BgeeiP17676.
CleanExiHS_CEBPB.
GenevisibleiP17676. HS.

Family and domain databases

InterProiIPR004827. bZIP.
IPR031106. C/EBP.
IPR016468. C/EBP_chordates.
[Graphical view]
PANTHERiPTHR23334. PTHR23334. 1 hit.
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005879. CCAAT/enhancer-binding. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A nuclear factor for IL-6 expression (NF-IL6) is a member of a C/EBP family."
    Akira S., Isshiki H., Sugita T., Tanabe O., Kinoshita S., Nishio Y., Nakajima T., Hirano T., Kishimoto T.
    EMBO J. 9:1897-1906(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  2. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. SeattleSNPs variation discovery resource
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-195.
  4. "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: Placenta.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Muscle and Skin.
  8. "Identification of a transcriptional regulatory factor for human aromatase cytochrome P450 gene expression as nuclear factor interleukin-6 (NF-IL6), a member of the CCAAT/enhancer-binding protein family."
    Toda K., Akira S., Kishimoto T., Sasaki H., Hashimoto K., Yamamoto Y., Sagara Y., Shizuta Y.
    Eur. J. Biochem. 231:292-299(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 241-323 (ISOFORMS 1/2/3).
  9. "Antioxidant-induced nuclear translocation of CCAAT/enhancer-binding protein beta. A critical role for protein kinase A-mediated phosphorylation of Ser299."
    Chinery R., Brockman J.A., Dransfield D.T., Coffey R.J.
    J. Biol. Chem. 272:30356-30361(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-288, MUTAGENESIS OF SER-288, SUBCELLULAR LOCATION.
  10. "C/EBPbeta phosphorylation by RSK creates a functional XEXD caspase inhibitory box critical for cell survival."
    Buck M., Poli V., Hunter T., Chojkier M.
    Mol. Cell 8:807-816(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-235.
  11. "Dynamic regulation of cyclooxygenase-2 promoter activity by isoforms of CCAAT/enhancer-binding proteins."
    Zhu Y., Saunders M.A., Yeh H., Deng W.G., Wu K.K.
    J. Biol. Chem. 277:6923-6928(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 3), ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), DNA-BINDING.
  12. "MEKK1 plays a critical role in activating the transcription factor C/EBP-beta-dependent gene expression in response to IFN-gamma."
    Roy S.K., Hu J., Meng Q., Xia Y., Shapiro P.S., Reddy S.P., Platanias L.C., Lindner D.J., Johnson P.F., Pritchard C., Pages G., Pouyssegur J., Kalvakolanu D.V.
    Proc. Natl. Acad. Sci. U.S.A. 99:7945-7950(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF THR-235.
  13. "Modification of CCAAT/enhancer-binding protein-beta by the small ubiquitin-like modifier (SUMO) family members, SUMO-2 and SUMO-3."
    Eaton E.M., Sealy L.
    J. Biol. Chem. 278:33416-33421(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-174.
  14. "Nine-amino-acid transactivation domain: establishment and prediction utilities."
    Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.
    Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  15. "G9a-mediated lysine methylation alters the function of CCAAT/enhancer-binding protein-beta."
    Pless O., Kowenz-Leutz E., Knoblich M., Lausen J., Beyermann M., Walsh M.J., Leutz A.
    J. Biol. Chem. 283:26357-26363(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-235.
  16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Crosstalk between C/EBPbeta phosphorylation, arginine methylation, and SWI/SNF/Mediator implies an indexing transcription factor code."
    Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.
    EMBO J. 29:1105-1115(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MED23; MED26; SMARCA2; SMARCB1 AND SMARCC1, METHYLATION AT ARG-3.
  18. "Endoplasmic reticulum stress-activated C/EBP homologous protein enhances nuclear factor-kappaB signals via repression of peroxisome proliferator-activated receptor gamma."
    Park S.H., Choi H.J., Yang H., Do K.H., Kim J., Lee D.W., Moon Y.
    J. Biol. Chem. 285:35330-35339(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DDIT3, SUBCELLULAR LOCATION, INDUCTION.
  19. "Transcriptional Regulation of Adipocyte Differentiation: A Central Role for CCAAT/Enhancer-binding Protein (C/EBP) beta."
    Guo L., Li X., Tang Q.
    J. Biol. Chem. 290:755-761(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW OF PTMS AND FUNCTION.
  20. "Structural analyses of DNA recognition by the AML1/Runx-1 Runt domain and its allosteric control by CBFbeta."
    Tahirov T.H., Inoue-Bungo T., Morii H., Fujikawa A., Sasaki M., Kimura K., Shiina M., Sato K., Kumasaka T., Yamamoto M., Ishii S., Ogata K.
    Cell 104:755-767(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 259-336 IN COMPLEX WITH RUNX1; CBFB AND DNA.
  21. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 259-345 IN COMPLEX WITH MOUSE MYB.

Entry informationi

Entry nameiCEBPB_HUMAN
AccessioniPrimary (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: July 22, 2015
This is version 175 of the entry and version 2 of the sequence. [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

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.