UniProtKB - P28033 (CEBPB_MOUSE)
CCAAT/enhancer-binding protein beta
Cebpb
Functioni
Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:16585579, PubMed:17911624, PubMed:18486321, PubMed:20111005).
Plays also a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis (PubMed:9727068, PubMed:10635333, PubMed:17301242, PubMed:17601773, PubMed:19478079, PubMed:24061474, PubMed:24216764).
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 (PubMed:15509779).
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 (PubMed:9727068, PubMed:10635333, PubMed:16585579).
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 (PubMed:17911624).
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:15985551, PubMed:17301242, PubMed:17601773, PubMed:20194620).
Essential for female reproduction because of a critical role in ovarian follicle development (PubMed:9303532).
Restricts osteoclastogenesis (PubMed:19440205).
Together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity).
1 PublicationBy similarity17 PublicationsEssential 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.
1 PublicationActs as a dominant negative through heterodimerization with isoform 2 (By similarity).
Promotes osteoblast differentiation and osteoclastogenesis (PubMed:19440205).
By similarity1 PublicationGO - Molecular functioni
- chromatin binding Source: UniProtKB
- DNA binding Source: MGI
- DNA-binding transcription activator activity, RNA polymerase II-specific Source: MGI
- DNA-binding transcription factor activity, RNA polymerase II-specific Source: UniProtKB
- DNA-binding transcription repressor activity, RNA polymerase II-specific Source: UniProtKB
- glucocorticoid receptor binding Source: MGI
- histone acetyltransferase binding Source: UniProtKB
- histone deacetylase binding Source: UniProtKB
- identical protein binding Source: UniProtKB
- kinase binding Source: UniProtKB
- protein heterodimerization activity Source: MGI
- protein homodimerization activity Source: MGI
- RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: MGI
- RNA polymerase II core promoter sequence-specific DNA binding Source: BHF-UCL
- RNA polymerase II transcription regulatory region sequence-specific DNA binding Source: MGI
- sequence-specific DNA binding Source: UniProtKB
- sequence-specific double-stranded DNA binding Source: MGI
- transcription cis-regulatory region binding Source: UniProtKB
- ubiquitin-like protein ligase binding Source: UniProtKB
GO - Biological processi
- brown fat cell differentiation Source: UniProtKB
- cellular response to amino acid stimulus Source: MGI
- cellular response to interleukin-1 Source: MGI
- cellular response to lipopolysaccharide Source: MGI
- cellular response to organic cyclic compound Source: Ensembl
- defense response to bacterium Source: UniProtKB
- embryonic placenta development Source: MGI
- fat cell differentiation Source: MGI
- granuloma formation Source: UniProtKB
- hepatocyte proliferation Source: UniProtKB
- intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
- liver regeneration Source: UniProtKB
- mammary gland epithelial cell differentiation Source: MGI
- mammary gland epithelial cell proliferation Source: MGI
- memory Source: Ensembl
- negative regulation of neuron apoptotic process Source: MGI
- negative regulation of T cell proliferation Source: UniProtKB
- negative regulation of transcription, DNA-templated Source: MGI
- negative regulation of transcription by RNA polymerase II Source: UniProtKB
- neuron differentiation Source: MGI
- ovarian follicle development Source: UniProtKB
- positive regulation of biomineral tissue development Source: MGI
- positive regulation of cold-induced thermogenesis Source: YuBioLab
- positive regulation of fat cell differentiation Source: GO_Central
- positive regulation of gene expression Source: MGI
- positive regulation of inflammatory response Source: ARUK-UCL
- positive regulation of interleukin-4 production Source: UniProtKB
- positive regulation of osteoblast differentiation Source: MGI
- positive regulation of sodium-dependent phosphate transport Source: MGI
- positive regulation of transcription, DNA-templated Source: MGI
- positive regulation of transcription by RNA polymerase II Source: UniProtKB
- positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: MGI
- regulation of cell differentiation Source: GO_Central
- regulation of dendritic cell differentiation Source: ARUK-UCL
- regulation of interleukin-6 production Source: MGI
- regulation of odontoblast differentiation Source: UniProtKB
- regulation of osteoclast differentiation Source: UniProtKB
- regulation of transcription, DNA-templated Source: UniProtKB
- regulation of transcription by RNA polymerase II Source: GO_Central
- response to endoplasmic reticulum stress Source: UniProtKB
- response to lipopolysaccharide Source: BHF-UCL
- T-helper 1 cell activation Source: UniProtKB
Keywordsi
Molecular function | Activator, DNA-binding |
Biological process | Differentiation, Transcription, Transcription regulation |
Enzyme and pathway databases
Reactomei | R-MMU-2559582, Senescence-Associated Secretory Phenotype (SASP) |
Names & Taxonomyi
Protein namesi | Recommended name: CCAAT/enhancer-binding protein betaImportedShort name: C/EBP beta Alternative name(s): AGP/EBP Interleukin-6-dependent-binding protein Short name: IL-6DBP Liver-enriched transcriptional activator Short name: LAP |
Gene namesi | Name:CebpbImported |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:88373, Cebpb |
VEuPathDBi | HostDB:ENSMUSG00000056501 |
Subcellular locationi
Nucleus
- C/EBP complex Source: ComplexPortal
- CHOP-C/EBP complex Source: MGI
- nuclear matrix Source: MGI
- nucleoplasm Source: MGI
- nucleus Source: MGI
- RNA polymerase II transcription regulator complex Source: MGI
Other locations
- chromatin Source: BHF-UCL
- condensed chromosome, centromeric region Source: MGI
- cytoplasm Source: MGI
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 39 | K → A or Q: No effect on interaction with EP300. 1 Publication | 1 | |
Mutagenesisi | 39 | K → R: Dominant negative. Loss of transactivation activity. No effect on interaction with EP300. 1 Publication | 1 | |
Mutagenesisi | 98 | K → R: No effect on transactivation activity. Not acetylated after glucocorticoid-stimulation and no increase of transactivation activity; when associated with R-101 and R-102. 2 Publications | 1 | |
Mutagenesisi | 101 | K → R: Not acetylated after glucocorticoid-stimulation and no increase of transactivation activity; when associated with R-98 and R-102. 1 Publication | 1 | |
Mutagenesisi | 102 | K → R: Not acetylated and no increase of transactivation activity after glucocorticoid-stimulation; when associated with R-98 and R-101. 1 Publication | 1 | |
Mutagenesisi | 133 | K → R: Not sumoylated. Decreases ubiquitination and increases stability. Loss of proliferation inhibition in T cells. No effect on transactivation activity. 3 Publications | 1 | |
Mutagenesisi | 135 | E → A: Not sumoylated and not ubiquitinated. 1 Publication | 1 | |
Mutagenesisi | 179 | T → A: Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-184 and A-188. 1 Publication | 1 | |
Mutagenesisi | 180 | S → A: Highly increases transactivation activity; when associated with A-181. 1 Publication | 1 | |
Mutagenesisi | 181 | S → A: Highly increases transactivation activity; when associated with A-180. 1 Publication | 1 | |
Mutagenesisi | 184 | S → A: Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-179 and A-188. 1 Publication | 1 | |
Mutagenesisi | 188 | T → A: Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-179 and A-184. 1 Publication | 1 | |
Mutagenesisi | 215 | K → R: No effect on transactivation activity. 1 Publication | 1 | |
Mutagenesisi | 217 | T → A: Loss of hepatocyte proliferation induction by TGFA. 1 Publication | 1 | |
Mutagenesisi | 217 | T → E: Induces hepatocyte proliferation. 1 Publication | 1 | |
Mutagenesisi | 276 | S → A: Reduces phosphorylation in response to calcium. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000076618 | 1 – 296 | CCAAT/enhancer-binding protein betaAdd BLAST | 296 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 3 | Asymmetric dimethylarginine; by CARM11 Publication | 1 | |
Modified residuei | 39 | N6-acetyllysine; alternate1 Publication | 1 | |
Modified residuei | 39 | N6-methylated lysine; alternate1 Publication | 1 | |
Modified residuei | 98 | N6-acetyllysine; by KAT2A and KAT2B1 Publication | 1 | |
Modified residuei | 101 | N6-acetyllysine; by KAT2A and KAT2B1 Publication | 1 | |
Modified residuei | 102 | N6-acetyllysine; by KAT2A and KAT2B; alternate1 Publication | 1 | |
Cross-linki | 102 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Cross-linki | 133 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate3 Publications | ||
Cross-linki | 133 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Cross-linki | 144 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 179 | Phosphothreonine; by GSK3-beta3 Publications | 1 | |
Glycosylationi | 180 | O-linked (GlcNAc) serine1 Publication | 1 | |
Glycosylationi | 181 | O-linked (GlcNAc) serine1 Publication | 1 | |
Modified residuei | 184 | Phosphoserine; by GSK3-betaCombined sources3 Publications | 1 | |
Modified residuei | 188 | Phosphothreonine; by RPS6KA1, CDK2 and MAPKCombined sources4 Publications | 1 | |
Cross-linki | 211 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 213 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 217 | Phosphothreonine; by RPS6KA1 and PKC/PRKCA1 Publication | 1 | |
Modified residuei | 239 | Phosphoserine; by PKC/PRKCABy similarity | 1 | |
Modified residuei | 276 | Phosphoserine; by CaMK21 Publication | 1 | |
Cross-linki | 283 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity |
Post-translational modificationi
Keywords - PTMi
Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
jPOSTi | P28033 |
MaxQBi | P28033 |
PaxDbi | P28033 |
PeptideAtlasi | P28033 |
PRIDEi | P28033 |
ProteomicsDBi | 283878 [P28033-1] 283879 [P28033-3] 283880 [P28033-2] |
PTM databases
GlyGeni | P28033, 2 sites |
iPTMneti | P28033 |
PhosphoSitePlusi | P28033 |
Expressioni
Tissue specificityi
Developmental stagei
Inductioni
Gene expression databases
Bgeei | ENSMUSG00000056501, Expressed in adrenal gland and 295 other tissues |
ExpressionAtlasi | P28033, baseline and differential |
Genevisiblei | P28033, MM |
Interactioni
Subunit structurei
Binds DNA as a homodimer and as a heterodimer.
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 CEBPA, CEBPD and CEBPE (By similarity).
Interacts with SIX1 (PubMed:27923061). Isoform 2 and isoform 3 also form heterodimers (By similarity).
Interacts with TRIM28 and PTGES2 (PubMed:9742105, PubMed:15879117).
Interacts with PRDM16 (PubMed:19641492).
Interacts with CCDC85B (PubMed:15644333).
Forms a complex with THOC5 (PubMed:19015024).
Interacts with ZNF638; this interaction increases transcriptional activation (PubMed:21602272).
Interacts with CIDEA and CIDEC (PubMed:22245780). Interaction with CIDEA increases transcriptional activation of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH. Interaction with CIDEC increases transcriptional activation of SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH.
Interacts with DDIT3/CHOP.
Interacts with EP300; recruits EP300 to chromatin.
Interacts with RORA; the interaction disrupts interaction with EP300 (PubMed:19324970).
Interacts (not methylated) with MED23, MED26, SMARCA2, SMARCB1 and SMARCC1 (PubMed:20111005).
Interacts with KAT2A and KAT2B (PubMed:17301242).
Interacts with ATF5; EP300 is required for ATF5 and CEBPB interaction and DNA binding (PubMed:24216764).
Interacts with NFE2L1; the heterodimer represses expression of DSPP during odontoblast differentiation (By similarity).
By similarity15 PublicationsBinary interactionsi
P28033
With | #Exp. | IntAct |
---|---|---|
Bhlhe41 [Q99PV5] | 5 | EBI-1029979,EBI-6143801 |
Kat2a [Q9JHD2] | 5 | EBI-1029979,EBI-2943116 |
KAT2B [Q92831] from Homo sapiens. | 2 | EBI-1029979,EBI-477430 |
GO - Molecular functioni
- glucocorticoid receptor binding Source: MGI
- histone acetyltransferase binding Source: UniProtKB
- histone deacetylase binding Source: UniProtKB
- identical protein binding Source: UniProtKB
- kinase binding Source: UniProtKB
- protein heterodimerization activity Source: MGI
- protein homodimerization activity Source: MGI
- ubiquitin-like protein ligase binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 198669, 17 interactors |
ComplexPortali | CPX-66, bZIP transcription factor complex, Cebpb-Ddit3 CPX-68, bZIP transcription factor complex, Cebpb-Cebpb CPX-685, c-Myb-C/EBPbeta complex |
DIPi | DIP-37539N |
IntActi | P28033, 14 interactors |
MINTi | P28033 |
STRINGi | 10090.ENSMUSP00000069850 |
Miscellaneous databases
RNActi | P28033, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P28033 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P28033 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 222 – 285 | bZIPPROSITE-ProRule annotationAdd BLAST | 64 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 22 | Required for Lys-133 sumoylationBy similarityAdd BLAST | 22 | |
Regioni | 22 – 104 | Required for MYC transcriptional repression1 PublicationAdd BLAST | 83 | |
Regioni | 171 – 199 | DisorderedSequence analysisAdd BLAST | 29 | |
Regioni | 226 – 246 | Basic motifPROSITE-ProRule annotationAdd BLAST | 21 | |
Regioni | 248 – 255 | Leucine-zipperPROSITE-ProRule annotation | 8 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 171 – 189 | Polar residuesSequence analysisAdd BLAST | 19 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG3119, Eukaryota |
GeneTreei | ENSGT00940000162137 |
HOGENOMi | CLU_043327_1_0_1 |
InParanoidi | P28033 |
OMAi | KNCKKAA |
PhylomeDBi | P28033 |
TreeFami | TF105008 |
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 |
s (3)i Sequence
Sequence statusi: Complete.
This entry describes 3 produced by isoformsialternative initiation. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MHRLLAWDAA CLPPPPAAFR PMEVANFYYE PDCLAYGAKA ARAAPRAPAA
60 70 80 90 100
EPAIGEHERA IDFSPYLEPL APAADFAAPA PAHHDFLSDL FADDYGAKPS
110 120 130 140 150
KKPADYGYVS LGRAGAKAAP PACFPPPPPA ALKAEPGFEP ADCKRADDAP
160 170 180 190 200
AMAAGFPFAL RAYLGYQATP SGSSGSLSTS SSSSPPGTPS PADAKAAPAA
210 220 230 240 250
CFAGPPAAPA KAKAKKTVDK LSDEYKMRRE RNNIAVRKSR DKAKMRNLET
260 270 280 290
QHKVLELTAE NERLQKKVEQ LSRELSTLRN LFKQLPEPLL ASAGHC
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_053976 | 1 – 151 | Missing in isoform 3. CuratedAdd BLAST | 151 | |
Alternative sequenceiVSP_053977 | 1 – 21 | Missing in isoform 2. CuratedAdd BLAST | 21 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M61007 mRNA Translation: AAA37192.1 X62600 mRNA Translation: CAA44484.1 S78572 Genomic DNA No translation available. |
CCDSi | CCDS17105.1 [P28033-1] |
PIRi | A36366 |
RefSeqi | NP_001274667.1, NM_001287738.1 [P28033-3] NP_001274668.1, NM_001287739.1 [P28033-2] NP_034013.1, NM_009883.4 [P28033-1] |
Genome annotation databases
Ensembli | ENSMUST00000070642; ENSMUSP00000069850; ENSMUSG00000056501 [P28033-1] |
GeneIDi | 12608 |
KEGGi | mmu:12608 |
UCSCi | uc008oaf.2, mouse [P28033-1] |
Keywords - Coding sequence diversityi
Alternative initiationSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M61007 mRNA Translation: AAA37192.1 X62600 mRNA Translation: CAA44484.1 S78572 Genomic DNA No translation available. |
CCDSi | CCDS17105.1 [P28033-1] |
PIRi | A36366 |
RefSeqi | NP_001274667.1, NM_001287738.1 [P28033-3] NP_001274668.1, NM_001287739.1 [P28033-2] NP_034013.1, NM_009883.4 [P28033-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1CI6 | X-ray | 2.60 | B | 224-285 | [»] | |
SMRi | P28033 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 198669, 17 interactors |
ComplexPortali | CPX-66, bZIP transcription factor complex, Cebpb-Ddit3 CPX-68, bZIP transcription factor complex, Cebpb-Cebpb CPX-685, c-Myb-C/EBPbeta complex |
DIPi | DIP-37539N |
IntActi | P28033, 14 interactors |
MINTi | P28033 |
STRINGi | 10090.ENSMUSP00000069850 |
PTM databases
GlyGeni | P28033, 2 sites |
iPTMneti | P28033 |
PhosphoSitePlusi | P28033 |
Proteomic databases
jPOSTi | P28033 |
MaxQBi | P28033 |
PaxDbi | P28033 |
PeptideAtlasi | P28033 |
PRIDEi | P28033 |
ProteomicsDBi | 283878 [P28033-1] 283879 [P28033-3] 283880 [P28033-2] |
Protocols and materials databases
Antibodypediai | 3782, 682 antibodies from 42 providers |
DNASUi | 12608 |
Genome annotation databases
Ensembli | ENSMUST00000070642; ENSMUSP00000069850; ENSMUSG00000056501 [P28033-1] |
GeneIDi | 12608 |
KEGGi | mmu:12608 |
UCSCi | uc008oaf.2, mouse [P28033-1] |
Organism-specific databases
CTDi | 1051 |
MGIi | MGI:88373, Cebpb |
VEuPathDBi | HostDB:ENSMUSG00000056501 |
Phylogenomic databases
eggNOGi | KOG3119, Eukaryota |
GeneTreei | ENSGT00940000162137 |
HOGENOMi | CLU_043327_1_0_1 |
InParanoidi | P28033 |
OMAi | KNCKKAA |
PhylomeDBi | P28033 |
TreeFami | TF105008 |
Enzyme and pathway databases
Reactomei | R-MMU-2559582, Senescence-Associated Secretory Phenotype (SASP) |
Miscellaneous databases
BioGRID-ORCSi | 12608, 10 hits in 66 CRISPR screens |
ChiTaRSi | Cebpb, mouse |
EvolutionaryTracei | P28033 |
PROi | PR:P28033 |
RNActi | P28033, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000056501, Expressed in adrenal gland and 295 other tissues |
ExpressionAtlasi | P28033, baseline and differential |
Genevisiblei | P28033, MM |
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 |
MobiDBi | Search... |
Entry informationi
Entry namei | CEBPB_MOUSE | |
Accessioni | P28033Primary (citable) accession number: P28033 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1992 |
Last sequence update: | August 1, 1992 | |
Last modified: | February 23, 2022 | |
This is version 196 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families