UniProtKB - P49715 (CEBPA_HUMAN)
CCAAT/enhancer-binding protein alpha
CEBPA
Functioni
Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta. Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes (PubMed:11242107).
During early embryogenesis, plays essential and redundant functions with CEBPB. Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP). Critical for the proper development of the liver and the lung (By similarity).
Necessary for terminal adipocyte differentiation, is required for postnatal maintenance of systemic energy homeostasis and lipid storage (By similarity).
To regulate these different processes at the proper moment and tissue, interplays with other transcription factors and modulators. Down-regulates the expression of genes that maintain cells in an undifferentiated and proliferative state through E2F1 repression, which is critical for its ability to induce adipocyte and granulocyte terminal differentiation. Reciprocally E2F1 blocks adipocyte differentiation by binding to specific promoters and repressing CEBPA binding to its target gene promoters. Proliferation arrest also depends on a functional binding to SWI/SNF complex (PubMed:14660596).
In liver, regulates gluconeogenesis and lipogenesis through different mechanisms. To regulate gluconeogenesis, functionally cooperates with FOXO1 binding to IRE-controlled promoters and regulating the expression of target genes such as PCK1 or G6PC1. To modulate lipogenesis, interacts and transcriptionally synergizes with SREBF1 in promoter activation of specific lipogenic target genes such as ACAS2. In adipose tissue, seems to act as FOXO1 coactivator accessing to ADIPOQ promoter through FOXO1 binding sites (By similarity).
By similarity2 PublicationsCan act as dominant-negative. Binds DNA and have transctivation activity, even if much less efficiently than isoform 2. Does not inhibit cell proliferation (PubMed:14660596).
By similarity1 PublicationDirectly and specifically enhances ribosomal DNA transcription interacting with RNA polymerase I-specific cofactors and inducing histone acetylation.
1 PublicationRegions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
DNA bindingi | 285 – 300 | By similarityAdd BLAST | 16 |
GO - Molecular functioni
- chromatin binding Source: Ensembl
- DNA binding Source: ProtInc
- DNA-binding transcription activator activity, RNA polymerase II-specific Source: BHF-UCL
- DNA-binding transcription factor activity Source: UniProtKB
- DNA-binding transcription factor activity, RNA polymerase II-specific Source: NTNU_SB
- identical protein binding Source: IntAct
- kinase binding Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: GO_Central
- RNA polymerase II-specific DNA-binding transcription factor binding Source: ARUK-UCL
- RNA polymerase I transcription regulatory region sequence-specific DNA binding Source: UniProtKB
- STAT family protein binding Source: UniProtKB
- transcription cis-regulatory region binding Source: UniProtKB
GO - Biological processi
- brown fat cell differentiation Source: Ensembl
- cell maturation Source: Ensembl
- cellular response to lithium ion Source: Ensembl
- cellular response to organic cyclic compound Source: Ensembl
- cellular response to tumor necrosis factor Source: Ensembl
- cholesterol metabolic process Source: Ensembl
- cytokine-mediated signaling pathway Source: UniProtKB
- embryonic placenta development Source: Ensembl
- fat cell differentiation Source: UniProtKB
- generation of precursor metabolites and energy Source: ProtInc
- glucose homeostasis Source: UniProtKB
- granulocyte differentiation Source: UniProtKB
- inner ear development Source: Ensembl
- interleukin-6-mediated signaling pathway Source: ARUK-UCL
- lipid homeostasis Source: UniProtKB
- liver development Source: UniProtKB
- lung development Source: UniProtKB
- macrophage differentiation Source: Ensembl
- mitochondrion organization Source: Ensembl
- myeloid cell differentiation Source: GO_Central
- negative regulation of cell population proliferation Source: UniProtKB
- negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: ParkinsonsUK-UCL
- negative regulation of transcription, DNA-templated Source: UniProtKB
- negative regulation of transcription by RNA polymerase II Source: Ensembl
- Notch signaling pathway Source: Ensembl
- positive regulation of DNA-templated transcription, initiation Source: UniProtKB
- positive regulation of fat cell differentiation Source: Ensembl
- positive regulation of gene expression Source: Ensembl
- positive regulation of inflammatory response Source: ARUK-UCL
- positive regulation of macrophage activation Source: ARUK-UCL
- positive regulation of osteoblast differentiation Source: Ensembl
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
- positive regulation of transcription by RNA polymerase II Source: BHF-UCL
- positive regulation of transcription by RNA polymerase III Source: UniProtKB
- regulation of transcription, DNA-templated Source: UniProtKB
- regulation of transcription by RNA polymerase II Source: GO_Central
- transcription by RNA polymerase I Source: UniProtKB
- urea cycle Source: Ensembl
- white fat cell differentiation Source: Ensembl
Keywordsi
Molecular function | Activator, Developmental protein, DNA-binding |
Biological process | Host-virus interaction, Transcription, Transcription regulation |
Enzyme and pathway databases
PathwayCommonsi | P49715 |
Reactomei | R-HSA-381340, Transcriptional regulation of white adipocyte differentiation R-HSA-9616222, Transcriptional regulation of granulopoiesis |
SignaLinki | P49715 |
SIGNORi | P49715 |
Names & Taxonomyi
Protein namesi | Recommended name: CCAAT/enhancer-binding protein alphaImportedShort name: C/EBP alphaImported |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:1833, CEBPA |
MIMi | 116897, gene |
neXtProti | NX_P49715 |
VEuPathDBi | HostDB:ENSG00000245848 |
Subcellular locationi
Nucleus
- C/EBP complex Source: ComplexPortal
- CHOP-C/EBP complex Source: ComplexPortal
- nucleolus Source: UniProtKB
- nucleoplasm Source: HPA
- nucleus Source: UniProtKB
- RNA polymerase II transcription regulator complex Source: BHF-UCL
Other locations
- chromatin Source: NTNU_SB
- intracellular membrane-bounded organelle Source: HPA
- transcription regulator complex Source: ARUK-UCL
Keywords - Cellular componenti
NucleusPathology & Biotechi
Involvement in diseasei
Leukemia, acute myelogenous (AML)3 Publications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_072677 | 84 | H → L in AML; no effect on expression; no effect on DNA-binding or transactivation activity. 1 PublicationCorresponds to variant dbSNP:rs28931590EnsemblClinVar. | 1 | |
Natural variantiVAR_072678 | 312 | Q → QK in AML; nuclear; no effect on expression; loss of DNA-binding and transactivation activity. 1 Publication | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 55 | I → A: Decreased interaction with TRIB1. 1 Publication | 1 | |
Mutagenesisi | 57 | E → T: No effect on interaction with TRIB1. 1 Publication | 1 | |
Mutagenesisi | 58 | H → D: No effect on interaction with TRIB1. 1 Publication | 1 | |
Mutagenesisi | 59 | E → A: Decreased interaction with TRIB1. 1 Publication | 1 | |
Mutagenesisi | 61 | S → A: Decreased interaction with TRIB1. 1 Publication | 1 | |
Mutagenesisi | 62 | I → A: Decreased interaction with TRIB1. 1 Publication | 1 | |
Mutagenesisi | 63 | D → A: No effect on interaction with TRIB1. 1 Publication | 1 | |
Mutagenesisi | 64 | I → A: Decreased interaction with TRIB1. 1 Publication | 1 | |
Mutagenesisi | 65 | S → A: No effect on interaction with TRIB1. 1 Publication | 1 | |
Mutagenesisi | 67 | Y → A: Decreased interaction with TRIB1. 1 Publication | 1 | |
Mutagenesisi | 67 | Y → F: No effect on interaction with TRIB1. 1 Publication | 1 | |
Mutagenesisi | 68 | I → A: Decreased interaction with TRIB1. 1 Publication | 1 | |
Mutagenesisi | 69 | D → A: No effect on interaction with TRIB1. 1 Publication | 1 |
Keywords - Diseasei
Disease variantOrganism-specific databases
DisGeNETi | 1050 |
GeneReviewsi | CEBPA |
MalaCardsi | CEBPA |
MIMi | 601626, phenotype |
OpenTargetsi | ENSG00000245848 |
Orphaneti | 319480, Acute myeloid leukemia with CEBPA somatic mutations 102724, Acute myeloid leukemia with t(8;21)(q22;q22) translocation 319465, Inherited acute myeloid leukemia |
PharmGKBi | PA26376 |
Miscellaneous databases
Pharosi | P49715, Tbio |
Genetic variation databases
BioMutai | CEBPA |
DMDMi | 166898082 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000076613 | 1 – 358 | CCAAT/enhancer-binding protein alphaAdd BLAST | 358 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 161 | N6-acetyllysine; alternateCombined sources | 1 | |
Cross-linki | 161 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources | ||
Modified residuei | 190 | Phosphoserine1 Publication | 1 | |
Modified residuei | 226 | Phosphothreonine; by GSK3By similarity | 1 | |
Modified residuei | 230 | Phosphothreonine; by GSK3By similarity | 1 | |
Modified residuei | 234 | Phosphoserine; by GSK3By similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | P49715 |
jPOSTi | P49715 |
MassIVEi | P49715 |
MaxQBi | P49715 |
PaxDbi | P49715 |
PeptideAtlasi | P49715 |
PRIDEi | P49715 |
ProteomicsDBi | 56054 |
PTM databases
iPTMneti | P49715 |
PhosphoSitePlusi | P49715 |
Expressioni
Gene expression databases
Bgeei | ENSG00000245848, Expressed in adipose tissue of abdominal region and 224 other tissues |
Genevisiblei | P49715, HS |
Organism-specific databases
HPAi | ENSG00000245848, Tissue enhanced (adipose tissue, liver, skin) |
Interactioni
Subunit structurei
Binds DNA as a homodimer and as a heterodimer. Can form stable heterodimers with CEBPB, CEBPD, CEBPE and CEBPG (By similarity).
Interacts with PRDM16 (By similarity).
Interacts with UBN1 (PubMed:10725330).
Interacts with ZNF638; this interaction increases transcriptional activation (By similarity).
Interacts with the complex TFDP2:E2F1; the interaction prevents CEBPA binding to target gene promoters and represses its transcriptional activity (PubMed:20176812).
Interacts with RB1 (PubMed:15107404).
Interacts (when phosphorylated at SER-190) with CDK2, CDK4, E2F4 and SMARCA2 (PubMed:15107404).
Interacts with SREBPF1 (By similarity).
Interacts with FOXO1 (via the Fork-head domain); the interaction increases when FOXO1 is deacetylated (By similarity).
Interacts with SIX1 (PubMed:27923061).
Interacts (via recognition sequence) with TRIB1 (PubMed:20410507, PubMed:26455797).
By similarity7 Publications(Microbial infection) Interacts with HBV protein X.
1 PublicationBinary interactionsi
P49715
Isoform 1 [P49715-1]
With | #Exp. | IntAct |
---|---|---|
TRIB1 - isoform 1 [Q96RU8-1] | 2 | EBI-16180754,EBI-16180744 |
GO - Molecular functioni
- identical protein binding Source: IntAct
- kinase binding Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- RNA polymerase II-specific DNA-binding transcription factor binding Source: ARUK-UCL
- STAT family protein binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 107479, 106 interactors |
ComplexPortali | CPX-509, bZIP transcription factor complex, CEBPA-CEBPB CPX-6469, bZIP transcription factor complex, ATF3-CEBPA CPX-6525, bZIP transcription factor complex, ATF4-CEBPA CPX-6586, bZIP transcription factor complex, ATF5-CEBPA CPX-69, bZIP transcription factor complex, CEBPA-DDIT3 CPX-7006, bZIP transcription factor complex, BATF-CEBPA CPX-7065, bZIP transcription factor complex, BATF2-CEBPA CPX-7095, bZIP transcription factor complex, BATF3-CEBPA CPX-71, bZIP transcription factor complex, CEBPA-CEBPA |
CORUMi | P49715 |
DIPi | DIP-37882N |
ELMi | P49715 |
IntActi | P49715, 31 interactors |
MINTi | P49715 |
STRINGi | 9606.ENSP00000427514 |
Miscellaneous databases
RNActi | P49715, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P49715 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 282 – 345 | bZIPPROSITE-ProRule annotationAdd BLAST | 64 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 70 | Required to repress E2F1:TFDP1-mediated transcription, to inhibit cell cycle and to induce adipocyte differentiationBy similarityAdd BLAST | 70 | |
Regioni | 1 – 55 | DisorderedSequence analysisAdd BLAST | 55 | |
Regioni | 54 – 72 | Required for interaction with TRIB11 PublicationAdd BLAST | 19 | |
Regioni | 128 – 204 | Required to induce adipocyte differentiationBy similarityAdd BLAST | 77 | |
Regioni | 178 – 201 | DisorderedSequence analysisAdd BLAST | 24 | |
Regioni | 182 – 198 | Required to functionally cooperate with SREBF1 in promoter activationBy similarityAdd BLAST | 17 | |
Regioni | 217 – 291 | DisorderedSequence analysisAdd BLAST | 75 | |
Regioni | 244 – 358 | Interaction with FOXO1By similarityAdd BLAST | 115 | |
Regioni | 286 – 313 | Basic motifPROSITE-ProRule annotationAdd BLAST | 28 | |
Regioni | 317 – 345 | Leucine-zipperPROSITE-ProRule annotationAdd BLAST | 29 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 179 – 201 | Pro residuesSequence analysisAdd BLAST | 23 | |
Compositional biasi | 222 – 242 | Pro residuesSequence analysisAdd BLAST | 21 | |
Compositional biasi | 277 – 291 | Basic and acidic residuesSequence analysisAdd BLAST | 15 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG3119, Eukaryota |
GeneTreei | ENSGT00940000162646 |
HOGENOMi | CLU_043327_2_0_1 |
InParanoidi | P49715 |
OMAi | MPHLQYQ |
OrthoDBi | 1284308at2759 |
PhylomeDBi | P49715 |
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 (4)i Sequence
Sequence statusi: Complete.
This entry describes 4 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
MESADFYEAE PRPPMSSHLQ SPPHAPSSAA FGFPRGAGPA QPPAPPAAPE
60 70 80 90 100
PLGGICEHET SIDISAYIDP AAFNDEFLAD LFQHSRQQEK AKAAVGPTGG
110 120 130 140 150
GGGGDFDYPG APAGPGGAVM PGGAHGPPPG YGCAAAGYLD GRLEPLYERV
160 170 180 190 200
GAPALRPLVI KQEPREEDEA KQLALAGLFP YQPPPPPPPS HPHPHPPPAH
210 220 230 240 250
LAAPHLQFQI AHCGQTTMHL QPGHPTPPPT PVPSPHPAPA LGAAGLPGPG
260 270 280 290 300
SALKGLGAAH PDLRASGGSG AGKAKKSVDK NSNEYRVRRE RNNIAVRKSR
310 320 330 340 350
DKAKQRNVET QQKVLELTSD NDRLRKRVEQ LSRELDTLRG IFRQLPESSL
VKAMGNCA
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 40 – 41 | AQ → PK in AAC50235 (PubMed:7575576).Curated | 2 | |
Sequence conflicti | 95 – 98 | VGPT → WAH in CAA72289 (Ref. 2) Curated | 4 | |
Sequence conflicti | 241 | L → V in CAA72289 (Ref. 2) Curated | 1 | |
Sequence conflicti | 248 – 250 | GPG → ALA in CAA72289 (Ref. 2) Curated | 3 | |
Sequence conflicti | 269 | S → T in AAC50235 (PubMed:7575576).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_072677 | 84 | H → L in AML; no effect on expression; no effect on DNA-binding or transactivation activity. 1 PublicationCorresponds to variant dbSNP:rs28931590EnsemblClinVar. | 1 | |
Natural variantiVAR_072678 | 312 | Q → QK in AML; nuclear; no effect on expression; loss of DNA-binding and transactivation activity. 1 Publication | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_057547 | 1 – 119 | Missing in isoform 3. Add BLAST | 119 | |
Alternative sequenceiVSP_057548 | 1 – 14 | Missing in isoform 2. Add BLAST | 14 | |
Alternative sequenceiVSP_057607 | 1 | M → MRGRGRAGSPGGRRRRPAQA GGRRGSPCRENSNSPM in isoform 4. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U34070 Genomic DNA Translation: AAC50235.1 Y11525 mRNA Translation: CAA72289.1 EU048234 Genomic DNA Translation: ABS82765.1 AC008738 Genomic DNA No translation available. BC027902 mRNA Translation: AAH27902.1 |
CCDSi | CCDS54243.1 [P49715-1] |
PIRi | JC4311 |
RefSeqi | NP_001272758.1, NM_001285829.1 [P49715-3] NP_001274353.1, NM_001287424.1 [P49715-4] NP_001274364.1, NM_001287435.1 [P49715-2] NP_004355.2, NM_004364.4 [P49715-1] |
Genome annotation databases
Ensembli | ENST00000498907; ENSP00000427514; ENSG00000245848 |
GeneIDi | 1050 |
KEGGi | hsa:1050 |
MANE-Selecti | ENST00000498907.3; ENSP00000427514.1; NM_004364.5; NP_004355.2 |
UCSCi | uc002nun.4, human [P49715-1] |
Keywords - Coding sequence diversityi
Alternative initiationSimilar proteinsi
Cross-referencesi
Web resourcesi
Atlas of Genetics and Cytogenetics in Oncology and Haematology |
SeattleSNPs |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U34070 Genomic DNA Translation: AAC50235.1 Y11525 mRNA Translation: CAA72289.1 EU048234 Genomic DNA Translation: ABS82765.1 AC008738 Genomic DNA No translation available. BC027902 mRNA Translation: AAH27902.1 |
CCDSi | CCDS54243.1 [P49715-1] |
PIRi | JC4311 |
RefSeqi | NP_001272758.1, NM_001285829.1 [P49715-3] NP_001274353.1, NM_001287424.1 [P49715-4] NP_001274364.1, NM_001287435.1 [P49715-2] NP_004355.2, NM_004364.4 [P49715-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
6DC0 | X-ray | 2.80 | A/B | 51-75 | [»] | |
SMRi | P49715 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 107479, 106 interactors |
ComplexPortali | CPX-509, bZIP transcription factor complex, CEBPA-CEBPB CPX-6469, bZIP transcription factor complex, ATF3-CEBPA CPX-6525, bZIP transcription factor complex, ATF4-CEBPA CPX-6586, bZIP transcription factor complex, ATF5-CEBPA CPX-69, bZIP transcription factor complex, CEBPA-DDIT3 CPX-7006, bZIP transcription factor complex, BATF-CEBPA CPX-7065, bZIP transcription factor complex, BATF2-CEBPA CPX-7095, bZIP transcription factor complex, BATF3-CEBPA CPX-71, bZIP transcription factor complex, CEBPA-CEBPA |
CORUMi | P49715 |
DIPi | DIP-37882N |
ELMi | P49715 |
IntActi | P49715, 31 interactors |
MINTi | P49715 |
STRINGi | 9606.ENSP00000427514 |
PTM databases
iPTMneti | P49715 |
PhosphoSitePlusi | P49715 |
Genetic variation databases
BioMutai | CEBPA |
DMDMi | 166898082 |
Proteomic databases
EPDi | P49715 |
jPOSTi | P49715 |
MassIVEi | P49715 |
MaxQBi | P49715 |
PaxDbi | P49715 |
PeptideAtlasi | P49715 |
PRIDEi | P49715 |
ProteomicsDBi | 56054 |
Protocols and materials databases
Antibodypediai | 38083, 719 antibodies from 40 providers |
DNASUi | 1050 |
Genome annotation databases
Ensembli | ENST00000498907; ENSP00000427514; ENSG00000245848 |
GeneIDi | 1050 |
KEGGi | hsa:1050 |
MANE-Selecti | ENST00000498907.3; ENSP00000427514.1; NM_004364.5; NP_004355.2 |
UCSCi | uc002nun.4, human [P49715-1] |
Organism-specific databases
CTDi | 1050 |
DisGeNETi | 1050 |
GeneCardsi | CEBPA |
GeneReviewsi | CEBPA |
HGNCi | HGNC:1833, CEBPA |
HPAi | ENSG00000245848, Tissue enhanced (adipose tissue, liver, skin) |
MalaCardsi | CEBPA |
MIMi | 116897, gene 601626, phenotype |
neXtProti | NX_P49715 |
OpenTargetsi | ENSG00000245848 |
Orphaneti | 319480, Acute myeloid leukemia with CEBPA somatic mutations 102724, Acute myeloid leukemia with t(8;21)(q22;q22) translocation 319465, Inherited acute myeloid leukemia |
PharmGKBi | PA26376 |
VEuPathDBi | HostDB:ENSG00000245848 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3119, Eukaryota |
GeneTreei | ENSGT00940000162646 |
HOGENOMi | CLU_043327_2_0_1 |
InParanoidi | P49715 |
OMAi | MPHLQYQ |
OrthoDBi | 1284308at2759 |
PhylomeDBi | P49715 |
TreeFami | TF105008 |
Enzyme and pathway databases
PathwayCommonsi | P49715 |
Reactomei | R-HSA-381340, Transcriptional regulation of white adipocyte differentiation R-HSA-9616222, Transcriptional regulation of granulopoiesis |
SignaLinki | P49715 |
SIGNORi | P49715 |
Miscellaneous databases
BioGRID-ORCSi | 1050, 68 hits in 1063 CRISPR screens |
ChiTaRSi | CEBPA, human |
GeneWikii | CEBPA |
GenomeRNAii | 1050 |
Pharosi | P49715, Tbio |
PROi | PR:P49715 |
RNActi | P49715, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000245848, Expressed in adipose tissue of abdominal region and 224 other tissues |
Genevisiblei | P49715, 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 |
MobiDBi | Search... |
Entry informationi
Entry namei | CEBPA_HUMAN | |
Accessioni | P49715Primary (citable) accession number: P49715 Secondary accession number(s): A7LNP2, P78319, Q05CA4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | February 5, 2008 | |
Last modified: | February 23, 2022 | |
This is version 201 of the entry and version 3 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, Reference proteomeDocuments
- Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) 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