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P49715

- CEBPA_HUMAN

UniProt

P49715 - CEBPA_HUMAN

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Protein

CCAAT/enhancer-binding protein alpha

Gene

CEBPA

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

Functioni

C/EBP is a DNA-binding protein that recognizes two different motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers.

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  4. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: UniProtKB
  5. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  6. transcription factor binding Source: UniProtKB
  7. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. acute-phase response Source: Ensembl
  2. brown fat cell differentiation Source: Ensembl
  3. cell maturation Source: Ensembl
  4. cellular response to lithium ion Source: Ensembl
  5. cellular response to organic cyclic compound Source: Ensembl
  6. cholesterol metabolic process Source: Ensembl
  7. cytokine-mediated signaling pathway Source: UniProtKB
  8. embryonic placenta development Source: Ensembl
  9. generation of precursor metabolites and energy Source: ProtInc
  10. inner ear development Source: Ensembl
  11. liver development Source: Ensembl
  12. lung development Source: Ensembl
  13. macrophage differentiation Source: Ensembl
  14. mitochondrion organization Source: Ensembl
  15. myeloid cell differentiation Source: UniProtKB
  16. negative regulation of cell proliferation Source: Ensembl
  17. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  18. organ regeneration Source: Ensembl
  19. positive regulation of fat cell differentiation Source: Ensembl
  20. positive regulation of osteoblast differentiation Source: Ensembl
  21. positive regulation of transcription from RNA polymerase III promoter Source: UniProtKB
  22. response to glucocorticoid Source: Ensembl
  23. response to vitamin B2 Source: Ensembl
  24. transcription, DNA-templated Source: UniProtKB
  25. transcription from RNA polymerase II promoter Source: ProtInc
  26. urea cycle Source: Ensembl
  27. viral process Source: UniProtKB-KW
  28. white fat cell differentiation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiP49715.

Names & Taxonomyi

Protein namesi
Recommended name:
CCAAT/enhancer-binding protein alpha
Short name:
C/EBP alpha
Gene namesi
Name:CEBPA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:1833. CEBPA.

Subcellular locationi

GO - Cellular componenti

  1. nuclear matrix Source: Ensembl
  2. nucleus Source: UniProtKB
  3. Rb-E2F complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

Orphaneti319480. Acute myeloid leukemia with CEBPA somatic mutations.
102724. Acute myeloid leukemia with t(8;21)(q22;q22) translocation.
319465. Inherited acute myeloid leukemia.
PharmGKBiPA26376.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358CCAAT/enhancer-binding protein alphaPRO_0000076613Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei161 – 1611N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP49715.
PRIDEiP49715.

PTM databases

PhosphoSiteiP49715.

Expressioni

Gene expression databases

BgeeiP49715.
CleanExiHS_CEBPA.
ExpressionAtlasiP49715. baseline.
GenevestigatoriP49715.

Interactioni

Subunit structurei

Interacts with PRDM16 (By similarity). Binds DNA as a dimer and can form stable heterodimers with C/EBP beta and gamma. Interacts with UBN1. Interacts with HBV protein X. Interacts with ZNF638; this interaction increases transcriptional activation (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CDX1P479023EBI-1172054,EBI-8514176
E2P031222EBI-1172054,EBI-7028618From a different organism.
E2P064224EBI-1172054,EBI-7136851From a different organism.
PARP1P098742EBI-1172054,EBI-355676

Protein-protein interaction databases

BioGridi107479. 97 interactions.
IntActiP49715. 13 interactions.
MINTiMINT-264048.

Structurei

3D structure databases

ProteinModelPortaliP49715.
SMRiP49715. Positions 281-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini282 – 34564bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni286 – 31328Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni317 – 34529Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi99 – 1046Poly-Gly
Compositional biasi183 – 1897Poly-Pro

Sequence similaritiesi

Belongs to the bZIP family. C/EBP subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000063192.
HOGENOMiHOG000013112.
HOVERGENiHBG050879.
InParanoidiP49715.
KOiK09055.
OMAiPPPGYGC.
OrthoDBiEOG7R56TQ.
PhylomeDBiP49715.
TreeFamiTF105008.

Family and domain databases

InterProiIPR004827. bZIP.
IPR016468. CCAAT/enhancer-binding.
[Graphical view]
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]

Sequencei

Sequence statusi: Complete.

P49715 [UniParc]FASTAAdd to Basket

« Hide

        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
Length:358
Mass (Da):37,561
Last modified:February 5, 2008 - v3
Checksum:i574C0A049E25BCAC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 412AQ → PK in AAC50235. (PubMed:7575576)Curated
Sequence conflicti95 – 984VGPT → WAH in CAA72289. 1 PublicationCurated
Sequence conflicti241 – 2411L → V in CAA72289. 1 PublicationCurated
Sequence conflicti248 – 2503GPG → ALA in CAA72289. 1 PublicationCurated
Sequence conflicti269 – 2691S → T in AAC50235. (PubMed:7575576)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U34070 Genomic DNA. Translation: AAC50235.1.
Y11525 mRNA. Translation: CAA72289.1.
EU048234 Genomic DNA. Translation: ABS82765.1.
BC027902 mRNA. Translation: AAH27902.1.
CCDSiCCDS54243.1.
PIRiJC4311.
RefSeqiNP_004355.2. NM_004364.4.
UniGeneiHs.76171.

Genome annotation databases

EnsembliENST00000498907; ENSP00000427514; ENSG00000245848.
GeneIDi1050.
KEGGihsa:1050.
UCSCiuc002nun.3. human.

Polymorphism databases

DMDMi166898082.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U34070 Genomic DNA. Translation: AAC50235.1 .
Y11525 mRNA. Translation: CAA72289.1 .
EU048234 Genomic DNA. Translation: ABS82765.1 .
BC027902 mRNA. Translation: AAH27902.1 .
CCDSi CCDS54243.1.
PIRi JC4311.
RefSeqi NP_004355.2. NM_004364.4.
UniGenei Hs.76171.

3D structure databases

ProteinModelPortali P49715.
SMRi P49715. Positions 281-340.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107479. 97 interactions.
IntActi P49715. 13 interactions.
MINTi MINT-264048.

PTM databases

PhosphoSitei P49715.

Polymorphism databases

DMDMi 166898082.

Proteomic databases

MaxQBi P49715.
PRIDEi P49715.

Protocols and materials databases

DNASUi 1050.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000498907 ; ENSP00000427514 ; ENSG00000245848 .
GeneIDi 1050.
KEGGi hsa:1050.
UCSCi uc002nun.3. human.

Organism-specific databases

CTDi 1050.
GeneCardsi GC19M033790.
GeneReviewsi CEBPA.
H-InvDB HIX0040095.
HGNCi HGNC:1833. CEBPA.
MIMi 116897. gene.
neXtProti NX_P49715.
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.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00530000063192.
HOGENOMi HOG000013112.
HOVERGENi HBG050879.
InParanoidi P49715.
KOi K09055.
OMAi PPPGYGC.
OrthoDBi EOG7R56TQ.
PhylomeDBi P49715.
TreeFami TF105008.

Enzyme and pathway databases

Reactomei REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinki P49715.

Miscellaneous databases

GeneWikii CEBPA.
GenomeRNAii 1050.
NextBioi 4397.
PROi P49715.
SOURCEi Search...

Gene expression databases

Bgeei P49715.
CleanExi HS_CEBPA.
ExpressionAtlasi P49715. baseline.
Genevestigatori P49715.

Family and domain databases

InterProi IPR004827. bZIP.
IPR016468. CCAAT/enhancer-binding.
[Graphical view ]
Pfami PF07716. bZIP_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF005879. CCAAT/enhancer-binding. 1 hit.
SMARTi SM00338. BRLZ. 1 hit.
[Graphical view ]
PROSITEi PS50217. BZIP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, sequence, and expression patterns of the human gene encoding CCAAT/enhancer binding protein alpha (C/EBP alpha)."
    Antonson P., Xanthopoulos K.G.
    Biochem. Biophys. Res. Commun. 215:106-113(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Umbilical cord.
  2. "Transcription factor C/EBP-alpha: novel sites of expression and cloning of the human gene."
    Swart G.W.M., van Groningen J.J.M., van Ruissen F., Bergers M., Schalwijk J.
    Biol. Chem. Hoppe-Seyler 378:373-379(1997)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. SeattleSNPs variation discovery resource
    Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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] OF 1-133.
    Tissue: Pancreas.
  5. "Interaction of hepatitis B viral X protein and CCAAT/enhancer-binding protein alpha synergistically activates the hepatitis B viral enhancer II/pregenomic promoter."
    Choi B.H., Park G.T., Rho H.M.
    J. Biol. Chem. 274:2858-2865(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HBV PROTEIN X.
  6. "Ubinuclein, a novel nuclear protein interacting with cellular and viral transcription factors."
    Aho S., Buisson M., Pajunen T., Ryoo Y.W., Giot J.-F., Gruffat H., Sergeant A., Uitto J.
    J. Cell Biol. 148:1165-1176(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBN1.
  7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCEBPA_HUMAN
AccessioniPrimary (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: October 29, 2014
This is version 140 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3