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P49715

- CEBPA_HUMAN

UniProt

P49715 - CEBPA_HUMAN

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
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (05 Feb 2008)
      Previous versions | rss
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    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. protein binding Source: IntAct
    3. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: UniProtKB
    4. sequence-specific DNA binding Source: InterPro
    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. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    23. response to glucocorticoid Source: Ensembl
    24. response to vitamin B2 Source: Ensembl
    25. transcription, DNA-templated Source: UniProtKB
    26. transcription from RNA polymerase II promoter Source: ProtInc
    27. urea cycle Source: Ensembl
    28. viral process Source: UniProtKB-KW
    29. white fat cell differentiation Source: Ensembl

    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

    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

    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

    PRIDEiP49715.

    PTM databases

    PhosphoSiteiP49715.

    Expressioni

    Gene expression databases

    BgeeiP49715.
    CleanExiHS_CEBPA.
    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. 95 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 annotationsAdd
    BLAST

    Region

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

    Phylogenomic databases

    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]
    ProtoNetiSearch...

    Sequencei

    Sequence statusi: Complete.

    P49715-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESADFYEAE PRPPMSSHLQ SPPHAPSSAA FGFPRGAGPA QPPAPPAAPE    50
    PLGGICEHET SIDISAYIDP AAFNDEFLAD LFQHSRQQEK AKAAVGPTGG 100
    GGGGDFDYPG APAGPGGAVM PGGAHGPPPG YGCAAAGYLD GRLEPLYERV 150
    GAPALRPLVI KQEPREEDEA KQLALAGLFP YQPPPPPPPS HPHPHPPPAH 200
    LAAPHLQFQI AHCGQTTMHL QPGHPTPPPT PVPSPHPAPA LGAAGLPGPG 250
    SALKGLGAAH PDLRASGGSG AGKAKKSVDK NSNEYRVRRE RNNIAVRKSR 300
    DKAKQRNVET QQKVLELTSD NDRLRKRVEQ LSRELDTLRG IFRQLPESSL 350
    VKAMGNCA 358
    Length:358
    Mass (Da):37,561
    Last modified:February 5, 2008 - v3
    Checksum:i574C0A049E25BCAC
    GO

    Sequence conflict

    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. 95 interactions.
    IntActi P49715. 13 interactions.
    MINTi MINT-264048.

    PTM databases

    PhosphoSitei P49715.

    Polymorphism databases

    DMDMi 166898082.

    Proteomic databases

    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

    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.
    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

    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 1, 2014
    This is version 139 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

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