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P17676

- CEBPB_HUMAN

UniProt

P17676 - CEBPB_HUMAN

Protein

CCAAT/enhancer-binding protein beta

Gene

CEBPB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 2 (22 Aug 2003)
      Previous versions | rss
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    Functioni

    Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. Binds to regulatory regions of several acute-phase and cytokines genes and probably plays a role in the regulation of acute-phase reaction, inflammation and hemopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Plays an important role in adipose tissue differentiation. Regulates the transcriptional induction of peroxisome proliferator-activated receptor gamma (PPARG) as well as other adipogenesis key player genes.1 Publication
    Isoform 3: acts as a dominant negative through heterodimerization with isoform 2.1 Publication

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. protein binding Source: UniProtKB
    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 Source: Ensembl
    6. sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

    1. acute-phase response Source: ProtInc
    2. brown fat cell differentiation Source: Ensembl
    3. cellular response to amino acid stimulus Source: Ensembl
    4. embryonic placenta development Source: Ensembl
    5. immune response Source: ProtInc
    6. inflammatory response Source: ProtInc
    7. mammary gland epithelial cell differentiation Source: Ensembl
    8. mammary gland epithelial cell proliferation Source: Ensembl
    9. negative regulation of neuron apoptotic process Source: Ensembl
    10. negative regulation of transcription, DNA-templated Source: Ensembl
    11. neuron differentiation Source: Ensembl
    12. positive regulation of fat cell differentiation Source: UniProtKB
    13. positive regulation of osteoblast differentiation Source: Ensembl
    14. regulation of interleukin-6 biosynthetic process Source: Ensembl
    15. regulation of transcription, DNA-templated Source: UniProtKB
    16. regulation of transcription involved in cell fate commitment Source: UniProtKB
    17. response to endoplasmic reticulum stress Source: UniProtKB
    18. response to lipopolysaccharide Source: Ensembl
    19. transcription from RNA polymerase II promoter Source: ProtInc

    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 beta
    Short name:
    C/EBP beta
    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:CEBPB
    Synonyms:TCF5
    ORF Names:PP9092
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:1834. CEBPB.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. nuclear chromatin Source: Ensembl
    3. nuclear matrix Source: Ensembl
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26377.

    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
    Cross-linki174 – 174Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei235 – 2351Phosphothreonine; by RPS6KA11 Publication

    Post-translational modificationi

    Sumoylated by polymeric chains of SUMO2 or SUMO3.1 Publication
    Phosphorylated at Thr-235 by RPS6KA1.1 Publication

    Keywords - PTMi

    Isopeptide bond, 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

    ArrayExpressiP17676.
    BgeeiP17676.
    CleanExiHS_CEBPB.
    GenevestigatoriP17676.

    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 EP300.3 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.
    TP53P046374EBI-969696,EBI-366083

    Protein-protein interaction databases

    BioGridi107480. 67 interactions.
    DIPiDIP-35345N.
    IntActiP17676. 9 interactions.
    MINTiMINT-230873.
    STRINGi9606.ENSP00000305422.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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
    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.
    HOGENOMiHOG000013112.
    HOVERGENiHBG050879.
    InParanoidiP17676.
    KOiK10048.
    OMAiCKKPAEY.
    OrthoDBiEOG7R56TQ.
    PhylomeDBiP17676.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative initiation. Align

    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

    MQRLVAWDPA CLPLPPPPPA FKSMEVANFY YEADCLAAAY GGKAAPAAPP    50
    AARPGPRPPA GELGSIGDHE RAIDFSPYLE PLGAPQAPAP ATATDTFEAA 100
    PPAPAPAPAS SGQHHDFLSD LFSDDYGGKN CKKPAEYGYV SLGRLGAAKG 150
    ALHPGCFAPL HPPPPPPPPP AELKAEPGFE PADCKRKEEA GAPGGGAGMA 200
    AGFPYALRAY LGYQAVPSGS SGSLSTSSSS SPPGTPSPAD AKAPPTACYA 250
    GAAPAPSQVK SKAKKTVDKH SDEYKIRRER NNIAVRKSRD KAKMRNLETQ 300
    HKVLELTAEN ERLQKKVEQL SRELSTLRNL FKQLPEPLLA SSGHC 345
    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:
    EMBL
    GenBank
    DDBJ
    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. [P17676-1]
    GeneIDi1051.
    KEGGihsa:1051.
    UCSCiuc002xvi.2. human. [P17676-1]

    Polymorphism databases

    DMDMi34223718.

    Keywords - Coding sequence diversityi

    Alternative initiation, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS13429.1. [P17676-1 ]
    PIRi S12788.
    S66246.
    RefSeqi NP_001272807.1. NM_001285878.1. [P17676-2 ]
    NP_001272808.1. NM_001285879.1. [P17676-3 ]
    NP_005185.2. NM_005194.3. [P17676-1 ]
    UniGenei Hs.517106.
    Hs.719041.
    Hs.720603.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GTW X-ray 1.85 A/B 259-336 [» ]
    1GU4 X-ray 1.80 A/B 259-336 [» ]
    1GU5 X-ray 2.10 A/B 259-336 [» ]
    1H88 X-ray 2.80 A/B 259-336 [» ]
    1H89 X-ray 2.45 A/B 273-336 [» ]
    1H8A X-ray 2.23 A/B 259-336 [» ]
    1HJB X-ray 3.00 A/B/D/E 259-345 [» ]
    1IO4 X-ray 3.00 A/B 259-336 [» ]
    2E42 X-ray 1.80 A/B 259-336 [» ]
    2E43 X-ray 2.10 A/B 259-336 [» ]
    ProteinModelPortali P17676.
    SMRi P17676. Positions 268-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107480. 67 interactions.
    DIPi DIP-35345N.
    IntActi P17676. 9 interactions.
    MINTi MINT-230873.
    STRINGi 9606.ENSP00000305422.

    PTM databases

    PhosphoSitei P17676.

    Polymorphism databases

    DMDMi 34223718.

    Proteomic databases

    MaxQBi P17676.
    PaxDbi P17676.
    PeptideAtlasi P17676.
    PRIDEi P17676.

    Protocols and materials databases

    DNASUi 1051.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303004 ; ENSP00000305422 ; ENSG00000172216 . [P17676-1 ]
    GeneIDi 1051.
    KEGGi hsa:1051.
    UCSCi uc002xvi.2. human. [P17676-1 ]

    Organism-specific databases

    CTDi 1051.
    GeneCardsi GC20P048807.
    H-InvDB HIX0174729.
    HGNCi HGNC:1834. CEBPB.
    HPAi CAB004213.
    MIMi 189965. gene.
    neXtProti NX_P17676.
    PharmGKBi PA26377.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG299311.
    HOGENOMi HOG000013112.
    HOVERGENi HBG050879.
    InParanoidi P17676.
    KOi K10048.
    OMAi CKKPAEY.
    OrthoDBi EOG7R56TQ.
    PhylomeDBi P17676.
    TreeFami TF105008.

    Enzyme and pathway databases

    Reactomei REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinki P17676.

    Miscellaneous databases

    EvolutionaryTracei P17676.
    GeneWikii CEBPB.
    GenomeRNAii 1051.
    NextBioi 4401.
    PROi P17676.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17676.
    Bgeei P17676.
    CleanExi HS_CEBPB.
    Genevestigatori P17676.

    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. "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. "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.
    10. "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.
    11. "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.
    12. "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.
    13. "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].
    14. "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.
    15. "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.
    16. 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: October 1, 2014
    This is version 166 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