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CEBPD

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
CEBPD
Identifiers
Aliases CEBPD , C/EBP-delta, CELF, CRP3, NF-IL6-beta, CCAAT/enhancer binding protein delta, CCAAT enhancer binding protein delta
External IDsOMIM: 116898; MGI: 103573; HomoloGene: 3808; GeneCards: CEBPD; OMA:CEBPD - orthologs
Gene location (Human)
Chromosome 8 (human)
Chr. Chromosome 8 (human) [1]
Band 8q11.21Start47,736,913 bp [1]
End47,738,164 bp [1]
Gene location (Mouse)
Chromosome 16 (mouse)
Chr. Chromosome 16 (mouse)[2]
Band 16 A2|16 10.09 cMStart15,705,150 bp [2]
End15,708,895 bp [2]
RNA expression pattern
Bgee
Human Mouse (ortholog)
  • pericardium

  • vena cava

  • lower lobe of lung

  • trachea

  • cardia

  • beta cell

  • mucosa of paranasal sinus

  • olfactory bulb

  • cartilage tissue

  • gastric mucosa
  • left lung lobe

  • granulocyte

  • umbilical cord

  • endothelial cell of lymphatic vessel

  • gastrula

  • right lung

  • muscle of thigh

  • carotid body

  • ankle

  • ankle joint
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

1052

12609

Ensembl

ENSG00000221869

ENSMUSG00000071637

UniProt

P49716

Q00322

RefSeq (mRNA)

NM_005195

NM_007679

RefSeq (protein)

NP_005186

NP_031705

Location (UCSC)Chr 8: 47.74 – 47.74 Mb Chr 16: 15.71 – 15.71 Mb
PubMed search[3] [4]
Wikidata

CCAAT/enhancer-binding protein delta is a protein that in humans is encoded by the CEBPD gene.[5] [6]

Function

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The protein encoded by this intronless gene is a bZIP transcription factor which can bind as a homodimer to certain DNA regulatory regions. It can also form heterodimers with the related protein CEBP-alpha. The encoded protein is important in the regulation of genes involved in immune and inflammatory responses, and may be involved in the regulation of genes associated with activation and/or differentiation of macrophages.[7]

Functions

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CEBPD is involved in regulation of apoptosis and cell proliferation. It probably acts as tumor suppressor.[8]

One study in mice showed that CEBPD prevents development of tubular injury and tubulointerstitial fibrogenesis during the progression of chronic obstructive nephropathy.[9]

Function of CEBPD gene can be effectively examined by siRNA knockdown based on an independent validation.[10]

Interactions

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CEBPD has been shown to interact with Mothers against decapentaplegic homolog 3.[11]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000221869Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000071637Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Cao Z, Umek RM, McKnight SL (September 1991). "Regulated expression of three C/EBP isoforms during adipose conversion of 3T3-L1 cells". Genes & Development. 5 (9): 1538–1552. doi:10.1101/gad.5.9.1538 . PMID 1840554.
  6. ^ Williams SC, Cantwell CA, Johnson PF (September 1991). "A family of C/EBP-related proteins capable of forming covalently linked leucine zipper dimers in vitro". Genes & Development. 5 (9): 1553–1567. doi:10.1101/gad.5.9.1553 . PMID 1884998.
  7. ^ "Entrez Gene: CEBPD CCAAT/enhancer binding protein (C/EBP), delta".
  8. ^ Gery S, Tanosaki S, Hofmann WK, Koppel A, Koeffler HP (February 2005). "C/EBPdelta expression in a BCR-ABL-positive cell line induces growth arrest and myeloid differentiation". Oncogene. 24 (9): 1589–1597. doi:10.1038/sj.onc.1208393. PMID 15674331. S2CID 24347537.
  9. ^ Duitman J, Borensztajn KS, Pulskens WP, Leemans JC, Florquin S, Spek CA (January 2014). "CCAAT-enhancer binding protein delta (C/EBPδ) attenuates tubular injury and tubulointerstitial fibrogenesis during chronic obstructive nephropathy". Laboratory Investigation; A Journal of Technical Methods and Pathology. 94 (1): 89–97. doi:10.1038/labinvest.2013.127 . PMID 24247561.
  10. ^ Munkácsy G, Sztupinszki Z, Herman P, Bán B, Pénzváltó Z, Szarvas N, et al. (September 2016). "Validation of RNAi Silencing Efficiency Using Gene Array Data shows 18.5% Failure Rate across 429 Independent Experiments". Molecular Therapy. Nucleic Acids. 5 (9) e366. doi:10.1038/mtna.2016.66. PMC 5056990 . PMID 27673562.
  11. ^ Choy L, Derynck R (March 2003). "Transforming growth factor-beta inhibits adipocyte differentiation by Smad3 interacting with CCAAT/enhancer-binding protein (C/EBP) and repressing C/EBP transactivation function". The Journal of Biological Chemistry. 278 (11): 9609–9619. doi:10.1074/jbc.M212259200 . PMID 12524424.

Further reading

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.


(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2 /EREBP -related factors
(0.6) Miscellaneous
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