RDBP

Negative elongation factor E is a protein that in humans is encoded by the RDBP gene.[5]

NELFE
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesNELFE, D6S45, NELF-E, RD, RDBP, RDP, negative elongation factor complex member E
External IDsOMIM: 154040 MGI: 102744 HomoloGene: 134736 GeneCards: NELFE
Orthologs
SpeciesHumanMouse
Entrez

7936

27632

Ensembl

ENSMUSG00000024369

UniProt

P18615

P19426

RefSeq (mRNA)

NM_002904

NM_001045863
NM_001045864
NM_138580

RefSeq (protein)

NP_002895

NP_001039328
NP_001039329
NP_613046

Location (UCSC)Chr 6: 31.95 – 31.96 MbChr 17: 35.07 – 35.08 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

The protein encoded by this gene is part of a complex termed negative elongation factor (NELF) which represses RNA polymerase II transcript elongation. This protein bears similarity to nuclear RNA-binding proteins; however, it has not been demonstrated that this protein binds RNA. The protein contains a tract of alternating basic and acidic residues, largely arginine (R) and aspartic acid (D). The gene localizes to the major histocompatibility complex (MHC class III) region on chromosome 6.[5]

Interactions

RDBP has been shown to interact with:

References

  1. ENSG00000206357, ENSG00000231044, ENSG00000204356, ENSG00000206268, ENSG00000233801 GRCh38: Ensembl release 89: ENSG00000229363, ENSG00000206357, ENSG00000231044, ENSG00000204356, ENSG00000206268, ENSG00000233801 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000024369 - Ensembl, 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. "Entrez Gene: RDBP RD RNA binding protein".
  6. Narita T, Yamaguchi Y, Yano K, Sugimoto S, Chanarat S, Wada T, Kim DK, Hasegawa J, Omori M, Inukai N, Endoh M, Yamada T, Handa H (Mar 2003). "Human transcription elongation factor NELF: identification of novel subunits and reconstitution of the functionally active complex". Molecular and Cellular Biology. 23 (6): 1863–73. doi:10.1128/mcb.23.6.1863-1873.2003. PMC 149481. PMID 12612062.
  7. Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM (Jan 2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. 83 (1): 153–67. doi:10.1016/s0888-7543(03)00235-0. PMID 14667819.
  8. Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

Further reading

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