Nucleoporin 214

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NUP214
Protein NUP214 PDB 2oit.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases NUP214, CAIN, CAN, D9S46E, N214, p250, nucleoporin 214kDa, nucleoporin 214
External IDs MGI: 1095411 HomoloGene: 38008 GeneCards: NUP214
Gene location (Human)
Chromosome 9 (human)
Chr. Chromosome 9 (human)[1]
Chromosome 9 (human)
Genomic location for NUP214
Genomic location for NUP214
Band No data available Start 131,125,561 bp[1]
End 131,234,670 bp[1]
RNA expression pattern
PBB GE NUP214 202155 s at fs.png

PBB GE NUP214 211261 at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005085
NM_001318324
NM_001318325

NM_172268

RefSeq (protein)

NP_001305253
NP_001305254
NP_005076

NP_758472

Location (UCSC) Chr 9: 131.13 – 131.23 Mb Chr 9: 31.97 – 32.05 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Nucleoporin 214 (Nup2014) is a protein that in humans is encoded by the NUP214 gene.[5][6][7]

Function[edit]

The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells. This gene is a member of the FG-repeat-containing nucleoporins. The protein encoded by this gene is localized to the cytoplasmic face of the nuclear pore complex where it is required for proper cell cycle progression and nucleocytoplasmic transport. The 3' portion of this gene forms a fusion gene with the DEK gene on chromosome 6 in a t(6,9) translocation associated with acute myeloid leukemia and myelodysplastic syndrome.[7]

Structure[edit]

The structure of the N-terminal domain of Nup214 reveals a sevenbladed beta-propeller fold followed by a 30-residue C-terminal extended peptide segment (CTE). The CTE folds back onto the beta propeller and binds to its bottom face.[8] The structure of the Nup214 NTD bound to the helicase Ddx19 in its ADP-bound state reveals the molecular basis for the interaction between the two proteins. A conserved residue of Ddx19 is shown to be crucial for complex formation in vitro and in vivo. Strikingly, the interaction surfaces exhibit strongly opposing surface potentials, with the helicase surface being positively and the Nup214 surface being negatively charged. Ddx19 is shown to bind RNA only in its ATP-bound state, and the binding of RNA and the Nup214 NTD is mutually exclusive.[9]

Interactions[edit]

NUP214 has been shown to interact with:

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000126883 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001855 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ Kraemer D, Wozniak RW, Blobel G, Radu A (Feb 1994). "The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm". Proceedings of the National Academy of Sciences of the United States of America. 91 (4): 1519–23. PMC 43191Freely accessible. PMID 8108440. doi:10.1073/pnas.91.4.1519. 
  6. ^ von Lindern M, Poustka A, Lerach H, Grosveld G (Aug 1990). "The (6;9) chromosome translocation, associated with a specific subtype of acute nonlymphocytic leukemia, leads to aberrant transcription of a target gene on 9q34". Molecular and Cellular Biology. 10 (8): 4016–26. PMC 360912Freely accessible. PMID 2370860. doi:10.1128/mcb.10.8.4016. 
  7. ^ a b "Entrez Gene: NUP214 nucleoporin 214kDa". 
  8. ^ Napetschnig J, Blobel G, Hoelz A (2007). "Crystal structure of the N-terminal domain of the human protooncogene Nup214/CAN". Proc. Natl. Acad. Sci. U.S.A. 104 (6): 1783–8. PMC 1794303Freely accessible. PMID 17264208. doi:10.1073/pnas.0610828104. 
  9. ^ a b Napetschnig J, Kassube SA, Debler EW, Wong RW, Blobel G, Hoelz A (2009). "Structural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19". Proc. Natl. Acad. Sci. U.S.A. 106 (9): 3089–94. PMC 2651337Freely accessible. PMID 19208808. doi:10.1073/pnas.0813267106. 
  10. ^ a b Herold A, Suyama M, Rodrigues JP, Braun IC, Kutay U, Carmo-Fonseca M, Bork P, Izaurralde E (Dec 2000). "TAP (NXF1) belongs to a multigene family of putative RNA export factors with a conserved modular architecture". Molecular and Cellular Biology. 20 (23): 8996–9008. PMC 86553Freely accessible. PMID 11073998. doi:10.1128/mcb.20.23.8996-9008.2000. 
  11. ^ Schmitt I, Gerace L (Nov 2001). "In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap". The Journal of Biological Chemistry. 276 (45): 42355–63. PMID 11551912. doi:10.1074/jbc.M103916200. 
  12. ^ Carman JA, Nadler SG (Mar 2004). "Direct association of tristetraprolin with the nucleoporin CAN/Nup214". Biochemical and Biophysical Research Communications. 315 (2): 445–9. PMID 14766228. doi:10.1016/j.bbrc.2004.01.080. 

Further reading[edit]