NUFIP2

Protein-coding gene in the species Homo sapiens
NUFIP2
Identifiers
AliasesNUFIP2, 182-FIP, 82-FIP, FIP-82, PIG1, FMR1 interacting protein 2, nuclear FMR1 interacting protein 2, NUFP2
External IDsOMIM: 609356 MGI: 1915814 HomoloGene: 10808 GeneCards: NUFIP2
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for NUFIP2
Genomic location for NUFIP2
Band17q11.2Start29,255,839 bp[1]
End29,294,148 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for NUFIP2
Genomic location for NUFIP2
Band11|11 B5Start77,576,981 bp[2]
End77,632,747 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • caput epididymis

  • corpus epididymis

  • secondary oocyte

  • tibialis anterior muscle

  • spongy bone

  • pancreatic epithelial cell

  • deltoid muscle

  • Achilles tendon

  • placenta

  • endothelial cell
Top expressed in
  • hand

  • body of femur

  • pineal gland

  • belly cord

  • secondary oocyte

  • foot

  • left colon

  • dermis

  • soleus muscle

  • tibialis anterior muscle
More reference expression data
BioGPS
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

57532

68564

Ensembl

ENSG00000108256

ENSMUSG00000037857

UniProt

Q7Z417

Q5F2E7

RefSeq (mRNA)

NM_020772

NM_001024205

RefSeq (protein)

NP_065823
NP_065823.1

NP_001019376

Location (UCSC)Chr 17: 29.26 – 29.29 MbChr 11: 77.58 – 77.63 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Nuclear fragile X mental retardation-interacting protein 2 is a protein that in humans is encoded by the NUFIP2 gene.[5][6][7]

Interactions

NUFIP2 has been shown to interact with FMR1 and Roquin-1.[8][5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000108256 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000037857 - 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. ^ a b Bardoni B, Castets M, Huot ME, Schenck A, Adinolfi S, Corbin F, Pastore A, Khandjian EW, Mandel JL (Jul 2003). "82-FIP, a novel FMRP (fragile X mental retardation protein) interacting protein, shows a cell cycle-dependent intracellular localization". Hum Mol Genet. 12 (14): 1689–98. doi:10.1093/hmg/ddg181. PMID 12837692.
  6. ^ Ramos A, Hollingworth D, Adinolfi S, Castets M, Kelly G, Frenkiel TA, Bardoni B, Pastore A (Jan 2006). "The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction". Structure. 14 (1): 21–31. doi:10.1016/j.str.2005.09.018. PMID 16407062.
  7. ^ "Entrez Gene: NUFIP2 nuclear fragile X mental retardation protein interacting protein 2".
  8. ^ Rehage, Nina (2018). "Binding of NUFIP2 to Roquin promotes recognition and regulation of ICOS mRNA". Nature Communications. 9 (1): 299. Bibcode:2018NatCo...9..299R. doi:10.1038/s41467-017-02582-1. PMC 5775257. PMID 29352114.

Further reading

  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Nagase T, Kikuno R, Ishikawa KI, et al. (2000). "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (1): 65–73. doi:10.1093/dnares/7.1.65. PMID 10718198.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Brill LM, Salomon AR, Ficarro SB, et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
  • Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
  • Ballif BA, Villén J, Beausoleil SA, et al. (2005). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell. Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.


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