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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Cytoplasmic FMR1-interacting protein 2''' is a [[protein]] that in humans is encoded by the ''CYFIP2'' [[gene]].<ref name="pmid11438699">{{cite journal | vauthors = Schenck A, Bardoni B, Moro A, Bagni C, Mandel JL | title = A highly conserved protein family interacting with the fragile X genetic condition protein (FMRP) and displaying selective interactions with FMRP-related proteins FXR1P and FXR2P | journal = Proc Natl Acad Sci U S A | volume = 98 | issue = 15 | pages = 8844–9 |date=Jul 2001 | pmid = 11438699 | pmc = 37523 | doi = 10.1073/pnas.151231598 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CYFIP2 cytoplasmic FMR1 interacting protein 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26999| accessdate = }}</ref> Cytoplasmic FMR1 interacting protein is a  1253 amino acid  long protein and is highly conserved sharing 99% sequence identity to the mouse protein.<ref name="pmid11438699"/><ref>https://www.genecards.org/cgi-bin/carddisp.pl?gene=GRIA4</ref> It is expressed mainly in brain tissues, white blood cells and the kidney.<ref name="pmid15075390">{{cite journal |vauthors=Su AI, Wiltshire T, Batalov S |title=A gene atlas of the mouse and human protein-encoding transcriptomes |journal=[[Proc. Natl. Acad. Sci. U.S.A.]] |volume=101 |issue=16 |pages=6062–7 |date=April 2004 |pmid=15075390 |pmc=395923 |doi=10.1073/pnas.0400782101 |url=http://www.pnas.org/cgi/pmidlookup?view=long&pmid=15075390|display-authors=etal}}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Cytoplasmic FMR1 interacting protein 2
| HGNCid = 13760
| Symbol = CYFIP2
| AltSymbols =; PIR121
| OMIM = 606323
| ECnumber = 
| Homologene = 7936
| MGIid = 1924134
| Function =
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0019717 |text = synaptosome}}
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 26999
    | Hs_Ensembl = ENSG00000055163
    | Hs_RefseqProtein = NP_001032409
    | Hs_RefseqmRNA = NM_001037332
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 156625669
    | Hs_GenLoc_end = 156755184
    | Hs_Uniprot = 
    | Mm_EntrezGene = 76884
    | Mm_Ensembl = ENSMUSG00000020340
    | Mm_RefseqmRNA = NM_133769
    | Mm_RefseqProtein = NP_598530
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 46037278
    | Mm_GenLoc_end = 46155773
    | Mm_Uniprot = 
  }}
}}
'''Cytoplasmic FMR1 interacting protein 2''', also known as '''CYFIP2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CYFIP2 cytoplasmic FMR1 interacting protein 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26999| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
CYFIP2 has been shown to [[Protein-protein interaction|interact]] with [[FMR1]].<ref name="pmid11438699"/><ref name="pmid12837692">{{cite journal | vauthors = Bardoni B, Castets M, Huot ME, Schenck A, Adinolfi S, Corbin F, Pastore A, Khandjian EW, Mandel JL | title = 82-FIP, a novel FMRP (fragile X mental retardation protein) interacting protein, shows a cell cycle-dependent intracellular localization | journal = Hum. Mol. Genet. | volume = 12 | issue = 14 | pages = 1689–98 |date=July 2003 | pmid = 12837692 | doi = 10.1093/hmg/ddg181 | url = }}</ref> CYFIP2 is a p-53 inducible protein<ref name="pmid10449408">{{cite journal |vauthors=Saller E, Tom E, Brunori M |title=Increased apoptosis induction by 121F mutant p53 |journal=[[EMBO J.]] |volume=18 |issue=16 |pages=4424–37 |date=August 1999 |pmid=10449408 |pmc=1171517 |doi=10.1093/emboj/18.16.4424|display-authors=etal}}</ref> and also interacts with the Fragile=X mental retardation protein.<ref name="b">Schenck, A., Bardoni, B., Moro, A., Bagni, C., Mandel, J.-L. (2001) Proceedings of the National Academy of Sciences of the United States of America, 98, 8844-8849.</ref>
{{PBB_Summary
 
| section_title =  
== RNA editing ==
| summary_text =  
 
}}
The pre-[[Messenger RNA|mRNA]] of this protein is subject to [[RNA editing]].<ref name="pmid15731336">{{cite journal | vauthors = Levanon EY, Hallegger M, Kinar Y, Shemesh R, Djinovic-Carugo K, Rechavi G, Jantsch MF, Eisenberg E | title = Evolutionarily conserved human targets of adenosine to inosine RNA editing | journal = Nucleic Acids Res. | volume = 33 | issue = 4 | pages = 1162–8 | year = 2005 | pmid = 15731336 | pmc = 549564 | doi = 10.1093/nar/gki239 | url = }}</ref> The editing site was previously recorded as a single nucleotide polymorphism (rs3207362) in the dbSNP.<ref name="pmid15731336"/>
 
=== Type ===
 
'''A to I''' RNA editing is catalyzed by a family of [[adenosine deaminase]]s acting on RNA (ADARs) that specifically recognize adenosines within double-stranded regions of pre-mRNAs and deaminate  them to [[inosine]]. Inosines  are recognised as guanosine by the cells translational machinery. There are three members of the ADAR family ADARs 1-3 with [[ADAR|ADAR1]]  and [[ADARB1|ADAR2]] being the only enzymatically active members. [[ADARB2|ADAR3]] is thought to have a regulatory role in the brain.  ADAR1 and ADAR 2 are widely expressed in tissues while ADAR3 is restricted to the brain. The double stranded regions of RNA are formed  by base-pairing between residues in the close to region of the editing site with residues usually in a  neighboring intron but can be an exonic sequence. The region that base pairs with the editing region is known as an Editing Complementary Sequence (ECS).
 
=== Site ===
 
An editing site was found in the pre-mRNA of this protein. The substitution occurs within amino acid position 320 in humans and also in mice.A possible double stranded RNA region has not been detected for this pre-mRNA.<ref name="pmid15731336"/> No double stranded region required by ADARs has predicted.Immunoprecipitation experiments and RNA interference have shown that ADAR 2 is likely to be the main editing enzyme for this site with ADAR 1 having a minor role.<ref name="pmid18430892">{{cite journal | vauthors = Riedmann EM, Schopoff S, Hartner JC, Jantsch MF | title = Specificity of ADAR-mediated RNA editing in newly identified targets | journal = RNA | volume = 14 | issue = 6 | pages = 1110–8 |date=June 2008 | pmid = 18430892 | pmc = 2390793 | doi = 10.1261/rna.923308 | url = }}</ref><ref name="pmid18407364">{{cite journal | vauthors = Nishimoto Y, Yamashita T, Hideyama T, Tsuji S, Suzuki N, Kwak S | title = Determination of editors at the novel A-to-I editing positions | journal = Neurosci. Res. | volume = 61 | issue = 2 | pages = 201–6 |date=June 2008 | pmid = 18407364 | doi = 10.1016/j.neures.2008.02.009 | url = }}</ref>
 
=== Regulation ===
 
Editing seems to be differentially regulated in different tissues. The highest level of editing occurs in the cerebellum with lower frequency of editing detected in human lung, prostrate and uterus tissues. Editing frequency varies from 30-85% depending on tissue.<ref name="pmid15731336"/><ref name="pmid18430892" />{<ref name="pmid18407364"/> There is some evidence for a  decrease in CYFIP2 editing with increased age.<ref name="pmid20538013">{{cite journal |vauthors=Nicholas A, de Magalhaes JP, Kraytsberg Y, Richfield EK, Levanon EY, Khrapko K |title=Age-related gene-specific changes of A-to-I mRNA editing in the human brain |journal=[[Mech. Ageing Dev.]] |volume=131 |issue=6 |pages=445–7 |date=June 2010 |pmid=20538013 |doi=10.1016/j.mad.2010.06.001 |url=http://linkinghub.elsevier.com/retrieve/pii/S0047-6374(10)00112-0 |pmc=2915444}}</ref>
 
==== Conservation ====
 
Editing of the pre-mRNA of this gene has been detected in mouse and chicken.<ref name="pmid15731336"/>
 
=== Effects of RNA editing ===
 
==== Structural ====
 
Editing results in a codon change resulting in a [[glutamic acid]] being translated instead of a [[lysine]].<ref name="pmid15731336"/>
 
==== Functional ====
 
Currently unknown but editing may have role in regulation of  apoptotic functions of this protein.It is thought that since the protein is p53 inducible that the protein may be pro-apopototic. Also ADAR1 knock out mice show increase in apoptosis which indicates editing may be involved in regulation of the cellular  process.<ref name="pmid10449408" /><ref name="pmid15731336"/>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|CYFIP2}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
| citations =
*{{cite journal  | vauthors=Kitamura T, Kitamura Y, Yonezawa K |title=Molecular cloning of p125Nap1, a protein that associates with an SH3 domain of Nck |journal=Biochem. Biophys. Res. Commun. |volume=219 |issue= 2 |pages= 509–14 |year= 1996 |pmid= 8605018 |doi=10.1006/bbrc.1996.0264 |display-authors=etal}}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |display-authors=etal}}
*{{cite journal  | author=Kitamura T, Kitamura Y, Yonezawa K, ''et al.'' |title=Molecular cloning of p125Nap1, a protein that associates with an SH3 domain of Nck. |journal=Biochem. Biophys. Res. Commun. |volume=219 |issue= 2 |pages= 509-14 |year= 1996 |pmid= 8605018 |doi=  }}
*{{cite journal  | vauthors=Witke W, Podtelejnikov AV, Di Nardo A |title=In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly |journal=EMBO J. |volume=17 |issue= 4 |pages= 967–76 |year= 1998 |pmid= 9463375 |doi= 10.1093/emboj/17.4.967 | pmc=1170446 |display-authors=etal}}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal  | vauthors=Saller E, Tom E, Brunori M |title=Increased apoptosis induction by 121F mutant p53 |journal=EMBO J. |volume=18 |issue= 16 |pages= 4424–37 |year= 1999 |pmid= 10449408 |doi= 10.1093/emboj/18.16.4424 | pmc=1171517 |display-authors=etal}}
*{{cite journal  | author=Witke W, Podtelejnikov AV, Di Nardo A, ''et al.'' |title=In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly. |journal=EMBO J. |volume=17 |issue= 4 |pages= 967-76 |year= 1998 |pmid= 9463375 |doi= 10.1093/emboj/17.4.967 }}
*{{cite journal  | vauthors=Hirosawa M, Nagase T, Ishikawa K |title=Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain |journal=DNA Res. |volume=6 |issue= 5 |pages= 329–36 |year= 2000 |pmid= 10574461 |doi=10.1093/dnares/6.5.329  |display-authors=etal}}
*{{cite journal  | author=Saller E, Tom E, Brunori M, ''et al.'' |title=Increased apoptosis induction by 121F mutant p53. |journal=EMBO J. |volume=18 |issue= 16 |pages= 4424-37 |year= 1999 |pmid= 10449408 |doi= 10.1093/emboj/18.16.4424 }}
*{{cite journal  | vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA Cloning Using In Vitro Site-Specific Recombination |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948 }}
*{{cite journal  | author=Hirosawa M, Nagase T, Ishikawa K, ''et al.'' |title=Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain. |journal=DNA Res. |volume=6 |issue= 5 |pages= 329-36 |year= 2000 |pmid= 10574461 |doi= }}
*{{cite journal  | vauthors=Wiemann S, Weil B, Wellenreuther R |title=Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.GR1547R  | pmc=311072 |display-authors=etal}}
*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
*{{cite journal  | vauthors=Eden S, Rohatgi R, Podtelejnikov AV |title=Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck |journal=Nature |volume=418 |issue= 6899 |pages= 790–3 |year= 2002 |pmid= 12181570 |doi= 10.1038/nature00859 |display-authors=etal}}
*{{cite journal  | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Schenck A, Bardoni B, Moro A, ''et al.'' |title=A highly conserved protein family interacting with the fragile X mental retardation protein (FMRP) and displaying selective interactions with FMRP-related proteins FXR1P and FXR2P. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 15 |pages= 8844-9 |year= 2001 |pmid= 11438699 |doi= 10.1073/pnas.151231598 }}
*{{cite journal  | vauthors=Salazar MA, Kwiatkowski AV, Pellegrini L |title=Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton |journal=J. Biol. Chem. |volume=278 |issue= 49 |pages= 49031–43 |year= 2004 |pmid= 14506234 |doi= 10.1074/jbc.M308104200 |display-authors=etal}}
*{{cite journal  | author=Eden S, Rohatgi R, Podtelejnikov AV, ''et al.'' |title=Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. |journal=Nature |volume=418 |issue= 6899 |pages= 790-3 |year= 2002 |pmid= 12181570 |doi= 10.1038/nature00859 }}
*{{cite journal  | vauthors=Brajenovic M, Joberty G, Küster B |title=Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network |journal=J. Biol. Chem. |volume=279 |issue= 13 |pages= 12804–11 |year= 2004 |pmid= 14676191 |doi= 10.1074/jbc.M312171200 |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Innocenti M, Zucconi A, Disanza A |title=Abi1 is essential for the formation and activation of a WAVE2 signalling complex |journal=Nat. Cell Biol. |volume=6 |issue= 4 |pages= 319–27 |year= 2004 |pmid= 15048123 |doi= 10.1038/ncb1105 |display-authors=etal}}
*{{cite journal  | author=Salazar MA, Kwiatkowski AV, Pellegrini L, ''et al.'' |title=Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton. |journal=J. Biol. Chem. |volume=278 |issue= 49 |pages= 49031-43 |year= 2004 |pmid= 14506234 |doi= 10.1074/jbc.M308104200 }}
*{{cite journal  | vauthors=Mayne M, Moffatt T, Kong H |title=CYFIP2 is highly abundant in CD4+ cells from multiple sclerosis patients and is involved in T cell adhesion |journal=Eur. J. Immunol. |volume=34 |issue= 4 |pages= 1217–27 |year= 2004 |pmid= 15048733 |doi= 10.1002/eji.200324726 |display-authors=etal}}
*{{cite journal  | author=Brajenovic M, Joberty G, Küster B, ''et al.'' |title=Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network. |journal=J. Biol. Chem. |volume=279 |issue= 13 |pages= 12804-11 |year= 2004 |pmid= 14676191 |doi= 10.1074/jbc.M312171200 }}
*{{cite journal  | vauthors=Jin J, Smith FD, Stark C |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436–50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051 |display-authors=etal}}
*{{cite journal  | author=Innocenti M, Zucconi A, Disanza A, ''et al.'' |title=Abi1 is essential for the formation and activation of a WAVE2 signalling complex. |journal=Nat. Cell Biol. |volume=6 |issue= 4 |pages= 319-27 |year= 2004 |pmid= 15048123 |doi= 10.1038/ncb1105 }}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Mayne M, Moffatt T, Kong H, ''et al.'' |title=CYFIP2 is highly abundant in CD4+ cells from multiple sclerosis patients and is involved in T cell adhesion. |journal=Eur. J. Immunol. |volume=34 |issue= 4 |pages= 1217-27 |year= 2004 |pmid= 15048733 |doi= 10.1002/eji.200324726 }}
*{{cite journal  | vauthors=Wiemann S, Arlt D, Huber W |title=From ORFeome to Biology: A Functional Genomics Pipeline |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704  | pmc=528930 |display-authors=etal}}
*{{cite journal  | author=Jin J, Smith FD, Stark C, ''et al.'' |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436-50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051 }}
*{{cite journal  | vauthors=Levanon EY, Hallegger M, Kinar Y |title=Evolutionarily conserved human targets of adenosine to inosine RNA editing |journal=Nucleic Acids Res. |volume=33 |issue= 4 |pages= 1162–8 |year= 2005 |pmid= 15731336 |doi= 10.1093/nar/gki239  | pmc=549564 |display-authors=etal}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | vauthors=Rual JF, Venkatesan K, Hao T |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |display-authors=etal}}
*{{cite journal  | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
*{{cite journal  | author=Levanon EY, Hallegger M, Kinar Y, ''et al.'' |title=Evolutionarily conserved human targets of adenosine to inosine RNA editing. |journal=Nucleic Acids Res. |volume=33 |issue= 4 |pages= 1162-8 |year= 2005 |pmid= 15731336 |doi= 10.1093/nar/gki239 }}
*{{cite journal  | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
}}
{{refend}}
{{refend}}
{{protein-stub}}
{{WikiDoc Sources}}

Latest revision as of 07:44, 23 March 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

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RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Cytoplasmic FMR1-interacting protein 2 is a protein that in humans is encoded by the CYFIP2 gene.[1][2] Cytoplasmic FMR1 interacting protein is a 1253 amino acid long protein and is highly conserved sharing 99% sequence identity to the mouse protein.[1][3] It is expressed mainly in brain tissues, white blood cells and the kidney.[4]

Interactions

CYFIP2 has been shown to interact with FMR1.[1][5] CYFIP2 is a p-53 inducible protein[6] and also interacts with the Fragile=X mental retardation protein.[7]

RNA editing

The pre-mRNA of this protein is subject to RNA editing.[8] The editing site was previously recorded as a single nucleotide polymorphism (rs3207362) in the dbSNP.[8]

Type

A to I RNA editing is catalyzed by a family of adenosine deaminases acting on RNA (ADARs) that specifically recognize adenosines within double-stranded regions of pre-mRNAs and deaminate them to inosine. Inosines are recognised as guanosine by the cells translational machinery. There are three members of the ADAR family ADARs 1-3 with ADAR1 and ADAR2 being the only enzymatically active members. ADAR3 is thought to have a regulatory role in the brain. ADAR1 and ADAR 2 are widely expressed in tissues while ADAR3 is restricted to the brain. The double stranded regions of RNA are formed by base-pairing between residues in the close to region of the editing site with residues usually in a neighboring intron but can be an exonic sequence. The region that base pairs with the editing region is known as an Editing Complementary Sequence (ECS).

Site

An editing site was found in the pre-mRNA of this protein. The substitution occurs within amino acid position 320 in humans and also in mice.A possible double stranded RNA region has not been detected for this pre-mRNA.[8] No double stranded region required by ADARs has predicted.Immunoprecipitation experiments and RNA interference have shown that ADAR 2 is likely to be the main editing enzyme for this site with ADAR 1 having a minor role.[9][10]

Regulation

Editing seems to be differentially regulated in different tissues. The highest level of editing occurs in the cerebellum with lower frequency of editing detected in human lung, prostrate and uterus tissues. Editing frequency varies from 30-85% depending on tissue.[8][9]{[10] There is some evidence for a decrease in CYFIP2 editing with increased age.[11]

Conservation

Editing of the pre-mRNA of this gene has been detected in mouse and chicken.[8]

Effects of RNA editing

Structural

Editing results in a codon change resulting in a glutamic acid being translated instead of a lysine.[8]

Functional

Currently unknown but editing may have role in regulation of apoptotic functions of this protein.It is thought that since the protein is p53 inducible that the protein may be pro-apopototic. Also ADAR1 knock out mice show increase in apoptosis which indicates editing may be involved in regulation of the cellular process.[6][8]

References

  1. ↑ 1.0 1.1 1.2 Schenck A, Bardoni B, Moro A, Bagni C, Mandel JL (Jul 2001). "A highly conserved protein family interacting with the fragile X genetic condition protein (FMRP) and displaying selective interactions with FMRP-related proteins FXR1P and FXR2P". Proc Natl Acad Sci U S A. 98 (15): 8844–9. doi:10.1073/pnas.151231598. PMC 37523. PMID 11438699.
  2. ↑ "Entrez Gene: CYFIP2 cytoplasmic FMR1 interacting protein 2".
  3. ↑ https://www.genecards.org/cgi-bin/carddisp.pl?gene=GRIA4
  4. ↑ Su AI, Wiltshire T, Batalov S, et al. (April 2004). "A gene atlas of the mouse and human protein-encoding transcriptomes". Proc. Natl. Acad. Sci. U.S.A. 101 (16): 6062–7. doi:10.1073/pnas.0400782101. PMC 395923. PMID 15075390.
  5. ↑ Bardoni B, Castets M, Huot ME, Schenck A, Adinolfi S, Corbin F, Pastore A, Khandjian EW, Mandel JL (July 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. ↑ 6.0 6.1 Saller E, Tom E, Brunori M, et al. (August 1999). "Increased apoptosis induction by 121F mutant p53". EMBO J. 18 (16): 4424–37. doi:10.1093/emboj/18.16.4424. PMC 1171517. PMID 10449408.
  7. ↑ Schenck, A., Bardoni, B., Moro, A., Bagni, C., Mandel, J.-L. (2001) Proceedings of the National Academy of Sciences of the United States of America, 98, 8844-8849.
  8. ↑ 8.0 8.1 8.2 8.3 8.4 8.5 8.6 Levanon EY, Hallegger M, Kinar Y, Shemesh R, Djinovic-Carugo K, Rechavi G, Jantsch MF, Eisenberg E (2005). "Evolutionarily conserved human targets of adenosine to inosine RNA editing". Nucleic Acids Res. 33 (4): 1162–8. doi:10.1093/nar/gki239. PMC 549564. PMID 15731336.
  9. ↑ 9.0 9.1 Riedmann EM, Schopoff S, Hartner JC, Jantsch MF (June 2008). "Specificity of ADAR-mediated RNA editing in newly identified targets". RNA. 14 (6): 1110–8. doi:10.1261/rna.923308. PMC 2390793. PMID 18430892.
  10. ↑ 10.0 10.1 Nishimoto Y, Yamashita T, Hideyama T, Tsuji S, Suzuki N, Kwak S (June 2008). "Determination of editors at the novel A-to-I editing positions". Neurosci. Res. 61 (2): 201–6. doi:10.1016/j.neures.2008.02.009. PMID 18407364.
  11. ↑ Nicholas A, de Magalhaes JP, Kraytsberg Y, Richfield EK, Levanon EY, Khrapko K (June 2010). "Age-related gene-specific changes of A-to-I mRNA editing in the human brain". Mech. Ageing Dev. 131 (6): 445–7. doi:10.1016/j.mad.2010.06.001. PMC 2915444. PMID 20538013.

External links

Further reading

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