CFAP298

CFAP298 is a gene found on the 21st chromosome at 21q22.1. A total of thirteen splice variants have been found, but only eleven protein coding ones.Ensembl http://ensembl.org The most common form of CFAP298 mRNA has 1427 base pairs broken into seven exons. Its closest neighbors on the chromosome are TCP10L, EVA1C, LOC100506185, OR7E23P, and SYNJ1.

The CFAP298 primary sequence is found in high quantity in most tissues. Some tissues with notable less expression are the ganglions, the heart, and the liver.C21orf59 GDS596 GEOprofile It is suspected CFAP298 is found in the brain early in development due to the two achaete-scute complex homologue transcription factor binding sites found in the promoter.{{cite web | title = Genomatix | url = http://www.genomatix.de/ | access-date = 2012-04-20 | archive-date = 2021-12-02 | archive-url = https://web.archive.org/web/20211202010908/https://www.genomatix.de/ | url-status = dead }}

The CFAP298 primary sequence consists of 290 amino acids with mass 33.093 kDa. The isoelectric point is 7.283, but is reduced to 5.86 if fully phosphorylated.{{cite web | url = http://www.phosphosite.org/proteinAction.do?id=6493&showAllSites=true | title = Cilia- and flagella-associated protein 298 | work = Phosphosite }} Several post-translational modifications have been found by mass spectroscopy: five phosphorylation sites, one methylation site, one ubiquitination site, and one acetylation site. Most of these modifications happen in the latter half of the protein.

The majority of the protein consists of the domain DUF2870. This domain is primarily found in homologues of CFAP298, but also in other uncharacterized proteins,[https://www.ncbi.nlm.nih.gov/cdd Conserved Domains] and it contains the majority of the sites that are modified after translation. The protein is predicted to consist mostly of alpha helices and lack beta strands.SDSC PELE

CFAP298 has been shown to localize to the cytosol and the nucleus,{{cite journal | vauthors = Hu YH, Warnatz HJ, Vanhecke D, Wagner F, Fiebitz A, Thamm S, Kahlem P, Lehrach H, Yaspo ML, Janitz M | display-authors = 6 | title = Cell array-based intracellular localization screening reveals novel functional features of human chromosome 21 proteins | journal = BMC Genomics | volume = 7 | pages = 155 | date = June 2006 | pmid = 16780588 | pmc = 1526728 | doi = 10.1186/1471-2164-7-155 | doi-access = free }} but has been predicted, albeit with less strength, to localize to the cytoskeleton, peroxisome, and the mitochondria.{{cite web | title = PsortII | url = http://www.psort.org/ }}

Through mass spectrometry, interactions with SUMO2,{{cite journal | vauthors = Golebiowski F, Matic I, Tatham MH, Cole C, Yin Y, Nakamura A, Cox J, Barton GJ, Mann M, Hay RT | display-authors = 6 | title = System-wide changes to SUMO modifications in response to heat shock | journal = Science Signaling | volume = 2 | issue = 72 | pages = ra24 | date = May 2009 | pmid = 19471022 | doi = 10.1126/scisignal.2000282 | s2cid = 33450256 }} a post-translational modification protein resembling ubiquitin, and Ubiquitin C{{cite journal | vauthors = Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP | display-authors = 6 | title = Systematic and quantitative assessment of the ubiquitin-modified proteome | journal = Molecular Cell | volume = 44 | issue = 2 | pages = 325–40 | date = October 2011 | pmid = 21906983 | pmc = 3200427 | doi = 10.1016/j.molcel.2011.08.025 }} have been identified. Through two-hybrid experiments, an interaction with MAPK6, a protein kinase, has been found.{{cite journal | vauthors = Vinayagam A, Stelzl U, Foulle R, Plassmann S, Zenkner M, Timm J, Assmus HE, Andrade-Navarro MA, Wanker EE | display-authors = 6 | title = A directed protein interaction network for investigating intracellular signal transduction | journal = Science Signaling | volume = 4 | issue = 189 | pages = rs8 | date = September 2011 | pmid = 21900206 | doi = 10.1126/scisignal.2001699 | s2cid = 7418133 }}

A study in zebrafish has shown CFAP298 is found in high concentrations in the Kupffer vesicles, and is intracellularly localized to the basal body of the cilia.{{cite thesis |last1=Schottenfeld |first1=Jodi |title=The role of PKD2 and C21ORF59 in patterning the left-right axis of the zebrafish embryo |date=2008 |id={{Gale|A195982386}} |oclc=236339661 }} Zebrafish mutant in CFAP298 homologue have defects in ciliary motility. Additionally, motile cilia in zebrafish and xenopus CFAP298 mutants are immotile and mispolarized, suggesting CFAP298 plays roles in planar cell polarity as well as ciliary motility.{{cite journal | vauthors = Jaffe KM, Grimes DT, Schottenfeld-Roames J, Werner ME, Ku TS, Kim SK, Pelliccia JL, Morante NF, Mitchell BJ, Burdine RD | display-authors = 6 | title = c21orf59/kurly Controls Both Cilia Motility and Polarization | journal = Cell Reports | volume = 14 | issue = 8 | pages = 1841–9 | date = March 2016 | pmid = 26904945 | pmc = 4775428 | doi = 10.1016/j.celrep.2016.01.069 }}

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• {{UCSC gene info|CFAP298}}

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