C11orf16

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

Gene C11orf16, chromosome 11 open reading frame 16, is a protein in humans that is encoded by the C11orf16 gene.{{cite journal|vauthors=Amid C, Bahr A, Mujica A, Sampson N, Bikar SE, Winterpacht A, Zabel B, Hankeln T, Schmidt ER|date=Aug 2001|title=Comparative genomic sequencing reveals a strikingly similar architecture of a conserved syntenic region on human chromosome 11p15.3 (including gene ST5) and mouse chromosome 7|journal=Cytogenet Cell Genet|volume=93|issue=3–4|pages=284–90|doi=10.1159/000056999|pmid=11528127|s2cid=27611036}}{{cite web|url=https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=56673|title=Entrez Gene: C11orf16 chromosome 11 open reading frame 16}} It has 7 exons, and the size of 467 amino acids.

Gene

=Location=

The gene C11orf16 is located on chromosome 11(p15.4), starting at 8,920,076bp and ending at 8,933,006bp.

File:C11orf16.png

=Gene neighborhood=

Gene [https://web.archive.org/web/20180507154844/http://www.wikigenes.org/e/gene/e/56787.html ASCL3] and AKIP1 are the neighbor genes of C11orf16 on chromosome 11.

=Expression=

==Human==

The gene does not have high expression throughout the body tissues. The percentile rank within the sample are higher in pancreas, ovary, and appendix.

File:Expression of C11orf16.png

==Mouse brain==

Even though the gene does not have a significant high expression in the mouse brain, it is most expressed in midbrain, isocortex, olfactory areas, and medulla.

=Transcription factors=

Some transcription factors that have the higher matrix similarity are Kruppel-like zinc finger protein 219, zinc finger protein 263, ZKSCAN12 (zinc finger protein with KRAB and SCAN domains 12), chorion-specific transcription factor GCMa, and Ras-responsive element binding protein 1.{{cite web|title=Genomatix|url=https://www.genomatix.de/?s=f235485dde95ccac200db8865073698a|access-date=2018-05-06|archive-date=2021-08-17|archive-url=https://web.archive.org/web/20210817155656/https://www.genomatix.de/?s=f235485dde95ccac200db8865073698a|url-status=dead}}

mRNA

=[[Isoform]]=

The predicted C11orf16 transcript variant X1 is 2386bp long and has NCBI accession number of XM_017018013.1.{{cite web|title=NCBI Nucleotide|date=22 November 2021 |url=https://www.ncbi.nlm.nih.gov/nuccore/XM_017018013.1}}

Homology

=Paralogs=

No paralogs were found for the C11orf16 gene through NCBI BLAST.

=[[Orthologs]]=

class="wikitable"
DescriptionCommon nameNCBI accession IDQuery coverE valueIdentityDate of divergence (MYA)
Homo sapiensHumanNP_065694.2100 %0100%N/A
Pongo abeliiSumatran orangutanPNJ2462884%095%15.2
Aotus nancymaaeNancy Ma's night monkeyXP_012312127.188%084%42.6
Chinchilla lanigeraLong-tailed chinchillaXP_013367496.197%068%88
Equus przewalskiiPrzewalski's horseXP_008512245.198%073%94
Cervus elaphus hippelaphusCentral European red deerOWK17675.199%067%94
Hipposideros armigerGreat roundleaf batXP_019511755.199%065%94
Neomonachus schauinslandiHawaiian monk sealXP_021541375.199%066%94
Lipotes vexilliferBaijiXP_007459933.198%068%94
Myotis brandtiiBrandt's batXP_005874017.198%1e-17467%94
Chelonia mydasGreen sea turtleXP_007057171.183%1e-5737%320
Balearica regulorum gibbericepsGrey crowned craneXP_010311948.170%6e-540%320

=Conservation=

The gene C11orf16 is conserved in many animal species including mammals, avians, and reptiles.

File:1.BOX.6735.9907.pdf

Protein

=Molecular weight=

The predicted molecular weight of the protein encoded by C11orf16 is 51 kilodaltons.{{cite web|title=Expasy|url=https://web.expasy.org/compute_pi/}}{{cite web|title=Sigma Antibodies|url=https://www.sigmaaldrich.com/catalog/product/sigma/sab2106115?lang=en®ion=US}}

=Domains and motifs=

Several protein domains and motifs were found including CHD5-like protein, tyrosine kinase phosphorylation site, protein kinase C phosphorylation site, N-myristoylation site, casein kinase II phosphorylation site, and cGMP-dependent protein kinase phosphorylation site.{{cite web|title=Motif Scan|url=https://myhits.isb-sib.ch/cgi-bin/motif_scan}} The picture indicates the location of the motifs.

File:PROTTER-motifs.png

=Secondary structure=

The protein is predicted to be made up with 21.2% of alpha helix, 15.2% of extended strand, and 63% of random coil.

File:Secondary_structure_of_C11orf16.png

=Post-translational modifications=

No transmembrane helices,{{cite web|title=TMHMM|url=http://www.cbs.dtu.dk/services/TMHMM/}} potential GPI-modification sites, or TM-proteins were found. There were seven predicted sumoylation sites,{{cite web|title=SUMOplot|url=http://www.abgent.com/sumoplot}} multiple phosporylation sites with most of them being unspecified,{{cn|date=June 2023}} and nine glycosylation sites.{{cite web|title=YingOYang|url=http://www.cbs.dtu.dk/services/YinOYang/}}

File:PROTTER-PTM.png

=Subcellular localization predictor=

The protein is predicted to be localized to the nucleus with the probability of 47.8%; mitochondria with the probability of 26.1%.{{cite web|title=PSORTII|url=https://psort.hgc.jp/cgi-bin/runpsort.pl}}{{Dead link|date=June 2019 |bot=InternetArchiveBot |fix-attempted=yes }}

=Protein interaction=

Proteins C1orf105 (Chromosome 1 open reading frame 105), PWWP2A, and SMYD1(SET and MYND domain containing 1) were found to be interacting with C11orf16.{{cite web|title=String|url=https://string-db.org/}}

Clinical significance

=Disease association=

Protein coded by C11orf16 gene is also predicted to have 19.61% sequence identity to tumor suppressor p53-binding protein suggesting that this gene might be involved with tumor suppressing process.{{cite web|title=SWISS-MODEL|url=https://swissmodel.expasy.org/interactive/c4PYLU/models/|access-date=2018-05-06|archive-url=https://web.archive.org/web/20180507085545/https://swissmodel.expasy.org/interactive/c4PYLU/models/|archive-date=2018-05-07|url-status=dead}}

References

{{reflist}}

Further reading

{{refbegin | 2}}

  • {{cite journal | vauthors=Kimura K, Wakamatsu A, Suzuki Y |title=Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 | pmc=1356129 |display-authors=etal}}
  • {{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 |bibcode=2005Natur.437.1173R |s2cid=4427026 |display-authors=etal}}
  • {{cite journal | vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 |doi-access=free }}
  • {{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 }}

{{refend}}

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