C11orf16

C11orf16
Identifiers
AliasesC11orf16, chromosome 11 open reading frame 16
External IDsMGI: 1928824 HomoloGene: 49631 GeneCards: C11orf16
Gene location (Human)
Chr.Chromosome 11 (human)[1]
Band11p15.4Start8,920,076 bp[1]
End8,933,006 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

56673

57355

Ensembl

ENSG00000176029

ENSMUSG00000031022

UniProt

Q9NQ32

Q9JJR6

RefSeq (mRNA)

NM_020643

NM_001040700
NM_020609

RefSeq (protein)

NP_065694

NP_001035790

Location (UCSC)Chr 11: 8.92 – 8.93 MbChr 7: 109.71 – 109.72 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Gene C11orf16, chromosome 11 open reading frame 16, is a protein in humans that is encoded by the C11orf16 gene.[5][6] 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.

Gene Neighborhood

Gene 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.

C11orf16 expression in human body sites extracted from NCBI GEO profile

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 martix 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.[7]

mRNA

Isoform

The predicted C11orf16 transcript variant X1 is 2386bp long and has NCBI accession number of XM_017018013.1.[8]

Homology

Paralogs

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

Orthologs

DescriptionCommon NameNCBI accession IDQuery CoverE valueIdentityDate of Divergent (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.

The multiple sequence alignment shows the conservation of the gene C11orf16

Protein

Molecular Weight

The predicted molecular weight of the protein encoded by C11orf16 is 51 kiloDaltons.[9][10]

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.[11] The picture indicates the location of the motifs.

The predicted motifs of C11orf16 are shown in different colors to the corresponding amino acids


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.

The secondary structure of protein C11orf16

Post-translational Modifications

No transmembrane helices[12], potential GPI-modification site, and TM-protein were found. There were 7 predicted sumoylation sites[13], multiple phosporylation cites with most of them being unsp[14], and 9 glycosylation cites[15].

Post translational modification of protein C11orf16[16]


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%.[17]


Protein Interaction

Proteins C1orf105(Chromosome 1 open reading frame105 ), PWWP2A, and SMYD1(SET and MYND domain containing 1) were found to be interacting with C11orf16[18].


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[19].

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000176029 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031022 - Ensembl, May 2017
  3. "Human PubMed Reference:".
  4. "Mouse PubMed Reference:".
  5. Amid C, Bahr A, Mujica A, Sampson N, Bikar SE, Winterpacht A, Zabel B, Hankeln T, Schmidt ER (Aug 2001). "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". Cytogenet Cell Genet. 93 (3–4): 284–90. doi:10.1159/000056999. PMID 11528127.
  6. "Entrez Gene: C11orf16 chromosome 11 open reading frame 16".
  7. "Genomatix".
  8. "NCBI Nucleotide".
  9. "Expasy".
  10. "Sigma Antibodies".
  11. "Motif Scan".
  12. "TMHMM".
  13. "SUMOplot".
  14. "NetPhos".
  15. "YingOYang".
  16. "PROTTER".
  17. "PSORTII".
  18. "STRING".
  19. "SWISS-MODEL".

Further reading

  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  • 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.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
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