KIAA0090 explained

KIAA0090 is a human gene coding for a protein of unknown function.[1] KIAA0090 has two aliases OTTHUMP00000002581 and RP1-43E13.1. The gene codes for multiple transcript variants which can localize to different subcellular compartments. KIAA0090 interacts with multiple effector proteins. KIAA0090 contains a conserved COG1520 WD40 like repeat domain thought to be the method of such interaction.

Characterization of the KIAA0090 gene and its transcript products

KIAA0090 is located on chromosome one in the p arm at location 1p36.132.[2] It covers 36.74 kb, from base pairs 19451486 to 19414744. The gene is composed of 37 gt-at introns/alternative introns with 57 exons expressed in 1 unspliced form of 4253 bp and 20 alternatively spliced forms of varying lengths.[3] The gene has 8 probable promoters.[4] The gene is flanked by UBR4 on its right and MRTO4 on its left.[1] This Information is graphically displayed in Figure 1.

Expressed Sequence Tags and isolated cDNA clones indicate KIAA0090 is expressed ubiquitously in low to moderate levels throughout the body.[5] This includes but is not limited to testis, tongue, lung, cerebellum, brain, mammary gland, trachea, placenta, esophageal, salivary gland, brain, hippocampus, amygdale, bone marrow, thalamus, spleen, uterus, thymus, kidney, eye, heart, gall bladder, prostate, liver, parathyroid gland, ovary, stomach, skeletal muscle, colon, pancreas, and skin. Expression of KIAA0090 changes throughout development (embryogenesis, fetal, adult, etc.)and during carcinogenesis. Evidence indicates a correlation between conditions and expression level but no data exists to suggest KIAA0090 is responsible for any disease or stage of development.

The mRNA for this gene codes for 18 protein isoforms6. The remaining 3 splice variants have no evidence supporting their ability to be translated.

Characterization of the KIAA0090 protein product

Analysis indicates the KIAA0090 unspliced protein product to be 993 amino acids long with an isoelectric point of 7.418 and a molecular weight of 111765.73 daltons.[6] [7] The primary structure of this protein contains 4 conserved domains.[8] This includes a signal peptide from position 1 to 22, a COG1520 WD40 like domain, a leucine zipper domain, a DUF1620 domain (domain of unknown function), and a transmembrane domain. These can be viewed in Figure 2. Several conserved cysteine residues are present at positions 226,235, 335, 364,449, 581, 675, 925, and 985.[9] Several internal localization signals are also present.[10] [11] [12] [13] [14] Dependent on splice outcome and posttranslational modification, these additional signals indicate the protein could localize to the peroxisome, the plasma membrane, outside the cell, the cytosol, the nucleus, or mitochondria.

Post translational modification of KIAA0090 can occur. 54 possible sites of phosphorylation exist; 33 serines, 10 threonines, and 11 tyrosines.[15] 3 sites of N-linked glycosylation are present at residues 370, 818, and 913[16] The signal peptide can be cleaved between residues 21 and 22.[13] This information is graphically displayed in Figure 3. Structure beyond the primary remains predicative. Bioinformatic analysis yields consensus data that is also displayed in Figure 3.[17] [18] The protein is highly conserved throughout Eukaryotes both in multi and single cellular organisms. This includes but is not limited to animals, plants, fungi, and protists.

The WD40 like domain COG1520 is KIAA0090s only identified functional effector domain. WD40 containing proteins are signal transducers involved in transduction of signals to binding factors, the centromeres, and other effectors.[19] Coimmunoprecipitation experiments have proven KIAA0090 interaction with these types of proteins; specifically the centromeric protein CENPH, the BAX Inhibitor TMBI4, the ADP ribosylation factor ARF6, the kinase TNIK, and the transcriptional repressor T22D1.[20] The number of splice variants indicates this list is probably not definitive. As further characterization is completed additional interactions would be expected.

Notes and References

  1. Web site: Enterez Gene, KIAA0090 . March 2010 . NCBI . 2010-03-21.
  2. Web site: Enterez Nucleotide, KIAA0090 . April 2010 . NCBI . 2010-04-23.
  3. Web site: Aceview . April 2010 . NCBI . 2010-04-23.
  4. Web site: El Dorado, KIAA0090 . Genomatix . Genomatix . 2010-05-10 . 2021-12-02 . https://web.archive.org/web/20211202010908/https://www.genomatix.de/ . dead .
  5. Web site: Unigene, KIAA0090 . March 2010 . NCBI . 2010-04-05.
  6. AASTATS; Jack Kramer, 1990. http://seqtool.sdsc.edu Accessed April 21, 2010
  7. PI; Program by Dr. Luca Toldo, developed at http://www.embl-heidelberg.de. Changed by Bjoern Kindler to print also the lowest found net charge. http://seqtool.sdsc.edu Accessed April 22, 2010
  8. Web site: Gene cards . 2010-02-14.
  9. Brendel V, Bucher P, Nourbakhsh IR, Blaisdell BE, Karlin S . Methods and algorithms for statistical analysis of protein sequences . Proc. Natl. Acad. Sci. U.S.A. . 89 . 6 . 2002–6 . March 1992 . 1549558 . 48584 . 10.1073/pnas.89.6.2002. 1992PNAS...89.2002B . free .
  10. Horton P, Park KJ, Obayashi T, Fujita N, Harada H, Adams-Collier CJ, Nakai K . WoLF PSORT: protein localization predictor . Nucleic Acids Res. . 35 . Web Server issue . W585–7 . July 2007 . 17517783 . 1933216 . 10.1093/nar/gkm259 .
  11. la Cour T, Kiemer L, Mølgaard A, Gupta R, Skriver K, Brunak S . Analysis and prediction of leucine-rich nuclear export signals . Protein Eng. Des. Sel. . 17 . 6 . 527–36 . June 2004 . 15314210 . 10.1093/protein/gzh062 . free .
  12. Bendtsen JD, Jensen LJ, Blom N, Von Heijne G, Brunak S . Feature-based prediction of non-classical and leaderless protein secretion . Protein Eng. Des. Sel. . 17 . 4 . 349–56 . April 2004 . 15115854 . 10.1093/protein/gzh037 . free .
  13. Bendtsen JD, Nielsen H, von Heijne G, Brunak S . Improved prediction of signal peptides: SignalP 3.0 . J. Mol. Biol. . 340 . 4 . 783–95 . July 2004 . 15223320 . 10.1016/j.jmb.2004.05.028 . 10.1.1.165.2784 .
  14. Gupta R, Brunak S . Prediction of glycosylation across the human proteome and the correlation to protein function . Pac Symp Biocomput . 310–22 . 2002 . 11928486 . 10.1142/9789812799623_0029. 978-981-02-4777-5 .
  15. Blom N, Gammeltoft S, Brunak S . Sequence and structure-based prediction of eukaryotic protein phosphorylation sites . J. Mol. Biol. . 294 . 5 . 1351–62 . December 1999 . 10600390 . 10.1006/jmbi.1999.3310 .
  16. NetNGlyc; Prediction of N-glycosylation sites in human proteins.R. Gupta, E. Jung and S. Brunak. In preparation, 2004. http://www.cbs.dtu.dk/services/NetNGlyc/ Accessed April 20, 2010.
  17. McGuffin LJ, Bryson K, Jones DT . The PSIPRED protein structure prediction server . Bioinformatics . 16 . 4 . 404–5 . April 2000 . 10869041 . 10.1093/bioinformatics/16.4.404. free .
  18. PROF; Aberystwyth University Computational Biology Group. Department of Computer Science, Aberystwyth SY23 3DB, Wales, UK. http://www.aber.ac.uk/~phiwww/prof/ Accessed: April 23, 2010
  19. Neer EJ, Schmidt CJ, Nambudripad R, Smith TF . The ancient regulatory-protein family of WD-repeat proteins . Nature . 371 . 6495 . 297–300 . September 1994 . 8090199 . 10.1038/371297a0 . 1994Natur.371..297N . 600856 .
  20. Prieto C, De Las Rivas J . APID: Agile Protein Interaction DataAnalyzer . Nucleic Acids Res. . 34 . Web Server issue . W298–302 . July 2006 . 16845013 . 1538863 . 10.1093/nar/gkl128 .