Coiled-coil_domain-containing_37_(FLJ40083)

Coiled-coil domain-containing 37 (FLJ40083)

Coiled-coil domain-containing 37 (FLJ40083)

Protein found in humans


Coiled-coil domain-containing 37, also known as FLJ40083, is a protein that in humans is encoded by the CCDC37 gene (3q21.3). There is no confirmed function of CCDC37.

Gene

Locus

The human gene CCDC37 is found on chromosome 3 at the band 3q21.3.[1] It extends from base pairs 90,403,731 to 90,429,231, making the gene 25,500 base pairs long. It is located on the plus strand and contains 17 exons.[citation needed]

Homology

Paralogs

There is only one paralog for CCDC37 found in humans, CCDC38. CCDC38 is located on chromosome 12.[2]

Orthologs

The ortholog space of CCDC37 is fairly broad including mammals, reptiles, birds, amphibians, fish, invertebrates, and fungi.[citation needed]

More information Genus and species, Common name ...

Protein

Primary sequence

The gene encodes a protein called CCDC37. This protein in 611 amino acids in length and has a molecular weight of 71.1 kilodaltons and an isoelectric point of pI=6.7.[citation needed]

Domains

CCDC37 contains a DUF4200 region located from amino acid 151 to 269.[1] There is no known function for DUF4200. CCDC37 also contains three coiled coil domains at amino acids 164–203, 392–436, and 526–571.[3]

Post-translational modifications

The protein has several probable post-translational modifications. It contains four possible PEST sequence at amino acids 17–36, 293–304, 337–360, and 360–395.[4] It also contains a possible substrate of N-acetyltransferase A at Ser2.[5]

Signal peptides

CCDC37 has a predicted nuclear localization via Reinhard's method[6] (reliability 94.1%) using a bipartite nuclear localization signal peptide starting at amino acid 155: KRQMFLLQYALDVKRRE.[7] CCDC37 also has a few predicted nuclear export signals I232, L235, I239, and M551.[8]

Expression

CCDC37 protein is widely expressed in mus musculus but only minimally so. Most areas that express CCDC37 have an expression level of 20-40%. Expression levels in the trigeminal nerve, testis, medial olfactory epithelium, dorsal root ganglia, and trachea are the highest with almost 75% expression.[9] CCDC37 is expressed in the cerebellum, medulla, and hippocampal formation in the brain of mus musculus.[10]

Between 20 and 30 days after birth in mus musculus, CCDC37 expression increases from less than 50% to about 85%.[11]

In rattus norvegicus CCDC37 is highly expressed in oligodendrocyte progenitor cells (approximately 85%) but only narrowly expressed in oligodendrocytes themselves (~40%).[12]

Interacting proteins

Transcription factors

There are many predicted transcription factor binding sites in the CCDC37 promoter.[citation needed] Below is a table of the best possibilities, which have high confidence values, evolutionary conservation, and/or multiple possible binding sites in the promoter.

More information Transcription Factor, Start ...

Interactions

There have been three proteins found to interact by physical association with CCDC37 through a yeast two-hybrid screen: histone-lysine N-methyltransferase (SUV39H1), histone-lysine N-methyltransferase (SUV39H2), and lysine-specific histone demethylase 1A (KDM1A).[13]

Clinical significance

In a study of the genes expressed in lung squamous cell carcinomas it was found that the promoter region of CCDC37 was hyper methylated causing down regulation of the expression of CCDC37.[14] In a separate study, CCDC37 was also found in spatial and temporal regions in mice that are associated with hereditary congenital facial paresis (HCFP) gene. However through knock out experiments in mice it was found that CCDC37 was unlikely to be a causative agent for the HCFP phenotype.[15]


References

  1. "CCDC37 coiled-coil domain containing 37 [Homo sapiens (human)] - Gene". Ncbi.nlm.nih.gov. Retrieved 2015-03-07.
  2. Dinkel, H. The eukaryotic linear motif resource ELM: 10 years and counting. Nucleic Acids Res. 2014 Jan;42(Database issue):D259-66.
  3. "EMBOSS: epestfind". Emboss.bioinformatics.nl. Retrieved 2015-03-07.
  4. Kiemer, Lars, Kyrlov Bendtsen, and Blom, Nikolai. NetAcet: Prediction of N-terminal Acetylation Sites. Bioinformatics, 2004.
  5. A. Reinhardt and T. Hubbard, Nucleic Acids Res. 26, 2230, 1998
  6. Dingwall C, Robbins J, Dilworth SM, Roberts B, Richardson WD (Sep 1988). "The nucleoplasmin nuclear location sequence is larger and more complex than that of SV-40 large T antigen". J. Cell Biol. 107 (3): 841–9.
  7. Analysis and prediction of leucine-rich nuclear export signals Tanja la Cour, Lars Kiemer, Anne Mølgaard, Ramneek Gupta, Karen Skriver and Søren Brunak Protein Eng. Des. Sel., 17(6):527-36, 2004.
  8. "4632676 - GEO Profiles - NCBI". Ncbi.nlm.nih.gov. 2014-11-12. Retrieved 2015-03-07.
  9. Primary publication: Lein, E.S. et al. (2007) Genome-wide atlas of gene expression in the adult mouse brain, Nature 445: 168-176. doi: 10.1038/nature05453; and
  10. "4786837 - GEO Profiles - NCBI". Ncbi.nlm.nih.gov. 2014-11-12. Retrieved 2015-03-07.
  11. "31253706 - GEO Profiles - NCBI". Ncbi.nlm.nih.gov. 2014-11-12. Retrieved 2015-03-07.
  12. Weimann, M. A Y2H-seq approach defines the human protein methyltransferase interactome. Nat Methods. 2013 Apr;10(4):339-42.
  13. Kwon, Yong-Jae PhD; Lee, Seog Joo MSc et al. Genome-Wide Analysis of DNA Methylation and the Gene Expression Change in Lung Cancer Journal of Thoracic Oncology: January 2012 - Volume 7 - Issue 1 - pp 20-33.

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