Symbols COIL; CLN80; p80-coilin
External IDs OMIM600272 MGI104842 HomoloGene3413 GeneCards: COIL Gene
RNA expression pattern
PBB GE COIL 203654 s at tn.png
PBB GE COIL 203653 s at tn.png
More reference expression data
Species Human Mouse
Entrez 8161 12812
Ensembl ENSG00000121058 ENSMUSG00000033983
UniProt P38432 n/a
RefSeq (mRNA) NM_004645.2 NM_016706.2
RefSeq (protein) NP_004636.1 NP_057915.2
Location (UCSC) Chr 17:
55.02 – 55.04 Mb
Chr 11:
88.83 – 88.85 Mb
PubMed search [1] [2]

Coilin is a protein that in humans is encoded by the COIL gene.[1][2]

Coilin protein is one of the main molecular components of Cajal bodies (CBs). Cajal bodies are nuclear suborganelles of varying number and composition that are involved in the post-transcriptional modification of small nuclear and small nucleolar RNAs. In addition to its structural role, coilin acts as glue to connect the CB to the nucleolus. The N-terminus of the coilin protein directs its self-oligomerization while the C-terminus influences the number of nuclear bodies assembled per cell. Differential methylation and phosphorylation of coilin likely influences its localization among nuclear bodies and the composition and assembly of Cajal bodies. This gene has pseudogenes on chromosome 4 and chromosome 14.[2]

To study CBs, coilin can be combined with GFP (Green Fluorescent Protein) to form Colin-GFP hybrid protein. The hybrid protein can then be used to locate CBs underneath a microscope, usually near the nucleolus of the cell. Other proteins that make up the CB include snRNPs and nucleolar snoRNPs.

Coilin got its name from the coiled shaped of the CB in which it is found. It was first identified using human autoimmune serum.


Coilin has been shown to interact with SMN1,[3][4] SNRPB,[4] Nucleolar phosphoprotein p130[5] and Ataxin 1.[6][7]


  1. ^ Chan EK, Takano S, Andrade LE, Hamel JC, Matera AG (Dec 1994). "Structure, expression and chromosomal localization of human p80-coilin gene". Nucleic Acids Res 22 (21): 4462–9. doi:10.1093/nar/22.21.4462. PMC 308480. PMID 7971277. 
  2. ^ a b "Entrez Gene: COIL coilin". 
  3. ^ Hebert, Michael D; Shpargel Karl B, Ospina Jason K, Tucker Karen E, Matera A Gregory (Sep. 2002). "Coilin methylation regulates nuclear body formation". Dev. Cell (United States) 3 (3): 329–37. doi:10.1016/S1534-5807(02)00222-8. ISSN 1534-5807. PMID 12361597. 
  4. ^ a b Hebert, M D; Szymczyk P W, Shpargel K B, Matera A G (Oct. 2001). "Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein". Genes Dev. (United States) 15 (20): 2720–9. doi:10.1101/gad.908401. ISSN 0890-9369. PMC 312817. PMID 11641277. 
  5. ^ Isaac, C; Yang Y, Meier U T (Jul. 1998). "Nopp140 functions as a molecular link between the nucleolus and the coiled bodies". J. Cell Biol. (UNITED STATES) 142 (2): 319–29. doi:10.1083/jcb.142.2.319. ISSN 0021-9525. PMC 2133063. PMID 9679133. 
  6. ^ Hong, Sunghoi; Ka Sojeong, Kim Sungjo, Park Yongjae, Kang Seongman (May. 2003). "p80 coilin, a coiled body-specific protein, interacts with ataxin-1, the SCA1 gene product". Biochim. Biophys. Acta (Netherlands) 1638 (1): 35–42. ISSN 0006-3002. PMID 12757932. 
  7. ^ Hong, Sunghoi; Lee Soyeon, Cho Ssang-Goo, Kang Seongman (Jun. 2008). "UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1". Biochem. Biophys. Res. Commun. (United States) 371 (2): 256–60. doi:10.1016/j.bbrc.2008.04.066. PMID 18439907. 

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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