Summary: Coilin N-terminus
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Coilin Edit Wikipedia article
|, Coil, C79982, Cln80, p80, p80-coilin, coilin|
Coilin is a protein that in humans is encoded by the COIL gene. Coilin got its name from the coiled shape of the Cajal bodies in which it is found. It was first identified using human autoimmune serum.
Coilin protein is one of the main molecular components of Cajal bodies. Cajal bodies are non-membrane bound nuclear bodies 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.
To study CBs, coilin can be combined with GFP (Green Fluorescent Protein) to form Coilin-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.
- GRCh38: Ensembl release 89: ENSG00000121058 - Ensembl, May 2017
- GRCm38: Ensembl release 89: ENSMUSG00000033983 - Ensembl, May 2017
- "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- 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): 4462â€“9. doi:10.1093/nar/22.21.4462. PMC 308480. PMID 7971277.
- "Entrez Gene: COIL coilin".
- Hong S, Ka S, Kim S, Park Y, Kang S (May 2003). "p80 coilin, a coiled body-specific protein, interacts with ataxin-1, the SCA1 gene product". Biochim. Biophys. Acta. 1638 (1): 35â€“42. doi:10.1016/s0925-4439(03)00038-3. PMID 12757932.
- Hong S, Lee S, Cho SG, Kang S (Jun 2008). "UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1". Biochem. Biophys. Res. Commun. 371 (2): 256â€“60. doi:10.1016/j.bbrc.2008.04.066. PMID 18439907.
- Isaac C, Yang Y, Meier UT (Jul 1998). "Nopp140 functions as a molecular link between the nucleolus and the coiled bodies". J. Cell Biol. 142 (2): 319â€“29. doi:10.1083/jcb.142.2.319. PMC 2133063. PMID 9679133.
- Hebert MD, Shpargel KB, Ospina JK, Tucker KE, Matera AG (Sep 2002). "Coilin methylation regulates nuclear body formation". Dev. Cell. 3 (3): 329â€“37. doi:10.1016/s1534-5807(02)00222-8. PMID 12361597.
- Hebert MD, Szymczyk PW, Shpargel KB, Matera AG (Oct 2001). "Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein". Genes Dev. 15 (20): 2720â€“9. doi:10.1101/gad.908401. PMC 312817. PMID 11641277.
- Ogg SC, Lamond AI (October 14, 2002). "Cajal bodies and coilin â€” moving towards function". J. Cell Biol. 159 (1): 17â€“21. doi:10.1083/jcb.200206111. PMC 2173504. PMID 12379800.
- Andrade LE, Chan EK, Raska I, Peebles CL, Roos G, Tan EM (1991). "Human autoantibody to a novel protein of the nuclear coiled body: immunological characterization and cDNA cloning of p80-coilin". J. Exp. Med. 173 (6): 1407â€“19. doi:10.1084/jem.173.6.1407. PMC 2190846. PMID 2033369.
- Bohmann K, Ferreira JA, Lamond AI (1996). "Mutational analysis of p80 coilin indicates a functional interaction between coiled bodies and the nucleolus". J. Cell Biol. 131 (4): 817â€“31. doi:10.1083/jcb.131.4.817. PMC 2200013. PMID 7490287.
- Carmo-Fonseca M, Ferreira J, Lamond AI (1993). "Assembly of snRNP-containing coiled bodies is regulated in interphase and mitosis--evidence that the coiled body is a kinetic nuclear structure". J. Cell Biol. 120 (4): 841â€“52. doi:10.1083/jcb.120.4.841. PMC 2200076. PMID 7679389.
- Robertson NG, Khetarpal U, GutiÃ©rrez-Espeleta GA, Bieber FR, Morton CC (1995). "Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening". Genomics. 23 (1): 42â€“50. doi:10.1006/geno.1994.1457. PMID 7829101.
- Kusuda J, Tanuma R, Gotoh E, Toyoda A, Hashimoto K (1995). "Assignment of a human autoimmune antigen, p80-coilin gene to chromosome 17q21-q23 and of its possible pseudogene to chromosome 14". Hum. Genet. 95 (2): 233â€“4. doi:10.1007/BF00209411. PMID 7860074.
- Lyon CE, Bohmann K, Sleeman J, Lamond AI (1997). "Inhibition of protein dephosphorylation results in the accumulation of splicing snRNPs and coiled bodies within the nucleolus". Exp. Cell Res. 230 (1): 84â€“93. doi:10.1006/excr.1996.3380. PMID 9013710.
- Parfenov VN, Davis DS, Pochukalina GN, Kostyuchek D, Murti KG (1998). "Dynamics of distribution of splicing components relative to the transcriptional state of human oocytes from antral follicles". J. Cell. Biochem. 69 (1): 72â€“80. doi:10.1002/(SICI)1097-4644(19980401)69:1<72::AID-JCB8>3.0.CO;2-S. PMID 9513048.
- Pochukalina GN, Davis DS, Kostiuchek DF, Murti KG, Parfenov VN (1998). "[Splicing factors in oocyte nuclei from human antral follicles]". Tsitologiia. 40 (4): 239â€“47. PMID 9644758.
- Isaac C, Yang Y, Meier UT (1998). "Nopp140 functions as a molecular link between the nucleolus and the coiled bodies". J. Cell Biol. 142 (2): 319â€“29. doi:10.1083/jcb.142.2.319. PMC 2133063. PMID 9679133.
- Liu J, Hebert MD, Ye Y, Templeton DJ, Kung H, Matera AG (2000). "Cell cycle-dependent localization of the CDK2-cyclin E complex in Cajal (coiled) bodies". J. Cell Sci. 113 (9): 1543â€“52. PMID 10751146.
- Hebert MD, Matera AG (2001). "Self-association of coilin reveals a common theme in nuclear body localization". Mol. Biol. Cell. 11 (12): 4159â€“71. doi:10.1091/mbc.11.12.4159. PMC 15064. PMID 11102515.
- Young PJ, Le TT, Dunckley M, Nguyen TM, Burghes AH, Morris GE (2001). "Nuclear gems and Cajal (coiled) bodies in fetal tissues: nucleolar distribution of the spinal muscular atrophy protein, SMN". Exp. Cell Res. 265 (2): 252â€“61. doi:10.1006/excr.2001.5186. PMID 11302690.
- Hebert MD, Szymczyk PW, Shpargel KB, Matera AG (2001). "Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein". Genes Dev. 15 (20): 2720â€“9. doi:10.1101/gad.908401. PMC 312817. PMID 11641277.
- Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1â€“11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
- Sleeman JE, Ajuh P, Lamond AI (2002). "snRNP protein expression enhances the formation of Cajal bodies containing p80-coilin and SMN". J. Cell Sci. 114 (Pt 24): 4407â€“19. PMID 11792806.
- Hebert MD, Shpargel KB, Ospina JK, Tucker KE, Matera AG (2002). "Coilin methylation regulates nuclear body formation". Dev. Cell. 3 (3): 329â€“37. doi:10.1016/S1534-5807(02)00222-8. PMID 12361597.
- Shpargel KB, Ospina JK, Tucker KE, Matera AG, Hebert MD (2003). "Control of Cajal body number is mediated by the coilin C-terminus". J. Cell Sci. 116 (Pt 2): 303â€“12. doi:10.1242/jcs.00211. PMID 12482916.
- Sleeman JE, Trinkle-Mulcahy L, Prescott AR, Ogg SC, Lamond AI (2004). "Cajal body proteins SMN and Coilin show differential dynamic behaviour in vivo". J. Cell Sci. 116 (Pt 10): 2039â€“50. doi:10.1242/jcs.00400. PMID 12679382.
- Hearst SM, Gilder AS, Negi SS, Davis MD, George EM, Whittom AA, Toyota CG, Husedzinovic A, Gruss OJ, Hebert MD (2009). "Cajal-body formation correlates with differential coilin phosphorylation in primary and transformed cell lines". J. Cell Sci. 122 (Pt 11): 1872â€“81. doi:10.1242/jcs.044040. PMC 2684838. PMID 19435804.
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Coilin N-terminus Provide feedback
No Pfam abstract.
This tab holds annotation information from the InterPro database.
InterPro entry IPR031722Coilin is a nuclear phosphoprotein that concentrates within Cajal bodies (CBs) and has a role in small nuclear ribonucleoprotein (snRNP) biogenesis [PUBMED:15862129]. Coilin also acts to repress polymerase I activity in response to cisplatin-induced DNA damage, which could indicate a link between the DNA damage response and the inhibition of rRNA synthesis [PUBMED:21289084]. Conservation at the amino acid level is highest within coilin's N- and C-termini. The first N-terminal 92-amino acid domain have been shown to self-interact and to be essential for proper targeting of coilin to CBs [PUBMED:7490287, PUBMED:11102515].
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|Number in seed:||39|
|Number in full:||358|
|Average length of the domain:||188.70 aa|
|Average identity of full alignment:||21 %|
|Average coverage of the sequence by the domain:||33.40 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
|Download:||download the raw HMM for this family|
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Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
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Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
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The tree shows the occurrence of this domain across different species. More...
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
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