CLNS1A

Methylosome subunit pICln is a protein that in humans is encoded by the CLNS1A gene.

CLNS1A
Identifiers
Aliases	CLNS1A, CLCI, CLNS1B, ICln, chloride nucleotide-sensitive channel 1A
External IDs	OMIM: 602158; MGI: 109638; HomoloGene: 990; GeneCards: CLNS1A; OMA:CLNS1A - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q14.1 Start 77,514,936 bp End 77,637,794 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7 E1|7 53.57 cM Start 97,345,841 bp End 97,370,003 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone Achilles tendon ganglionic eminence body of pancreas right adrenal gland right adrenal cortex left ovary C1 segment left adrenal gland monocyte Top expressed in motor neuron primitive streak medial ganglionic eminence condyle fossa vestibular membrane of cochlear duct hair follicle Rostral migratory stream renal corpuscle internal carotid artery More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein heterodimerization activity protein binding RNA binding Cellular component plasma membrane cytoskeleton nucleoplasm nucleus methylosome pICln-Sm protein complex cytosol cytoplasm Biological process cell volume homeostasis chloride transport spliceosomal snRNP assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1207 12729 Ensembl ENSG00000074201 ENSMUSG00000025439 UniProt P54105 Q61189 Q923F1 RefSeq (mRNA) NM_001311202 NM_001293 NM_001311199 NM_001311200 NM_001311201 NM_023671 RefSeq (protein) NP_001284 NP_001298128 NP_001298129 NP_001298130 NP_001298131 NP_076160 Location (UCSC) Chr 11: 77.51 – 77.64 Mb Chr 7: 97.35 – 97.37 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Interactions

CLNS1A has been shown to interact with:

• ITGA2B,
• PRMT5,
• SNRPD1, and
• SNRPD3.

See also

• Chloride channel

Further reading

• Calinisan V, Gravem D, Chen RP, Brittin S, Mohandas N, Lecomte MC, Gascard P (2006). "New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium". Front. Biosci. 11: 1646–66. doi:10.2741/1911. PMID 16368544. S2CID 26325962.1646-66&rft.date=2006&rft_id=https://api.semanticscholar.org/CorpusID:26325962#id-name=S2CID&rft_id=info:pmid/16368544&rft_id=info:doi/10.2741/1911&rft.aulast=Calinisan&rft.aufirst=V&rft.au=Gravem, D&rft.au=Chen, RP&rft.au=Brittin, S&rft.au=Mohandas, N&rft.au=Lecomte, MC&rft.au=Gascard, P&rft_id=https://digital.library.unt.edu/ark:/67531/metadc892527/&rfr_id=info:sid/en.wikipedia.org:CLNS1A" class="Z3988">
• Buyse G, de Greef C, Raeymaekers L, Droogmans G, Nilius B, Eggermont J (1996). "The ubiquitously expressed pICln protein forms homomeric complexes in vitro". Biochem. Biophys. Res. Commun. 218 (3): 822–7. doi:10.1006/bbrc.1996.0146. PMID 8579598.822-7&rft.date=1996&rft_id=info:doi/10.1006/bbrc.1996.0146&rft_id=info:pmid/8579598&rft.aulast=Buyse&rft.aufirst=G&rft.au=de Greef, C&rft.au=Raeymaekers, L&rft.au=Droogmans, G&rft.au=Nilius, B&rft.au=Eggermont, J&rft_id=https://doi.org/10.1006%2Fbbrc.1996.0146&rfr_id=info:sid/en.wikipedia.org:CLNS1A" class="Z3988">
• Schwartz RS, Rybicki AC, Nagel RL (1997). "Molecular cloning and expression of a chloride channel-associated protein pICln in human young red blood cells: association with actin". Biochem. J. 327 (2): 609–16. doi:10.1042/bj3270609. PMC 1218836. PMID 9386336.609-16&rft.date=1997&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1218836#id-name=PMC&rft_id=info:pmid/9386336&rft_id=info:doi/10.1042/bj3270609&rft.aulast=Schwartz&rft.aufirst=RS&rft.au=Rybicki, AC&rft.au=Nagel, RL&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1218836&rfr_id=info:sid/en.wikipedia.org:CLNS1A" class="Z3988">
• Bekri S, Adélaïde J, Merscher S, Grosgeorge J, Caroli-Bosc F, Perucca-Lostanlen D, Kelley PM, Pébusque MJ, Theillet C, Birnbaum D, Gaudray P (1998). "Detailed map of a region commonly amplified at 11q13→q14 in human breast carcinoma". Cytogenet. Cell Genet. 79 (1–2): 125–31. doi:10.1159/000134699. PMID 9533029.1–2&rft.pages=125-31&rft.date=1998&rft_id=info:doi/10.1159/000134699&rft_id=info:pmid/9533029&rft.aulast=Bekri&rft.aufirst=S&rft.au=Adélaïde, J&rft.au=Merscher, S&rft.au=Grosgeorge, J&rft.au=Caroli-Bosc, F&rft.au=Perucca-Lostanlen, D&rft.au=Kelley, PM&rft.au=Pébusque, MJ&rft.au=Theillet, C&rft.au=Birnbaum, D&rft.au=Gaudray, P&rfr_id=info:sid/en.wikipedia.org:CLNS1A" class="Z3988">
• Krapivinsky G, Pu W, Wickman K, Krapivinsky L, Clapham DE (1998). "pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology". J. Biol. Chem. 273 (18): 10811–4. doi:10.1074/jbc.273.18.10811. PMID 9556550.10811-4&rft.date=1998&rft_id=info:doi/10.1074/jbc.273.18.10811&rft_id=info:pmid/9556550&rft.aulast=Krapivinsky&rft.aufirst=G&rft.au=Pu, W&rft.au=Wickman, K&rft.au=Krapivinsky, L&rft.au=Clapham, DE&rft_id=https://doi.org/10.1074%2Fjbc.273.18.10811&rfr_id=info:sid/en.wikipedia.org:CLNS1A" class="Z3988">
• Tang CJ, Tang TK (1998). "The 30-kD domain of protein 4.1 mediates its binding to the carboxyl terminus of pICln, a protein involved in cellular volume regulation". Blood. 92 (4): 1442–7. doi:10.1182/blood.V92.4.1442. PMID 9694734.1442-7&rft.date=1998&rft_id=info:doi/10.1182/blood.V92.4.1442&rft_id=info:pmid/9694734&rft.aulast=Tang&rft.aufirst=CJ&rft.au=Tang, TK&rfr_id=info:sid/en.wikipedia.org:CLNS1A" class="Z3988">
• Pu WT, Krapivinsky GB, Krapivinsky L, Clapham DE (1999). "pICln inhibits snRNP biogenesis by binding core spliceosomal proteins". Mol. Cell. Biol. 19 (6): 4113–20. doi:10.1128/MCB.19.6.4113. PMC 104370. PMID 10330151.4113-20&rft.date=1999&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC104370#id-name=PMC&rft_id=info:pmid/10330151&rft_id=info:doi/10.1128/MCB.19.6.4113&rft.aulast=Pu&rft.aufirst=WT&rft.au=Krapivinsky, GB&rft.au=Krapivinsky, L&rft.au=Clapham, DE&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC104370&rfr_id=info:sid/en.wikipedia.org:CLNS1A" class="Z3988">
• Hubert MD, Levitan I, Hoffman MM, Zraggen M, Hofreiter ME, Garber SS (2000). "Modulation of volume regulated anion current by I(Cln)". Biochim. Biophys. Acta. 1466 (1–2): 105–14. doi:10.1016/S0005-2736(00)00177-2. PMID 10825435.1–2&rft.pages=105-14&rft.date=2000&rft_id=info:doi/10.1016/S0005-2736(00)00177-2&rft_id=info:pmid/10825435&rft.aulast=Hubert&rft.aufirst=MD&rft.au=Levitan, I&rft.au=Hoffman, MM&rft.au=Zraggen, M&rft.au=Hofreiter, ME&rft.au=Garber, SS&rft_id=https://doi.org/10.1016%2FS0005-2736%2800%2900177-2&rfr_id=info:sid/en.wikipedia.org:CLNS1A" class="Z3988">
• Friesen WJ, Paushkin S, Wyce A, Massenet S, Pesiridis GS, Van Duyne G, Rappsilber J, Mann M, Dreyfuss G (2001). "The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins". Mol. Cell. Biol. 21 (24): 8289–300. doi:10.1128/MCB.21.24.8289-8300.2001. PMC 99994. PMID 11713266.8289-300&rft.date=2001&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC99994#id-name=PMC&rft_id=info:pmid/11713266&rft_id=info:doi/10.1128/MCB.21.24.8289-8300.2001&rft.aulast=Friesen&rft.aufirst=WJ&rft.au=Paushkin, S&rft.au=Wyce, A&rft.au=Massenet, S&rft.au=Pesiridis, GS&rft.au=Van Duyne, G&rft.au=Rappsilber, J&rft.au=Mann, M&rft.au=Dreyfuss, G&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC99994&rfr_id=info:sid/en.wikipedia.org:CLNS1A" class="Z3988">
• Meister G, Eggert C, Bühler D, Brahms H, Kambach C, Fischer U (2002). "Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln". Curr. Biol. 11 (24): 1990–4. doi:10.1016/S0960-9822(01)00592-9. hdl:11858/00-001M-0000-0012-F501-7. PMID 11747828. S2CID 14742376.1990-4&rft.date=2002&rft_id=info:hdl/11858/00-001M-0000-0012-F501-7&rft_id=https://api.semanticscholar.org/CorpusID:14742376#id-name=S2CID&rft_id=info:pmid/11747828&rft_id=info:doi/10.1016/S0960-9822(01)00592-9&rft.aulast=Meister&rft.aufirst=G&rft.au=Eggert, C&rft.au=Bühler, D&rft.au=Brahms, H&rft.au=Kambach, C&rft.au=Fischer, U&rfr_id=info:sid/en.wikipedia.org:CLNS1A" class="Z3988">
• Friesen WJ, Wyce A, Paushkin S, Abel L, Rappsilber J, Mann M, Dreyfuss G (2002). "A novel WD repeat protein component of the methylosome binds Sm proteins". J. Biol. Chem. 277 (10): 8243–7. doi:10.1074/jbc.M109984200. PMID 11756452.8243-7&rft.date=2002&rft_id=info:doi/10.1074/jbc.M109984200&rft_id=info:pmid/11756452&rft.aulast=Friesen&rft.aufirst=WJ&rft.au=Wyce, A&rft.au=Paushkin, S&rft.au=Abel, L&rft.au=Rappsilber, J&rft.au=Mann, M&rft.au=Dreyfuss, G&rft_id=https://doi.org/10.1074%2Fjbc.M109984200&rfr_id=info:sid/en.wikipedia.org:CLNS1A" class="Z3988">
• Meyer G, Rodighiero S, Guizzardi F, Bazzini C, Bottà G, Bertocchi C, Garavaglia L, Dossena S, Manfredi R, Sironi C, Catania A, Paulmichl M (2004). "Volume-regulated Cl⁻ channels in human pleural mesothelioma cells". FEBS Lett. 559 (1–3): 45–50. Bibcode:2004FEBSL.559...45M. doi:10.1016/S0014-5793(04)00020-1. PMID 14960305. S2CID 24747269.1–3&rft.pages=45-50&rft.date=2004&rft_id=info:doi/10.1016/S0014-5793(04)50020-1&rft_id=https://api.semanticscholar.org/CorpusID:24747269#id-name=S2CID&rft_id=info:pmid/14960305&rft_id=info:bibcode/2004FEBSL.559...45M&rft.aulast=Meyer&rft.aufirst=G&rft.au=Rodighiero, S&rft.au=Guizzardi, F&rft.au=Bazzini, C&rft.au=Bottà, G&rft.au=Bertocchi, C&rft.au=Garavaglia, L&rft.au=Dossena, S&rft.au=Manfredi, R&rft.au=Sironi, C&rft.au=Catania, A&rft.au=Paulmichl, M&rfr_id=info:sid/en.wikipedia.org:CLNS1A" class="Z3988">
• Larkin D, Murphy D, Reilly DF, Cahill M, Sattler E, Harriott P, Cahill DJ, Moran N (2004). "ICln, a novel integrin alphaIIbbeta3-associated protein, functionally regulates platelet activation". J. Biol. Chem. 279 (26): 27286–93. doi:10.1074/jbc.M402159200. PMID 15075326.27286-93&rft.date=2004&rft_id=info:doi/10.1074/jbc.M402159200&rft_id=info:pmid/15075326&rft.aulast=Larkin&rft.aufirst=D&rft.au=Murphy, D&rft.au=Reilly, DF&rft.au=Cahill, M&rft.au=Sattler, E&rft.au=Harriott, P&rft.au=Cahill, DJ&rft.au=Moran, N&rft_id=https://doi.org/10.1074%2Fjbc.M402159200&rfr_id=info:sid/en.wikipedia.org:CLNS1A" class="Z3988">
• Fürst J, Schedlbauer A, Gandini R, Garavaglia ML, Saino S, Gschwentner M, Sarg B, Lindner H, Jakab M, Ritter M, Bazzini C, Botta G, Meyer G, Kontaxis G, Tilly BC, Konrat R, Paulmichl M (2005). "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4". J. Biol. Chem. 280 (35): 31276–82. doi:10.1074/jbc.M500541200. PMID 15905169.31276-82&rft.date=2005&rft_id=info:doi/10.1074/jbc.M500541200&rft_id=info:pmid/15905169&rft.aulast=Fürst&rft.aufirst=J&rft.au=Schedlbauer, A&rft.au=Gandini, R&rft.au=Garavaglia, ML&rft.au=Saino, S&rft.au=Gschwentner, M&rft.au=Sarg, B&rft.au=Lindner, H&rft.au=Jakab, M&rft.au=Ritter, M&rft.au=Bazzini, C&rft.au=Botta, G&rft.au=Meyer, G&rft.au=Kontaxis, G&rft.au=Tilly, BC&rft.au=Konrat, R&rft.au=Paulmichl, M&rft_id=https://doi.org/10.1074%2Fjbc.M500541200&rfr_id=info:sid/en.wikipedia.org:CLNS1A" class="Z3988">
• Azzouz TN, Pillai RS, Däpp C, Chari A, Meister G, Kambach C, Fischer U, Schümperli D (2005). "Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes". J. Biol. Chem. 280 (41): 34435–40. doi:10.1074/jbc.M505077200. hdl:21.11116/0000-0007-E5F1-6. PMID 16087681.34435-40&rft.date=2005&rft_id=info:hdl/21.11116/0000-0007-E5F1-6&rft_id=info:pmid/16087681&rft_id=info:doi/10.1074/jbc.M505077200&rft.aulast=Azzouz&rft.aufirst=TN&rft.au=Pillai, RS&rft.au=Däpp, C&rft.au=Chari, A&rft.au=Meister, G&rft.au=Kambach, C&rft.au=Fischer, U&rft.au=Schümperli, D&rft_id=https://doi.org/10.1074%2Fjbc.M505077200&rfr_id=info:sid/en.wikipedia.org:CLNS1A" class="Z3988">

External links

• CLNS1A protein, human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• Human CLNS1A genome location and CLNS1A gene details page in the UCSC Genome Browser.

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