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1.A.47.1.1
The nucleotide-sensitive ion channel, ICln

Accession Number:P54105
Protein Name:ICln aka CLNS1A
Length:237
Molecular Weight:26215.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Cytoplasm1
Substrate ions

Cross database links:

Genevestigator: P54105
eggNOG: prNOG16940
HEGENOM: HBG444799
RefSeq: NP_001284.1   
Entrez Gene ID: 1207   
OMIM: 602158  gene
KEGG: hsa:1207   

Gene Ontology

GO:0005856 C:cytoskeleton
GO:0005634 C:nucleus
GO:0005886 C:plasma membrane
GO:0005515 F:protein binding
GO:0008015 P:blood circulation
GO:0006884 P:cell volume homeostasis
GO:0006821 P:chloride transport
GO:0000387 P:spliceosomal snRNP assembly

References (20)

[1] “The ubiquitously expressed pICln protein forms homomeric complexes in vitro.”  Buyse G.et.al.   8579598
[2] “Molecular cloning of the human volume-sensitive chloride conductance regulatory protein, pICln, from ocular ciliary epithelium.”  Anquita J.et.al.   7887970
[3] “Molecular cloning and expression of a chloride channel-associated protein pI(Cln) in human young red blood cells: association with actin.”  Schwartz R.S.et.al.   9359436
[4] “Modulation of volume regulated anion current by I(Cln).”  Hubert M.D.et.al.   10825435
[5] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[6] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[7] “pICln inhibits snRNP biogenesis by binding core spliceosomal proteins.”  Pu W.T.et.al.   10330151
[8] “The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins.”  Friesen W.J.et.al.   11713266
[9] “Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes.”  Azzouz T.N.et.al.   16087681
[10] “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.”  Olsen J.V.et.al.   17081983
[11] “Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.”  Giorgianni F.et.al.   17487921
[12] “Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.”  Molina H.et.al.   17287340
[13] “ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.”  Matsuoka S.et.al.   17525332
[14] “Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.”  Carrascal M.et.al.   19367720
[15] “Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.”  Daub H.et.al.   18691976
[16] “A quantitative atlas of mitotic phosphorylation.”  Dephoure N.et.al.   18669648
[17] “Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.”  Han G.et.al.   18318008
[18] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[19] “Large-scale proteomics analysis of the human kinome.”  Oppermann F.S.et.al.   19369195
[20] “Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.”  Mayya V.et.al.   19690332

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FASTA formatted sequence
1:	MSFLKSFPPP GPAEGLLRQQ PDTEAVLNGK GLGTGTLYIA ESRLSWLDGS GLGFSLEYPT 
61:	ISLHALSRDR SDCLGEHLYV MVNAKFEEES KEPVADEEEE DSDDDVEPIT EFRFVPSDKS 
121:	ALEAMFTAMC ECQALHPDPE DEDSDDYDGE EYDVEAHEQG QGDIPTFYTY EEGLSHLTAE 
181:	GQATLERLEG MLSQSVSSQY NMAGVRTEDS IRDYEDGMEV DTTPTVAGQF EDADVDH