| |
|---|---|
| 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 | |
External Searches:
|
|
Analyze:
| Predict TMSs (Predict number of transmembrane segments) | ||||
| 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