Details for: CLNS1A
Associated with
Other Information
Genular Protein ID: 2627404289
Symbol: ICLN_HUMAN
Name: Methylosome subunit pICln
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 8579598
Title: The ubiquitously expressed pICln protein forms homomeric complexes in vitro.
PubMed ID: 8579598
PubMed ID: 7887970
Title: Molecular cloning of the human volume-sensitive chloride conductance regulatory protein, pICln, from ocular ciliary epithelium.
PubMed ID: 7887970
PubMed ID: 9359436
Title: Molecular cloning and expression of a chloride channel-associated protein pI(Cln) in human young red blood cells: association with actin.
PubMed ID: 9359436
DOI: 10.1042/bj3270609
PubMed ID: 10825435
Title: Modulation of volume regulated anion current by I(Cln).
PubMed ID: 10825435
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 10330151
Title: pICln inhibits snRNP biogenesis by binding core spliceosomal proteins.
PubMed ID: 10330151
PubMed ID: 11747828
Title: Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln.
PubMed ID: 11747828
PubMed ID: 11713266
Title: The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins.
PubMed ID: 11713266
PubMed ID: 16087681
Title: Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes.
PubMed ID: 16087681
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 17487921
Title: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.
PubMed ID: 17487921
PubMed ID: 17525332
Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.
PubMed ID: 17525332
PubMed ID: 18984161
Title: An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs.
PubMed ID: 18984161
PubMed ID: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 18318008
Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.
PubMed ID: 18318008
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19369195
Title: Large-scale proteomics analysis of the human kinome.
PubMed ID: 19369195
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21081503
Title: RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity.
PubMed ID: 21081503
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
Sequence Information:
- Length: 237
- Mass: 26215
- Checksum: AE9C09884A6FF158
- Sequence:
MSFLKSFPPP GPAEGLLRQQ PDTEAVLNGK GLGTGTLYIA ESRLSWLDGS GLGFSLEYPT ISLHALSRDR SDCLGEHLYV MVNAKFEEES KEPVADEEEE DSDDDVEPIT EFRFVPSDKS ALEAMFTAMC ECQALHPDPE DEDSDDYDGE EYDVEAHEQG QGDIPTFYTY EEGLSHLTAE GQATLERLEG MLSQSVSSQY NMAGVRTEDS IRDYEDGMEV DTTPTVAGQF EDADVDH
Genular Protein ID: 2186699761
Symbol: E9PMI6_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 16554811
Title: Human chromosome 11 DNA sequence and analysis including novel gene identification.
PubMed ID: 16554811
DOI: 10.1038/nature04632
PubMed ID: 17525332
Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.
PubMed ID: 17525332
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
Sequence Information:
- Length: 167
- Mass: 18259
- Checksum: 5C7241CA193A0D6D
- Sequence:
MSFLKSFPPP GPAEGLLRQQ PDTEAVLNGK GLGTGTLYIA ESRLSWLDGS GLGFSLEYPT ISLHALSRDR SDCLGEHLYV MVNAKFEEQG QGDIPTFYTY EEGLSHLTAE GQATLERLEG MLSQSVSSQY NMAGVRTEDS IRDYEDGMEV DTTPTVAGQF EDADVDH
Genular Protein ID: 3748960313
Symbol: E9PJF4_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 16554811
Title: Human chromosome 11 DNA sequence and analysis including novel gene identification.
PubMed ID: 16554811
DOI: 10.1038/nature04632
PubMed ID: 17487921
Title: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.
PubMed ID: 17487921
PubMed ID: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 18318008
Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.
PubMed ID: 18318008
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19369195
Title: Large-scale proteomics analysis of the human kinome.
PubMed ID: 19369195
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
Sequence Information:
- Length: 179
- Mass: 19743
- Checksum: F025C0B5645CBFE1
- Sequence:
MSFLKSFPPP GPAEGLLRQQ PDTEAVLNGK GLGTGTLYIA ESRLSWLDGS GLGFSLEYPT ISLHALSRDR SDCLGEHLYV MVNAKFEEES KEPVADEEEE DSDDDVEPIT EFRFVPSDKS ALEAMFTAMC ECQALHPDPE DEDSDDYDGE EYDVEAHDGM EVDTTPTVAG QFEDADVDH
Genular Protein ID: 2671242236
Symbol: J3KN38_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 16554811
Title: Human chromosome 11 DNA sequence and analysis including novel gene identification.
PubMed ID: 16554811
DOI: 10.1038/nature04632
PubMed ID: 17525332
Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.
PubMed ID: 17525332
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
Sequence Information:
- Length: 203
- Mass: 22348
- Checksum: 4B2130D4EEFE1BF8
- Sequence:
MSFLKSFPPP GPAEGLLRQQ PDTEAVLNGK GLGTGTLYIA ESRLSWLDGS GLGFSLEYPT ISLHALSRDR SDCLGEHLYV MVNAKFEVEA MFTAMCECQA LHPDPEDEDS DDYDGEEYDV EAHEQGQGDI PTFYTYEEGL SHLTAEGQAT LERLEGMLSQ SVSSQYNMAG VRTEDSIRDY EDGMEVDTTP TVAGQFEDAD VDH
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.