Details for: CLNS1A

Gene ID: 1207

Symbol: CLNS1A

Ensembl ID: ENSG00000074201

Description: chloride nucleotide-sensitive channel 1A

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

DOI: 10.1006/bbrc.1996.0146

PubMed ID: 7887970

Title: Molecular cloning of the human volume-sensitive chloride conductance regulatory protein, pICln, from ocular ciliary epithelium.

PubMed ID: 7887970

DOI: 10.1006/bbrc.1995.1309

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

DOI: 10.1016/s0005-2736(00)00177-2

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

DOI: 10.1128/mcb.19.6.4113

PubMed ID: 11747828

Title: Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln.

PubMed ID: 11747828

DOI: 10.1016/s0960-9822(01)00592-9

PubMed ID: 11713266

Title: The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins.

PubMed ID: 11713266

DOI: 10.1128/mcb.21.24.8289-8300.2001

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

DOI: 10.1074/jbc.m505077200

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

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

DOI: 10.1002/elps.200600782

PubMed ID: 17525332

Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

PubMed ID: 17525332

DOI: 10.1126/science.1140321

PubMed ID: 18984161

Title: An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs.

PubMed ID: 18984161

DOI: 10.1016/j.cell.2008.09.020

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

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

DOI: 10.1002/pmic.200700884

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

DOI: 10.1074/mcp.m800588-mcp200

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

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

DOI: 10.1074/jbc.m110.148486

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

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

DOI: 10.1016/j.jprot.2013.11.014

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

DOI: 10.1126/science.1140321

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

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

DOI: 10.1016/j.jprot.2013.11.014

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

DOI: 10.1016/j.cell.2006.09.026

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

DOI: 10.1002/elps.200600782

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

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

DOI: 10.1002/pmic.200700884

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

DOI: 10.1074/mcp.M800588-MCP200

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

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

DOI: 10.1016/j.jprot.2013.11.014

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

DOI: 10.1126/science.1140321

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

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

DOI: 10.1016/j.jprot.2013.11.014

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.