Details for: MCOLN1

Gene ID: 57192

Symbol: MCOLN1

Ensembl ID: ENSG00000090674

Description: mucolipin TRP cation channel 1

Associated with

Other Information

Genular Protein ID: 3723265550

Symbol: MCLN1_HUMAN

Name: MG-2

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11013137

Title: Cloning of the gene encoding a novel integral membrane protein, mucolipidin, and identification of the two major founder mutations causing mucolipidosis type IV.

PubMed ID: 11013137

DOI: 10.1016/s0002-9297(07)62941-3

PubMed ID: 11030752

Title: Mucolipidosis type IV is caused by mutations in a gene encoding a novel transient receptor potential channel.

PubMed ID: 11030752

DOI: 10.1093/hmg/9.17.2471

PubMed ID: 10973263

Title: Identification of the gene causing mucolipidosis type IV.

PubMed ID: 10973263

DOI: 10.1038/79095

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: 12459486

Title: Identification and characterization of the single channel function of human mucolipin-1 implicated in mucolipidosis type IV, a disorder affecting the lysosomal pathway.

PubMed ID: 12459486

DOI: 10.1016/s0014-5793(02)03670-0

PubMed ID: 15336987

Title: Functional links between mucolipin-1 and Ca2+-dependent membrane trafficking in mucolipidosis IV.

PubMed ID: 15336987

DOI: 10.1016/j.bbrc.2004.08.045

PubMed ID: 15178326

Title: Overexpression of wild-type and mutant mucolipin proteins in mammalian cells: effects on the late endocytic compartment organization.

PubMed ID: 15178326

DOI: 10.1016/j.febslet.2004.04.080

PubMed ID: 14749347

Title: Molecular pathophysiology of mucolipidosis type IV: pH dysregulation of the mucolipin-1 cation channel.

PubMed ID: 14749347

DOI: 10.1093/hmg/ddh067

PubMed ID: 16257972

Title: TRP-ML1 is a lysosomal monovalent cation channel that undergoes proteolytic cleavage.

PubMed ID: 16257972

DOI: 10.1074/jbc.m508210200

PubMed ID: 16497227

Title: Two di-leucine motifs regulate trafficking of mucolipin-1 to lysosomes.

PubMed ID: 16497227

DOI: 10.1111/j.1600-0854.2006.00387.x

PubMed ID: 16978393

Title: Mucolipin-1 is a lysosomal membrane protein required for intracellular lactosylceramide traffic.

PubMed ID: 16978393

DOI: 10.1111/j.1600-0854.2006.00475.x

PubMed ID: 17897319

Title: Integral and associated lysosomal membrane proteins.

PubMed ID: 17897319

DOI: 10.1111/j.1600-0854.2007.00643.x

PubMed ID: 17988215

Title: Mucolipin 1 channel activity is regulated by protein kinase A-mediated phosphorylation.

PubMed ID: 17988215

DOI: 10.1042/bj20070713

PubMed ID: 18794901

Title: The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel.

PubMed ID: 18794901

DOI: 10.1038/nature07311

PubMed ID: 19864416

Title: Identification of the penta-EF-hand protein ALG-2 as a Ca2+-dependent interactor of mucolipin-1.

PubMed ID: 19864416

DOI: 10.1074/jbc.m109.047241

PubMed ID: 19159218

Title: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.

PubMed ID: 19159218

DOI: 10.1021/pr8008012

PubMed ID: 19885840

Title: Functional multimerization of mucolipin channel proteins.

PubMed ID: 19885840

DOI: 10.1002/jcp.21956

PubMed ID: 21256127

Title: The cation channel mucolipin-1 is a bifunctional protein that facilitates membrane remodeling via its serine lipase domain.

PubMed ID: 21256127

DOI: 10.1016/j.yexcr.2011.01.008

PubMed ID: 21224396

Title: LAPTMs regulate lysosomal function and interact with mucolipin 1: new clues for understanding mucolipidosis type IV.

PubMed ID: 21224396

DOI: 10.1242/jcs.076240

PubMed ID: 22733759

Title: Phosphoinositide isoforms determine compartment-specific ion channel activity.

PubMed ID: 22733759

DOI: 10.1073/pnas.1202194109

PubMed ID: 25130899

Title: Cellular zinc levels are modulated by TRPML1-TMEM163 interaction.

PubMed ID: 25130899

DOI: 10.1111/tra.12205

PubMed ID: 25720963

Title: Lysosomal calcium signalling regulates autophagy through calcineurin and TFEB.

PubMed ID: 25720963

DOI: 10.1038/ncb3114

PubMed ID: 25733853

Title: Up-regulation of lysosomal TRPML1 channels is essential for lysosomal adaptation to nutrient starvation.

PubMed ID: 25733853

DOI: 10.1073/pnas.1419669112

PubMed ID: 27623384

Title: PIKfyve Regulates Vacuole Maturation and Nutrient Recovery following Engulfment.

PubMed ID: 27623384

DOI: 10.1016/j.devcel.2016.08.001

PubMed ID: 27787197

Title: Regulation of mTORC1 by lysosomal calcium and calmodulin.

PubMed ID: 27787197

DOI: 10.7554/elife.19360

PubMed ID: 27357649

Title: MCOLN1 is a ROS sensor in lysosomes that regulates autophagy.

PubMed ID: 27357649

DOI: 10.1038/ncomms12109

PubMed ID: 28112729

Title: Structural basis of dual Ca(2+)/pH regulation of the endolysosomal TRPML1 channel.

PubMed ID: 28112729

DOI: 10.1038/nsmb.3362

PubMed ID: 29019983

Title: Human TRPML1 channel structures in open and closed conformations.

PubMed ID: 29019983

DOI: 10.1038/nature24036

PubMed ID: 11317355

Title: Mucolipidosis type IV: novel MCOLN1 mutations in Jewish and non-Jewish patients and the frequency of the disease in the Ashkenazi Jewish population.

PubMed ID: 11317355

DOI: 10.1002/humu.1115

PubMed ID: 12182165

Title: The neurogenetics of mucolipidosis type IV.

PubMed ID: 12182165

DOI: 10.1212/wnl.59.3.306

PubMed ID: 15523648

Title: Transfer of a mitochondrial DNA fragment to MCOLN1 causes an inherited case of mucolipidosis IV.

PubMed ID: 15523648

DOI: 10.1002/humu.20094

PubMed ID: 16959974

Title: The consensus coding sequences of human breast and colorectal cancers.

PubMed ID: 16959974

DOI: 10.1126/science.1133427

Sequence Information:

  • Length: 580
  • Mass: 65022
  • Checksum: 7E7691F58D01C804
  • Sequence:
  • MTAPAGPRGS ETERLLTPNP GYGTQAGPSP APPTPPEEED LRRRLKYFFM SPCDKFRAKG 
    RKPCKLMLQV VKILVVTVQL ILFGLSNQLA VTFREENTIA FRHLFLLGYS DGADDTFAAY 
    TREQLYQAIF HAVDQYLALP DVSLGRYAYV RGGGDPWTNG SGLALCQRYY HRGHVDPAND 
    TFDIDPMVVT DCIQVDPPER PPPPPSDDLT LLESSSSYKN LTLKFHKLVN VTIHFRLKTI 
    NLQSLINNEI PDCYTFSVLI TFDNKAHSGR IPISLETQAH IQECKHPSVF QHGDNSFRLL 
    FDVVVILTCS LSFLLCARSL LRGFLLQNEF VGFMWRQRGR VISLWERLEF VNGWYILLVT 
    SDVLTISGTI MKIGIEAKNL ASYDVCSILL GTSTLLVWVG VIRYLTFFHN YNILIATLRV 
    ALPSVMRFCC CVAVIYLGYC FCGWIVLGPY HVKFRSLSMV SECLFSLING DDMFVTFAAM 
    QAQQGRSSLV WLFSQLYLYS FISLFIYMVL SLFIALITGA YDTIKHPGGA GAEESELQAY 
    IAQCQDSPTS GKFRRGSGSA CSLLCCCGRD PSEEHSLLVN

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.