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Q9GZU1

- MCLN1_HUMAN

UniProt

Q9GZU1 - MCLN1_HUMAN

Protein

Mucolipin-1

Gene

MCOLN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Cation channel probably playing a role in the endocytic pathway and in the control of membrane trafficking of proteins and lipids. Could play a major role in Ca2+ transport regulating lysosomal exocytosis.2 Publications

    Enzyme regulationi

    Channel function is transiently modulated by changes in Ca2+, and inhibited by a reduction of pH; pH changes modify the aggregation state of unitary channels.

    GO - Molecular functioni

    1. cation channel activity Source: UniProtKB
    2. NAADP-sensitive calcium-release channel activity Source: Ensembl

    GO - Biological processi

    1. calcium ion transmembrane transport Source: Reactome
    2. cation transport Source: UniProtKB
    3. cellular iron ion homeostasis Source: Reactome
    4. ion transmembrane transport Source: Reactome
    5. release of sequestered calcium ion into cytosol Source: Ensembl
    6. transferrin transport Source: Reactome
    7. transmembrane transport Source: Reactome

    Keywords - Molecular functioni

    Ion channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_169333. TRP channels.
    REACT_25283. Transferrin endocytosis and recycling.

    Protein family/group databases

    TCDBi1.A.5.3.1. the polycystin cation channel (pcc) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mucolipin-1
    Alternative name(s):
    MG-2
    Mucolipidin
    Gene namesi
    Name:MCOLN1
    Synonyms:ML4
    ORF Names:MSTP080
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:13356. MCOLN1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. endosome membrane Source: Reactome
    3. integral component of membrane Source: UniProtKB
    4. integral component of plasma membrane Source: UniProtKB
    5. late endosome membrane Source: UniProtKB-SubCell
    6. lysosomal membrane Source: UniProtKB
    7. plasma membrane Source: HPA
    8. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Endosome, Lysosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Mucolipidosis type IV (MLIV) [MIM:252650]: Autosomal recessive lysosomal storage disorder characterized by severe psychomotor retardation and ophthalmologic abnormalities, including corneal opacity, retinal degeneration and strabismus. Storage bodies of lipids and water-soluble substances are seen by electron microscopy in almost every cell type of the patients. Most patients are unable to speak or walk independently and reach a maximal developmental level of 1-2 years. All patients have constitutive achlorhydia associated with a secondary elevation of serum gastrin levels. MLIV may be due to a defect in sorting and/or transport along the late endocytic pathway. MLIV is found at relatively high frequency among Ashkenazi Jews.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061L → P in MLIV. 1 Publication
    VAR_019369
    Natural varianti232 – 2321T → P in MLIV; fails to localize to late endosomes. 1 Publication
    VAR_019370
    Natural varianti362 – 3621D → Y in MLIV; affects channel activity. 2 Publications
    VAR_019371
    Natural varianti403 – 4031R → C in MLIV. 1 Publication
    VAR_038380
    Natural varianti408 – 4081Missing in MLIV; mild psychomotor involvement; does not affect channel activity; affects channel inhibition by low pH; still localizes to late endosomes. 3 Publications
    VAR_019372
    Natural varianti446 – 4461V → L in MLIV; does not affect channel activity; affects channel inhibition by low pH. 1 Publication
    VAR_019373
    Natural varianti447 – 4471L → P in MLIV. 1 Publication
    VAR_019374
    Natural varianti465 – 4651F → L in MLIV; still localizes to late endosomes. 1 Publication
    VAR_019375

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 463RLK → AAA: Abolishes interaction with PDCD6 and decreases formation of aberrant endosomes upon overexpression. 1 Publication
    Mutagenesisi44 – 441R → A: Abolishes interaction with PDCD6. 1 Publication
    Mutagenesisi45 – 451L → A: Abolishes interaction with PDCD6. 1 Publication
    Mutagenesisi47 – 493YFF → AAA: Abolishes interaction with PDCD6.

    Keywords - Diseasei

    Disease mutation, Mucolipidosis

    Organism-specific databases

    MIMi252650. phenotype.
    Orphaneti578. Mucolipidosis type 4.
    PharmGKBiPA30699.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 580580Mucolipin-1PRO_0000215362Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei10 – 101PhosphoserineBy similarity
    Glycosylationi230 – 2301N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9GZU1.
    PaxDbiQ9GZU1.
    PRIDEiQ9GZU1.

    PTM databases

    PhosphoSiteiQ9GZU1.

    Expressioni

    Tissue specificityi

    Widely expressed in adult and fetal tissues.3 Publications

    Gene expression databases

    ArrayExpressiQ9GZU1.
    BgeeiQ9GZU1.
    CleanExiHS_MCOLN1.
    GenevestigatoriQ9GZU1.

    Organism-specific databases

    HPAiHPA031763.

    Interactioni

    Subunit structurei

    Forms multimeric complexes. Interacts with PDCD6.2 Publications

    Protein-protein interaction databases

    BioGridi121441. 2 interactions.
    IntActiQ9GZU1. 2 interactions.
    MINTiMINT-1409368.
    STRINGi9606.ENSP00000264079.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9GZU1.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei66 – 8621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei297 – 31721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei350 – 37021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei388 – 40821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei428 – 44821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei497 – 51721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG149591.
    HOGENOMiHOG000232158.
    HOVERGENiHBG052430.
    InParanoidiQ9GZU1.
    KOiK04992.
    OMAiAIFHAVD.
    OrthoDBiEOG7V1FQ9.
    PhylomeDBiQ9GZU1.
    TreeFamiTF317783.

    Family and domain databases

    InterProiIPR013122. PKD1_2_channel.
    [Graphical view]
    PfamiPF08016. PKD_channel. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9GZU1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTAPAGPRGS ETERLLTPNP GYGTQAGPSP APPTPPEEED LRRRLKYFFM    50
    SPCDKFRAKG RKPCKLMLQV VKILVVTVQL ILFGLSNQLA VTFREENTIA 100
    FRHLFLLGYS DGADDTFAAY TREQLYQAIF HAVDQYLALP DVSLGRYAYV 150
    RGGGDPWTNG SGLALCQRYY HRGHVDPAND TFDIDPMVVT DCIQVDPPER 200
    PPPPPSDDLT LLESSSSYKN LTLKFHKLVN VTIHFRLKTI NLQSLINNEI 250
    PDCYTFSVLI TFDNKAHSGR IPISLETQAH IQECKHPSVF QHGDNSFRLL 300
    FDVVVILTCS LSFLLCARSL LRGFLLQNEF VGFMWRQRGR VISLWERLEF 350
    VNGWYILLVT SDVLTISGTI MKIGIEAKNL ASYDVCSILL GTSTLLVWVG 400
    VIRYLTFFHN YNILIATLRV ALPSVMRFCC CVAVIYLGYC FCGWIVLGPY 450
    HVKFRSLSMV SECLFSLING DDMFVTFAAM QAQQGRSSLV WLFSQLYLYS 500
    FISLFIYMVL SLFIALITGA YDTIKHPGGA GAEESELQAY IAQCQDSPTS 550
    GKFRRGSGSA CSLLCCCGRD PSEEHSLLVN 580
    Length:580
    Mass (Da):65,022
    Last modified:March 1, 2001 - v1
    Checksum:i7E7691F58D01C804
    GO

    Sequence cautioni

    The sequence CAC07813.1 differs from that shown. Reason: Probable cloning artifact.
    The sequence AAQ13604.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence EAW69031.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence EAW69034.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti164 – 19128ALCQR…MVVTD → LSASGTTTEATWTRPTTHLT LIRWWLLVN in AAG42242. (PubMed:10973263)CuratedAdd
    BLAST
    Sequence conflicti203 – 2031P → S in CAC08215. (PubMed:11013137)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061L → P in MLIV. 1 Publication
    VAR_019369
    Natural varianti232 – 2321T → P in MLIV; fails to localize to late endosomes. 1 Publication
    VAR_019370
    Natural varianti331 – 3311V → L in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036453
    Natural varianti362 – 3621D → Y in MLIV; affects channel activity. 2 Publications
    VAR_019371
    Natural varianti403 – 4031R → C in MLIV. 1 Publication
    VAR_038380
    Natural varianti408 – 4081Missing in MLIV; mild psychomotor involvement; does not affect channel activity; affects channel inhibition by low pH; still localizes to late endosomes. 3 Publications
    VAR_019372
    Natural varianti446 – 4461V → L in MLIV; does not affect channel activity; affects channel inhibition by low pH. 1 Publication
    VAR_019373
    Natural varianti447 – 4471L → P in MLIV. 1 Publication
    VAR_019374
    Natural varianti465 – 4651F → L in MLIV; still localizes to late endosomes. 1 Publication
    VAR_019375

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ293659 mRNA. Translation: CAC07813.1. Sequence problems.
    AJ293970 mRNA. Translation: CAC08215.1.
    AF287269 mRNA. Translation: AAG00797.1.
    AF287270 Genomic DNA. Translation: AAG00798.1.
    AF249319 mRNA. Translation: AAG10422.1.
    AF305579
    , AF305572, AF305573, AF305574, AF305575, AF305576, AF305577, AF305578 Genomic DNA. Translation: AAG42242.1.
    AK026102 mRNA. Translation: BAB15360.1.
    CH471139 Genomic DNA. Translation: EAW69031.1. Sequence problems.
    CH471139 Genomic DNA. Translation: EAW69034.1. Sequence problems.
    BC005149 mRNA. Translation: AAH05149.1.
    AF171088 mRNA. Translation: AAQ13604.1. Different initiation.
    CCDSiCCDS12180.1.
    RefSeqiNP_065394.1. NM_020533.2.
    UniGeneiHs.631858.

    Genome annotation databases

    EnsembliENST00000264079; ENSP00000264079; ENSG00000090674.
    GeneIDi57192.
    KEGGihsa:57192.
    UCSCiuc002mgo.3. human.

    Polymorphism databases

    DMDMi50401163.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ293659 mRNA. Translation: CAC07813.1 . Sequence problems.
    AJ293970 mRNA. Translation: CAC08215.1 .
    AF287269 mRNA. Translation: AAG00797.1 .
    AF287270 Genomic DNA. Translation: AAG00798.1 .
    AF249319 mRNA. Translation: AAG10422.1 .
    AF305579
    , AF305572 , AF305573 , AF305574 , AF305575 , AF305576 , AF305577 , AF305578 Genomic DNA. Translation: AAG42242.1 .
    AK026102 mRNA. Translation: BAB15360.1 .
    CH471139 Genomic DNA. Translation: EAW69031.1 . Sequence problems.
    CH471139 Genomic DNA. Translation: EAW69034.1 . Sequence problems.
    BC005149 mRNA. Translation: AAH05149.1 .
    AF171088 mRNA. Translation: AAQ13604.1 . Different initiation.
    CCDSi CCDS12180.1.
    RefSeqi NP_065394.1. NM_020533.2.
    UniGenei Hs.631858.

    3D structure databases

    ProteinModelPortali Q9GZU1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121441. 2 interactions.
    IntActi Q9GZU1. 2 interactions.
    MINTi MINT-1409368.
    STRINGi 9606.ENSP00000264079.

    Chemistry

    GuidetoPHARMACOLOGYi 501.

    Protein family/group databases

    TCDBi 1.A.5.3.1. the polycystin cation channel (pcc) family.

    PTM databases

    PhosphoSitei Q9GZU1.

    Polymorphism databases

    DMDMi 50401163.

    Proteomic databases

    MaxQBi Q9GZU1.
    PaxDbi Q9GZU1.
    PRIDEi Q9GZU1.

    Protocols and materials databases

    DNASUi 57192.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264079 ; ENSP00000264079 ; ENSG00000090674 .
    GeneIDi 57192.
    KEGGi hsa:57192.
    UCSCi uc002mgo.3. human.

    Organism-specific databases

    CTDi 57192.
    GeneCardsi GC19P007587.
    GeneReviewsi MCOLN1.
    H-InvDB HIX0023287.
    HGNCi HGNC:13356. MCOLN1.
    HPAi HPA031763.
    MIMi 252650. phenotype.
    605248. gene.
    neXtProti NX_Q9GZU1.
    Orphaneti 578. Mucolipidosis type 4.
    PharmGKBi PA30699.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG149591.
    HOGENOMi HOG000232158.
    HOVERGENi HBG052430.
    InParanoidi Q9GZU1.
    KOi K04992.
    OMAi AIFHAVD.
    OrthoDBi EOG7V1FQ9.
    PhylomeDBi Q9GZU1.
    TreeFami TF317783.

    Enzyme and pathway databases

    Reactomei REACT_169333. TRP channels.
    REACT_25283. Transferrin endocytosis and recycling.

    Miscellaneous databases

    GeneWikii MCOLN1.
    GenomeRNAii 57192.
    NextBioi 63278.
    PROi Q9GZU1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9GZU1.
    Bgeei Q9GZU1.
    CleanExi HS_MCOLN1.
    Genevestigatori Q9GZU1.

    Family and domain databases

    InterProi IPR013122. PKD1_2_channel.
    [Graphical view ]
    Pfami PF08016. PKD_channel. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the gene encoding a novel integral membrane protein, mucolipidin, and identification of the two major founder mutations causing mucolipidosis type IV."
      Bassi M.T., Manzoni M., Monti E., Pizzo M.T., Ballabio A., Borsani G.
      Am. J. Hum. Genet. 67:1110-1120(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROBABLE FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INVOLVEMENT IN MUCOLIPIDOSIS IV.
    2. "Mucolipidosis type IV is caused by mutations in a gene encoding a novel transient receptor potential channel."
      Sun M., Goldin E., Stahl S., Falardeau J.L., Kennedy J.C., Acierno J.S. Jr., Bove C., Kaneski C.R., Nagle J., Bromley M.C., Colman M., Schiffmann R., Slaugenhaupt S.A.
      Hum. Mol. Genet. 9:2471-2478(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, VARIANTS MLIV TYR-362; PHE-408 DEL AND LEU-446.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INVOLVEMENT IN MUCOLIPIDOSIS IV.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 391-580.
      Tissue: Aorta.
    8. "Identification and characterization of the single channel function of human mucolipin-1 implicated in mucolipidosis type IV, a disorder affecting the lysosomal pathway."
      LaPlante J.M., Falardeau J., Sun M., Kanazirska M., Brown E.M., Slaugenhaupt S.A., Vassilev P.M.
      FEBS Lett. 532:183-187(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTIONAL CHARACTERIZATION, REGULATION BY CALCIUM, SUBCELLULAR LOCATION.
    9. "Overexpression of wild-type and mutant mucolipin proteins in mammalian cells: effects on the late endocytic compartment organization."
      Manzoni M., Monti E., Bresciani R., Bozzato A., Barlati S., Bassi M.T., Borsani G.
      FEBS Lett. 567:219-224(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS MLIV PRO-232; PHE-408 DEL AND LEU-465.
    10. "Molecular pathophysiology of mucolipidosis type IV: pH dysregulation of the mucolipin-1 cation channel."
      Raychowdhury M.K., Gonzalez-Perrett S., Montalbetti N., Timpanaro G.A., Chasan B., Goldmann W.H., Stahl S., Cooney A., Goldin E., Cantiello H.F.
      Hum. Mol. Genet. 13:617-627(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTIONAL CHARACTERIZATION, SUBUNIT, CHARACTERIZATION OF VARIANTS MLIV TYR-362; PHE-408 DEL AND LEU-446.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Placenta.
    12. "Identification of the penta-EF-hand protein ALG-2 as a Ca2+-dependent interactor of mucolipin-1."
      Vergarajauregui S., Martina J.A., Puertollano R.
      J. Biol. Chem. 284:36357-36366(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDCD6, MUTAGENESIS OF ARG-44; LEU-45; 44-ARG--LYS-46 AND 47-TYR--PHE-49.
    13. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-230.
      Tissue: Liver.
    14. "Mucolipidosis type IV: novel MCOLN1 mutations in Jewish and non-Jewish patients and the frequency of the disease in the Ashkenazi Jewish population."
      Bargal R., Avidan N., Olender Z., Ben-Asher E., Zeigler M., Raas-Rothschild A., Frumkin A., Ben-Yoseph O., Friedlender Y., Lancet D., Bach G.
      Hum. Mutat. 17:397-402(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MLIV PRO-232; PHE-408 DEL AND LEU-465.
    15. Cited for: VARIANTS MLIV PRO-106; TYR-362; PHE-408 DEL AND PRO-447.
    16. "Transfer of a mitochondrial DNA fragment to MCOLN1 causes an inherited case of mucolipidosis IV."
      Goldin E., Stahl S., Cooney A.M., Kaneski C.R., Gupta S., Brady R.O., Ellis J.R., Schiffmann R.
      Hum. Mutat. 24:460-465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MLIV CYS-403.
    17. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-331.

    Entry informationi

    Entry nameiMCLN1_HUMAN
    AccessioniPrimary (citable) accession number: Q9GZU1
    Secondary accession number(s): D6W647
    , Q7Z4F7, Q9H292, Q9H4B3, Q9H4B5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3