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Q9GZU1

- MCLN1_HUMAN

UniProt

Q9GZU1 - MCLN1_HUMAN

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Protein
Mucolipin-1
Gene
MCOLN1, ML4, MSTP080
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.3 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. NAADP-sensitive calcium-release channel activity Source: Ensembl
  2. cation channel activity Source: UniProtKB
Complete GO annotation...

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
Complete GO annotation...

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

Cell membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein 4 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei66 – 8621Helical; Reviewed prediction
Add
BLAST
Transmembranei297 – 31721Helical; Reviewed prediction
Add
BLAST
Transmembranei350 – 37021Helical; Reviewed prediction
Add
BLAST
Transmembranei388 – 40821Helical; Reviewed prediction
Add
BLAST
Transmembranei428 – 44821Helical; Reviewed prediction
Add
BLAST
Transmembranei497 – 51721Helical; Reviewed prediction
Add
BLAST

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.6 Publications
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. 2 Publications
VAR_019370
Natural varianti362 – 3621D → Y in MLIV; affects channel activity. 3 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. 5 Publications
VAR_019372
Natural varianti446 – 4461V → L in MLIV; does not affect channel activity; affects channel inhibition by low pH. 2 Publications
VAR_019373
Natural varianti447 – 4471L → P in MLIV. 1 Publication
VAR_019374
Natural varianti465 – 4651F → L in MLIV; still localizes to late endosomes. 2 Publications
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. 1 Publication

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-1
PRO_0000215362Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Phosphoserine By 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.

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.

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. 2 Publications
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. 3 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. 5 Publications
VAR_019372
Natural varianti446 – 4461V → L in MLIV; does not affect channel activity; affects channel inhibition by low pH. 2 Publications
VAR_019373
Natural varianti447 – 4471L → P in MLIV. 1 Publication
VAR_019374
Natural varianti465 – 4651F → L in MLIV; still localizes to late endosomes. 2 Publications
VAR_019375

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 19128ALCQR…MVVTD → LSASGTTTEATWTRPTTHLT LIRWWLLVN in AAG42242. 1 Publication
Add
BLAST
Sequence conflicti203 – 2031P → S in CAC08215. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 121 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

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