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Q9GZU1

- MCLN1_HUMAN

UniProt

Q9GZU1 - MCLN1_HUMAN

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Protein

Mucolipin-1

Gene

MCOLN1

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.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
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

Topology

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

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. lysosomal membrane Source: UniProtKB
  6. plasma membrane Source: HPA
  7. 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.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. 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-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

BgeeiQ9GZU1.
CleanExiHS_MCOLN1.
ExpressionAtlasiQ9GZU1. baseline and differential.
GenevestigatoriQ9GZU1.

Organism-specific databases

HPAiHPA031763.

Interactioni

Subunit structurei

Forms multimeric complexes. Interacts with PDCD6.2 Publications

Protein-protein interaction databases

BioGridi121441. 3 interactions.
IntActiQ9GZU1. 2 interactions.
MINTiMINT-1409368.
STRINGi9606.ENSP00000264079.

Structurei

3D structure databases

ProteinModelPortaliQ9GZU1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG149591.
GeneTreeiENSGT00390000017126.
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

        10         20         30         40         50
MTAPAGPRGS ETERLLTPNP GYGTQAGPSP APPTPPEEED LRRRLKYFFM
60 70 80 90 100
SPCDKFRAKG RKPCKLMLQV VKILVVTVQL ILFGLSNQLA VTFREENTIA
110 120 130 140 150
FRHLFLLGYS DGADDTFAAY TREQLYQAIF HAVDQYLALP DVSLGRYAYV
160 170 180 190 200
RGGGDPWTNG SGLALCQRYY HRGHVDPAND TFDIDPMVVT DCIQVDPPER
210 220 230 240 250
PPPPPSDDLT LLESSSSYKN LTLKFHKLVN VTIHFRLKTI NLQSLINNEI
260 270 280 290 300
PDCYTFSVLI TFDNKAHSGR IPISLETQAH IQECKHPSVF QHGDNSFRLL
310 320 330 340 350
FDVVVILTCS LSFLLCARSL LRGFLLQNEF VGFMWRQRGR VISLWERLEF
360 370 380 390 400
VNGWYILLVT SDVLTISGTI MKIGIEAKNL ASYDVCSILL GTSTLLVWVG
410 420 430 440 450
VIRYLTFFHN YNILIATLRV ALPSVMRFCC CVAVIYLGYC FCGWIVLGPY
460 470 480 490 500
HVKFRSLSMV SECLFSLING DDMFVTFAAM QAQQGRSSLV WLFSQLYLYS
510 520 530 540 550
FISLFIYMVL SLFIALITGA YDTIKHPGGA GAEESELQAY IAQCQDSPTS
560 570 580
GKFRRGSGSA CSLLCCCGRD PSEEHSLLVN
Length:580
Mass (Da):65,022
Last modified:March 1, 2001 - v1
Checksum:i7E7691F58D01C804
GO

Sequence cautioni

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

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 3 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.
GeneTreei ENSGT00390000017126.
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

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

Gene expression databases

Bgeei Q9GZU1.
CleanExi HS_MCOLN1.
ExpressionAtlasi Q9GZU1. baseline and differential.
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: November 26, 2014
This is version 124 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