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Q6VVB1

- NHLC1_HUMAN

UniProt

Q6VVB1 - NHLC1_HUMAN

Protein

E3 ubiquitin-protein ligase NHLRC1

Gene

NHLRC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase. Together with the phosphatase EPM2A/laforin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. In complex with EPM2A/laforin and HSP70, suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Ubiquitinates the glycogen-targeting protein phosphatase subunits PPP1R3C/PTG and PPP1R3D in a laforin-dependent manner and targets them for proteasome-dependent degradation, thus decreasing glycogen accumulation. Polyubiquitinates EPM2A/laforin and ubiquitinates AGL and targets them for proteasome-dependent degradation. Also promotes proteasome-independent protein degradation through the macroautophagy pathway.6 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri26 – 7247RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. ubiquitin-protein transferase activity Source: UniProtKB
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. autophagy Source: UniProtKB-KW
    2. carbohydrate metabolic process Source: Reactome
    3. glucose metabolic process Source: Reactome
    4. glycogen biosynthetic process Source: Reactome
    5. positive regulation of protein ubiquitination Source: Ensembl
    6. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    7. protein polyubiquitination Source: UniProtKB
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Autophagy, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_169208. Glycogen synthesis.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase NHLRC1 (EC:6.3.2.-)
    Alternative name(s):
    Malin
    NHL repeat-containing protein 1
    Gene namesi
    Name:NHLRC1
    Synonyms:EPM2B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21576. NHLRC1.

    Subcellular locationi

    Endoplasmic reticulum. Nucleus
    Note: Localizes at the endoplasmic reticulum and, to a lesser extent, in the nucleus.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endoplasmic reticulum Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB
    4. perinuclear region of cytoplasm Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Epilepsy, progressive myoclonic 2 (EPM2) [MIM:254780]: An autosomal recessive and severe form of adolescent-onset progressive epilepsy. Typically, as seizures increase in frequency, cognitive function declines towards dementia, and affected individuals die usually within 10 years after onset. EPM2 occurs worldwide, but it is particularly common in the mediterranean countries of southern Europe and northern Africa, in southern India and in the Middle East. At the cellular level, it is characterized by accumulation of starch-like polyglucosans called Lafora bodies (LBs) that are most abundant in organs with the highest glucose metabolism: brain, heart, liver and skeletal muscle. Among other conditions involving polyglucosans, EPM2 is unique in that the inclusions are in neuronal dendrites but not axons and the forming polyglucosan fibrils are associated with the endoplasmic reticulum.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221S → R in EPM2; does not significantly alters the subcellular location as compared to the wild-type. 1 Publication
    VAR_046387
    Natural varianti26 – 261C → S in EPM2. 1 Publication
    Corresponds to variant rs28940575 [ dbSNP | Ensembl ].
    VAR_019482
    Natural varianti33 – 331F → S in EPM2. 1 Publication
    VAR_019483
    Natural varianti46 – 461C → Y in EPM2; loss of interaction with EPM2A and increased levels of PPP1R3C and glycogen; compound heterozygote with A-69. 1 Publication
    VAR_070793
    Natural varianti67 – 671E → Q in EPM2. 1 Publication
    VAR_046388
    Natural varianti68 – 681C → Y in EPM2. 1 Publication
    VAR_046389
    Natural varianti69 – 691P → A in EPM2; severely reduced interaction with EPM2A and increased levels of PPP1R3C and glycogen; in one patient compound heterozygote with Y-46. 2 Publications
    Corresponds to variant rs28940576 [ dbSNP | Ensembl ].
    VAR_019484
    Natural varianti87 – 871L → P in EPM2. 1 Publication
    VAR_019485
    Natural varianti126 – 1261L → P in EPM2; the mutant protein targeted exclusively nucleus as compared to predominantly cytoplasmic and partially nuclear localization of the wild-type protein. 1 Publication
    VAR_046390
    Natural varianti146 – 1461D → N in EPM2; severely reduced interaction with EPM2A and increased levels of PPP1R3C and glycogen; in one patient compound heterozygote with P-261. 2 Publications
    VAR_019487
    Natural varianti153 – 1531I → M in EPM2. 1 Publication
    VAR_046391
    Natural varianti160 – 1601C → R in EPM2. 1 Publication
    Corresponds to variant rs200595273 [ dbSNP | Ensembl ].
    VAR_046392
    Natural varianti198 – 1981I → N in EPM2. 1 Publication
    VAR_046393
    Natural varianti219 – 2191W → R in EPM2. 1 Publication
    VAR_046394
    Natural varianti233 – 2331D → A in EPM2. 1 Publication
    VAR_046395
    Natural varianti245 – 2451D → N in EPM2. 1 Publication
    VAR_046396
    Natural varianti253 – 2531R → K in EPM2. 1 Publication
    VAR_046397
    Natural varianti261 – 2611L → P in EPM2; loss of interaction with EPM2A and increased levels of PPP1R3C and glycogen; compound heterozygote with N-146. 1 Publication
    VAR_070794
    Natural varianti264 – 2641P → H in EPM2. 1 Publication
    VAR_046398
    Natural varianti279 – 2791L → P in EPM2; significantly alters the distribution of the protein; a great majority of cells expressing the mutant form formed perinuclear inclusion when compared with the wild-type form. 1 Publication
    VAR_046399
    Natural varianti294 – 2952Missing in EPM2.
    VAR_046400
    Natural varianti302 – 3021Q → P in EPM2; loss of interaction with EPM2A. 1 Publication
    VAR_019488
    Natural varianti308 – 3081D → A in EPM2. 1 Publication
    VAR_046401

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi280 – 2801E → K: Loss of interaction with EP2MA. 1 Publication

    Keywords - Diseasei

    Disease mutation, Epilepsy

    Organism-specific databases

    MIMi254780. phenotype.
    Orphaneti501. Lafora disease.
    PharmGKBiPA134916338.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 395395E3 ubiquitin-protein ligase NHLRC1PRO_0000055980Add
    BLAST

    Proteomic databases

    PaxDbiQ6VVB1.
    PRIDEiQ6VVB1.

    Expressioni

    Tissue specificityi

    Expressed in brain, cerebellum, spinal cord, medulla, heart, liver, skeletal muscle and pancreas.1 Publication

    Gene expression databases

    BgeeiQ6VVB1.
    CleanExiHS_NHLRC1.
    GenevestigatoriQ6VVB1.

    Interactioni

    Subunit structurei

    Interacts with AGL. Interacts (via the NHL repeats) with EPM2A/laforin. Forms a complex with EPM2A/laforin and HSP70.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Epm2aQ9WUA512EBI-6426628,EBI-1040928From a different organism.

    Protein-protein interaction databases

    BioGridi132073. 16 interactions.
    IntActiQ6VVB1. 7 interactions.
    MINTiMINT-8374086.
    STRINGi9606.ENSP00000345464.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6VVB1.
    SMRiQ6VVB1. Positions 23-76, 117-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati113 – 15745NHL 1Add
    BLAST
    Repeati161 – 20444NHL 2Add
    BLAST
    Repeati205 – 24541NHL 3Add
    BLAST
    Repeati248 – 30053NHL 4Add
    BLAST
    Repeati301 – 34949NHL 5Add
    BLAST
    Repeati350 – 39344NHL 6Add
    BLAST

    Domaini

    The RING domain is essential for ubiquitin E3 ligase activity.1 Publication

    Sequence similaritiesi

    Contains 6 NHL repeats.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri26 – 7247RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG255948.
    HOGENOMiHOG000113780.
    HOVERGENiHBG052617.
    InParanoidiQ6VVB1.
    KOiK10602.
    OMAiPRNLPCG.
    OrthoDBiEOG7VX8W6.
    PhylomeDBiQ6VVB1.
    TreeFamiTF331018.

    Family and domain databases

    Gene3Di2.120.10.30. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR013017. NHL_repeat_subgr.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF14634. zf-RING_5. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS51125. NHL. 6 hits.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6VVB1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAEASESGP ALHELMREAE ISLLECKVCF EKFGHRQQRR PRNLSCGHVV    50
    CLACVAALAH PRTLALECPF CRRACRGCDT SDCLPVLHLI ELLGSALRQS 100
    PAAHRAAPSA PGALTCHHTF GGWGTLVNPT GLALCPKTGR VVVVHDGRRR 150
    VKIFDSGGGC AHQFGEKGDA AQDIRYPVDV TITNDCHVVV TDAGDRSIKV 200
    FDFFGQIKLV IGGQFSLPWG VETTPQNGIV VTDAEAGSLH LLDVDFAEGV 250
    LRRTERLQAH LCNPRGVAVS WLTGAIAVLE HPLALGTGVC STRVKVFSSS 300
    MQLVGQVDTF GLSLYFPSKI TASAVTFDHQ GNVIVADTSG PAILCLGKPE 350
    EFPVPKPMVT HGLSHPVALT FTKENSLLVL DTASHSIKVY KVDWG 395
    Length:395
    Mass (Da):42,293
    Last modified:July 19, 2004 - v2
    Checksum:i3E8339D00165FBED
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221S → R in EPM2; does not significantly alters the subcellular location as compared to the wild-type. 1 Publication
    VAR_046387
    Natural varianti26 – 261C → S in EPM2. 1 Publication
    Corresponds to variant rs28940575 [ dbSNP | Ensembl ].
    VAR_019482
    Natural varianti33 – 331F → S in EPM2. 1 Publication
    VAR_019483
    Natural varianti46 – 461C → Y in EPM2; loss of interaction with EPM2A and increased levels of PPP1R3C and glycogen; compound heterozygote with A-69. 1 Publication
    VAR_070793
    Natural varianti67 – 671E → Q in EPM2. 1 Publication
    VAR_046388
    Natural varianti68 – 681C → Y in EPM2. 1 Publication
    VAR_046389
    Natural varianti69 – 691P → A in EPM2; severely reduced interaction with EPM2A and increased levels of PPP1R3C and glycogen; in one patient compound heterozygote with Y-46. 2 Publications
    Corresponds to variant rs28940576 [ dbSNP | Ensembl ].
    VAR_019484
    Natural varianti87 – 871L → P in EPM2. 1 Publication
    VAR_019485
    Natural varianti111 – 1111P → L Common polymorphism. 3 Publications
    Corresponds to variant rs10949483 [ dbSNP | Ensembl ].
    VAR_019486
    Natural varianti126 – 1261L → P in EPM2; the mutant protein targeted exclusively nucleus as compared to predominantly cytoplasmic and partially nuclear localization of the wild-type protein. 1 Publication
    VAR_046390
    Natural varianti146 – 1461D → N in EPM2; severely reduced interaction with EPM2A and increased levels of PPP1R3C and glycogen; in one patient compound heterozygote with P-261. 2 Publications
    VAR_019487
    Natural varianti153 – 1531I → M in EPM2. 1 Publication
    VAR_046391
    Natural varianti160 – 1601C → R in EPM2. 1 Publication
    Corresponds to variant rs200595273 [ dbSNP | Ensembl ].
    VAR_046392
    Natural varianti198 – 1981I → N in EPM2. 1 Publication
    VAR_046393
    Natural varianti219 – 2191W → R in EPM2. 1 Publication
    VAR_046394
    Natural varianti233 – 2331D → A in EPM2. 1 Publication
    VAR_046395
    Natural varianti245 – 2451D → N in EPM2. 1 Publication
    VAR_046396
    Natural varianti253 – 2531R → K in EPM2. 1 Publication
    VAR_046397
    Natural varianti261 – 2611L → P in EPM2; loss of interaction with EPM2A and increased levels of PPP1R3C and glycogen; compound heterozygote with N-146. 1 Publication
    VAR_070794
    Natural varianti264 – 2641P → H in EPM2. 1 Publication
    VAR_046398
    Natural varianti279 – 2791L → P in EPM2; significantly alters the distribution of the protein; a great majority of cells expressing the mutant form formed perinuclear inclusion when compared with the wild-type form. 1 Publication
    VAR_046399
    Natural varianti294 – 2952Missing in EPM2.
    VAR_046400
    Natural varianti302 – 3021Q → P in EPM2; loss of interaction with EPM2A. 1 Publication
    VAR_019488
    Natural varianti308 – 3081D → A in EPM2. 1 Publication
    VAR_046401

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY324850 mRNA. Translation: AAQ19671.1.
    AL589723 Genomic DNA. Translation: CAH71232.1.
    BC103888 mRNA. Translation: AAI03889.1.
    BC103889 mRNA. Translation: AAI03890.1.
    BC103890 mRNA. Translation: AAI03891.1.
    BK001510 mRNA. Translation: DAA01954.1.
    CCDSiCCDS4542.1.
    RefSeqiNP_940988.2. NM_198586.2.
    UniGeneiHs.348351.

    Genome annotation databases

    EnsembliENST00000340650; ENSP00000345464; ENSG00000187566.
    GeneIDi378884.
    KEGGihsa:378884.
    UCSCiuc003ncl.1. human.

    Polymorphism databases

    DMDMi50400890.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    The Lafora progressive myoclonus epilepsy mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY324850 mRNA. Translation: AAQ19671.1 .
    AL589723 Genomic DNA. Translation: CAH71232.1 .
    BC103888 mRNA. Translation: AAI03889.1 .
    BC103889 mRNA. Translation: AAI03890.1 .
    BC103890 mRNA. Translation: AAI03891.1 .
    BK001510 mRNA. Translation: DAA01954.1 .
    CCDSi CCDS4542.1.
    RefSeqi NP_940988.2. NM_198586.2.
    UniGenei Hs.348351.

    3D structure databases

    ProteinModelPortali Q6VVB1.
    SMRi Q6VVB1. Positions 23-76, 117-337.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 132073. 16 interactions.
    IntActi Q6VVB1. 7 interactions.
    MINTi MINT-8374086.
    STRINGi 9606.ENSP00000345464.

    Polymorphism databases

    DMDMi 50400890.

    Proteomic databases

    PaxDbi Q6VVB1.
    PRIDEi Q6VVB1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340650 ; ENSP00000345464 ; ENSG00000187566 .
    GeneIDi 378884.
    KEGGi hsa:378884.
    UCSCi uc003ncl.1. human.

    Organism-specific databases

    CTDi 378884.
    GeneCardsi GC06M018065.
    GeneReviewsi NHLRC1.
    HGNCi HGNC:21576. NHLRC1.
    MIMi 254780. phenotype.
    608072. gene.
    neXtProti NX_Q6VVB1.
    Orphaneti 501. Lafora disease.
    PharmGKBi PA134916338.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG255948.
    HOGENOMi HOG000113780.
    HOVERGENi HBG052617.
    InParanoidi Q6VVB1.
    KOi K10602.
    OMAi PRNLPCG.
    OrthoDBi EOG7VX8W6.
    PhylomeDBi Q6VVB1.
    TreeFami TF331018.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_169208. Glycogen synthesis.

    Miscellaneous databases

    GeneWikii NHLRC1.
    GenomeRNAii 378884.
    NextBioi 100856.
    PROi Q6VVB1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q6VVB1.
    CleanExi HS_NHLRC1.
    Genevestigatori Q6VVB1.

    Family and domain databases

    Gene3Di 2.120.10.30. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR013017. NHL_repeat_subgr.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF14634. zf-RING_5. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS51125. NHL. 6 hits.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS EPM2 SER-26; SER-33; ALA-69; PRO-87; ASN-146 AND PRO-302, VARIANT LEU-111.
    2. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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], VARIANT LEU-111.
    4. "Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin."
      Gentry M.S., Worby C.A., Dixon J.E.
      Proc. Natl. Acad. Sci. U.S.A. 102:8501-8506(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EPM2A, DOMAIN RING, CHARACTERIZATION OF VARIANT EPM2 PRO-302, MUTAGENESIS OF GLU-280.
    5. "A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease."
      Cheng A., Zhang M., Gentry M.S., Worby C.A., Dixon J.E., Saltiel A.R.
      Genes Dev. 21:2399-2409(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AGL.
    6. "Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG)."
      Worby C.A., Gentry M.S., Dixon J.E.
      J. Biol. Chem. 283:4069-4076(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The malin-laforin complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system."
      Garyali P., Siwach P., Singh P.K., Puri R., Mittal S., Sengupta S., Parihar R., Ganesh S.
      Hum. Mol. Genet. 18:688-700(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COMPLEX FORMATION WITH EPM2A AND HSP70.
    8. "Glycogenic activity of R6, a protein phosphatase 1 regulatory subunit, is modulated by the laforin-malin complex."
      Rubio-Villena C., Garcia-Gimeno M.A., Sanz P.
      Int. J. Biochem. Cell Biol. 45:1479-1488(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Mutations in the NHLRC1 gene are the common cause for Lafora disease in the Japanese population."
      Singh S., Suzuki T., Uchiyama A., Kumada S., Moriyama N., Hirose S., Takahashi Y., Sugie H., Mizoguchi K., Inoue Y., Kimura K., Sawaishi Y., Yamakawa K., Ganesh S.
      J. Hum. Genet. 50:347-352(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EPM2 MET-153; ARG-160; ARG-219; ASN-245 AND LYS-253, VARIANT LEU-111.
    10. Cited for: VARIANTS EPM2 GLN-67; TYR-68; ASN-198; ALA-233; HIS-264; 294-VAL-LYS-295 DEL AND ALA-308.
    11. "Lafora disease in the Indian population: EPM2A and NHLRC1 gene mutations and their impact on subcellular localization of laforin and malin."
      Singh S., Satishchandra P., Shankar S.K., Ganesh S.
      Hum. Mutat. 29:E1-12(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EPM2 ARG-22; PRO-126 AND PRO-279, CHARACTERIZATION OF VARIANTS EPM2 ARG-22; PRO-126 AND PRO-279.
    12. Cited for: VARIANTS EPM2 TYR-46; ALA-69; ASN-146 AND PRO-261, CHARACTERIZATION OF VARIANTS EPM2 TYR-46; ALA-69; ASN-146 AND PRO-261, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EPM2A.

    Entry informationi

    Entry nameiNHLC1_HUMAN
    AccessioniPrimary (citable) accession number: Q6VVB1
    Secondary accession number(s): Q3SYB1, Q5VUK7, Q6IMH1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 102 of the entry and version 2 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 6
      Human chromosome 6: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3