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Protein

E3 ubiquitin-protein ligase NHLRC1

Gene

NHLRC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. ubiquitin-protein transferase activity Source: UniProtKB
  3. 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. pathogenesis Source: Reactome
  6. positive regulation of protein ubiquitination Source: Ensembl
  7. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  8. protein polyubiquitination Source: UniProtKB
  9. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Autophagy, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_169208. Glycogen synthesis.
REACT_264430. Myoclonic epilepsy of Lafora.
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 Componenti: 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
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Nucleus

Pathology & Biotechi

Involvement in diseasei

Epilepsy, progressive myoclonic 2 (EPM2)5 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:254780
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; compound heterozygote with A-69; loss of interaction with EPM2A; increased levels of PPP1R3C and glycogen. 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; compound heterozygote with Y-46; severely reduced interaction with EPM2A; increased levels of PPP1R3C and glycogen. 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; compound heterozygote with P-261; severely reduced interaction with EPM2A; increased levels of PPP1R3C and glycogen. 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; compound heterozygote with N-146; loss of interaction with EPM2A; increased levels of PPP1R3C and glycogen. 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. 1 Publication
VAR_046400
Natural varianti302 – 3021Q → P in EPM2; loss of interaction with EPM2A. 2 Publications
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. 18 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.
GeneTreeiENSGT00730000111361.
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

        10         20         30         40         50
MAAEASESGP ALHELMREAE ISLLECKVCF EKFGHRQQRR PRNLSCGHVV
60 70 80 90 100
CLACVAALAH PRTLALECPF CRRACRGCDT SDCLPVLHLI ELLGSALRQS
110 120 130 140 150
PAAHRAAPSA PGALTCHHTF GGWGTLVNPT GLALCPKTGR VVVVHDGRRR
160 170 180 190 200
VKIFDSGGGC AHQFGEKGDA AQDIRYPVDV TITNDCHVVV TDAGDRSIKV
210 220 230 240 250
FDFFGQIKLV IGGQFSLPWG VETTPQNGIV VTDAEAGSLH LLDVDFAEGV
260 270 280 290 300
LRRTERLQAH LCNPRGVAVS WLTGAIAVLE HPLALGTGVC STRVKVFSSS
310 320 330 340 350
MQLVGQVDTF GLSLYFPSKI TASAVTFDHQ GNVIVADTSG PAILCLGKPE
360 370 380 390
EFPVPKPMVT HGLSHPVALT FTKENSLLVL DTASHSIKVY KVDWG
Length:395
Mass (Da):42,293
Last modified:July 18, 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; compound heterozygote with A-69; loss of interaction with EPM2A; increased levels of PPP1R3C and glycogen. 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; compound heterozygote with Y-46; severely reduced interaction with EPM2A; increased levels of PPP1R3C and glycogen. 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; compound heterozygote with P-261; severely reduced interaction with EPM2A; increased levels of PPP1R3C and glycogen. 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; compound heterozygote with N-146; loss of interaction with EPM2A; increased levels of PPP1R3C and glycogen. 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. 1 Publication
VAR_046400
Natural varianti302 – 3021Q → P in EPM2; loss of interaction with EPM2A. 2 Publications
VAR_019488
Natural varianti308 – 3081D → A in EPM2. 1 Publication
VAR_046401

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi132073. 18 interactions.
IntActiQ6VVB1. 7 interactions.
MINTiMINT-8374086.
STRINGi9606.ENSP00000345464.

Polymorphism databases

DMDMi50400890.

Proteomic databases

PaxDbiQ6VVB1.
PRIDEiQ6VVB1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi378884.
GeneCardsiGC06M018065.
GeneReviewsiNHLRC1.
HGNCiHGNC:21576. NHLRC1.
MIMi254780. phenotype.
608072. gene.
neXtProtiNX_Q6VVB1.
Orphaneti501. Lafora disease.
PharmGKBiPA134916338.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG255948.
GeneTreeiENSGT00730000111361.
HOGENOMiHOG000113780.
HOVERGENiHBG052617.
InParanoidiQ6VVB1.
KOiK10602.
OMAiPRNLPCG.
OrthoDBiEOG7VX8W6.
PhylomeDBiQ6VVB1.
TreeFamiTF331018.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_169208. Glycogen synthesis.
REACT_264430. Myoclonic epilepsy of Lafora.

Miscellaneous databases

GeneWikiiNHLRC1.
GenomeRNAii378884.
NextBioi100856.
PROiQ6VVB1.
SOURCEiSearch...

Gene expression databases

BgeeiQ6VVB1.
CleanExiHS_NHLRC1.
GenevestigatoriQ6VVB1.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2002) [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(2003) [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(2004) [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(2006) [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(2007) [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(2008) [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(2012) [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(2004) [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(2007) [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 18, 2004
Last sequence update: July 18, 2004
Last modified: March 31, 2015
This is version 107 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.