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Q6VVB1

- NHLC1_HUMAN

UniProt

Q6VVB1 - NHLC1_HUMAN

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Protein
E3 ubiquitin-protein ligase NHLRC1
Gene
NHLRC1, EPM2B
Organism
Homo sapiens (Human)
Status
Reviewed - 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-type
Add
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
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.
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.3 Publications

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) [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.
Note: The disease is caused by mutations affecting the gene represented in this entry.7 Publications
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. 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 NHLRC1
PRO_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. 3 interactions.
MINTiMINT-8374086.
STRINGi9606.ENSP00000345464.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Domaini

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

Sequence similaritiesi

Contains 6 NHL repeats.

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

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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. 2 Publications
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. 3 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

« 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(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: September 3, 2014
This is version 101 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

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