NHLRC1
entrez
378884
canonical
uniprot
Q6VVB1
canonical
ensembl
ENSG00000187566
resolver
ensp
ENSP00000345464
resolver
enst
ENST00000340650
resolver
genesymbol
NHLRC1
resolver
genesymbol_syn
EPM2B
resolver
hgnc
HGNC:21576
resolver
uniprot
Q3SYB1
resolver
uniprot
Q5VUK7
resolver
uniprot
Q6IMH1
resolver
uniprot_entry
NHLC1_HUMAN
resolver
uniprot_sec
Q3SYB1
resolver
uniprot_sec
Q5VUK7
resolver
uniprot_sec
Q6IMH1
resolver
amino_acid_sequence
MAAEASESGPALHELMREAEISLLECKVCFEKFGHRQQRRPRNLSCGHVVCLACVAALAHPRTLALECPFCRRACRGCDTSDCLPVLHLIELLGSALRQSPAAHRAAPSAPGALTCHHTFGGWGTLVNPTGLALCPKTGRVVVVHDGRRRVKIFDSGGGCAHQFGEKGDAAQDIRYPVDVTITNDCHVVVTDAGDRSIKVFDFFGQIKLVIGGQFSLPWGVETTPQNGIVVTDAEAGSLHLLDVDFAEGVLRRTERLQAHLCNPRGVAVSWLTGAIAVLEHPLALGTGVCSTRVKVFSSSMQLVGQVDTFGLSLYFPSKITASAVTFDHQGNVIVADTSGPAILCLGKPEEFPVPKPMVTHGLSHPVALTFTKENSLLVLDTASHSIKVYKVDWG
uniprot
proteins
disease_involvement
DISEASE: Myoclonic epilepsy of Lafora 2 (MELF2) [MIM:620681]: A form of progressive myoclonic epilepsy, a clinically and genetically heterogeneous group of disorders defined by the combination of action and reflex myoclonus, other types of epileptic seizures, and progressive neurodegeneration and neurocognitive impairment. MELF2 is an autosomal recessive, severe form characterized by onset of progressive neurodegeneration between 8 and 18 years of age. Initial features can include headache, myoclonic jerks, generalized seizures, and often visual hallucination. Typically, as seizures increase in frequency, cognitive function declines towards dementia, and affected individuals die usually within 10 years after onset. At the cellular level, MELF2 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. {ECO:0000269|PubMed:12958597, ECO:0000269|PubMed:15781812, ECO:0000269|PubMed:15930137, ECO:0000269|PubMed:16021330, ECO:0000269|PubMed:18311786, ECO:0000269|PubMed:21505799}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:15930137, ECO:0000269|PubMed:17908927, ECO:0000269|PubMed:18070875, ECO:0000269|PubMed:19036738, ECO:0000269|PubMed:21505799, ECO:0000269|PubMed:23624058}.
uniprot
proteins
mass_dalton
42293
uniprot
proteins
mutagenesis
MUTAGEN 280; /note="E->K: Loss of interaction with EP2MA."; /evidence="ECO:0000269|PubMed:15930137
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
pubmed
12958597
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15781812
uniprot
proteins
pubmed
15930137
uniprot
proteins
pubmed
16021330
uniprot
proteins
pubmed
17908927
uniprot
proteins
pubmed
18070875
uniprot
proteins
pubmed
18311786
uniprot
proteins
pubmed
19036738
uniprot
proteins
pubmed
21505799
uniprot
proteins
pubmed
22961547
uniprot
proteins
pubmed
23624058
uniprot
proteins
sequence_length
395
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum. Nucleus. Note=Localizes at the endoplasmic reticulum and, to a lesser extent, in the nucleus.
uniprot
proteins