HSCARG
entrez
57407
canonical
uniprot
Q9HBL8
canonical
ensembl
ENSG00000153406
resolver
ensembl
ENSG00000274684
resolver
ensp
ENSP00000283429
resolver
ensp
ENSP00000383962
resolver
ensp
ENSP00000458762
resolver
ensp
ENSP00000460263
resolver
ensp
ENSP00000478990
resolver
ensp
ENSP00000479569
resolver
ensp
ENSP00000488644
resolver
ensp
ENSP00000488692
resolver
ensp
ENSP00000576150
resolver
ensp
ENSP00000576151
resolver
ensp
ENSP00000678109
resolver
ensp
ENSP00000678111
resolver
ensp
ENSP00000715255
resolver
ensp
ENSP00000739218
resolver
enst
ENST00000283429
resolver
enst
ENST00000404295
resolver
enst
ENST00000574425
resolver
enst
ENST00000574733
resolver
enst
ENST00000616587
resolver
enst
ENST00000621810
resolver
enst
ENST00000632013
resolver
enst
ENST00000633085
resolver
enst
ENST00000906091
resolver
enst
ENST00000906092
resolver
genesymbol
HSCARG
resolver
genesymbol
NMRAL1
resolver
genesymbol_syn
HSCARG
resolver
hgnc
HGNC:24987
resolver
uniprot
A0A384P622
resolver
uniprot_entry
A0A384P622_HUMAN
resolver
uniprot_entry
NMRL1_HUMAN
resolver
amino_acid_sequence
MVDKKLVVVFGGTGAQGGSVARTLLEDGTFKVRVVTRNPRKKAAKELRLQGAEVVQGDQDDQVIMELALNGAYATFIVTNYWESCSQEQEVKQGKLLADLARRLGLHYVVYSGLENIKKLTAGRLAAAHFDGKGEVEEYFRDIGVPMTSVRLPCYFENLLSHFLPQKAPDGKSYLLSLPTGDVPMDGMSVSDLGPVVLSLLKMPEKYVGQNIGLSTCRHTAEEYAALLTKHTRKVVHDAKMTPEDYEKLGFPGARDLANMFRFYALRPDRDIELTLRLNPKALTLDQWLEQHKGDFNLL
uniprot
proteins
function
FUNCTION: Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsequently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer. {ECO:0000269|PubMed:17496144, ECO:0000269|PubMed:18263583, ECO:0000269|PubMed:19254724}.
uniprot
proteins
mass_dalton
33344
uniprot
proteins
mutagenesis
MUTAGEN 37; /note="R->A: Impairs binding to NADPH; abolishes the ability to dimerize; enhances binding to ASS1; reduces perinuclear localization."; /evidence="ECO:0000269|PubMed:19254724"; MUTAGEN 41; /note="K->S: Does not impair binding to NADPH; maintains the dimerization properties as the wild type; does not affect binding to ASS1; does not affect perinuclear localization."; /evidence="ECO:0000269|PubMed:19254724"; MUTAGEN 81; /note="Y->A: Impairs binding to NADPH; abolishes the ability to dimerize; enhances binding to ASS1; reduces perinuclear localization."; /evidence="ECO:0000269|PubMed:19254724"; MUTAGEN 133; /note="K->A: Impairs binding to NADPH; enhances binding to ASS1; reduces perinuclear localization."; /evidence="ECO:0000269|PubMed:19254724
uniprot
proteins
protein_family
NmrA-type oxidoreductase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
17496144
uniprot
proteins
pubmed
18263583
uniprot
proteins
pubmed
19254724
uniprot
proteins
pubmed
22814378
uniprot
proteins
sequence_length
299
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Note=Under normal redox growth conditions localizes in the cytoplasm and perinuclear region. Nuclear localization is promoted by increased intracellular nitric oxide and reduced NADPH/NADP(+) ratios.
uniprot
proteins