Version 5.4
| Homo sapiens Protein: NMRAL1 | |||||||||||||||||||
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| Summary | |||||||||||||||||||
| InnateDB Protein | IDBP-749396.3 | ||||||||||||||||||
| Last Modified | 2014-10-13 [Report errors or provide feedback] | ||||||||||||||||||
| Gene Symbol | NMRAL1 | ||||||||||||||||||
| Protein Name | |||||||||||||||||||
| Synonyms | |||||||||||||||||||
| Species | Homo sapiens | ||||||||||||||||||
| Ensembl Protein | ENSP00000458762 | ||||||||||||||||||
| InnateDB Gene | IDBG-12821 (NMRAL1) | ||||||||||||||||||
| Protein Structure |
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| UniProt Annotation | |||||||||||||||||||
| 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 subsecuently 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:0000269PubMed:17496144, ECO:0000269PubMed:18263583, ECO:0000269PubMed:19254724}. | ||||||||||||||||||
| Subcellular Localization | 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. | ||||||||||||||||||
| Disease Associations | |||||||||||||||||||
| Tissue Specificity | |||||||||||||||||||
| Comments | |||||||||||||||||||
| Interactions | |||||||||||||||||||
| Number of Interactions |
This gene and/or its encoded proteins are associated with 12 experimentally validated interaction(s) in this database.
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| Gene Ontology | |||||||||||||||||||
Molecular Function |
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| Biological Process |
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| Cellular Component |
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| Protein Structure and Domains | |||||||||||||||||||
| PDB ID | |||||||||||||||||||
| InterPro |
IPR002198
Short-chain dehydrogenase/reductase SDR IPR003148 Regulator of K+ conductance, N-terminal IPR008030 NmrA-like domain |
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| PFAM |
PF00106
PF02254 PF05368 |
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| PRINTS |
PR00080
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| PIRSF |
PIRSF000126
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| SMART | |||||||||||||||||||
| TIGRFAMs | |||||||||||||||||||
| Post-translational Modifications | |||||||||||||||||||
| Modification | |||||||||||||||||||
| Cross-References | |||||||||||||||||||
| SwissProt | Q9HBL8 | ||||||||||||||||||
| PhosphoSite | PhosphoSite-Q9HBL8 | ||||||||||||||||||
| TrEMBL | |||||||||||||||||||
| UniProt Splice Variant | |||||||||||||||||||
| Entrez Gene | 57407 | ||||||||||||||||||
| UniGene | Hs.630160 | ||||||||||||||||||
| RefSeq | XP_006720969 | ||||||||||||||||||
| HUGO | HGNC:24987 | ||||||||||||||||||
| OMIM | |||||||||||||||||||
| CCDS | CCDS10516 | ||||||||||||||||||
| HPRD | 13678 | ||||||||||||||||||
| IMGT | |||||||||||||||||||
| EMBL | AC007606 AC012676 AF225419 BC002927 BC007364 | ||||||||||||||||||
| GenPept | AAG09721 AAH02927 AAH07364 | ||||||||||||||||||