Q62433 (NDRG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 104.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Protein NDRG1 Alternative name(s): N-myc downstream-regulated gene 1 protein Short name=Protein Ndr1 | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 394 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Stress-responsive protein involved in hormone responses, cell growth, and differentiation. Acts as a tumor suppressor in many cell types. Necessary but not sufficient for p53/TP53-mediated caspase activation and apoptosis. Required for vesicular recycling of CDH1 and TF. May also function in lipid trafficking. Protects cells from spindle disruption damage. Functions in p53/TP53-dependent mitotic spindle checkpoint. Regulates microtubule dynamics and maintains euploidy By similarity. Has a role in cell trafficking notably of the Schwann cell and is necessary for the maintenance and development of the peripheral nerve myelin sheath. Ref.5 Ref.9 |
| Subunit structure | Interacts with RAB4A (membrane-bound form); the interaction involves NDRG1 in vesicular recycling of CDH1. Interacts with APOA1, APOA2, PRA1 and RTN1 By similarity. |
| Subcellular location | Cytoplasm › cytosol. Cytoplasm › cytoskeleton › centrosome. Nucleus. Cell membrane By similarity. Note: Mainly cytoplasmic but differentially localized to other regions. Associates with the plasma membrane in intestinal epithelia and lactating mammary gland. Translocated to the nucleus in a p53/TP53-dependent manner. In prostate epithelium and placental chorion, located in both the cytoplasm and in the nucleus. No nuclear localization in colon epithelium cells. In intestinal mucosa, prostate and renal cortex, located predominantly adjacent to adherens junctions. Cytoplasmic with granular staining in proximal tubular cells of the kidney and salivary gland ducts. Recruits to the membrane of recycling/sorting and late endosomes via binding to phosphatidylinositol 4-phosphate. Associates with microtubules. Colocalizes with TUBG1 in the centrosome. Cytoplasmic location increased with hypoxia. Phosphorylated form found associated with centromeres during S-phase of mitosis and with the plasma membrane By similarity. Ref.1 Ref.4 Ref.5 Ref.9 |
| Tissue specificity | Widely expressed, with highest levels in kidney followed by brain, pancreas, small intestine, colon and spleen (at protein level). Also detected in heart and preputial gland, and in much smaller quantities in other tissues. Not detected in duodenum and prostate. Highly expressed in Schwann cells. Ref.2 Ref.4 Ref.5 Ref.8 |
| Developmental stage | In early stages of embryo development, expression low when MYCN expression is high. Later, when MYCN levels diminish, levels increase. Ref.1 |
| Induction | Repressed by testosterone and also to a lesser extent by dihydrotestosterone. Down-regulated by MYCN. Ref.1 Ref.2 |
| Post-translational modification | Under stress conditions, phosphorylated in the C-terminal on many serine and threonine residues. Phosphorylated in vitro by PKA. Phosphorylation enhanced by increased intracellular cAMP levels. Homocysteine induces dephosphorylation. Phosphorylation by SGK1 is cell cycle dependent By similarity. Ref.4 |
| Disruption phenotype | Mutant mice exhibit defects in peripheral nerve development. Initial hind limb weakness developed around age 12 weeks, and significant functional impairment (dragging of hind legs) and muscle atrophy became apparent at age 1 year. After about 5 weeks extensive demyelination of nerve fibers is observed. In later life, large inclusions were seen in the adaxonal Schwann cell cytoplasm. There is no evidence of apoptotic response. Ref.5 Ref.9 |
| Sequence similarities | Belongs to the NDRG family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 394 | 394 | Protein NDRG1 | PRO_0000159574 | |||||
Regions | |||||||||
| Repeat | 339 – 348 | 10 | 1 | ||||||
| Repeat | 349 – 358 | 10 | 2 | ||||||
| Repeat | 359 – 368 | 10 | 3 | ||||||
| Region | 339 – 368 | 30 | 3 X 10 AA tandem repeats of G-[PST]-R-S-R-S-H-T-S-E | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 326 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 328 | 1 | Phosphothreonine; by SGK1 Ref.6 | ||||||
| Modified residue | 330 | 1 | Phosphoserine; by SGK1 Ref.6 | ||||||
| Modified residue | 332 | 1 | Phosphoserine; by SGK1 By similarity | ||||||
| Modified residue | 333 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 335 | 1 | Phosphothreonine Ref.6 | ||||||
| Modified residue | 336 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 346 | 1 | Phosphothreonine; by SGK1 Ref.4 Ref.7 | ||||||
| Modified residue | 356 | 1 | Phosphothreonine; by SGK1 By similarity | ||||||
| Modified residue | 362 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 364 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 366 | 1 | Phosphothreonine; by SGK1 By similarity | ||||||
| Modified residue | 375 | 1 | Phosphothreonine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 33 – 35 | 3 | QEQ → LEE in AAB58249. Ref.2 | ||||||
| Sequence conflict | 89 | 1 | F → P in AAB58249. Ref.2 | ||||||
| Sequence conflict | 103 – 109 | 7 | APSFPVG → PLPSQW in AAB58249. Ref.2 | ||||||
| Sequence conflict | 141 – 148 | 8 | AGAYILTR → PWXLHPDP in AAB58249. Ref.2 | ||||||
| Sequence conflict | 191 – 208 | 18 | VVSHL…NVEVV → CVPPLRXGGDTQQRGGM in AAB58249. Ref.2 | ||||||
| Sequence conflict | 241 | 1 | R → A in AAB58249. Ref.2 | ||||||
| Sequence conflict | 298 – 350 | 53 | PAKLA…TSEGP → RPSLLRPSSTLCRHGIHAFC QHDSPDRVPHPVWLQCHILE GT in AAB58249. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "N-myc-dependent repression of ndr1, a gene identified by direct subtraction of whole mouse embryo cDNAs between wild type and N-myc mutant." Shimono A., Okuda T., Kondoh H. Mech. Dev. 83:39-52(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION. Tissue: Embryo. |
| [2] | "Cloning and characterization of TDD5, an androgen target gene that is differentially repressed by testosterone and dihydrotestosterone." Lin T.-M., Chang C. Proc. Natl. Acad. Sci. U.S.A. 94:4988-4993(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION. Tissue: Hybridoma. |
| [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]. Strain: FVB/N. Tissue: Kidney. |
| [4] | "Exploitation of KESTREL to identify NDRG family members as physiological substrates for SGK1 and GSK3." Murray J.T., Campbell D.G., Morrice N., Auld G.C., Shpiro N., Marquez R., Peggie M., Bain J., Bloomberg G.B., Grahammer F., Lang F., Wulff P., Kuhl D., Cohen P. Biochem. J. 384:477-488(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-346; THR-356 AND THR-366, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY. |
| [5] | "Ndrg1-deficient mice exhibit a progressive demyelinating disorder of peripheral nerves." Okuda T., Higashi Y., Kokame K., Tanaka C., Kondoh H., Miyata T. Mol. Cell. Biol. 24:3949-3956(2004) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION. |
| [6] | "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328; SER-330; THR-335 AND SER-336, MASS SPECTROMETRY. Tissue: Liver. |
| [7] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-346 AND SER-362, MASS SPECTROMETRY. Tissue: Melanoma. |
| [8] | "NDRG4 protein-deficient mice exhibit spatial learning deficits and vulnerabilities to cerebral ischemia." Yamamoto H., Kokame K., Okuda T., Nakajo Y., Yanamoto H., Miyata T. J. Biol. Chem. 286:26158-26165(2011) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY. |
| [9] | "Ndrg1 in development and maintenance of the myelin sheath." King R.H., Chandler D., Lopaticki S., Huang D., Blake J., Muddle J.R., Kilpatrick T., Nourallah M., Miyata T., Okuda T., Carter K.W., Hunter M., Angelicheva D., Morahan G., Kalaydjieva L. Neurobiol. Dis. 42:368-380(2011) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, CHARACTERISTICS OF A MOUSE MODEL OF CMT4D, FUNCTION, SUBCELLULAR LOCATION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U60593 mRNA. Translation: AAB03484.1. U52073 mRNA. Translation: AAB58249.1. BC015282 mRNA. Translation: AAH15282.1. BC071235 mRNA. Translation: AAH71235.1. |
| IPI | IPI00125960. |
| RefSeq | NP_032707.2. NM_008681.2. |
| UniGene | Mm.30837. |
3D structure databases | |
| ProteinModelPortal | Q62433. |
| SMR | Q62433. Positions 33-315. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q62433. 1 interaction. |
Protein family/group databases | |
| MEROPS | S33.987. |
PTM databases | |
| PhosphoSite | Q62433. |
Proteomic databases | |
| PaxDb | Q62433. |
| PRIDE | Q62433. |
Protocols and materials databases | |
| DNASU | 17988. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000005256; ENSMUSP00000005256; ENSMUSG00000005125. |
| GeneID | 17988. |
| KEGG | mmu:17988. |
Organism-specific databases | |
| CTD | 10397. |
| MGI | MGI:1341799. Ndrg1. |
Phylogenomic databases | |
| eggNOG | NOG310435. |
| GeneTree | ENSGT00390000001874. |
| HOGENOM | HOG000230891. |
| HOVERGEN | HBG052591. |
| InParanoid | Q62433. |
| OMA | LHGSIHV. |
| OrthoDB | EOG4QC15K. |
Gene expression databases | |
| ArrayExpress | Q62433. |
| Bgee | Q62433. |
| CleanEx | MM_NDRG1. |
| Genevestigator | Q62433. |
| GermOnline | ENSMUSG00000005125. Mus musculus. |
Family and domain databases | |
| InterPro | IPR004142. Ndr. [Graphical view] |
| PANTHER | PTHR11034. PTHR11034. 1 hit. |
| Pfam | PF03096. Ndr. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | NDRG1. mouse. |
| NextBio | 292963. |
| SOURCE | Search... |
Entry information
| Entry name | NDRG1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q62433 Secondary accession number(s): P97862 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
