Q92597 · NDRG1_HUMAN
- ProteinProtein NDRG1
- GeneNDRG1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids394 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. 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. 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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | adherens junction | |
Cellular Component | centrosome | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | microtubule | |
Cellular Component | microtubule cytoskeleton | |
Cellular Component | nucleus | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | recycling endosome membrane | |
Molecular Function | cadherin binding | |
Molecular Function | gamma-tubulin binding | |
Molecular Function | microtubule binding | |
Molecular Function | small GTPase binding | |
Biological Process | cellular response to hypoxia | |
Biological Process | DNA damage response, signal transduction by p53 class mediator | |
Biological Process | mast cell activation | |
Biological Process | negative regulation of cell population proliferation | |
Biological Process | peripheral nervous system myelin maintenance | |
Biological Process | response to metal ion | |
Biological Process | signal transduction |
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProtein NDRG1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ92597
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Charcot-Marie-Tooth disease 4D (CMT4D)
- Note
- DescriptionA recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie-Tooth disease are designated CMT4.
- See alsoMIM:601455
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_050234 | 67 | in dbSNP:rs2233319 | |||
Sequence: M → V | ||||||
Natural variant | VAR_050235 | 111 | in dbSNP:rs2233328 | |||
Sequence: M → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 553 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, modified residue (large scale data), chain.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Modified residue | 2 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000159573 | 2-394 | UniProt | Protein NDRG1 | |||
Sequence: SREMQDVDLAEVKPLVEKGETITGLLQEFDVQEQDIETLHGSVHVTLCGTPKGNRPVILTYHDIGMNHKTCYNPLFNYEDMQEITQHFAVCHVDAPGQQDGAASFPAGYMYPSMDQLAEMLPGVLQQFGLKSIIGMGTGAGAYILTRFALNNPEMVEGLVLINVNPCAEGWMDWAASKISGWTQALPDMVVSHLFGKEEMQSNVEVVHTYRQHIVNDMNPGNLHLFINAYNSRRDLEIERPMPGTHTVTLQCPALLVVGDSSPAVDAVVECNSKLDPTKTTLLKMADCGGLPQISQPAKLAEAFKYFVQGMGYMPSASMTRLMRSRTASGSSVTSLDGTRSRSHTSEGTRSRSHTSEGTRSRSHTSEGAHLDITPNSGAAGNSAGPKSMEVSC | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 319 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 319 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 326 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 326 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 328 | UniProt | Phosphothreonine; by SGK1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 328 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 330 | UniProt | Phosphoserine; by SGK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 330 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 332 | UniProt | Phosphoserine; by SGK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 332 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 333 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 333 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 335 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 335 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 336 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 336 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 340 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 340 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 342 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 342 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 344 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 346 | UniProt | Phosphothreonine; by SGK1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 346 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 352 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 352 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 354 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 356 | UniProt | Phosphothreonine; by SGK1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 356 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 362 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 362 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 364 | UniProt | Phosphoserine; by SGK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 364 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 366 | UniProt | Phosphothreonine; by SGK1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 366 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 367 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 375 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 375 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 378 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 384 | PRIDE | Phosphoserine | ||||
Sequence: S |
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.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous; expressed most prominently in placental membranes and prostate, kidney, small intestine, and ovary tissues. Also expressed in heart, brain, skeletal muscle, lung, liver and pancreas. Low levels in peripheral blood leukocytes and in tissues of the immune system. Expressed mainly in epithelial cells. Also found in Schwann cells of peripheral neurons. Reduced expression in adenocarcinomas compared to normal tissues. In colon, prostate and placental membranes, the cells that border the lumen show the highest expression.
Induction
By homocysteine, 2-mercaptoethanol, tunicamycin in endothelial cells. Induced approximately 20-fold during in vitro differentiation of the colon carcinoma cell lines HT-29-D4 and Caco-2. Induced by oxidative stress in colon cancers. Decreased expression in colon adenomas and adenocarcinomas. Induced by nickel compounds in all tested cell lines. The primary signal for its induction is an elevation of free intracellular calcium ion caused by nickel ion exposure. Okadaic acid, a serine/threonine phosphatase inhibitor, induced its expression more rapidly and more efficiently than nickel.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with RAB4A (membrane-bound form); the interaction involves NDRG1 in vesicular recycling of CDH1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q92597 | ATP1A1 P05023 | 2 | EBI-716486, EBI-358778 | |
BINARY | Q92597 | CANX P27824 | 2 | EBI-716486, EBI-355947 | |
BINARY | Q92597 | CSTPP1 Q9H6J7-2 | 3 | EBI-716486, EBI-13328871 | |
BINARY | Q92597 | CTNNB1 P35222 | 3 | EBI-716486, EBI-491549 | |
BINARY | Q92597 | DCLRE1B Q9H816 | 3 | EBI-716486, EBI-3508943 | |
BINARY | Q92597 | FOXD4L6 Q3SYB3 | 3 | EBI-716486, EBI-6425864 | |
BINARY | Q92597 | LDHAL6B Q9BYZ2 | 3 | EBI-716486, EBI-1108377 | |
BINARY | Q92597 | MED28 Q9H204 | 3 | EBI-716486, EBI-514199 | |
BINARY | Q92597 | MSRB2 Q9Y3D2 | 3 | EBI-716486, EBI-9092052 | |
BINARY | Q92597 | RNF111 Q6ZNA4-2 | 3 | EBI-716486, EBI-21535400 | |
BINARY | Q92597 | RYBP Q8N488 | 3 | EBI-716486, EBI-752324 | |
BINARY | Q92597 | SAP30 O75446 | 3 | EBI-716486, EBI-632609 | |
BINARY | Q92597 | SPAG8 Q99932-2 | 3 | EBI-716486, EBI-11959123 | |
BINARY | Q92597 | SPATA2L Q8IUW3 | 3 | EBI-716486, EBI-2510414 | |
BINARY | Q92597 | TTC33 Q6PID6 | 3 | EBI-716486, EBI-2555404 | |
BINARY | Q92597 | XRCC6 P12956 | 2 | EBI-716486, EBI-353208 | |
BINARY | Q92597 | ZMAT2 Q96NC0 | 3 | EBI-716486, EBI-2682299 | |
BINARY | Q92597-3 | AK6 Q9Y3D8 | 3 | EBI-10278703, EBI-2896123 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 325-343 | Polar residues | ||||
Sequence: RSRTASGSSVTSLDGTRSR | ||||||
Region | 325-394 | Disordered | ||||
Sequence: RSRTASGSSVTSLDGTRSRSHTSEGTRSRSHTSEGTRSRSHTSEGAHLDITPNSGAAGNSAGPKSMEVSC | ||||||
Repeat | 339-348 | 1 | ||||
Sequence: GTRSRSHTSE | ||||||
Region | 339-368 | 3 X 10 AA tandem repeats of G-T-R-S-R-S-H-T-S-E | ||||
Sequence: GTRSRSHTSEGTRSRSHTSEGTRSRSHTSE | ||||||
Compositional bias | 344-368 | Basic and acidic residues | ||||
Sequence: SHTSEGTRSRSHTSEGTRSRSHTSE | ||||||
Repeat | 349-358 | 2 | ||||
Sequence: GTRSRSHTSE | ||||||
Repeat | 359-368 | 3 | ||||
Sequence: GTRSRSHTSE | ||||||
Compositional bias | 369-394 | Polar residues | ||||
Sequence: GAHLDITPNSGAAGNSAGPKSMEVSC |
Sequence similarities
Belongs to the NDRG family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q92597-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length394
- Mass (Da)42,835
- Last updated1997-02-01 v1
- Checksum4C816B9C85E3756F
Q92597-2
- Name2
- Differences from canonical
- 1-66: Missing
Q92597-3
- Name3
- Differences from canonical
- 1-81: Missing
Computationally mapped potential isoform sequences
There are 26 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A6Q8PFG2 | A0A6Q8PFG2_HUMAN | NDRG1 | 68 | ||
A0A6Q8PFB3 | A0A6Q8PFB3_HUMAN | NDRG1 | 34 | ||
A0A6Q8PFR8 | A0A6Q8PFR8_HUMAN | NDRG1 | 40 | ||
A0A6Q8PFP2 | A0A6Q8PFP2_HUMAN | NDRG1 | 62 | ||
A0A6Q8PGD3 | A0A6Q8PGD3_HUMAN | NDRG1 | 56 | ||
A0A6Q8PGJ1 | A0A6Q8PGJ1_HUMAN | NDRG1 | 26 | ||
A0A6Q8PGF1 | A0A6Q8PGF1_HUMAN | NDRG1 | 35 | ||
A0A6Q8PF28 | A0A6Q8PF28_HUMAN | NDRG1 | 65 | ||
A0A6Q8PF71 | A0A6Q8PF71_HUMAN | NDRG1 | 57 | ||
A0A6Q8PF06 | A0A6Q8PF06_HUMAN | NDRG1 | 28 | ||
A0A6Q8PF16 | A0A6Q8PF16_HUMAN | NDRG1 | 120 | ||
E7ESM1 | E7ESM1_HUMAN | NDRG1 | 141 | ||
A0A6Q8PHF2 | A0A6Q8PHF2_HUMAN | NDRG1 | 21 | ||
A0A6Q8PHI0 | A0A6Q8PHI0_HUMAN | NDRG1 | 101 | ||
A0A7I2ST14 | A0A7I2ST14_HUMAN | NDRG1 | 387 | ||
E5RIM2 | E5RIM2_HUMAN | NDRG1 | 216 | ||
E5RJ98 | E5RJ98_HUMAN | NDRG1 | 95 | ||
E5RIV1 | E5RIV1_HUMAN | NDRG1 | 193 | ||
E5RIR1 | E5RIR1_HUMAN | NDRG1 | 158 | ||
E5RK17 | E5RK17_HUMAN | NDRG1 | 167 | ||
E5RJY1 | E5RJY1_HUMAN | NDRG1 | 103 | ||
E5RG99 | E5RG99_HUMAN | NDRG1 | 100 | ||
E5RGG6 | E5RGG6_HUMAN | NDRG1 | 42 | ||
E5RGM5 | E5RGM5_HUMAN | NDRG1 | 165 | ||
E5RH82 | E5RH82_HUMAN | NDRG1 | 156 | ||
E5RI76 | E5RI76_HUMAN | NDRG1 | 133 |
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_045038 | 1-66 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_045037 | 1-81 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 145 | in Ref. 2; CAA63430 | ||||
Sequence: I → T | ||||||
Compositional bias | 325-343 | Polar residues | ||||
Sequence: RSRTASGSSVTSLDGTRSR | ||||||
Compositional bias | 344-368 | Basic and acidic residues | ||||
Sequence: SHTSEGTRSRSHTSEGTRSRSHTSE | ||||||
Compositional bias | 369-394 | Polar residues | ||||
Sequence: GAHLDITPNSGAAGNSAGPKSMEVSC |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D87953 EMBL· GenBank· DDBJ | BAA13505.1 EMBL· GenBank· DDBJ | mRNA | ||
X92845 EMBL· GenBank· DDBJ | CAA63430.1 EMBL· GenBank· DDBJ | mRNA | ||
AF004162 EMBL· GenBank· DDBJ | AAC13419.1 EMBL· GenBank· DDBJ | mRNA | ||
AF186190 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CR456842 EMBL· GenBank· DDBJ | CAG33123.1 EMBL· GenBank· DDBJ | mRNA | ||
AK091147 EMBL· GenBank· DDBJ | BAG52292.1 EMBL· GenBank· DDBJ | mRNA | ||
AK126924 EMBL· GenBank· DDBJ | BAG54400.1 EMBL· GenBank· DDBJ | mRNA | ||
AK296794 EMBL· GenBank· DDBJ | BAH12432.1 EMBL· GenBank· DDBJ | mRNA | ||
AF192304 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471060 EMBL· GenBank· DDBJ | EAW92164.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003175 EMBL· GenBank· DDBJ | AAH03175.1 EMBL· GenBank· DDBJ | mRNA | ||
AF230380 EMBL· GenBank· DDBJ | AAF71305.1 EMBL· GenBank· DDBJ | mRNA |