Q9C0E8 · LNP_HUMAN
- ProteinEndoplasmic reticulum junction formation protein lunapark
- GeneLNPK
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids428 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the stabilization of nascent three-way ER tubular junctions within the ER network (PubMed:24223779, PubMed:25404289, PubMed:25548161, PubMed:27619977).
May also play a role as a curvature-stabilizing protein within the three-way ER tubular junction network (PubMed:25404289).
May be involved in limb development (By similarity).
Is involved in central nervous system development (PubMed:30032983).
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 | |||
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Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | endoplasmic reticulum tubular network | |
Cellular Component | endoplasmic reticulum tubular network membrane | |
Cellular Component | membrane | |
Cellular Component | nucleoplasm | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Biological Process | blood coagulation | |
Biological Process | embryonic digit morphogenesis | |
Biological Process | embryonic forelimb morphogenesis | |
Biological Process | endoplasmic reticulum organization | |
Biological Process | endoplasmic reticulum tubular network maintenance | |
Biological Process | endoplasmic reticulum tubular network organization | |
Biological Process | limb development | |
Biological Process | positive regulation of endoplasmic reticulum tubular network organization | |
Biological Process | regulation of chondrocyte differentiation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameEndoplasmic reticulum junction formation protein lunapark
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9C0E8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 2-45 | Cytoplasmic | ||||
Sequence: GGLFSRWRTKPSTVEVLESIDKEIQALEEFREKNQRLQKLWVGR | ||||||
Transmembrane | 46-66 | Helical | ||||
Sequence: LILYSSVLYLFTCLIVYLWYL | ||||||
Topological domain | 67-77 | Lumenal | ||||
Sequence: PDEFTARLAMT | ||||||
Transmembrane | 78-98 | Helical | ||||
Sequence: LPFFAFPLIIWSIRTVIIFFF | ||||||
Topological domain | 99-428 | Cytoplasmic | ||||
Sequence: SKRTERNNEALDDLKSQRKKILEEVMEKETYKTAKLILERFDPDSKKAKECEPPSAGAAVTARPGQEIRQRTAAQRNLSPTPASPNQGPPPQVPVSPGPPKDSSAPGGPPERTVTPALSSNVLPRHLGSPATSVPGMGLHPPGPPLARPILPRERGALDRIVEYLVGDGPQNRYALICQQCFSHNGMALKEEFEYIAFRCAYCFFLNPARKTRPQAPRLPEFSFEKRQVVEGSSSVGPLPSGSVLSSDNQFNEESLEHDVLDDNTEQTDDKIPATEQTNQVIEKASDSEEPEEKQETENEEASVIETNSTVPGADSIPDPELSGESLTAE |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Neurodevelopmental disorder with epilepsy and hypoplasia of the corpus callosum (NEDEHCC)
- Note
- DescriptionAn autosomal recessive disorder characterized by severe psychomotor delay, intellectual disability, hypotonia, epilepsy, and corpus callosum hypoplasia. Some patients show mild cerebellar hypoplasia and atrophy.
- See alsoMIM:618090
Natural variants in NEDEHCC
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_081176 | 251-428 | missing | in NEDEHCC |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2 | Abolishes myristoylation. Inhibits three-way ER tubular junction formation. Does not inhibit transmembrane domain 1-induced membrane translocation. | ||||
Sequence: G → A | ||||||
Mutagenesis | 177 | Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-179; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. | ||||
Sequence: S → A | ||||||
Mutagenesis | 177 | Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-179; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. | ||||
Sequence: S → D | ||||||
Mutagenesis | 179 | Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. | ||||
Sequence: T → A | ||||||
Mutagenesis | 179 | Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. | ||||
Sequence: T → D | ||||||
Mutagenesis | 182 | Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. | ||||
Sequence: S → A | ||||||
Mutagenesis | 182 | Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. | ||||
Sequence: S → D | ||||||
Mutagenesis | 194 | Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-202; A-211; A-213; A-218; A-227 and A-231. | ||||
Sequence: S → A | ||||||
Mutagenesis | 194 | Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-202; A-211; A-213; A-218; A-227 and A-231. | ||||
Sequence: S → D | ||||||
Mutagenesis | 202 | Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-211; A-213; A-218; A-227 and A-231. | ||||
Sequence: S → A | ||||||
Mutagenesis | 202 | Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-211; A-213; A-218; A-227 and A-231. | ||||
Sequence: S → D | ||||||
Mutagenesis | 211 | Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-213; A-218; A-227 and A-231. | ||||
Sequence: T → A | ||||||
Mutagenesis | 211 | Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-213; A-218; A-227 and A-231. | ||||
Sequence: T → D | ||||||
Mutagenesis | 213 | Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-218; A-227 and A-231. | ||||
Sequence: T → A | ||||||
Mutagenesis | 213 | Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-218; A-227 and A-231. | ||||
Sequence: T → D | ||||||
Mutagenesis | 218 | Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-227 and A-231. | ||||
Sequence: S → A | ||||||
Mutagenesis | 218 | Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-227 and A-231. | ||||
Sequence: S → D | ||||||
Mutagenesis | 227 | Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-231. | ||||
Sequence: S → A | ||||||
Mutagenesis | 227 | Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-231. | ||||
Sequence: S → D | ||||||
Mutagenesis | 231 | Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-227. | ||||
Sequence: S → A | ||||||
Mutagenesis | 231 | Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-227. | ||||
Sequence: S → D | ||||||
Natural variant | VAR_081176 | 251-428 | in NEDEHCC | |||
Sequence: Missing | ||||||
Mutagenesis | 276-301 | No change in N-myristoylation. Inhibits three-way ER tubular junction formation. | ||||
Sequence: CQQCFSHNGMALKEEFEYIAFRCAYC → AQQAFSHNGMALKEEFEYIAFRAAYA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 518 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Lipidation | 2 | UniProt | N-myristoyl glycine | ||||
Sequence: G | |||||||
Chain | PRO_0000248310 | 2-428 | UniProt | Endoplasmic reticulum junction formation protein lunapark | |||
Sequence: GGLFSRWRTKPSTVEVLESIDKEIQALEEFREKNQRLQKLWVGRLILYSSVLYLFTCLIVYLWYLPDEFTARLAMTLPFFAFPLIIWSIRTVIIFFFSKRTERNNEALDDLKSQRKKILEEVMEKETYKTAKLILERFDPDSKKAKECEPPSAGAAVTARPGQEIRQRTAAQRNLSPTPASPNQGPPPQVPVSPGPPKDSSAPGGPPERTVTPALSSNVLPRHLGSPATSVPGMGLHPPGPPLARPILPRERGALDRIVEYLVGDGPQNRYALICQQCFSHNGMALKEEFEYIAFRCAYCFFLNPARKTRPQAPRLPEFSFEKRQVVEGSSSVGPLPSGSVLSSDNQFNEESLEHDVLDDNTEQTDDKIPATEQTNQVIEKASDSEEPEEKQETENEEASVIETNSTVPGADSIPDPELSGESLTAE | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 114 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 153 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 177 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 177 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 179 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 182 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 182 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 194 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 194 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 211 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 213 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 213 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 217 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 217 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 227 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 227 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 230 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 321 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 353 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 384 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 384 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 414 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation occurs at Ser-114, Ser-153, Ser-194, Thr-211 and Ser-353 during mitosis; these phosphorylations reduce both its homodimerization and the ER three-way tubular junction formation (PubMed:27619977).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9C0E8 | SYNPR Q8TBG9 | 2 | EBI-1047206, EBI-10273251 | |
BINARY | Q9C0E8-2 | ANXA1 P04083 | 3 | EBI-11024283, EBI-354007 | |
BINARY | Q9C0E8-2 | KLHL12 Q53G59 | 6 | EBI-11024283, EBI-740929 | |
BINARY | Q9C0E8-2 | LMO3 Q8TAP4-4 | 3 | EBI-11024283, EBI-11742507 | |
BINARY | Q9C0E8-2 | NOC4L Q9BVI4 | 3 | EBI-11024283, EBI-395927 | |
BINARY | Q9C0E8-2 | PAX6 P26367 | 3 | EBI-11024283, EBI-747278 | |
BINARY | Q9C0E8-2 | PLIN3 O60664 | 3 | EBI-11024283, EBI-725795 | |
BINARY | Q9C0E8-2 | SYP P08247 | 3 | EBI-11024283, EBI-9071725 | |
BINARY | Q9C0E8-2 | YIF1A O95070 | 3 | EBI-11024283, EBI-2799703 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for coiled coil, region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 16-41 | |||||
Sequence: EVLESIDKEIQALEEFREKNQRLQKL | ||||||
Coiled coil | 102-128 | |||||
Sequence: TERNNEALDDLKSQRKKILEEVMEKET | ||||||
Region | 143-247 | Disordered | ||||
Sequence: SKKAKECEPPSAGAAVTARPGQEIRQRTAAQRNLSPTPASPNQGPPPQVPVSPGPPKDSSAPGGPPERTVTPALSSNVLPRHLGSPATSVPGMGLHPPGPPLARP | ||||||
Compositional bias | 166-180 | Polar residues | ||||
Sequence: IRQRTAAQRNLSPTP | ||||||
Compositional bias | 181-204 | Pro residues | ||||
Sequence: ASPNQGPPPQVPVSPGPPKDSSAP | ||||||
Zinc finger | 276-301 | C4-type; plays a role in ER morphology | ||||
Sequence: CQQCFSHNGMALKEEFEYIAFRCAYC | ||||||
Region | 356-428 | Disordered | ||||
Sequence: HDVLDDNTEQTDDKIPATEQTNQVIEKASDSEEPEEKQETENEEASVIETNSTVPGADSIPDPELSGESLTAE |
Domain
Transmembrane domain 1 and 2 are probably sufficient to mediate membrane translocation and topology formation in a N-myristoylation-independent manner (PubMed:24223779).
Transmembrane domain 2 is sufficient to block the protein secretion pathway (PubMed:24223779).
The two coiled-coil domains are necessary for its endoplasmic reticulum (ER) three-way tubular junction localization (PubMed:27619977).
The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation (PubMed:24223779, PubMed:27619977).
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q9C0E8-1
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
- Length428
- Mass (Da)47,740
- Last updated2006-09-05 v2
- ChecksumF5BBA4186C2691BF
Q9C0E8-2
- Name2
- Differences from canonical
- 1-9: MGGLFSRWR → MEGK
Q9C0E8-3
- Name3
- Differences from canonical
- 1-123: Missing
Q9C0E8-4
- Name4
- Differences from canonical
- 235-235: M → MEMGLPHIAQAGLEHLSSSDLSTSTSQSAGIT
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_020239 | 1-9 | in isoform 2 | |||
Sequence: MGGLFSRWR → MEGK | ||||||
Alternative sequence | VSP_020238 | 1-123 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 166-180 | Polar residues | ||||
Sequence: IRQRTAAQRNLSPTP | ||||||
Compositional bias | 181-204 | Pro residues | ||||
Sequence: ASPNQGPPPQVPVSPGPPKDSSAP | ||||||
Alternative sequence | VSP_054427 | 235 | in isoform 4 | |||
Sequence: M → MEMGLPHIAQAGLEHLSSSDLSTSTSQSAGIT | ||||||
Sequence conflict | 262 | in Ref. 2; BAB71207 | ||||
Sequence: Y → H | ||||||
Sequence conflict | 374 | in Ref. 4; AAH31530 | ||||
Sequence: E → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB051502 EMBL· GenBank· DDBJ | BAB21806.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK056532 EMBL· GenBank· DDBJ | BAB71207.1 EMBL· GenBank· DDBJ | mRNA | ||
AC016751 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC016915 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC031530 EMBL· GenBank· DDBJ | AAH31530.1 EMBL· GenBank· DDBJ | mRNA | ||
BC105132 EMBL· GenBank· DDBJ | AAI05133.1 EMBL· GenBank· DDBJ | mRNA | ||
BC105134 EMBL· GenBank· DDBJ | AAI05135.1 EMBL· GenBank· DDBJ | mRNA | ||
BC110329 EMBL· GenBank· DDBJ | AAI10330.1 EMBL· GenBank· DDBJ | mRNA | ||
BC143681 EMBL· GenBank· DDBJ | AAI43682.1 EMBL· GenBank· DDBJ | mRNA | ||
AL832947 EMBL· GenBank· DDBJ | CAH56306.1 EMBL· GenBank· DDBJ | mRNA |