Q12929 · EPS8_HUMAN
- ProteinEpidermal growth factor receptor kinase substrate 8
- GeneEPS8
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids822 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture. Depending on its association with other signal transducers, can regulate different processes. Together with SOS1 and ABI1, forms a trimeric complex that participates in transduction of signals from Ras to Rac by activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. Acts as a direct regulator of actin dynamics by binding actin filaments and has both barbed-end actin filament capping and actin bundling activities depending on the context. Displays barbed-end actin capping activity when associated with ABI1, thereby regulating actin-based motility process: capping activity is auto-inhibited and inhibition is relieved upon ABI1 interaction. Also shows actin bundling activity when associated with BAIAP2, enhancing BAIAP2-dependent membrane extensions and promoting filopodial protrusions. Involved in the regulation of processes such as axonal filopodia growth, stereocilia length, dendritic cell migration and cancer cell migration and invasion. Acts as a regulator of axonal filopodia formation in neurons: in the absence of neurotrophic factors, negatively regulates axonal filopodia formation via actin-capping activity. In contrast, it is phosphorylated in the presence of BDNF leading to inhibition of its actin-capping activity and stimulation of filopodia formation. Component of a complex with WHRN and MYO15A that localizes at stereocilia tips and is required for elongation of the stereocilia actin core. Indirectly involved in cell cycle progression; its degradation following ubiquitination being required during G2 phase to promote cell shape changes.
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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Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEpidermal growth factor receptor kinase substrate 8
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ12929
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes at the tips of the stereocilia of the inner and outer hair cells (By similarity).
Localizes to the midzone of dividing cells
Localizes to the midzone of dividing cells
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Deafness, autosomal recessive, 102 (DFNB102)
- Note
- DescriptionA form of non-syndromic deafness characterized by profound hearing loss affecting all frequencies. Vestibular function is unaffected.
- See alsoMIM:615974
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_050971 | 761 | in dbSNP:rs7137185 | |||
Sequence: D → E | ||||||
Natural variant | VAR_050972 | 806 | in dbSNP:rs1802658 | |||
Sequence: A → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,012 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 chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000086994 | 1-822 | UniProt | Epidermal growth factor receptor kinase substrate 8 | |||
Sequence: MNGHISNHPSSFGMYPSQMNGYGSSPTFSQTDREHGSKTSAKALYEQRKNYARDSVSSVSDISQYRVEHLTTFVLDRKDAMITVDDGIRKLKLLDAKGKVWTQDMILQVDDRAVSLIDLESKNELENFPLNTIQHCQAVMHSCSYDSVLALVCKEPTQNKPDLHLFQCDEVKANLISEDIESAISDSKGGKQKRRPDALRMISNADPSIPPPPRAPAPAPPGTVTQVDVRSRVAAWSAWAADQGDFEKPRQYHEQEETPEMMAARIDRDVQILNHILDDIEFFITKLQKAAEAFSELSKRKKNKKGKRKGPGEGVLTLRAKPPPPDEFLDCFQKFKHGFNLLAKLKSHIQNPSAADLVHFLFTPLNMVVQATGGPELASSVLSPLLNKDTIDFLNYTVNGDERQLWMSLGGTWMKARAEWPKEQFIPPYVPRFRNGWEPPMLNFMGATMEQDLYQLAESVANVAEHQRKQEIKRLSTEHSSVSEYHPADGYAFSSNIYTRGSHLDQGEAAVAFKPTSNRHIDRNYEPLKTQPKKYAKSKYDFVARNNSELSVLKDDILEILDDRKQWWKVRNASGDSGFVPNNILDIVRPPESGLGRADPPYTHTIQKQRMEYGPRPADTPPAPSPPPTPAPVPVPLPPSTPAPVPVSKVPANITRQNSSSSDSGGSIVRDSQRHKQLPVDRRKSQMEEVQDELIHRLTIGRSAAQKKFHVPRQNVPVINITYDSTPEDVKTWLQSKGFNPVTVNSLGVLNGAQLFSLNKDELRTVCPEGARVYSQITVQKAALEDSSGSSELQEIMRRRQEKISAAASDSGVESFDEGSSH | |||||||
Modified residue (large scale data) | 55 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 58 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 58 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 223 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 223 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 252 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 298 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 317 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 317 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 476 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 476 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 485 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 491 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 498 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 516 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 517 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 525 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 574 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 602 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 605 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 620 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 625 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 625 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 629 | UniProt | Phosphothreonine; by MAPK | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 629 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 655 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 659 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 659 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 660 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 661 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 662 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 662 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 664 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 667 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 672 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 685 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 685 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 699 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 723 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 774 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 809 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 811 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 811 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 815 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 815 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 820 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 821 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Ubiquitinated by the SCF(FBXW5) E3 ubiquitin-protein ligase complex during G2 phase, leading to its transient degradation and subsequent cell shape changes required to allow mitotic progression. Reappears at the midzone of dividing cells (By similarity).
Phosphorylation at Ser-625 and Thr-629 by MAPK following BDNF treatment promotes removal from actin and filopodia formation (By similarity).
Phosphorylated by several receptor tyrosine kinases
Phosphorylated by several receptor tyrosine kinases
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in all tissues analyzed, including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Expressed in all epithelial and fibroblastic lines examined and in some, but not all, hematopoietic cells.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer. Part of a complex consisting of ABI1, EPS8 and SOS1. Interacts with MYO15A and WHRN. Interacts with LANCL1 (By similarity).
Interacts with EGFR; mediates EPS8 phosphorylation (By similarity).
Interacts with BAIAP2. Interacts with SHB
Interacts with EGFR; mediates EPS8 phosphorylation (By similarity).
Interacts with BAIAP2. Interacts with SHB
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q12929 | ALDH7A1 P49419 | 2 | EBI-375576, EBI-726842 | |
BINARY | Q12929 | BAIAP2 Q9UQB8 | 12 | EBI-375576, EBI-525456 | |
BINARY | Q12929 | BAIAP2 Q9UQB8-4 | 4 | EBI-375576, EBI-6174091 | |
BINARY | Q12929 | BAIAP2L1 Q9UHR4 | 4 | EBI-375576, EBI-2483278 | |
BINARY | Q12929 | BORCS6 Q96GS4 | 3 | EBI-375576, EBI-10193358 | |
BINARY | Q12929 | BYSL Q13895 | 3 | EBI-375576, EBI-358049 | |
BINARY | Q12929 | C19orf25 Q9UFG5 | 3 | EBI-375576, EBI-741214 | |
BINARY | Q12929 | CASK O14936 | 3 | EBI-375576, EBI-1215506 | |
BINARY | Q12929 | EGFR P00533 | 4 | EBI-375576, EBI-297353 | |
BINARY | Q12929 | FBXW5 Q969U6-1 | 3 | EBI-375576, EBI-16031873 | |
BINARY | Q12929 | GOLGA8DP Q0D2H9 | 3 | EBI-375576, EBI-10181276 | |
BINARY | Q12929 | GRB2 P62993 | 3 | EBI-375576, EBI-401755 | |
BINARY | Q12929 | HNRNPC P07910 | 3 | EBI-375576, EBI-357966 | |
BINARY | Q12929 | INPP5J Q15735 | 3 | EBI-375576, EBI-10236940 | |
BINARY | Q12929 | RUNX1T1 Q06455-4 | 3 | EBI-375576, EBI-10224192 | |
BINARY | Q12929 | SMARCE1 Q969G3 | 3 | EBI-375576, EBI-455078 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-34 | Polar residues | ||||
Sequence: MNGHISNHPSSFGMYPSQMNGYGSSPTFSQTDRE | ||||||
Region | 1-39 | Disordered | ||||
Sequence: MNGHISNHPSSFGMYPSQMNGYGSSPTFSQTDREHGSKT | ||||||
Domain | 64-194 | PTB | ||||
Sequence: QYRVEHLTTFVLDRKDAMITVDDGIRKLKLLDAKGKVWTQDMILQVDDRAVSLIDLESKNELENFPLNTIQHCQAVMHSCSYDSVLALVCKEPTQNKPDLHLFQCDEVKANLISEDIESAISDSKGGKQKR | ||||||
Region | 202-225 | Disordered | ||||
Sequence: ISNADPSIPPPPRAPAPAPPGTVT | ||||||
Compositional bias | 206-220 | Pro residues | ||||
Sequence: DPSIPPPPRAPAPAP | ||||||
Region | 298-320 | Disordered | ||||
Sequence: SKRKKNKKGKRKGPGEGVLTLRA | ||||||
Domain | 531-590 | SH3 | ||||
Sequence: QPKKYAKSKYDFVARNNSELSVLKDDILEILDDRKQWWKVRNASGDSGFVPNNILDIVRP | ||||||
Region | 612-689 | Disordered | ||||
Sequence: EYGPRPADTPPAPSPPPTPAPVPVPLPPSTPAPVPVSKVPANITRQNSSSSDSGGSIVRDSQRHKQLPVDRRKSQMEE | ||||||
Compositional bias | 617-646 | Pro residues | ||||
Sequence: PADTPPAPSPPPTPAPVPVPLPPSTPAPVP | ||||||
Region | 649-822 | Effector region | ||||
Sequence: KVPANITRQNSSSSDSGGSIVRDSQRHKQLPVDRRKSQMEEVQDELIHRLTIGRSAAQKKFHVPRQNVPVINITYDSTPEDVKTWLQSKGFNPVTVNSLGVLNGAQLFSLNKDELRTVCPEGARVYSQITVQKAALEDSSGSSELQEIMRRRQEKISAAASDSGVESFDEGSSH | ||||||
Compositional bias | 651-668 | Polar residues | ||||
Sequence: PANITRQNSSSSDSGGSI | ||||||
Compositional bias | 674-689 | Basic and acidic residues | ||||
Sequence: RHKQLPVDRRKSQMEE | ||||||
Region | 680-698 | Amphipathic helix | ||||
Sequence: VDRRKSQMEEVQDELIHRL | ||||||
Region | 718-738 | Helix bundle 1 | ||||
Sequence: VINITYDSTPEDVKTWLQSKG | ||||||
Region | 752-757 | Helix bundle 2 | ||||
Sequence: GAQLFS | ||||||
Region | 762-767 | Helix bundle 3 | ||||
Sequence: ELRTVC | ||||||
Region | 766-785 | Helix bundle 4 | ||||
Sequence: VCPEGARVYSQITVQKAALE | ||||||
Region | 787-822 | Disordered | ||||
Sequence: SSGSSELQEIMRRRQEKISAAASDSGVESFDEGSSH |
Domain
The effector region is required for activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. It mediates both barbed-end actin capping and actin bundling activities. The capping activity is mediated by an amphipathic helix that binds within the hydrophobic pocket at the barbed ends of actin blocking further addition of actin monomers, while the bundling activity is mediated by a compact 4 helix bundle, which contacts 3 actin subunits along the filament (By similarity).
The SH3 domain mediates interaction with SHB.
Sequence similarities
Belongs to the EPS8 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q12929-1
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
- Length822
- Mass (Da)91,882
- Last updated1996-11-01 v1
- ChecksumAC5EB1D28B784B3B
Q12929-2
- Name2
- Differences from canonical
- 1-260: Missing
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8Y4W2 | A0A2R8Y4W2_HUMAN | EPS8 | 830 | ||
A0A2R8YE63 | A0A2R8YE63_HUMAN | EPS8 | 839 | ||
H0YFG1 | H0YFG1_HUMAN | EPS8 | 68 | ||
F5GYM8 | F5GYM8_HUMAN | EPS8 | 120 | ||
F5H714 | F5H714_HUMAN | EPS8 | 41 | ||
F5H3Q6 | F5H3Q6_HUMAN | EPS8 | 128 | ||
F5H0R8 | F5H0R8_HUMAN | EPS8 | 200 | ||
F5H2B8 | F5H2B8_HUMAN | EPS8 | 68 | ||
F5H1B5 | F5H1B5_HUMAN | EPS8 | 67 |
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-34 | Polar residues | ||||
Sequence: MNGHISNHPSSFGMYPSQMNGYGSSPTFSQTDRE | ||||||
Alternative sequence | VSP_056460 | 1-260 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 73 | in Ref. 2; BAF84466 | ||||
Sequence: F → S | ||||||
Sequence conflict | 128 | in Ref. 2; BAF84466 | ||||
Sequence: F → S | ||||||
Sequence conflict | 194 | in Ref. 2; BAF84466 | ||||
Sequence: R → G | ||||||
Sequence conflict | 205 | in Ref. 2; BAF85620 | ||||
Sequence: A → S | ||||||
Compositional bias | 206-220 | Pro residues | ||||
Sequence: DPSIPPPPRAPAPAP | ||||||
Sequence conflict | 497 | in Ref. 2; BAF85620 | ||||
Sequence: I → V | ||||||
Compositional bias | 617-646 | Pro residues | ||||
Sequence: PADTPPAPSPPPTPAPVPVPLPPSTPAPVP | ||||||
Sequence conflict | 631 | in Ref. 5; AAH30010 | ||||
Sequence: A → V | ||||||
Compositional bias | 651-668 | Polar residues | ||||
Sequence: PANITRQNSSSSDSGGSI | ||||||
Compositional bias | 674-689 | Basic and acidic residues | ||||
Sequence: RHKQLPVDRRKSQMEE | ||||||
Sequence conflict | 705 | in Ref. 2; BAF85620 | ||||
Sequence: A → T |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U12535 EMBL· GenBank· DDBJ | AAA62280.1 EMBL· GenBank· DDBJ | mRNA | ||
AK291777 EMBL· GenBank· DDBJ | BAF84466.1 EMBL· GenBank· DDBJ | mRNA | ||
AK292931 EMBL· GenBank· DDBJ | BAF85620.1 EMBL· GenBank· DDBJ | mRNA | ||
AK301834 EMBL· GenBank· DDBJ | BAG63278.1 EMBL· GenBank· DDBJ | mRNA | ||
AK316134 EMBL· GenBank· DDBJ | BAH14505.1 EMBL· GenBank· DDBJ | mRNA | ||
AK316239 EMBL· GenBank· DDBJ | BAH14610.1 EMBL· GenBank· DDBJ | mRNA | ||
AC022073 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC073651 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC092753 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471094 EMBL· GenBank· DDBJ | EAW96354.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471094 EMBL· GenBank· DDBJ | EAW96355.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC030010 EMBL· GenBank· DDBJ | AAH30010.1 EMBL· GenBank· DDBJ | mRNA |