O14965 · AURKA_HUMAN
- ProteinAurora kinase A
- GeneAURKA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids403 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression (PubMed:11039908, PubMed:12390251, PubMed:17125279, PubMed:17360485, PubMed:18615013, PubMed:26246606).
Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis (PubMed:14523000, PubMed:26246606).
Required for normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase (PubMed:27335426).
Required for initial activation of CDK1 at centrosomes (PubMed:13678582, PubMed:15128871).
Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2 (PubMed:11551964, PubMed:14702041, PubMed:15128871, PubMed:15147269, PubMed:15987997, PubMed:17604723, PubMed:18056443, PubMed:18615013).
Regulates KIF2A tubulin depolymerase activity (PubMed:19351716).
Important for microtubule formation and/or stabilization (PubMed:18056443).
Required for normal axon formation (PubMed:19812038).
Plays a role in microtubule remodeling during neurite extension (PubMed:19668197).
Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and destabilizing p53/TP53 (PubMed:14702041).
Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity (PubMed:11551964).
Inhibits cilia outgrowth (By similarity).
Required for cilia disassembly via phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (PubMed:17604723, PubMed:20643351).
Regulates protein levels of the anti-apoptosis protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through the phosphorylation of the transcription factor FOXP1 (PubMed:28218735).
Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis (PubMed:14523000, PubMed:26246606).
Required for normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase (PubMed:27335426).
Required for initial activation of CDK1 at centrosomes (PubMed:13678582, PubMed:15128871).
Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2 (PubMed:11551964, PubMed:14702041, PubMed:15128871, PubMed:15147269, PubMed:15987997, PubMed:17604723, PubMed:18056443, PubMed:18615013).
Regulates KIF2A tubulin depolymerase activity (PubMed:19351716).
Important for microtubule formation and/or stabilization (PubMed:18056443).
Required for normal axon formation (PubMed:19812038).
Plays a role in microtubule remodeling during neurite extension (PubMed:19668197).
Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and destabilizing p53/TP53 (PubMed:14702041).
Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity (PubMed:11551964).
Inhibits cilia outgrowth (By similarity).
Required for cilia disassembly via phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (PubMed:17604723, PubMed:20643351).
Regulates protein levels of the anti-apoptosis protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through the phosphorylation of the transcription factor FOXP1 (PubMed:28218735).
Miscellaneous
Centrosome amplification can occur when the cycles are uncoupled, and this amplification is associated with cancer and with an increase in the levels of chromosomal instability.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Activation of CDK1, appears to be an upstream event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2 act also as activators. Inactivated by the G2 checkpoint. Inhibited by GADD45A and p53/TP53, and through dephosphorylation by protein phosphatase type 1 (PP1). MLN8054 is also a potent and selective inhibitor. Activated during the early phase of cilia disassembly in the presence of CIMAP3. Inhibited by the small molecule inhibitor VX-680 (PubMed:28218735).
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 143 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 162 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 211-213 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EYA | ||||||
Active site | 256 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 260-261 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EN | ||||||
Binding site | 274 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAurora kinase A
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO14965
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Detected at the neurite hillock in developing neurons (By similarity).
Localizes at the centrosome in mitotic cells from early prophase until telophase, but also localizes to the spindle pole MTs from prophase to anaphase (PubMed:17229885, PubMed:21225229, PubMed:9606188).
Colocalized with SIRT2 at centrosome (PubMed:22014574).
Moves to the midbody during both telophase and cytokinesis (PubMed:17726514).
Associates with both the pericentriolar material (PCM) and centrioles (PubMed:22014574).
The localization to the spindle poles is regulated by AAAS (PubMed:26246606).
Localizes at the centrosome in mitotic cells from early prophase until telophase, but also localizes to the spindle pole MTs from prophase to anaphase (PubMed:17229885, PubMed:21225229, PubMed:9606188).
Colocalized with SIRT2 at centrosome (PubMed:22014574).
Moves to the midbody during both telophase and cytokinesis (PubMed:17726514).
Associates with both the pericentriolar material (PCM) and centrioles (PubMed:22014574).
The localization to the spindle poles is regulated by AAAS (PubMed:26246606).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_030840 | 11 | in dbSNP:rs6069717 | |||
Sequence: G → R | ||||||
Natural variant | VAR_030841 | 31 | in dbSNP:rs2273535 | |||
Sequence: F → I | ||||||
Natural variant | VAR_041127 | 50 | in dbSNP:rs34572020 | |||
Sequence: P → L | ||||||
Natural variant | VAR_030842 | 57 | increased kinase activity; dbSNP:rs1047972 | |||
Sequence: I → V | ||||||
Natural variant | VAR_061745 | 104 | in dbSNP:rs2230743 | |||
Sequence: S → L | ||||||
Natural variant | VAR_041128 | 155 | in a colorectal adenocarcinoma sample; somatic mutation; reduces interaction with TPX2 | |||
Sequence: S → R | ||||||
Mutagenesis | 162 | Loss of kinase activity. | ||||
Sequence: K → R | ||||||
Mutagenesis | 165 | Decreases the interaction with phosphatase type 1 isoforms. | ||||
Sequence: F → A | ||||||
Natural variant | VAR_041129 | 174 | in a metastatic melanoma sample; somatic mutation; constitutively enhanced kinase activity | |||
Sequence: V → M | ||||||
Mutagenesis | 198 | Reduces interaction with TPX2. Reduces kinase activity tenfold. Promotes interaction with the AURKB binding partners INCENP and BIRC5 that are normally not bound by AURKA. | ||||
Sequence: G → N | ||||||
Mutagenesis | 205 | Reduces ubiquitination and proteasomal degradation. | ||||
Sequence: R → A | ||||||
Mutagenesis | 274 | Abolishes cilia disassembly and kinase activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 287 | No direct effect on catalytic activity. | ||||
Sequence: T → A | ||||||
Mutagenesis | 287 | Enhances interaction with TPX2. | ||||
Sequence: T → E | ||||||
Mutagenesis | 288 | Reduces cilia disassembly and kinase activity. | ||||
Sequence: T → A | ||||||
Mutagenesis | 288 | Mimics phosphorylation state and increases kinase activity. | ||||
Sequence: T → D | ||||||
Mutagenesis | 290 | Enhances stability; when associated with A-393. | ||||
Sequence: C → A | ||||||
Mutagenesis | 334 | Reduces binding to MYCN. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 335 | Reduces binding to MYCN. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 346 | Decreases the interaction with phosphatase type 1 isoforms. | ||||
Sequence: F → A | ||||||
Natural variant | VAR_041130 | 373 | in dbSNP:rs33923703 | |||
Sequence: M → V | ||||||
Mutagenesis | 393 | Enhances stability; when associated with A-290. | ||||
Sequence: C → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 729 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 chain, modified residue, cross-link, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000086692 | 1-403 | UniProt | Aurora kinase A | |||
Sequence: MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRIPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSSKPSNCQNKESASKQS | |||||||
Modified residue | 41 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 51 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 258 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 287 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 288 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 288 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 342 | UniProt | Phosphoserine; by PKA and PAK | ||||
Sequence: S |
Post-translational modification
Activated by phosphorylation at Thr-288; this brings about a change in the conformation of the activation segment. Phosphorylation at Thr-288 varies during the cell cycle and is highest during M phase. Autophosphorylated at Thr-288 upon TPX2 binding. Thr-288 can be phosphorylated by several kinases, including PAK and PKA. Protein phosphatase type 1 (PP1) binds AURKA and inhibits its activity by dephosphorylating Thr-288 during mitosis. Phosphorylation at Ser-342 decreases the kinase activity. PPP2CA controls degradation by dephosphorylating Ser-51 at the end of mitosis.
Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL7) during mitosis, leading to its degradation by the proteasome (By similarity).
Ubiquitinated by CHFR, leading to its degradation by the proteasome (By similarity).
Ubiquitinated by the anaphase-promoting complex (APC), leading to its degradation by the proteasome (PubMed:10851084, PubMed:11039908).
Ubiquitinated by the CUL3-KLHL18 ligase leading to its activation at the centrosome which is required for initiating mitotic entry (PubMed:23213400).
Ubiquitination mediated by CUL3-KLHL18 ligase does not lead to its degradation by the proteasome (PubMed:23213400).
Ubiquitinated by CHFR, leading to its degradation by the proteasome (By similarity).
Ubiquitinated by the anaphase-promoting complex (APC), leading to its degradation by the proteasome (PubMed:10851084, PubMed:11039908).
Ubiquitinated by the CUL3-KLHL18 ligase leading to its activation at the centrosome which is required for initiating mitotic entry (PubMed:23213400).
Ubiquitination mediated by CUL3-KLHL18 ligase does not lead to its degradation by the proteasome (PubMed:23213400).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in testis and weakly in skeletal muscle, thymus and spleen. Also highly expressed in colon, ovarian, prostate, neuroblastoma, breast and cervical cancer cell lines.
Induction
Expression is cell-cycle regulated, low in G1/S, accumulates during G2/M, and decreases rapidly after.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Part of a complex composed of NEDD9, AURKA and CTTN; within the complex NEDD9 acts as a scaffold protein and is required for complex formation (PubMed:24574519).
Identified in a complex with AUNIP and NIN (PubMed:20596670).
Interacts with FBXL7 (By similarity).
Interacts with CPEB1, JTB, TACC1, TPX2, PPP2CA, as well as with the protein phosphatase type 1 (PP1) isoforms PPP1CA, PPP1CB and PPP1CC (PubMed:11551964, PubMed:14580337, PubMed:14603251, PubMed:15966895, PubMed:17229885, PubMed:18662907, PubMed:19357306, PubMed:19668197, PubMed:19801554, PubMed:21225229, PubMed:27837025).
Interacts also with its substrates ARHGEF2, BORA, KIF2A, PARD3, and p53/TP53 (PubMed:14702041, PubMed:16890155, PubMed:17488622, PubMed:19351716, PubMed:19812038).
Interaction with BORA promotes phosphorylation of PLK1 (By similarity).
Interacts with CIMAP3 (PubMed:20643351).
Interacts with GADD45A, competing with its oligomerization (PubMed:20460379).
Interacts (via C-terminus) with AUNIP (via C-terminus) (PubMed:20596670).
Interacts with FRY; this interaction facilitates AURKA-mediated PLK1 phosphorylation (PubMed:22753416).
Interacts with SIRT2 (PubMed:17726514, PubMed:22014574).
Interacts with MYCN; interaction is phospho-independent and triggers AURKA activation; AURKA competes with FBXW7 for binding to unphosphorylated MYCN but not for binding to phosphorylated MYCN (PubMed:27837025).
Interacts with HNRNPU (PubMed:21242313, PubMed:25986610).
Interacts with AAAS (PubMed:26246606).
Interacts with KLHL18 and CUL3 (PubMed:23213400).
Interacts with FOXP1 (PubMed:28218735).
Interacts with HDAC6; AURKA-mediated phosphorylation of HDAC6 promotes deacetylation of alpha-tubulin (PubMed:17604723).
Identified in a complex with AUNIP and NIN (PubMed:20596670).
Interacts with FBXL7 (By similarity).
Interacts with CPEB1, JTB, TACC1, TPX2, PPP2CA, as well as with the protein phosphatase type 1 (PP1) isoforms PPP1CA, PPP1CB and PPP1CC (PubMed:11551964, PubMed:14580337, PubMed:14603251, PubMed:15966895, PubMed:17229885, PubMed:18662907, PubMed:19357306, PubMed:19668197, PubMed:19801554, PubMed:21225229, PubMed:27837025).
Interacts also with its substrates ARHGEF2, BORA, KIF2A, PARD3, and p53/TP53 (PubMed:14702041, PubMed:16890155, PubMed:17488622, PubMed:19351716, PubMed:19812038).
Interaction with BORA promotes phosphorylation of PLK1 (By similarity).
Interacts with CIMAP3 (PubMed:20643351).
Interacts with GADD45A, competing with its oligomerization (PubMed:20460379).
Interacts (via C-terminus) with AUNIP (via C-terminus) (PubMed:20596670).
Interacts with FRY; this interaction facilitates AURKA-mediated PLK1 phosphorylation (PubMed:22753416).
Interacts with SIRT2 (PubMed:17726514, PubMed:22014574).
Interacts with MYCN; interaction is phospho-independent and triggers AURKA activation; AURKA competes with FBXW7 for binding to unphosphorylated MYCN but not for binding to phosphorylated MYCN (PubMed:27837025).
Interacts with HNRNPU (PubMed:21242313, PubMed:25986610).
Interacts with AAAS (PubMed:26246606).
Interacts with KLHL18 and CUL3 (PubMed:23213400).
Interacts with FOXP1 (PubMed:28218735).
Interacts with HDAC6; AURKA-mediated phosphorylation of HDAC6 promotes deacetylation of alpha-tubulin (PubMed:17604723).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O14965 | AURKAIP1 Q9NWT8 | 2 | EBI-448680, EBI-448665 | |
BINARY | O14965 | BIRC5 O15392 | 2 | EBI-448680, EBI-518823 | |
BINARY | O14965 | BORA Q6PGQ7 | 3 | EBI-448680, EBI-719836 | |
BINARY | O14965 | EGFR P00533 | 4 | EBI-448680, EBI-297353 | |
BINARY | O14965 | HNRNPK P61978 | 2 | EBI-448680, EBI-304185 | |
BINARY | O14965 | IK Q13123 | 3 | EBI-448680, EBI-713456 | |
BINARY | O14965 | IKBKB O14920 | 2 | EBI-448680, EBI-81266 | |
BINARY | O14965 | INCENP Q9NQS7 | 2 | EBI-448680, EBI-307907 | |
BINARY | O14965 | INCENP Q9NQS7-1 | 2 | EBI-448680, EBI-15767972 | |
BINARY | O14965 | MYCN P04198 | 12 | EBI-448680, EBI-878369 | |
BINARY | O14965 | NPM1 P06748 | 3 | EBI-448680, EBI-78579 | |
BINARY | O14965 | PLK1 P53350 | 4 | EBI-448680, EBI-476768 | |
BINARY | O14965 | PTPRD P23468 | 2 | EBI-448680, EBI-2682990 | |
XENO | O14965 | Sirt2 Q8VDQ8 | 5 | EBI-448680, EBI-911012 | |
BINARY | O14965 | SPAG5 Q96R06 | 3 | EBI-448680, EBI-413317 | |
BINARY | O14965 | TP73 O15350 | 11 | EBI-448680, EBI-389606 | |
BINARY | O14965 | TPX2 Q9ULW0 | 10 | EBI-448680, EBI-1037322 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-125 | Disordered | ||||
Sequence: MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRIPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKNEESKK | ||||||
Compositional bias | 28-105 | Polar residues | ||||
Sequence: TQQFPCQNPLPVNSGQAQRVLCPSNSSQRIPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSA | ||||||
Domain | 133-383 | Protein kinase | ||||
Sequence: FEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWI | ||||||
Region | 280-293 | Activation segment | ||||
Sequence: HAPSSRRTTLCGTL |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length403
- Mass (Da)45,823
- Last updated2022-02-23 v3
- Checksum7C2E7B438D969187
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 28-105 | Polar residues | ||||
Sequence: TQQFPCQNPLPVNSGQAQRVLCPSNSSQRIPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D84212 EMBL· GenBank· DDBJ | BAA23592.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AF008551 EMBL· GenBank· DDBJ | AAC12708.1 EMBL· GenBank· DDBJ | mRNA | ||
AF011467 EMBL· GenBank· DDBJ | AAC23448.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF011468 EMBL· GenBank· DDBJ | AAC63902.1 EMBL· GenBank· DDBJ | mRNA | ||
AF195947 EMBL· GenBank· DDBJ | AAF29508.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF195942 EMBL· GenBank· DDBJ | AAF29508.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF195943 EMBL· GenBank· DDBJ | AAF29508.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF195944 EMBL· GenBank· DDBJ | AAF29508.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF195945 EMBL· GenBank· DDBJ | AAF29508.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF195946 EMBL· GenBank· DDBJ | AAF29508.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL121914 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471077 EMBL· GenBank· DDBJ | EAW75550.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75551.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75552.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75553.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75554.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75555.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75556.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75557.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75558.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75559.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75561.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75562.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001280 EMBL· GenBank· DDBJ | AAH01280.1 EMBL· GenBank· DDBJ | mRNA | ||
BC002499 EMBL· GenBank· DDBJ | AAH02499.1 EMBL· GenBank· DDBJ | mRNA | ||
BC006423 EMBL· GenBank· DDBJ | AAH06423.1 EMBL· GenBank· DDBJ | mRNA | ||
BC027464 EMBL· GenBank· DDBJ | AAH27464.1 EMBL· GenBank· DDBJ | mRNA |