O43318 · M3K7_HUMAN
- ProteinMitogen-activated protein kinase kinase kinase 7
- GeneMAP3K7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids606 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays an important role in the cascades of cellular responses evoked by changes in the environment (PubMed:10094049, PubMed:11460167, PubMed:12589052, PubMed:16845370, PubMed:16893890, PubMed:21512573, PubMed:8663074, PubMed:9079627).
Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR) (PubMed:16893890, PubMed:9079627).
Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7 (PubMed:11460167, PubMed:8663074).
These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs); both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1) (PubMed:11460167, PubMed:12589052, PubMed:8663074).
Independently of MAP2Ks and p38 MAPKs, acts as a key activator of NF-kappa-B by promoting activation of the I-kappa-B-kinase (IKK) core complex (PubMed:12589052, PubMed:8663074).
Mechanistically, recruited to polyubiquitin chains of RIPK2 and IKBKG/NEMO via TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3, and catalyzes phosphorylation and activation of IKBKB/IKKB component of the IKK complex, leading to NF-kappa-B activation (PubMed:10094049, PubMed:11460167).
In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B (PubMed:16893890).
Promotes TRIM5 capsid-specific restriction activity (PubMed:21512573).
Phosphorylates RIPK1 at 'Ser-321' which positively regulates RIPK1 interaction with RIPK3 to promote necroptosis but negatively regulates RIPK1 kinase activity and its interaction with FADD to mediate apoptosis (By similarity).
Phosphorylates STING1 in response to cGAMP-activation, promoting association between STEEP1 and STING1 and STING1 translocation to COPII vesicles (PubMed:37832545).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Activity regulation
Activated by 'Lys-63'-linked polyubiquitination and by autophosphorylation (PubMed:10702308, PubMed:11460167, PubMed:12242293, PubMed:29291351).
Association with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2 promotes activation through autophosphorylation, whereas PPM1B/PP2CB, PP2A and PPP6C dephosphorylation leads to inactivation (PubMed:11104763, PubMed:17079228, PubMed:37832545).
Ceramides are also able to activate MAP3K7/TAK1 (PubMed:9079627).
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMitogen-activated protein kinase kinase kinase 7
- 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 accessionO43318
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Frontometaphyseal dysplasia 2 (FMD2)
- Note
- DescriptionA form of frontometaphyseal dysplasia, a progressive sclerosing skeletal dysplasia affecting the long bones and skull. Characteristic features include supraorbital hyperostosis, cranial hyperostosis, undermodeling of the small bones, flared metaphyses, and digital anomalies. Extra-skeletal manifestations include hearing loss, cardiac malformations, and stenosis, particularly of the upper airway and urinary tract. FMD2 inheritance is autosomal dominant.
- See alsoMIM:617137
Natural variants in FMD2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_077342 | 70 | E>Q | in FMD2; dbSNP:rs886039231 | |
VAR_077343 | 100 | V>E | in FMD2; dbSNP:rs886039232 | |
VAR_077345 | 168 | G>R | in FMD2; increases autophosphorylation; no effect on MAPK signaling; no effect on NF-kappa-B signaling; dbSNP:rs886039233 | |
VAR_077347 | 512 | P>L | in FMD2; does not affect interaction with TAB2; does not affect homodimerization; increases autophosphorylation; increases MAPK signaling; increases NF-kappa-B signaling; dbSNP:rs886039230 |
Cardiospondylocarpofacial syndrome (CSCF)
- Note
- DescriptionA syndrome characterized by growth retardation, dysmorphic facial features, brachydactyly with carpal-tarsal fusion and extensive posterior cervical vertebral synostosis, cardiac septal defects with valve dysplasia, and deafness with inner ear malformations. CSCF transmission pattern is consistent with autosomal dominant inheritance.
- See alsoMIM:157800
Natural variants in CSCF
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_077341 | 50 | missing | in CSCF; dbSNP:rs886039236 | |
VAR_077344 | 110 | G>C | in CSCF; dbSNP:rs886039235 | |
VAR_077346 | 241 | W>R | in CSCF; dbSNP:rs886039237 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 34 | No effect on ubiquitination. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_077341 | 50 | in CSCF; dbSNP:rs886039236 | |||
Sequence: Missing | ||||||
Mutagenesis | 63 | Loss of kinase activity. Loss of autophosphorylation. | ||||
Sequence: K → W | ||||||
Natural variant | VAR_077342 | 70 | in FMD2; dbSNP:rs886039231 | |||
Sequence: E → Q | ||||||
Natural variant | VAR_077343 | 100 | in FMD2; dbSNP:rs886039232 | |||
Sequence: V → E | ||||||
Natural variant | VAR_077344 | 110 | in CSCF; dbSNP:rs886039235 | |||
Sequence: G → C | ||||||
Mutagenesis | 158 | Abolishes ubiquitination. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_077345 | 168 | in FMD2; increases autophosphorylation; no effect on MAPK signaling; no effect on NF-kappa-B signaling; dbSNP:rs886039233 | |||
Sequence: G → R | ||||||
Mutagenesis | 209 | Strongly decreases ubiquitination. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_077346 | 241 | in CSCF; dbSNP:rs886039237 | |||
Sequence: W → R | ||||||
Natural variant | VAR_080761 | 410 | found in a consanguineous family with intellectual disability; uncertain significance; dbSNP:rs201721045 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_077347 | 512 | in FMD2; does not affect interaction with TAB2; does not affect homodimerization; increases autophosphorylation; increases MAPK signaling; increases NF-kappa-B signaling; dbSNP:rs886039230 | |||
Sequence: P → L | ||||||
Mutagenesis | 512 | Enhances autophosphorylation; Alters MAPK signaling. | ||||
Sequence: P → R or A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 513 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, cross-link, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000086252 | 1-606 | UniProt | Mitogen-activated protein kinase kinase kinase 7 | |||
Sequence: MSTASAASSSSSSSAGEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQYSDEGQSNSATSTGSFMDIASTNTSNKSDTNMEQVPATNDTIKRLESKLLKNQAKQQSESGRLSLGASRGSSVESLPPTSEGKRMSADMSEIEARIAATTAYSKPKRGHRKTASFGNILDVPEIVISGNGQPRRRSIQDLTVTGTEPGQVSSRSSSPSVRMITTSGPTSEKPTRSHPWTPDDSTDTNGSDNSIPMAYLTLDHQLQPLAPCPNSKESMAVFEQHCKMAQEYMKVQTEIALLLQRKQELVAELDQDEKDQQNTSRLVQEHKKLLDENKSLSTYYQQCKKQLEVIRSQQQKRQGTS | |||||||
Cross-link | 72 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 158 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue | 184 | UniProt | (Microbial infection) O-acetylthreonine; by Yersinia YopJ; alternate | ||||
Sequence: T | |||||||
Modified residue | 184 | UniProt | Phosphothreonine; by autocatalysis; alternate | ||||
Sequence: T | |||||||
Modified residue | 187 | UniProt | (Microbial infection) O-acetylthreonine; by Yersinia YopJ; alternate | ||||
Sequence: T | |||||||
Modified residue | 187 | UniProt | Phosphothreonine; by autocatalysis; alternate | ||||
Sequence: T | |||||||
Modified residue | 192 | UniProt | Phosphoserine; by autocatalysis | ||||
Sequence: S | |||||||
Cross-link | 209 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 331 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 333 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 341 | UniProt | (Microbial infection) O-acetylthreonine; by Yersinia YopJ; alternate | ||||
Sequence: T | |||||||
Modified residue | 367 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 367 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 375 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 389 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 389 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 393 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 415 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 417 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 439 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 439 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 444 | UniProt | (Microbial infection) O-acetylthreonine; by Yersinia YopJ; alternate | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 444 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 446 | UniProt | (Microbial infection) O-acetylthreonine; by Yersinia YopJ; alternate | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 446 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 448 | UniProt | (Microbial infection) O-acetylthreonine; by Yersinia YopJ; alternate | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 454 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 455 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 455 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 459 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 467 | UniProt | (Microbial infection) O-acetylthreonine; by Yersinia YopJ; alternate | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 472 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Requires 'Lys-63'-linked polyubiquitination for autophosphorylation and subsequent activation. 'Lys-63'-linked ubiquitination does not lead to proteasomal degradation. Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains. Deubiquitinated by Y.enterocolitica YopP
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binds both upstream activators and downstream substrates in multimolecular complexes. Interacts with TAB1/MAP3K7IP1, TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3 (PubMed:10838074, PubMed:11460167, PubMed:12242293, PubMed:14670075, PubMed:16289117, PubMed:19675569, PubMed:8638164).
Identified in the TRIKA2 complex composed of MAP3K7/TAK1, TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2 (PubMed:11460167).
Interacts with PPM1L and PPM1B/PP2CB (PubMed:11104763).
Interaction with PP2A and PPP6C leads to its repressed activity (PubMed:17079228).
Interacts with TRAF6 and TAB1/MAP3K7IP1; during IL-1 signaling (PubMed:10094049, PubMed:12242293).
Interacts with TAOK1 and TAOK2; interaction with TAOK2 interferes with MAP3K7 interaction with IKKA, thus preventing NF-kappa-B activation (PubMed:16893890).
Interacts with DYNC2I2 (via WD domains) (PubMed:19521662).
Interacts with CYLD and RBCK1 (PubMed:17449468, PubMed:17548520).
Interacts with TGFBR1; induces MAP3K7/TAK1 activation by TRAF6 (PubMed:18758450).
Interacts with MAPK8IP1 and SMAD6 (By similarity).
Interacts with isoform 1 of VRK2 (PubMed:18286207).
Interacts with DAB2; the interaction is induced by TGF-beta stimulation and may mediate TGF-beta stimulated JNK activation (PubMed:15894542).
Interacts with TRIM5 (PubMed:21512573).
Part of a complex containing ITCH, NDFIP1 and MAP3K7 (By similarity).
Interacts with IFIT5; the interaction synergizes the recruitment of IKK to MAP3K7 and enhances IKK phosphorylation (PubMed:26334375).
Interacts with PLEKHM1 (via N- and C-terminus) (By similarity).
Interacts with TRIM8 (PubMed:22084099).
Found in a complex with SH3RF1, RAC2, MAP2K7/MKK7, MAPK8IP1/JIP1, MAPK8/JNK1 and MAPK9/JNK2 (By similarity).
Interacts with SASH1 (PubMed:23776175).
Interacts with RIPK1 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | O43318 | cagA B5Z6S0 | 4 | EBI-358684, EBI-7287204 | |
BINARY | O43318 | CDC37 Q16543 | 4 | EBI-358684, EBI-295634 | |
BINARY | O43318 | IKBKB O14920 | 6 | EBI-358684, EBI-81266 | |
BINARY | O43318 | MAP2K7 O14733 | 3 | EBI-358684, EBI-492605 | |
BINARY | O43318 | MAPK8IP1 Q9UQF2 | 11 | EBI-358684, EBI-78404 | |
XENO | O43318 | N P0DTC9 | 4 | EBI-358684, EBI-25475856 | |
BINARY | O43318 | PPP6C O00743 | 4 | EBI-358684, EBI-359751 | |
BINARY | O43318 | STAT3 P40763 | 4 | EBI-358684, EBI-518675 | |
BINARY | O43318 | TAB1 Q15750 | 10 | EBI-358684, EBI-358643 | |
BINARY | O43318 | TAB2 Q9NYJ8 | 8 | EBI-358684, EBI-358708 | |
BINARY | O43318 | TAB3 Q8N5C8 | 5 | EBI-358684, EBI-359964 | |
BINARY | O43318 | TNIK Q9UKE5 | 3 | EBI-358684, EBI-1051794 | |
BINARY | O43318 | TRAF6 Q9Y4K3 | 2 | EBI-358684, EBI-359276 | |
BINARY | O43318 | UBC P0CG48 | 4 | EBI-358684, EBI-3390054 | |
BINARY | O43318-2 | CDC37 Q16543 | 5 | EBI-358700, EBI-295634 | |
BINARY | O43318-2 | HSP90AA1 P07900 | 5 | EBI-358700, EBI-296047 | |
BINARY | O43318-2 | TAB1 Q15750 | 3 | EBI-358700, EBI-358643 | |
BINARY | O43318-2 | TAB2 Q9NYJ8 | 2 | EBI-358700, EBI-358708 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-300 | Interaction with MAPK8IP1 | ||||
Sequence: MSTASAASSSSSSSAGEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQY | ||||||
Domain | 36-291 | Protein kinase | ||||
Sequence: IEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYF | ||||||
Region | 301-338 | Disordered | ||||
Sequence: PCQYSDEGQSNSATSTGSFMDIASTNTSNKSDTNMEQV | ||||||
Compositional bias | 303-338 | Polar residues | ||||
Sequence: QYSDEGQSNSATSTGSFMDIASTNTSNKSDTNMEQV | ||||||
Compositional bias | 354-382 | Polar residues | ||||
Sequence: KNQAKQQSESGRLSLGASRGSSVESLPPT | ||||||
Region | 354-391 | Disordered | ||||
Sequence: KNQAKQQSESGRLSLGASRGSSVESLPPTSEGKRMSAD | ||||||
Region | 443-493 | Disordered | ||||
Sequence: LTVTGTEPGQVSSRSSSPSVRMITTSGPTSEKPTRSHPWTPDDSTDTNGSD |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
O43318-1
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.
- Name1B
- Length606
- Mass (Da)67,196
- Last updated1998-06-01 v1
- Checksum3D8F8147CD174013
O43318-2
- Name1A
- Differences from canonical
- 404-430: Missing
O43318-3
- Name1C
O43318-4
- Name1D
Computationally mapped potential isoform sequences
There are 13 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8V8TRC0 | A0A8V8TRC0_HUMAN | MAP3K7 | 305 | ||
A0A8V8TRC2 | A0A8V8TRC2_HUMAN | MAP3K7 | 40 | ||
A0A8V8TRC6 | A0A8V8TRC6_HUMAN | MAP3K7 | 100 | ||
A0A8V8TQE8 | A0A8V8TQE8_HUMAN | MAP3K7 | 137 | ||
A0A8V8TQF2 | A0A8V8TQF2_HUMAN | MAP3K7 | 557 | ||
A0A8V8TQF4 | A0A8V8TQF4_HUMAN | MAP3K7 | 90 | ||
A0A8V8TQF8 | A0A8V8TQF8_HUMAN | MAP3K7 | 476 | ||
A0A8V8TQL7 | A0A8V8TQL7_HUMAN | MAP3K7 | 194 | ||
A0A8V8TR14 | A0A8V8TR14_HUMAN | MAP3K7 | 58 | ||
A0A8V8TR17 | A0A8V8TR17_HUMAN | MAP3K7 | 604 | ||
A0A8V8TQ28 | A0A8V8TQ28_HUMAN | MAP3K7 | 220 | ||
A0A8V8TPV8 | A0A8V8TPV8_HUMAN | MAP3K7 | 140 | ||
A0A8V8TPW3 | A0A8V8TPW3_HUMAN | MAP3K7 | 261 |
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 303-338 | Polar residues | ||||
Sequence: QYSDEGQSNSATSTGSFMDIASTNTSNKSDTNMEQV | ||||||
Compositional bias | 354-382 | Polar residues | ||||
Sequence: KNQAKQQSESGRLSLGASRGSSVESLPPT | ||||||
Alternative sequence | VSP_004886 | 404-430 | in isoform 1A and isoform 1D | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_004887 | 509-518 | in isoform 1C and isoform 1D | |||
Sequence: PLAPCPNSKE → ARTSCRTGPG | ||||||
Alternative sequence | VSP_004888 | 519-606 | in isoform 1C and isoform 1D | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB009357 EMBL· GenBank· DDBJ | BAA25026.1 EMBL· GenBank· DDBJ | mRNA | ||
AB009356 EMBL· GenBank· DDBJ | BAA25025.1 EMBL· GenBank· DDBJ | mRNA | ||
AB009358 EMBL· GenBank· DDBJ | BAA25027.2 EMBL· GenBank· DDBJ | mRNA | ||
AF218074 EMBL· GenBank· DDBJ | AAF27652.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ314875 EMBL· GenBank· DDBJ | ABC40734.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK315774 EMBL· GenBank· DDBJ | BAG38124.1 EMBL· GenBank· DDBJ | mRNA | ||
AL121964 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL121837 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471051 EMBL· GenBank· DDBJ | EAW48525.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471051 EMBL· GenBank· DDBJ | EAW48526.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471051 EMBL· GenBank· DDBJ | EAW48527.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471051 EMBL· GenBank· DDBJ | EAW48529.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC017715 EMBL· GenBank· DDBJ | AAH17715.1 EMBL· GenBank· DDBJ | mRNA |