Q5TCQ9 · MAGI3_HUMAN
- ProteinMembrane-associated guanylate kinase, WW and PDZ domain-containing protein 3
- GeneMAGI3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1481 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Miscellaneous
Features
Showing features for binding site.
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 | bicellular tight junction | |
Cellular Component | cell junction | |
Cellular Component | cell-cell junction | |
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | guanylate kinase activity | |
Biological Process | apoptotic process | |
Biological Process | intracellular signal transduction | |
Biological Process | signal transduction |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
The subsequence IIGGDRPDEFLQVKNVLKDGPAAQDGKIAPGDVIVDINGNCVLGHTHADVVQMFQLVPVNQYVNLTLCRGYPLPDDSEDP, which contains the PDZ_6 domain, shows transcriptional repressor activity in a high-throughput recruitment assay.
Names & Taxonomy
Protein names
- Recommended nameMembrane-associated guanylate kinase, WW and PDZ domain-containing protein 3
- Alternative names
Gene names
- Community suggested namesMAGI3
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5TCQ9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,458 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000341407 | 1-1481 | UniProt | Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3 | |||
Sequence: MSKTLKKKKHWLSKVQECAVSWAGPPGDFGAEIRGGAERGEFPYLGRLREEPGGGTCCVVSGKAPSPGDVLLEVNGTPVSGLTNRDTLAVIRHFREPIRLKTVKPGKVINKDLRHYLSLQFQKGSIDHKLQQVIRDNLYLRTIPCTTRAPRDGEVPGVDYNFISVEQFKALEESGALLESGTYDGNFYGTPKPPAEPSPFQPDPVDQVLFDNEFDAESQRKRTTSVSKMERMDSSLPEEEEDEDKEAINGSGNAENRERHSESSDWMKTVPSYNQTNSSMDFRNYMMRDETLEPLPKNWEMAYTDTGMIYFIDHNTKTTTWLDPRLCKKAKAPEDCEDGELPYGWEKIEDPQYGTYYVDHLNQKTQFENPVEEAKRKKQLGQVEIGSSKPDMEKSHFTRDPSQLKGVLVRASLKKSTMGFGFTIIGGDRPDEFLQVKNVLKDGPAAQDGKIAPGDVIVDINGNCVLGHTHADVVQMFQLVPVNQYVNLTLCRGYPLPDDSEDPVVDIVAATPVINGQSLTKGETCMNPQDFKPGAMVLEQNGKSGHTLTGDGLNGPSDASEQRVSMASSGSSQPELVTIPLIKGPKGFGFAIADSPTGQKVKMILDSQWCQGLQKGDIIKEIYHQNVQNLTHLQVVEVLKQFPVGADVPLLILRGGPPSPTKTAKMKTDKKENAGSLEAINEPIPQPMPFPPSIIRSGSPKLDPSEVYLKSKTLYEDKPPNTKDLDVFLRKQESGFGFRVLGGDGPDQSIYIGAIIPLGAAEKDGRLRAADELMCIDGIPVKGKSHKQVLDLMTTAARNGHVLLTVRRKIFYGEKQPEDDSSQAFISTQNGSPRLNRAEVPARPAPQEPYDVVLQRKENEGFGFVILTSKNKPPPGVIPHKIGRVIEGSPADRCGKLKVGDHISAVNGQSIVELSHDNIVQLIKDAGVTVTLTVIAEEEHHGPPSGTNSARQSPALQHRPMGQSQANHIPGDRSALEGEIGKDVSTSYRHSWSDHKHLAQPDTAVISVVGSRHNQNLGCYPVELERGPRGFGFSLRGGKEYNMGLFILRLAEDGPAIKDGRIHVGDQIVEINGEPTQGITHTRAIELIQAGGNKVLLLLRPGTGLIPDHGDWDINNPSSSNVIYDEQSPLPPSSHFASIFEESHVPVIEESLRVQICEKAEELKDIVPEKKSTLNENQPEIKHQSLLQKNVSKRDPPSSHGHSNKKNLLKVENGVTRRGRSVSPKKPASQHSEEHLDKIPSPLKNNPKRRPRDQSLSPSKGENKSCQVSTRAGSGQDQCRKSRGRSASPKKQQKIEGSKAPSNAEAKLLEGKSRRIAGYTGSNAEQIPDGKEKSDVIRKDAKQNQLEKSRTRSPEKKIKRMVEKSLPSKMTNKTTSKEVSENEKGKKVTTGETSSSNDKIGENVQLSEKRLKQEPEEKVVSNKTEDHKGKELEAADKNKETGRFKPESSSPVKKTLITPGPWKVPSGNKVTGTIGMAEKRQ | |||||||
Modified residue | 234 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 235 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 251 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 595 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 595 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 659 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 676 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 699 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 699 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 822 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 828 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 832 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 832 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 915 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 953 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 991 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1221 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1223 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1255 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1257 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1259 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1450 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with ADGRB1, LPAR2/EDG4, GRIN2B and PTEN. Does not interact with HTLV TAX2 or TAX3 proteins. Interacts with DLL1 (By similarity).
Interacts with PRRG4 (via cytoplasmic domain) (PubMed:23873930).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q5TCQ9 | ADRB1 P08588 | 5 | EBI-310506, EBI-991009 | |
BINARY | Q5TCQ9 | ADRB2 P07550 | 9 | EBI-310506, EBI-491169 | |
BINARY | Q5TCQ9 | MED28 Q9H204 | 2 | EBI-310506, EBI-514199 | |
BINARY | Q5TCQ9 | PRRG4 Q9BZD6 | 2 | EBI-310506, EBI-3918643 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-106 | PDZ 1 | ||||
Sequence: CAVSWAGPPGDFGAEIRGGAERGEFPYLGRLREEPGGGTCCVVSGKAPSPGDVLLEVNGTPVSGLTNRDTLAVIRHFREPIRLKTVKPG | ||||||
Region | 18-106 | Interaction with ADRB1 and TGFA | ||||
Sequence: CAVSWAGPPGDFGAEIRGGAERGEFPYLGRLREEPGGGTCCVVSGKAPSPGDVLLEVNGTPVSGLTNRDTLAVIRHFREPIRLKTVKPG | ||||||
Domain | 114-288 | Guanylate kinase-like | ||||
Sequence: RHYLSLQFQKGSIDHKLQQVIRDNLYLRTIPCTTRAPRDGEVPGVDYNFISVEQFKALEESGALLESGTYDGNFYGTPKPPAEPSPFQPDPVDQVLFDNEFDAESQRKRTTSVSKMERMDSSLPEEEEDEDKEAINGSGNAENRERHSESSDWMKTVPSYNQTNSSMDFRNYMMR | ||||||
Region | 182-273 | Disordered | ||||
Sequence: TYDGNFYGTPKPPAEPSPFQPDPVDQVLFDNEFDAESQRKRTTSVSKMERMDSSLPEEEEDEDKEAINGSGNAENRERHSESSDWMKTVPSY | ||||||
Compositional bias | 213-235 | Basic and acidic residues | ||||
Sequence: EFDAESQRKRTTSVSKMERMDSS | ||||||
Compositional bias | 247-265 | Basic and acidic residues | ||||
Sequence: AINGSGNAENRERHSESSD | ||||||
Domain | 293-326 | WW 1 | ||||
Sequence: EPLPKNWEMAYTDTGMIYFIDHNTKTTTWLDPRL | ||||||
Domain | 339-372 | WW 2 | ||||
Sequence: GELPYGWEKIEDPQYGTYYVDHLNQKTQFENPVE | ||||||
Domain | 410-492 | PDZ 2 | ||||
Sequence: RASLKKSTMGFGFTIIGGDRPDEFLQVKNVLKDGPAAQDGKIAPGDVIVDINGNCVLGHTHADVVQMFQLVPVNQYVNLTLCR | ||||||
Region | 410-492 | Interaction with PTEN | ||||
Sequence: RASLKKSTMGFGFTIIGGDRPDEFLQVKNVLKDGPAAQDGKIAPGDVIVDINGNCVLGHTHADVVQMFQLVPVNQYVNLTLCR | ||||||
Region | 542-570 | Disordered | ||||
Sequence: GKSGHTLTGDGLNGPSDASEQRVSMASSG | ||||||
Domain | 578-654 | PDZ 3 | ||||
Sequence: TIPLIKGPKGFGFAIADSPTGQKVKMILDSQWCQGLQKGDIIKEIYHQNVQNLTHLQVVEVLKQFPVGADVPLLILR | ||||||
Domain | 726-808 | PDZ 4 | ||||
Sequence: DVFLRKQESGFGFRVLGGDGPDQSIYIGAIIPLGAAEKDGRLRAADELMCIDGIPVKGKSHKQVLDLMTTAARNGHVLLTVRR | ||||||
Region | 726-808 | Interaction with ADGRB1 | ||||
Sequence: DVFLRKQESGFGFRVLGGDGPDQSIYIGAIIPLGAAEKDGRLRAADELMCIDGIPVKGKSHKQVLDLMTTAARNGHVLLTVRR | ||||||
Compositional bias | 821-835 | Polar residues | ||||
Sequence: SSQAFISTQNGSPRL | ||||||
Region | 821-843 | Disordered | ||||
Sequence: SSQAFISTQNGSPRLNRAEVPAR | ||||||
Domain | 851-938 | PDZ 5 | ||||
Sequence: DVVLQRKENEGFGFVILTSKNKPPPGVIPHKIGRVIEGSPADRCGKLKVGDHISAVNGQSIVELSHDNIVQLIKDAGVTVTLTVIAEE | ||||||
Region | 851-938 | Interaction with LPAR2 and GRIN2B | ||||
Sequence: DVVLQRKENEGFGFVILTSKNKPPPGVIPHKIGRVIEGSPADRCGKLKVGDHISAVNGQSIVELSHDNIVQLIKDAGVTVTLTVIAEE | ||||||
Region | 939-976 | Disordered | ||||
Sequence: EHHGPPSGTNSARQSPALQHRPMGQSQANHIPGDRSAL | ||||||
Compositional bias | 945-970 | Polar residues | ||||
Sequence: SGTNSARQSPALQHRPMGQSQANHIP | ||||||
Domain | 1021-1103 | PDZ 6 | ||||
Sequence: PVELERGPRGFGFSLRGGKEYNMGLFILRLAEDGPAIKDGRIHVGDQIVEINGEPTQGITHTRAIELIQAGGNKVLLLLRPGT | ||||||
Region | 1170-1481 | Disordered | ||||
Sequence: KKSTLNENQPEIKHQSLLQKNVSKRDPPSSHGHSNKKNLLKVENGVTRRGRSVSPKKPASQHSEEHLDKIPSPLKNNPKRRPRDQSLSPSKGENKSCQVSTRAGSGQDQCRKSRGRSASPKKQQKIEGSKAPSNAEAKLLEGKSRRIAGYTGSNAEQIPDGKEKSDVIRKDAKQNQLEKSRTRSPEKKIKRMVEKSLPSKMTNKTTSKEVSENEKGKKVTTGETSSSNDKIGENVQLSEKRLKQEPEEKVVSNKTEDHKGKELEAADKNKETGRFKPESSSPVKKTLITPGPWKVPSGNKVTGTIGMAEKRQ | ||||||
Compositional bias | 1178-1194 | Polar residues | ||||
Sequence: QPEIKHQSLLQKNVSKR | ||||||
Compositional bias | 1195-1213 | Basic and acidic residues | ||||
Sequence: DPPSSHGHSNKKNLLKVEN | ||||||
Compositional bias | 1227-1257 | Basic and acidic residues | ||||
Sequence: PASQHSEEHLDKIPSPLKNNPKRRPRDQSLS | ||||||
Compositional bias | 1258-1282 | Polar residues | ||||
Sequence: PSKGENKSCQVSTRAGSGQDQCRKS | ||||||
Compositional bias | 1328-1366 | Basic and acidic residues | ||||
Sequence: PDGKEKSDVIRKDAKQNQLEKSRTRSPEKKIKRMVEKSL | ||||||
Compositional bias | 1403-1447 | Basic and acidic residues | ||||
Sequence: NVQLSEKRLKQEPEEKVVSNKTEDHKGKELEAADKNKETGRFKPE |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q5TCQ9-4
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
- Length1,481
- Mass (Da)162,949
- Last updated2018-03-28 v3
- Checksum9C2B604D9B1B1B97
Q5TCQ9-1
- Name4
- Differences from canonical
- 359-359: D → DFTLVAQAGVQWHDLGSLQPPPPGFN
Q5TCQ9-2
- Name2
- Differences from canonical
- 359-359: D → DFTLVAQAGVQWHDLGSLQPPPPGFN
- 1111-1125: DWDINNPSSSNVIYD → LAPSGLCSYVKPEQH
- 1126-1481: Missing
Q5TCQ9-3
- Name3
- Differences from canonical
- 1111-1125: DWDINNPSSSNVIYD → LAPSGLCSYVKPEQH
- 1126-1481: Missing
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 9 | in Ref. 2; AAG43837 | ||||
Sequence: K → R | ||||||
Sequence conflict | 59 | in Ref. 1; AAG24545 | ||||
Sequence: V → I | ||||||
Sequence conflict | 66-68 | in Ref. 1; AAG24545 | ||||
Sequence: SPG → NPS | ||||||
Compositional bias | 213-235 | Basic and acidic residues | ||||
Sequence: EFDAESQRKRTTSVSKMERMDSS | ||||||
Sequence conflict | 246 | in Ref. 1; AAG24545 | ||||
Sequence: E → G | ||||||
Compositional bias | 247-265 | Basic and acidic residues | ||||
Sequence: AINGSGNAENRERHSESSD | ||||||
Sequence conflict | 257 | in Ref. 2; AAG43837 | ||||
Sequence: R → G | ||||||
Alternative sequence | VSP_059502 | 359 | in isoform 4 and isoform 2 | |||
Sequence: D → DFTLVAQAGVQWHDLGSLQPPPPGFN | ||||||
Sequence conflict | 466 | in Ref. 1; AAG24545 | ||||
Sequence: L → F | ||||||
Sequence conflict | 548 | in Ref. 1; AAG24545 | ||||
Sequence: L → S | ||||||
Sequence conflict | 616 | in Ref. 1; AAG24545 | ||||
Sequence: G → E | ||||||
Sequence conflict | 660 | in Ref. 1; AAG24545 | ||||
Sequence: P → T | ||||||
Sequence conflict | 776 | in Ref. 2; AAG43837 | ||||
Sequence: I → V | ||||||
Sequence conflict | 798 | in Ref. 2; AAG43837 | ||||
Sequence: R → P | ||||||
Compositional bias | 821-835 | Polar residues | ||||
Sequence: SSQAFISTQNGSPRL | ||||||
Sequence conflict | 917 | in Ref. 1; AAG24545 | ||||
Sequence: D → A | ||||||
Compositional bias | 945-970 | Polar residues | ||||
Sequence: SGTNSARQSPALQHRPMGQSQANHIP | ||||||
Sequence conflict | 993 | in Ref. 2; AAG43837 | ||||
Sequence: S → P | ||||||
Alternative sequence | VSP_059503 | 1111-1125 | in isoform 3 and isoform 2 | |||
Sequence: DWDINNPSSSNVIYD → LAPSGLCSYVKPEQH | ||||||
Alternative sequence | VSP_059504 | 1126-1481 | in isoform 3 and isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 1178-1194 | Polar residues | ||||
Sequence: QPEIKHQSLLQKNVSKR | ||||||
Compositional bias | 1195-1213 | Basic and acidic residues | ||||
Sequence: DPPSSHGHSNKKNLLKVEN | ||||||
Compositional bias | 1227-1257 | Basic and acidic residues | ||||
Sequence: PASQHSEEHLDKIPSPLKNNPKRRPRDQSLS | ||||||
Compositional bias | 1258-1282 | Polar residues | ||||
Sequence: PSKGENKSCQVSTRAGSGQDQCRKS | ||||||
Compositional bias | 1328-1366 | Basic and acidic residues | ||||
Sequence: PDGKEKSDVIRKDAKQNQLEKSRTRSPEKKIKRMVEKSL | ||||||
Compositional bias | 1403-1447 | Basic and acidic residues | ||||
Sequence: NVQLSEKRLKQEPEEKVVSNKTEDHKGKELEAADKNKETGRFKPE |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF257238 EMBL· GenBank· DDBJ | AAG24545.1 EMBL· GenBank· DDBJ | mRNA | ||
AF213259 EMBL· GenBank· DDBJ | AAG43837.1 EMBL· GenBank· DDBJ | mRNA | ||
AL133517 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL365225 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL389921 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL390759 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471122 EMBL· GenBank· DDBJ | EAW56561.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471122 EMBL· GenBank· DDBJ | EAW56559.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471122 EMBL· GenBank· DDBJ | EAW56560.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471122 EMBL· GenBank· DDBJ | EAW56563.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471122 EMBL· GenBank· DDBJ | EAW56562.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC130409 EMBL· GenBank· DDBJ | AAI30410.1 EMBL· GenBank· DDBJ | mRNA | ||
AB046854 EMBL· GenBank· DDBJ | BAB13460.1 EMBL· GenBank· DDBJ | mRNA | ||
AK026417 EMBL· GenBank· DDBJ | BAB15479.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |