O15117 · FYB1_HUMAN
- ProteinFYN-binding protein 1
- GeneFYB1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids783 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells (By similarity).
May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (PubMed:10747096, PubMed:16980616).
Modulates the expression of IL2 (By similarity).
Involved in platelet activation (By similarity).
Prevents the degradation of SKAP1 and SKAP2 (PubMed:15849195).
May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells (By similarity).
May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (PubMed:10747096, PubMed:16980616).
Modulates the expression of IL2 (By similarity).
Involved in platelet activation (By similarity).
Prevents the degradation of SKAP1 and SKAP2 (PubMed:15849195).
May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells (By similarity).
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 | actin cytoskeleton | |
Cellular Component | anchoring junction | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Cellular Component | protein-containing complex | |
Molecular Function | lipid binding | |
Molecular Function | protein-containing complex binding | |
Molecular Function | signaling receptor binding | |
Biological Process | immune response | |
Biological Process | integrin-mediated signaling pathway | |
Biological Process | protein localization to plasma membrane | |
Biological Process | T cell receptor signaling pathway |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFYN-binding protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO15117
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with TMEM47 at cell-cell contacts in podocytes.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Thrombocytopenia 3 (THC3)
- Note
- DescriptionA form of thrombocytopenia, a hematologic disorder defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting. THC3 is an autosomal recessive form characterized by onset in infancy.
- See alsoMIM:273900
Natural variants in THC3
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_078810 | 131-783 | missing | in THC3 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_056880 | 51 | in dbSNP:rs1642515 | |||
Sequence: P → L | ||||||
Natural variant | VAR_078810 | 131-783 | in THC3 | |||
Sequence: Missing | ||||||
Natural variant | VAR_056881 | 332 | in dbSNP:rs3749741 | |||
Sequence: K → R | ||||||
Natural variant | VAR_060592 | 672 | in dbSNP:rs379707 | |||
Sequence: V → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,159 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000087396 | 1-783 | UniProt | FYN-binding protein 1 | |||
Sequence: MAKYNTGGNPTEDVSVNSRPFRVTGPNSSSGIQARKNLFNNQGNASPPAGPSNVPKFGSPKPPVAVKPSSEEKPDKEPKPPFLKPTGAGQRFGTPASLTTRDPEAKVGFLKPVGPKPINLPKEDSKPTFPWPPGNKPSLHSVNQDHDLKPLGPKSGPTPPTSENEQKQAFPKLTGVKGKFMSASQDLEPKPLFPKPAFGQKPPLSTENSHEDESPMKNVSSSKGSPAPLGVRSKSGPLKPAREDSENKDHAGEISSLPFPGVVLKPAASRGGPGLSKNGEEKKEDRKIDAAKNTFQSKINQEELASGTPPARFPKAPSKLTVGGPWGQSQEKEKGDKNSATPKQKPLPPLFTLGPPPPKPNRPPNVDLTKFHKTSSGNSTSKGQTSYSTTSLPPPPPSHPASQPPLPASHPSQPPVPSLPPRNIKPPFDLKSPVNEDNQDGVTHSDGAGNLDEEQDSEGETYEDIEASKEREKKREKEEKKRLELEKKEQKEKEKKEQEIKKKFKLTGPIQVIHLAKACCDVKGGKNELSFKQGEQIEIIRITDNPEGKWLGRTARGSYGYIKTTAVEIDYDSLKLKKDSLGAPSRPIEDDQEVYDDVAEQDDISSHSQSGSGGIFPPPPDDDIYDGIEEEDADDGFPAPPKQLDMGDEVYDDVDTSDFPVSSAEMSQGTNVGKAKTEEKDLKKLKKQEKEEKDFRKKFKYDGEIRVLYSTKVTTSITSKKWGTRDLQVKPGESLEVIQTTDDTKVLCRNEEGKYGYVLRSYLADNDGEIYDDIADGCIYDND | |||||||
Modified residue | 3 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 28 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 46 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 46 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 52 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 158 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 182 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 184 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 205 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 206 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 209 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 214 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 221 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 222 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 225 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 225 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 245 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 308 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 329 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 387 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 457 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 457 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 558 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 571 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 571 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 573 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 573 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 580 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 651 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 734 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 755 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 757 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
T-cell receptor ligation leads to increased tyrosine phosphorylation.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Expressed in hematopoietic tissues such as myeloid and T-cells, spleen and thymus. Not expressed in B-cells, nor in non-lymphoid tissues.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Part of a complex consisting of SKAP2, FYB1 and PTPNS1 (By similarity).
Part of a complex consisting of SKAP2, FYB1 and LILRB3 (By similarity).
Part of a complex consisting of SKAP1, FYB1 and CLNK (By similarity).
Interacts with CLNK (via its SH2 domain); this interaction allows SKAP1 and FYB1 to recruit FYN to the complex, thus promoting the phosphorylation of CLNK by FYN (By similarity).
Interacts with FYN (PubMed:15849195, PubMed:27335501, PubMed:9207119).
Interacts with LCP2 (PubMed:27335501, PubMed:9207119).
Interacts with SKAP1 (PubMed:10856234, PubMed:15849195, PubMed:16461356, PubMed:27335501, PubMed:9671755, PubMed:9748251, PubMed:9755858).
Interacts with SKAP2 (PubMed:10942756, PubMed:9671755, PubMed:9755858).
Interacts with FASLG (PubMed:19807924).
Interacts with EVL (PubMed:10747096).
Interacts with TMEM47 (By similarity).
Interacts with LCK (PubMed:27335501).
Part of a complex consisting of SKAP2, FYB1 and LILRB3 (By similarity).
Part of a complex consisting of SKAP1, FYB1 and CLNK (By similarity).
Interacts with CLNK (via its SH2 domain); this interaction allows SKAP1 and FYB1 to recruit FYN to the complex, thus promoting the phosphorylation of CLNK by FYN (By similarity).
Interacts with FYN (PubMed:15849195, PubMed:27335501, PubMed:9207119).
Interacts with LCP2 (PubMed:27335501, PubMed:9207119).
Interacts with SKAP1 (PubMed:10856234, PubMed:15849195, PubMed:16461356, PubMed:27335501, PubMed:9671755, PubMed:9748251, PubMed:9755858).
Interacts with SKAP2 (PubMed:10942756, PubMed:9671755, PubMed:9755858).
Interacts with FASLG (PubMed:19807924).
Interacts with EVL (PubMed:10747096).
Interacts with TMEM47 (By similarity).
Interacts with LCK (PubMed:27335501).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O15117 | FYN P06241 | 4 | EBI-1753267, EBI-515315 | |
BINARY | O15117 | LCP2 Q13094 | 9 | EBI-1753267, EBI-346946 | |
BINARY | O15117 | NCK1 P16333 | 3 | EBI-1753267, EBI-389883 | |
BINARY | O15117 | NCK2 O43639 | 3 | EBI-1753267, EBI-713635 | |
BINARY | O15117 | SKAP1 Q86WV1 | 6 | EBI-1753267, EBI-2477305 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, coiled coil, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-49 | Polar residues | ||||
Sequence: MAKYNTGGNPTEDVSVNSRPFRVTGPNSSSGIQARKNLFNNQGNASPPA | ||||||
Region | 1-502 | Disordered | ||||
Sequence: MAKYNTGGNPTEDVSVNSRPFRVTGPNSSSGIQARKNLFNNQGNASPPAGPSNVPKFGSPKPPVAVKPSSEEKPDKEPKPPFLKPTGAGQRFGTPASLTTRDPEAKVGFLKPVGPKPINLPKEDSKPTFPWPPGNKPSLHSVNQDHDLKPLGPKSGPTPPTSENEQKQAFPKLTGVKGKFMSASQDLEPKPLFPKPAFGQKPPLSTENSHEDESPMKNVSSSKGSPAPLGVRSKSGPLKPAREDSENKDHAGEISSLPFPGVVLKPAASRGGPGLSKNGEEKKEDRKIDAAKNTFQSKINQEELASGTPPARFPKAPSKLTVGGPWGQSQEKEKGDKNSATPKQKPLPPLFTLGPPPPKPNRPPNVDLTKFHKTSSGNSTSKGQTSYSTTSLPPPPPSHPASQPPLPASHPSQPPVPSLPPRNIKPPFDLKSPVNEDNQDGVTHSDGAGNLDEEQDSEGETYEDIEASKEREKKREKEEKKRLELEKKEQKEKEKKEQEIKK | ||||||
Compositional bias | 237-251 | Basic and acidic residues | ||||
Sequence: PLKPAREDSENKDHA | ||||||
Compositional bias | 276-292 | Basic and acidic residues | ||||
Sequence: SKNGEEKKEDRKIDAAK | ||||||
Compositional bias | 348-364 | Pro residues | ||||
Sequence: PPLFTLGPPPPKPNRPP | ||||||
Region | 348-448 | Interaction with SKAP1 | ||||
Sequence: PPLFTLGPPPPKPNRPPNVDLTKFHKTSSGNSTSKGQTSYSTTSLPPPPPSHPASQPPLPASHPSQPPVPSLPPRNIKPPFDLKSPVNEDNQDGVTHSDGA | ||||||
Compositional bias | 368-389 | Polar residues | ||||
Sequence: LTKFHKTSSGNSTSKGQTSYST | ||||||
Compositional bias | 390-427 | Pro residues | ||||
Sequence: TSLPPPPPSHPASQPPLPASHPSQPPVPSLPPRNIKPP | ||||||
Coiled coil | 456-507 | |||||
Sequence: DSEGETYEDIEASKEREKKREKEEKKRLELEKKEQKEKEKKEQEIKKKFKLT | ||||||
Motif | 462-465 | SH2-binding | ||||
Sequence: YEDI | ||||||
Compositional bias | 462-502 | Basic and acidic residues | ||||
Sequence: YEDIEASKEREKKREKEEKKRLELEKKEQKEKEKKEQEIKK | ||||||
Motif | 469-505 | Nuclear localization signal | ||||
Sequence: KEREKKREKEEKKRLELEKKEQKEKEKKEQEIKKKFK | ||||||
Domain | 511-572 | SH3 1 | ||||
Sequence: QVIHLAKACCDVKGGKNELSFKQGEQIEIIRITDNPEGKWLGRTARGSYGYIKTTAVEIDYD | ||||||
Motif | 595-598 | SH2-binding; to LCP2 | ||||
Sequence: YDDV | ||||||
Region | 598-678 | Disordered | ||||
Sequence: VAEQDDISSHSQSGSGGIFPPPPDDDIYDGIEEEDADDGFPAPPKQLDMGDEVYDDVDTSDFPVSSAEMSQGTNVGKAKTE | ||||||
Motif | 625-628 | SH2-binding; to FYN | ||||
Sequence: YDGI | ||||||
Motif | 674-700 | Nuclear localization signal | ||||
Sequence: KAKTEEKDLKKLKKQEKEEKDFRKKFK | ||||||
Domain | 700-768 | SH3 2 | ||||
Sequence: KYDGEIRVLYSTKVTTSITSKKWGTRDLQVKPGESLEVIQTTDDTKVLCRNEEGKYGYVLRSYLADNDG |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
O15117-1
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.
- NameFYB-120
- Length783
- Mass (Da)85,387
- Last updated2009-11-24 v2
- Checksum4EE28EF12AA0E457
O15117-2
- NameFYB-130
- Differences from canonical
- 636-636: G → GSTLQVQEKSNTWSWGILKMLKGKDDRKKSIREKPKVSDSDNNEGSS
O15117-3
- Name3
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8YEE1 | A0A2R8YEE1_HUMAN | FYB1 | 69 | ||
D6RFJ5 | D6RFJ5_HUMAN | FYB1 | 174 | ||
D6RER7 | D6RER7_HUMAN | FYB1 | 114 | ||
D6RC38 | D6RC38_HUMAN | FYB1 | 22 | ||
D6RAE8 | D6RAE8_HUMAN | FYB1 | 62 |
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_047288 | 1 | in isoform 3 | |||
Sequence: M → MDGKADVKSLM | ||||||
Compositional bias | 1-49 | Polar residues | ||||
Sequence: MAKYNTGGNPTEDVSVNSRPFRVTGPNSSSGIQARKNLFNNQGNASPPA | ||||||
Sequence conflict | 27 | in Ref. 4; BAF83092 | ||||
Sequence: N → S | ||||||
Compositional bias | 237-251 | Basic and acidic residues | ||||
Sequence: PLKPAREDSENKDHA | ||||||
Sequence conflict | 273 | in Ref. 2; AAC51300 | ||||
Sequence: P → L | ||||||
Sequence conflict | 275 | in Ref. 1; AAB62226 | ||||
Sequence: L → V | ||||||
Compositional bias | 276-292 | Basic and acidic residues | ||||
Sequence: SKNGEEKKEDRKIDAAK | ||||||
Compositional bias | 348-364 | Pro residues | ||||
Sequence: PPLFTLGPPPPKPNRPP | ||||||
Compositional bias | 368-389 | Polar residues | ||||
Sequence: LTKFHKTSSGNSTSKGQTSYST | ||||||
Compositional bias | 390-427 | Pro residues | ||||
Sequence: TSLPPPPPSHPASQPPLPASHPSQPPVPSLPPRNIKPP | ||||||
Compositional bias | 462-502 | Basic and acidic residues | ||||
Sequence: YEDIEASKEREKKREKEEKKRLELEKKEQKEKEKKEQEIKK | ||||||
Sequence conflict | 541 | in Ref. 4; BAF83092 | ||||
Sequence: R → C | ||||||
Alternative sequence | VSP_042309 | 636 | in isoform FYB-130 and isoform 3 | |||
Sequence: G → GSTLQVQEKSNTWSWGILKMLKGKDDRKKSIREKPKVSDSDNNEGSS | ||||||
Sequence conflict | 674 | in Ref. 4; BAF83092 | ||||
Sequence: K → E | ||||||
Sequence conflict | 729 | in Ref. 4; BAF83092 | ||||
Sequence: V → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF001862 EMBL· GenBank· DDBJ | AAB62226.1 EMBL· GenBank· DDBJ | mRNA | ||
U93049 EMBL· GenBank· DDBJ | AAC51300.1 EMBL· GenBank· DDBJ | mRNA | ||
AF198052 EMBL· GenBank· DDBJ | AAF62400.1 EMBL· GenBank· DDBJ | mRNA | ||
AK290403 EMBL· GenBank· DDBJ | BAF83092.1 EMBL· GenBank· DDBJ | mRNA | ||
AK297077 EMBL· GenBank· DDBJ | BAG59594.1 EMBL· GenBank· DDBJ | mRNA | ||
AC008964 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC010633 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC025471 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471119 EMBL· GenBank· DDBJ | EAW55984.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC117449 EMBL· GenBank· DDBJ | AAI17450.1 EMBL· GenBank· DDBJ | mRNA | ||
BC143645 EMBL· GenBank· DDBJ | AAI43646.1 EMBL· GenBank· DDBJ | mRNA |