Q9Y6D6 · BIG1_HUMAN
- ProteinBrefeldin A-inhibited guanine nucleotide-exchange protein 1
- GeneARFGEF1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1849 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturation of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined.
Activity regulation
Inhibited by brefeldin A.
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 | cytosol | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Cellular Component | nuclear matrix | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | small nuclear ribonucleoprotein complex | |
Cellular Component | trans-Golgi network | |
Molecular Function | guanyl-nucleotide exchange factor activity | |
Molecular Function | myosin binding | |
Molecular Function | protein kinase A regulatory subunit binding | |
Biological Process | endomembrane system organization | |
Biological Process | exocytosis | |
Biological Process | Golgi organization | |
Biological Process | negative regulation of actin filament polymerization | |
Biological Process | negative regulation of GTPase activity | |
Biological Process | positive regulation of wound healing | |
Biological Process | protein glycosylation | |
Biological Process | protein transport | |
Biological Process | regulation of ARF protein signal transduction | |
Biological Process | regulation of establishment of cell polarity |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBrefeldin A-inhibited guanine nucleotide-exchange protein 1
- Short namesBrefeldin A-inhibited GEP 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 accessionQ9Y6D6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Translocates from cytoplasm to membranes and nucleus upon cAMP treatment.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Developmental delay, impaired speech, and behavioral abnormalities, with or without seizures (DEDISB)
- Note
- DescriptionAn autosomal dominant disorder characterized by mild to moderately impaired intellectual development, language delay, motor deficits, and behavioral abnormalities including aggression, hyperactivity, and autism spectrum disorder. About half of individuals develop various types of seizures. More variable features include dysmorphic facial features, mild ocular anomalies, and non-specific findings on brain imaging.
- See alsoMIM:619964
Natural variants in DEDISB
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_087629 | 648-1849 | missing | in DEDISB; decreased protein abundance | |
VAR_087630 | 798 | D>N | in DEDISB; decreased protein abundance; dbSNP:rs1840520188 | |
VAR_087631 | 842-1849 | missing | in DEDISB | |
VAR_087632 | 1455-1849 | missing | in DEDISB | |
VAR_087633 | 1774-1849 | missing | in DEDISB |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 105 | Loss of interaction with ARL1. | ||||
Sequence: K → D | ||||||
Mutagenesis | 109 | LLoss of interaction with ARL1. | ||||
Sequence: Y → K | ||||||
Mutagenesis | 156 | Loss of interaction with ARL1. | ||||
Sequence: L → D | ||||||
Mutagenesis | 200 | Loss of interaction with ARL1. | ||||
Sequence: Q → E | ||||||
Mutagenesis | 221 | No effect on self-association. | ||||
Sequence: E → K | ||||||
Natural variant | VAR_028749 | 273 | in dbSNP:rs4321984 | |||
Sequence: D → Y | ||||||
Natural variant | VAR_036155 | 316 | in a colorectal cancer sample; somatic mutation | |||
Sequence: G → E | ||||||
Natural variant | VAR_087629 | 648-1849 | in DEDISB; decreased protein abundance | |||
Sequence: Missing | ||||||
Mutagenesis | 712-714 | Inhibits nuclear localization. | ||||
Sequence: KPK → AAA | ||||||
Natural variant | VAR_087630 | 798 | in DEDISB; decreased protein abundance; dbSNP:rs1840520188 | |||
Sequence: D → N | ||||||
Natural variant | VAR_087631 | 842-1849 | in DEDISB | |||
Sequence: Missing | ||||||
Mutagenesis | 883 | Abolishes cAMP-induced nuclear localization. | ||||
Sequence: S → A | ||||||
Mutagenesis | 883 | No effect on cAMP-induced nuclear localization. | ||||
Sequence: S → D | ||||||
Natural variant | VAR_087632 | 1455-1849 | in DEDISB | |||
Sequence: Missing | ||||||
Natural variant | VAR_087633 | 1774-1849 | in DEDISB | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,350 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_0000120207 | 1-1849 | UniProt | Brefeldin A-inhibited guanine nucleotide-exchange protein 1 | |||
Sequence: MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKAETEKQSPPHGEAKAGSSTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGNAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMEKERHRQHHHLLQSPVSHHEPESPQLRYLPPQTVDHISQEHEGDLDLHTNDVDKSLQDDTEPENGSDISSAENEQTEADQATAAETLSKNEVLYDGENHDCEEKPQDIVQNIVEEMVNIVVGDMGEGTTINASADGNIGTIEDGSDSENIQANGIPGTPISVAYTPSLPDDRLSVSSNDTQESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPIFRTNEMFINAIKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQSVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTLGQEKPSEQEMSEIKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFNKKPKRGIQYLQEQGMLGTTPEDIAQFLHQEERLDSTQVGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRMFLEGFRLPGEAQKIDRLMEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGKKISMKETKELTIPTKSSKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAFSVGLQDCDDTEVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGTKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFSVFHLAASDQDESIVELAFQTTGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQAFKEYTSDDMNVAPEDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKTYGHTYEKHWWQDLFRIVFRIFDNMKLPEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIWDKTCNCTLDIFKTTIPHALLTWRPNSGETAPPPPSPVSEKPLDTISQKSVDIHDSIQPRSVDNRPQAPLVSASAVNEEVSKIKSTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSKKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLFKLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYMDESRVSAWEEVQQRLLNVCSEALSYFLTLTSESHREAWTNLLLLFLTKVLKISDNRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGVVFQISQPPEQELGINKQ | |||||||
Modified residue (large scale data) | 48 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 52 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 52 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 234 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 243 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 286 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 286 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 289 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 290 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 394 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 396 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 397 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 397 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 407 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 410 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 410 | 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) | 670 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1079 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1079 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1555 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1558 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1564 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1566 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1566 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1569 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1569 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1580 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated. In vitro phosphorylated by PKA reducing its GEF activity and dephosphorylated by phosphatase PP1.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in placenta, lung, heart, brain, kidney and pancreas.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer (PubMed:17640864).
Interacts with ARFGEF2/BIG2; both proteins are probably part of the same or very similar macromolecular complexes (PubMed:10716990).
Interacts with FKBP2 (PubMed:12606707).
Interacts with MYO9B (PubMed:15644318).
Interacts with PRKAR1A and PRKAR2A (PubMed:12571360).
Interacts with PPP1CC (PubMed:17360629).
Interacts with NCL, FBL, NUP62 and U3 small nucleolar RNA (PubMed:14973189, PubMed:18292223).
Interacts with DPY30 (PubMed:19651892).
Interacts with PDE3A (PubMed:19332778).
Interacts with KANK1 (PubMed:22084092).
Interacts with TBC1D22A and TBC1D22B (PubMed:23572552).
Interacts (via N-terminus) with ARL1 (PubMed:27373159, PubMed:27436755).
Interacts with ARFGEF2/BIG2; both proteins are probably part of the same or very similar macromolecular complexes (PubMed:10716990).
Interacts with FKBP2 (PubMed:12606707).
Interacts with MYO9B (PubMed:15644318).
Interacts with PRKAR1A and PRKAR2A (PubMed:12571360).
Interacts with PPP1CC (PubMed:17360629).
Interacts with NCL, FBL, NUP62 and U3 small nucleolar RNA (PubMed:14973189, PubMed:18292223).
Interacts with DPY30 (PubMed:19651892).
Interacts with PDE3A (PubMed:19332778).
Interacts with KANK1 (PubMed:22084092).
Interacts with TBC1D22A and TBC1D22B (PubMed:23572552).
Interacts (via N-terminus) with ARL1 (PubMed:27373159, PubMed:27436755).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y6D6 | ARFGEF2 Q9Y6D5 | 14 | EBI-1044254, EBI-2837511 | |
BINARY | Q9Y6D6 | KANK1 Q14678 | 8 | EBI-1044254, EBI-2556221 | |
BINARY | Q9Y6D6 | KIF21A Q7Z4S6 | 7 | EBI-1044254, EBI-2691397 | |
BINARY | Q9Y6D6 | KIF21A Q7Z4S6-2 | 4 | EBI-1044254, EBI-6251716 | |
BINARY | Q9Y6D6 | MYCBP Q99417 | 6 | EBI-1044254, EBI-716185 | |
BINARY | Q9Y6D6 | MYO9B Q13459-2 | 2 | EBI-1044254, EBI-6251250 | |
BINARY | Q9Y6D6 | NCL P19338 | 5 | EBI-1044254, EBI-346967 | |
BINARY | Q9Y6D6 | PDE3A Q14432 | 6 | EBI-1044254, EBI-7192066 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-224 | DCB; DCB:DCB domain and DCB:HUS domain interaction | ||||
Sequence: YEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKAETEKQSPPHGEAKAGSSTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGNAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMEKER | ||||||
Region | 46-65 | Disordered | ||||
Sequence: AETEKQSPPHGEAKAGSSTL | ||||||
Compositional bias | 216-236 | Basic and acidic residues | ||||
Sequence: EAKQMEKERHRQHHHLLQSPV | ||||||
Region | 216-248 | Disordered | ||||
Sequence: EAKQMEKERHRQHHHLLQSPVSHHEPESPQLRY | ||||||
Compositional bias | 264-281 | Basic and acidic residues | ||||
Sequence: DLDLHTNDVDKSLQDDTE | ||||||
Region | 264-302 | Disordered | ||||
Sequence: DLDLHTNDVDKSLQDDTEPENGSDISSAENEQTEADQAT | ||||||
Compositional bias | 282-302 | Polar residues | ||||
Sequence: PENGSDISSAENEQTEADQAT | ||||||
Region | 378-413 | Disordered | ||||
Sequence: TPISVAYTPSLPDDRLSVSSNDTQESGNSSGPSPGA | ||||||
Compositional bias | 390-413 | Polar residues | ||||
Sequence: DDRLSVSSNDTQESGNSSGPSPGA | ||||||
Region | 557-577 | HUS; DCB:HUS domain interaction | ||||
Sequence: ADAQSVVDIYVNYDCDLNAAN | ||||||
Domain | 709-840 | SEC7 | ||||
Sequence: FNKKPKRGIQYLQEQGMLGTTPEDIAQFLHQEERLDSTQVGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRMFLEGFRLPGEAQKIDRLMEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHS | ||||||
Motif | 711-715 | Nuclear localization signal (NLS) | ||||
Sequence: KKPKR | ||||||
Region | 1543-1562 | Disordered | ||||
Sequence: RPNSGETAPPPPSPVSEKPL |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,849
- Mass (Da)208,767
- Last updated2006-10-17 v2
- Checksum1EB2547F28F63BCA
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 216-236 | Basic and acidic residues | ||||
Sequence: EAKQMEKERHRQHHHLLQSPV | ||||||
Sequence conflict | 233 | in Ref. 1; AAD38427 | ||||
Sequence: Q → P | ||||||
Compositional bias | 264-281 | Basic and acidic residues | ||||
Sequence: DLDLHTNDVDKSLQDDTE | ||||||
Compositional bias | 282-302 | Polar residues | ||||
Sequence: PENGSDISSAENEQTEADQAT | ||||||
Compositional bias | 390-413 | Polar residues | ||||
Sequence: DDRLSVSSNDTQESGNSSGPSPGA | ||||||
Sequence conflict | 620 | in Ref. 1; AAD38427 | ||||
Sequence: L → S | ||||||
Sequence conflict | 1055 | in Ref. 1; AAD38427 | ||||
Sequence: E → K | ||||||
Sequence conflict | 1590 | in Ref. 3; BAA91912 | ||||
Sequence: V → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF084520 EMBL· GenBank· DDBJ | AAD38427.1 EMBL· GenBank· DDBJ | mRNA | ||
AF111162 EMBL· GenBank· DDBJ | AAD43651.1 EMBL· GenBank· DDBJ | mRNA | ||
AK001788 EMBL· GenBank· DDBJ | BAA91912.1 EMBL· GenBank· DDBJ | mRNA | ||
AL117446 EMBL· GenBank· DDBJ | CAB55931.1 EMBL· GenBank· DDBJ | mRNA |