Q9UPA5 · BSN_HUMAN
- ProteinProtein bassoon
- GeneBSN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids3926 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Scaffold protein of the presynaptic cytomatrix at the active zone (CAZ) which is the place in the synapse where neurotransmitter is released (PubMed:12812759).
After synthesis, participates in the formation of Golgi-derived membranous organelles termed Piccolo-Bassoon transport vesicles (PTVs) that are transported along axons to sites of nascent synaptic contacts (PubMed:19380881).
At the presynaptic active zone, regulates the spatial organization of synaptic vesicle cluster, the protein complexes that execute membrane fusion and compensatory endocytosis (By similarity).
Functions also in processes other than assembly such as the regulation of specific presynaptic protein ubiquitination by interacting with SIAH1 or the regulation of presynaptic autophagy by associating with ATG5 (By similarity).
Mediates also synapse to nucleus communication leading to reconfiguration of gene expression by associating with the transcriptional corepressor CTBP1 and by subsequently reducing the size of its pool available for nuclear import (By similarity).
Inhibits the activity of the proportion of DAO enzyme that localizes to the presynaptic active zone, which may modulate synaptic transmission (By similarity).
After synthesis, participates in the formation of Golgi-derived membranous organelles termed Piccolo-Bassoon transport vesicles (PTVs) that are transported along axons to sites of nascent synaptic contacts (PubMed:19380881).
At the presynaptic active zone, regulates the spatial organization of synaptic vesicle cluster, the protein complexes that execute membrane fusion and compensatory endocytosis (By similarity).
Functions also in processes other than assembly such as the regulation of specific presynaptic protein ubiquitination by interacting with SIAH1 or the regulation of presynaptic autophagy by associating with ATG5 (By similarity).
Mediates also synapse to nucleus communication leading to reconfiguration of gene expression by associating with the transcriptional corepressor CTBP1 and by subsequently reducing the size of its pool available for nuclear import (By similarity).
Inhibits the activity of the proportion of DAO enzyme that localizes to the presynaptic active zone, which may modulate synaptic transmission (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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Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein bassoon
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UPA5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane ; Peripheral membrane protein
Note: In retina, is localized in the outer plexiform layer at ribbon synapses formed by rods and cones but was absent from basal synaptic contacts formed by cones. In the retinal inner plexiform layer localized to conventional inhibitory GABAergic synapses, made by amacrine cells, but absent from the bipolar cell ribbon synapses.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_055105 | 741 | in dbSNP:rs34762726 | |||
Sequence: A → T | ||||||
Natural variant | VAR_055106 | 1213 | in dbSNP:rs35762866 | |||
Sequence: G → D | ||||||
Natural variant | VAR_055107 | 3863 | in dbSNP:rs2005557 | |||
Sequence: A → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 4,366 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue, modified residue (large scale data), glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Lipidation | 2 | UniProt | N-myristoyl glycine | ||||
Sequence: G | |||||||
Chain | PRO_0000065002 | 2-3926 | UniProt | Protein bassoon | |||
Sequence: GNEVSLEGGAGDGPLPPGGAGPGPGPGPGPGAGKPPSAPAGGGQLPAAGAARSTAVPPVPGPGPGPGPGPGPGSTSRRLDPKEPLGNQRAASPTPKQASATTPGHESPRETRAQGPAGQEADGPRRTLQVDSRTQRSGRSPSVSPDRGSTPTSPYSVPQIAPLPSSTLCPICKTSDLTSTPSQPNFNTCTQCHNKVCNQCGFNPNPHLTQVKEWLCLNCQMQRALGMDMTTAPRSKSQQQLHSPALSPAHSPAKQPLGKPDQERSRGPGGPQPGSRQAETARATSVPGPAQAAAPPEVGRVSPQPPQPTKPSTAEPRPPAGEAPAKSATAVPAGLGATEQTQEGLTGKLFGLGASLLTQASTLMSVQPEADTQGQPAPSKGTPKIVFNDASKEAGPKPLGSGPGPGPAPGAKTEPGARMGPGSGPGALPKTGGTTSPKHGRAEHQAASKAAAKPKTMPKERAICPLCQAELNVGSKSPANYNTCTTCRLQVCNLCGFNPTPHLVEKTEWLCLNCQTKRLLEGSLGEPTPLPPPTSQQPPVGAPHRASGTSPLKQKGPQGLGQPSGPLPAKASPLSTKASPLPSKASPQAKPLRASEPSKTPSSVQEKKTRVPTKAEPMPKPPPETTPTPATPKVKSGVRRAEPATPVVKAVPEAPKGGEAEDLVGKPYSQDASRSPQSLSDTGYSSDGISSSQSEITGVVQQEVEQLDSAGVTGPHPPSPSEIHKVGSSMRPLLQAQGLAPSERSKPLSSGTGEEQKQRPHSLSITPEAFDSDEELEDILEEDEDSAEWRRRREQQDTAESSDDFGSQLRHDYVEDSSEGGLSPLPPQPPARAAELTDEDFMRRQILEMSAEEDNLEEDDTATSGRGLAKHGTQKGGPRPRPEPSQEPAALPKRRLPHNATTGYEELLPEGGSAEATDGSGTLQGGLRRFKTIELNSTGSYGHELDLGQGPDPSLDREPELEMESLTGSPEDRSRGEHSSTLPASTPSYTSGTSPTSLSSLEEDSDSSPSRRQRLEEAKQQRKARHRSHGPLLPTIEDSSEEEELREEEELLREQEKMREVEQQRIRSTARKTRRDKEELRAQRRRERSKTPPSNLSPIEDASPTEELRQAAEMEELHRSSCSEYSPSPSLDSEAEALDGGPSRLYKSGSEYNLPTFMSLYSPTETPSGSSTTPSSGRPLKSAEEAYEEMMRKAELLQRQQGQAAGARGPHGGPSQPTGPRGLGSFEYQDTTDREYGQAAQPAAEGTPASLGAAVYEEILQTSQSIVRMRQASSRDLAFAEDKKKEKQFLNAESAYMDPMKQNGGPLTPGTSPTQLAAPVSFSTPTSSDSSGGRVIPDVRVTQHFAKETQDPLKLHSSPASPSSASKEIGMPFSQGPGTPATTAVAPCPAGLPRGYMTPASPAGSERSPSPSSTAHSYGHSPTTANYGSQTEDLPQAPSGLAAAGRAAREKPLSASDGEGGTPQPSRAYSYFASSSPPLSPSSPSESPTFSPGKMGPRATAEFSTQTPSPAPASDMPRSPGAPTPSPMVAQGTQTPHRPSTPRLVWQESSQEAPFMVITLASDASSQTRMVHASASTSPLCSPTETQPTTHGYSQTTPPSVSQLPPEPPGPPGFPRVPSAGADGPLALYGWGALPAENISLCRISSVPGTSRVEPGPRTPGTAVVDLRTAVKPTPIILTDQGMDLTSLAVEARKYGLALDPIPGRQSTAVQPLVINLNAQEHTFLATATTVSITMASSVFMAQQKQPVVYGDPYQSRLDFGQGGGSPVCLAQVKQVEQAVQTAPYRSGPRGRPREAKFARYNLPNQVAPLARRDVLITQMGTAQSIGLKPGPVPEPGAEPHRATPAELRSHALPGARKPHTVVVQMGEGTAGTVTTLLPEEPAGALDLTGMRPESQLACCDMVYKLPFGSSCTGTFHPAPSVPEKSMADAAPPGQSSSPFYGPRDPEPPEPPTYRAQGVVGPGPHEEQRPYPQGLPGRLYSSMSDTNLAEAGLNYHAQRIGQLFQGPGRDSAMDLSSLKHSYSLGFADGRYLGQGLQYGSVTDLRHPTDLLAHPLPMRRYSSVSNIYSDHRYGPRGDAVGFQEASLAQYSATTAREISRMCAALNSMDQYGGRHGSGGGGPDLVQYQPQHGPGLSAPQSLVPLRPGLLGNPTFPEGHPSPGNLAQYGPAAGQGTAVRQLLPSTATVRAADGMIYSTINTPIAATLPITTQPASVLRPMVRGGMYRPYASGGITAVPLTSLTRVPMIAPRVPLGPTGLYRYPAPSRFPIASSVPPAEGPVYLGKPAAAKAPGAGGPSRPEMPVGAAREEPLPTTTPAAIKEAAGAPAPAPLAGQKPPADAAPGGGSGALSRPGFEKEEASQEERQRKQQEQLLQLERERVELEKLRQLRLQEELERERVELQRHREEEQLLVQRELQELQTIKHHVLQQQQEERQAQFALQREQLAQQRLQLEQIQQLQQQLQQQLEEQKQRQKAPFPAACEAPGRGPPLAAAELAQNGQYWPPLTHAAFIAMAGPEGLGQPREPVLHRGLPSSASDMSLQTEEQWEASRSGIKKRHSMPRLRDACELESGTEPCVVRRIADSSVQTDDEDGESRYLLSRRRRARRSADCSVQTDDEDSAEWEQPVRRRRSRLPRHSDSGSDSKHDATASSSSAAATVRAMSSVGIQTISDCSVQTEPDQLPRVSPAIHITAATDPKVEIVRYISAPEKTGRGESLACQTEPDGQAQGVAGPQLVGPTAISPYLPGIQIVTPGPLGRFEKKKPDPLEIGYQAHLPPESLSQLVSRQPPKSPQVLYSPVSPLSPHRLLDTSFASSERLNKAHVSPQKHFTADSALRQQTLPRPMKTLQRSLSDPKPLSPTAEESAKERFSLYQHQGGLGSQVSALPPNSLVRKVKRTLPSPPPEEAHLPLAGQASPQLYAASLLQRGLTGPTTVPATKASLLRELDRDLRLVEHESTKLRKKQAELDEEEKEIDAKLKYLELGITQRKESLAKDRGGRDYPPLRGLGEHRDYLSDSELNQLRLQGCTTPAGQFVDFPATAAAPATPSGPTAFQQPRFQPPAPQYSAGSGGPTQNGFPAHQAPTYPGPSTYPAPAFPPGASYPAEPGLPNQQAFRPTGHYAGQTPMPTTQSTLFPVPADSRAPLQKPRQTSLADLEQKVPTNYEVIASPVVPMSSAPSETSYSGPAVSSGYEQGKVPEVPRAGDRGSVSQSPAPTYPSDSHYTSLEQNVPRNYVMIDDISELTKDSTSTAPDSQRLEPLGPGSSGRPGKEPGEPGVLDGPTLPCCYARGEEESEEDSYDPRGKGGHLRSMESNGRPASTHYYGDSDYRHGARVEKYGPGPMGPKHPSKSLAPAAISSKRSKHRKQGMEQKISKFSPIEEAKDVESDLASYPPPAVSSSLVSRGRKFQDEITYGLKKNVYEQQKYYGMSSRDAVEDDRIYGGSSRSRAPSAYSGEKLSSHDFSGWGKGYEREREAVERLQKAGPKPSSLSMAHSRVRPPMRSQASEEESPVSPLGRPRPAGGPLPPGGDTCPQFCSSHSMPDVQEHVKDGPRAHAYKREEGYILDDSHCVVSDSEAYHLGQEETDWFDKPRDARSDRFRHHGGHAVSSSSQKRGPARHSYHDYDEPPEEGLWPHDEGGPGRHASAKEHRHGDHGRHSGRHTGEEPGRRAAKPHARDLGRHEARPHSQPSSAPAMPKKGQPGYPSSAEYSQPSRASSAYHHASDSKKGSRQAHSGPAALQSKAEPQAQPQLQGRQAAPGPQQSQSPSSRQIPSGAASRQPQTQQQQQGLGLQPPQQALTQARLQQQSQPTTRGSAPAASQPAGKPQPGPSTATGPQPAGPPRAEQTNGSKGTAKAPQQGRAPQAQPAPGPGPAGVKAGARPGGTPGAPAGQPGADGESVFSKILPGGAAEQAGKLTEAVSAFGKKFSSFW | |||||||
Modified residue | 145 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 148 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 244 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 244 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 248 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 248 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 252 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 867 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 970 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1040 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1040 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1041 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1041 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1090 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1090 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1092 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1092 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1098 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1098 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1104 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1104 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1226 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1309 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Glycosylation | 1343 | UniProt | O-linked (GlcNAc) threonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1362 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 1384 | UniProt | O-linked (GlcNAc) threonine | ||||
Sequence: T | |||||||
Modified residue | 1477 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1477 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1481 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1484 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1486 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1488 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1488 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1787 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 1791 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 1801 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 1801 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 1813 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 1985 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2041 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2041 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2046 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 2063 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2076 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 2250 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 2260 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 2266 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Glycosylation | 2314 | UniProt | O-linked (GlcNAc) threonine | ||||
Sequence: T | |||||||
Modified residue | 2570 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2587 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2587 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2614 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Glycosylation | 2691 | UniProt | O-linked (GlcNAc) threonine | ||||
Sequence: T | |||||||
Modified residue | 2802 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2849 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2851 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2851 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2857 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2857 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 2936 | UniProt | O-linked (GlcNAc) threonine | ||||
Sequence: T | |||||||
Modified residue | 3013 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3013 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 3291 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 3373 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 3492 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 3509 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 3808 | UniProt | Omega-N-methylarginine | ||||
Sequence: R |
Post-translational modification
Myristoylated. The N-terminal myristoylation is not sufficient for presynaptic localization (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with PCLO, ERC2/CAST1, RIMS1 and UNC13A (By similarity).
Interacts with TPRG1L (By similarity).
Interacts with DYNLL1 and DYNLL2; these interactions potentially link PTVs to dynein and myosin V motor complexes (PubMed:19380881).
Interacts with ATG5; this interaction is important for the regulation of presynaptic autophagy (By similarity).
Interacts (via C-terminus) with TRIO (via N-terminus) (By similarity).
Interacts with CTBP1 (By similarity).
Interacts with SIAH1; this interaction negatively regulates SIAH1 E3 ligase activity (By similarity).
Interacts (via coiled region) with DAO; the interaction is direct (By similarity).
Interacts with TPRG1L (By similarity).
Interacts with DYNLL1 and DYNLL2; these interactions potentially link PTVs to dynein and myosin V motor complexes (PubMed:19380881).
Interacts with ATG5; this interaction is important for the regulation of presynaptic autophagy (By similarity).
Interacts (via C-terminus) with TRIO (via N-terminus) (By similarity).
Interacts with CTBP1 (By similarity).
Interacts with SIAH1; this interaction negatively regulates SIAH1 E3 ligase activity (By similarity).
Interacts (via coiled region) with DAO; the interaction is direct (By similarity).
Protein-protein interaction databases
Miscellaneous
Family & Domains
Features
Showing features for region, compositional bias, zinc finger, repeat, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-161 | Disordered | ||||
Sequence: MGNEVSLEGGAGDGPLPPGGAGPGPGPGPGPGAGKPPSAPAGGGQLPAAGAARSTAVPPVPGPGPGPGPGPGPGSTSRRLDPKEPLGNQRAASPTPKQASATTPGHESPRETRAQGPAGQEADGPRRTLQVDSRTQRSGRSPSVSPDRGSTPTSPYSVPQI | ||||||
Compositional bias | 18-36 | Pro residues | ||||
Sequence: PGGAGPGPGPGPGPGAGKP | ||||||
Region | 23-32 | 5 X 2 AA tandem repeats of P-G | ||||
Sequence: PGPGPGPGPG | ||||||
Compositional bias | 58-72 | Pro residues | ||||
Sequence: PPVPGPGPGPGPGPG | ||||||
Region | 61-74 | 7 X 2 AA tandem repeats of P-G | ||||
Sequence: PGPGPGPGPGPGPG | ||||||
Compositional bias | 91-109 | Polar residues | ||||
Sequence: AASPTPKQASATTPGHESP | ||||||
Compositional bias | 129-161 | Polar residues | ||||
Sequence: LQVDSRTQRSGRSPSVSPDRGSTPTSPYSVPQI | ||||||
Zinc finger | 170-193 | C4-type | ||||
Sequence: CPICKTSDLTSTPSQPNFNTCTQC | ||||||
Zinc finger | 198-220 | C4-type | ||||
Sequence: CNQCGFNPNPHLTQVKEWLCLNC | ||||||
Region | 231-343 | Disordered | ||||
Sequence: TTAPRSKSQQQLHSPALSPAHSPAKQPLGKPDQERSRGPGGPQPGSRQAETARATSVPGPAQAAAPPEVGRVSPQPPQPTKPSTAEPRPPAGEAPAKSATAVPAGLGATEQTQ | ||||||
Compositional bias | 232-247 | Polar residues | ||||
Sequence: TAPRSKSQQQLHSPAL | ||||||
Compositional bias | 300-319 | Pro residues | ||||
Sequence: GRVSPQPPQPTKPSTAEPRP | ||||||
Compositional bias | 366-380 | Polar residues | ||||
Sequence: SVQPEADTQGQPAPS | ||||||
Region | 366-459 | Disordered | ||||
Sequence: SVQPEADTQGQPAPSKGTPKIVFNDASKEAGPKPLGSGPGPGPAPGAKTEPGARMGPGSGPGALPKTGGTTSPKHGRAEHQAASKAAAKPKTMP | ||||||
Zinc finger | 465-488 | C4-type | ||||
Sequence: CPLCQAELNVGSKSPANYNTCTTC | ||||||
Zinc finger | 493-515 | C4-type | ||||
Sequence: CNLCGFNPTPHLVEKTEWLCLNC | ||||||
Region | 524-927 | Disordered | ||||
Sequence: SLGEPTPLPPPTSQQPPVGAPHRASGTSPLKQKGPQGLGQPSGPLPAKASPLSTKASPLPSKASPQAKPLRASEPSKTPSSVQEKKTRVPTKAEPMPKPPPETTPTPATPKVKSGVRRAEPATPVVKAVPEAPKGGEAEDLVGKPYSQDASRSPQSLSDTGYSSDGISSSQSEITGVVQQEVEQLDSAGVTGPHPPSPSEIHKVGSSMRPLLQAQGLAPSERSKPLSSGTGEEQKQRPHSLSITPEAFDSDEELEDILEEDEDSAEWRRRREQQDTAESSDDFGSQLRHDYVEDSSEGGLSPLPPQPPARAAELTDEDFMRRQILEMSAEEDNLEEDDTATSGRGLAKHGTQKGGPRPRPEPSQEPAALPKRRLPHNATTGYEELLPEGGSAEATDGSGTLQGG | ||||||
Repeat | 571-577 | 1 | ||||
Sequence: KASPLST | ||||||
Region | 571-591 | 3 X 7 AA tandem repeats of K-A-S-P-[LQ]-[APS]-[KST] | ||||
Sequence: KASPLSTKASPLPSKASPQAK | ||||||
Repeat | 578-584 | 2 | ||||
Sequence: KASPLPS | ||||||
Repeat | 585-591 | 3 | ||||
Sequence: KASPQAK | ||||||
Compositional bias | 594-609 | Polar residues | ||||
Sequence: RASEPSKTPSSVQEKK | ||||||
Compositional bias | 616-630 | Pro residues | ||||
Sequence: AEPMPKPPPETTPTP | ||||||
Compositional bias | 671-709 | Polar residues | ||||
Sequence: QDASRSPQSLSDTGYSSDGISSSQSEITGVVQQEVEQLD | ||||||
Compositional bias | 743-766 | Polar residues | ||||
Sequence: SERSKPLSSGTGEEQKQRPHSLSI | ||||||
Compositional bias | 771-785 | Acidic residues | ||||
Sequence: FDSDEELEDILEEDE | ||||||
Compositional bias | 786-818 | Basic and acidic residues | ||||
Sequence: DSAEWRRRREQQDTAESSDDFGSQLRHDYVEDS | ||||||
Compositional bias | 837-852 | Basic and acidic residues | ||||
Sequence: LTDEDFMRRQILEMSA | ||||||
Region | 940-1248 | Disordered | ||||
Sequence: GSYGHELDLGQGPDPSLDREPELEMESLTGSPEDRSRGEHSSTLPASTPSYTSGTSPTSLSSLEEDSDSSPSRRQRLEEAKQQRKARHRSHGPLLPTIEDSSEEEELREEEELLREQEKMREVEQQRIRSTARKTRRDKEELRAQRRRERSKTPPSNLSPIEDASPTEELRQAAEMEELHRSSCSEYSPSPSLDSEAEALDGGPSRLYKSGSEYNLPTFMSLYSPTETPSGSSTTPSSGRPLKSAEEAYEEMMRKAELLQRQQGQAAGARGPHGGPSQPTGPRGLGSFEYQDTTDREYGQAAQPAAEGT | ||||||
Compositional bias | 951-979 | Basic and acidic residues | ||||
Sequence: GPDPSLDREPELEMESLTGSPEDRSRGEH | ||||||
Compositional bias | 980-1005 | Polar residues | ||||
Sequence: SSTLPASTPSYTSGTSPTSLSSLEED | ||||||
Compositional bias | 1006-1024 | Basic and acidic residues | ||||
Sequence: SDSSPSRRQRLEEAKQQRK | ||||||
Coiled coil | 1037-1092 | |||||
Sequence: IEDSSEEEELREEEELLREQEKMREVEQQRIRSTARKTRRDKEELRAQRRRERSKT | ||||||
Compositional bias | 1051-1092 | Basic and acidic residues | ||||
Sequence: ELLREQEKMREVEQQRIRSTARKTRRDKEELRAQRRRERSKT | ||||||
Compositional bias | 1107-1121 | Basic and acidic residues | ||||
Sequence: EELRQAAEMEELHRS | ||||||
Compositional bias | 1150-1180 | Polar residues | ||||
Sequence: GSEYNLPTFMSLYSPTETPSGSSTTPSSGRP | ||||||
Coiled coil | 1181-1208 | |||||
Sequence: LKSAEEAYEEMMRKAELLQRQQGQAAGA | ||||||
Coiled coil | 1276-1294 | |||||
Sequence: RDLAFAEDKKKEKQFLNAE | ||||||
Region | 1298-1547 | Disordered | ||||
Sequence: MDPMKQNGGPLTPGTSPTQLAAPVSFSTPTSSDSSGGRVIPDVRVTQHFAKETQDPLKLHSSPASPSSASKEIGMPFSQGPGTPATTAVAPCPAGLPRGYMTPASPAGSERSPSPSSTAHSYGHSPTTANYGSQTEDLPQAPSGLAAAGRAAREKPLSASDGEGGTPQPSRAYSYFASSSPPLSPSSPSESPTFSPGKMGPRATAEFSTQTPSPAPASDMPRSPGAPTPSPMVAQGTQTPHRPSTPRLVW | ||||||
Compositional bias | 1306-1334 | Polar residues | ||||
Sequence: GPLTPGTSPTQLAAPVSFSTPTSSDSSGG | ||||||
Compositional bias | 1355-1382 | Polar residues | ||||
Sequence: KLHSSPASPSSASKEIGMPFSQGPGTPA | ||||||
Compositional bias | 1404-1437 | Polar residues | ||||
Sequence: AGSERSPSPSSTAHSYGHSPTTANYGSQTEDLPQ | ||||||
Compositional bias | 1460-1491 | Polar residues | ||||
Sequence: EGGTPQPSRAYSYFASSSPPLSPSSPSESPTF | ||||||
Compositional bias | 1527-1547 | Polar residues | ||||
Sequence: SPMVAQGTQTPHRPSTPRLVW | ||||||
Compositional bias | 1570-1601 | Polar residues | ||||
Sequence: RMVHASASTSPLCSPTETQPTTHGYSQTTPPS | ||||||
Region | 1570-1620 | Disordered | ||||
Sequence: RMVHASASTSPLCSPTETQPTTHGYSQTTPPSVSQLPPEPPGPPGFPRVPS | ||||||
Compositional bias | 1602-1619 | Pro residues | ||||
Sequence: VSQLPPEPPGPPGFPRVP | ||||||
Region | 1924-1978 | Disordered | ||||
Sequence: PEKSMADAAPPGQSSSPFYGPRDPEPPEPPTYRAQGVVGPGPHEEQRPYPQGLPG | ||||||
Region | 2287-2310 | Disordered | ||||
Sequence: AAKAPGAGGPSRPEMPVGAAREEP | ||||||
Region | 2324-2370 | Disordered | ||||
Sequence: GAPAPAPLAGQKPPADAAPGGGSGALSRPGFEKEEASQEERQRKQQE | ||||||
Coiled coil | 2351-2476 | |||||
Sequence: RPGFEKEEASQEERQRKQQEQLLQLERERVELEKLRQLRLQEELERERVELQRHREEEQLLVQRELQELQTIKHHVLQQQQEERQAQFALQREQLAQQRLQLEQIQQLQQQLQQQLEEQKQRQKAP | ||||||
Compositional bias | 2355-2370 | Basic and acidic residues | ||||
Sequence: EKEEASQEERQRKQQE | ||||||
Region | 2532-2568 | Disordered | ||||
Sequence: PSSASDMSLQTEEQWEASRSGIKKRHSMPRLRDACEL | ||||||
Compositional bias | 2548-2568 | Basic and acidic residues | ||||
Sequence: ASRSGIKKRHSMPRLRDACEL | ||||||
Region | 2601-2655 | Disordered | ||||
Sequence: RRRARRSADCSVQTDDEDSAEWEQPVRRRRSRLPRHSDSGSDSKHDATASSSSAA | ||||||
Region | 2721-3268 | Interaction with DAO | ||||
Sequence: EPDGQAQGVAGPQLVGPTAISPYLPGIQIVTPGPLGRFEKKKPDPLEIGYQAHLPPESLSQLVSRQPPKSPQVLYSPVSPLSPHRLLDTSFASSERLNKAHVSPQKHFTADSALRQQTLPRPMKTLQRSLSDPKPLSPTAEESAKERFSLYQHQGGLGSQVSALPPNSLVRKVKRTLPSPPPEEAHLPLAGQASPQLYAASLLQRGLTGPTTVPATKASLLRELDRDLRLVEHESTKLRKKQAELDEEEKEIDAKLKYLELGITQRKESLAKDRGGRDYPPLRGLGEHRDYLSDSELNQLRLQGCTTPAGQFVDFPATAAAPATPSGPTAFQQPRFQPPAPQYSAGSGGPTQNGFPAHQAPTYPGPSTYPAPAFPPGASYPAEPGLPNQQAFRPTGHYAGQTPMPTTQSTLFPVPADSRAPLQKPRQTSLADLEQKVPTNYEVIASPVVPMSSAPSETSYSGPAVSSGYEQGKVPEVPRAGDRGSVSQSPAPTYPSDSHYTSLEQNVPRNYVMIDDISELTKDSTSTAPDSQRLEPLGPGSSGRPGKE | ||||||
Region | 2845-2865 | Disordered | ||||
Sequence: TLQRSLSDPKPLSPTAEESAK | ||||||
Coiled coil | 2939-2981 | |||||
Sequence: SLLRELDRDLRLVEHESTKLRKKQAELDEEEKEIDAKLKYLEL | ||||||
Region | 3039-3375 | Disordered | ||||
Sequence: AAAPATPSGPTAFQQPRFQPPAPQYSAGSGGPTQNGFPAHQAPTYPGPSTYPAPAFPPGASYPAEPGLPNQQAFRPTGHYAGQTPMPTTQSTLFPVPADSRAPLQKPRQTSLADLEQKVPTNYEVIASPVVPMSSAPSETSYSGPAVSSGYEQGKVPEVPRAGDRGSVSQSPAPTYPSDSHYTSLEQNVPRNYVMIDDISELTKDSTSTAPDSQRLEPLGPGSSGRPGKEPGEPGVLDGPTLPCCYARGEEESEEDSYDPRGKGGHLRSMESNGRPASTHYYGDSDYRHGARVEKYGPGPMGPKHPSKSLAPAAISSKRSKHRKQGMEQKISKFSPI | ||||||
Compositional bias | 3045-3078 | Polar residues | ||||
Sequence: PSGPTAFQQPRFQPPAPQYSAGSGGPTQNGFPAH | ||||||
Compositional bias | 3083-3102 | Pro residues | ||||
Sequence: YPGPSTYPAPAFPPGASYPA | ||||||
Compositional bias | 3114-3134 | Polar residues | ||||
Sequence: PTGHYAGQTPMPTTQSTLFPV | ||||||
Compositional bias | 3171-3186 | Polar residues | ||||
Sequence: MSSAPSETSYSGPAVS | ||||||
Compositional bias | 3206-3228 | Polar residues | ||||
Sequence: VSQSPAPTYPSDSHYTSLEQNVP | ||||||
Compositional bias | 3286-3306 | Basic and acidic residues | ||||
Sequence: RGEEESEEDSYDPRGKGGHLR | ||||||
Region | 3424-3551 | Disordered | ||||
Sequence: GMSSRDAVEDDRIYGGSSRSRAPSAYSGEKLSSHDFSGWGKGYEREREAVERLQKAGPKPSSLSMAHSRVRPPMRSQASEEESPVSPLGRPRPAGGPLPPGGDTCPQFCSSHSMPDVQEHVKDGPRAH | ||||||
Compositional bias | 3462-3477 | Basic and acidic residues | ||||
Sequence: WGKGYEREREAVERLQ | ||||||
Region | 3572-3897 | Disordered | ||||
Sequence: EAYHLGQEETDWFDKPRDARSDRFRHHGGHAVSSSSQKRGPARHSYHDYDEPPEEGLWPHDEGGPGRHASAKEHRHGDHGRHSGRHTGEEPGRRAAKPHARDLGRHEARPHSQPSSAPAMPKKGQPGYPSSAEYSQPSRASSAYHHASDSKKGSRQAHSGPAALQSKAEPQAQPQLQGRQAAPGPQQSQSPSSRQIPSGAASRQPQTQQQQQGLGLQPPQQALTQARLQQQSQPTTRGSAPAASQPAGKPQPGPSTATGPQPAGPPRAEQTNGSKGTAKAPQQGRAPQAQPAPGPGPAGVKAGARPGGTPGAPAGQPGADGESVFS | ||||||
Compositional bias | 3575-3600 | Basic and acidic residues | ||||
Sequence: HLGQEETDWFDKPRDARSDRFRHHGG | ||||||
Compositional bias | 3612-3680 | Basic and acidic residues | ||||
Sequence: PARHSYHDYDEPPEEGLWPHDEGGPGRHASAKEHRHGDHGRHSGRHTGEEPGRRAAKPHARDLGRHEAR | ||||||
Compositional bias | 3700-3715 | Polar residues | ||||
Sequence: PSSAEYSQPSRASSAY | ||||||
Compositional bias | 3737-3813 | Polar residues | ||||
Sequence: SKAEPQAQPQLQGRQAAPGPQQSQSPSSRQIPSGAASRQPQTQQQQQGLGLQPPQQALTQARLQQQSQPTTRGSAPA | ||||||
Compositional bias | 3836-3855 | Polar residues | ||||
Sequence: PPRAEQTNGSKGTAKAPQQG |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length3,926
- Mass (Da)416,469
- Last updated2009-05-05 v4
- Checksum69B3AA86AD437356
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 18-36 | Pro residues | ||||
Sequence: PGGAGPGPGPGPGPGAGKP | ||||||
Compositional bias | 58-72 | Pro residues | ||||
Sequence: PPVPGPGPGPGPGPG | ||||||
Compositional bias | 91-109 | Polar residues | ||||
Sequence: AASPTPKQASATTPGHESP | ||||||
Compositional bias | 129-161 | Polar residues | ||||
Sequence: LQVDSRTQRSGRSPSVSPDRGSTPTSPYSVPQI | ||||||
Compositional bias | 232-247 | Polar residues | ||||
Sequence: TAPRSKSQQQLHSPAL | ||||||
Compositional bias | 300-319 | Pro residues | ||||
Sequence: GRVSPQPPQPTKPSTAEPRP | ||||||
Compositional bias | 366-380 | Polar residues | ||||
Sequence: SVQPEADTQGQPAPS | ||||||
Compositional bias | 594-609 | Polar residues | ||||
Sequence: RASEPSKTPSSVQEKK | ||||||
Compositional bias | 616-630 | Pro residues | ||||
Sequence: AEPMPKPPPETTPTP | ||||||
Compositional bias | 671-709 | Polar residues | ||||
Sequence: QDASRSPQSLSDTGYSSDGISSSQSEITGVVQQEVEQLD | ||||||
Compositional bias | 743-766 | Polar residues | ||||
Sequence: SERSKPLSSGTGEEQKQRPHSLSI | ||||||
Compositional bias | 771-785 | Acidic residues | ||||
Sequence: FDSDEELEDILEEDE | ||||||
Compositional bias | 786-818 | Basic and acidic residues | ||||
Sequence: DSAEWRRRREQQDTAESSDDFGSQLRHDYVEDS | ||||||
Compositional bias | 837-852 | Basic and acidic residues | ||||
Sequence: LTDEDFMRRQILEMSA | ||||||
Compositional bias | 951-979 | Basic and acidic residues | ||||
Sequence: GPDPSLDREPELEMESLTGSPEDRSRGEH | ||||||
Compositional bias | 980-1005 | Polar residues | ||||
Sequence: SSTLPASTPSYTSGTSPTSLSSLEED | ||||||
Compositional bias | 1006-1024 | Basic and acidic residues | ||||
Sequence: SDSSPSRRQRLEEAKQQRK | ||||||
Compositional bias | 1051-1092 | Basic and acidic residues | ||||
Sequence: ELLREQEKMREVEQQRIRSTARKTRRDKEELRAQRRRERSKT | ||||||
Compositional bias | 1107-1121 | Basic and acidic residues | ||||
Sequence: EELRQAAEMEELHRS | ||||||
Compositional bias | 1150-1180 | Polar residues | ||||
Sequence: GSEYNLPTFMSLYSPTETPSGSSTTPSSGRP | ||||||
Compositional bias | 1306-1334 | Polar residues | ||||
Sequence: GPLTPGTSPTQLAAPVSFSTPTSSDSSGG | ||||||
Compositional bias | 1355-1382 | Polar residues | ||||
Sequence: KLHSSPASPSSASKEIGMPFSQGPGTPA | ||||||
Compositional bias | 1404-1437 | Polar residues | ||||
Sequence: AGSERSPSPSSTAHSYGHSPTTANYGSQTEDLPQ | ||||||
Compositional bias | 1460-1491 | Polar residues | ||||
Sequence: EGGTPQPSRAYSYFASSSPPLSPSSPSESPTF | ||||||
Compositional bias | 1527-1547 | Polar residues | ||||
Sequence: SPMVAQGTQTPHRPSTPRLVW | ||||||
Compositional bias | 1570-1601 | Polar residues | ||||
Sequence: RMVHASASTSPLCSPTETQPTTHGYSQTTPPS | ||||||
Compositional bias | 1602-1619 | Pro residues | ||||
Sequence: VSQLPPEPPGPPGFPRVP | ||||||
Compositional bias | 2355-2370 | Basic and acidic residues | ||||
Sequence: EKEEASQEERQRKQQE | ||||||
Compositional bias | 2548-2568 | Basic and acidic residues | ||||
Sequence: ASRSGIKKRHSMPRLRDACEL | ||||||
Compositional bias | 3045-3078 | Polar residues | ||||
Sequence: PSGPTAFQQPRFQPPAPQYSAGSGGPTQNGFPAH | ||||||
Compositional bias | 3083-3102 | Pro residues | ||||
Sequence: YPGPSTYPAPAFPPGASYPA | ||||||
Compositional bias | 3114-3134 | Polar residues | ||||
Sequence: PTGHYAGQTPMPTTQSTLFPV | ||||||
Compositional bias | 3171-3186 | Polar residues | ||||
Sequence: MSSAPSETSYSGPAVS | ||||||
Compositional bias | 3206-3228 | Polar residues | ||||
Sequence: VSQSPAPTYPSDSHYTSLEQNVP | ||||||
Compositional bias | 3286-3306 | Basic and acidic residues | ||||
Sequence: RGEEESEEDSYDPRGKGGHLR | ||||||
Compositional bias | 3462-3477 | Basic and acidic residues | ||||
Sequence: WGKGYEREREAVERLQ | ||||||
Compositional bias | 3575-3600 | Basic and acidic residues | ||||
Sequence: HLGQEETDWFDKPRDARSDRFRHHGG | ||||||
Compositional bias | 3612-3680 | Basic and acidic residues | ||||
Sequence: PARHSYHDYDEPPEEGLWPHDEGGPGRHASAKEHRHGDHGRHSGRHTGEEPGRRAAKPHARDLGRHEAR | ||||||
Compositional bias | 3700-3715 | Polar residues | ||||
Sequence: PSSAEYSQPSRASSAY | ||||||
Compositional bias | 3737-3813 | Polar residues | ||||
Sequence: SKAEPQAQPQLQGRQAAPGPQQSQSPSSRQIPSGAASRQPQTQQQQQGLGLQPPQQALTQARLQQQSQPTTRGSAPA | ||||||
Compositional bias | 3836-3855 | Polar residues | ||||
Sequence: PPRAEQTNGSKGTAKAPQQG | ||||||
Sequence conflict | 3925 | in Ref. 1; AAC83555 | ||||
Sequence: F → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF052224 EMBL· GenBank· DDBJ | AAC83555.1 EMBL· GenBank· DDBJ | mRNA | ||
AC099668 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC104452 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
Y18448 EMBL· GenBank· DDBJ | CAA77176.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y18449 EMBL· GenBank· DDBJ | CAA77176.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y18450 EMBL· GenBank· DDBJ | CAA77176.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y18451 EMBL· GenBank· DDBJ | CAA77176.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB007894 EMBL· GenBank· DDBJ | BAA23707.1 EMBL· GenBank· DDBJ | mRNA |