Q9QX74 · SHAN2_RAT
- ProteinSH3 and multiple ankyrin repeat domains protein 2
- GeneShank2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1474 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Seems to be an adapter protein in the postsynaptic density (PSD) of excitatory synapses that interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors, and the actin-based cytoskeleton. May play a role in the structural and functional organization of the dendritic spine and synaptic junction.
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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Names & Taxonomy
Protein names
- Recommended nameSH3 and multiple ankyrin repeat domains protein 2
- Short namesShank2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ9QX74
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with cortactin in growth cones in differentiating hippocampal neurons. Present in the dendritic spines of cerebellar Purkinje cells (By similarity).
Colocalizes with cortactin in growth cones in differentiating hippocampal neurons. Colocalized with PDE4D to the apical membrane of colonic crypt cells
Colocalizes with cortactin in growth cones in differentiating hippocampal neurons. Colocalized with PDE4D to the apical membrane of colonic crypt cells
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000174674 | 1-1474 | SH3 and multiple ankyrin repeat domains protein 2 | |||
Sequence: MKSLLNAFTKKEVPFREAPAYSNRRRRPPNTLAAPRVLLRSNSDNNLNAGAPEWAVCSAATSHRSLSPQLLQQTPSKPDGATKSLGSYAPGPRSRSPSLNRLGGAGEDGKRPQPPHWHVGSPFTPGANKDSLSTFEYPGPRRKLYSAVPGRLFVAIKPYQPQVDGEIPLHRGDRVKVLSIGEGGFWEGSARGHIGWFPAECVEEVQCKPRDSQAETRADRSKKLFRHYTVGSYDSFDAASDCIIEDKTVVLQKKDNEGFGFVLRGAKADTPIEEFTPTPAFPALQYLESVDEGGVAWQAGLRTGDFLIEVNNENVVKVGHRQVVNMIRQGGNHLVLKVVTVTRNLDPDDTARKKAPPPPKRAPTTALTLRSKSMTAELEELGLSLVDKASVRKKKDKPEEIVPASKPSRTAENVAIESRVATIKQRPTSRCFPAASDVNSVYERQGIAVMTPTVPGSPKGPFLGLPRGTMRRQKSIDSRIFLSGITEEERQFLAPPMLKFTRSLSMPDTSEDIPPPPQSVPPSPPPPSPTTYNCPRSPTPRVYGTIKPAFNQNPVAKVPPATRSDTVATMMREKGMFYRRELDRFSLDSEDVYSRSPAPQAAFRTKRGQMPENPYSEVGKIASKAVYVPAKPARRKGMLVKQSNVEDSPEKTCSIPIPTIIVKEPSTSSSGKSSQGSSMEIDPQATEPGQLRPDDSLTVSSPFAAAIAGAVRDREKRLEARRNSPAFLSTDLGDEDVGLGPPAPRMQPSKFPEEGGFGDEDETEQPLLPTPGAAPRELENHFLGGGEAGAQGEAGGPLSSTSKAKGPESGPAAALKSSSPASPENYVHPLTGRLLDPSSPLALALSARDRAMQESQQGHKGEAPKADLNKPLYIDTKMRPSVESGFPPVTRQNTRGPLRRQETENKYETDLSKDRRADDKKNMLINIVDTAQQKSAGLLMVHTVDIPVAGPPLEEEEDREDGDTKPDHSPSTVPEGVPKTEGALQISAAPEPAAAPGRTIVAAGSVEEAVILPFRIPPPPLASVDLDEDFLFTEPLPPPLEFANSFDIPDDRAASVPALADLVKQKKSDTPQPPSLNSSQPANSTDSKKPAGISNCLPSSFLPPPESFDAVTDSGIEEVDSRSSSDHHLETTSTISTVSSISTLSSEGGESMDTCTVYADGQAFVVDKPPVPPKPKMKPIVHKSNALYQDTLPEEDTDGFVIPPPAPPPPPGSAQAGVAKVIQPRTSKLWGDVTEVKSPILSGPKANVISELNSILQQMNRGKSVKPGEGLELPVGAKSANLAPRSPEVMSTVSGTRSTTVTFTVRPGTSQPITLQSRPPDYESRTSGPRRAPSPVVSPTELSKEILPTPPSAAAASPSPTLSDVFSLPSQSPAGDLFGLNPAGRSRSPSPSILQQPISNKPFTTKPVHLWTKPDVADWLESLNLGEHKETFMDNEIDGSHLPNLQKEDLIDLGVTRVGHRMNIERALKQLLDR | ||||||
Modified residue | 162 | In isoform Q9QX74-4; Phosphoserine | ||||
Sequence: Q | ||||||
Modified residue | 162 | In isoform Q9QX74-5; Phosphoserine | ||||
Sequence: Q | ||||||
Modified residue | 162 | In isoform Q9QX74-6; Phosphoserine | ||||
Sequence: Q | ||||||
Modified residue | 373 | In isoform Q9QX74-2; Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 373 | In isoform Q9QX74-3; Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 457 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 486 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 586 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 724 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 903 | Phosphothreonine | ||||
Sequence: T | ||||||
Glycosylation | 1292 | O-linked (GlcNAc) threonine | ||||
Sequence: T | ||||||
Modified residue | 1334 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1338 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in epithelial cells (at protein level). All isoforms except isoform 7 are expressed predominantly in brain, with highest levels in olfactory bulb, cerebral cortex, cerebellum, central gray matter and hippocampus. Moderate levels of expression are seen in the caudate putamen, thalamic nuclei and brain stem. In cerebellum primarily expressed in Purkinje cells. Isoform 7 is not expressed in brain but expressed in liver, cholangiocytes and thymus. Isoform 7 is present in pancreas, colonic mucosa and thymocytes (at protein level).
Developmental stage
Expressed during early postnatal brain development, especially in the caudate putamen and thalamic nuclei. Expression in the cerebral cortex, the hippocampus and the cerebellum is moderate to high at P5 and shows a stable expression throughout development. Isoforms 1, 2, 4 and 6 are predominantly expressed in cerebellum up to the age of approximately 3 weeks. Isoform 1 expression decreases during development of cortex but slightly increases in cerebellum.
Gene expression databases
Interaction
Subunit
Is part of a complex with DLG4/PSD-95 and DLGAP1/GKAP. Interacts with CTTN/cortactin SH3 domain, DLGAP1/GKAP and alpha-latrotoxin receptor 1. Interacts with DNM2, DBNL, GRID2, BAIAP2, SLC9A3, PLCB3 and CFTR. Interacts with ABI1 (via SH3 domain). Interacts (via proline-rich region) with PDE4D isoform 5 (via N-terminal region). Interacts with PDE4D isoform 33, isoform 4, isoform 7, isoform 8 and isoform 9 but not isoform 32 and isoform 6. Interacts weakly with PDE4D isoform 31. Interacts with ABI1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q9QX74 | Arhgef7 Q9ES28-2 | 4 | EBI-397902, EBI-8620514 | |
XENO | Q9QX74 | CFTR P13569 | 3 | EBI-397902, EBI-349854 | |
BINARY | Q9QX74 | Pde4d P14270-8 | 4 | EBI-397902, EBI-9032440 | |
BINARY | Q9QX74 | Plcb3 Q99JE6 | 4 | EBI-397902, EBI-36481538 | |
BINARY | Q9QX74 | Slc9a3 P26433 | 5 | EBI-397902, EBI-961694 | |
XENO | Q9QX74-4 | Arhgef7 Q9ES28 | 3 | EBI-36481413, EBI-642580 | |
BINARY | Q9QX74-7 | Cacna1d P27732 | 2 | EBI-20939146, EBI-8072674 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 66-81 | Polar residues | ||||
Sequence: LSPQLLQQTPSKPDGA | ||||||
Region | 66-125 | Disordered | ||||
Sequence: LSPQLLQQTPSKPDGATKSLGSYAPGPRSRSPSLNRLGGAGEDGKRPQPPHWHVGSPFTP | ||||||
Domain | 148-207 | SH3 | ||||
Sequence: VPGRLFVAIKPYQPQVDGEIPLHRGDRVKVLSIGEGGFWEGSARGHIGWFPAECVEEVQC | ||||||
Domain | 248-342 | PDZ | ||||
Sequence: TVVLQKKDNEGFGFVLRGAKADTPIEEFTPTPAFPALQYLESVDEGGVAWQAGLRTGDFLIEVNNENVVKVGHRQVVNMIRQGGNHLVLKVVTVT | ||||||
Region | 392-413 | Disordered | ||||
Sequence: RKKKDKPEEIVPASKPSRTAEN | ||||||
Region | 504-534 | Disordered | ||||
Sequence: LSMPDTSEDIPPPPQSVPPSPPPPSPTTYNC | ||||||
Compositional bias | 510-534 | Pro residues | ||||
Sequence: SEDIPPPPQSVPPSPPPPSPTTYNC | ||||||
Region | 659-920 | Disordered | ||||
Sequence: TIIVKEPSTSSSGKSSQGSSMEIDPQATEPGQLRPDDSLTVSSPFAAAIAGAVRDREKRLEARRNSPAFLSTDLGDEDVGLGPPAPRMQPSKFPEEGGFGDEDETEQPLLPTPGAAPRELENHFLGGGEAGAQGEAGGPLSSTSKAKGPESGPAAALKSSSPASPENYVHPLTGRLLDPSSPLALALSARDRAMQESQQGHKGEAPKADLNKPLYIDTKMRPSVESGFPPVTRQNTRGPLRRQETENKYETDLSKDRRADDK | ||||||
Compositional bias | 661-684 | Polar residues | ||||
Sequence: IVKEPSTSSSGKSSQGSSMEIDPQ | ||||||
Compositional bias | 897-920 | Basic and acidic residues | ||||
Sequence: PLRRQETENKYETDLSKDRRADDK | ||||||
Region | 947-995 | Disordered | ||||
Sequence: PVAGPPLEEEEDREDGDTKPDHSPSTVPEGVPKTEGALQISAAPEPAAA | ||||||
Region | 1057-1153 | Disordered | ||||
Sequence: PALADLVKQKKSDTPQPPSLNSSQPANSTDSKKPAGISNCLPSSFLPPPESFDAVTDSGIEEVDSRSSSDHHLETTSTISTVSSISTLSSEGGESMD | ||||||
Compositional bias | 1068-1094 | Polar residues | ||||
Sequence: SDTPQPPSLNSSQPANSTDSKKPAGIS | ||||||
Compositional bias | 1128-1152 | Polar residues | ||||
Sequence: HLETTSTISTVSSISTLSSEGGESM | ||||||
Motif | 1169-1175 | SH3-binding | ||||
Sequence: PPVPPKP | ||||||
Region | 1195-1216 | Disordered | ||||
Sequence: EDTDGFVIPPPAPPPPPGSAQA | ||||||
Compositional bias | 1200-1214 | Pro residues | ||||
Sequence: FVIPPPAPPPPPGSA | ||||||
Region | 1260-1401 | Disordered | ||||
Sequence: NRGKSVKPGEGLELPVGAKSANLAPRSPEVMSTVSGTRSTTVTFTVRPGTSQPITLQSRPPDYESRTSGPRRAPSPVVSPTELSKEILPTPPSAAAASPSPTLSDVFSLPSQSPAGDLFGLNPAGRSRSPSPSILQQPISNK | ||||||
Compositional bias | 1285-1323 | Polar residues | ||||
Sequence: RSPEVMSTVSGTRSTTVTFTVRPGTSQPITLQSRPPDYE | ||||||
Compositional bias | 1356-1370 | Polar residues | ||||
Sequence: ASPSPTLSDVFSLPS | ||||||
Compositional bias | 1385-1401 | Polar residues | ||||
Sequence: RSRSPSPSILQQPISNK | ||||||
Domain | 1411-1474 | SAM | ||||
Sequence: WTKPDVADWLESLNLGEHKETFMDNEIDGSHLPNLQKEDLIDLGVTRVGHRMNIERALKQLLDR |
Domain
The PDZ domain is required for interaction with GRID2, PLCB3, SLC9A3 and CFTR.
Sequence similarities
Belongs to the SHANK family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 7 isoforms produced by Alternative splicing. So far detected are complete isoforms 2 to 5. Experimental confirmation may be lacking for some isoforms.
Q9QX74-1
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.
- Name1
- Length1,474
- Mass (Da)158,684
- Last updated2002-07-26 v2
- ChecksumF503D44D0D9AB7C1
Q9QX74-2
- Name2
- Differences from canonical
- 382-385: Missing
Q9QX74-3
- Name3
Q9QX74-4
- Name4
Q9QX74-5
- Name5
Q9QX74-6
- Name6
Q9QX74-7
- Name7
- SynonymsE
- NoteContains 6 ANK repeats at positions 196-226, 230-259, 263-293, 297-326, 330-359, 363-393.
- Differences from canonical
- 1-12: MKSLLNAFTKKE → MPRSPTSSEDEMAQSFSDYSVGSESDSSKEETIYDTIRATTEKPGGVKMEDLQGNTLVIRVVIQDLQQTKCIRFNPDATVWVAKQRILCTLNQGLKDVLNYGLFQPASNGRDGKFLDEERLLREYPQPMGQGVPSLEFRYKKRVYKQSNLDEKQLARLHTKTNLKKFMDHTQHRSVEKLVKLLDRGLDPNFHDLETGETPLTLAAQLDGSMEVIKALRNGGAHLDFRSRDGMTALHKAARMRNQVALKTLLELGASPDYKDSYGLTPLYHTAIVGGDPYCCELLLHEHASVCCKDENGWHEIHQACRYGHVQHLEHLLFYGADMSAQNASGNTALHICALYNQDSCARVLLFRGGDKELKNYNSQTPFQVAIIAGNFELAEYIKNHKETDI
- 382-395: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
M0R5T5 | M0R5T5_RAT | Shank2 | 1472 | ||
A0A8L2RC58 | A0A8L2RC58_RAT | Shank2 | 1278 | ||
A0A8L2QYJ0 | A0A8L2QYJ0_RAT | Shank2 | 1832 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_020049 | 1-12 | in isoform 7 | |||
Sequence: MKSLLNAFTKKE → MPRSPTSSEDEMAQSFSDYSVGSESDSSKEETIYDTIRATTEKPGGVKMEDLQGNTLVIRVVIQDLQQTKCIRFNPDATVWVAKQRILCTLNQGLKDVLNYGLFQPASNGRDGKFLDEERLLREYPQPMGQGVPSLEFRYKKRVYKQSNLDEKQLARLHTKTNLKKFMDHTQHRSVEKLVKLLDRGLDPNFHDLETGETPLTLAAQLDGSMEVIKALRNGGAHLDFRSRDGMTALHKAARMRNQVALKTLLELGASPDYKDSYGLTPLYHTAIVGGDPYCCELLLHEHASVCCKDENGWHEIHQACRYGHVQHLEHLLFYGADMSAQNASGNTALHICALYNQDSCARVLLFRGGDKELKNYNSQTPFQVAIIAGNFELAEYIKNHKETDI | ||||||
Alternative sequence | VSP_006081 | 1-211 | in isoform 4, isoform 5 and isoform 6 | |||
Sequence: Missing | ||||||
Sequence conflict | 35-41 | in Ref. 4 | ||||
Sequence: PRVLLRS → QKNLGAA | ||||||
Compositional bias | 66-81 | Polar residues | ||||
Sequence: LSPQLLQQTPSKPDGA | ||||||
Sequence conflict | 152 | in Ref. 3; AAF02497 | ||||
Sequence: L → F | ||||||
Alternative sequence | VSP_006082 | 212-239 | in isoform 4, isoform 5 and isoform 6 | |||
Sequence: SQAETRADRSKKLFRHYTVGSYDSFDAA → MMSVPGGGAATVMMTGYNNGRYPRNSLY | ||||||
Sequence conflict | 369 | in Ref. 1; AAC62226 | ||||
Sequence: L → V | ||||||
Alternative sequence | VSP_006083 | 382-385 | in isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_020050 | 382-395 | in isoform 7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_006084 | 388-394 | in isoform 3 and isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_006085 | 468-476 | in isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_006086 | 468-483 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 510-534 | Pro residues | ||||
Sequence: SEDIPPPPQSVPPSPPPPSPTTYNC | ||||||
Compositional bias | 661-684 | Polar residues | ||||
Sequence: IVKEPSTSSSGKSSQGSSMEIDPQ | ||||||
Compositional bias | 897-920 | Basic and acidic residues | ||||
Sequence: PLRRQETENKYETDLSKDRRADDK | ||||||
Compositional bias | 1068-1094 | Polar residues | ||||
Sequence: SDTPQPPSLNSSQPANSTDSKKPAGIS | ||||||
Compositional bias | 1128-1152 | Polar residues | ||||
Sequence: HLETTSTISTVSSISTLSSEGGESM | ||||||
Compositional bias | 1200-1214 | Pro residues | ||||
Sequence: FVIPPPAPPPPPGSA | ||||||
Compositional bias | 1285-1323 | Polar residues | ||||
Sequence: RSPEVMSTVSGTRSTTVTFTVRPGTSQPITLQSRPPDYE | ||||||
Compositional bias | 1356-1370 | Polar residues | ||||
Sequence: ASPSPTLSDVFSLPS | ||||||
Compositional bias | 1385-1401 | Polar residues | ||||
Sequence: RSRSPSPSILQQPISNK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF060116 EMBL· GenBank· DDBJ | AAC62226.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ249562 EMBL· GenBank· DDBJ | CAB56522.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ131899 EMBL· GenBank· DDBJ | CAB44314.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ131899 EMBL· GenBank· DDBJ | CAB44312.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ131899 EMBL· GenBank· DDBJ | CAB44313.1 EMBL· GenBank· DDBJ | mRNA | ||
AY298755 EMBL· GenBank· DDBJ | AAP85236.1 EMBL· GenBank· DDBJ | mRNA | ||
AF141903 EMBL· GenBank· DDBJ | AAF02497.1 EMBL· GenBank· DDBJ | mRNA | ||
AF159048 EMBL· GenBank· DDBJ | AAD42977.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |