Q86TB9 · PATL1_HUMAN
- ProteinProtein PAT1 homolog 1
- GenePATL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids770 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
RNA-binding protein involved in deadenylation-dependent decapping of mRNAs, leading to the degradation of mRNAs (PubMed:17936923, PubMed:20543818, PubMed:20584987, PubMed:20852261).
Acts as a scaffold protein that connects deadenylation and decapping machinery (PubMed:17936923, PubMed:20543818, PubMed:20584987, PubMed:20852261).
Required for cytoplasmic mRNA processing body (P-body) assembly (PubMed:17936923, PubMed:20543818, PubMed:20584987, PubMed:20852261).
Acts as a scaffold protein that connects deadenylation and decapping machinery (PubMed:17936923, PubMed:20543818, PubMed:20584987, PubMed:20852261).
Required for cytoplasmic mRNA processing body (P-body) assembly (PubMed:17936923, PubMed:20543818, PubMed:20584987, PubMed:20852261).
(Microbial infection) In case of infection, required for translation and replication of hepatitis C virus (HCV).
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic ribonucleoprotein granule | |
Cellular Component | cytosol | |
Cellular Component | nuclear speck | |
Cellular Component | P-body | |
Cellular Component | PML body | |
Molecular Function | poly(G) binding | |
Molecular Function | poly(U) RNA binding | |
Molecular Function | RNA binding | |
Biological Process | deadenylation-dependent decapping of nuclear-transcribed mRNA | |
Biological Process | P-body assembly |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein PAT1 homolog 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 accessionQ86TB9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 86 | Loss of nuclear export; when associated with A-90, A-93 and A-95. | ||||
Sequence: L → A | ||||||
Mutagenesis | 90 | Loss of nuclear export; when associated with A-86, A-93 and A-95. | ||||
Sequence: L → A | ||||||
Mutagenesis | 93 | Loss of nuclear export; when associated with A-86, A-90 and A-95. | ||||
Sequence: M → A | ||||||
Mutagenesis | 95 | Loss of nuclear export; when associated with A-86, A-90 and A-93. | ||||
Sequence: I → A | ||||||
Mutagenesis | 519 | In mut1; Abolishes RNA-binding, localization to P-body and interaction with the decapping machinery; when associated with A-520; A-591; A-595; A-625 and A-626. | ||||
Sequence: R → A | ||||||
Mutagenesis | 520 | In mut1; Abolishes RNA-binding, localization to P-body and interaction with the decapping machinery; when associated with A-519; A-591; A-595; A-625 and A-626. | ||||
Sequence: R → A | ||||||
Mutagenesis | 523 | In mut2; Abolishes interaction with the decapping machinery and localization to P-body; when associated with A-527; A-530 and S-534. | ||||
Sequence: L → A | ||||||
Mutagenesis | 527 | In mut2; Abolishes interaction with the decapping machinery and localization to P-body; when associated with S-523; A-530 and S-534. | ||||
Sequence: E → A | ||||||
Mutagenesis | 530 | In mut2; Abolishes interaction with the decapping machinery and localization to P-body; when associated with S-523; A-527 and S-534. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 534 | In mut2; Abolishes interaction with the decapping machinery and localization to P-body; when associated with S-523; A-527 and A-530. | ||||
Sequence: L → S | ||||||
Mutagenesis | 539-557 | In mut3; does not affect neither RNA-binding,interaction with the decapping machinery, nor localization to P-body. | ||||
Sequence: YERRYLLSLEEERPALMDD → GSGSGSG | ||||||
Mutagenesis | 591 | In mut1; Abolishes RNA-binding, localization to P-body and interaction with the decapping machinery; when associated with A-519; A-520; A-595; A-625 and A-626. | ||||
Sequence: R → A | ||||||
Mutagenesis | 595 | In mut1; Abolishes RNA-binding, localization to P-body and interaction with the decapping machinery; when associated with A-519; A-520; A-591; A-625 and A-626. | ||||
Sequence: R → A | ||||||
Mutagenesis | 625 | In mut1; Abolishes RNA-binding, localization to P-body and interaction with the decapping machinery; when associated with A-519; A-520; A-591; A-595 and A-626. | ||||
Sequence: K → A | ||||||
Mutagenesis | 626 | In mut1; Abolishes RNA-binding, localization to P-body and interaction with the decapping machinery; when associated with A-519; A-520; A-591; A-595 and A-625. | ||||
Sequence: K → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 719 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 chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000320963 | 1-770 | UniProt | Protein PAT1 homolog 1 | |||
Sequence: MFRYESLEDCPLDEDEDAFQGLGEEDEEIDQFNDDTFGSGAVDDDWQEAHERLAELEEKLPVAVNEQTGNGERDEMDLLGDHEENLAERLSKMVIENELEDPAIMRAVQTRPVLQPQPGSLNSSIWDGSEVLRRIRGPLLAQEMPTVSVLEYALPQRPPQGPEDDRDLSERALPRRSTSPIIGSPPVRAVPIGTPPKQMAVPSFTQQILCPKPVHVRPPMPPRYPAPYGERMSPNQLCSVPNSSLLGHPFPPSVPPVLSPLQRAQLLGGAQLQPGRMSPSQFARVPGFVGSPLAAMNPKLLQGRVGQMLPPAPGFRAFFSAPPSATPPPQQHPPGPGPHLQNLRSQAPMFRPDTTHLHPQHRRLLHQRQQQNRSQHRNLNGAGDRGSHRSSHQDHLRKDPYANLMLQREKDWVSKIQMMQLQSTDPYLDDFYYQNYFEKLEKLSAAEEIQGDGPKKERTKLITPQVAKLEHAYKPVQFEGSLGKLTVSSVNNPRKMIDAVVTSRSEDDETKEKQVRDKRRKTLVIIEKTYSLLLDVEDYERRYLLSLEEERPALMDDRKHKICSMYDNLRGKLPGQERPSDDHFVQIMCIRKGKRMVARILPFLSTEQAADILMTTARNLPFLIKKDAQDEVLPCLLSPFSLLLYHLPSVSITSLLRQLMNLPQSAATPALSNPHLTAVLQNKFGLSLLLILLSRGEDLQSSDPATESTQNNQWTEVMFMATRELLRIPQAALAKPISIPTNLVSLFSRYVDRQKLNLLETKLQLVQGIR | |||||||
Modified residue (large scale data) | 120 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 177 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 177 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 178 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 178 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 179 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 179 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 184 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 184 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 194 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 194 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 217 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 223 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 263 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 278 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 278 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 284 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 291 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 385 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 473 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts (via region A) with DDX6/RCK (PubMed:20543818, PubMed:20584987, PubMed:31422817, PubMed:31439631).
Interacts (via region H and region C) with LSM1 and LSM4 (PubMed:20584987, PubMed:20852261).
Interacts (via region N) with DCP1A, DCP2, EDC3, EDC4 and XRN1 (PubMed:20543818, PubMed:20584987).
Interacts with the CCR4-NOT complex (PubMed:20584987).
Interacts with the Lsm-containing SMN-Sm protein complex (PubMed:20543818).
Interacts with EIF4ENIF1/4E-T (PubMed:26027925, PubMed:32354837).
Interacts (via region H and region C) with LSM1 and LSM4 (PubMed:20584987, PubMed:20852261).
Interacts (via region N) with DCP1A, DCP2, EDC3, EDC4 and XRN1 (PubMed:20543818, PubMed:20584987).
Interacts with the CCR4-NOT complex (PubMed:20584987).
Interacts with the Lsm-containing SMN-Sm protein complex (PubMed:20543818).
Interacts with EIF4ENIF1/4E-T (PubMed:26027925, PubMed:32354837).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q86TB9 | CNOT1 A5YKK6 | 3 | EBI-2562092, EBI-1222758 | |
BINARY | Q86TB9 | CNOT6 Q9ULM6 | 3 | EBI-2562092, EBI-2104530 | |
BINARY | Q86TB9 | CNOT7 Q9UIV1 | 5 | EBI-2562092, EBI-2105113 | |
BINARY | Q86TB9 | CNOT8 Q9UFF9 | 3 | EBI-2562092, EBI-742299 | |
BINARY | Q86TB9 | DCP1A Q9NPI6 | 2 | EBI-2562092, EBI-374238 | |
BINARY | Q86TB9 | DDX6 P26196 | 16 | EBI-2562092, EBI-351257 | |
BINARY | Q86TB9 | FHL3 Q13643 | 8 | EBI-2562092, EBI-741101 | |
BINARY | Q86TB9 | GOLGA2 Q08379 | 6 | EBI-2562092, EBI-618309 | |
BINARY | Q86TB9 | KRTAP6-2 Q3LI66 | 3 | EBI-2562092, EBI-11962084 | |
BINARY | Q86TB9 | LSM1 O15116 | 19 | EBI-2562092, EBI-347619 | |
BINARY | Q86TB9 | LSM2 Q9Y333 | 3 | EBI-2562092, EBI-347416 | |
BINARY | Q86TB9 | LSM6 P62312 | 5 | EBI-2562092, EBI-373310 | |
BINARY | Q86TB9 | NFKBID Q8NI38 | 3 | EBI-2562092, EBI-10271199 | |
BINARY | Q86TB9 | PSMA3 P25788 | 3 | EBI-2562092, EBI-348380 | |
BINARY | Q86TB9 | TSC1 Q86WV8 | 3 | EBI-2562092, EBI-12806590 | |
BINARY | Q86TB9 | WWOX Q9NZC7-5 | 5 | EBI-2562092, EBI-12040603 | |
BINARY | Q86TB9 | ZMYND12 Q9H0C1 | 3 | EBI-2562092, EBI-12030590 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-26 | Disordered | ||||
Sequence: MFRYESLEDCPLDEDEDAFQGLGEED | ||||||
Region | 1-84 | Region A; interaction with DDX6/RCK | ||||
Sequence: MFRYESLEDCPLDEDEDAFQGLGEEDEEIDQFNDDTFGSGAVDDDWQEAHERLAELEEKLPVAVNEQTGNGERDEMDLLGDHEE | ||||||
Region | 1-397 | Involved in nuclear foci localization | ||||
Sequence: MFRYESLEDCPLDEDEDAFQGLGEEDEEIDQFNDDTFGSGAVDDDWQEAHERLAELEEKLPVAVNEQTGNGERDEMDLLGDHEENLAERLSKMVIENELEDPAIMRAVQTRPVLQPQPGSLNSSIWDGSEVLRRIRGPLLAQEMPTVSVLEYALPQRPPQGPEDDRDLSERALPRRSTSPIIGSPPVRAVPIGTPPKQMAVPSFTQQILCPKPVHVRPPMPPRYPAPYGERMSPNQLCSVPNSSLLGHPFPPSVPPVLSPLQRAQLLGGAQLQPGRMSPSQFARVPGFVGSPLAAMNPKLLQGRVGQMLPPAPGFRAFFSAPPSATPPPQQHPPGPGPHLQNLRSQAPMFRPDTTHLHPQHRRLLHQRQQQNRSQHRNLNGAGDRGSHRSSHQDHLR | ||||||
Compositional bias | 9-26 | Acidic residues | ||||
Sequence: DCPLDEDEDAFQGLGEED | ||||||
Region | 85-388 | Region N; interaction with decapping machinery | ||||
Sequence: NLAERLSKMVIENELEDPAIMRAVQTRPVLQPQPGSLNSSIWDGSEVLRRIRGPLLAQEMPTVSVLEYALPQRPPQGPEDDRDLSERALPRRSTSPIIGSPPVRAVPIGTPPKQMAVPSFTQQILCPKPVHVRPPMPPRYPAPYGERMSPNQLCSVPNSSLLGHPFPPSVPPVLSPLQRAQLLGGAQLQPGRMSPSQFARVPGFVGSPLAAMNPKLLQGRVGQMLPPAPGFRAFFSAPPSATPPPQQHPPGPGPHLQNLRSQAPMFRPDTTHLHPQHRRLLHQRQQQNRSQHRNLNGAGDRGSH | ||||||
Motif | 86-95 | Nuclear export signal | ||||
Sequence: LAERLSKMVI | ||||||
Region | 223-397 | Involved in RNA-binding | ||||
Sequence: RYPAPYGERMSPNQLCSVPNSSLLGHPFPPSVPPVLSPLQRAQLLGGAQLQPGRMSPSQFARVPGFVGSPLAAMNPKLLQGRVGQMLPPAPGFRAFFSAPPSATPPPQQHPPGPGPHLQNLRSQAPMFRPDTTHLHPQHRRLLHQRQQQNRSQHRNLNGAGDRGSHRSSHQDHLR | ||||||
Region | 314-344 | Disordered | ||||
Sequence: GFRAFFSAPPSATPPPQQHPPGPGPHLQNLR | ||||||
Compositional bias | 322-336 | Pro residues | ||||
Sequence: PPSATPPPQQHPPGP | ||||||
Region | 360-399 | Disordered | ||||
Sequence: QHRRLLHQRQQQNRSQHRNLNGAGDRGSHRSSHQDHLRKD | ||||||
Compositional bias | 371-386 | Polar residues | ||||
Sequence: QNRSQHRNLNGAGDRG | ||||||
Region | 389-448 | Region H | ||||
Sequence: RSSHQDHLRKDPYANLMLQREKDWVSKIQMMQLQSTDPYLDDFYYQNYFEKLEKLSAAEE | ||||||
Region | 398-770 | Involved in nuclear speckle localization | ||||
Sequence: KDPYANLMLQREKDWVSKIQMMQLQSTDPYLDDFYYQNYFEKLEKLSAAEEIQGDGPKKERTKLITPQVAKLEHAYKPVQFEGSLGKLTVSSVNNPRKMIDAVVTSRSEDDETKEKQVRDKRRKTLVIIEKTYSLLLDVEDYERRYLLSLEEERPALMDDRKHKICSMYDNLRGKLPGQERPSDDHFVQIMCIRKGKRMVARILPFLSTEQAADILMTTARNLPFLIKKDAQDEVLPCLLSPFSLLLYHLPSVSITSLLRQLMNLPQSAATPALSNPHLTAVLQNKFGLSLLLILLSRGEDLQSSDPATESTQNNQWTEVMFMATRELLRIPQAALAKPISIPTNLVSLFSRYVDRQKLNLLETKLQLVQGIR | ||||||
Region | 449-770 | Region C | ||||
Sequence: IQGDGPKKERTKLITPQVAKLEHAYKPVQFEGSLGKLTVSSVNNPRKMIDAVVTSRSEDDETKEKQVRDKRRKTLVIIEKTYSLLLDVEDYERRYLLSLEEERPALMDDRKHKICSMYDNLRGKLPGQERPSDDHFVQIMCIRKGKRMVARILPFLSTEQAADILMTTARNLPFLIKKDAQDEVLPCLLSPFSLLLYHLPSVSITSLLRQLMNLPQSAATPALSNPHLTAVLQNKFGLSLLLILLSRGEDLQSSDPATESTQNNQWTEVMFMATRELLRIPQAALAKPISIPTNLVSLFSRYVDRQKLNLLETKLQLVQGIR |
Domain
The region A, also named N-term, mediates the interaction with DDX6/RCK and is required for cytoplasmic mRNA processing body assembly.
The region C, also named Pat-C, is required for RNA-binding and mediates the binding with the Lsm-containing SMN-Sm protein complex and the decapping machinery. It folds into an alpha-alpha superhelix, exposing conserved and basic residues on one side of the domain.
Sequence similarities
Belongs to the PAT1 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q86TB9-1
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
- Length770
- Mass (Da)86,850
- Last updated2008-02-26 v2
- Checksum65F7038C4AAC356B
Q86TB9-2
- Name2
- Differences from canonical
- 1-143: Missing
Q86TB9-3
- Name3
- Differences from canonical
- 1-659: Missing
Q86TB9-4
- Name4
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_031778 | 1-143 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_031777 | 1-659 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 9-26 | Acidic residues | ||||
Sequence: DCPLDEDEDAFQGLGEED | ||||||
Sequence conflict | 160 | in Ref. 2; BAG54601 | ||||
Sequence: Q → H | ||||||
Alternative sequence | VSP_040576 | 242-271 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 322-336 | Pro residues | ||||
Sequence: PPSATPPPQQHPPGP | ||||||
Compositional bias | 371-386 | Polar residues | ||||
Sequence: QNRSQHRNLNGAGDRG | ||||||
Alternative sequence | VSP_040577 | 662-698 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 735 | in Ref. 2; BAC04305 and 3; CAD89916 | ||||
Sequence: K → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB065087 EMBL· GenBank· DDBJ | BAB93524.1 EMBL· GenBank· DDBJ | mRNA | ||
AK094193 EMBL· GenBank· DDBJ | BAC04305.1 EMBL· GenBank· DDBJ | mRNA | ||
AK127943 EMBL· GenBank· DDBJ | BAG54601.1 EMBL· GenBank· DDBJ | mRNA | ||
AL831992 EMBL· GenBank· DDBJ | CAD89916.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AP000442 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AP000640 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC065264 EMBL· GenBank· DDBJ | AAH65264.2 EMBL· GenBank· DDBJ | mRNA | ||
BC109038 EMBL· GenBank· DDBJ | AAI09039.1 EMBL· GenBank· DDBJ | mRNA | ||
BC109039 EMBL· GenBank· DDBJ | AAI09040.1 EMBL· GenBank· DDBJ | mRNA | ||
BC111047 EMBL· GenBank· DDBJ | AAI11048.1 EMBL· GenBank· DDBJ | mRNA |