Q68EM7 · RHG17_HUMAN
- ProteinRho GTPase-activating protein 17
- GeneARHGAP17
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids881 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex formed with AMOT acts by regulating the uptake of polarity proteins at tight junctions, possibly by deciding whether tight junction transmembrane proteins are recycled back to the plasma membrane or sent elsewhere. Participates in the Ca2+-dependent regulation of exocytosis, possibly by catalyzing GTPase activity of Rho family proteins and by inducing the reorganization of the cortical actin filaments. Acts as a GTPase activator in vitro for RAC1.
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 | bicellular tight junction | |
Cellular Component | cytosol | |
Cellular Component | plasma membrane | |
Molecular Function | GTPase activator activity | |
Molecular Function | SH3 domain binding | |
Biological Process | actin filament organization | |
Biological Process | calcium-ion regulated exocytosis | |
Biological Process | regulation of actin cytoskeleton organization | |
Biological Process | regulation of Rac protein signal transduction | |
Biological Process | signal transduction |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRho GTPase-activating protein 17
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ68EM7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Peripheral membrane protein
Note: Associates with membranes and concentrates at sites of cell-cell contact.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 288 | Loss of function; leading to defects in tight junction maintenance. | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,585 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_0000280462 | 1-881 | UniProt | Rho GTPase-activating protein 17 | |||
Sequence: MKKQFNRMKQLANQTVGRAEKTEVLSEDLLQIERRLDTVRSICHHSHKRLVACFQGQHGTDAERRHKKLPLTALAQNMQEASTQLEDSLLGKMLETCGDAENQLALELSQHEVFVEKEIVDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARWNQAHKSSGTNFQGLPSKIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEKTLPEMRAHQDKWAEKPAFGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSDPHAVAGALKSYLRELPEPLMTFNLYEEWTQVASVQDQDKKLQDLWRTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLLWARNEGTLAEMAAATSVHVVAVIEPIIQHADWFFPEEVEFNVSEAFVPLTTPSSNHSFHTGNDSDSGTLERKRPASMAVMEGDLVKKESFGVKLMDFQAHRRGGTLNRKHISPAFQPPLPPTDGSTVVPAGPEPPPQSSRAESSSGGGTVPSSAGILEQGPSPGDGSPPKPKDPVSAAVPAPGRNNSQIASGQNQPQAAAGSHQLSMGQPHNAAGPSPHTLRRAVKKPAPAPPKPGNPPPGHPGGQSSSGTSQHPPSLSPKPPTRSPSPPTQHTGQPPGQPSAPSQLSAPRRYSSSLSPIQAPNHPPPQPPTQATPLMHTKPNSQGPPNPMALPSEHGLEQPSHTPPQTPTPPSTPPLGKQNPSLPAPQTLAGGNPETAQPHAGTLPRPRPVPKPRNRPSVPPPPQPPGVHSAGDSSLTNTAPTASKIVTDSNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL | |||||||
Modified residue (large scale data) | 161 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 162 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 164 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 252 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 484 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 484 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 497 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 520 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 551 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 560 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 570 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 575 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 575 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 584 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 599 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 610 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 614 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 625 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 628 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 667 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 674 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 676 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 679 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 679 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 682 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 682 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 702 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 702 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 704 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 704 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 706 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 743 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 753 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 753 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 757 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 757 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 759 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 759 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 762 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 762 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 763 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 763 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 786 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 793 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 808 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 840 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 845 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 859 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed. Expressed at higher level in heart and placenta.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Component of a complex whose core is composed of ARHGAP17, AMOT, PALS1, PATJ and PARD3/PAR3. Interacts with NHERF1, FNBP1, TRIP10, CAPZA (CAPZA1, CAPZA2 or CAPZA3), CAPZB, CD2AP and SH3KBP1/CIN85.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q68EM7 | AMOT Q4VCS5 | 2 | EBI-1642807, EBI-2511319 | |
BINARY | Q68EM7 | AMOT Q4VCS5-2 | 4 | EBI-1642807, EBI-3891843 | |
BINARY | Q68EM7 | SH3BP1 Q9Y3L3 | 4 | EBI-1642807, EBI-346869 | |
BINARY | Q68EM7 | TRIP10 Q15642 | 3 | EBI-1642807, EBI-739936 | |
BINARY | Q68EM7 | TRIP10 Q15642-2 | 3 | EBI-1642807, EBI-6550597 | |
BINARY | Q68EM7 | WDR49 Q8IV35 | 2 | EBI-1642807, EBI-20892940 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-246 | BAR | ||||
Sequence: QTVGRAEKTEVLSEDLLQIERRLDTVRSICHHSHKRLVACFQGQHGTDAERRHKKLPLTALAQNMQEASTQLEDSLLGKMLETCGDAENQLALELSQHEVFVEKEIVDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARWNQAHKSSGTNFQGLPSKIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEKTLPEMRAHQDKWAE | ||||||
Domain | 252-442 | Rho-GAP | ||||
Sequence: TPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSDPHAVAGALKSYLRELPEPLMTFNLYEEWTQVASVQDQDKKLQDLWRTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLLWARNEGTLAEMAAATSVHVVAVIEPIIQHADWFF | ||||||
Region | 459-482 | Disordered | ||||
Sequence: TPSSNHSFHTGNDSDSGTLERKRP | ||||||
Region | 511-881 | Disordered | ||||
Sequence: GGTLNRKHISPAFQPPLPPTDGSTVVPAGPEPPPQSSRAESSSGGGTVPSSAGILEQGPSPGDGSPPKPKDPVSAAVPAPGRNNSQIASGQNQPQAAAGSHQLSMGQPHNAAGPSPHTLRRAVKKPAPAPPKPGNPPPGHPGGQSSSGTSQHPPSLSPKPPTRSPSPPTQHTGQPPGQPSAPSQLSAPRRYSSSLSPIQAPNHPPPQPPTQATPLMHTKPNSQGPPNPMALPSEHGLEQPSHTPPQTPTPPSTPPLGKQNPSLPAPQTLAGGNPETAQPHAGTLPRPRPVPKPRNRPSVPPPPQPPGVHSAGDSSLTNTAPTASKIVTDSNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL | ||||||
Compositional bias | 522-544 | Pro residues | ||||
Sequence: AFQPPLPPTDGSTVVPAGPEPPP | ||||||
Compositional bias | 545-564 | Polar residues | ||||
Sequence: QSSRAESSSGGGTVPSSAGI | ||||||
Compositional bias | 589-621 | Polar residues | ||||
Sequence: APGRNNSQIASGQNQPQAAAGSHQLSMGQPHNA | ||||||
Compositional bias | 636-650 | Pro residues | ||||
Sequence: PAPAPPKPGNPPPGH | ||||||
Compositional bias | 664-685 | Pro residues | ||||
Sequence: PSLSPKPPTRSPSPPTQHTGQP | ||||||
Compositional bias | 686-708 | Polar residues | ||||
Sequence: PGQPSAPSQLSAPRRYSSSLSPI | ||||||
Compositional bias | 709-723 | Pro residues | ||||
Sequence: QAPNHPPPQPPTQAT | ||||||
Motif | 753-766 | SH3-binding | ||||
Sequence: TPPQTPTPPSTPPL | ||||||
Compositional bias | 753-771 | Pro residues | ||||
Sequence: TPPQTPTPPSTPPLGKQNP | ||||||
Compositional bias | 794-818 | Pro residues | ||||
Sequence: LPRPRPVPKPRNRPSVPPPPQPPGV | ||||||
Compositional bias | 820-847 | Polar residues | ||||
Sequence: SAGDSSLTNTAPTASKIVTDSNSRVSEP |
Domain
The BAR domain mediates the interaction with the coiled coil domain of AMOT, leading to its recruitment to tight junctions.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 7 isoforms produced by Alternative splicing.
Q68EM7-1
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
- Length881
- Mass (Da)95,437
- Last updated2004-10-11 v1
- Checksum92029DBFFEAD1001
Q68EM7-2
- Name2
- Differences from canonical
- 497-574: Missing
Q68EM7-3
- Name3
- Differences from canonical
- 1-273: Missing
Q68EM7-4
- Name4
- SynonymsRICH1B
Q68EM7-5
- Name5
- Differences from canonical
- 839-881: DSNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL → GFQNRIAASFLKCTQTQPAKTCLAASCWI
Q68EM7-6
- Name6
- Differences from canonical
- 840-881: SNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL → V
Q68EM7-7
- Name7
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_023683 | 1-273 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_023682 | 1-467 | in isoform 7 | |||
Sequence: Missing | ||||||
Sequence conflict | 139 | in Ref. 2; BAB55203 | ||||
Sequence: K → E | ||||||
Sequence conflict | 167 | in Ref. 1; CAC37948 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 186 | in Ref. 1; CAC37948 | ||||
Sequence: K → R | ||||||
Alternative sequence | VSP_023684 | 215-226 | in isoform 4 | |||
Sequence: LLEAQADYHRKA → ISGRKNQPLGLP | ||||||
Alternative sequence | VSP_023685 | 227-881 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 255 | in Ref. 2; BAB14506 | ||||
Sequence: E → A | ||||||
Sequence conflict | 404 | in Ref. 2; BAB55203 | ||||
Sequence: G → A | ||||||
Alternative sequence | VSP_023686 | 468-496 | in isoform 7 | |||
Sequence: TGNDSDSGTLERKRPASMAVMEGDLVKKE → MCGFNTCGPMGFCLSSLLAWCVDCFFSLC | ||||||
Alternative sequence | VSP_023687 | 497-574 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 522-544 | Pro residues | ||||
Sequence: AFQPPLPPTDGSTVVPAGPEPPP | ||||||
Compositional bias | 545-564 | Polar residues | ||||
Sequence: QSSRAESSSGGGTVPSSAGI | ||||||
Sequence conflict | 575 | in Ref. 2; BAC86144 | ||||
Sequence: S → C | ||||||
Compositional bias | 589-621 | Polar residues | ||||
Sequence: APGRNNSQIASGQNQPQAAAGSHQLSMGQPHNA | ||||||
Compositional bias | 636-650 | Pro residues | ||||
Sequence: PAPAPPKPGNPPPGH | ||||||
Compositional bias | 664-685 | Pro residues | ||||
Sequence: PSLSPKPPTRSPSPPTQHTGQP | ||||||
Compositional bias | 686-708 | Polar residues | ||||
Sequence: PGQPSAPSQLSAPRRYSSSLSPI | ||||||
Compositional bias | 709-723 | Pro residues | ||||
Sequence: QAPNHPPPQPPTQAT | ||||||
Compositional bias | 753-771 | Pro residues | ||||
Sequence: TPPQTPTPPSTPPLGKQNP | ||||||
Compositional bias | 794-818 | Pro residues | ||||
Sequence: LPRPRPVPKPRNRPSVPPPPQPPGV | ||||||
Compositional bias | 820-847 | Polar residues | ||||
Sequence: SAGDSSLTNTAPTASKIVTDSNSRVSEP | ||||||
Alternative sequence | VSP_023688 | 839-881 | in isoform 5 | |||
Sequence: DSNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL → GFQNRIAASFLKCTQTQPAKTCLAASCWI | ||||||
Alternative sequence | VSP_023689 | 840-881 | in isoform 6 | |||
Sequence: SNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL → V | ||||||
Sequence conflict | 855 | in Ref. 2; BAB55203 | ||||
Sequence: M → V |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ306731 EMBL· GenBank· DDBJ | CAC37948.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ306732 EMBL· GenBank· DDBJ | CAC37949.1 EMBL· GenBank· DDBJ | mRNA | ||
AK001170 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AK023281 EMBL· GenBank· DDBJ | BAB14506.1 EMBL· GenBank· DDBJ | mRNA | ||
AK027567 EMBL· GenBank· DDBJ | BAB55203.1 EMBL· GenBank· DDBJ | mRNA | ||
AK125358 EMBL· GenBank· DDBJ | BAC86144.1 EMBL· GenBank· DDBJ | mRNA | ||
AK291691 EMBL· GenBank· DDBJ | BAF84380.1 EMBL· GenBank· DDBJ | mRNA | ||
AL833975 EMBL· GenBank· DDBJ | CAD38819.1 EMBL· GenBank· DDBJ | mRNA | ||
BC001241 EMBL· GenBank· DDBJ | AAH01241.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC080195 EMBL· GenBank· DDBJ | AAH80195.1 EMBL· GenBank· DDBJ | mRNA | ||
AF163257 EMBL· GenBank· DDBJ | AAQ13586.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF173885 EMBL· GenBank· DDBJ | AAQ13632.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |