Q91V57 · CHIN_MOUSE
- ProteinN-chimaerin
- GeneChn1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids459 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
GTPase-activating protein for p21-rac and a phorbol ester receptor. May play an important role in neuronal signal-transduction mechanisms (By similarity).
Involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance
Involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance
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 | |
---|---|---|
Molecular Function | ephrin receptor binding | |
Molecular Function | GTPase activator activity | |
Molecular Function | metal ion binding | |
Biological Process | ephrin receptor signaling pathway | |
Biological Process | motor neuron axon guidance | |
Biological Process | regulation of axonogenesis | |
Biological Process | regulation of GTPase activity | |
Biological Process | regulation of small GTPase mediated signal transduction |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN-chimaerin
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ91V57
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Mice are viable and fertile but display a loss of coordination of limb movement which phenocopies the one of Epha4 mutant mice.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 13 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000056695 | 2-459 | N-chimaerin | |||
Sequence: ALTLFDTDEYRPPVWKSYLYQLQQEAPHPRRVTCTCEVENRPKYYGREYHGMISREETDQLLSVAEGSYLIRESQRQPGTYTLALRFGSQTRNFRLYYDGKHFVGEKRFESIHDLVTDGLITLYIETKAAEYIAKMTINPIYEHIGYTTLNREPAYKQHMAVLKETHDEKEATGQDGVSEKRLTSLVRRATLKENEQIPKYEKVHNFKVHTFRGPHWCEYCANFMWGLIAQGVKCADCGLNVHKQCSKMVPNDCKPDLKHVKKVYSCDLTTLVKAHITKRPMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEKADISVNMYEDINIITGALKLYFRDLPIPLITYDAYPKFIESAKIMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMRSPELDPMAALNDIRYQRLVVELLIKNEDILF | ||||||
Modified residue | 192 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 340 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated. Phosphorylation is EPHA4 kinase activity-dependent.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with EPHA4; effector of EPHA4 in axon guidance linking EPHA4 activation to RAC1 regulation. May also interact with EPHB1 and EPHB2.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q91V57-1 | Epha4 Q03137 | 2 | EBI-1539203, EBI-1539152 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 49-135 | SH2 | ||||
Sequence: EYHGMISREETDQLLSVAEGSYLIRESQRQPGTYTLALRFGSQTRNFRLYYDGKHFVGEKRFESIHDLVTDGLITLYIETKAAEYIA | ||||||
Zinc finger | 205-255 | Phorbol-ester/DAG-type | ||||
Sequence: VHNFKVHTFRGPHWCEYCANFMWGLIAQGVKCADCGLNVHKQCSKMVPNDC | ||||||
Domain | 268-459 | Rho-GAP | ||||
Sequence: CDLTTLVKAHITKRPMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEKADISVNMYEDINIITGALKLYFRDLPIPLITYDAYPKFIESAKIMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMRSPELDPMAALNDIRYQRLVVELLIKNEDILF |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q91V57-1
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
- Length459
- Mass (Da)53,193
- Last updated2006-09-05 v2
- ChecksumEE10CCDA8229C0B0
Q91V57-2
- Name2
- Differences from canonical
- 1-183: MALTLFDTDEYRPPVWKSYLYQLQQEAPHPRRVTCTCEVENRPKYYGREYHGMISREETDQLLSVAEGSYLIRESQRQPGTYTLALRFGSQTRNFRLYYDGKHFVGEKRFESIHDLVTDGLITLYIETKAAEYIAKMTINPIYEHIGYTTLNREPAYKQHMAVLKETHDEKEATGQDGVSEKR → MPSKESWSGRKANRATVHKAKPEGRQQGLLIAALGMKLGSQKSSVTIWQPLKLFAYSQ
Q91V57-3
- Name3
- Differences from canonical
- 1-249: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_020145 | 1-183 | in isoform 2 | |||
Sequence: MALTLFDTDEYRPPVWKSYLYQLQQEAPHPRRVTCTCEVENRPKYYGREYHGMISREETDQLLSVAEGSYLIRESQRQPGTYTLALRFGSQTRNFRLYYDGKHFVGEKRFESIHDLVTDGLITLYIETKAAEYIAKMTINPIYEHIGYTTLNREPAYKQHMAVLKETHDEKEATGQDGVSEKR → MPSKESWSGRKANRATVHKAKPEGRQQGLLIAALGMKLGSQKSSVTIWQPLKLFAYSQ | ||||||
Alternative sequence | VSP_020146 | 1-249 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 253 | in Ref. 4; AAH54770 | ||||
Sequence: N → I | ||||||
Sequence conflict | 275 | in Ref. 2; BAE28074 | ||||
Sequence: K → E | ||||||
Sequence conflict | 331 | in Ref. 2; BAC33996 | ||||
Sequence: N → K |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF332069 EMBL· GenBank· DDBJ | AAK56097.1 EMBL· GenBank· DDBJ | mRNA | ||
AF332070 EMBL· GenBank· DDBJ | AAK56098.1 EMBL· GenBank· DDBJ | mRNA | ||
AK049943 EMBL· GenBank· DDBJ | BAC33996.1 EMBL· GenBank· DDBJ | mRNA | ||
AK007182 EMBL· GenBank· DDBJ | BAB24888.1 EMBL· GenBank· DDBJ | mRNA | ||
AK075606 EMBL· GenBank· DDBJ | BAC35853.1 EMBL· GenBank· DDBJ | mRNA | ||
AK147686 EMBL· GenBank· DDBJ | BAE28074.1 EMBL· GenBank· DDBJ | mRNA | ||
AL928889 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC010825 EMBL· GenBank· DDBJ | AAH10825.1 EMBL· GenBank· DDBJ | mRNA | ||
BC024796 EMBL· GenBank· DDBJ | AAH24796.1 EMBL· GenBank· DDBJ | mRNA | ||
BC025023 EMBL· GenBank· DDBJ | AAH25023.1 EMBL· GenBank· DDBJ | mRNA | ||
BC054770 EMBL· GenBank· DDBJ | AAH54770.1 EMBL· GenBank· DDBJ | mRNA |