P15882 · CHIN_HUMAN
- 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. 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 | |
---|---|---|
Cellular Component | cytosol | |
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 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
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP15882
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Involvement in disease
Duane retraction syndrome 2 (DURS2)
- Note
- DescriptionA form of Duane retraction syndrome, a congenital eye movement disorder characterized by a failure of cranial nerve VI (the abducens nerve) to develop normally, resulting in restriction or absence of abduction, adduction or both, narrowing of the palpebral fissure, and retraction of the globe on attempted adduction. Undiagnosed in children, it can lead to amblyopia, a permanent uncorrectable loss of vision.
- See alsoMIM:604356
Natural variants in DURS2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_047940 | 20 | L>F | in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA); dbSNP:rs121912792 | |
VAR_047941 | 126 | I>M | in DURS2; behaves as a dominant gain-of -function allele that increases CHN1 activity in vitro; dbSNP:rs121912793 | |
VAR_047942 | 143 | Y>H | in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA); dbSNP:rs121912794 | |
VAR_047943 | 223 | A>V | in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA); dbSNP:rs121912795 | |
VAR_047944 | 228 | G>S | in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; dbSNP:rs121912796 | |
VAR_047945 | 252 | P>Q | in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA); dbSNP:rs121912797 | |
VAR_047946 | 313 | E>K | in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; dbSNP:rs121912798 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_047940 | 20 | in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA); dbSNP:rs121912792 | |||
Sequence: L → F | ||||||
Natural variant | VAR_047941 | 126 | in DURS2; behaves as a dominant gain-of -function allele that increases CHN1 activity in vitro; dbSNP:rs121912793 | |||
Sequence: I → M | ||||||
Natural variant | VAR_047942 | 143 | in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA); dbSNP:rs121912794 | |||
Sequence: Y → H | ||||||
Natural variant | VAR_047943 | 223 | in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA); dbSNP:rs121912795 | |||
Sequence: A → V | ||||||
Natural variant | VAR_047944 | 228 | in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; dbSNP:rs121912796 | |||
Sequence: G → S | ||||||
Natural variant | VAR_047945 | 252 | in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA); dbSNP:rs121912797 | |||
Sequence: P → Q | ||||||
Natural variant | VAR_047946 | 313 | in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; dbSNP:rs121912798 | |||
Sequence: E → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 478 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000056694 | 2-459 | UniProt | N-chimaerin | |||
Sequence: ALTLFDTDEYRPPVWKSYLYQLQQEAPHPRRITCTCEVENRPKYYGREFHGMISREAADQLLIVAEGSYLIRESQRQPGTYTLALRFGSQTRNFRLYYDGKHFVGEKRFESIHDLVTDGLITLYIETKAAEYIAKMTINPIYEHVGYTTLNREPAYKKHMPVLKETHDERDSTGQDGVSEKRLTSLVRRATLKENEQIPKYEKIHNFKVHTFRGPHWCEYCANFMWGLIAQGVKCADCGLNVHKQCSKMVPNDCKPDLKHVKKVYSCDLTTLVKAHTTKRPMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEKADISVNMYEDINIITGALKLYFRDLPIPLITYDAYPKFIESAKIMDPDEQLETLHEALKLLPPAHCETLRYLMAHLKRVTLHEKENLMNAENLGIVFGPTLMRSPELDAMAALNDIRYQRLVVELLIKNEDILF | |||||||
Modified residue (large scale data) | 11 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 192 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 340 | UniProt | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated. Phosphorylation is EPHA4 kinase activity-dependent (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
In neurons in brain regions that are involved in learning and memory processes.
Developmental stage
Increases in amount during brain development coincident with synaptogenesis.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with EPHA4; effector of EPHA4 in axon guidance linking EPHA4 activation to RAC1 regulation.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P15882 | ANKK1 Q8NFD2 | 3 | EBI-718947, EBI-13280688 | |
BINARY | P15882 | HEMK1 Q9Y5R4 | 8 | EBI-718947, EBI-10329202 | |
BINARY | P15882 | MAPK1 P28482 | 3 | EBI-718947, EBI-959949 | |
BINARY | P15882 | NCK2 O43639 | 16 | EBI-718947, EBI-713635 |
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: EFHGMISREAADQLLIVAEGSYLIRESQRQPGTYTLALRFGSQTRNFRLYYDGKHFVGEKRFESIHDLVTDGLITLYIETKAAEYIA | ||||||
Zinc finger | 205-255 | Phorbol-ester/DAG-type | ||||
Sequence: IHNFKVHTFRGPHWCEYCANFMWGLIAQGVKCADCGLNVHKQCSKMVPNDC | ||||||
Domain | 268-459 | Rho-GAP | ||||
Sequence: CDLTTLVKAHTTKRPMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEKADISVNMYEDINIITGALKLYFRDLPIPLITYDAYPKFIESAKIMDPDEQLETLHEALKLLPPAHCETLRYLMAHLKRVTLHEKENLMNAENLGIVFGPTLMRSPELDAMAALNDIRYQRLVVELLIKNEDILF |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P15882-1
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.
- NameAlpha-2
- Length459
- Mass (Da)53,172
- Last updated2002-07-11 v3
- Checksum04C4CC9BCC611389
P15882-2
- NameAlpha-1
- Differences from canonical
- 1-183: MALTLFDTDEYRPPVWKSYLYQLQQEAPHPRRITCTCEVENRPKYYGREFHGMISREAADQLLIVAEGSYLIRESQRQPGTYTLALRFGSQTRNFRLYYDGKHFVGEKRFESIHDLVTDGLITLYIETKAAEYIAKMTINPIYEHVGYTTLNREPAYKKHMPVLKETHDERDSTGQDGVSEKR → MPSKESWSGRKTNRAAVHKSKQEGRQQDLLIAALGMKLGSPKSSVTIWQPLKLFAYSQ
P15882-3
- Name3
- Differences from canonical
- 184-209: Missing
Computationally mapped potential isoform sequences
There are 24 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9J1N1 | C9J1N1_HUMAN | CHN1 | 239 | ||
C9J3G1 | C9J3G1_HUMAN | CHN1 | 322 | ||
C9J3V9 | C9J3V9_HUMAN | CHN1 | 277 | ||
F8WCQ9 | F8WCQ9_HUMAN | CHN1 | 165 | ||
F8WAY4 | F8WAY4_HUMAN | CHN1 | 35 | ||
C9JR98 | C9JR98_HUMAN | CHN1 | 285 | ||
F8W6K2 | F8W6K2_HUMAN | CHN1 | 204 | ||
A0A494BZY1 | A0A494BZY1_HUMAN | CHN1 | 145 | ||
B8ZZ96 | B8ZZ96_HUMAN | CHN1 | 275 | ||
A0A494C1H3 | A0A494C1H3_HUMAN | CHN1 | 47 | ||
A0A494C1M7 | A0A494C1M7_HUMAN | CHN1 | 351 | ||
A0A494C1P5 | A0A494C1P5_HUMAN | CHN1 | 87 | ||
A0A494C1Q9 | A0A494C1Q9_HUMAN | CHN1 | 83 | ||
A0A494C1R0 | A0A494C1R0_HUMAN | CHN1 | 234 | ||
A0A494C0V1 | A0A494C0V1_HUMAN | CHN1 | 68 | ||
A0A494C1D3 | A0A494C1D3_HUMAN | CHN1 | 54 | ||
A0A494C0I4 | A0A494C0I4_HUMAN | CHN1 | 145 | ||
A0A494C0I5 | A0A494C0I5_HUMAN | CHN1 | 204 | ||
A0A494C0L5 | A0A494C0L5_HUMAN | CHN1 | 61 | ||
A0A494C0R6 | A0A494C0R6_HUMAN | CHN1 | 81 | ||
A0A494C158 | A0A494C158_HUMAN | CHN1 | 48 | ||
A0A494C047 | A0A494C047_HUMAN | CHN1 | 255 | ||
A0A494C072 | A0A494C072_HUMAN | CHN1 | 49 | ||
A0A494C0C9 | A0A494C0C9_HUMAN | CHN1 | 323 |
Sequence caution
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_001636 | 1-183 | in isoform Alpha-1 | |||
Sequence: MALTLFDTDEYRPPVWKSYLYQLQQEAPHPRRITCTCEVENRPKYYGREFHGMISREAADQLLIVAEGSYLIRESQRQPGTYTLALRFGSQTRNFRLYYDGKHFVGEKRFESIHDLVTDGLITLYIETKAAEYIAKMTINPIYEHVGYTTLNREPAYKKHMPVLKETHDERDSTGQDGVSEKR → MPSKESWSGRKTNRAAVHKSKQEGRQQDLLIAALGMKLGSPKSSVTIWQPLKLFAYSQ | ||||||
Alternative sequence | VSP_043297 | 184-209 | in isoform 3 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X51408 EMBL· GenBank· DDBJ | CAA35769.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
Z22641 EMBL· GenBank· DDBJ | CAA80354.1 EMBL· GenBank· DDBJ | mRNA | ||
AK055060 EMBL· GenBank· DDBJ | BAG51458.1 EMBL· GenBank· DDBJ | mRNA | ||
AK289941 EMBL· GenBank· DDBJ | BAF82630.1 EMBL· GenBank· DDBJ | mRNA | ||
AK300890 EMBL· GenBank· DDBJ | BAG62531.1 EMBL· GenBank· DDBJ | mRNA | ||
AC007435 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC018890 EMBL· GenBank· DDBJ | AAY14688.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC020596 EMBL· GenBank· DDBJ | AAY14940.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471058 EMBL· GenBank· DDBJ | EAX11117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471058 EMBL· GenBank· DDBJ | EAX11118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471058 EMBL· GenBank· DDBJ | EAX11119.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC011393 EMBL· GenBank· DDBJ | AAH11393.1 EMBL· GenBank· DDBJ | mRNA | ||
S75654 EMBL· GenBank· DDBJ | AAB33506.1 EMBL· GenBank· DDBJ | Genomic DNA |