Q9H3Q1 · BORG4_HUMAN
- ProteinCdc42 effector protein 4
- GeneCDC42EP4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids356 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts.
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 | actin cytoskeleton | |
Cellular Component | adherens junction | |
Cellular Component | cytoplasm | |
Cellular Component | cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | endomembrane system | |
Cellular Component | microtubule cytoskeleton | |
Cellular Component | phagocytic vesicle | |
Cellular Component | plasma membrane | |
Molecular Function | RNA binding | |
Molecular Function | small GTPase binding | |
Biological Process | cellular response to type II interferon | |
Biological Process | positive regulation of actin filament polymerization | |
Biological Process | positive regulation of pseudopodium assembly | |
Biological Process | regulation of cell shape | |
Biological Process | Rho protein signal transduction |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCdc42 effector protein 4
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H3Q1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endomembrane system ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 426 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000212655 | 1-356 | UniProt | Cdc42 effector protein 4 | |||
Sequence: MPILKQLVSSSVHSKRRSRADLTAEMISAPLGDFRHTMHVGRAGDAFGDTSFLNSKAGEPDGESLDEQPSSSSSKRSLLSRKFRGSKRSQSVTRGEREQRDMLGSLRDSALFVKNAMSLPQLNEKEAAEKGTSKLPKSLSSSPVKKANDGEGGDEEAGTEEAVPRRNGAAGPHSPDPLLDEQAFGDLTDLPVVPKATYGLKHAESIMSFHIDLGPSMLGDVLSIMDKEEWDPEEGEGGYHGDEGAAGTITQAPPYAVAAPPLARQEGKAGPDLPSLPSHALEDEGWAAAAPSPGSARSMGSHTTRDSSSLSSCTSGILEERSPAFRGPDRARAAVSRQPDKEFSFMDEEEEDEIRV | |||||||
Modified residue | 5 | UniProt | N6-methyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 11 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 18 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 18 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 51 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 64 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 64 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 72 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 105 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 105 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 109 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 109 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 118 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 118 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 138 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 138 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 140 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 140 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 141 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 142 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 142 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 174 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 174 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 239 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 292 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 292 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 295 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 295 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 309 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 322 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 344 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Not detected in any of the adult tissues tested. May be expressed only in fetal or embryonic tissues.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with CDC42 and RHOQ, in a GTP-dependent manner.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9H3Q1 | FAM9B Q8IZU0 | 5 | EBI-744665, EBI-10175124 | |
BINARY | Q9H3Q1 | HTT P42858 | 3 | EBI-744665, EBI-466029 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 27-41 | CRIB | ||||
Sequence: ISAPLGDFRHTMHVG | ||||||
Region | 51-102 | Disordered | ||||
Sequence: SFLNSKAGEPDGESLDEQPSSSSSKRSLLSRKFRGSKRSQSVTRGEREQRDM | ||||||
Compositional bias | 65-79 | Polar residues | ||||
Sequence: LDEQPSSSSSKRSLL | ||||||
Region | 122-182 | Disordered | ||||
Sequence: LNEKEAAEKGTSKLPKSLSSSPVKKANDGEGGDEEAGTEEAVPRRNGAAGPHSPDPLLDEQ | ||||||
Compositional bias | 148-162 | Basic and acidic residues | ||||
Sequence: NDGEGGDEEAGTEEA | ||||||
Region | 257-356 | Disordered | ||||
Sequence: VAAPPLARQEGKAGPDLPSLPSHALEDEGWAAAAPSPGSARSMGSHTTRDSSSLSSCTSGILEERSPAFRGPDRARAAVSRQPDKEFSFMDEEEEDEIRV | ||||||
Compositional bias | 296-318 | Polar residues | ||||
Sequence: ARSMGSHTTRDSSSLSSCTSGIL | ||||||
Compositional bias | 323-344 | Basic and acidic residues | ||||
Sequence: PAFRGPDRARAAVSRQPDKEFS |
Sequence similarities
Belongs to the BORG/CEP family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9H3Q1-1
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
- Length356
- Mass (Da)37,980
- Last updated2001-03-01 v1
- Checksum2CF677C60C6EF1B5
Q9H3Q1-2
- Name2
- Differences from canonical
- 57-126: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 2 | in Ref. 5; AAH10451 | ||||
Sequence: P → L | ||||||
Sequence conflict | 33 | in Ref. 2; AAD16299 | ||||
Sequence: D → T | ||||||
Alternative sequence | VSP_055544 | 57-126 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 65-79 | Polar residues | ||||
Sequence: LDEQPSSSSSKRSLL | ||||||
Compositional bias | 148-162 | Basic and acidic residues | ||||
Sequence: NDGEGGDEEAGTEEA | ||||||
Sequence conflict | 288 | in Ref. 2; AAD16299 | ||||
Sequence: A → T | ||||||
Sequence conflict | 296 | in Ref. 2; AAD16299 | ||||
Sequence: A → T | ||||||
Compositional bias | 296-318 | Polar residues | ||||
Sequence: ARSMGSHTTRDSSSLSSCTSGIL | ||||||
Compositional bias | 323-344 | Basic and acidic residues | ||||
Sequence: PAFRGPDRARAAVSRQPDKEFS | ||||||
Sequence conflict | 339 | in Ref. 2; AAD16299 | ||||
Sequence: P → PP | ||||||
Sequence conflict | 355 | in Ref. 2; AAD16299 | ||||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB042237 EMBL· GenBank· DDBJ | BAB17272.1 EMBL· GenBank· DDBJ | mRNA | ||
AF099664 EMBL· GenBank· DDBJ | AAD16299.1 EMBL· GenBank· DDBJ | mRNA | ||
AK097835 EMBL· GenBank· DDBJ | BAG53539.1 EMBL· GenBank· DDBJ | mRNA | ||
AC087301 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC002774 EMBL· GenBank· DDBJ | AAH02774.1 EMBL· GenBank· DDBJ | mRNA | ||
BC010451 EMBL· GenBank· DDBJ | AAH10451.1 EMBL· GenBank· DDBJ | mRNA |