Q9Y4F1 · FARP1_HUMAN
- ProteinFERM, ARHGEF and pleckstrin domain-containing protein 1
- GeneFARP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1045 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as a guanine nucleotide exchange factor for RAC1. May play a role in semaphorin signaling. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses (By similarity).
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 | cytoplasmic side of plasma membrane | |
Cellular Component | cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | dendrite | |
Cellular Component | dendritic spine | |
Cellular Component | extrinsic component of postsynaptic membrane | |
Cellular Component | filopodium | |
Cellular Component | glutamatergic synapse | |
Molecular Function | cytoskeletal protein binding | |
Molecular Function | guanyl-nucleotide exchange factor activity | |
Molecular Function | small GTPase binding | |
Biological Process | dendrite morphogenesis | |
Biological Process | enzyme-linked receptor protein signaling pathway | |
Biological Process | positive regulation of skeletal muscle acetylcholine-gated channel clustering | |
Biological Process | postsynaptic actin cytoskeleton organization | |
Biological Process | Rac protein signal transduction | |
Biological Process | regulation of presynapse assembly | |
Biological Process | retrograde trans-synaptic signaling by trans-synaptic protein complex | |
Biological Process | synapse assembly |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFERM, ARHGEF and pleckstrin domain-containing protein 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 accessionQ9Y4F1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Recruited to the cell membrane via interaction with CADM1.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_048362 | 8 | in dbSNP:rs9300466 | |||
Sequence: P → L | ||||||
Natural variant | VAR_035851 | 714 | in a breast cancer sample; somatic mutation; dbSNP:rs1458028855 | |||
Sequence: R → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,322 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_0000232753 | 1-1045 | UniProt | FERM, ARHGEF and pleckstrin domain-containing protein 1 | |||
Sequence: MGEIEQRPTPGSRLGAPENSGISTLERGQKPPPTPSGKLVSIKIQMLDDTQEAFEVPQRAPGKVLLDAVCNHLNLVEGDYFGLEFPDHKKITVWLDLLKPIVKQIRRPKHVVVKFVVKFFPPDHTQLQEELTRYLFALQVKQDLAQGRLTCNDTSAALLISHIVQSEIGDFDEALDREHLAKNKYIPQQDALEDKIVEFHHNHIGQTPAESDFQLLEIARRLEMYGIRLHPAKDREGTKINLAVANTGILVFQGFTKINAFNWAKVRKLSFKRKRFLIKLRPDANSAYQDTLEFLMASRDFCKSFWKICVEHHAFFRLFEEPKPKPKPVLFSRGSSFRFSGRTQKQVLDYVKEGGHKKVQFERKHSKIHSIRSLASQPTELNSEVLEQSQQSTSLTFGEGAESPGGQSCRRGKEPKVSAGEPGSHPSPAPRRSPAGNKQADGAASAPTEEEEEVVKDRTQQSKPQPPQPSTGSLTGSPHLSELSVNSQGGVAPANVTLSPNLSPDTKQASPLISPLLNDQACPRTDDEDEGRRKRFPTDKAYFIAKEVSTTERTYLKDLEVITSWFQSTVSKEDAMPEALKSLIFPNFEPLHKFHTNFLKEIEQRLALWEGRSNAQIRDYQRIGDVMLKNIQGMKHLAAHLWKHSEALEALENGIKSSRRLENFCRDFELQKVCYLPLNTFLLRPLHRLMHYKQVLERLCKHHPPSHADFRDCRAALAEITEMVAQLHGTMIKMENFQKLHELKKDLIGIDNLVVPGREFIRLGSLSKLSGKGLQQRMFFLFNDVLLYTSRGLTASNQFKVHGQLPLYGMTIEESEDEWGVPHCLTLRGQRQSIIVAASSRSEMEKWVEDIQMAIDLAEKSSSPAPEFLASSPPDNKSPDEATAADQESEDDLSASRTSLERQAPHRGNTMVHVCWHRNTSVSMVDFSIAVENQLSGNLLRKFKNSNGWQKLWVVFTNFCLFFYKSHQDNHPLASLPLLGYSLTIPSESENIQKDYVFKLHFKSHVYYFRAESEYTFERWMEVIRSATSSASRPHVLSHKESLVY | |||||||
Modified residue (large scale data) | 12 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 20 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 20 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 23 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 24 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 24 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 34 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 340 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 340 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 373 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 389 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 403 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 403 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 418 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 418 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 424 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 427 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 427 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 433 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 433 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 503 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 510 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 510 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 514 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 514 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 525 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 613 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 833 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 833 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 863 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 871 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 872 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 872 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 878 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 878 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 883 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 883 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 889 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 889 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 894 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 896 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 896 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 899 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 899 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1038 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1042 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in cAMP-treated chondrocytes, but not in untreated chondrocytes. Detected in fetal brain, heart and spleen, and in adult testis, kidney and lung.
Induction
Up-regulated in response to cAMP in cultured embryonic chondrocytes.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with CADM1. Interacts with RAC1 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y4F1 | PIH1D1 Q9NWS0 | 3 | EBI-5235630, EBI-357318 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-37 | Disordered | ||||
Sequence: MGEIEQRPTPGSRLGAPENSGISTLERGQKPPPTPSG | ||||||
Compositional bias | 16-30 | Polar residues | ||||
Sequence: APENSGISTLERGQK | ||||||
Domain | 40-320 | FERM | ||||
Sequence: VSIKIQMLDDTQEAFEVPQRAPGKVLLDAVCNHLNLVEGDYFGLEFPDHKKITVWLDLLKPIVKQIRRPKHVVVKFVVKFFPPDHTQLQEELTRYLFALQVKQDLAQGRLTCNDTSAALLISHIVQSEIGDFDEALDREHLAKNKYIPQQDALEDKIVEFHHNHIGQTPAESDFQLLEIARRLEMYGIRLHPAKDREGTKINLAVANTGILVFQGFTKINAFNWAKVRKLSFKRKRFLIKLRPDANSAYQDTLEFLMASRDFCKSFWKICVEHHAFFRLFE | ||||||
Region | 361-534 | Disordered | ||||
Sequence: FERKHSKIHSIRSLASQPTELNSEVLEQSQQSTSLTFGEGAESPGGQSCRRGKEPKVSAGEPGSHPSPAPRRSPAGNKQADGAASAPTEEEEEVVKDRTQQSKPQPPQPSTGSLTGSPHLSELSVNSQGGVAPANVTLSPNLSPDTKQASPLISPLLNDQACPRTDDEDEGRRK | ||||||
Compositional bias | 371-401 | Polar residues | ||||
Sequence: IRSLASQPTELNSEVLEQSQQSTSLTFGEGA | ||||||
Compositional bias | 460-515 | Polar residues | ||||
Sequence: QQSKPQPPQPSTGSLTGSPHLSELSVNSQGGVAPANVTLSPNLSPDTKQASPLISP | ||||||
Domain | 540-730 | DH | ||||
Sequence: KAYFIAKEVSTTERTYLKDLEVITSWFQSTVSKEDAMPEALKSLIFPNFEPLHKFHTNFLKEIEQRLALWEGRSNAQIRDYQRIGDVMLKNIQGMKHLAAHLWKHSEALEALENGIKSSRRLENFCRDFELQKVCYLPLNTFLLRPLHRLMHYKQVLERLCKHHPPSHADFRDCRAALAEITEMVAQLHGT | ||||||
Domain | 759-856 | PH 1 | ||||
Sequence: EFIRLGSLSKLSGKGLQQRMFFLFNDVLLYTSRGLTASNQFKVHGQLPLYGMTIEESEDEWGVPHCLTLRGQRQSIIVAASSRSEMEKWVEDIQMAID | ||||||
Region | 864-903 | Disordered | ||||
Sequence: PAPEFLASSPPDNKSPDEATAADQESEDDLSASRTSLERQ | ||||||
Domain | 932-1029 | PH 2 | ||||
Sequence: ENQLSGNLLRKFKNSNGWQKLWVVFTNFCLFFYKSHQDNHPLASLPLLGYSLTIPSESENIQKDYVFKLHFKSHVYYFRAESEYTFERWMEVIRSATS |
Domain
Intramolecular interaction between the DH domain and the PH domains can stabilize the protein in an autoinhibited conformation.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9Y4F1-1
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
- Length1,045
- Mass (Da)118,633
- Last updated1999-11-01 v1
- Checksum0E8B2D61C0F58417
Q9Y4F1-2
- Name2
- Differences from canonical
- 758-758: R → RPGSFSLMRTPHLGQARRIPCAPERRPLLLVK
Q9Y4F1-3
- Name3
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 16-30 | Polar residues | ||||
Sequence: APENSGISTLERGQK | ||||||
Alternative sequence | VSP_040989 | 58-129 | in isoform 3 | |||
Sequence: QRAPGKVLLDAVCNHLNLVEGDYFGLEFPDHKKITVWLDLLKPIVKQIRRPKHVVVKFVVKFFPPDHTQLQE → MVSSSSFLKATGSSWTGWVLRCSMKPKHHSHLIEKFGEDRILTHLTGSISYTNWAGSRSLAVTVTEELLNLF | ||||||
Alternative sequence | VSP_040990 | 130-1045 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 371-401 | Polar residues | ||||
Sequence: IRSLASQPTELNSEVLEQSQQSTSLTFGEGA | ||||||
Compositional bias | 460-515 | Polar residues | ||||
Sequence: QQSKPQPPQPSTGSLTGSPHLSELSVNSQGGVAPANVTLSPNLSPDTKQASPLISP | ||||||
Sequence conflict | 644 | in Ref. 3; AAH71592 | ||||
Sequence: H → Y | ||||||
Alternative sequence | VSP_017976 | 758 | in isoform 2 | |||
Sequence: R → RPGSFSLMRTPHLGQARRIPCAPERRPLLLVK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB008430 EMBL· GenBank· DDBJ | BAA24267.1 EMBL· GenBank· DDBJ | mRNA | ||
AL136300 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL137249 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL161896 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL445223 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC041595 EMBL· GenBank· DDBJ | AAH41595.1 EMBL· GenBank· DDBJ | mRNA | ||
BC065020 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BC071592 EMBL· GenBank· DDBJ | AAH71592.1 EMBL· GenBank· DDBJ | mRNA |