Q9Y4F1 · FARP1_HUMAN

  • Protein
    FERM, ARHGEF and pleckstrin domain-containing protein 1
  • Gene
    FARP1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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 annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasmic side of plasma membrane
Cellular Componentcytoskeleton
Cellular Componentcytosol
Cellular Componentdendrite
Cellular Componentdendritic spine
Cellular Componentextrinsic component of postsynaptic membrane
Cellular Componentfilopodium
Cellular Componentglutamatergic synapse
Molecular Functioncytoskeletal protein binding
Molecular Functionguanyl-nucleotide exchange factor activity
Molecular Functionsmall GTPase binding
Biological Processdendrite morphogenesis
Biological Processenzyme-linked receptor protein signaling pathway
Biological Processpositive regulation of skeletal muscle acetylcholine-gated channel clustering
Biological Processpostsynaptic actin cytoskeleton organization
Biological ProcessRac protein signal transduction
Biological Processregulation of presynapse assembly
Biological Processretrograde trans-synaptic signaling by trans-synaptic protein complex
Biological Processsynapse assembly

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    FERM, ARHGEF and pleckstrin domain-containing protein 1
  • Alternative names
    • Chondrocyte-derived ezrin-like protein
    • FERM, RhoGEF and pleckstrin domain-containing protein 1
    • Pleckstrin homology domain-containing family C member 2 (PH domain-containing family C member 2)

Gene names

    • Name
      FARP1
    • Synonyms
      CDEP, PLEKHC2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9Y4F1
  • Secondary accessions
    • Q5JVI9
    • Q6IQ29

Proteomes

Organism-specific databases

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_0483628in dbSNP:rs9300466
Natural variantVAR_035851714in a breast cancer sample; somatic mutation; dbSNP:rs1458028855

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.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00002327531-1045UniProtFERM, ARHGEF and pleckstrin domain-containing protein 1
Modified residue (large scale data)12PRIDEPhosphoserine
Modified residue20UniProtPhosphoserine
Modified residue (large scale data)20PRIDEPhosphoserine
Modified residue23UniProtPhosphoserine
Modified residue (large scale data)23PRIDEPhosphoserine
Modified residue24UniProtPhosphothreonine
Modified residue (large scale data)24PRIDEPhosphothreonine
Modified residue (large scale data)34PRIDEPhosphothreonine
Modified residue340UniProtPhosphoserine
Modified residue (large scale data)340PRIDEPhosphoserine
Modified residue373UniProtPhosphoserine
Modified residue389UniProtPhosphoserine
Modified residue403UniProtPhosphoserine
Modified residue (large scale data)403PRIDEPhosphoserine
Modified residue418UniProtPhosphoserine
Modified residue (large scale data)418PRIDEPhosphoserine
Modified residue (large scale data)424PRIDEPhosphoserine
Modified residue427UniProtPhosphoserine
Modified residue (large scale data)427PRIDEPhosphoserine
Modified residue433UniProtPhosphoserine
Modified residue (large scale data)433PRIDEPhosphoserine
Modified residue (large scale data)503PRIDEPhosphoserine
Modified residue510UniProtPhosphoserine
Modified residue (large scale data)510PRIDEPhosphoserine
Modified residue514UniProtPhosphoserine
Modified residue (large scale data)514PRIDEPhosphoserine
Modified residue (large scale data)525PRIDEPhosphothreonine
Modified residue (large scale data)613PRIDEPhosphoserine
Modified residue833UniProtPhosphoserine
Modified residue (large scale data)833PRIDEPhosphoserine
Modified residue (large scale data)863PRIDEPhosphoserine
Modified residue (large scale data)871PRIDEPhosphoserine
Modified residue872UniProtPhosphoserine
Modified residue (large scale data)872PRIDEPhosphoserine
Modified residue878UniProtPhosphoserine
Modified residue (large scale data)878PRIDEPhosphoserine
Modified residue883UniProtPhosphothreonine
Modified residue (large scale data)883PRIDEPhosphothreonine
Modified residue889UniProtPhosphoserine
Modified residue (large scale data)889PRIDEPhosphoserine
Modified residue (large scale data)894PRIDEPhosphoserine
Modified residue896UniProtPhosphoserine
Modified residue (large scale data)896PRIDEPhosphoserine
Modified residue899UniProtPhosphoserine
Modified residue (large scale data)899PRIDEPhosphoserine
Modified residue (large scale data)1038PRIDEPhosphoserine
Modified residue (large scale data)1042PRIDEPhosphoserine

Keywords

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

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9Y4F1PIH1D1 Q9NWS03EBI-5235630, EBI-357318

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-37Disordered
Compositional bias16-30Polar residues
Domain40-320FERM
Region361-534Disordered
Compositional bias371-401Polar residues
Compositional bias460-515Polar residues
Domain540-730DH
Domain759-856PH 1
Region864-903Disordered
Domain932-1029PH 2

Domain

Intramolecular interaction between the DH domain and the PH domains can stabilize the protein in an autoinhibited conformation.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

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.

  • Length
    1,045
  • Mass (Da)
    118,633
  • Last updated
    1999-11-01 v1
  • Checksum
    0E8B2D61C0F58417
MGEIEQRPTPGSRLGAPENSGISTLERGQKPPPTPSGKLVSIKIQMLDDTQEAFEVPQRAPGKVLLDAVCNHLNLVEGDYFGLEFPDHKKITVWLDLLKPIVKQIRRPKHVVVKFVVKFFPPDHTQLQEELTRYLFALQVKQDLAQGRLTCNDTSAALLISHIVQSEIGDFDEALDREHLAKNKYIPQQDALEDKIVEFHHNHIGQTPAESDFQLLEIARRLEMYGIRLHPAKDREGTKINLAVANTGILVFQGFTKINAFNWAKVRKLSFKRKRFLIKLRPDANSAYQDTLEFLMASRDFCKSFWKICVEHHAFFRLFEEPKPKPKPVLFSRGSSFRFSGRTQKQVLDYVKEGGHKKVQFERKHSKIHSIRSLASQPTELNSEVLEQSQQSTSLTFGEGAESPGGQSCRRGKEPKVSAGEPGSHPSPAPRRSPAGNKQADGAASAPTEEEEEVVKDRTQQSKPQPPQPSTGSLTGSPHLSELSVNSQGGVAPANVTLSPNLSPDTKQASPLISPLLNDQACPRTDDEDEGRRKRFPTDKAYFIAKEVSTTERTYLKDLEVITSWFQSTVSKEDAMPEALKSLIFPNFEPLHKFHTNFLKEIEQRLALWEGRSNAQIRDYQRIGDVMLKNIQGMKHLAAHLWKHSEALEALENGIKSSRRLENFCRDFELQKVCYLPLNTFLLRPLHRLMHYKQVLERLCKHHPPSHADFRDCRAALAEITEMVAQLHGTMIKMENFQKLHELKKDLIGIDNLVVPGREFIRLGSLSKLSGKGLQQRMFFLFNDVLLYTSRGLTASNQFKVHGQLPLYGMTIEESEDEWGVPHCLTLRGQRQSIIVAASSRSEMEKWVEDIQMAIDLAEKSSSPAPEFLASSPPDNKSPDEATAADQESEDDLSASRTSLERQAPHRGNTMVHVCWHRNTSVSMVDFSIAVENQLSGNLLRKFKNSNGWQKLWVVFTNFCLFFYKSHQDNHPLASLPLLGYSLTIPSESENIQKDYVFKLHFKSHVYYFRAESEYTFERWMEVIRSATSSASRPHVLSHKESLVY

Q9Y4F1-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 758-758: R → RPGSFSLMRTPHLGQARRIPCAPERRPLLLVK

Q9Y4F1-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 58-129: QRAPGKVLLDAVCNHLNLVEGDYFGLEFPDHKKITVWLDLLKPIVKQIRRPKHVVVKFVVKFFPPDHTQLQE → MVSSSSFLKATGSSWTGWVLRCSMKPKHHSHLIEKFGEDRILTHLTGSISYTNWAGSRSLAVTVTEELLNLF
    • 130-1045: Missing

Computationally mapped potential isoform sequences

There are 6 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9JME2C9JME2_HUMANFARP11076
A0A1B0GV68A0A1B0GV68_HUMANFARP1801
H0Y783H0Y783_HUMANFARP1215
M0R262M0R262_HUMANFARP1171
M0QXT1M0QXT1_HUMANFARP1248
M0QYB0M0QYB0_HUMANFARP1203

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Compositional bias16-30Polar residues
Alternative sequenceVSP_04098958-129in isoform 3
Alternative sequenceVSP_040990130-1045in isoform 3
Compositional bias371-401Polar residues
Compositional bias460-515Polar residues
Sequence conflict644in Ref. 3; AAH71592
Alternative sequenceVSP_017976758in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp