Q9H3Q1 · BORG4_HUMAN

  • Protein
    Cdc42 effector protein 4
  • Gene
    CDC42EP4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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 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 Componentactin cytoskeleton
Cellular Componentadherens junction
Cellular Componentcytoplasm
Cellular Componentcytoskeleton
Cellular Componentcytosol
Cellular Componentendomembrane system
Cellular Componentmicrotubule cytoskeleton
Cellular Componentphagocytic vesicle
Cellular Componentplasma membrane
Molecular FunctionRNA binding
Molecular Functionsmall GTPase binding
Biological Processcellular response to type II interferon
Biological Processpositive regulation of actin filament polymerization
Biological Processpositive regulation of pseudopodium assembly
Biological Processregulation of cell shape
Biological ProcessRho protein signal transduction

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cdc42 effector protein 4
  • Alternative names
    • Binder of Rho GTPases 4

Gene names

    • Name
      CDC42EP4
    • Synonyms
      BORG4, CEP4

Organism names

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

Accessions

  • Primary accession
    Q9H3Q1
  • Secondary accessions
    • B3KUS7
    • O95828
    • Q96FT3

Proteomes

Organism-specific databases

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.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

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

TypeIDPosition(s)SourceDescription
ChainPRO_00002126551-356UniProtCdc42 effector protein 4
Modified residue5UniProtN6-methyllysine
Modified residue (large scale data)10PRIDEPhosphoserine
Modified residue (large scale data)11PRIDEPhosphoserine
Modified residue18UniProtPhosphoserine
Modified residue (large scale data)18PRIDEPhosphoserine
Modified residue (large scale data)23PRIDEPhosphothreonine
Modified residue (large scale data)51PRIDEPhosphoserine
Modified residue64UniProtPhosphoserine
Modified residue (large scale data)64PRIDEPhosphoserine
Modified residue (large scale data)72PRIDEPhosphoserine
Modified residue105UniProtPhosphoserine
Modified residue (large scale data)105PRIDEPhosphoserine
Modified residue109UniProtPhosphoserine
Modified residue (large scale data)109PRIDEPhosphoserine
Modified residue118UniProtPhosphoserine
Modified residue (large scale data)118PRIDEPhosphoserine
Modified residue138UniProtPhosphoserine
Modified residue (large scale data)138PRIDEPhosphoserine
Modified residue140UniProtPhosphoserine
Modified residue (large scale data)140PRIDEPhosphoserine
Modified residue (large scale data)141PRIDEPhosphoserine
Modified residue142UniProtPhosphoserine
Modified residue (large scale data)142PRIDEPhosphoserine
Modified residue174UniProtPhosphoserine
Modified residue (large scale data)174PRIDEPhosphoserine
Modified residue (large scale data)239PRIDEPhosphotyrosine
Modified residue292UniProtPhosphoserine
Modified residue (large scale data)292PRIDEPhosphoserine
Modified residue295UniProtPhosphoserine
Modified residue (large scale data)295PRIDEPhosphoserine
Modified residue (large scale data)309PRIDEPhosphoserine
Modified residue (large scale data)322PRIDEPhosphoserine
Modified residue (large scale data)344PRIDEPhosphoserine

Keywords

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

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9H3Q1FAM9B Q8IZU05EBI-744665, EBI-10175124
BINARY Q9H3Q1HTT P428583EBI-744665, EBI-466029

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain27-41CRIB
Region51-102Disordered
Compositional bias65-79Polar residues
Region122-182Disordered
Compositional bias148-162Basic and acidic residues
Region257-356Disordered
Compositional bias296-318Polar residues
Compositional bias323-344Basic and acidic residues

Sequence similarities

Belongs to the BORG/CEP family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

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.

  • Length
    356
  • Mass (Da)
    37,980
  • Last updated
    2001-03-01 v1
  • Checksum
    2CF677C60C6EF1B5
MPILKQLVSSSVHSKRRSRADLTAEMISAPLGDFRHTMHVGRAGDAFGDTSFLNSKAGEPDGESLDEQPSSSSSKRSLLSRKFRGSKRSQSVTRGEREQRDMLGSLRDSALFVKNAMSLPQLNEKEAAEKGTSKLPKSLSSSPVKKANDGEGGDEEAGTEEAVPRRNGAAGPHSPDPLLDEQAFGDLTDLPVVPKATYGLKHAESIMSFHIDLGPSMLGDVLSIMDKEEWDPEEGEGGYHGDEGAAGTITQAPPYAVAAPPLARQEGKAGPDLPSLPSHALEDEGWAAAAPSPGSARSMGSHTTRDSSSLSSCTSGILEERSPAFRGPDRARAAVSRQPDKEFSFMDEEEEDEIRV

Q9H3Q1-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
J3KRZ9J3KRZ9_HUMANCDC42EP4127
J3QQS6J3QQS6_HUMANCDC42EP473
J3QR93J3QR93_HUMANCDC42EP479

Features

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

TypeIDPosition(s)Description
Sequence conflict2in Ref. 5; AAH10451
Sequence conflict33in Ref. 2; AAD16299
Alternative sequenceVSP_05554457-126in isoform 2
Compositional bias65-79Polar residues
Compositional bias148-162Basic and acidic residues
Sequence conflict288in Ref. 2; AAD16299
Sequence conflict296in Ref. 2; AAD16299
Compositional bias296-318Polar residues
Compositional bias323-344Basic and acidic residues
Sequence conflict339in Ref. 2; AAD16299
Sequence conflict355in Ref. 2; AAD16299

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

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