P28322 · ETV4_MOUSE

  • Protein
    ETS translocation variant 4
  • Gene
    Etv4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Transcriptional activator (PubMed:1547944).
May play a role in keratinocyte differentiation (By similarity).

Features

Showing features for dna binding.

148550100150200250300350400450
TypeIDPosition(s)Description
DNA binding342-422ETS

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 Componentnucleus
Molecular FunctionDNA binding
Molecular FunctionDNA-binding transcription factor activity, RNA polymerase II-specific
Molecular Functionsequence-specific DNA binding
Biological Processbranching involved in mammary gland duct morphogenesis
Biological Processmotor neuron axon guidance
Biological Processnegative regulation of mammary gland epithelial cell proliferation
Biological Processpositive regulation of DNA-templated transcription
Biological Processpositive regulation of gene expression
Biological Processpositive regulation of keratinocyte differentiation
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processregulation of transcription by RNA polymerase II
Biological Processstem cell differentiation
Biological Processtranscription by RNA polymerase II

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ETS translocation variant 4
  • Alternative names
    • Polyomavirus enhancer activator 3 (Protein PEA3)

Gene names

    • Name
      Etv4
    • Synonyms
      Pea-3, Pea3

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P28322
  • Secondary accessions
    • Q3UMZ6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, cross-link, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002041171-485ETS translocation variant 4
Cross-link6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link95Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residue100Phosphoserine
Cross-link138Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue139Phosphoserine
Modified residue148Phosphoserine
Modified residue215Phosphoserine
Cross-link227Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-link261Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-link323Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)

Post-translational modification

Sumoylated; enhanced upon ERK/MAP kinase pathway activation it positively regulates the transcriptional activator capacity. Sumoylation at Lys-95 probably requires phosphorylation at Ser-100. Transiently polysumoylated and desumoylated by SENP1. Sumoylation is a prerequisite to polyubiquitination which in turn increases proteasomal-mediated degradation. Probably polyubiquitinated by RNF4 and deubiquitinated by USP2.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Epididymis and brain.

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region79-114Disordered
Region135-214Disordered
Compositional bias151-176Polar residues

Sequence similarities

Belongs to the ETS family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

P28322-1

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
    485
  • Mass (Da)
    54,008
  • Last updated
    2013-09-18 v2
  • Checksum
    3A5FF4EFD7E828EF
MERRMKGGYLDQRVPYTFCSKSPGNGSLGEALMVPQGKLMDPGSLPPSDSEDLFQDLSHFQETWLAEAQVPDSDEQFVPDFHSENSFHSPTTRIKKEPQSPRTDPALSCSRKPPLPYHHGEQCLYSSAYDSPRQIAIKSPAPGAPGQSPLQPFSRAEQQQSLLRASSSSQSHPGHGYLGEHSSVFQQPVDMCHSFTSPQGGGREPLPAPYQHQLSEPCPPYPQQNFKQEYHDPLYEQAGQPASSQGGVSGHRYPGAGVVIKQERTDFAYDSDVPGCASMYLHPEGFSGPSPGDGVMGYGYEKSLRPFPDDVCIVPEKFEGDIKQEGIGAFREGPPYQRRGALQLWQFLVALLDDPTNAHFIAWTGRGMEFKLIEPEEVARLWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCEPEALFSLAFPDNQRPALKAEFDRPVSEEDTVPLSHLDESPAYLPELTGPAPPFGHRGGYSY

P28322-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-1: M → MTKSSNHNCLLRPENKPGLWGPGAQAASLRPSPATLVVSSPGHAEHPPAAPAQTPGPQVSASARGPGPVAGGSGRM
    • 86-86: S → LA
    • 127-132: Missing

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A2A5C2A2A5C2_MOUSEEtv4480
A2A5C3A2A5C3_MOUSEEtv4486

Features

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

TypeIDPosition(s)Description
Alternative sequenceVSP_0479431in isoform 2
Alternative sequenceVSP_04794486in isoform 2
Alternative sequenceVSP_047945127-132in isoform 2
Compositional bias151-176Polar residues
Sequence conflict316in Ref. 1; CAA44872

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X63190
EMBL· GenBank· DDBJ
CAA44872.1
EMBL· GenBank· DDBJ
mRNA
AK144590
EMBL· GenBank· DDBJ
BAE25952.1
EMBL· GenBank· DDBJ
mRNA
AL591436
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

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.
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