P50548 · ERF_HUMAN

  • Protein
    ETS domain-containing transcription factor ERF
  • Gene
    ERF
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Potent transcriptional repressor that binds to the H1 element of the Ets2 promoter. May regulate other genes involved in cellular proliferation. Required for extraembryonic ectoderm differentiation, ectoplacental cone cavity closure, and chorioallantoic attachment (By similarity).
May be important for regulating trophoblast stem cell differentiation (By similarity).

Features

Showing features for dna binding.

154850100150200250300350400450500
TypeIDPosition(s)Description
DNA binding27-107ETS

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 Componentchromatin
Cellular Componentcytosol
Cellular Componentnucleoplasm
Cellular Componentnucleus
Molecular FunctionDNA-binding transcription factor activity, RNA polymerase II-specific
Molecular FunctionDNA-binding transcription repressor activity, RNA polymerase II-specific
Molecular Functionsequence-specific DNA binding
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processregulation of transcription by RNA polymerase II

Keywords

Enzyme and pathway databases

Community curation (1)

The subsequence SEGESEEVEVTDISDEDEEDGEVFKTPRAPPAPPKPEPGEAPGASQCMPLKLRFKRRWSEDCRLEGGGGPAGGFEDEGED shows transcriptional repressor activity in a high-throughput recruitment assay.

Names & Taxonomy

Protein names

  • Recommended name
    ETS domain-containing transcription factor ERF
  • Alternative names
    • Ets2 repressor factor
    • PE-2

Gene names

    • Name
      ERF
Community curation (2)

Organism names

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

Accessions

  • Primary accession
    P50548
  • Secondary accessions
    • B2RAP1
    • B7Z4R0
    • Q59G38
    • Q9UPI7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Involvement in disease

Craniosynostosis 4 (CRS4)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A primary abnormality of skull growth involving premature fusion of one or more cranial sutures. The growth velocity of the skull often cannot match that of the developing brain resulting in an abnormal head shape and, in some cases, increased intracranial pressure, which must be treated promptly to avoid permanent neurodevelopmental disability.
  • See also
    MIM:600775
Natural variants in CRS4
Variant IDPosition(s)ChangeDescription
VAR_07009865R>Qin CRS4; dbSNP:rs587777009
VAR_07009986R>Cin CRS4; dbSNP:rs587777008

Chitayat syndrome (CHYTS)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    An autosomal dominant syndrome characterized by hyperphalangism, partial syndactyly, bilateral accessory phalanx resulting in shortened index fingers, hallux valgus, brachydactyly, facial anomalies, diffuse bronchomalacia, and respiratory distress at birth and in infancy.
  • See also
    MIM:617180
Natural variants in CHYTS
Variant IDPosition(s)ChangeDescription
VAR_07804389Y>Cin CHYTS; dbSNP:rs886041001

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variantVAR_07009865in CRS4; dbSNP:rs587777009
Natural variantVAR_07009986in CRS4; dbSNP:rs587777008
Natural variantVAR_07804389in CHYTS; dbSNP:rs886041001
Natural variantVAR_048947205in dbSNP:rs1053655
Mutagenesis526Loss of a phosphorylation site.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 643 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

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

TypeIDPosition(s)SourceDescription
ChainPRO_00002041011-548UniProtETS domain-containing transcription factor ERF
Modified residue3UniProtPhosphothreonine
Modified residue (large scale data)3PRIDEPhosphothreonine
Modified residue7UniProtPhosphothreonine
Modified residue (large scale data)7PRIDEPhosphothreonine
Modified residue20UniProtPhosphoserine
Modified residue (large scale data)20PRIDEPhosphoserine
Modified residue (large scale data)21PRIDEPhosphoserine
Modified residue24UniProtPhosphoserine
Modified residue (large scale data)24PRIDEPhosphoserine
Modified residue (large scale data)131PRIDEPhosphoserine
Modified residue (large scale data)148PRIDEPhosphothreonine
Modified residue (large scale data)154PRIDEPhosphoserine
Modified residue (large scale data)156PRIDEPhosphothreonine
Modified residue (large scale data)161PRIDEPhosphoserine
Modified residue185UniProtPhosphoserine
Modified residue (large scale data)185PRIDEPhosphoserine
Modified residue (large scale data)187PRIDEPhosphoserine
Modified residue190UniProtPhosphoserine
Modified residue (large scale data)190PRIDEPhosphoserine
Modified residue (large scale data)193PRIDEPhosphothreonine
Modified residue327UniProtPhosphoserine
Modified residue (large scale data)327PRIDEPhosphoserine
Modified residue (large scale data)357PRIDEPhosphothreonine
Modified residue (large scale data)362PRIDEPhosphoserine
Modified residue431UniProtPhosphoserine
Modified residue435UniProtPhosphoserine
Modified residue441UniProtPhosphothreonine
Modified residue444UniProtPhosphoserine
Modified residue (large scale data)444PRIDEPhosphoserine
Cross-link465UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link481UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link512UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue526UniProtPhosphothreonine; by MAPK1
Modified residue (large scale data)526PRIDEPhosphothreonine
Modified residue531UniProtPhosphoserine
Modified residue (large scale data)531PRIDEPhosphoserine
Modified residue532UniProtPhosphoserine
Modified residue (large scale data)532PRIDEPhosphoserine
Modified residue (large scale data)542PRIDEPhosphoserine
Modified residue548UniProtPhosphoserine
Modified residue (large scale data)548PRIDEPhosphoserine

Post-translational modification

Phosphorylated by multiple kinases including MAPK1/ERK2 at THR-526. Phosphorylation regulates the activity of ERF.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Highest levels in testis, ovary, pancreas, and heart.

Gene expression databases

Organism-specific databases

Interaction

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region130-169Disordered
Compositional bias143-169Polar residues
Region184-225Disordered
Region280-304Disordered
Compositional bias342-359Pro residues
Region342-478Disordered
Compositional bias360-377Polar residues
Compositional bias434-450Acidic residues
Region492-548Disordered

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.

P50548-1

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
    548
  • Mass (Da)
    58,703
  • Last updated
    2004-07-19 v2
  • Checksum
    01242339B8D328ED
MKTPADTGFAFPDWAYKPESSPGSRQIQLWHFILELLRKEEYQGVIAWQGDYGEFVIKDPDEVARLWGVRKCKPQMNYDKLSRALRYYYNKRILHKTKGKRFTYKFNFNKLVLVNYPFIDVGLAGGAVPQSAPPVPSGGSHFRFPPSTPSEVLSPTEDPRSPPACSSSSSSLFSAVVARRLGRGSVSDCSDGTSELEEPLGEDPRARPPGPPDLGAFRGPPLARLPHDPGVFRVYPRPRGGPEPLSPFPVSPLAGPGSLLPPQLSPALPMTPTHLAYTPSPTLSPMYPSGGGGPSGSGGGSHFSFSPEDMKRYLQAHTQSVYNYHLSPRAFLHYPGLVVPQPQRPDKCPLPPMAPETPPVPSSASSSSSSSSSPFKFKLQPPPLGRRQRAAGEKAVAGADKSGGSAGGLAEGAGALAPPPPPPQIKVEPISEGESEEVEVTDISDEDEEDGEVFKTPRAPPAPPKPEPGEAPGASQCMPLKLRFKRRWSEDCRLEGGGGPAGGFEDEGEDKKVRGEGPGEAGGPLTPRRVSSDLQHATAQLSLEHRDS

P50548-2

  • 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
A0AAQ5BII5A0AAQ5BII5_HUMANERF191
M0QXN0M0QXN0_HUMANERF98
M0QX79M0QX79_HUMANERF61

Sequence caution

The sequence BAD92508.1 differs from that shown. Reason: Miscellaneous discrepancy The sequence differs from that shown because it seems to be derived from a pre-mRNA.

Features

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

TypeIDPosition(s)Description
Alternative sequenceVSP_0554871-75in isoform 2
Compositional bias143-169Polar residues
Compositional bias342-359Pro residues
Compositional bias360-377Polar residues
Sequence conflict381in Ref. 1; AAA86686
Sequence conflict398in Ref. 1; AAA86686
Compositional bias434-450Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U15655
EMBL· GenBank· DDBJ
AAA86686.1
EMBL· GenBank· DDBJ
mRNA
AK297666
EMBL· GenBank· DDBJ
BAH12646.1
EMBL· GenBank· DDBJ
mRNA
AK314278
EMBL· GenBank· DDBJ
BAG36938.1
EMBL· GenBank· DDBJ
mRNA
AB209271
EMBL· GenBank· DDBJ
BAD92508.1
EMBL· GenBank· DDBJ
Transcribed RNA Sequence problems.
AC006486
EMBL· GenBank· DDBJ
AAD11987.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471126
EMBL· GenBank· DDBJ
EAW57116.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471126
EMBL· GenBank· DDBJ
EAW57118.1
EMBL· GenBank· DDBJ
Genomic DNA
BC022231
EMBL· GenBank· DDBJ
AAH22231.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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