ETV4
entrez
2118
canonical
uniprot
P43268
canonical
ensembl
ENSG00000175832
resolver
ensp
ENSP00000321835
resolver
ensp
ENSP00000440023
resolver
ensp
ENSP00000443846
resolver
ensp
ENSP00000465718
resolver
ensp
ENSP00000468636
resolver
ensp
ENSP00000527902
resolver
ensp
ENSP00000527903
resolver
ensp
ENSP00000747873
resolver
genesymbol
ETV4
resolver
genesymbol_syn
E1AF
resolver
genesymbol_syn
PEA3
resolver
hgnc
HGNC:3493
resolver
uniprot
A8K314
resolver
uniprot
B7Z5J3
resolver
uniprot
B7Z9J6
resolver
uniprot
Q96AW9
resolver
uniprot_entry
ETV4_HUMAN
resolver
uniprot_sec
A8K314
resolver
uniprot_sec
B7Z5J3
resolver
uniprot_sec
B7Z9J6
resolver
uniprot_sec
Q96AW9
resolver
amino_acid_sequence
MERRMKAGYLDQQVPYTFSSKSPGNGSLREALIGPLGKLMDPGSLPPLDSEDLFQDLSHFQETWLAEAQVPDSDEQFVPDFHSENLAFHSPTTRIKKEPQSPRTDPALSCSRKPPLPYHHGEQCLYSSAYDPPRQIAIKSPAPGALGQSPLQPFPRAEQRNFLRSSGTSQPHPGHGYLGEHSSVFQQPLDICHSFTSQGGGREPLPAPYQHQLSEPCPPYPQQSFKQEYHDPLYEQAGQPAVDQGGVNGHRYPGAGVVIKQEQTDFAYDSDVTGCASMYLHTEGFSGPSPGDGAMGYGYEKPLRPFPDDVCVVPEKFEGDIKQEGVGAFREGPPYQRRGALQLWQFLVALLDDPTNAHFIAWTGRGMEFKLIEPEEVARLWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCEPEALFSLAFPDNQRPALKAEFDRPVSEEDTVPLSHLDESPAYLPELAGPAQPFGPKGGYSY
uniprot
proteins
function
FUNCTION: Transcriptional activator (PubMed:19307308, PubMed:31552090). Regulates the positioning of motor neurons within the lateral medial column of the spinal cord and controls the terminal arborization of specific motor neuron axons within their target muscles (By similarity). Required for the expression of CDH8 and SEMA3E in ETV4-expressing motor neurons and for the exclusion of CDH7 expression from these neurons (By similarity). May play a role in keratinocyte differentiation (PubMed:31552090). {ECO:0000250|UniProtKB:P28322, ECO:0000269|PubMed:19307308, ECO:0000269|PubMed:31552090}.; FUNCTION: (Microbial infection) Binds to the enhancer of the adenovirus E1A gene and acts as a transcriptional activator; the core-binding sequence is 5'-[AC]GGA[AT]GT-3'. {ECO:0000269|PubMed:8441666}.
uniprot
proteins
mass_dalton
53938
uniprot
proteins
mutagenesis
MUTAGEN 96; /note="K->R: Altered sumoylation pattern. Loss of sumoylation, ubiquitination and transcriptional activator function; when associated with R-226 and R-260."; /evidence="ECO:0000269|PubMed:19307308"; MUTAGEN 98; /note="E->A: Loss of polysumoylation and ubiquitination; when associated with A-228; A-262; A-324 and A-443."; /evidence="ECO:0000269|PubMed:19307308"; MUTAGEN 101; /note="S->A: Loss of sumoylation at K-96."; /evidence="ECO:0000269|PubMed:19307308"; MUTAGEN 101; /note="S->E: Normal sumoylation at K-96."; /evidence="ECO:0000269|PubMed:19307308"; MUTAGEN 102; /note="P->A: Loss of sumoylation at K-96."; /evidence="ECO:0000269|PubMed:19307308"; MUTAGEN 226; /note="K->R: Altered sumoylation pattern. Loss of sumoylation, ubiquitination and transcriptional activator function; when associated with R-96 and R-260."; /evidence="ECO:0000269|PubMed:19307308"; MUTAGEN 228; /note="E->A: Loss of polysumoylation and ubiquitination; when associated with A-98; A-262; A-324 and A-443."; /evidence="ECO:0000269|PubMed:19307308"; MUTAGEN 260; /note="K->R: Altered sumoylation pattern. Loss of sumoylation, ubiquitination and transcriptional activator function; when associated with R-96 and R-226."; /evidence="ECO:0000269|PubMed:19307308"; MUTAGEN 262; /note="E->A: Loss of polysumoylation and ubiquitination; when associated with A-98; A-228; A-324 and A-443."; /evidence="ECO:0000269|PubMed:19307308"; MUTAGEN 324; /note="E->A: Loss of polysumoylation and ubiquitination; when associated with A-98; A-228; A-262 and A-443."; /evidence="ECO:0000269|PubMed:19307308"; MUTAGEN 443; /note="E->A: Loss of polysumoylation and ubiquitination; when associated with A-98; A-228; A-262 and A-324."; /evidence="ECO:0000269|PubMed:19307308
uniprot
proteins
post_translational_modification
PTM: Sumoylated; enhanced upon ERK/MAP kinase pathway activation, it positively regulates the transcriptional activator capacity. Sumoylation at Lys-96 probably requires phosphorylation at Ser-101. 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. {ECO:0000269|PubMed:19307308}.
uniprot
proteins
protein_family
ETS family
uniprot
proteins
pubmed
10564827
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19307308
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
31552090
uniprot
proteins
pubmed
7774926
uniprot
proteins
pubmed
8441666
uniprot
proteins
sequence_length
484
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
uniprot
proteins