Snai1
entrez
20613
canonical
uniprot
Q02085
canonical
ensembl
ENSMUSG00000042821
resolver
ensp
ENSMUSP00000050581
resolver
enst
ENSMUST00000052631
resolver
genesymbol
Snai1
resolver
genesymbol_syn
Sna
resolver
uniprot
Q4FK48
resolver
uniprot_entry
Q4FK48_MOUSE
resolver
uniprot_entry
SNAI1_MOUSE
resolver
amino_acid_sequence
MPRSFLVRKPSDPRRKPNYSELQDACVEFTFQQPYDQAHLLAAIPPPEVLNPAASLPTLIWDSLLVPQVRPVAWATLPLRESPKAVELTSLSDEDSGKSSQPPSPPSPAPSSFSSTSASSLEAEAFIAFPGLGQLPKQLARLSVAKDPQSRKIFNCKYCNKEYLSLGALKMHIRSHTLPCVCTTCGKAFSRPWLLQGHVRTHTGEKPFSCSHCNRAFADRSNLRAHLQTHSDVKRYQCQACARTFSRMSLLHKHQESGCSGGPR
uniprot
proteins
function
FUNCTION: Involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration. Binds to 3 E-boxes of the E-cadherin gene promoter and to the promoters of CLDN7 and KRT8 and, in association with histone demethylase KDM1A which it recruits to the promoters, causes a decrease in dimethylated H3K4 levels and represses transcription. Involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration. Binds to 3 E-boxes of the E-cadherin/CDH1 gene promoter and to the promoters of CLDN7 and KRT8 and, in association with histone demethylase KDM1A which it recruits to the promoters, causes a decrease in dimethylated H3K4 levels and represses transcription. The N-terminal SNAG domain competes with histone H3 for the same binding site on the histone demethylase complex formed by KDM1A and RCOR1, and thereby inhibits demethylation of histone H3 at 'Lys-4' (in vitro) (By similarity). During EMT, involved with LOXL2 in negatively regulating pericentromeric heterochromatin transcription (PubMed:24239292). SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits (PubMed:24239292). Associates with EGR1 and SP1 to mediate 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced up-regulation of CDKN2B, possibly by binding to the CDKN2B promoter region 5'-TCACA-3'. In addition, may also activate the CDKN2B promoter by itself. {ECO:0000250|UniProtKB:O95863, ECO:0000269|PubMed:10655586, ECO:0000269|PubMed:11689706, ECO:0000269|PubMed:24239292}.
uniprot
proteins
mass_dalton
29190
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by GSK3B. Once phosphorylated, it becomes a target for ubiquitination by BTRC, the ECS(SPSB3) or the SCF(FBXO11) complexes. Phosphorylation by CSNK1E, probably at Ser-104, provides the priming site for the subsequent phosphorylation by GSK3B, probably at Ser-100 and Ser-96. Phosphorylation by PAK1 may modulate its transcriptional activity by promoting increased accumulation in the nucleus. Phosphorylation at Ser-11 and Ser-104 positively regulates its function in induction of EMT and/or cell survival, respectively. Phosphorylation by LATS2, upon mitotic stress, oncogenic stress or Hippo pathway activation, occurs in the nucleus and promotes nuclear retention and stabilization of total cellular protein level. {ECO:0000250|UniProtKB:O95863}.; PTM: Ubiquitinated on Lys-98, Lys-137 and Lys-146 by FBXL14 and BTRC leading to degradation. BTRC-triggered ubiquitination requires previous GSK3B-mediated SNAI1 phosphorylation. Ubiquitinated by the SCF(FBXO11) complex; ubiquitination requires previous GSK3B-mediated SNAI1 phosphorylation. Ubiquitinated by the ECS(SPSB3) complex; ubiquitination requires previous GSK3B-mediated SNAI1 phosphorylation. Ubiquitination induced upon interaction with NOTCH1 or p53 is mediated by MDM2. Ubiquitinated in a FBXL5-dependent manner; preventing interaction with DNA and promoting its degradation. Deubiquitinated by USP37; leading to stabilization. {ECO:0000250|UniProtKB:O95863}.; PTM: O-GlcNAcylation at Ser-112 is enhanced in hyperglycaemic conditions, it opposes phosphorylation by GSK3B, and stabilizes the protein. {ECO:0000250}.; PTM: ADP-ribosylation by PARP1 increases protein half-life and may be involved in TGFB-induced SNAI1 up-regulation. {ECO:0000250}.
uniprot
proteins
protein_family
Snail C2H2-type zinc-finger protein family
uniprot
proteins
pubmed
10655586
uniprot
proteins
pubmed
11689706
uniprot
proteins
pubmed
12832491
uniprot
proteins
pubmed
1295727
uniprot
proteins
pubmed
1483390
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18331720
uniprot
proteins
pubmed
19386897
uniprot
proteins
pubmed
19923321
uniprot
proteins
pubmed
19955572
uniprot
proteins
pubmed
21577210
uniprot
proteins
pubmed
24239292
uniprot
proteins
pubmed
9271672
uniprot
proteins
sequence_length
264
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12832491}. Cytoplasm {ECO:0000269|PubMed:12832491}. Note=Once phosphorylated (probably on Ser-107, Ser-111, Ser-115 and Ser-119) it is exported from the nucleus to the cytoplasm where subsequent phosphorylation of the destruction motif and ubiquitination involving BTRC occurs. {ECO:0000250|UniProtKB:O95863}.
uniprot
proteins