Set
entrez
56086
canonical
uniprot
Q9EQU5
canonical
ensembl
ENSMUSG00000054766
resolver
ensp
ENSMUSP00000070002
resolver
ensp
ENSMUSP00000099930
resolver
genesymbol
Set
resolver
uniprot
A2BE95
resolver
uniprot
Q3T9S3
resolver
uniprot
Q9CY82
resolver
uniprot
Q9D0A9
resolver
uniprot
Q9Z181
resolver
uniprot_entry
Q3T9S3_MOUSE
resolver
uniprot_entry
SET_MOUSE
resolver
uniprot_sec
A2BE95
resolver
uniprot_sec
Q9CY82
resolver
uniprot_sec
Q9D0A9
resolver
uniprot_sec
Q9Z181
resolver
amino_acid_sequence
MAPKRQSAILPQPKKPRPAAAPKLEDKSASPGLPKGEKEQQEAIEHIDEVQNEIDRLNEQASEEILKVEQKYNKLRQPFFQKRSELIAKIPNFWVTTFVNHPQVSALLGEEDEEALHYLTRVEVTEFEDIKSGYRIDFYFDENPYFENKVLSKEFHLNESGDPSSKSTEIKWKSGKDLTKRSSQTQNKASRKRQHEEPESFFTWFTDHSDAGADELGEVIKDDIWPNPLQYYLVPDMDDEEGEAEDDDDDDEEEEGLEDIDEEGDEDEGEEDDDEDEGEEGEEDEGEDD
uniprot
proteins
function
FUNCTION: Multitasking protein, involved in apoptosis, transcription, nucleosome assembly and histone chaperoning. Isoform 2 anti-apoptotic activity is mediated by inhibition of the GZMA-activated DNase, NME1. In the course of cytotoxic T-lymphocyte (CTL)-induced apoptosis, GZMA cleaves SET, disrupting its binding to NME1 and releasing NME1 inhibition. Isoform 1 and isoform 2 are potent inhibitors of protein phosphatase 2A. Isoform 1 and isoform 2 inhibit EP300/CREBBP and PCAF-mediated acetylation of histones (HAT) and nucleosomes, most probably by masking the accessibility of lysines of histones to the acetylases. The predominant target for inhibition is histone H4. HAT inhibition leads to silencing of HAT-dependent transcription and prevents active demethylation of DNA. Both isoforms stimulate DNA replication of the adenovirus genome complexed with viral core proteins; however, isoform 2 specific activity is higher (By similarity). {ECO:0000250}.
uniprot
proteins
mass_dalton
33378
uniprot
proteins
mutagenesis
MUTAGEN 4; /note="K->Q: Almost abolishes N-terminal methylation at A-2."; /evidence="ECO:0000269|PubMed:20668449
uniprot
proteins
post_translational_modification
PTM: Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group.; PTM: N-terminus of isoform 1 is methylated by METTL11A/NTM1. Mainly trimethylated. {ECO:0000269|PubMed:20668449}.; PTM: [Isoform 2]: Cleaved after Lys-176 by GZMA. The cleavage inhibits its nucleosome assembly activity and disrupts the inhibition on NME1 (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
Nucleosome assembly protein (NAP) family
uniprot
proteins
pubmed
11078917
uniprot
proteins
pubmed
11231286
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17947660
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19524510
uniprot
proteins
pubmed
20668449
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22872859
uniprot
proteins
pubmed
23806337
uniprot
proteins
sequence_length
289
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=In the cytoplasm, found both in the cytosol and associated with the endoplasmic reticulum. The SET complex is associated with the endoplasmic reticulum. Following CTL attack and cleavage by GZMA, moves rapidly to the nucleus, where it is found in the nucleoplasm, avoiding the nucleolus. Similar translocation to the nucleus is also observed for lymphocyte-activated killer cells after the addition of calcium (By similarity). {ECO:0000250}.
uniprot
proteins