SLFN12
entrez
55106
canonical
uniprot
Q8IYM2
canonical
ensembl
ENSG00000172123
resolver
ensp
ENSP00000302077
resolver
ensp
ENSP00000378063
resolver
ensp
ENSP00000394903
resolver
ensp
ENSP00000398315
resolver
ensp
ENSP00000404175
resolver
ensp
ENSP00000519535
resolver
ensp
ENSP00000519536
resolver
ensp
ENSP00000604546
resolver
ensp
ENSP00000604548
resolver
ensp
ENSP00000631715
resolver
enst
ENST00000304905
resolver
enst
ENST00000394562
resolver
enst
ENST00000445092
resolver
enst
ENST00000447040
resolver
enst
ENST00000452764
resolver
enst
ENST00000714254
resolver
enst
ENST00000714255
resolver
enst
ENST00000934488
resolver
enst
ENST00000934489
resolver
enst
ENST00000961656
resolver
genesymbol
SLFN12
resolver
hgnc
HGNC:25500
resolver
uniprot
A8K711
resolver
uniprot
Q9NP47
resolver
uniprot_entry
SLN12_HUMAN
resolver
uniprot_sec
A8K711
resolver
uniprot_sec
Q9NP47
resolver
amino_acid_sequence
MNISVDLETNYAELVLDVGRVTLGENSRKKMKDCKLRKKQNESVSRAMCALLNSGGGVIKAEIENEDYSYTKDGIGLDLENSFSNILLFVPEYLDFMQNGNYFLIFVKSWSLNTSGLRITTLSSNLYKRDITSAKVMNATAALEFLKDMKKTRGRLYLRPELLAKRPCVDIQEENNMKALAGVFFDRTELDRKEKLTFTESTHVEIKNFSTEKLLQRIKEILPQYVSAFANTDGGYLFIGLNEDKEIIGFKAEMSDLDDLEREIEKSIRKMPVHHFCMEKKKINYSCKFLGVYDKGSLCGYVCALRVERFCCAVFAKEPDSWHVKDNRVMQLTRKEWIQFMVEAEPKFSSSYEEVISQINTSLPAPHSWPLLEWQRQRHHCPGLSGRITYTPENLCRKLFLQHEGLKQLICEEMDSVRKGSLIFSRSWSVDLGLQENHKVLCDALLISQDSPPVLYTFHMVQDEEFKGYSTQTALTLKQKLAKIGGYTKKVCVMTKIFYLSPEGMTSCQYDLRSQVIYPESYYFTRRKYLLKALFKALKRLKSLRDQFSFAENLYQIIGIDCFQKNDKKMFKSCRRLT
uniprot
proteins
ec_number
3.1.-.-
uniprot
proteins
function
FUNCTION: Ribonuclease which is part of an E2/17beta-estradiol-induced pro-apoptotic signaling pathway. E2 stabilizes the PDE3A/SLFN12 complex in the cytosol, promoting the dephosphorylation of SLFN12 and activating its pro-apoptotic ribosomal RNA/rRNA ribonuclease activity. This apoptotic pathway might be relevant in tissues with high concentration of E2 and be for instance involved in placenta remodeling (PubMed:31420216, PubMed:34272366, PubMed:34707099, PubMed:35104454). May play a role in cell differentiation (PubMed:30045019). {ECO:0000269|PubMed:30045019, ECO:0000269|PubMed:31420216, ECO:0000269|PubMed:34272366, ECO:0000269|PubMed:34707099, ECO:0000269|PubMed:35104454}.
uniprot
proteins
mass_dalton
66972
uniprot
proteins
mutagenesis
MUTAGEN 200; /note="E->A: Decreased ribosomal RNA ribonuclease activity."; /evidence="ECO:0000269|PubMed:34272366"; MUTAGEN 205; /note="E->A: Decreased ribosomal RNA ribonuclease activity."; /evidence="ECO:0000269|PubMed:34272366"; MUTAGEN 213; /note="K->R: Loss of function in the E2-induced apoptotic signaling pathway."; /evidence="ECO:0000269|PubMed:31420216"; MUTAGEN 233; /note="D->Q: Loss of interaction with SERPINB2."; /evidence="ECO:0000269|PubMed:30045019"; MUTAGEN 368; /note="S->A: Increased ribonuclease activity; when associated with A-573."; /evidence="ECO:0000269|PubMed:35104454"; MUTAGEN 368; /note="S->E: Decreased ribonuclease activity; when associated with E-573."; /evidence="ECO:0000269|PubMed:35104454"; MUTAGEN 573; /note="S->A: Increased ribonuclease activity; when associated with A-368."; /evidence="ECO:0000269|PubMed:35104454"; MUTAGEN 573; /note="S->E: Decreased ribonuclease activity; when associated with E-368."; /evidence="ECO:0000269|PubMed:35104454
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-368 and Ser-573 negatively regulates the ribonuclease activity (PubMed:35104454). Dephosphorylation is induced by the interaction with PDE3A and stimulates the rRNA ribonuclease activity (PubMed:35104454). {ECO:0000269|PubMed:35104454}.
uniprot
proteins
protein_family
Schlafen family
uniprot
proteins
protein_family
Subgroup II subfamily
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
30045019
uniprot
proteins
pubmed
31420216
uniprot
proteins
pubmed
34272366
uniprot
proteins
pubmed
34707099
uniprot
proteins
pubmed
35104454
uniprot
proteins
sequence_length
578
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:35104454}. Cytoplasm, cytosol {ECO:0000269|PubMed:35104454}.
uniprot
proteins