FASLG
entrez
356
canonical
uniprot
P48023
canonical
ensembl
ENSG00000117560
resolver
ensp
ENSP00000344739
resolver
ensp
ENSP00000356694
resolver
genesymbol
FASLG
resolver
genesymbol
TNFSF6
resolver
genesymbol_syn
APT1LG1
resolver
genesymbol_syn
CD95L
resolver
genesymbol_syn
FASL
resolver
genesymbol_syn
FASLG
resolver
genesymbol_syn
TNFSF6
resolver
genesymbol_syn
TNLG1A
resolver
hgnc
HGNC:11936
resolver
uniprot
Q53ZZ1
resolver
uniprot
Q9BZP9
resolver
uniprot_entry
Q53ZZ1_HUMAN
resolver
uniprot_entry
TNFL6_HUMAN
resolver
uniprot_sec
Q9BZP9
resolver
amino_acid_sequence
MQQPFNYPYPQIYWVDSSASSPWAPPGTVLPCPTSVPRRPGQRRPPPPPPPPPLPPPPPPPPLPPLPLPPLKKRGNHSTGLCLLVMFFMVLVALVGLGLGMFQLFHLQKELAELRESTSQMHTASSLEKQIGHPSPPPEKKELRKVAHLTGKSNSRSMPLEWEDTYGIVLLSGVKYKKGGLVINETGLYFVYSKVYFRGQSCNNLPLSHKVYMRNSKYPQDLVMMEGKMMSYCTTGQMWARSSYLGAVFNLTSADHLYVNVSELSLVNFEESQTFFGLYKL
uniprot
proteins
disease_involvement
DISEASE: Autoimmune lymphoproliferative syndrome 1B (ALPS1B) [MIM:601859]: A disorder of apoptosis that manifests in early childhood and results in the accumulation of autoreactive lymphocytes. It is characterized by non-malignant lymphadenopathy with hepatosplenomegaly, and autoimmune hemolytic anemia, thrombocytopenia and neutropenia. {ECO:0000269|PubMed:26334989, ECO:0000269|PubMed:8787672}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells (PubMed:26334989, PubMed:9228058). Involved in cytotoxic T-cell-mediated apoptosis, natural killer cell-mediated apoptosis and in T-cell development (PubMed:7528780, PubMed:9228058, PubMed:9427603). Initiates fratricidal/suicidal activation-induced cell death (AICD) in antigen-activated T-cells contributing to the termination of immune responses (By similarity). TNFRSF6/FAS-mediated apoptosis also has a role in the induction of peripheral tolerance (By similarity). Binds to TNFRSF6B/DcR3, a decoy receptor that blocks apoptosis (PubMed:27806260). {ECO:0000250|UniProtKB:P41047, ECO:0000269|PubMed:17557115, ECO:0000269|PubMed:27806260, ECO:0000269|PubMed:7528780, ECO:0000269|PubMed:9228058, ECO:0000269|PubMed:9427603}.; FUNCTION: [Tumor necrosis factor ligand superfamily member 6, soluble form]: Induces FAS-mediated activation of NF-kappa-B, initiating non-apoptotic signaling pathways (By similarity). Can induce apoptosis but does not appear to be essential for this process (PubMed:27806260). {ECO:0000250|UniProtKB:P41047, ECO:0000269|PubMed:27806260}.; FUNCTION: [FasL intracellular domain]: Cytoplasmic form induces gene transcription inhibition. {ECO:0000269|PubMed:17557115}.
uniprot
proteins
mass_dalton
31485
uniprot
proteins
mutagenesis
MUTAGEN 206; /note="P->D,F,R: Lowers binding to TNFRSF6 and reduces cytotoxicity more than 100-fold."; /evidence="ECO:0000269|PubMed:9228058"; MUTAGEN 218; /note="Y->F,R: Lowers binding to TNFRSF6 and abolishes cytotoxicity."; /evidence="ECO:0000269|PubMed:9228058"; MUTAGEN 275; /note="F->L: Abolishes binding to TNRFSF6 and cytotoxicity."; /evidence="ECO:0000269|PubMed:9228058
uniprot
proteins
post_translational_modification
PTM: The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form undergoes two successive intramembrane proteolytic cleavages. The first one is processed by ADAM10 producing an N-terminal fragment, which lacks the receptor-binding extracellular domain. This ADAM10-processed FasL (FasL APL) remnant form is still membrane anchored and further processed by SPPL2A that liberates the FasL intracellular domain (FasL ICD). FasL shedding by ADAM10 is a prerequisite for subsequent intramembrane cleavage by SPPL2A in T-cells. {ECO:0000269|PubMed:17557115, ECO:0000269|PubMed:9427603}.; PTM: N-glycosylated (PubMed:9228058). Glycosylation enhances apoptotic activity (PubMed:27806260). {ECO:0000269|PubMed:27806260, ECO:0000269|PubMed:9228058}.; PTM: Phosphorylated by FGR on tyrosine residues; this is required for ubiquitination and subsequent internalization. {ECO:0000269|PubMed:17164290}.; PTM: Monoubiquitinated. {ECO:0000269|PubMed:17164290}.
uniprot
proteins
protein_family
Tumor necrosis factor family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17164290
uniprot
proteins
pubmed
17557115
uniprot
proteins
pubmed
19807924
uniprot
proteins
pubmed
26334989
uniprot
proteins
pubmed
27806260
uniprot
proteins
pubmed
7528780
uniprot
proteins
pubmed
7826947
uniprot
proteins
pubmed
7980502
uniprot
proteins
pubmed
8787672
uniprot
proteins
pubmed
9228058
uniprot
proteins
pubmed
9427603
uniprot
proteins
sequence_length
281
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17557115, ECO:0000269|PubMed:9427603}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasmic vesicle lumen {ECO:0000269|PubMed:17164290}. Lysosome lumen {ECO:0000269|PubMed:17164290}. Note=Is internalized into multivesicular bodies of secretory lysosomes after phosphorylation by FGR and monoubiquitination (PubMed:17164290). Colocalizes with the SPPL2A protease at the cell membrane (PubMed:17557115). {ECO:0000269|PubMed:17164290, ECO:0000269|PubMed:17557115}.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 6, soluble form]: Secreted {ECO:0000269|PubMed:9427603}. Note=May be released into the extracellular fluid by cleavage from the cell surface. {ECO:0000269|PubMed:9427603}.; SUBCELLULAR LOCATION: [FasL intracellular domain]: Nucleus {ECO:0000269|PubMed:17557115}. Note=The FasL ICD cytoplasmic form is translocated into the nucleus. {ECO:0000269|PubMed:17557115}.
uniprot
proteins
transmembrane_region
TRANSMEM 81..102; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins