BTLA
entrez
151888
canonical
uniprot
Q7Z6A9
canonical
ensembl
ENSG00000186265
resolver
ensp
ENSP00000333919
resolver
ensp
ENSP00000373178
resolver
ensp
ENSP00000528337
resolver
genesymbol
BTLA
resolver
hgnc
HGNC:21087
resolver
uniprot
Q3B831
resolver
uniprot
Q3HS85
resolver
uniprot
Q400G7
resolver
uniprot
Q6ZNH9
resolver
uniprot_entry
BTLA_HUMAN
resolver
uniprot_entry
Q400G7_HUMAN
resolver
uniprot_sec
Q3B831
resolver
uniprot_sec
Q3HS85
resolver
uniprot_sec
Q6ZNH9
resolver
amino_acid_sequence
MKTLPAMLGTGKLFWVFFLIPYLDIWNIHGKESCDVQLYIKRQSEHSILAGDPFELECPVKYCANRPHVTWCKLNGTTCVKLEDRQTSWKEEKNISFFILHFEPVLPNDNGSYRCSANFQSNLIESHSTTLYVTDVKSASERPSKDEMASRPWLLYRLLPLGGLPLLITTCFCLFCCLRRHQGKQNELSDTAGREINLVDAHLKSEQTEASTRQNSQVLLSETGIYDNDPDLCFRMQEGSEVYSNPCLEENKPGIVYASLNHSVIGPNSRLARNVKEAPTEYASICVRS
uniprot
proteins
function
FUNCTION: Inhibitory receptor on lymphocytes that negatively regulates antigen receptor signaling via PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed:12796776, PubMed:14652006, PubMed:15568026, PubMed:18193050). May interact in cis (on the same cell) or in trans (on other cells) with TNFRSF14 (PubMed:19915044). In cis interactions, appears to play an immune regulatory role inhibiting in trans interactions in naive T cells to maintain a resting state. In trans interactions, can predominate during adaptive immune response to provide survival signals to effector T cells (PubMed:19915044). {ECO:0000269|PubMed:12796776, ECO:0000269|PubMed:14652006, ECO:0000269|PubMed:15568026, ECO:0000269|PubMed:18193050, ECO:0000269|PubMed:19915044}.
uniprot
proteins
mass_dalton
32834
uniprot
proteins
mutagenesis
MUTAGEN 226; /note="Y->F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-257 and/or F-282."; /evidence="ECO:0000269|PubMed:12796776, ECO:0000269|PubMed:14652006"; MUTAGEN 257; /note="Y->F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-226 and/or F-282."; /evidence="ECO:0000269|PubMed:12796776, ECO:0000269|PubMed:14652006"; MUTAGEN 282; /note="Y->F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-226 and/or F-257."; /evidence="ECO:0000269|PubMed:12796776, ECO:0000269|PubMed:14652006
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on Tyr residues by TNFRSF14 and by antigen receptors cross-linking, both inducing association with PTPN6 and PTPN11. {ECO:0000269|PubMed:15568026}.; PTM: N-glycosylated. {ECO:0000269|PubMed:12796776}.
uniprot
proteins
pubmed
12796776
uniprot
proteins
pubmed
14652006
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15568026
uniprot
proteins
pubmed
16169851
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
18193050
uniprot
proteins
pubmed
19915044
uniprot
proteins
sequence_length
289
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12796776}; Single-pass type I membrane protein {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 158..178; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins