Btla
entrez
208154
canonical
uniprot
Q7TSA3
canonical
ensembl
ENSMUSG00000052013
resolver
ensp
ENSMUSP00000067877
resolver
ensp
ENSMUSP00000099866
resolver
ensp
ENSMUSP00000186434
resolver
enst
ENSMUST00000063654
resolver
enst
ENSMUST00000102802
resolver
genesymbol
Btla
resolver
uniprot
A0A0R4J1A0
resolver
uniprot
E9QNY6
resolver
uniprot
Q32MV8
resolver
uniprot_entry
A0A0R4J1A0_MOUSE
resolver
uniprot_entry
BTLA_MOUSE
resolver
uniprot_entry
E9QNY6_MOUSE
resolver
uniprot_entry
Q32MV8_MOUSE
resolver
amino_acid_sequence
MKTVPAMLGTPRLFREFFILHLGLWSILCEKATKRNDEECPVQLTITRNSKQSARTGELFKIQCPVKYCVHRPNVTWCKHNGTICVPLEVSPQLYTSWEENQSVPVFVLHFKPIHLSDNGSYSCSTNFNSQVINSHSVTIHVRERTQNSSEHPLITVSDIPDATNASGPSTMEERPGRTWLLYTLLPLGALLLLLACVCLLCFLKRIQGKEKKPSDLAGRDTNLVDIPASSRTNHQALPSGTGIYDNDPWSSMQDESELTISLQSERNNQGIVYASLNHCVIGRNPRQENNMQEAPTEYASICVRS
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). 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:19915044}.
uniprot
proteins
mass_dalton
34337
uniprot
proteins
mutagenesis
MUTAGEN 44; /note="L->H: Loss of interaction with TNFRSF14."; /evidence="ECO:0000269|PubMed:18178834"; MUTAGEN 48; /note="R->D: Loss of interaction with TNFRSF14."; /evidence="ECO:0000269|PubMed:18178834"; MUTAGEN 65; /note="P->A: Loss of interaction with TNFRSF14."; /evidence="ECO:0000269|PubMed:18178834"; MUTAGEN 136; /note="H->D: Loss of interaction with TNFRSF14."; /evidence="ECO:0000269|PubMed:18178834"; MUTAGEN 245; /note="Y->F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-274 and/or F-299."; /evidence="ECO:0000269|PubMed:12796776, ECO:0000269|PubMed:14652006"; MUTAGEN 274; /note="Y->F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-245 and/or F-299."; /evidence="ECO:0000269|PubMed:12796776, ECO:0000269|PubMed:14652006"; MUTAGEN 299; /note="Y->F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-245 and/or F-274."; /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
15568026
uniprot
proteins
pubmed
15749870
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18178834
uniprot
proteins
pubmed
19915044
uniprot
proteins
sequence_length
306
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 184..204; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins