Pirb
entrez
18733
canonical
uniprot
P97484
canonical
ensembl
ENSMUSG00000058818
resolver
ensp
ENSMUSP00000077546
resolver
ensp
ENSMUSP00000285625
resolver
ensp
ENSMUSP00000350833
resolver
enst
ENSMUST00000078451
resolver
genesymbol
Pirb
resolver
genesymbol_syn
Lilrb3
resolver
uniprot_entry
LIRB3_MOUSE
resolver
amino_acid_sequence
MSCTFTALLRLGLTLSLWIPVLTGSLPKPILRVQPDSVVSRRTKVTFLCEETIGANEYRLYKDGKLYKTVTKNKQKPENKAEFSFSNVDLSNAGQYRCSYSTQYKSSGYSDLLELVVTGHYWTPSLLAQASPVVTSGGYVTLQCESWHNDHKFILTVEGPQKLSWTQDSQYNYSTRKYHALFSVGPVTPNQRWICRCYSYDRNRPYVWSPPSESVELLVSGNLQKPTIKAEPGSVITSKRAMTIWCQGNLDAEVYFLHNEKSQKTQSTQTLQEPGNKGKFFIPSVTLQHAGQYRCYCYGSAGWSQPSDTLELVVTGIYEYYEPRLSVLPSPVVTAGGNMTLHCASDFPYDKFILTKEDKKFGNSLDTEHISSSGQYRALFIIGPTTPTHTGAFRCYGYYKNAPQLWSVPSALQQILISGLSKKPSLLTHQGHILDPGMTLTLQCFSDINYDRFALHKVGGADIMQHSSQQTDTGFSVANFTLGYVSSSTGGQYRCYGAHNLSSEWSASSEPLDILITGQLPLTPSLSVQPNHTVHSGETVSLLCWSMDSVDTFILSKEGSAQQPLRLKSKSHDQQSQAEFSMSAVTSHLSGTYRCYGAQDSSFYLLSSASAPVELTVSGPIETSTPPPTMSMPLGGLHMYLKALIGVSVAFILFLFIFIFILLRRRHRGKFRKDVQKEKDLQLSSGAEEPITRKGELQKRPNPAAATQEESLYASVEDMQTEDGVELNSWTPPEEDPQGETYAQVKPSRLRKAGHVSPSVMSREQLNTEYEQAEEGQGANNQAAESGESQDVTYAQLCSRTLRQGAAASPLSQAGEAPEEPSVYATLAAARPEAVPKDMEQ
uniprot
proteins
function
FUNCTION: May act as receptor for class I MHC antigens. Becomes activated upon coligation of PIRB and immune receptors, such as FCGR2B and the B-cell receptor. Down-regulates antigen-induced B-cell activation by recruiting phosphatases to its immunoreceptor tyrosine-based inhibitor motifs (ITIM). {ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:10611342, ECO:0000269|PubMed:9482905}.
uniprot
proteins
mass_dalton
93054
uniprot
proteins
mutagenesis
MUTAGEN 794; /note="Y->F: Abolishes interaction with PTPN6/SHP-1 and PTPN11/SHP-2; when associated with F-824."; /evidence="ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:9482905"; MUTAGEN 824; /note="Y->F: Abolishes interaction with PTPN6/SHP-1 and PTPN11/SHP-2; when associated with F-794."; /evidence="ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:9482905
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues by LYN. Phosphorylation at Tyr-794 and Tyr-824 by LYN is important for interaction with PTPN6/SHP-1 and PTPN11/SHP-2. {ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:10611342}.
uniprot
proteins
pubmed
10327049
uniprot
proteins
pubmed
10611342
uniprot
proteins
pubmed
11207596
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
9054430
uniprot
proteins
pubmed
9482905
uniprot
proteins
sequence_length
841
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:9054430, ECO:0000269|PubMed:9482905}; Single-pass type I membrane protein {ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:9054430, ECO:0000269|PubMed:9482905}.
uniprot
proteins
transmembrane_region
TRANSMEM 643..663; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins