LAIR1
entrez
3903
canonical
uniprot
Q6GTX8
canonical
ensembl
ENSG00000167613
resolver
ensembl
ENSG00000274110
resolver
ensembl
ENSG00000276053
resolver
ensembl
ENSG00000276163
resolver
ensembl
ENSG00000278154
resolver
ensp
ENSP00000301193
resolver
ensp
ENSP00000319204
resolver
ensp
ENSP00000375622
resolver
ensp
ENSP00000375623
resolver
ensp
ENSP00000391003
resolver
ensp
ENSP00000418998
resolver
ensp
ENSP00000478405
resolver
ensp
ENSP00000478853
resolver
ensp
ENSP00000479006
resolver
ensp
ENSP00000479133
resolver
ensp
ENSP00000479294
resolver
ensp
ENSP00000479649
resolver
ensp
ENSP00000479682
resolver
ensp
ENSP00000479707
resolver
ensp
ENSP00000479951
resolver
ensp
ENSP00000480619
resolver
ensp
ENSP00000480659
resolver
ensp
ENSP00000481204
resolver
ensp
ENSP00000481597
resolver
ensp
ENSP00000482922
resolver
ensp
ENSP00000483622
resolver
enst
ENST00000313038
resolver
enst
ENST00000391743
resolver
enst
ENST00000434277
resolver
enst
ENST00000610549
resolver
enst
ENST00000614937
resolver
enst
ENST00000614946
resolver
enst
ENST00000616612
resolver
enst
ENST00000616724
resolver
enst
ENST00000618291
resolver
enst
ENST00000618434
resolver
enst
ENST00000619717
resolver
enst
ENST00000619817
resolver
enst
ENST00000620077
resolver
enst
ENST00000620357
resolver
enst
ENST00000620726
resolver
enst
ENST00000621291
resolver
enst
ENST00000621769
resolver
enst
ENST00000622097
resolver
genesymbol
LAIR1
resolver
genesymbol_syn
CD305
resolver
hgnc
HGNC:6477
resolver
uniprot
A0A0G2JMI0
resolver
uniprot
A0A0G2JNK8
resolver
uniprot
A0A140T8W3
resolver
uniprot
A8MZ84
resolver
uniprot
D3YTC8
resolver
uniprot_entry
A0A0G2JMI0_HUMAN
resolver
uniprot_entry
A0A0G2JNK8_HUMAN
resolver
uniprot_entry
A0A140T8W3_HUMAN
resolver
uniprot_entry
A8MZ84_HUMAN
resolver
uniprot_entry
D3YTC8_HUMAN
resolver
uniprot_entry
LAIR1_HUMAN
resolver
amino_acid_sequence
MSPHPTALLGLVLCLAQTIHTQEEDLPRPSISAEPGTVIPLGSHVTFVCRGPVGVQTFRLERDSRSTYNDTEDVSQASPSESEARFRIDSVREGNAGLYRCIYYKPPKWSEQSDYLELLVKESSGGPDSPDTEPGSSAGPTQRPSDNSHNEHAPASQGLKAEHLYILIGVSVVFLFCLLLLVLFCLHRQNQIKQGPPRSKDEEQKPQQRPDLAVDVLERTADKATVNGLPEKDRETDTSALAAGSSQEVTYAQLDHWALTQRTARAVSPQSTKPMAESITYAAVARH
uniprot
proteins
function
FUNCTION: Functions as an inhibitory receptor that plays a constitutive negative regulatory role on cytolytic function of natural killer (NK) cells, B-cells and T-cells. Activation by Tyr phosphorylation results in recruitment and activation of the phosphatases PTPN6 and PTPN11. It also reduces the increase of intracellular calcium evoked by B-cell receptor ligation. May also play its inhibitory role independently of SH2-containing phosphatases. Modulates cytokine production in CD4+ T-cells, down-regulating IL2 and IFNG production while inducing secretion of transforming growth factor beta. Also down-regulates IgG and IgE production in B-cells as well as IL8, IL10 and TNF secretion. Inhibits proliferation and induces apoptosis in myeloid leukemia cell lines as well as prevents nuclear translocation of NF-kappa-B p65 subunit/RELA and phosphorylation of I-kappa-B alpha/CHUK in these cells. Inhibits the differentiation of peripheral blood precursors towards dendritic cells. {ECO:0000269|PubMed:10229813, ECO:0000269|PubMed:10764762, ECO:0000269|PubMed:11069054, ECO:0000269|PubMed:11160222, ECO:0000269|PubMed:12072189, ECO:0000269|PubMed:15939744, ECO:0000269|PubMed:15950745, ECO:0000269|PubMed:16380958, ECO:0000269|PubMed:9285412, ECO:0000269|PubMed:9692876}.
uniprot
proteins
mass_dalton
31469
uniprot
proteins
mutagenesis
MUTAGEN 251; /note="Y->F: Reduced tyrosine phosphorylation and loss of binding to PTPN6 and CSK as well as complete loss of inhibitory activity. Loss of phosphorylation and of inhibition of calcium mobilization; when associated with F-281."; /evidence="ECO:0000269|PubMed:10764762, ECO:0000269|PubMed:14565933, ECO:0000269|PubMed:16380958"; MUTAGEN 281; /note="Y->F: Reduced tyrosine phosphorylation and loss of binding to PTPN6. Partial inhibition of cytotoxic activity."; /evidence="ECO:0000269|PubMed:10764762, ECO:0000269|PubMed:14565933, ECO:0000269|PubMed:16380958
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Tyr-251 and Tyr-281 activates it. May be phosphorylated by LCK. {ECO:0000269|PubMed:10764762}.; PTM: N-glycosylated. {ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:9285412}.
uniprot
proteins
pubmed
10229813
uniprot
proteins
pubmed
10540327
uniprot
proteins
pubmed
10764762
uniprot
proteins
pubmed
11069054
uniprot
proteins
pubmed
11160222
uniprot
proteins
pubmed
12072189
uniprot
proteins
pubmed
12757266
uniprot
proteins
pubmed
14565933
uniprot
proteins
pubmed
14604962
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15939744
uniprot
proteins
pubmed
15950745
uniprot
proteins
pubmed
16380958
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20007810
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
9285412
uniprot
proteins
pubmed
9692876
uniprot
proteins
sequence_length
287
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10229813, ECO:0000269|PubMed:11160222, ECO:0000269|PubMed:9285412}; Single-pass type I membrane protein {ECO:0000269|PubMed:10229813, ECO:0000269|PubMed:11160222, ECO:0000269|PubMed:9285412}.
uniprot
proteins
transmembrane_region
TRANSMEM 166..186; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins