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Leukocyte immunoglobulin-like receptor subfamily B member 1 (LIR-1) (Leukocyte immunoglobulin-like receptor 1) (CD85 antigen-like family member J) (Immunoglobulin-like transcript 2) (ILT-2) (Monocyte/macrophage immunoglobulin-like receptor 7) (MIR-7) (CD antigen CD85j)

 LIRB1_HUMAN             Reviewed;         650 AA.
Q8NHL6; A2IXV4; A8MXT0; O75024; O75025; Q8NHJ9; Q8NHK0;
03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
07-APR-2021, entry version 174.
RecName: Full=Leukocyte immunoglobulin-like receptor subfamily B member 1;
Short=LIR-1 {ECO:0000303|PubMed:11114384};
Short=Leukocyte immunoglobulin-like receptor 1;
AltName: Full=CD85 antigen-like family member J;
AltName: Full=Immunoglobulin-like transcript 2;
Short=ILT-2 {ECO:0000303|PubMed:11114384};
AltName: Full=Monocyte/macrophage immunoglobulin-like receptor 7;
Short=MIR-7;
AltName: CD_antigen=CD85j {ECO:0000303|PubMed:11907092, ECO:0000303|PubMed:24453251};
Flags: Precursor;
Name=LILRB1 {ECO:0000303|PubMed:20600445, ECO:0000312|HGNC:HGNC:6605};
Synonyms=ILT2 {ECO:0000303|PubMed:24453251},
LIR1 {ECO:0000303|PubMed:28636952}, MIR7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
PubMed=9259559; DOI=10.1016/s0960-9822(06)00263-6;
Wagtmann N., Rojo S., Eichler E., Mohrenweiser H., Long E.O.;
"A new human gene complex encoding the killer cell inhibitory receptors and
related monocyte/macrophage receptors.";
Curr. Biol. 7:615-618(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), VARIANTS PRO-68; THR-142;
ILE-155 AND LYS-625, INTERACTION WITH H301 AND PTPN6, PHOSPHORYLATION,
TISSUE SPECIFICITY, AND FUNCTION.
TISSUE=Lymphoblast;
PubMed=9285411; DOI=10.1016/s1074-7613(00)80529-4;
Cosman D., Fanger N., Borges L., Kubin M., Chin W., Peterson L., Hsu M.-L.;
"A novel immunoglobulin superfamily receptor for cellular and viral MHC
class I molecules.";
Immunity 7:273-282(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=10941837; DOI=10.1007/s002510000183;
Liu W.R., Kim J., Nwankwo C., Ashworth L.K., Arm J.P.;
"Genomic organization of the human leukocyte immunoglobulin-like receptors
within the leukocyte receptor complex on chromosome 19q13.4.";
Immunogenetics 51:659-669(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), ALTERNATIVE SPLICING, SUBCELLULAR
LOCATION (ISOFORM 5), AND VARIANTS PRO-68; THR-93; THR-142 AND ILE-155.
PubMed=19658091; DOI=10.1002/eji.200839080;
Jones D.C., Roghanian A., Brown D.P., Chang C., Allen R.L., Trowsdale J.,
Young N.T.;
"Alternative mRNA splicing creates transcripts encoding soluble proteins
from most LILR genes.";
Eur. J. Immunol. 39:3195-3206(2009).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-68; THR-93; THR-142;
ILE-155 AND LYS-625.
PubMed=20600445; DOI=10.1016/j.humimm.2010.06.015;
Davidson C.L., Li N.L., Burshtyn D.N.;
"LILRB1 polymorphism and surface phenotypes of natural killer cells.";
Hum. Immunol. 71:942-949(2010).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Canavez F.C.;
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PRO-68;
THR-142; ILE-155 AND LYS-625.
TISSUE=B-cell;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH PTPN6 AND FCGR1A, PHOSPHORYLATION, TISSUE SPECIFICITY, AND
FUNCTION.
PubMed=9842885;
DOI=10.1002/(sici)1521-4141(199811)28:11<3423::aid-immu3423>3.0.co;2-2;
Fanger N.A., Cosman D., Peterson L., Braddy S.C., Maliszewski C.R.,
Borges L.;
"The MHC class I binding proteins LIR-1 and LIR-2 inhibit Fc receptor-
mediated signaling in monocytes.";
Eur. J. Immunol. 28:3423-3434(1998).
[10]
INTERACTION WITH HHV-5 PROTEIN UL18.
PubMed=10591185; DOI=10.1016/s1074-7613(00)80135-1;
Chapman T.L., Heikeman A.P., Bjorkman P.J.;
"The inhibitory receptor LIR-1 uses a common binding interaction to
recognize class I MHC molecules and the viral homolog UL18.";
Immunity 11:603-613(1999).
[11]
PHOSPHORYLATION AT TYR-533; TYR-614 AND TYR-644, MUTAGENESIS OF TYR-533;
TYR-562; TYR-614 AND TYR-644, INTERACTION WITH FCER1A, AND FUNCTION.
PubMed=11907092; DOI=10.4049/jimmunol.168.7.3351;
Bellon T., Kitzig F., Sayos J., Lopez-Botet M.;
"Mutational analysis of immunoreceptor tyrosine-based inhibition motifs of
the Ig-like transcript 2 (CD85j) leukocyte receptor.";
J. Immunol. 168:3351-3359(2002).
[12]
FUNCTION, SUBUNIT, AND INTERACTION WITH HLA-G.
PubMed=16455647; DOI=10.1074/jbc.m512305200;
Shiroishi M., Kuroki K., Ose T., Rasubala L., Shiratori I., Arase H.,
Tsumoto K., Kumagai I., Kohda D., Maenaka K.;
"Efficient leukocyte Ig-like receptor signaling and crystal structure of
disulfide-linked HLA-G dimer.";
J. Biol. Chem. 281:10439-10447(2006).
[13]
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=19304799; DOI=10.1073/pnas.0901173106;
Li C., Houser B.L., Nicotra M.L., Strominger J.L.;
"HLA-G homodimer-induced cytokine secretion through HLA-G receptors on
human decidual macrophages and natural killer cells.";
Proc. Natl. Acad. Sci. U.S.A. 106:5767-5772(2009).
[14]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=20448110; DOI=10.1182/blood-2009-07-234872;
Gregori S., Tomasoni D., Pacciani V., Scirpoli M., Battaglia M.,
Magnani C.F., Hauben E., Roncarolo M.G.;
"Differentiation of type 1 T regulatory cells (Tr1) by tolerogenic DC-10
requires the IL-10-dependent ILT4/HLA-G pathway.";
Blood 116:935-944(2010).
[15]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=24453251; DOI=10.4049/jimmunol.1300438;
Naji A., Menier C., Morandi F., Agaugue S., Maki G., Ferretti E., Bruel S.,
Pistoia V., Carosella E.D., Rouas-Freiss N.;
"Binding of HLA-G to ITIM-bearing Ig-like transcript 2 receptor suppresses
B cell responses.";
J. Immunol. 192:1536-1546(2014).
[16]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=29262349; DOI=10.1016/j.immuni.2017.11.018;
Fu B., Zhou Y., Ni X., Tong X., Xu X., Dong Z., Sun R., Tian Z., Wei H.;
"Natural Killer Cells Promote Fetal Development through the Secretion of
Growth-Promoting Factors.";
Immunity 47:1100-1113(2017).
[17]
FUNCTION, SUBUNIT, AND INTERACTION WITH HLA-F.
PubMed=28636952; DOI=10.1016/j.immuni.2017.06.002;
Dulberger C.L., McMurtrey C.P., Holzemer A., Neu K.E., Liu V.,
Steinbach A.M., Garcia-Beltran W.F., Sulak M., Jabri B., Lynch V.J.,
Altfeld M., Hildebrand W.H., Adams E.J.;
"Human Leukocyte Antigen F Presents Peptides and Regulates Immunity through
Interactions with NK Cell Receptors.";
Immunity 46:1018-1029(2017).
[18]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 25-221, AND DISULFIDE BONDS.
PubMed=11114384; DOI=10.1016/s1074-7613(00)00071-6;
Chapman T.L., Heikema A.P., West A.P. Jr., Bjorkman P.J.;
"Crystal structure and ligand binding properties of the D1D2 region of the
inhibitory receptor LIR-1 (ILT2).";
Immunity 13:727-736(2000).
-!- FUNCTION: Receptor for class I MHC antigens. Recognizes a broad
spectrum of HLA-A, HLA-B, HLA-C, HLA-G and HLA-F alleles
(PubMed:16455647, PubMed:28636952). Receptor for H301/UL18, a human
cytomegalovirus class I MHC homolog. Ligand binding results in
inhibitory signals and down-regulation of the immune response.
Engagement of LILRB1 present on natural killer cells or T-cells by
class I MHC molecules protects the target cells from lysis. Interaction
with HLA-B or HLA-E leads to inhibition of FCER1A signaling and
serotonin release. Inhibits FCGR1A-mediated phosphorylation of cellular
proteins and mobilization of intracellular calcium ions
(PubMed:11907092, PubMed:9285411, PubMed:9842885). Recognizes HLA-G in
complex with B2M/beta-2 microglobulin and a nonamer self-peptide
(PubMed:16455647). Upon interaction with peptide-bound HLA-G-B2M
complex, triggers secretion of growth-promoting factors by decidual NK
cells (PubMed:29262349, PubMed:19304799). Reprograms B cells toward an
immune suppressive phenotype (PubMed:24453251).
{ECO:0000269|PubMed:11907092, ECO:0000269|PubMed:16455647,
ECO:0000269|PubMed:19304799, ECO:0000269|PubMed:24453251,
ECO:0000269|PubMed:28636952, ECO:0000269|PubMed:29262349,
ECO:0000269|PubMed:9285411, ECO:0000269|PubMed:9842885}.
-!- SUBUNIT: Binds PTPN6 when phosphorylated (PubMed:9285411). Binds FCER1A
and FCGR1A (PubMed:9842885, PubMed:11907092). Interacts with human
cytomegalovirus/HHV-5 protein UL18 (PubMed:10591185). Interacts with
peptide-bound HLA-G-B2M complex (PubMed:16455647). Interacts with
peptide-bound HLA-F-B2M complex but not with peptide-free HLA-F open
conformer. It does not probe the peptide sequence directly
(PubMed:28636952). {ECO:0000269|PubMed:10591185,
ECO:0000269|PubMed:11907092, ECO:0000269|PubMed:16455647,
ECO:0000269|PubMed:28636952, ECO:0000269|PubMed:9285411,
ECO:0000269|PubMed:9842885}.
-!- INTERACTION:
Q8NHL6; P17693: HLA-G; NbExp=5; IntAct=EBI-2805262, EBI-1043063;
Q8NHL6; P29350: PTPN6; NbExp=4; IntAct=EBI-2805262, EBI-78260;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20448110,
ECO:0000269|PubMed:24453251, ECO:0000269|PubMed:29262349,
ECO:0000305|PubMed:19658091}; Single-pass type I membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: [Isoform 5]: Secreted
{ECO:0000269|PubMed:19658091}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q8NHL6-1; Sequence=Displayed;
Name=2;
IsoId=Q8NHL6-2; Sequence=VSP_008456;
Name=3;
IsoId=Q8NHL6-3; Sequence=VSP_008456, VSP_008457;
Name=4;
IsoId=Q8NHL6-4; Sequence=VSP_008457;
Name=5; Synonyms=65 Kda, sLILRB1;
IsoId=Q8NHL6-5; Sequence=VSP_008456, VSP_057087, VSP_057088;
-!- TISSUE SPECIFICITY: Expressed in B cells, monocytes and various
dendritic cell (DC) subsets including myeloid, plasmacytoid and
tolerogenic DCs (at protein level) (PubMed:20448110, PubMed:9285411,
PubMed:9842885, PubMed:24453251). Expressed in decidual macrophages (at
protein level) (PubMed:19304799). Expressed in decidual NK cells (at
protein level) (PubMed:29262349). {ECO:0000269|PubMed:19304799,
ECO:0000269|PubMed:20448110, ECO:0000269|PubMed:24453251,
ECO:0000269|PubMed:29262349, ECO:0000269|PubMed:9285411,
ECO:0000269|PubMed:9842885}.
-!- DOMAIN: Contains 4 copies of a cytoplasmic motif that is referred to as
the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
involved in modulation of cellular responses. The phosphorylated ITIM
motif can bind the SH2 domain of several SH2-containing phosphatases.
-!- PTM: Phosphorylated on tyrosine residues. Dephosphorylated by PTPN6.
{ECO:0000269|PubMed:11907092, ECO:0000269|PubMed:9285411,
ECO:0000269|PubMed:9842885}.
-!- MISCELLANEOUS: [Isoform 5]: May act as dominant negative regulator and
block the interaction between membrane-associated isoforms and HLA-
class I. {ECO:0000269|PubMed:19658091}.
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EMBL; AF004230; AAB67710.1; -; mRNA.
EMBL; AF009220; AAB63521.1; -; mRNA.
EMBL; AF009221; AAB63522.1; -; mRNA.
EMBL; AF189277; AAG08984.1; -; Genomic_DNA.
EMBL; EU915608; ACK56074.1; -; mRNA.
EMBL; HM135394; ADJ55944.1; -; Genomic_DNA.
EMBL; HM135401; ADJ55951.1; -; Genomic_DNA.
EMBL; AF283984; AAL36988.1; -; mRNA.
EMBL; AF283985; AAL36989.1; -; mRNA.
EMBL; AC009892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015731; AAH15731.1; -; mRNA.
CCDS; CCDS42614.1; -. [Q8NHL6-3]
CCDS; CCDS42615.1; -. [Q8NHL6-2]
CCDS; CCDS42616.1; -. [Q8NHL6-4]
CCDS; CCDS42617.1; -. [Q8NHL6-1]
RefSeq; NP_001075106.2; NM_001081637.2.
RefSeq; NP_001075107.2; NM_001081638.3.
RefSeq; NP_001075108.2; NM_001081639.3.
RefSeq; NP_001265327.2; NM_001278398.2.
RefSeq; NP_001265328.2; NM_001278399.2.
RefSeq; NP_006660.4; NM_006669.6.
PDB; 1G0X; X-ray; 2.10 A; A=25-221.
PDB; 1P7Q; X-ray; 3.40 A; D=25-221.
PDB; 1UFU; X-ray; 3.00 A; A=25-221.
PDB; 1UGN; X-ray; 1.80 A; A=24-221.
PDB; 1VDG; X-ray; 2.80 A; A/B=24-220.
PDB; 3D2U; X-ray; 2.21 A; D/H=24-221.
PDB; 4LL9; X-ray; 2.69 A; A/B/C=222-417.
PDB; 4NO0; X-ray; 2.70 A; D=27-221.
PDB; 5KNM; X-ray; 3.30 A; D=24-221.
PDB; 6AEE; X-ray; 3.30 A; G/H=25-417.
PDB; 6EWA; X-ray; 2.39 A; D/H=27-221.
PDB; 6EWC; X-ray; 3.20 A; D/H=27-221.
PDB; 6EWO; X-ray; 2.30 A; D/H=27-221.
PDB; 6K60; X-ray; 3.15 A; D/H=24-220.
PDBsum; 1G0X; -.
PDBsum; 1P7Q; -.
PDBsum; 1UFU; -.
PDBsum; 1UGN; -.
PDBsum; 1VDG; -.
PDBsum; 3D2U; -.
PDBsum; 4LL9; -.
PDBsum; 4NO0; -.
PDBsum; 5KNM; -.
PDBsum; 6AEE; -.
PDBsum; 6EWA; -.
PDBsum; 6EWC; -.
PDBsum; 6EWO; -.
PDBsum; 6K60; -.
SMR; Q8NHL6; -.
BioGRID; 116070; 7.
IntAct; Q8NHL6; 14.
MINT; Q8NHL6; -.
STRING; 9606.ENSP00000315997; -.
GlyGen; Q8NHL6; 3 sites.
iPTMnet; Q8NHL6; -.
PhosphoSitePlus; Q8NHL6; -.
BioMuta; LILRB1; -.
DMDM; 37537910; -.
jPOST; Q8NHL6; -.
MassIVE; Q8NHL6; -.
PaxDb; Q8NHL6; -.
PeptideAtlas; Q8NHL6; -.
PRIDE; Q8NHL6; -.
ProteomicsDB; 73718; -. [Q8NHL6-1]
ProteomicsDB; 73719; -. [Q8NHL6-2]
ProteomicsDB; 73720; -. [Q8NHL6-3]
ProteomicsDB; 73721; -. [Q8NHL6-4]
DNASU; 10859; -.
Ensembl; ENST00000612636; ENSP00000479887; ENSG00000277807. [Q8NHL6-3]
Ensembl; ENST00000616408; ENSP00000481700; ENSG00000274669.
Ensembl; ENST00000617686; ENSP00000478282; ENSG00000277807. [Q8NHL6-4]
Ensembl; ENST00000618055; ENSP00000480365; ENSG00000277807. [Q8NHL6-1]
Ensembl; ENST00000618681; ENSP00000479753; ENSG00000277807. [Q8NHL6-2]
GeneID; 10859; -.
KEGG; hsa:10859; -.
UCSC; uc032iow.2; human. [Q8NHL6-1]
CTD; 10859; -.
DisGeNET; 10859; -.
GeneCards; LILRB1; -.
HGNC; HGNC:6605; LILRB1.
MIM; 604811; gene.
neXtProt; NX_Q8NHL6; -.
PharmGKB; PA30379; -.
eggNOG; ENOG502RYEX; Eukaryota.
InParanoid; Q8NHL6; -.
OrthoDB; 1000446at2759; -.
PhylomeDB; Q8NHL6; -.
TreeFam; TF336644; -.
PathwayCommons; Q8NHL6; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
SIGNOR; Q8NHL6; -.
BioGRID-ORCS; 10859; 2 hits in 962 CRISPR screens.
ChiTaRS; LILRB1; human.
EvolutionaryTrace; Q8NHL6; -.
GeneWiki; LILRB1; -.
GenomeRNAi; 10859; -.
Pharos; Q8NHL6; Tbio.
PRO; PR:Q8NHL6; -.
Proteomes; UP000005640; Chromosome 19.
RNAct; Q8NHL6; protein.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030107; F:HLA-A specific inhibitory MHC class I receptor activity; IDA:UniProtKB.
GO; GO:0030109; F:HLA-B specific inhibitory MHC class I receptor activity; IDA:UniProtKB.
GO; GO:0042288; F:MHC class I protein binding; IDA:UniProtKB.
GO; GO:0032393; F:MHC class I receptor activity; IDA:UniProtKB.
GO; GO:0023029; F:MHC class Ib protein binding; IDA:UniProtKB.
GO; GO:0023025; F:MHC class Ib protein complex binding; IDA:UniProtKB.
GO; GO:0032394; F:MHC class Ib receptor activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0008157; F:protein phosphatase 1 binding; IPI:UniProtKB.
GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0097028; P:dendritic cell differentiation; IEP:UniProtKB.
GO; GO:0002774; P:Fc receptor mediated inhibitory signaling pathway; IDA:UniProtKB.
GO; GO:0002767; P:immune response-inhibiting cell surface receptor signaling pathway; NAS:BHF-UCL.
GO; GO:0046636; P:negative regulation of alpha-beta T cell activation; IDA:UniProtKB.
GO; GO:0051926; P:negative regulation of calcium ion transport; IDA:UniProtKB.
GO; GO:2001186; P:negative regulation of CD8-positive, alpha-beta T cell activation; IDA:UniProtKB.
GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; IDA:UniProtKB.
GO; GO:2000669; P:negative regulation of dendritic cell apoptotic process; IDA:UniProtKB.
GO; GO:2001199; P:negative regulation of dendritic cell differentiation; IMP:UniProtKB.
GO; GO:0045806; P:negative regulation of endocytosis; IDA:UniProtKB.
GO; GO:0032688; P:negative regulation of interferon-beta production; IDA:UniProtKB.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0032693; P:negative regulation of interleukin-10 production; IDA:UniProtKB.
GO; GO:0032695; P:negative regulation of interleukin-12 production; IDA:UniProtKB.
GO; GO:0032945; P:negative regulation of mononuclear cell proliferation; IDA:UniProtKB.
GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB.
GO; GO:2001205; P:negative regulation of osteoclast development; IDA:UniProtKB.
GO; GO:0014063; P:negative regulation of serotonin secretion; IDA:UniProtKB.
GO; GO:2001189; P:negative regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IDA:UniProtKB.
GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; IDA:UniProtKB.
GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:UniProtKB.
GO; GO:0071635; P:negative regulation of transforming growth factor beta production; IDA:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:UniProtKB.
GO; GO:2001193; P:positive regulation of gamma-delta T cell activation involved in immune response; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0060907; P:positive regulation of macrophage cytokine production; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; NAS:BHF-UCL.
GO; GO:0031623; P:receptor internalization; TAS:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
GO; GO:0002309; P:T cell proliferation involved in immune response; IDA:UniProtKB.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
Pfam; PF00047; ig; 1.
Pfam; PF13895; Ig_2; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 3.
SUPFAM; SSF48726; SSF48726; 4.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Membrane;
Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1..23
/evidence="ECO:0000255"
CHAIN 24..650
/note="Leukocyte immunoglobulin-like receptor subfamily B
member 1"
/id="PRO_0000014820"
TOPO_DOM 24..461
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 462..482
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 483..650
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 27..115
/note="Ig-like C2-type 1"
DOMAIN 116..221
/note="Ig-like C2-type 2"
DOMAIN 222..312
/note="Ig-like C2-type 3"
DOMAIN 313..409
/note="Ig-like C2-type 4"
MOTIF 531..536
/note="ITIM motif 1"
MOTIF 560..565
/note="ITIM motif 2"
MOTIF 612..617
/note="ITIM motif 3"
MOTIF 642..647
/note="ITIM motif 4"
MOD_RES 533
/note="Phosphotyrosine"
/evidence="ECO:0000305|PubMed:11907092"
MOD_RES 614
/note="Phosphotyrosine"
/evidence="ECO:0000305|PubMed:11907092"
MOD_RES 644
/note="Phosphotyrosine"
/evidence="ECO:0000305|PubMed:11907092"
CARBOHYD 281
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 302
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 341
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 49..98
/evidence="ECO:0000269|PubMed:11114384,
ECO:0007744|PDB:1G0X"
DISULFID 145..197
/evidence="ECO:0000269|PubMed:11114384,
ECO:0007744|PDB:1G0X"
DISULFID 157..167
/evidence="ECO:0000269|PubMed:11114384,
ECO:0007744|PDB:1G0X"
DISULFID 246..297
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:11114384, ECO:0007744|PDB:1G0X"
DISULFID 346..397
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:11114384, ECO:0007744|PDB:1G0X"
VAR_SEQ 437
/note="S -> SA (in isoform 2, isoform 3 and isoform 5)"
/evidence="ECO:0000303|PubMed:19658091,
ECO:0000303|PubMed:9285411"
/id="VSP_008456"
VAR_SEQ 455
/note="L -> E (in isoform 5)"
/evidence="ECO:0000303|PubMed:19658091"
/id="VSP_057087"
VAR_SEQ 456..650
/note="Missing (in isoform 5)"
/evidence="ECO:0000303|PubMed:19658091"
/id="VSP_057088"
VAR_SEQ 550
/note="R -> RQ (in isoform 3 and isoform 4)"
/evidence="ECO:0000303|PubMed:20600445,
ECO:0000303|PubMed:9259559, ECO:0000303|PubMed:9285411"
/id="VSP_008457"
VARIANT 68
/note="L -> P (in dbSNP:rs1061679)"
/evidence="ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:19658091, ECO:0000269|PubMed:20600445,
ECO:0000269|PubMed:9285411"
/id="VAR_016993"
VARIANT 93
/note="A -> T (in dbSNP:rs12460501)"
/evidence="ECO:0000269|PubMed:19658091,
ECO:0000269|PubMed:20600445"
/id="VAR_049888"
VARIANT 142
/note="I -> T (in dbSNP:rs1061680)"
/evidence="ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:19658091, ECO:0000269|PubMed:20600445,
ECO:0000269|PubMed:9285411"
/id="VAR_016994"
VARIANT 155
/note="S -> I (in dbSNP:rs1061681)"
/evidence="ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:19658091, ECO:0000269|PubMed:20600445,
ECO:0000269|PubMed:9285411"
/id="VAR_016995"
VARIANT 301
/note="H -> Y (in dbSNP:rs1045818)"
/id="VAR_059398"
VARIANT 459
/note="L -> V (in dbSNP:rs1138737)"
/id="VAR_067316"
VARIANT 620
/note="L -> F (in dbSNP:rs634222)"
/id="VAR_016996"
VARIANT 625
/note="E -> K (in dbSNP:rs16985478)"
/evidence="ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:20600445, ECO:0000269|PubMed:9285411"
/id="VAR_067317"
MUTAGEN 533
/note="Y->F: Impairs receptor phosphorylation and abolishes
inhibition of serotonin release. No effect on PTPN6
binding; when associated with F-562."
/evidence="ECO:0000269|PubMed:11907092"
MUTAGEN 562
/note="Y->F: No effect on PTPN6 binding; when associated
with F-533."
/evidence="ECO:0000269|PubMed:11907092"
MUTAGEN 614
/note="Y->F: No effect on PTPN6 binding. Abolishes PTPN6
binding; when associated with F-644."
/evidence="ECO:0000269|PubMed:11907092"
MUTAGEN 644
/note="Y->F: Reduces PTPN6 binding. Abolishes PTPN6
binding; when associated with F-614."
/evidence="ECO:0000269|PubMed:11907092"
CONFLICT 557
/note="P -> L (in Ref. 6; AAL36989)"
/evidence="ECO:0000305"
STRAND 30..35
/evidence="ECO:0007744|PDB:1UGN"
STRAND 37..40
/evidence="ECO:0007744|PDB:1UGN"
STRAND 45..50
/evidence="ECO:0007744|PDB:1UGN"
STRAND 52..54
/evidence="ECO:0007744|PDB:1VDG"
STRAND 58..65
/evidence="ECO:0007744|PDB:1UGN"
HELIX 68..71
/evidence="ECO:0007744|PDB:1UGN"
HELIX 75..78
/evidence="ECO:0007744|PDB:1UGN"
TURN 79..81
/evidence="ECO:0007744|PDB:1UGN"
STRAND 82..87
/evidence="ECO:0007744|PDB:1UGN"
HELIX 90..92
/evidence="ECO:0007744|PDB:1UGN"
STRAND 94..102
/evidence="ECO:0007744|PDB:1UGN"
TURN 103..105
/evidence="ECO:0007744|PDB:1UGN"
STRAND 114..119
/evidence="ECO:0007744|PDB:1UGN"
STRAND 126..131
/evidence="ECO:0007744|PDB:1UGN"
STRAND 133..136
/evidence="ECO:0007744|PDB:1UGN"
STRAND 141..146
/evidence="ECO:0007744|PDB:1UGN"
STRAND 152..159
/evidence="ECO:0007744|PDB:1UGN"
STRAND 161..163
/evidence="ECO:0007744|PDB:6AEE"
STRAND 167..169
/evidence="ECO:0007744|PDB:1UGN"
HELIX 172..174
/evidence="ECO:0007744|PDB:1G0X"
STRAND 179..184
/evidence="ECO:0007744|PDB:1UGN"
STRAND 189..191
/evidence="ECO:0007744|PDB:6EWA"
STRAND 193..200
/evidence="ECO:0007744|PDB:1UGN"
STRAND 204..208
/evidence="ECO:0007744|PDB:3D2U"
STRAND 215..220
/evidence="ECO:0007744|PDB:1UGN"
STRAND 227..232
/evidence="ECO:0007744|PDB:4LL9"
STRAND 234..236
/evidence="ECO:0007744|PDB:4LL9"
STRAND 242..250
/evidence="ECO:0007744|PDB:4LL9"
STRAND 253..259
/evidence="ECO:0007744|PDB:4LL9"
STRAND 266..270
/evidence="ECO:0007744|PDB:4LL9"
STRAND 274..276
/evidence="ECO:0007744|PDB:6AEE"
STRAND 278..284
/evidence="ECO:0007744|PDB:4LL9"
HELIX 289..291
/evidence="ECO:0007744|PDB:4LL9"
STRAND 293..300
/evidence="ECO:0007744|PDB:4LL9"
STRAND 314..320
/evidence="ECO:0007744|PDB:4LL9"
STRAND 322..329
/evidence="ECO:0007744|PDB:4LL9"
STRAND 341..350
/evidence="ECO:0007744|PDB:4LL9"
STRAND 353..364
/evidence="ECO:0007744|PDB:4LL9"
STRAND 367..370
/evidence="ECO:0007744|PDB:4LL9"
STRAND 372..374
/evidence="ECO:0007744|PDB:6AEE"
STRAND 375..386
/evidence="ECO:0007744|PDB:4LL9"
HELIX 389..391
/evidence="ECO:0007744|PDB:4LL9"
STRAND 393..401
/evidence="ECO:0007744|PDB:4LL9"
STRAND 404..408
/evidence="ECO:0007744|PDB:4LL9"
SEQUENCE 650 AA; 70819 MW; 549196EA4ED2767C CRC64;
MTPILTVLIC LGLSLGPRTH VQAGHLPKPT LWAEPGSVIT QGSPVTLRCQ GGQETQEYRL
YREKKTALWI TRIPQELVKK GQFPIPSITW EHAGRYRCYY GSDTAGRSES SDPLELVVTG
AYIKPTLSAQ PSPVVNSGGN VILQCDSQVA FDGFSLCKEG EDEHPQCLNS QPHARGSSRA
IFSVGPVSPS RRWWYRCYAY DSNSPYEWSL PSDLLELLVL GVSKKPSLSV QPGPIVAPEE
TLTLQCGSDA GYNRFVLYKD GERDFLQLAG AQPQAGLSQA NFTLGPVSRS YGGQYRCYGA
HNLSSEWSAP SDPLDILIAG QFYDRVSLSV QPGPTVASGE NVTLLCQSQG WMQTFLLTKE
GAADDPWRLR STYQSQKYQA EFPMGPVTSA HAGTYRCYGS QSSKPYLLTH PSDPLELVVS
GPSGGPSSPT TGPTSTSGPE DQPLTPTGSD PQSGLGRHLG VVIGILVAVI LLLLLLLLLF
LILRHRRQGK HWTSTQRKAD FQHPAGAVGP EPTDRGLQWR SSPAADAQEE NLYAAVKHTQ
PEDGVEMDTR SPHDEDPQAV TYAEVKHSRP RREMASPPSP LSGEFLDTKD RQAEEDRQMD
TEAAASEAPQ DVTYAQLHSL TLRREATEPP PSQEGPSPAV PSIYATLAIH


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WP1004: Kit Receptor Signaling Pathway
WP407: Kit Receptor Signaling Pathway
WP1235: Signaling of Hepatocyte Growth Factor Receptor
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WP1284: EPO Receptor Signaling
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WP480: T Cell Receptor Signaling Pathway
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WP897: Androgen receptor signaling pathway
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WP193: Signaling of Hepatocyte Growth Factor Receptor
WP732: Serotonin Receptor 2 and ELK-SRF/GATA4 signaling
WP1161: TGF-beta Receptor Signaling Pathway
WP75: Toll-like receptor signaling pathway

Related Genes :
[LILRB1 ILT2 LIR1 MIR7] Leukocyte immunoglobulin-like receptor subfamily B member 1 (LIR-1) (Leukocyte immunoglobulin-like receptor 1) (CD85 antigen-like family member J) (Immunoglobulin-like transcript 2) (ILT-2) (Monocyte/macrophage immunoglobulin-like receptor 7) (MIR-7) (CD antigen CD85j)
[LILRB2 ILT4 LIR2 MIR10] Leukocyte immunoglobulin-like receptor subfamily B member 2 (LIR-2) (Leukocyte immunoglobulin-like receptor 2) (CD85 antigen-like family member D) (Immunoglobulin-like transcript 4) (ILT-4) (Monocyte/macrophage immunoglobulin-like receptor 10) (MIR-10) (CD antigen CD85d)
[LILRA2 ILT1 LIR7] Leukocyte immunoglobulin-like receptor subfamily A member 2 (CD85 antigen-like family member H) (Immunoglobulin-like transcript 1) (ILT-1) (Leukocyte immunoglobulin-like receptor 7) (LIR-7) (CD antigen CD85h)
[LILRA5 ILT11 LILRB7 LIR9] Leukocyte immunoglobulin-like receptor subfamily A member 5 (CD85 antigen-like family member F) (Immunoglobulin-like transcript 11) (ILT-11) (Leukocyte immunoglobulin-like receptor 9) (LIR-9) (CD antigen CD85f)
[LILRA3 ILT6 LIR4] Leukocyte immunoglobulin-like receptor subfamily A member 3 (CD85 antigen-like family member E) (Immunoglobulin-like transcript 6) (ILT-6) (Leukocyte immunoglobulin-like receptor 4) (LIR-4) (Monocyte inhibitory receptor HM43/HM31) (CD antigen CD85e)
[LILRA4 ILT7] Leukocyte immunoglobulin-like receptor subfamily A member 4 (CD85 antigen-like family member G) (Immunoglobulin-like transcript 7) (ILT-7) (CD antigen CD85g)
[Lilrb3 Pirb] Leukocyte immunoglobulin-like receptor subfamily B member 3 (LIR-3) (Leukocyte immunoglobulin-like receptor 3) (Cell-surface glycoprotein p91) (Paired immunoglobulin-like receptor B) (PIR-B)
[Cd300c2 Cd300c Clm4 Igsf7 Lmir2] CMRF-35-like molecule 4 (CLM-4) (CD300C molecule 2) (Dendritic cell-derived Ig-like receptor 1) (DIgR1) (Immunoglobulin superfamily member 7) (IgSF7) (Leukocyte mono-Ig-like receptor 2) (Myeloid-associated immunoglobulin-like receptor 2) (MAIR-2) (MAIR-II)
[Cd300lf Clm1 Lmir3] CMRF35-like molecule 1 (CLM-1) (CD300 antigen-like family member F) (Leukocyte mono-Ig-like receptor 3) (Myeloid-associated immunoglobulin-like receptor 5) (MAIR-5) (MAIR-V) (CD antigen CD300f)
[KIR2DS2 CD158J NKAT5] Killer cell immunoglobulin-like receptor 2DS2 (CD158 antigen-like family member J) (MHC class I NK cell receptor) (NK receptor 183 ActI) (Natural killer-associated transcript 5) (NKAT-5) (p58 natural killer cell receptor clone CL-49) (p58 NK receptor CL-49) (CD antigen CD158j)
[CD300LF CD300F CLM1 IGSF13 IREM1 NKIR UNQ3105/PRO10111] CMRF35-like molecule 1 (CLM-1) (CD300 antigen-like family member F) (Immune receptor expressed on myeloid cells 1) (IREM-1) (Immunoglobulin superfamily member 13) (IgSF13) (NK inhibitory receptor) (CD antigen CD300f)
[CD300A CMRF35H IGSF12 HSPC083] CMRF35-like molecule 8 (CLM-8) (CD300 antigen-like family member A) (CMRF-35-H9) (CMRF35-H9) (CMRF35-H) (IRC1/IRC2) (Immunoglobulin superfamily member 12) (IgSF12) (Inhibitory receptor protein 60) (IRp60) (NK inhibitory receptor) (CD antigen CD300a)
[KIR2DS1 CD158H] Killer cell immunoglobulin-like receptor 2DS1 (CD158 antigen-like family member H) (MHC class I NK cell receptor Eb6 ActI) (CD antigen CD158h)
[Fcgr2 Fcgr2b Ly-17] Low affinity immunoglobulin gamma Fc region receptor II (Fc gamma receptor IIB) (Fc-gamma RII) (Fc-gamma-RIIB) (FcRII) (IgG Fc receptor II beta) (Lymphocyte antigen 17) (Ly-17) (CD antigen CD32)
[SIRPA BIT MFR MYD1 PTPNS1 SHPS1 SIRP] Tyrosine-protein phosphatase non-receptor type substrate 1 (SHP substrate 1) (SHPS-1) (Brain Ig-like molecule with tyrosine-based activation motifs) (Bit) (CD172 antigen-like family member A) (Inhibitory receptor SHPS-1) (Macrophage fusion receptor) (MyD-1 antigen) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (Signal-regulatory protein alpha-2) (Sirp-alpha-2) (Signal-regulatory protein alpha-3) (Sirp-alpha-3) (p84) (CD antigen CD172a)
[KIR2DS5 CD158G NKAT9] Killer cell immunoglobulin-like receptor 2DS5 (CD158 antigen-like family member G) (MHC class I NK cell receptor) (Natural killer-associated transcript 9) (NKAT-9) (CD antigen CD158g)
[Cd79a Iga Mb-1] B-cell antigen receptor complex-associated protein alpha chain (Ig-alpha) (MB-1 membrane glycoprotein) (Membrane-bound immunoglobulin-associated protein) (Surface IgM-associated protein) (CD antigen CD79a)
[IGLL1 IGL1] Immunoglobulin lambda-like polypeptide 1 (CD179 antigen-like family member B) (Ig lambda-5) (Immunoglobulin omega polypeptide) (Immunoglobulin-related protein 14.1) (CD antigen CD179b)
[Cd79b Igb] B-cell antigen receptor complex-associated protein beta chain (B-cell-specific glycoprotein B29) (Ig-beta) (Immunoglobulin-associated B29 protein) (CD antigen CD79b)
[Havcr2 Tim3 Timd3] Hepatitis A virus cellular receptor 2 homolog (HAVcr-2) (T-cell immunoglobulin and mucin domain-containing protein 3) (TIMD-3) (T-cell immunoglobulin mucin receptor 3) (TIM-3) (T-cell membrane protein 3) (CD antigen CD366)
[CD84 SLAMF5] SLAM family member 5 (Cell surface antigen MAX.3) (Hly9-beta) (Leukocyte differentiation antigen CD84) (Signaling lymphocytic activation molecule 5) (CD antigen CD84)
[FCGR2B CD32 FCG2 IGFR2] Low affinity immunoglobulin gamma Fc region receptor II-b (IgG Fc receptor II-b) (CDw32) (Fc-gamma RII-b) (Fc-gamma-RIIb) (FcRII-b) (CD antigen CD32)
[Havcr2 Tim3 Timd3] Hepatitis A virus cellular receptor 2 homolog (HAVcr-2) (T-cell immunoglobulin and mucin domain-containing protein 3) (TIMD-3) (T-cell immunoglobulin mucin receptor 3) (TIM-3) (T-cell membrane protein 3) (CD antigen CD366)
[CD79A IGA MB1] B-cell antigen receptor complex-associated protein alpha chain (Ig-alpha) (MB-1 membrane glycoprotein) (Membrane-bound immunoglobulin-associated protein) (Surface IgM-associated protein) (CD antigen CD79a)
[Sirpa Bit Myd1 Ptpns1 Shps1 Sirp] Tyrosine-protein phosphatase non-receptor type substrate 1 (SHP substrate 1) (SHPS-1) (Brain Ig-like molecule with tyrosine-based activation motifs) (Bit) (CD172 antigen-like family member A) (Inhibitory receptor SHPS-1) (MyD-1 antigen) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (mSIRP-alpha1) (p84) (CD antigen CD172a)
[KIR3DS1 NKAT10] Killer cell immunoglobulin-like receptor 3DS1 (MHC class I NK cell receptor) (Natural killer-associated transcript 10) (NKAT-10)
[Ptprc Ly-5] Receptor-type tyrosine-protein phosphatase C (EC 3.1.3.48) (Leukocyte common antigen) (L-CA) (Lymphocyte antigen 5) (Ly-5) (T200) (CD antigen CD45)
[CXCR4] C-X-C chemokine receptor type 4 (CXC-R4) (CXCR-4) (FB22) (Fusin) (HM89) (LCR1) (Leukocyte-derived seven transmembrane domain receptor) (LESTR) (Lipopolysaccharide-associated protein 3) (LAP-3) (LPS-associated protein 3) (NPYRL) (Stromal cell-derived factor 1 receptor) (SDF-1 receptor) (CD antigen CD184)
[Sirpa Bit Mfr Ptpns1 Shps1 Sirp] Tyrosine-protein phosphatase non-receptor type substrate 1 (SHP substrate 1) (SHPS-1) (Brain Ig-like molecule with tyrosine-based activation motifs) (Bit) (CD172 antigen-like family member A) (Inhibitory receptor SHPS-1) (Macrophage fusion receptor) (Macrophage membrane protein MFP150) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (CD antigen CD172a)
[CD79B B29 IGB] B-cell antigen receptor complex-associated protein beta chain (B-cell-specific glycoprotein B29) (Ig-beta) (Immunoglobulin-associated B29 protein) (CD antigen CD79b)

Bibliography :