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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.
25-OCT-2017, entry version 150.
RecName: Full=Leukocyte immunoglobulin-like receptor subfamily B member 1;
Short=LIR-1;
Short=Leukocyte immunoglobulin-like receptor 1;
AltName: Full=CD85 antigen-like family member J;
AltName: Full=Immunoglobulin-like transcript 2;
Short=ILT-2;
AltName: Full=Monocyte/macrophage immunoglobulin-like receptor 7;
Short=MIR-7;
AltName: CD_antigen=CD85j;
Flags: Precursor;
Name=LILRB1; Synonyms=ILT2, LIR1, 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]
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 and HLA-G alleles. 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 the signal triggered by FCER1A and inhibits
serotonin release. Inhibits FCGR1A-mediated phosphorylation of
cellular proteins and mobilization of intracellular calcium ions.
{ECO:0000269|PubMed:11907092, ECO:0000269|PubMed:9285411,
ECO:0000269|PubMed:9842885}.
-!- SUBUNIT: Binds PTPN6 when phosphorylated. Binds FCER1A and FCGR1A.
Interacts with human cytomegalovirus/HHV-5 protein UL18.
{ECO:0000269|PubMed:10591185, ECO:0000269|PubMed:11907092,
ECO:0000269|PubMed:9285411, ECO:0000269|PubMed:9842885}.
-!- INTERACTION:
P29350:PTPN6; NbExp=4; IntAct=EBI-2805262, EBI-78260;
-!- SUBCELLULAR LOCATION: Cell membrane {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;
Note=May act as dominant negative regulator and block the
interaction between membrane-associated isoforms and HLA-class
I. {ECO:0000269|PubMed:19658091};
-!- TISSUE SPECIFICITY: Expressed predominantly on B-cells and
monocytes, and at lower levels on dendritic cells. Detected on a
low percentage of T-cells and natural killer (NK) cells.
{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}.
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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.
UniGene; Hs.667388; -.
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.
PDBsum; 1G0X; -.
PDBsum; 1P7Q; -.
PDBsum; 1UFU; -.
PDBsum; 1UGN; -.
PDBsum; 1VDG; -.
PDBsum; 3D2U; -.
PDBsum; 4LL9; -.
PDBsum; 4NO0; -.
PDBsum; 5KNM; -.
ProteinModelPortal; Q8NHL6; -.
SMR; Q8NHL6; -.
BioGrid; 116070; 7.
IntAct; Q8NHL6; 9.
MINT; MINT-7144935; -.
STRING; 9606.ENSP00000315997; -.
iPTMnet; Q8NHL6; -.
PhosphoSitePlus; Q8NHL6; -.
BioMuta; LILRB1; -.
DMDM; 37537910; -.
PaxDb; Q8NHL6; -.
PeptideAtlas; Q8NHL6; -.
PRIDE; Q8NHL6; -.
DNASU; 10859; -.
Ensembl; ENST00000448689; ENSP00000409968; ENSG00000104972.
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; -.
H-InvDB; HIX0137208; -.
HGNC; HGNC:6605; LILRB1.
MIM; 604811; gene.
neXtProt; NX_Q8NHL6; -.
PharmGKB; PA30379; -.
eggNOG; ENOG410IKJD; Eukaryota.
eggNOG; ENOG41116BR; LUCA.
HOGENOM; HOG000234395; -.
HOVERGEN; HBG074353; -.
InParanoid; Q8NHL6; -.
KO; K06512; -.
OrthoDB; EOG091G0D6W; -.
PhylomeDB; Q8NHL6; -.
TreeFam; TF336644; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
SIGNOR; Q8NHL6; -.
ChiTaRS; LILRB1; human.
EvolutionaryTrace; Q8NHL6; -.
GeneWiki; LILRB1; -.
GenomeRNAi; 10859; -.
PRO; PR:Q8NHL6; -.
Proteomes; UP000005640; Chromosome 19.
CleanEx; HS_LILRB1; -.
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: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:0032609; P:interferon-gamma production; IDA:UniProtKB.
GO; GO:0072643; P:interferon-gamma secretion; IDA:UniProtKB.
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:0002740; P:negative regulation of cytokine secretion 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:0035548; P:negative regulation of interferon-beta secretion; IDA:UniProtKB.
GO; GO:0045077; P:negative regulation of interferon-gamma biosynthetic process; IDA:UniProtKB.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:2001180; P:negative regulation of interleukin-10 secretion; IDA:UniProtKB.
GO; GO:2001183; P:negative regulation of interleukin-12 secretion; 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:2001202; P:negative regulation of transforming growth factor-beta secretion; IDA:UniProtKB.
GO; GO:0042536; P:negative regulation of tumor necrosis factor biosynthetic process; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0045919; P:positive regulation of cytolysis; 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:0045944; P:positive regulation of transcription from RNA polymerase II promoter; 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; 1.20.5.100; -; 1.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
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;
Complete proteome; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 650 Leukocyte immunoglobulin-like receptor
subfamily B member 1.
/FTId=PRO_0000014820.
TOPO_DOM 24 461 Extracellular. {ECO:0000255}.
TRANSMEM 462 482 Helical. {ECO:0000255}.
TOPO_DOM 483 650 Cytoplasmic. {ECO:0000255}.
DOMAIN 27 115 Ig-like C2-type 1.
DOMAIN 116 221 Ig-like C2-type 2.
DOMAIN 222 312 Ig-like C2-type 3.
DOMAIN 313 409 Ig-like C2-type 4.
MOTIF 531 536 ITIM motif 1.
MOTIF 560 565 ITIM motif 2.
MOTIF 612 617 ITIM motif 3.
MOTIF 642 647 ITIM motif 4.
MOD_RES 533 533 Phosphotyrosine.
{ECO:0000305|PubMed:11907092}.
MOD_RES 614 614 Phosphotyrosine.
{ECO:0000305|PubMed:11907092}.
MOD_RES 644 644 Phosphotyrosine.
{ECO:0000305|PubMed:11907092}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 302 302 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 49 98 {ECO:0000244|PDB:1G0X,
ECO:0000269|PubMed:11114384}.
DISULFID 145 197 {ECO:0000244|PDB:1G0X,
ECO:0000269|PubMed:11114384}.
DISULFID 157 167 {ECO:0000244|PDB:1G0X,
ECO:0000269|PubMed:11114384}.
DISULFID 246 297 {ECO:0000244|PDB:1G0X,
ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:11114384}.
DISULFID 346 397 {ECO:0000244|PDB:1G0X,
ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:11114384}.
VAR_SEQ 437 437 S -> SA (in isoform 2, isoform 3 and
isoform 5). {ECO:0000303|PubMed:19658091,
ECO:0000303|PubMed:9285411}.
/FTId=VSP_008456.
VAR_SEQ 455 455 L -> E (in isoform 5).
{ECO:0000303|PubMed:19658091}.
/FTId=VSP_057087.
VAR_SEQ 456 650 Missing (in isoform 5).
{ECO:0000303|PubMed:19658091}.
/FTId=VSP_057088.
VAR_SEQ 550 550 R -> RQ (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:20600445,
ECO:0000303|PubMed:9259559,
ECO:0000303|PubMed:9285411}.
/FTId=VSP_008457.
VARIANT 68 68 L -> P (in dbSNP:rs1061679).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:19658091,
ECO:0000269|PubMed:20600445,
ECO:0000269|PubMed:9285411}.
/FTId=VAR_016993.
VARIANT 93 93 A -> T (in dbSNP:rs12460501).
{ECO:0000269|PubMed:19658091,
ECO:0000269|PubMed:20600445}.
/FTId=VAR_049888.
VARIANT 142 142 I -> T (in dbSNP:rs1061680).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:19658091,
ECO:0000269|PubMed:20600445,
ECO:0000269|PubMed:9285411}.
/FTId=VAR_016994.
VARIANT 155 155 S -> I (in dbSNP:rs1061681).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:19658091,
ECO:0000269|PubMed:20600445,
ECO:0000269|PubMed:9285411}.
/FTId=VAR_016995.
VARIANT 301 301 H -> Y (in dbSNP:rs1045818).
/FTId=VAR_059398.
VARIANT 459 459 L -> V (in dbSNP:rs45511398).
/FTId=VAR_067316.
VARIANT 620 620 L -> F (in dbSNP:rs634222).
/FTId=VAR_016996.
VARIANT 625 625 E -> K (in dbSNP:rs16985478).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:20600445,
ECO:0000269|PubMed:9285411}.
/FTId=VAR_067317.
MUTAGEN 533 533 Y->F: Impairs receptor phosphorylation
and abolishes inhibition of serotonin
release. No effect on PTPN6 binding; when
associated with F-562.
{ECO:0000269|PubMed:11907092}.
MUTAGEN 562 562 Y->F: No effect on PTPN6 binding; when
associated with F-533.
{ECO:0000269|PubMed:11907092}.
MUTAGEN 614 614 Y->F: No effect on PTPN6 binding.
Abolishes PTPN6 binding; when associated
with F-644.
{ECO:0000269|PubMed:11907092}.
MUTAGEN 644 644 Y->F: Reduces PTPN6 binding. Abolishes
PTPN6 binding; when associated with F-
614. {ECO:0000269|PubMed:11907092}.
CONFLICT 557 557 P -> L (in Ref. 6; AAL36989).
{ECO:0000305}.
STRAND 30 35 {ECO:0000244|PDB:1UGN}.
STRAND 37 40 {ECO:0000244|PDB:1UGN}.
STRAND 45 50 {ECO:0000244|PDB:1UGN}.
STRAND 52 54 {ECO:0000244|PDB:1VDG}.
STRAND 58 65 {ECO:0000244|PDB:1UGN}.
HELIX 68 71 {ECO:0000244|PDB:1UGN}.
HELIX 75 78 {ECO:0000244|PDB:1UGN}.
TURN 79 81 {ECO:0000244|PDB:1UGN}.
STRAND 82 87 {ECO:0000244|PDB:1UGN}.
HELIX 90 92 {ECO:0000244|PDB:1UGN}.
STRAND 94 102 {ECO:0000244|PDB:1UGN}.
TURN 103 105 {ECO:0000244|PDB:1UGN}.
STRAND 114 119 {ECO:0000244|PDB:1UGN}.
STRAND 126 131 {ECO:0000244|PDB:1UGN}.
STRAND 133 136 {ECO:0000244|PDB:1UGN}.
STRAND 141 146 {ECO:0000244|PDB:1UGN}.
STRAND 152 159 {ECO:0000244|PDB:1UGN}.
STRAND 167 169 {ECO:0000244|PDB:1UGN}.
HELIX 172 174 {ECO:0000244|PDB:1G0X}.
STRAND 179 184 {ECO:0000244|PDB:1UGN}.
STRAND 193 200 {ECO:0000244|PDB:1UGN}.
STRAND 204 208 {ECO:0000244|PDB:3D2U}.
STRAND 215 220 {ECO:0000244|PDB:1UGN}.
STRAND 227 232 {ECO:0000244|PDB:4LL9}.
STRAND 234 236 {ECO:0000244|PDB:4LL9}.
STRAND 242 250 {ECO:0000244|PDB:4LL9}.
STRAND 253 259 {ECO:0000244|PDB:4LL9}.
STRAND 266 270 {ECO:0000244|PDB:4LL9}.
STRAND 278 284 {ECO:0000244|PDB:4LL9}.
HELIX 289 291 {ECO:0000244|PDB:4LL9}.
STRAND 293 300 {ECO:0000244|PDB:4LL9}.
STRAND 314 320 {ECO:0000244|PDB:4LL9}.
STRAND 322 329 {ECO:0000244|PDB:4LL9}.
STRAND 341 350 {ECO:0000244|PDB:4LL9}.
STRAND 353 364 {ECO:0000244|PDB:4LL9}.
STRAND 367 370 {ECO:0000244|PDB:4LL9}.
STRAND 375 386 {ECO:0000244|PDB:4LL9}.
HELIX 389 391 {ECO:0000244|PDB:4LL9}.
STRAND 393 401 {ECO:0000244|PDB:4LL9}.
STRAND 404 408 {ECO:0000244|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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