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Q8NHL6 (LIRB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leukocyte immunoglobulin-like receptor subfamily B member 1

Short name=LIR-1
Short name=Leukocyte immunoglobulin-like receptor 1
Alternative name(s):
CD85 antigen-like family member J
Immunoglobulin-like transcript 2
Short name=ILT-2
Monocyte/macrophage immunoglobulin-like receptor 7
Short name=MIR-7
CD_antigen=CD85j
Gene names
Name:LILRB1
Synonyms:ILT2, LIR1, MIR7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length650 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2 Ref.8 Ref.10

Subunit structure

Binds PTPN6 when phosphorylated. Binds FCER1A and FCGR1A. Interacts with human cytomegalovirus/HHV-5 protein UL18. Ref.2 Ref.8 Ref.9 Ref.10

Subcellular location

Membrane; Single-pass type I membrane protein.

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. Ref.2 Ref.8

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.

Post-translational modification

Phosphorylated on tyrosine residues. Dephosphorylated by PTPN6. Ref.2 Ref.8 Ref.10

Sequence similarities

Contains 4 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
   Biological processAdaptive immunity
Immunity
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc receptor mediated inhibitory signaling pathway

Inferred from direct assay Ref.8. Source: UniProtKB

T cell proliferation involved in immune response

Inferred from direct assay PubMed 18094328. Source: UniProtKB

cellular response to lipopolysaccharide

Inferred from expression pattern PubMed 18094328. Source: UniProtKB

defense response to virus

Inferred from direct assay PubMed 15585844. Source: UniProtKB

dendritic cell differentiation

Inferred from expression pattern PubMed 18094328. Source: UniProtKB

immune response-inhibiting cell surface receptor signaling pathway

Non-traceable author statement PubMed 18550825. Source: BHF-UCL

interferon-gamma production

Inferred from direct assay Ref.10. Source: UniProtKB

interferon-gamma secretion

Inferred from direct assay PubMed 15585844. Source: UniProtKB

negative regulation of CD8-positive, alpha-beta T cell activation

Inferred from direct assay PubMed 21213105. Source: UniProtKB

negative regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell

Inferred from direct assay PubMed 18094328. Source: UniProtKB

negative regulation of T cell mediated cytotoxicity

Inferred from direct assay PubMed 21213105. Source: UniProtKB

negative regulation of T cell proliferation

Inferred from direct assay PubMed 15585844. Source: UniProtKB

negative regulation of alpha-beta T cell activation

Inferred from direct assay PubMed 21213105. Source: UniProtKB

negative regulation of calcium ion transport

Inferred from direct assay Ref.8. Source: UniProtKB

negative regulation of cell cycle

Inferred from direct assay PubMed 21551166. Source: UniProtKB

negative regulation of cytokine secretion involved in immune response

Inferred from direct assay PubMed 18094328. Source: UniProtKB

negative regulation of dendritic cell apoptotic process

Inferred from direct assay PubMed 18094328. Source: UniProtKB

negative regulation of dendritic cell differentiation

Inferred from mutant phenotype PubMed 18684926. Source: UniProtKB

negative regulation of endocytosis

Inferred from direct assay PubMed 18094328. Source: UniProtKB

negative regulation of interferon-beta secretion

Inferred from direct assay PubMed 21213105. Source: UniProtKB

negative regulation of interferon-gamma biosynthetic process

Inferred from direct assay PubMed 18684926. Source: UniProtKB

negative regulation of interferon-gamma production

Inferred from direct assay PubMed 17869268. Source: UniProtKB

negative regulation of interleukin-10 secretion

Inferred from direct assay PubMed 18094328. Source: UniProtKB

negative regulation of interleukin-12 secretion

Inferred from direct assay PubMed 18094328. Source: UniProtKB

negative regulation of mononuclear cell proliferation

Inferred from direct assay PubMed 21551166. Source: UniProtKB

negative regulation of natural killer cell mediated cytotoxicity

Inferred from direct assay PubMed 18398485. Source: UniProtKB

negative regulation of osteoclast development

Inferred from direct assay PubMed 18802077. Source: UniProtKB

negative regulation of serotonin secretion

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of transforming growth factor-beta secretion

Inferred from direct assay PubMed 18094328. Source: UniProtKB

negative regulation of tumor necrosis factor biosynthetic process

Inferred from direct assay PubMed 18684926. Source: UniProtKB

positive regulation of apoptotic process

Inferred from direct assay PubMed 21551166. Source: UniProtKB

positive regulation of cytolysis

Inferred from direct assay PubMed 18684926. Source: UniProtKB

positive regulation of defense response to virus by host

Inferred from direct assay PubMed 18398485. Source: UniProtKB

positive regulation of gamma-delta T cell activation involved in immune response

Inferred from direct assay PubMed 21233315. Source: UniProtKB

positive regulation of gene expression

Inferred from direct assay PubMed 18094328. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Non-traceable author statement PubMed 18550825. Source: BHF-UCL

receptor internalization

Traceable author statement PubMed 17869268. Source: UniProtKB

regulation of immune response

Traceable author statement. Source: Reactome

response to virus

Inferred from direct assay PubMed 17869268PubMed 18094328Ref.2. Source: UniProtKB

signal transduction

Inferred from direct assay PubMed 18802077. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15585844. Source: UniProtKB

external side of plasma membrane

Inferred from direct assay PubMed 15585844PubMed 17869268PubMed 18094328PubMed 18684926PubMed 21233315PubMed 21551166Ref.2. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionHLA-A specific inhibitory MHC class I receptor activity

Inferred from direct assay PubMed 18684926. Source: UniProtKB

HLA-B specific inhibitory MHC class I receptor activity

Inferred from direct assay Ref.10. Source: UniProtKB

MHC class I protein binding

Inferred from direct assay PubMed 18094328PubMed 18802077PubMed 21213105Ref.8. Source: UniProtKB

MHC class I receptor activity

Inferred from direct assay PubMed 17869268PubMed 18094328PubMed 18398485PubMed 18802077PubMed 21213105PubMed 21233315Ref.2Ref.8. Source: UniProtKB

SH2 domain binding

Inferred from direct assay Ref.10. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction PubMed 21213105. Source: UniProtKB

protein phosphatase 1 binding

Inferred from physical interaction Ref.10PubMed 18802077Ref.2Ref.8. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NHL6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8NHL6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     437-437: S → SA
Isoform 3 (identifier: Q8NHL6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     437-437: S → SA
     550-550: R → RQ
Isoform 4 (identifier: Q8NHL6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     550-550: R → RQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 650627Leukocyte immunoglobulin-like receptor subfamily B member 1
PRO_0000014820

Regions

Topological domain24 – 461438Extracellular Potential
Transmembrane462 – 48221Helical; Potential
Topological domain483 – 650168Cytoplasmic Potential
Domain27 – 11589Ig-like C2-type 1
Domain116 – 221106Ig-like C2-type 2
Domain222 – 31291Ig-like C2-type 3
Domain313 – 40997Ig-like C2-type 4
Motif531 – 5366ITIM motif 1
Motif560 – 5656ITIM motif 2
Motif612 – 6176ITIM motif 3
Motif642 – 6476ITIM motif 4

Amino acid modifications

Modified residue5331Phosphotyrosine Probable
Modified residue6141Phosphotyrosine Probable
Modified residue6441Phosphotyrosine Probable
Glycosylation2811N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Potential
Glycosylation3411N-linked (GlcNAc...) Potential
Disulfide bond49 ↔ 98
Disulfide bond145 ↔ 197
Disulfide bond157 ↔ 167
Disulfide bond246 ↔ 297 Potential
Disulfide bond346 ↔ 397 Potential

Natural variations

Alternative sequence4371S → SA in isoform 2 and isoform 3.
VSP_008456
Alternative sequence5501R → RQ in isoform 3 and isoform 4.
VSP_008457
Natural variant681L → P. Ref.2 Ref.5 Ref.7
Corresponds to variant rs1061679 [ dbSNP | Ensembl ].
VAR_016993
Natural variant931A → T. Ref.5
Corresponds to variant rs12460501 [ dbSNP | Ensembl ].
VAR_049888
Natural variant1421I → T. Ref.2 Ref.5 Ref.7
Corresponds to variant rs1061680 [ dbSNP | Ensembl ].
VAR_016994
Natural variant1551S → I. Ref.2 Ref.5 Ref.7
Corresponds to variant rs1061681 [ dbSNP | Ensembl ].
VAR_016995
Natural variant3011H → Y.
Corresponds to variant rs1045818 [ dbSNP | Ensembl ].
VAR_059398
Natural variant4591L → V.
Corresponds to variant rs45511398 [ dbSNP | Ensembl ].
VAR_067316
Natural variant6201L → F.
Corresponds to variant rs634222 [ dbSNP | Ensembl ].
VAR_016996
Natural variant6251E → K. Ref.2 Ref.5 Ref.7
Corresponds to variant rs16985478 [ dbSNP | Ensembl ].
VAR_067317

Experimental info

Mutagenesis5331Y → F: Impairs receptor phosphorylation and abolishes inhibition of serotonin release. No effect on PTPN6 binding; when associated with F-562. Ref.10
Mutagenesis5621Y → F: No effect on PTPN6 binding; when associated with F-533. Ref.10
Mutagenesis6141Y → F: No effect on PTPN6 binding. Abolishes PTPN6 binding; when associated with F-644. Ref.10
Mutagenesis6441Y → F: Reduces PTPN6 binding. Abolishes PTPN6 binding; when associated with F-614. Ref.10
Sequence conflict5571P → L in AAL36989. Ref.4

Secondary structure

.............................................................................. 650
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 549196EA4ED2767C

FASTA65070,819
        10         20         30         40         50         60 
MTPILTVLIC LGLSLGPRTH VQAGHLPKPT LWAEPGSVIT QGSPVTLRCQ GGQETQEYRL 

        70         80         90        100        110        120 
YREKKTALWI TRIPQELVKK GQFPIPSITW EHAGRYRCYY GSDTAGRSES SDPLELVVTG 

       130        140        150        160        170        180 
AYIKPTLSAQ PSPVVNSGGN VILQCDSQVA FDGFSLCKEG EDEHPQCLNS QPHARGSSRA 

       190        200        210        220        230        240 
IFSVGPVSPS RRWWYRCYAY DSNSPYEWSL PSDLLELLVL GVSKKPSLSV QPGPIVAPEE 

       250        260        270        280        290        300 
TLTLQCGSDA GYNRFVLYKD GERDFLQLAG AQPQAGLSQA NFTLGPVSRS YGGQYRCYGA 

       310        320        330        340        350        360 
HNLSSEWSAP SDPLDILIAG QFYDRVSLSV QPGPTVASGE NVTLLCQSQG WMQTFLLTKE 

       370        380        390        400        410        420 
GAADDPWRLR STYQSQKYQA EFPMGPVTSA HAGTYRCYGS QSSKPYLLTH PSDPLELVVS 

       430        440        450        460        470        480 
GPSGGPSSPT TGPTSTSGPE DQPLTPTGSD PQSGLGRHLG VVIGILVAVI LLLLLLLLLF 

       490        500        510        520        530        540 
LILRHRRQGK HWTSTQRKAD FQHPAGAVGP EPTDRGLQWR SSPAADAQEE NLYAAVKHTQ 

       550        560        570        580        590        600 
PEDGVEMDTR SPHDEDPQAV TYAEVKHSRP RREMASPPSP LSGEFLDTKD RQAEEDRQMD 

       610        620        630        640        650 
TEAAASEAPQ DVTYAQLHSL TLRREATEPP PSQEGPSPAV PSIYATLAIH 

« Hide

Isoform 2 [UniParc].

Checksum: 7D4F9D838D844AA6
Show »

FASTA65170,890
Isoform 3 [UniParc].

Checksum: 93AF8F021A22949D
Show »

FASTA65271,019
Isoform 4 [UniParc].

Checksum: 3266510973E1C2A1
Show »

FASTA65170,948

References

« Hide 'large scale' references
[1]"A new human gene complex encoding the killer cell inhibitory receptors and related monocyte/macrophage receptors."
Wagtmann N., Rojo S., Eichler E., Mohrenweiser H., Long E.O.
Curr. Biol. 7:615-618(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[2]"A novel immunoglobulin superfamily receptor for cellular and viral MHC class I molecules."
Cosman D., Fanger N., Borges L., Kubin M., Chin W., Peterson L., Hsu M.-L.
Immunity 7:273-282(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, FUNCTION.
Tissue: Lymphoblast.
[3]"Genomic organization of the human leukocyte immunoglobulin-like receptors within the leukocyte receptor complex on chromosome 19q13.4."
Liu W.R., Kim J., Nwankwo C., Ashworth L.K., Arm J.P.
Immunogenetics 51:659-669(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]Canavez F.C.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2).
[5]"LILRB1 polymorphism and surface phenotypes of natural killer cells."
Davidson C.L., Li N.L., Burshtyn D.N.
Hum. Immunol. 71:942-949(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANTS PRO-68; THR-93; THR-142; ILE-155 AND LYS-625.
[6]"The DNA sequence and biology of human chromosome 19."
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. expand/collapse author list , 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.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS PRO-68; THR-142; ILE-155 AND LYS-625.
Tissue: B-cell.
[8]"The MHC class I binding proteins LIR-1 and LIR-2 inhibit Fc receptor-mediated signaling in monocytes."
Fanger N.A., Cosman D., Peterson L., Braddy S.C., Maliszewski C.R., Borges L.
Eur. J. Immunol. 28:3423-3434(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPN6 AND FCGR1A, PHOSPHORYLATION, TISSUE SPECIFICITY, FUNCTION.
[9]"The inhibitory receptor LIR-1 uses a common binding interaction to recognize class I MHC molecules and the viral homolog UL18."
Chapman T.L., Heikeman A.P., Bjorkman P.J.
Immunity 11:603-613(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-5 PROTEIN UL18.
[10]"Mutational analysis of immunoreceptor tyrosine-based inhibition motifs of the Ig-like transcript 2 (CD85j) leukocyte receptor."
Bellon T., Kitzig F., Sayos J., Lopez-Botet M.
J. Immunol. 168:3351-3359(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-533; TYR-614 AND TYR-644, MUTAGENESIS OF TYR-533; TYR-562; TYR-614 AND TYR-644, INTERACTION WITH FCER1A, FUNCTION.
[11]"Crystal structure and ligand binding properties of the D1D2 region of the inhibitory receptor LIR-1 (ILT2)."
Chapman T.L., Heikema A.P., West A.P. Jr., Bjorkman P.J.
Immunity 13:727-736(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-221.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF004230 mRNA. Translation: AAB67710.1.
AF009220 mRNA. Translation: AAB63521.1.
AF009221 mRNA. Translation: AAB63522.1.
AF189277 Genomic DNA. Translation: AAG08984.1.
AF283984 mRNA. Translation: AAL36988.1.
AF283985 mRNA. Translation: AAL36989.1.
HM135394 Genomic DNA. Translation: ADJ55944.1.
HM135401 Genomic DNA. Translation: ADJ55951.1.
AC009892 Genomic DNA. No translation available.
BC015731 mRNA. Translation: AAH15731.1.
RefSeqNP_001075106.2. NM_001081637.2.
NP_001075107.2. NM_001081638.3.
NP_001075108.2. NM_001081639.3.
NP_001265327.2. NM_001278398.2.
NP_006660.4. NM_006669.6.
UniGeneHs.667388.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G0XX-ray2.10A25-221[»]
1P7QX-ray3.40D25-221[»]
1UFUX-ray3.00A25-221[»]
1UGNX-ray1.80A24-221[»]
1VDGX-ray2.80A/B24-220[»]
3D2UX-ray2.21D/H24-221[»]
4LL9X-ray2.69A/B/C222-417[»]
ProteinModelPortalQ8NHL6.
SMRQ8NHL6. Positions 25-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116070. 6 interactions.
IntActQ8NHL6. 4 interactions.
MINTMINT-7144935.
STRING9606.ENSP00000315997.

PTM databases

PhosphoSiteQ8NHL6.

Polymorphism databases

DMDM37537910.

Proteomic databases

PaxDbQ8NHL6.
PRIDEQ8NHL6.

Protocols and materials databases

DNASU10859.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324602; ENSP00000315997; ENSG00000104972. [Q8NHL6-3]
ENST00000396315; ENSP00000379608; ENSG00000104972. [Q8NHL6-3]
ENST00000396321; ENSP00000379614; ENSG00000104972. [Q8NHL6-1]
ENST00000396327; ENSP00000379618; ENSG00000104972. [Q8NHL6-2]
ENST00000396331; ENSP00000379622; ENSG00000104972. [Q8NHL6-1]
ENST00000396332; ENSP00000379623; ENSG00000104972. [Q8NHL6-4]
ENST00000434867; ENSP00000405243; ENSG00000104972. [Q8NHL6-1]
ENST00000572011; ENSP00000459938; ENSG00000262985. [Q8NHL6-3]
ENST00000572228; ENSP00000461279; ENSG00000262985. [Q8NHL6-4]
ENST00000572646; ENSP00000459516; ENSG00000262985. [Q8NHL6-1]
ENST00000572972; ENSP00000460306; ENSG00000262985. [Q8NHL6-3]
ENST00000573436; ENSP00000458421; ENSG00000262727.
ENST00000573974; ENSP00000458874; ENSG00000262985. [Q8NHL6-1]
ENST00000573979; ENSP00000459643; ENSG00000262985. [Q8NHL6-2]
ENST00000574258; ENSP00000461328; ENSG00000262727.
ENST00000575328; ENSP00000458881; ENSG00000262985. [Q8NHL6-1]
ENST00000575581; ENSP00000459894; ENSG00000262727.
GeneID10859.
KEGGhsa:10859.
UCSCuc002qgj.3. human. [Q8NHL6-1]
uc002qgk.3. human. [Q8NHL6-2]
uc002qgl.3. human. [Q8NHL6-4]
uc002qgm.3. human. [Q8NHL6-3]

Organism-specific databases

CTD10859.
GeneCardsGC19P055085.
H-InvDBHIX0137208.
HGNCHGNC:6605. LILRB1.
MIM604811. gene.
neXtProtNX_Q8NHL6.
PharmGKBPA30379.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG25855.
HOGENOMHOG000234395.
HOVERGENHBG074353.
KOK06512.
PhylomeDBQ8NHL6.
TreeFamTF336644.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ8NHL6.
BgeeQ8NHL6.
CleanExHS_LILRB1.
GenevestigatorQ8NHL6.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTSM00409. IG. 3 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLILRB1. human.
EvolutionaryTraceQ8NHL6.
GeneWikiLILRB1.
GenomeRNAi10859.
NextBio41223.
PROQ8NHL6.
SOURCESearch...

Entry information

Entry nameLIRB1_HUMAN
AccessionPrimary (citable) accession number: Q8NHL6
Secondary accession number(s): A2IXV4 expand/collapse secondary AC list , A8MXT0, O75024, O75025, Q8NHJ9, Q8NHK0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries