Q8NHL6 (LIRB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	650 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
Sequence similarities	Contains 4 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
Biological process	Adaptive immunity Immunity
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Fc 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 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 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 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 transcription from RNA polymerase II promoter Non-traceable author statement PubMed 18550825. Source: BHF-UCL receptor internalization Traceable author statement PubMed 17869268. Source: UniProtKB
Cellular_component	cytoplasm 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 to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	HLA-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 SH2 domain binding Inferred from direct assay Ref.10. 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Potential

Chain

24 – 650

627

Leukocyte immunoglobulin-like receptor subfamily B member 1

PRO_0000014820

Regions

Topological domain

24 – 461

438

Extracellular Potential

Transmembrane

462 – 482

21

Helical; Potential

Topological domain

483 – 650

168

Cytoplasmic Potential

Domain

27 – 115

89

Ig-like C2-type 1

Domain

116 – 221

106

Ig-like C2-type 2

Domain

222 – 312

91

Ig-like C2-type 3

Domain

313 – 409

97

Ig-like C2-type 4

Motif

531 – 536

6

ITIM motif 1

Motif

560 – 565

6

ITIM motif 2

Motif

612 – 617

6

ITIM motif 3

Motif

642 – 647

6

ITIM motif 4

Amino acid modifications

Modified residue

533

1

Phosphotyrosine

Modified residue

614

1

Phosphotyrosine

Modified residue

644

1

Phosphotyrosine

Glycosylation

281

1

N-linked (GlcNAc...) Potential

Glycosylation

302

1

N-linked (GlcNAc...) Potential

Glycosylation

341

1

N-linked (GlcNAc...) Potential

Disulfide bond

49 ↔ 98

Disulfide bond

145 ↔ 197

Disulfide bond

157 ↔ 167

Disulfide bond

246 ↔ 297

Potential

Disulfide bond

346 ↔ 397

Potential

Natural variations

Alternative sequence

437

1

S → SA in isoform 2 and isoform 3.

VSP_008456

Alternative sequence

550

1

R → RQ in isoform 3 and isoform 4.

VSP_008457

Natural variant

68

1

L → P. Ref.2 Ref.5 Ref.7
Corresponds to variant rs1061679 [ dbSNP | Ensembl ].

VAR_016993

Natural variant

93

1

A → T. Ref.5
Corresponds to variant rs12460501 [ dbSNP | Ensembl ].

VAR_049888

Natural variant

142

1

I → T. Ref.2 Ref.5 Ref.7
Corresponds to variant rs1061680 [ dbSNP | Ensembl ].

VAR_016994

Natural variant

155

1

S → I. Ref.2 Ref.5 Ref.7
Corresponds to variant rs1061681 [ dbSNP | Ensembl ].

VAR_016995

Natural variant

301

1

H → Y.
Corresponds to variant rs1045818 [ dbSNP | Ensembl ].

VAR_059398

Natural variant

459

1

L → V.
Corresponds to variant rs45511398 [ dbSNP | Ensembl ].

VAR_067316

Natural variant

620

1

L → F.
Corresponds to variant rs634222 [ dbSNP | Ensembl ].

VAR_016996

Natural variant

625

1

E → K. Ref.2 Ref.5 Ref.7
Corresponds to variant rs16985478 [ dbSNP | Ensembl ].

VAR_067317

Experimental info

Mutagenesis

533

1

Y → F: Impairs receptor phosphorylation and abolishes inhibition of serotonin release. No effect on PTPN6 binding; when associated with F-562. Ref.10

Mutagenesis

562

1

Y → F: No effect on PTPN6 binding; when associated with F-533. Ref.10

Mutagenesis

614

1

Y → F: No effect on PTPN6 binding. Abolishes PTPN6 binding; when associated with F-644. Ref.10

Mutagenesis

644

1

Y → F: Reduces PTPN6 binding. Abolishes PTPN6 binding; when associated with F-614. Ref.10

Sequence conflict

557

1

P → L in AAL36989. Ref.4

Secondary structure

1

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650

Helix Strand Turn

Details...

Beta strand

30 – 35

6

Beta strand

37 – 40

4

Beta strand

45 – 50

6

Beta strand

52 – 54

3

Beta strand

58 – 65

8

Helix

68 – 71

4

Helix

75 – 78

4

Turn

79 – 81

3

Beta strand

82 – 87

6

Helix

90 – 92

3

Beta strand

94 – 102

9

Turn

103 – 105

3

Beta strand

114 – 119

6

Beta strand

126 – 131

6

Beta strand

133 – 136

4

Beta strand

141 – 146

6

Beta strand

152 – 159

8

Beta strand

167 – 169

3

Helix

172 – 174

3

Beta strand

179 – 184

6

Beta strand

193 – 200

8

Beta strand

204 – 208

5

Beta strand

215 – 220

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 549196EA4ED2767C	FASTA	650	70,819
	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
	Isoform 2 [UniParc]. Checksum: 7D4F9D838D844AA6	FASTA	651	70,890
	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 TGPTSTSAGP EDQPLTPTGS DPQSGLGRHL GVVIGILVAV ILLLLLLLLL 490 500 510 520 530 540 FLILRHRRQG KHWTSTQRKA DFQHPAGAVG PEPTDRGLQW RSSPAADAQE ENLYAAVKHT 550 560 570 580 590 600 QPEDGVEMDT RSPHDEDPQA VTYAEVKHSR PRREMASPPS PLSGEFLDTK DRQAEEDRQM 610 620 630 640 650 DTEAAASEAP QDVTYAQLHS LTLRREATEP PPSQEGPSPA VPSIYATLAI H
	Isoform 3 [UniParc]. Checksum: 93AF8F021A22949D	FASTA	652	71,019
	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 TGPTSTSAGP EDQPLTPTGS DPQSGLGRHL GVVIGILVAV ILLLLLLLLL 490 500 510 520 530 540 FLILRHRRQG KHWTSTQRKA DFQHPAGAVG PEPTDRGLQW RSSPAADAQE ENLYAAVKHT 550 560 570 580 590 600 QPEDGVEMDT RQSPHDEDPQ AVTYAEVKHS RPRREMASPP SPLSGEFLDT KDRQAEEDRQ 610 620 630 640 650 MDTEAAASEA PQDVTYAQLH SLTLRREATE PPPSQEGPSP AVPSIYATLA IH
	Isoform 4 [UniParc]. Checksum: 3266510973E1C2A1	FASTA	651	70,948
	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 QSPHDEDPQA VTYAEVKHSR PRREMASPPS PLSGEFLDTK DRQAEEDRQM 610 620 630 640 650 DTEAAASEAP QDVTYAQLHS LTLRREATEP PPSQEGPSPA VPSIYATLAI H

References

	« Hide 'large scale' referencesShow '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. , 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: 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.

IPI

IPI00020967.
IPI00643313.
IPI00658078.
IPI00853070.

RefSeq

NP_001075106.1. NM_001081637.1.
NP_001075107.1. NM_001081638.1.
NP_001075108.1. NM_001081639.1.
NP_006660.3. NM_006669.3.

UniGene

Hs.667388.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G0X	X-ray	2.10	A	25-221	[»]
1P7Q	X-ray	3.40	D	25-221	[»]
1UFU	X-ray	3.00	A	25-221	[»]
1UGN	X-ray	1.80	A	24-221	[»]
1VDG	X-ray	2.80	A/B	24-220	[»]
3D2U	X-ray	2.21	D/H	24-221	[»]

ProteinModelPortal

Q8NHL6.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8NHL6. 2 interactions.

MINT

MINT-7144935.

STRING

9606.ENSP00000315997.

PTM databases

PhosphoSite

Q8NHL6.

Polymorphism databases

DMDM

37537910.

Proteomic databases

PaxDb

Q8NHL6.

PRIDE

Q8NHL6.

Protocols and materials databases

DNASU

10859.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000324602; ENSP00000315997; ENSG00000104972.
ENST00000396315; ENSP00000379608; ENSG00000104972.
ENST00000396321; ENSP00000379614; ENSG00000104972.
ENST00000396327; ENSP00000379618; ENSG00000104972.
ENST00000396331; ENSP00000379622; ENSG00000104972.
ENST00000396332; ENSP00000379623; ENSG00000104972.
ENST00000434867; ENSP00000405243; ENSG00000104972.
ENST00000572011; ENSP00000459938; ENSG00000262985.
ENST00000572228; ENSP00000461279; ENSG00000262985.
ENST00000572646; ENSP00000459516; ENSG00000262985.
ENST00000572972; ENSP00000460306; ENSG00000262985.
ENST00000573436; ENSP00000458421; ENSG00000262727.
ENST00000573974; ENSP00000458874; ENSG00000262985.
ENST00000573979; ENSP00000459643; ENSG00000262985.
ENST00000574258; ENSP00000461328; ENSG00000262727.
ENST00000575328; ENSP00000458881; ENSG00000262985.
ENST00000575581; ENSP00000459894; ENSG00000262727.

GeneID

10859.

KEGG

hsa:10859.

UCSC

uc002qgj.3. human.
uc002qgk.3. human.
uc002qgm.3. human.

Organism-specific databases

CTD

10859.

GeneCards

GC19P055085.

H-InvDB

HIX0137208.

HGNC

HGNC:6605. LILRB1.

MIM

604811. gene.

neXtProt

NX_Q8NHL6.

PharmGKB

PA30379.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG25855.

HOGENOM

HOG000234395.

HOVERGEN

HBG074353.

KO

K06512.

OrthoDB

EOG43R3MG.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q8NHL6.

Bgee

Q8NHL6.

CleanEx

HS_LILRB1.

Genevestigator

Q8NHL6.

GermOnline

ENSG00000104972. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 4 hits.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]

SMART

SM00409. IG. 3 hits.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

LILRB1. human.

EvolutionaryTrace

Q8NHL6.

GenomeRNAi

10859.

NextBio

41223.

SOURCE

Search...

Entry information

Entry name

LIRB1_HUMAN

Accession

Primary (citable) accession number: Q8NHL6
Secondary accession number(s): A2IXV4 , A8MXT0, O75024, O75025, Q8NHJ9, Q8NHK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.