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Protein

Leukocyte immunoglobulin-like receptor subfamily B member 1

Gene

LILRB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  • HLA-A specific inhibitory MHC class I receptor activity Source: UniProtKB
  • HLA-B specific inhibitory MHC class I receptor activity Source: UniProtKB
  • MHC class I protein binding Source: UniProtKB
  • MHC class I receptor activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein phosphatase 1 binding Source: UniProtKB
  • SH2 domain binding Source: UniProtKB

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • cellular response to lipopolysaccharide Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • dendritic cell differentiation Source: UniProtKB
  • Fc receptor mediated inhibitory signaling pathway Source: UniProtKB
  • immune response-inhibiting cell surface receptor signaling pathway Source: BHF-UCL
  • interferon-gamma production Source: UniProtKB
  • interferon-gamma secretion Source: UniProtKB
  • negative regulation of alpha-beta T cell activation Source: UniProtKB
  • negative regulation of calcium ion transport Source: UniProtKB
  • negative regulation of CD8-positive, alpha-beta T cell activation Source: UniProtKB
  • negative regulation of cell cycle Source: UniProtKB
  • negative regulation of cytokine secretion involved in immune response Source: UniProtKB
  • negative regulation of dendritic cell apoptotic process Source: UniProtKB
  • negative regulation of dendritic cell differentiation Source: UniProtKB
  • negative regulation of endocytosis Source: UniProtKB
  • negative regulation of interferon-beta secretion Source: UniProtKB
  • negative regulation of interferon-gamma biosynthetic process Source: UniProtKB
  • negative regulation of interferon-gamma production Source: UniProtKB
  • negative regulation of interleukin-10 secretion Source: UniProtKB
  • negative regulation of interleukin-12 secretion Source: UniProtKB
  • negative regulation of mononuclear cell proliferation Source: UniProtKB
  • negative regulation of natural killer cell mediated cytotoxicity Source: UniProtKB
  • negative regulation of osteoclast development Source: UniProtKB
  • negative regulation of serotonin secretion Source: UniProtKB
  • negative regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell Source: UniProtKB
  • negative regulation of T cell mediated cytotoxicity Source: UniProtKB
  • negative regulation of T cell proliferation Source: UniProtKB
  • negative regulation of transforming growth factor-beta secretion Source: UniProtKB
  • negative regulation of tumor necrosis factor biosynthetic process Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of cytolysis Source: UniProtKB
  • positive regulation of defense response to virus by host Source: UniProtKB
  • positive regulation of gamma-delta T cell activation involved in immune response Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • receptor internalization Source: UniProtKB
  • regulation of immune response Source: Reactome
  • response to virus Source: UniProtKB
  • signal transduction Source: UniProtKB
  • T cell proliferation involved in immune response Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Adaptive immunity, Immunity

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104972-MONOMER.
ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
SIGNORiQ8NHL6.

Protein family/group databases

MEROPSiI43.951.

Names & Taxonomyi

Protein namesi
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 namesi
Name:LILRB1
Synonyms:ILT2, LIR1, MIR7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:6605. LILRB1.

Subcellular locationi

Isoform 5 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini24 – 461ExtracellularSequence analysisAdd BLAST438
Transmembranei462 – 482HelicalSequence analysisAdd BLAST21
Topological domaini483 – 650CytoplasmicSequence analysisAdd BLAST168

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • external side of plasma membrane Source: UniProtKB
  • extracellular region Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi533Y → F: Impairs receptor phosphorylation and abolishes inhibition of serotonin release. No effect on PTPN6 binding; when associated with F-562. 1 Publication1
Mutagenesisi562Y → F: No effect on PTPN6 binding; when associated with F-533. 1 Publication1
Mutagenesisi614Y → F: No effect on PTPN6 binding. Abolishes PTPN6 binding; when associated with F-644. 1 Publication1
Mutagenesisi644Y → F: Reduces PTPN6 binding. Abolishes PTPN6 binding; when associated with F-614. 1 Publication1

Organism-specific databases

DisGeNETi10859.
OpenTargetsiENSG00000277807.
PharmGKBiPA30379.

Polymorphism and mutation databases

BioMutaiLILRB1.
DMDMi37537910.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000001482024 – 650Leukocyte immunoglobulin-like receptor subfamily B member 1Add BLAST627

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi49 ↔ 98Combined sources1 Publication
Disulfide bondi145 ↔ 197Combined sources1 Publication
Disulfide bondi157 ↔ 167Combined sources1 Publication
Disulfide bondi246 ↔ 297PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi281N-linked (GlcNAc...)Sequence analysis1
Glycosylationi302N-linked (GlcNAc...)Sequence analysis1
Glycosylationi341N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi346 ↔ 397PROSITE-ProRule annotationCombined sources1 Publication
Modified residuei533Phosphotyrosine1 Publication1
Modified residuei614Phosphotyrosine1 Publication1
Modified residuei644Phosphotyrosine1 Publication1

Post-translational modificationi

Phosphorylated on tyrosine residues. Dephosphorylated by PTPN6.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ8NHL6.
PeptideAtlasiQ8NHL6.
PRIDEiQ8NHL6.

PTM databases

iPTMnetiQ8NHL6.
PhosphoSitePlusiQ8NHL6.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiENSG00000104972.
CleanExiHS_LILRB1.

Interactioni

Subunit structurei

Binds PTPN6 when phosphorylated. Binds FCER1A and FCGR1A. Interacts with human cytomegalovirus/HHV-5 protein UL18.4 Publications

GO - Molecular functioni

  • MHC class I protein binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein phosphatase 1 binding Source: UniProtKB
  • SH2 domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116070. 7 interactors.
IntActiQ8NHL6. 4 interactors.
MINTiMINT-7144935.
STRINGi9606.ENSP00000315997.

Structurei

Secondary structure

1650
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 35Combined sources6
Beta strandi37 – 40Combined sources4
Beta strandi45 – 50Combined sources6
Beta strandi52 – 54Combined sources3
Beta strandi58 – 65Combined sources8
Helixi68 – 71Combined sources4
Helixi75 – 78Combined sources4
Turni79 – 81Combined sources3
Beta strandi82 – 87Combined sources6
Helixi90 – 92Combined sources3
Beta strandi94 – 102Combined sources9
Turni103 – 105Combined sources3
Beta strandi114 – 119Combined sources6
Beta strandi126 – 131Combined sources6
Beta strandi133 – 136Combined sources4
Beta strandi141 – 146Combined sources6
Beta strandi152 – 159Combined sources8
Beta strandi167 – 169Combined sources3
Helixi172 – 174Combined sources3
Beta strandi179 – 184Combined sources6
Beta strandi193 – 200Combined sources8
Beta strandi204 – 208Combined sources5
Beta strandi215 – 220Combined sources6
Beta strandi227 – 232Combined sources6
Beta strandi234 – 236Combined sources3
Beta strandi242 – 250Combined sources9
Beta strandi253 – 259Combined sources7
Beta strandi266 – 270Combined sources5
Beta strandi278 – 284Combined sources7
Helixi289 – 291Combined sources3
Beta strandi293 – 300Combined sources8
Beta strandi314 – 320Combined sources7
Beta strandi322 – 329Combined sources8
Beta strandi341 – 350Combined sources10
Beta strandi353 – 364Combined sources12
Beta strandi367 – 370Combined sources4
Beta strandi375 – 386Combined sources12
Helixi389 – 391Combined sources3
Beta strandi393 – 401Combined sources9
Beta strandi404 – 408Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4NO0X-ray2.70D27-221[»]
ProteinModelPortaliQ8NHL6.
SMRiQ8NHL6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NHL6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 115Ig-like C2-type 1Add BLAST89
Domaini116 – 221Ig-like C2-type 2Add BLAST106
Domaini222 – 312Ig-like C2-type 3Add BLAST91
Domaini313 – 409Ig-like C2-type 4Add BLAST97

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi531 – 536ITIM motif 16
Motifi560 – 565ITIM motif 26
Motifi612 – 617ITIM motif 36
Motifi642 – 647ITIM motif 46

Domaini

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IKJD. Eukaryota.
ENOG41116BR. LUCA.
HOGENOMiHOG000234395.
HOVERGENiHBG074353.
InParanoidiQ8NHL6.
KOiK06512.
OMAiQAVTHAP.
OrthoDBiEOG091G0D6W.
PhylomeDBiQ8NHL6.
TreeFamiTF336644.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF13895. Ig_2. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 4 hits.
SM00408. IGc2. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8NHL6-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTPILTVLIC LGLSLGPRTH VQAGHLPKPT LWAEPGSVIT QGSPVTLRCQ
60 70 80 90 100
GGQETQEYRL YREKKTALWI TRIPQELVKK GQFPIPSITW EHAGRYRCYY
110 120 130 140 150
GSDTAGRSES SDPLELVVTG AYIKPTLSAQ PSPVVNSGGN VILQCDSQVA
160 170 180 190 200
FDGFSLCKEG EDEHPQCLNS QPHARGSSRA IFSVGPVSPS RRWWYRCYAY
210 220 230 240 250
DSNSPYEWSL PSDLLELLVL GVSKKPSLSV QPGPIVAPEE TLTLQCGSDA
260 270 280 290 300
GYNRFVLYKD GERDFLQLAG AQPQAGLSQA NFTLGPVSRS YGGQYRCYGA
310 320 330 340 350
HNLSSEWSAP SDPLDILIAG QFYDRVSLSV QPGPTVASGE NVTLLCQSQG
360 370 380 390 400
WMQTFLLTKE GAADDPWRLR STYQSQKYQA EFPMGPVTSA HAGTYRCYGS
410 420 430 440 450
QSSKPYLLTH PSDPLELVVS GPSGGPSSPT TGPTSTSGPE DQPLTPTGSD
460 470 480 490 500
PQSGLGRHLG VVIGILVAVI LLLLLLLLLF LILRHRRQGK HWTSTQRKAD
510 520 530 540 550
FQHPAGAVGP EPTDRGLQWR SSPAADAQEE NLYAAVKHTQ PEDGVEMDTR
560 570 580 590 600
SPHDEDPQAV TYAEVKHSRP RREMASPPSP LSGEFLDTKD RQAEEDRQMD
610 620 630 640 650
TEAAASEAPQ DVTYAQLHSL TLRREATEPP PSQEGPSPAV PSIYATLAIH
Length:650
Mass (Da):70,819
Last modified:October 1, 2002 - v1
Checksum:i549196EA4ED2767C
GO
Isoform 2 (identifier: Q8NHL6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     437-437: S → SA

Show »
Length:651
Mass (Da):70,890
Checksum:i7D4F9D838D844AA6
GO
Isoform 3 (identifier: Q8NHL6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     437-437: S → SA
     550-550: R → RQ

Show »
Length:652
Mass (Da):71,019
Checksum:i93AF8F021A22949D
GO
Isoform 4 (identifier: Q8NHL6-4) [UniParc]FASTAAdd to basket

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

Show »
Length:651
Mass (Da):70,948
Checksum:i3266510973E1C2A1
GO
Isoform 5 (identifier: Q8NHL6-5) [UniParc]FASTAAdd to basket
Also known as: 65 Kda, sLILRB1

The sequence of this isoform differs from the canonical sequence as follows:
     437-437: S → SA
     455-455: L → E
     456-650: Missing.

Note: May act as dominant negative regulator and block the interaction between membrane-associated isoforms and HLA-class I.1 Publication
Show »
Length:456
Mass (Da):49,356
Checksum:iDCF5CD284081A591
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti557P → L in AAL36989 (Ref. 6) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01699368L → P.4 PublicationsCorresponds to variant rs1061679dbSNPEnsembl.1
Natural variantiVAR_04988893A → T.2 PublicationsCorresponds to variant rs12460501dbSNPEnsembl.1
Natural variantiVAR_016994142I → T.4 PublicationsCorresponds to variant rs1061680dbSNPEnsembl.1
Natural variantiVAR_016995155S → I.4 PublicationsCorresponds to variant rs1061681dbSNPEnsembl.1
Natural variantiVAR_059398301H → Y.Corresponds to variant rs1045818dbSNPEnsembl.1
Natural variantiVAR_067316459L → V.Corresponds to variant rs45511398dbSNPEnsembl.1
Natural variantiVAR_016996620L → F.Corresponds to variant rs634222dbSNPEnsembl.1
Natural variantiVAR_067317625E → K.3 PublicationsCorresponds to variant rs16985478dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_008456437S → SA in isoform 2, isoform 3 and isoform 5. 2 Publications1
Alternative sequenceiVSP_057087455L → E in isoform 5. 1 Publication1
Alternative sequenceiVSP_057088456 – 650Missing in isoform 5. 1 PublicationAdd BLAST195
Alternative sequenceiVSP_008457550R → RQ in isoform 3 and isoform 4. 3 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004230 mRNA. Translation: AAB67710.1.
AF009220 mRNA. Translation: AAB63521.1.
AF009221 mRNA. Translation: AAB63522.1.
AF189277 Genomic DNA. Translation: AAG08984.1.
EU915608 mRNA. Translation: ACK56074.1.
HM135394 Genomic DNA. Translation: ADJ55944.1.
HM135401 Genomic DNA. Translation: ADJ55951.1.
AF283984 mRNA. Translation: AAL36988.1.
AF283985 mRNA. Translation: AAL36989.1.
AC009892 Genomic DNA. No translation available.
BC015731 mRNA. Translation: AAH15731.1.
CCDSiCCDS42614.1. [Q8NHL6-3]
CCDS42615.1. [Q8NHL6-2]
CCDS42616.1. [Q8NHL6-4]
CCDS42617.1. [Q8NHL6-1]
RefSeqiNP_001075106.2. NM_001081637.2.
NP_001075107.2. NM_001081638.3.
NP_001075108.2. NM_001081639.3.
NP_001265327.2. NM_001278398.2.
NP_001265328.2. NM_001278399.2.
NP_006660.4. NM_006669.6.
UniGeneiHs.667388.

Genome annotation databases

EnsembliENST00000448689; ENSP00000409968; ENSG00000104972.
ENST00000612636; ENSP00000479887; ENSG00000277807. [Q8NHL6-3]
ENST00000616408; ENSP00000481700; ENSG00000274669.
ENST00000617686; ENSP00000478282; ENSG00000277807. [Q8NHL6-4]
ENST00000618055; ENSP00000480365; ENSG00000277807. [Q8NHL6-1]
ENST00000618681; ENSP00000479753; ENSG00000277807. [Q8NHL6-2]
GeneIDi10859.
KEGGihsa:10859.
UCSCiuc032iow.2. human. [Q8NHL6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004230 mRNA. Translation: AAB67710.1.
AF009220 mRNA. Translation: AAB63521.1.
AF009221 mRNA. Translation: AAB63522.1.
AF189277 Genomic DNA. Translation: AAG08984.1.
EU915608 mRNA. Translation: ACK56074.1.
HM135394 Genomic DNA. Translation: ADJ55944.1.
HM135401 Genomic DNA. Translation: ADJ55951.1.
AF283984 mRNA. Translation: AAL36988.1.
AF283985 mRNA. Translation: AAL36989.1.
AC009892 Genomic DNA. No translation available.
BC015731 mRNA. Translation: AAH15731.1.
CCDSiCCDS42614.1. [Q8NHL6-3]
CCDS42615.1. [Q8NHL6-2]
CCDS42616.1. [Q8NHL6-4]
CCDS42617.1. [Q8NHL6-1]
RefSeqiNP_001075106.2. NM_001081637.2.
NP_001075107.2. NM_001081638.3.
NP_001075108.2. NM_001081639.3.
NP_001265327.2. NM_001278398.2.
NP_001265328.2. NM_001278399.2.
NP_006660.4. NM_006669.6.
UniGeneiHs.667388.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4NO0X-ray2.70D27-221[»]
ProteinModelPortaliQ8NHL6.
SMRiQ8NHL6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116070. 7 interactors.
IntActiQ8NHL6. 4 interactors.
MINTiMINT-7144935.
STRINGi9606.ENSP00000315997.

Protein family/group databases

MEROPSiI43.951.

PTM databases

iPTMnetiQ8NHL6.
PhosphoSitePlusiQ8NHL6.

Polymorphism and mutation databases

BioMutaiLILRB1.
DMDMi37537910.

Proteomic databases

PaxDbiQ8NHL6.
PeptideAtlasiQ8NHL6.
PRIDEiQ8NHL6.

Protocols and materials databases

DNASUi10859.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000448689; ENSP00000409968; ENSG00000104972.
ENST00000612636; ENSP00000479887; ENSG00000277807. [Q8NHL6-3]
ENST00000616408; ENSP00000481700; ENSG00000274669.
ENST00000617686; ENSP00000478282; ENSG00000277807. [Q8NHL6-4]
ENST00000618055; ENSP00000480365; ENSG00000277807. [Q8NHL6-1]
ENST00000618681; ENSP00000479753; ENSG00000277807. [Q8NHL6-2]
GeneIDi10859.
KEGGihsa:10859.
UCSCiuc032iow.2. human. [Q8NHL6-1]

Organism-specific databases

CTDi10859.
DisGeNETi10859.
GeneCardsiLILRB1.
H-InvDBHIX0137208.
HGNCiHGNC:6605. LILRB1.
MIMi604811. gene.
neXtProtiNX_Q8NHL6.
OpenTargetsiENSG00000277807.
PharmGKBiPA30379.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IKJD. Eukaryota.
ENOG41116BR. LUCA.
HOGENOMiHOG000234395.
HOVERGENiHBG074353.
InParanoidiQ8NHL6.
KOiK06512.
OMAiQAVTHAP.
OrthoDBiEOG091G0D6W.
PhylomeDBiQ8NHL6.
TreeFamiTF336644.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104972-MONOMER.
ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
SIGNORiQ8NHL6.

Miscellaneous databases

ChiTaRSiLILRB1. human.
EvolutionaryTraceiQ8NHL6.
GeneWikiiLILRB1.
GenomeRNAii10859.
PROiQ8NHL6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000104972.
CleanExiHS_LILRB1.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF13895. Ig_2. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 4 hits.
SM00408. IGc2. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLIRB1_HUMAN
AccessioniPrimary (citable) accession number: Q8NHL6
Secondary accession number(s): A2IXV4
, A8MXT0, O75024, O75025, Q8NHJ9, Q8NHK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.