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Q8NHL6

- LIRB1_HUMAN

UniProt

Q8NHL6 - LIRB1_HUMAN

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Protein
Leukocyte immunoglobulin-like receptor subfamily B member 1
Gene
LILRB1, ILT2, LIR1, MIR7
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. HLA-A specific inhibitory MHC class I receptor activity Source: UniProtKB
  2. HLA-B specific inhibitory MHC class I receptor activity Source: UniProtKB
  3. MHC class I protein binding Source: UniProtKB
  4. MHC class I receptor activity Source: UniProtKB
  5. SH2 domain binding Source: UniProtKB
  6. protein homodimerization activity Source: UniProtKB
  7. protein phosphatase 1 binding Source: UniProtKB

GO - Biological processi

  1. Fc receptor mediated inhibitory signaling pathway Source: UniProtKB
  2. T cell proliferation involved in immune response Source: UniProtKB
  3. cellular response to lipopolysaccharide Source: UniProtKB
  4. defense response to virus Source: UniProtKB
  5. dendritic cell differentiation Source: UniProtKB
  6. immune response-inhibiting cell surface receptor signaling pathway Source: BHF-UCL
  7. interferon-gamma production Source: UniProtKB
  8. interferon-gamma secretion Source: UniProtKB
  9. negative regulation of CD8-positive, alpha-beta T cell activation Source: UniProtKB
  10. negative regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell Source: UniProtKB
  11. negative regulation of T cell mediated cytotoxicity Source: UniProtKB
  12. negative regulation of T cell proliferation Source: UniProtKB
  13. negative regulation of alpha-beta T cell activation Source: UniProtKB
  14. negative regulation of calcium ion transport Source: UniProtKB
  15. negative regulation of cell cycle Source: UniProtKB
  16. negative regulation of cytokine secretion involved in immune response Source: UniProtKB
  17. negative regulation of dendritic cell apoptotic process Source: UniProtKB
  18. negative regulation of dendritic cell differentiation Source: UniProtKB
  19. negative regulation of endocytosis Source: UniProtKB
  20. negative regulation of interferon-beta secretion Source: UniProtKB
  21. negative regulation of interferon-gamma biosynthetic process Source: UniProtKB
  22. negative regulation of interferon-gamma production Source: UniProtKB
  23. negative regulation of interleukin-10 secretion Source: UniProtKB
  24. negative regulation of interleukin-12 secretion Source: UniProtKB
  25. negative regulation of mononuclear cell proliferation Source: UniProtKB
  26. negative regulation of natural killer cell mediated cytotoxicity Source: UniProtKB
  27. negative regulation of osteoclast development Source: UniProtKB
  28. negative regulation of serotonin secretion Source: UniProtKB
  29. negative regulation of transforming growth factor-beta secretion Source: UniProtKB
  30. negative regulation of tumor necrosis factor biosynthetic process Source: UniProtKB
  31. positive regulation of apoptotic process Source: UniProtKB
  32. positive regulation of cytolysis Source: UniProtKB
  33. positive regulation of defense response to virus by host Source: UniProtKB
  34. positive regulation of gamma-delta T cell activation involved in immune response Source: UniProtKB
  35. positive regulation of gene expression Source: UniProtKB
  36. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  37. receptor internalization Source: UniProtKB
  38. regulation of immune response Source: Reactome
  39. response to virus Source: UniProtKB
  40. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Adaptive immunity, Immunity

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.

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
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:6605. LILRB1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 461438Extracellular Reviewed prediction
Add
BLAST
Transmembranei462 – 48221Helical; Reviewed prediction
Add
BLAST
Topological domaini483 – 650168Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. external side of plasma membrane Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi533 – 5331Y → F: Impairs receptor phosphorylation and abolishes inhibition of serotonin release. No effect on PTPN6 binding; when associated with F-562. 1 Publication
Mutagenesisi562 – 5621Y → F: No effect on PTPN6 binding; when associated with F-533. 1 Publication
Mutagenesisi614 – 6141Y → F: No effect on PTPN6 binding. Abolishes PTPN6 binding; when associated with F-644. 1 Publication
Mutagenesisi644 – 6441Y → F: Reduces PTPN6 binding. Abolishes PTPN6 binding; when associated with F-614. 1 Publication

Organism-specific databases

PharmGKBiPA30379.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 650627Leukocyte immunoglobulin-like receptor subfamily B member 1
PRO_0000014820Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 98
Disulfide bondi145 ↔ 197
Disulfide bondi157 ↔ 167
Disulfide bondi246 ↔ 297 Reviewed prediction
Glycosylationi281 – 2811N-linked (GlcNAc...) Reviewed prediction
Glycosylationi302 – 3021N-linked (GlcNAc...) Reviewed prediction
Glycosylationi341 – 3411N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi346 ↔ 397 Reviewed prediction
Modified residuei533 – 5331Phosphotyrosine Inferred
Modified residuei614 – 6141Phosphotyrosine Inferred
Modified residuei644 – 6441Phosphotyrosine Inferred

Post-translational modificationi

Phosphorylated on tyrosine residues. Dephosphorylated by PTPN6.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ8NHL6.
PRIDEiQ8NHL6.

PTM databases

PhosphoSiteiQ8NHL6.

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

ArrayExpressiQ8NHL6.
BgeeiQ8NHL6.
CleanExiHS_LILRB1.
GenevestigatoriQ8NHL6.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi116070. 6 interactions.
IntActiQ8NHL6. 4 interactions.
MINTiMINT-7144935.
STRINGi9606.ENSP00000315997.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 356
Beta strandi37 – 404
Beta strandi45 – 506
Beta strandi52 – 543
Beta strandi58 – 658
Helixi68 – 714
Helixi75 – 784
Turni79 – 813
Beta strandi82 – 876
Helixi90 – 923
Beta strandi94 – 1029
Turni103 – 1053
Beta strandi114 – 1196
Beta strandi126 – 1316
Beta strandi133 – 1364
Beta strandi141 – 1466
Beta strandi152 – 1598
Beta strandi167 – 1693
Helixi172 – 1743
Beta strandi179 – 1846
Beta strandi193 – 2008
Beta strandi204 – 2085
Beta strandi215 – 2206
Beta strandi227 – 2326
Beta strandi234 – 2363
Beta strandi242 – 2509
Beta strandi253 – 2597
Beta strandi266 – 2705
Beta strandi278 – 2847
Helixi289 – 2913
Beta strandi293 – 3008
Beta strandi314 – 3207
Beta strandi322 – 3298
Beta strandi341 – 35010
Beta strandi353 – 36412
Beta strandi367 – 3704
Beta strandi375 – 38612
Helixi389 – 3913
Beta strandi393 – 4019
Beta strandi404 – 4085

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ8NHL6.
SMRiQ8NHL6. Positions 25-417.

Miscellaneous databases

EvolutionaryTraceiQ8NHL6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 11589Ig-like C2-type 1
Add
BLAST
Domaini116 – 221106Ig-like C2-type 2
Add
BLAST
Domaini222 – 31291Ig-like C2-type 3
Add
BLAST
Domaini313 – 40997Ig-like C2-type 4
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi531 – 5366ITIM motif 1
Motifi560 – 5656ITIM motif 2
Motifi612 – 6176ITIM motif 3
Motifi642 – 6476ITIM motif 4

Domaini

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG25855.
HOGENOMiHOG000234395.
HOVERGENiHBG074353.
KOiK06512.
PhylomeDBiQ8NHL6.
TreeFamiTF336644.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTiSM00409. IG. 3 hits.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

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

MTPILTVLIC LGLSLGPRTH VQAGHLPKPT LWAEPGSVIT QGSPVTLRCQ    50
GGQETQEYRL YREKKTALWI TRIPQELVKK GQFPIPSITW EHAGRYRCYY 100
GSDTAGRSES SDPLELVVTG AYIKPTLSAQ PSPVVNSGGN VILQCDSQVA 150
FDGFSLCKEG EDEHPQCLNS QPHARGSSRA IFSVGPVSPS RRWWYRCYAY 200
DSNSPYEWSL PSDLLELLVL GVSKKPSLSV QPGPIVAPEE TLTLQCGSDA 250
GYNRFVLYKD GERDFLQLAG AQPQAGLSQA NFTLGPVSRS YGGQYRCYGA 300
HNLSSEWSAP SDPLDILIAG QFYDRVSLSV QPGPTVASGE NVTLLCQSQG 350
WMQTFLLTKE GAADDPWRLR STYQSQKYQA EFPMGPVTSA HAGTYRCYGS 400
QSSKPYLLTH PSDPLELVVS GPSGGPSSPT TGPTSTSGPE DQPLTPTGSD 450
PQSGLGRHLG VVIGILVAVI LLLLLLLLLF LILRHRRQGK HWTSTQRKAD 500
FQHPAGAVGP EPTDRGLQWR SSPAADAQEE NLYAAVKHTQ PEDGVEMDTR 550
SPHDEDPQAV TYAEVKHSRP RREMASPPSP LSGEFLDTKD RQAEEDRQMD 600
TEAAASEAPQ DVTYAQLHSL TLRREATEPP PSQEGPSPAV PSIYATLAIH 650
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681L → P.3 Publications
Corresponds to variant rs1061679 [ dbSNP | Ensembl ].
VAR_016993
Natural varianti93 – 931A → T.1 Publication
Corresponds to variant rs12460501 [ dbSNP | Ensembl ].
VAR_049888
Natural varianti142 – 1421I → T.3 Publications
Corresponds to variant rs1061680 [ dbSNP | Ensembl ].
VAR_016994
Natural varianti155 – 1551S → I.3 Publications
Corresponds to variant rs1061681 [ dbSNP | Ensembl ].
VAR_016995
Natural varianti301 – 3011H → Y.
Corresponds to variant rs1045818 [ dbSNP | Ensembl ].
VAR_059398
Natural varianti459 – 4591L → V.
Corresponds to variant rs45511398 [ dbSNP | Ensembl ].
VAR_067316
Natural varianti620 – 6201L → F.
Corresponds to variant rs634222 [ dbSNP | Ensembl ].
VAR_016996
Natural varianti625 – 6251E → K.3 Publications
Corresponds to variant rs16985478 [ dbSNP | Ensembl ].
VAR_067317

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei437 – 4371S → SA in isoform 2 and isoform 3.
VSP_008456
Alternative sequencei550 – 5501R → RQ in isoform 3 and isoform 4.
VSP_008457

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti557 – 5571P → L in AAL36989. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
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_006660.4. NM_006669.6.
UniGeneiHs.667388.

Genome annotation databases

EnsembliENST00000324602; 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.
GeneIDi10859.
KEGGihsa:10859.
UCSCiuc002qgj.3. human. [Q8NHL6-1]
uc002qgk.3. human. [Q8NHL6-2]
uc002qgl.3. human. [Q8NHL6-4]
uc002qgm.3. human. [Q8NHL6-3]

Polymorphism databases

DMDMi37537910.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS42614.1. [Q8NHL6-3 ]
CCDS42615.1. [Q8NHL6-2 ]
CCDS42616.1. [Q8NHL6-4 ]
CCDS42617.1. [Q8NHL6-1 ]
RefSeqi NP_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.
UniGenei Hs.667388.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4LL9 X-ray 2.69 A/B/C 222-417 [» ]
ProteinModelPortali Q8NHL6.
SMRi Q8NHL6. Positions 25-417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116070. 6 interactions.
IntActi Q8NHL6. 4 interactions.
MINTi MINT-7144935.
STRINGi 9606.ENSP00000315997.

PTM databases

PhosphoSitei Q8NHL6.

Polymorphism databases

DMDMi 37537910.

Proteomic databases

PaxDbi Q8NHL6.
PRIDEi Q8NHL6.

Protocols and materials databases

DNASUi 10859.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000324602 ; 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 .
GeneIDi 10859.
KEGGi hsa:10859.
UCSCi uc002qgj.3. human. [Q8NHL6-1 ]
uc002qgk.3. human. [Q8NHL6-2 ]
uc002qgl.3. human. [Q8NHL6-4 ]
uc002qgm.3. human. [Q8NHL6-3 ]

Organism-specific databases

CTDi 10859.
GeneCardsi GC19P055085.
H-InvDB HIX0137208.
HGNCi HGNC:6605. LILRB1.
MIMi 604811. gene.
neXtProti NX_Q8NHL6.
PharmGKBi PA30379.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG25855.
HOGENOMi HOG000234395.
HOVERGENi HBG074353.
KOi K06512.
PhylomeDBi Q8NHL6.
TreeFami TF336644.

Enzyme and pathway databases

Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.

Miscellaneous databases

ChiTaRSi LILRB1. human.
EvolutionaryTracei Q8NHL6.
GeneWikii LILRB1.
GenomeRNAii 10859.
NextBioi 41223.
PROi Q8NHL6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8NHL6.
Bgeei Q8NHL6.
CleanExi HS_LILRB1.
Genevestigatori Q8NHL6.

Family and domain databases

Gene3Di 2.60.40.10. 4 hits.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view ]
SMARTi SM00409. IG. 3 hits.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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: 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.

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: September 3, 2014
This is version 121 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

External Data

Dasty 3

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