Q8NHL6 · LIRB1_HUMAN
- ProteinLeukocyte immunoglobulin-like receptor subfamily B member 1
- GeneLILRB1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids650 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 FCER1A signaling and serotonin release. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions (PubMed:11907092, PubMed:9285411, PubMed:9842885).
Recognizes HLA-G in complex with B2M/beta-2 microglobulin and a nonamer self-peptide (PubMed:16455647).
Upon interaction with peptide-bound HLA-G-B2M complex, triggers secretion of growth-promoting factors by decidual NK cells (PubMed:19304799, PubMed:29262349).
Reprograms B cells toward an immune suppressive phenotype (PubMed:24453251).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLeukocyte immunoglobulin-like receptor subfamily B member 1
- Short namesLIR-1 ; Leukocyte immunoglobulin-like receptor 1
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8NHL6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 5
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 24-461 | Extracellular | ||||
Sequence: GHLPKPTLWAEPGSVITQGSPVTLRCQGGQETQEYRLYREKKTALWITRIPQELVKKGQFPIPSITWEHAGRYRCYYGSDTAGRSESSDPLELVVTGAYIKPTLSAQPSPVVNSGGNVILQCDSQVAFDGFSLCKEGEDEHPQCLNSQPHARGSSRAIFSVGPVSPSRRWWYRCYAYDSNSPYEWSLPSDLLELLVLGVSKKPSLSVQPGPIVAPEETLTLQCGSDAGYNRFVLYKDGERDFLQLAGAQPQAGLSQANFTLGPVSRSYGGQYRCYGAHNLSSEWSAPSDPLDILIAGQFYDRVSLSVQPGPTVASGENVTLLCQSQGWMQTFLLTKEGAADDPWRLRSTYQSQKYQAEFPMGPVTSAHAGTYRCYGSQSSKPYLLTHPSDPLELVVSGPSGGPSSPTTGPTSTSGPEDQPLTPTGSDPQSGLGRHLGV | ||||||
Transmembrane | 462-482 | Helical | ||||
Sequence: VIGILVAVILLLLLLLLLFLI | ||||||
Topological domain | 483-650 | Cytoplasmic | ||||
Sequence: LRHRRQGKHWTSTQRKADFQHPAGAVGPEPTDRGLQWRSSPAADAQEENLYAAVKHTQPEDGVEMDTRSPHDEDPQAVTYAEVKHSRPRREMASPPSPLSGEFLDTKDRQAEEDRQMDTEAAASEAPQDVTYAQLHSLTLRREATEPPPSQEGPSPAVPSIYATLAIH |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_016993 | 68 | in dbSNP:rs1061679 | |||
Sequence: L → P | ||||||
Natural variant | VAR_049888 | 93 | in dbSNP:rs12460501 | |||
Sequence: A → T | ||||||
Natural variant | VAR_016994 | 142 | in dbSNP:rs1061680 | |||
Sequence: I → T | ||||||
Natural variant | VAR_016995 | 155 | in dbSNP:rs1061681 | |||
Sequence: S → I | ||||||
Natural variant | VAR_059398 | 301 | in dbSNP:rs1045818 | |||
Sequence: H → Y | ||||||
Natural variant | VAR_067316 | 459 | in dbSNP:rs1138737 | |||
Sequence: L → V | ||||||
Mutagenesis | 533 | Impairs receptor phosphorylation and abolishes inhibition of serotonin release. No effect on PTPN6 binding; when associated with F-562. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 562 | No effect on PTPN6 binding; when associated with F-533. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 614 | No effect on PTPN6 binding. Abolishes PTPN6 binding; when associated with F-644. | ||||
Sequence: Y → F | ||||||
Natural variant | VAR_016996 | 620 | in dbSNP:rs634222 | |||
Sequence: L → F | ||||||
Natural variant | VAR_067317 | 625 | in dbSNP:rs16985478 | |||
Sequence: E → K | ||||||
Mutagenesis | 644 | Reduces PTPN6 binding. Abolishes PTPN6 binding; when associated with F-614. | ||||
Sequence: Y → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 802 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-23 | UniProt | |||||
Sequence: MTPILTVLICLGLSLGPRTHVQA | |||||||
Chain | PRO_0000014820 | 24-650 | UniProt | Leukocyte immunoglobulin-like receptor subfamily B member 1 | |||
Sequence: GHLPKPTLWAEPGSVITQGSPVTLRCQGGQETQEYRLYREKKTALWITRIPQELVKKGQFPIPSITWEHAGRYRCYYGSDTAGRSESSDPLELVVTGAYIKPTLSAQPSPVVNSGGNVILQCDSQVAFDGFSLCKEGEDEHPQCLNSQPHARGSSRAIFSVGPVSPSRRWWYRCYAYDSNSPYEWSLPSDLLELLVLGVSKKPSLSVQPGPIVAPEETLTLQCGSDAGYNRFVLYKDGERDFLQLAGAQPQAGLSQANFTLGPVSRSYGGQYRCYGAHNLSSEWSAPSDPLDILIAGQFYDRVSLSVQPGPTVASGENVTLLCQSQGWMQTFLLTKEGAADDPWRLRSTYQSQKYQAEFPMGPVTSAHAGTYRCYGSQSSKPYLLTHPSDPLELVVSGPSGGPSSPTTGPTSTSGPEDQPLTPTGSDPQSGLGRHLGVVIGILVAVILLLLLLLLLFLILRHRRQGKHWTSTQRKADFQHPAGAVGPEPTDRGLQWRSSPAADAQEENLYAAVKHTQPEDGVEMDTRSPHDEDPQAVTYAEVKHSRPRREMASPPSPLSGEFLDTKDRQAEEDRQMDTEAAASEAPQDVTYAQLHSLTLRREATEPPPSQEGPSPAVPSIYATLAIH | |||||||
Disulfide bond | 49↔98 | UniProt | |||||
Sequence: CQGGQETQEYRLYREKKTALWITRIPQELVKKGQFPIPSITWEHAGRYRC | |||||||
Disulfide bond | 145↔197 | UniProt | |||||
Sequence: CDSQVAFDGFSLCKEGEDEHPQCLNSQPHARGSSRAIFSVGPVSPSRRWWYRC | |||||||
Disulfide bond | 157↔167 | UniProt | |||||
Sequence: CKEGEDEHPQC | |||||||
Disulfide bond | 246↔297 | UniProt | |||||
Sequence: CGSDAGYNRFVLYKDGERDFLQLAGAQPQAGLSQANFTLGPVSRSYGGQYRC | |||||||
Glycosylation | 281 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 302 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 341 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 346↔397 | UniProt | |||||
Sequence: CQSQGWMQTFLLTKEGAADDPWRLRSTYQSQKYQAEFPMGPVTSAHAGTYRC | |||||||
Modified residue | 533 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 533 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 576 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 579 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 614 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 619 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 644 | UniProt | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in decidual macrophages (at protein level) (PubMed:19304799).
Expressed in decidual NK cells (at protein level) (PubMed:29262349).
Interaction
Subunit
Binds FCER1A and FCGR1A (PubMed:11907092, PubMed:9842885).
Interacts with human cytomegalovirus/HHV-5 protein UL18 (PubMed:10591185).
Interacts with peptide-bound HLA-G-B2M complex (PubMed:16455647).
Interacts with peptide-bound HLA-F-B2M complex but not with peptide-free HLA-F open conformer. It does not probe the peptide sequence directly (PubMed:28636952).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8NHL6 | HLA-G P17693 | 8 | EBI-2805262, EBI-1043063 | |
BINARY | Q8NHL6 | PTPN6 P29350 | 4 | EBI-2805262, EBI-78260 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 27-115 | Ig-like C2-type 1 | ||||
Sequence: PKPTLWAEPGSVITQGSPVTLRCQGGQETQEYRLYREKKTALWITRIPQELVKKGQFPIPSITWEHAGRYRCYYGSDTAGRSESSDPLE | ||||||
Domain | 116-221 | Ig-like C2-type 2 | ||||
Sequence: LVVTGAYIKPTLSAQPSPVVNSGGNVILQCDSQVAFDGFSLCKEGEDEHPQCLNSQPHARGSSRAIFSVGPVSPSRRWWYRCYAYDSNSPYEWSLPSDLLELLVLG | ||||||
Domain | 222-312 | Ig-like C2-type 3 | ||||
Sequence: VSKKPSLSVQPGPIVAPEETLTLQCGSDAGYNRFVLYKDGERDFLQLAGAQPQAGLSQANFTLGPVSRSYGGQYRCYGAHNLSSEWSAPSD | ||||||
Domain | 313-409 | Ig-like C2-type 4 | ||||
Sequence: PLDILIAGQFYDRVSLSVQPGPTVASGENVTLLCQSQGWMQTFLLTKEGAADDPWRLRSTYQSQKYQAEFPMGPVTSAHAGTYRCYGSQSSKPYLLT | ||||||
Region | 415-451 | Disordered | ||||
Sequence: LELVVSGPSGGPSSPTTGPTSTSGPEDQPLTPTGSDP | ||||||
Compositional bias | 423-451 | Polar residues | ||||
Sequence: SGGPSSPTTGPTSTSGPEDQPLTPTGSDP | ||||||
Region | 491-524 | Disordered | ||||
Sequence: HWTSTQRKADFQHPAGAVGPEPTDRGLQWRSSPA | ||||||
Motif | 531-536 | ITIM motif 1 | ||||
Sequence: NLYAAV | ||||||
Motif | 560-565 | ITIM motif 2 | ||||
Sequence: VTYAEV | ||||||
Region | 563-650 | Disordered | ||||
Sequence: AEVKHSRPRREMASPPSPLSGEFLDTKDRQAEEDRQMDTEAAASEAPQDVTYAQLHSLTLRREATEPPPSQEGPSPAVPSIYATLAIH | ||||||
Compositional bias | 587-602 | Basic and acidic residues | ||||
Sequence: DTKDRQAEEDRQMDTE | ||||||
Motif | 612-617 | ITIM motif 3 | ||||
Sequence: VTYAQL | ||||||
Motif | 642-647 | ITIM motif 4 | ||||
Sequence: SIYATL |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 5 isoforms produced by Alternative splicing.
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.
- Name1
- Length650
- Mass (Da)70,819
- Last updated2002-10-01 v1
- Checksum549196EA4ED2767C
Q8NHL6-2
- Name2
- Differences from canonical
- 437-437: S → SA
Q8NHL6-3
- Name3
Q8NHL6-4
- Name4
- Differences from canonical
- 550-550: R → RQ
Q8NHL6-5
- Name5
- Synonyms65 Kda, sLILRB1
- NoteMay act as dominant negative regulator and block the interaction between membrane-associated isoforms and HLA-class I.
Computationally mapped potential isoform sequences
There are 19 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A8MVE2 | A8MVE2_HUMAN | LILRB1 | 634 | ||
D9IDM5 | D9IDM5_HUMAN | LILRB1 | 651 | ||
D9IDM6 | D9IDM6_HUMAN | LILRB1 | 651 | ||
F6RVM3 | F6RVM3_HUMAN | LILRB1 | 510 | ||
A0A0G2JP64 | A0A0G2JP64_HUMAN | LILRB1 | 668 | ||
A0A0G2JP80 | A0A0G2JP80_HUMAN | LILRB1 | 652 | ||
A0A0G2JQ15 | A0A0G2JQ15_HUMAN | LILRB1 | 668 | ||
A0A0G2JQ44 | A0A0G2JQ44_HUMAN | LILRB1 | 651 | ||
A0A0G2JQ46 | A0A0G2JQ46_HUMAN | LILRB1 | 634 | ||
F6TER3 | F6TER3_HUMAN | LILRB1 | 701 | ||
A0A0G2JMG0 | A0A0G2JMG0_HUMAN | LILRB1 | 67 | ||
A0A0G2JLS4 | A0A0G2JLS4_HUMAN | LILRB1 | 684 | ||
A0A0G2JNK9 | A0A0G2JNK9_HUMAN | LILRB1 | 510 | ||
A0A0G2JNM2 | A0A0G2JNM2_HUMAN | LILRB1 | 667 | ||
A0A0G2JNR3 | A0A0G2JNR3_HUMAN | LILRB1 | 510 | ||
A0A0G2JNQ6 | A0A0G2JNQ6_HUMAN | LILRB1 | 652 | ||
A0A0B4J1W1 | A0A0B4J1W1_HUMAN | LILRB1 | 650 | ||
A0A087WSV6 | A0A087WSV6_HUMAN | LILRB1 | 652 | ||
A0A087WSX8 | A0A087WSX8_HUMAN | LILRB1 | 651 |
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 423-451 | Polar residues | ||||
Sequence: SGGPSSPTTGPTSTSGPEDQPLTPTGSDP | ||||||
Alternative sequence | VSP_008456 | 437 | in isoform 2, isoform 3 and isoform 5 | |||
Sequence: S → SA | ||||||
Alternative sequence | VSP_057087 | 455 | in isoform 5 | |||
Sequence: L → E | ||||||
Alternative sequence | VSP_057088 | 456-650 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_008457 | 550 | in isoform 3 and isoform 4 | |||
Sequence: R → RQ | ||||||
Sequence conflict | 557 | in Ref. 6; AAL36989 | ||||
Sequence: P → L | ||||||
Compositional bias | 587-602 | Basic and acidic residues | ||||
Sequence: DTKDRQAEEDRQMDTE |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF004230 EMBL· GenBank· DDBJ | AAB67710.1 EMBL· GenBank· DDBJ | mRNA | ||
AF009220 EMBL· GenBank· DDBJ | AAB63521.1 EMBL· GenBank· DDBJ | mRNA | ||
AF009221 EMBL· GenBank· DDBJ | AAB63522.1 EMBL· GenBank· DDBJ | mRNA | ||
AF189277 EMBL· GenBank· DDBJ | AAG08984.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EU915608 EMBL· GenBank· DDBJ | ACK56074.1 EMBL· GenBank· DDBJ | mRNA | ||
HM135394 EMBL· GenBank· DDBJ | ADJ55944.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
HM135401 EMBL· GenBank· DDBJ | ADJ55951.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF283984 EMBL· GenBank· DDBJ | AAL36988.1 EMBL· GenBank· DDBJ | mRNA | ||
AF283985 EMBL· GenBank· DDBJ | AAL36989.1 EMBL· GenBank· DDBJ | mRNA | ||
AC009892 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC015731 EMBL· GenBank· DDBJ | AAH15731.1 EMBL· GenBank· DDBJ | mRNA |