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Protein

Leukocyte-associated immunoglobulin-like receptor 1

Gene

LAIR1

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

Functioni

Functions as an inhibitory receptor that plays a constitutive negative regulatory role on cytolytic function of natural killer (NK) cells, B-cells and T-cells. Activation by Tyr phosphorylation results in recruitment and activation of the phosphatases PTPN6 and PTPN11. It also reduces the increase of intracellular calcium evoked by B-cell receptor ligation. May also play its inhibitory role independently of SH2-containing phosphatases. Modulates cytokine production in CD4+ T-cells, down-regulating IL2 and IFNG production while inducing secretion of transforming growth factor beta. Down-regulates also IgG and IgE production in B-cells as well as IL8, IL10 and TNF secretion. Inhibits proliferation and induces apoptosis in myeloid leukemia cell lines as well as prevents nuclear translocation of NF-kappa-B p65 subunit/RELA and phosphorylation of I-kappa-B alpha/CHUK in these cells. Inhibits the differentiation of peripheral blood precursors towards dendritic cells.10 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Adaptive immunity, Immunity

Enzyme and pathway databases

ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.

Names & Taxonomyi

Protein namesi
Recommended name:
Leukocyte-associated immunoglobulin-like receptor 1
Short name:
LAIR-1
Short name:
hLAIR1
Alternative name(s):
CD_antigen: CD305
Gene namesi
Name:LAIR1
Synonyms:CD305
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:6477. LAIR1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 165144ExtracellularSequence analysisAdd
BLAST
Transmembranei166 – 18621HelicalSequence analysisAdd
BLAST
Topological domaini187 – 287101CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi251 – 2511Y → F: Reduced tyrosine phosphorylation and loss of binding to PTPN6 and CSK as well as complete loss of inhibitory activity. Loss of phosphorylation and of inhibition of calcium mobilization; when associated with F-281. 3 Publications
Mutagenesisi281 – 2811Y → F: Reduced tyrosine phosphorylation and loss of binding to PTPN6. Partial inhibition of cytotoxic activity. 3 Publications

Organism-specific databases

PharmGKBiPA30266.

Polymorphism and mutation databases

BioMutaiLAIR1.
DMDMi74736490.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 287266Leukocyte-associated immunoglobulin-like receptor 1PRO_0000250682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 1011 Publication
Glycosylationi69 – 691N-linked (GlcNAc...)1 Publication
Modified residuei251 – 2511Phosphotyrosine1 Publication
Modified residuei281 – 2811Phosphotyrosine1 Publication

Post-translational modificationi

Phosphorylation at Tyr-251 and Tyr-281 activates it. May be phosphorylated by LCK.1 Publication
N-glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ6GTX8.
MaxQBiQ6GTX8.
PaxDbiQ6GTX8.
PRIDEiQ6GTX8.

PTM databases

iPTMnetiQ6GTX8.
PhosphoSiteiQ6GTX8.
SwissPalmiQ6GTX8.

Expressioni

Tissue specificityi

Expressed on the majority of peripheral mononuclear cells, including natural killer (NK) cells, T-cells, B-cells, monocytes, and dendritic cells. Highly expressed in naive T-cells and B-cells but no expression on germinal center B-cells. Abnormally low expression in naive B-cells from HIV-1 infected patients. Very low expression in NK cells from a patient with chronic active Epstein-Barr virus infection.4 Publications

Developmental stagei

Complete loss of expression when naive B-cells proliferates and differentiates into Ig-producing plasma cells under in vitro stimulation.1 Publication

Inductioni

By T-cell receptor stimulation in a process that requires p38 MAP kinase and ERK signaling.1 Publication

Gene expression databases

BgeeiQ6GTX8.
CleanExiHS_LAIR1.
ExpressionAtlasiQ6GTX8. baseline and differential.
GenevisibleiQ6GTX8. HS.

Organism-specific databases

HPAiHPA011155.

Interactioni

Subunit structurei

Interacts with SH2 domains of tyrosine-protein phosphatases PTPN6 and PTPN11. The interaction with PTPN6 is constitutive. Interacts with the SH2 domain of CSK. Binds with high affinity to extracellular matrix collagens, the interaction is functionally important.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PTPN6P293505EBI-965864,EBI-78260

Protein-protein interaction databases

BioGridi110098. 4 interactions.
IntActiQ6GTX8. 2 interactions.
MINTiMINT-8020337.
STRINGi9606.ENSP00000375622.

Structurei

Secondary structure

1
287
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 356Combined sources
Beta strandi37 – 404Combined sources
Beta strandi45 – 517Combined sources
Beta strandi57 – 626Combined sources
Helixi63 – 653Combined sources
Beta strandi67 – 715Combined sources
Beta strandi75 – 784Combined sources
Beta strandi81 – 9010Combined sources
Helixi93 – 953Combined sources
Beta strandi97 – 1059Combined sources
Beta strandi116 – 1216Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KGRX-ray1.80A/B/C22-122[»]
3RP1X-ray2.60A/B/C/D22-123[»]
ProteinModelPortaliQ6GTX8.
SMRiQ6GTX8. Positions 25-122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6GTX8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 11789Ig-like C2-typeAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi249 – 2546ITIM motif 1
Motifi279 – 2846ITIM motif 2

Domaini

ITIM (immunoreceptor tyrosine-based inhibitor motif) motif is a cytoplasmic motif present in 2 copies in the intracellular part of LAIR1. When phosphorylated, ITIM motif can bind the SH2 domain of several SH2-containing phosphatases, leading to down-regulation of cell activation.1 Publication

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J37Q. Eukaryota.
ENOG41119RI. LUCA.
HOGENOMiHOG000015184.
HOVERGENiHBG081887.
InParanoidiQ6GTX8.
KOiK06725.
PhylomeDBiQ6GTX8.
TreeFamiTF336644.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
PfamiPF13895. Ig_2. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.

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. AlignAdd to basket

Isoform 1 (identifier: Q6GTX8-1) [UniParc]FASTAAdd to basket

Also known as: LAIR-1a

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
MSPHPTALLG LVLCLAQTIH TQEEDLPRPS ISAEPGTVIP LGSHVTFVCR
60 70 80 90 100
GPVGVQTFRL ERESRSTYND TEDVSQASPS ESEARFRIDS VSEGNAGPYR
110 120 130 140 150
CIYYKPPKWS EQSDYLELLV KETSGGPDSP DTEPGSSAGP TQRPSDNSHN
160 170 180 190 200
EHAPASQGLK AEHLYILIGV SVVFLFCLLL LVLFCLHRQN QIKQGPPRSK
210 220 230 240 250
DEEQKPQQRP DLAVDVLERT ADKATVNGLP EKDRETDTSA LAAGSSQEVT
260 270 280
YAQLDHWALT QRTARAVSPQ STKPMAESIT YAAVARH
Length:287
Mass (Da):31,412
Last modified:July 19, 2004 - v1
Checksum:i752EFB2FCC29B8E8
GO
Isoform 2 (identifier: Q6GTX8-2) [UniParc]FASTAAdd to basket

Also known as: LAIR-1b

The sequence of this isoform differs from the canonical sequence as follows:
     122-138: Missing.

Note: Functions as an inhibitory receptor in NK cells and T-cells.
Show »
Length:270
Mass (Da):29,840
Checksum:i8F7106914E4B4347
GO
Isoform 3 (identifier: Q6GTX8-3) [UniParc]FASTAAdd to basket

Also known as: LAIR-1c

The sequence of this isoform differs from the canonical sequence as follows:
     23-23: Missing.
     122-138: Missing.

Show »
Length:269
Mass (Da):29,710
Checksum:iCC0246DC14189301
GO
Isoform 4 (identifier: Q6GTX8-4) [UniParc]FASTAAdd to basket

Also known as: LAIR-1d

The sequence of this isoform differs from the canonical sequence as follows:
     210-287: Missing.

Show »
Length:209
Mass (Da):23,049
Checksum:i080127D8FC665567
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti63 – 631E → D.
Corresponds to variant rs3745442 [ dbSNP | Ensembl ].
VAR_027598

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei23 – 231Missing in isoform 3. 1 PublicationVSP_020710
Alternative sequencei122 – 13817Missing in isoform 2 and isoform 3. 2 PublicationsVSP_020711Add
BLAST
Alternative sequencei210 – 28778Missing in isoform 4. 1 PublicationVSP_020712Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF013249 mRNA. Translation: AAB69324.1.
AF109683 mRNA. Translation: AAF17107.1.
AF251509 mRNA. Translation: AAF71274.2.
AF251510 mRNA. Translation: AAF71275.2.
CR542051 mRNA. Translation: CAG46848.1.
BC027899 mRNA. Translation: AAH27899.1.
CCDSiCCDS12891.1. [Q6GTX8-1]
CCDS12892.1. [Q6GTX8-2]
CCDS74448.1. [Q6GTX8-3]
RefSeqiNP_001275952.2. NM_001289023.2.
NP_001275954.2. NM_001289025.2.
NP_002278.2. NM_002287.5.
NP_068352.2. NM_021706.4.
UniGeneiHs.572535.

Genome annotation databases

EnsembliENST00000348231; ENSP00000301193; ENSG00000167613.
ENST00000391742; ENSP00000375622; ENSG00000167613.
ENST00000474878; ENSP00000418998; ENSG00000167613.
ENST00000610549; ENSP00000481204; ENSG00000276053. [Q6GTX8-3]
ENST00000614937; ENSP00000479006; ENSG00000278154. [Q6GTX8-3]
ENST00000614946; ENSP00000478853; ENSG00000274110. [Q6GTX8-3]
ENST00000616612; ENSP00000479682; ENSG00000278154. [Q6GTX8-1]
ENST00000618434; ENSP00000479133; ENSG00000274110. [Q6GTX8-1]
ENST00000619717; ENSP00000479707; ENSG00000276053. [Q6GTX8-1]
ENST00000619817; ENSP00000480619; ENSG00000276163. [Q6GTX8-2]
ENST00000620077; ENSP00000482922; ENSG00000276053. [Q6GTX8-2]
ENST00000620357; ENSP00000479649; ENSG00000278154. [Q6GTX8-2]
ENST00000620726; ENSP00000478405; ENSG00000276163. [Q6GTX8-3]
ENST00000622097; ENSP00000480659; ENSG00000274110. [Q6GTX8-2]
GeneIDi3903.
KEGGihsa:3903.
UCSCiuc032idt.2. human. [Q6GTX8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF013249 mRNA. Translation: AAB69324.1.
AF109683 mRNA. Translation: AAF17107.1.
AF251509 mRNA. Translation: AAF71274.2.
AF251510 mRNA. Translation: AAF71275.2.
CR542051 mRNA. Translation: CAG46848.1.
BC027899 mRNA. Translation: AAH27899.1.
CCDSiCCDS12891.1. [Q6GTX8-1]
CCDS12892.1. [Q6GTX8-2]
CCDS74448.1. [Q6GTX8-3]
RefSeqiNP_001275952.2. NM_001289023.2.
NP_001275954.2. NM_001289025.2.
NP_002278.2. NM_002287.5.
NP_068352.2. NM_021706.4.
UniGeneiHs.572535.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KGRX-ray1.80A/B/C22-122[»]
3RP1X-ray2.60A/B/C/D22-123[»]
ProteinModelPortaliQ6GTX8.
SMRiQ6GTX8. Positions 25-122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110098. 4 interactions.
IntActiQ6GTX8. 2 interactions.
MINTiMINT-8020337.
STRINGi9606.ENSP00000375622.

PTM databases

iPTMnetiQ6GTX8.
PhosphoSiteiQ6GTX8.
SwissPalmiQ6GTX8.

Polymorphism and mutation databases

BioMutaiLAIR1.
DMDMi74736490.

Proteomic databases

EPDiQ6GTX8.
MaxQBiQ6GTX8.
PaxDbiQ6GTX8.
PRIDEiQ6GTX8.

Protocols and materials databases

DNASUi3903.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000348231; ENSP00000301193; ENSG00000167613.
ENST00000391742; ENSP00000375622; ENSG00000167613.
ENST00000474878; ENSP00000418998; ENSG00000167613.
ENST00000610549; ENSP00000481204; ENSG00000276053. [Q6GTX8-3]
ENST00000614937; ENSP00000479006; ENSG00000278154. [Q6GTX8-3]
ENST00000614946; ENSP00000478853; ENSG00000274110. [Q6GTX8-3]
ENST00000616612; ENSP00000479682; ENSG00000278154. [Q6GTX8-1]
ENST00000618434; ENSP00000479133; ENSG00000274110. [Q6GTX8-1]
ENST00000619717; ENSP00000479707; ENSG00000276053. [Q6GTX8-1]
ENST00000619817; ENSP00000480619; ENSG00000276163. [Q6GTX8-2]
ENST00000620077; ENSP00000482922; ENSG00000276053. [Q6GTX8-2]
ENST00000620357; ENSP00000479649; ENSG00000278154. [Q6GTX8-2]
ENST00000620726; ENSP00000478405; ENSG00000276163. [Q6GTX8-3]
ENST00000622097; ENSP00000480659; ENSG00000274110. [Q6GTX8-2]
GeneIDi3903.
KEGGihsa:3903.
UCSCiuc032idt.2. human. [Q6GTX8-1]

Organism-specific databases

CTDi3903.
GeneCardsiLAIR1.
H-InvDBHIX0137494.
HGNCiHGNC:6477. LAIR1.
HPAiHPA011155.
MIMi602992. gene.
neXtProtiNX_Q6GTX8.
PharmGKBiPA30266.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J37Q. Eukaryota.
ENOG41119RI. LUCA.
HOGENOMiHOG000015184.
HOVERGENiHBG081887.
InParanoidiQ6GTX8.
KOiK06725.
PhylomeDBiQ6GTX8.
TreeFamiTF336644.

Enzyme and pathway databases

ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.

Miscellaneous databases

ChiTaRSiLAIR1. human.
EvolutionaryTraceiQ6GTX8.
GeneWikiiLAIR1.
GenomeRNAii3903.
PROiQ6GTX8.
SOURCEiSearch...

Gene expression databases

BgeeiQ6GTX8.
CleanExiHS_LAIR1.
ExpressionAtlasiQ6GTX8. baseline and differential.
GenevisibleiQ6GTX8. HS.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
PfamiPF13895. Ig_2. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "LAIR-1, a novel inhibitory receptor expressed on human mononuclear leukocytes."
    Meyaard L., Adema G.J., Chang C., Woollatt E., Sutherland G.R., Lanier L.L., Phillips J.H.
    Immunity 7:283-290(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, SUBCELLULAR LOCATION, DOMAIN ITIM MOTIF, INTERACTION WITH PTPN6 AND PTPN11, FUNCTION.
  2. "Leukocyte-associated Ig-like receptor-1 functions as an inhibitory receptor on cytotoxic T cells."
    Meyaard L., Hurenkamp J., Clevers H., Lanier L.L., Phillips J.H.
    J. Immunol. 162:5800-5804(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION.
  3. "Identification and characterization of leukocyte-associated Ig-like receptor-1 as a major anchor protein of tyrosine phosphatase SHP-1 in hematopoietic cells."
    Xu M.-J., Zhao R., Zhao Z.J.
    J. Biol. Chem. 275:17440-17446(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, PHOSPHORYLATION AT TYR-251 AND TYR-281, MUTAGENESIS OF TYR-251 AND TYR-281, INTERACTION WITH PTPN6.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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).
    Tissue: Pancreas.
  6. "p40/LAIR-1 regulates the differentiation of peripheral blood precursors to dendritic cells induced by granulocyte-monocyte colony-stimulating factor."
    Poggi A., Tomasello E., Ferrero E., Zocchi M.R., Moretta L.
    Eur. J. Immunol. 28:2086-2091(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Leukocyte-associated immunoglobulin-like receptor-1 (LAIR-1) is differentially expressed during human B cell differentiation and inhibits B cell receptor-mediated signaling."
    van der Vuurst de Vries A.-R., Clevers H., Logtenberg T., Meyaard L.
    Eur. J. Immunol. 29:3160-3167(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  8. "Engagement of the leukocyte-associated Ig-like receptor-1 induces programmed cell death and prevents NF-kappaB nuclear translocation in human myeloid leukemias."
    Poggi A., Pellegatta F., Leone B.E., Moretta L., Zocchi M.R.
    Eur. J. Immunol. 30:2751-2758(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Constitutive association of SHP-1 with leukocyte-associated Ig-like receptor-1 in human T cells."
    Sathish J.G., Johnson K.G., Fuller K.J., LeRoy F.G., Meyaard L., Sims M.J., Matthews R.J.
    J. Immunol. 166:1763-1770(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PTPN6, FUNCTION.
  10. "Surface density expression of the leukocyte-associated Ig-like receptor-1 is directly related to inhibition of human T-cell functions."
    Saverino D., Fabbi M., Merlo A., Ravera G., Grossi C.E., Ciccone E.
    Hum. Immunol. 63:534-546(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Differential contribution of the immunoreceptor tyrosine-based inhibitory motifs of human leukocyte-associated Ig-like receptor-1 to inhibitory function and phosphatase recruitment."
    Verbrugge A., de Ruiter T., Clevers H., Meyaard L.
    Int. Immunol. 15:1349-1358(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-251 AND TYR-281.
  12. "Chronic active Epstein-Barr virus infection associated with low expression of leukocyte-associated immunoglobulin-like receptor-1 (LAIR-1) on natural killer cells."
    Aoukaty A., Lee I.-F., Wu J., Tan R.
    J. Clin. Immunol. 23:141-145(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  13. "Mechanisms of hypergammaglobulinemia and impaired antigen-specific humoral immunity in HIV-1 infection."
    De Milito A., Nilsson A., Titanji K., Thorstensson R., Reizenstein E., Narita M., Grutzmeier S., Sonnerborg A., Chiodi F.
    Blood 103:2180-2186(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  14. "Inhibitory receptors CD85j, LAIR-1, and CD152 down-regulate immunoglobulin and cytokine production by human B lymphocytes."
    Merlo A., Tenca C., Fais F., Battini L., Ciccone E., Grossi C.E., Saverino D.
    Clin. Diagn. Lab. Immunol. 12:705-712(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "The inhibitory leukocyte-associated Ig-like receptor-1 (LAIR-1) is expressed at high levels by human naive T cells and inhibits TCR mediated activation."
    Maasho K., Masilamani M., Valas R., Basu S., Coligan J.E., Borrego F.
    Mol. Immunol. 42:1521-1530(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
  16. "Leukocyte-associated Ig-like receptor-1 has SH2 domain-containing phosphatase-independent function and recruits C-terminal Src kinase."
    Verbrugge A., Rijkers E.S.K., de Ruiter T., Meyaard L.
    Eur. J. Immunol. 36:190-198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSK, MUTAGENESIS OF TYR-251 AND TYR-281, FUNCTION.
  17. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69.
    Tissue: Leukemic T-cell.
  18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Crystal structure and collagen-binding site of immune inhibitory receptor LAIR-1: unexpected implications for collagen binding by platelet receptor GPVI."
    Brondijk T.H., de Ruiter T., Ballering J., Wienk H., Lebbink R.J., van Ingen H., Boelens R., Farndale R.W., Meyaard L., Huizinga E.G.
    Blood 115:1364-1373(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-122, INTERACTION WITH COLLAGENS, DISULFIDE BOND.

Entry informationi

Entry nameiLAIR1_HUMAN
AccessioniPrimary (citable) accession number: Q6GTX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: July 19, 2004
Last modified: June 8, 2016
This is version 112 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.