Q91Y57 · SIG12_MOUSE

  • Protein
    Sialic acid-binding Ig-like lectin 12
  • Gene
    Siglec12
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Putative adhesion molecule that mediates sialic-acid dependent binding to cells. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules.

Features

Showing features for binding site.

146750100150200250300350400450
TypeIDPosition(s)Description
Binding site126N-acetylneuraminate (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentexternal side of plasma membrane
Cellular Componentmembrane
Cellular Componentplasma membrane
Molecular Functionmonosaccharide binding
Molecular Functionsialic acid binding
Biological Processcell adhesion
Biological Processinflammatory response
Biological Processnegative regulation of inflammatory response
Biological Processnegative regulation of phagocytosis, engulfment
Biological Processphagocytosis, engulfment

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Sialic acid-binding Ig-like lectin 12
  • Short names
    Siglec-12
  • Alternative names
    • Myeloid inhibitory siglec (MIS)
    • Sialic acid-binding Ig-like lectin 5 (Siglec-5)
    • Sialic acid-binding Ig-like lectin E (Siglec-E; mSiglec-E)
    • Sialic acid-binding Ig-like lectin-like 1 (Siglec-L1)

Gene names

    • Name
      Siglec12
    • Synonyms
      Siglec5, Siglece, Siglecl1

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q91Y57
  • Secondary accessions
    • E9QMD1

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain19-353Extracellular
Transmembrane354-374Helical
Topological domain375-467Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis432Abolishes binding to PTPN6 and PTPN11.
Mutagenesis455Reduces binding to PTPN6.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 35 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, modified residue.

TypeIDPosition(s)Description
Signal1-18
ChainPRO_000001495419-467Sialic acid-binding Ig-like lectin 12
Disulfide bond40↔176
Disulfide bond45↔108
Glycosylation46N-linked (GlcNAc...) asparagine
Glycosylation167N-linked (GlcNAc...) asparagine
Disulfide bond170↔219
Glycosylation197N-linked (GlcNAc...) asparagine
Glycosylation216N-linked (GlcNAc...) asparagine
Glycosylation227N-linked (GlcNAc...) asparagine
Glycosylation237N-linked (GlcNAc...) asparagine
Glycosylation244N-linked (GlcNAc...) asparagine
Glycosylation262N-linked (GlcNAc...) asparagine
Disulfide bond278↔323
Glycosylation287N-linked (GlcNAc...) asparagine
Glycosylation294N-linked (GlcNAc...) asparagine
Modified residue432Phosphotyrosine
Modified residue455Phosphotyrosine

Post-translational modification

Phosphorylation of Tyr-432 is required for binding to PTPN6 and PTPN11. Phosphorylation of Tyr-455 is involved in binding to PTPN6. Tyr-432 needs to be phosphorylated prior to Tyr-455.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed by monocytic/myeloid lineage cells. Found at higher levels in spleen, liver and heart. Found at lower levels in kidney and lung.

Gene expression databases

Interaction

Subunit

Homodimer; disulfide-linked. Interacts with PTPN6/SHP-1 and PTPN11/SHP-2 upon phosphorylation.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q91Y57Tlr4 Q9QUK63EBI-16826475, EBI-1534575

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain21-141Ig-like V-type
Domain152-239Ig-like C2-type 1
Domain242-339Ig-like C2-type 2
Motif430-435ITIM motif
Motif453-458SLAM-like motif

Domain

Contains 1 copy 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.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    467
  • Mass (Da)
    51,901
  • Last updated
    2011-07-27 v3
  • Checksum
    E220C29755FE21DE
MLLLLLLLLLWGIKGVEGQNPQEVFTLNVERKVVVQEGLCVLVPCNFSYLKKRLTDWTDSDPVHGFWYREGTDRRKDSIVATNNPIRKAVKETRNRFFLLGDPWRNDCSLNIREIRKKDAGLYFFRLERGKTKYNYMWDKMTLVVTALTNTPQILLPETLEAGHPSNLTCSVPWDCGWTAPPIFSWTGTSVSFLSTNTTGSSVLTITPQPQDHGTNLTCQVTLPGTNVSTRMTIRLNVSYAPKNLTVTIYQGADSVSTILKNGSSLPISEGQSLRLICSTDSYPPANLSWSWDNLTLCPSKLSKPGLLELFPVHLKHGGVYTCQAQHALGSQHISLSLSPQSSATLSEMMMGTFVGSGVTALLFLSVCILLLAVRSYRRKPARPAVVAPHPDALKVSVSQNPLVESQADDSSEPLPSILEAAPSSTEEEIHYATLSFHEMKPMNLWGQQDTTTEYSEIKFPQRTAWP

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0U1RPP9A0A0U1RPP9_MOUSESiglece221

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict2in Ref. 2; AAK49917
Sequence conflict24in Ref. 2; AAK49917
Sequence conflict102in Ref. 2; AAK49917
Sequence conflict234in Ref. 1; AAG38598

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF317298
EMBL· GenBank· DDBJ
AAG38598.1
EMBL· GenBank· DDBJ
mRNA
AF329269
EMBL· GenBank· DDBJ
AAK49917.1
EMBL· GenBank· DDBJ
mRNA
AC151989
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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