Q14165 · MLEC_HUMAN

  • Protein
    Malectin
  • Gene
    MLEC
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Carbohydrate-binding protein with a strong ligand preference for Glc2-N-glycan. May play a role in the early steps of protein N-glycosylation (By similarity).

Features

Showing features for binding site.

129220406080100120140160180200220240260280
TypeIDPosition(s)Description
Binding site82a carbohydrate (UniProtKB | ChEBI)
Binding site104a carbohydrate (UniProtKB | ChEBI)
Binding site131a carbohydrate (UniProtKB | ChEBI)
Binding site132a carbohydrate (UniProtKB | ChEBI)
Binding site201a carbohydrate (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 Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum membrane
Cellular Componentmembrane
Cellular Componentoligosaccharyltransferase complex
Cellular Componentplasma membrane
Cellular Componentspecific granule membrane
Molecular Functioncarbohydrate binding
Molecular Functionenzyme binding
Biological Processprotein N-linked glycosylation

Keywords

Enzyme and pathway databases

Protein family/group databases

    • CBM57Carbohydrate-Binding Module Family 57

Names & Taxonomy

Protein names

  • Recommended name
    Malectin

Gene names

    • Name
      MLEC
    • Synonyms
      KIAA0152

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q14165

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain29-269Lumenal
Transmembrane270-290Helical
Topological domain291-292Cytoplasmic

Keywords

Disease & Variants

Variants

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

The viewer provides 232 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain, modified residue (large scale data), glycosylation.

TypeIDPosition(s)SourceDescription
Signal1-28UniProt
ChainPRO_000001398229-292UniProtMalectin
Modified residue (large scale data)239PRIDEPhosphotyrosine
Glycosylation268UniProtN-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

2D gel databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with the oligosaccharyltransferase (OST) complex.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q14165RPN1 P048433EBI-1046466, EBI-355963

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region221-265Disordered
Compositional bias248-265Polar residues

Sequence similarities

Belongs to the malectin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    292
  • Mass (Da)
    32,234
  • Last updated
    1996-11-01 v1
  • Checksum
    448D673A5A1A8F09
MLGAWAVEGTAVALLRLLLLLLPPAIRGPGLGVAGVAGAAGAGLPESVIWAVNAGGEAHVDVHGIHFRKDPLEGRVGRASDYGMKLPILRSNPEDQILYQTERYNEETFGYEVPIKEEGDYVLVLKFAEVYFAQSQQKVFDVRLNGHVVVKDLDIFDRVGHSTAHDEIIPMSIRKGKLSVQGEVSTFTGKLYIEFVKGYYDNPKVCALYIMAGTVDDVPKLQPHPGLEKKEEEEEEEEYDEGSNLKKQTNKNRVQSGPRTPNPYASDNSSLMFPILVAFGVFIPTLFCLCRL

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H0YG07H0YG07_HUMANMLEC173
F5GX14F5GX14_HUMANMLEC217
F5H1S8F5H1S8_HUMANMLEC146

Sequence caution

The sequence BAA09773.2 differs from that shown. Reason: Erroneous initiation

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias248-265Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D63486
EMBL· GenBank· DDBJ
BAA09773.2
EMBL· GenBank· DDBJ
mRNA Different initiation
BC000371
EMBL· GenBank· DDBJ
AAH00371.1
EMBL· GenBank· DDBJ
mRNA
BC016297
EMBL· GenBank· DDBJ
AAH16297.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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