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Protein / target

Mucin-2

Encoded byMUC2Q02817Homo sapiensSwiss-Prot
1
Research papers

Protein at a glance

Biological role

Extracellular matrix structural constituent

Strongest disease association

Vascular Diseases

Via encoding gene MUC2 · Genetic evidence · score 0.56

Research activity

Emerging research

1 papers · latest 2020

Derived from structured UniProt, Open Targets and literature data on this page.

Protein profile

UniProt 2026_02

Canonical identity and biological annotation from UniProt.

Function overview

Coats the epithelia of the intestines and other mucus membrane-containing organs to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces.

View complete UniProt function annotation

Coats the epithelia of the intestines and other mucus membrane-containing organs to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces (PubMed:17058067, PubMed:19432394, PubMed:33031746). Major constituent of the colon mucus, which is mainly formed by large polymeric networks of MUC2 secreted by goblet cells that cover the exposed surfaces of intestine (PubMed:19432394, PubMed:33031746). MUC2 networks form hydrogels that guard the underlying epithelium from pathogens and other hazardous matter entering from the outside world, while permitting nutrient absorption and gas exchange (PubMed:33031746, PubMed:36206754). Acts as a divalent copper chaperone that protects intestinal cells from copper toxicity and facilitates nutritional copper unptake into cells (PubMed:36206754). Binds both Cu(2+) and its reduced form, Cu(1+), at two juxtaposed binding sites: Cu(2+), once reduced to Cu(1+) by vitamin C (ascorbate) or other dietary antioxidants, transits to the other binding site (PubMed:36206754). MUC2-bound Cu(1+) is protected from oxidation in aerobic environments, and can be released for nutritional delivery to cells (PubMed:36206754). Mucin gels store antimicrobial molecules that participate in innate immunity (PubMed:33031746). Mucin glycoproteins also house and feed the microbiome, lubricate tissue surfaces, and may facilitate the removal of contaminants and waste products from the body (PubMed:33031746). Goblet cells synthesize two forms of MUC2 mucin that differ in branched chain O-glycosylation and the site of production in the colon: a (1) 'thick' mucus that wraps the microbiota to form fecal pellets is produced in the proximal, ascending colon (By similarity). 'Thick' mucus transits along the descending colon and is lubricated by a (2) 'thin' MUC2 mucus produced in the distal colon which adheres to the 'thick' mucus (By similarity)

Subcellular location

Secreted
Domains and Gene Ontology detail (21)

Domains & features

VWFD 1TILVWFD 2VWFD 3VWFD 4VWFC 1VWFC 2CTCK

Gene Ontology

  • Cextracellular matrix
  • CGolgi lumen
  • Cinner mucus layer
  • Cmucus layer
  • Couter mucus layer
  • Cplasma membrane
  • Fcupric ion binding
  • Fcuprous ion binding
  • Fextracellular matrix structural constituent
  • Pdetoxification of copper ion
  • Phost-mediated modulation of intestinal microbiota composition
  • Pmaintenance of gastrointestinal epithelium

5289 aa · 551 kDa

Biological roles

What this protein does, drawn together from its UniProt function, Gene Ontology terms and Reactome pathways.

Cell adhesionGO
View supporting evidence

Cell adhesion

  • ·extracellular matrix
  • ·extracellular matrix structural constituent

Concepts derived from UniProt GO Reactome — each badge above shows which sources supported that role.

Translational evidence

Open Targets 26

Why this target matters therapeutically, strongest evidence first. Disease associations are gene-level (via the gene that encodes this protein) and open into the full confidence synthesis; the development universe, tractability and safety annotations are target-level, from Open Targets.

Strongest disease associations · via encoding gene MUC2

Gene-level evidence surfaced through the gene MUC2that encodes this protein — not a direct protein–disease relationship. Ranked by Forefront's causal-directness weighting, so genetically- and clinically-evidenced diseases lead over ones that merely share the literature.

Vascular Diseases
0.56Moderately supported

Genetic evidence dominant · Open Targets 0.34

Kidney Diseases
0.46Limited support

Genetic evidence dominant · Open Targets 0.28

Diabetes Mellitus
0.45Limited support

Genetic evidence dominant · Open Targets 0.27

Atrial septal defect
0.36Limited support

Genetic evidence dominant · Open Targets 0.22

Lung Diseases, Interstitial
0.35Limited support

Genetic evidence dominant · Open Targets 0.21

View evidence synthesis (5)
Vascular DiseasesModerately supported
0.56
agreement 0.440.68
Genetic100%

Open Targets aggregate 0.34 · 1 independent evidence family

Kidney DiseasesLimited support
0.46
agreement 0.340.58
Genetic100%

Open Targets aggregate 0.28 · 1 independent evidence family

Diabetes MellitusLimited support
0.45
agreement 0.310.59
Genetic95%Literature5%

Open Targets aggregate 0.27 · 2 independent evidence families

Atrial septal defectLimited support
0.36
agreement 0.240.48
Genetic100%

Open Targets aggregate 0.22 · 1 independent evidence family

Lung Diseases, InterstitialLimited support
0.35
agreement 0.210.49
Genetic92%Literature8%

Open Targets aggregate 0.21 · 2 independent evidence families

The evidence agreement range shows how closely the independent evidence families agree — it is not a statistical confidence interval, and nothing here is fitted to outcome data. Derived from Open Targets evidence types under Forefront weighting; the per-type scores above show the calculation.

Show all associations
Vascular Diseases0.34
Kidney Diseases0.28
Diabetes Mellitus0.27
Atrial septal defect0.22
Lung Diseases, Interstitial0.21
Idiopathic Pulmonary Fibrosis0.14
Asthma0.12
Colorectal Neoplasms0.11
Neoplasms0.11

Research activity

1 papers · to 2020

Papers linked directly to this protein. This is the protein's own literature — descriptor-derived papers are kept separate below.

Most cited

Recent

Europe PMC papers linked directly to this protein.

Related family literature

7

Papers about “Mucins” — a broader family this protein belongs to. Shown as context; not counted as papers specifically about this protein.

Mucus Structure, Viscoelastic Properties, and Composition in Chronic Respiratory Diseases.

Abrami M · International journal of molecular sciences · 2024

via Mucins

MUC1 and MUC16: critical for immune modulation in cancer therapeutics.

Chen X · Frontiers in immunology · 2024

via Mucins

Mucins and the Microbiome.

Hansson GC · Annual review of biochemistry · 2020

via Mucins

Intestinal goblet cells and mucins in health and disease: recent insights and progress.

Kim YS · Current gastroenterology reports · 2010

via Mucins

Europe PMC literature, reached through curated HGNC family membership. Membership is a taxonomic relationship — it does not imply this protein participates in every mechanism these papers discuss.