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MMP1 (Interstitial collagenase) is an enzyme. The public catalogues list it as a drug target and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to HR-positive / HER2-negative breast cancer.
Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.
CIViC holds 1 clinical evidence item and 0 assertions across 1 variant, naming Sacituzumab Govitecan.
In plain words · MMP1 (Interstitial collagenase) is an enzyme. The public catalogues list it as a drug target and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to HR-positive / HER2-negative breast cancer.
MMP1 (Interstitial collagenase) is an enzyme. The public catalogues list it as a drug target and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to HR-positive / HER2-negative breast cancer.
Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X.
No product in this corpus aims at MMP1 yet. Inhibitors are shaped to fit the enzyme's active site so the reaction the cancer relies on stops.
Specificity not established: no corpus medicine is aimed at it and the catalogues give it only the roles drug-target, biomarker; HPA finds the RNA tissue enhanced, which says where the protein sits but not whether the tumour differs from normal tissue. HPA MMP1: RNA tissue enhanced (gallbladder 71 nTPM, stomach 1 44 nTPM, urinary bladder 49 nTPM); no normal tissue stained high. Distribution: 1 cancer family in the corpus carries a prevalence row, label threshold or catalogue link for it (Breast cancer (all types)); Open Targets associates it with 0 specific cancer types at or above 0.5. (No rule of scripts/fetch-target-specificity.ts fired.)
Sources: Human Protein Atlas MMP1 tissue; Open Targets ENSG00000196611 associations
First described 1986. Earliest sequence paper UniProt cites for the protein: Whitham S.E. et al, Biochem. J, 1986, "Comparison of human stromelysin and collagenase by cloning and sequence analysis". Source.
Sources: HGNC HGNC:7155 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt P03956 (protein name, function text, keywords and locations (REST API)); CIViC gene MMP1 (1 evidence items, 0 assertions, 1 variants; diseases: Oestrogen Receptor-positive Breast Cancer (GraphQL API, CC0))
Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity. Location: Secreted, extracellular space, extracellular matrix (UniProt). Locus 11q22.2 (HGNC).
RNA: tissue enhanced (gallbladder 71 nTPM, stomach 1 44 nTPM, urinary bladder 49 nTPM), detected in some normal tissues.
No normal tissue stained high.
RNA cancer enhanced: Head and Neck Squamous Cell Carcinoma 496 pTPM.
No cancer sample stained medium or high.
Human Protein Atlas version 25.1, antibody staining at reliability approved, enhanced or supported; used under CC BY-SA 3.0. Staining counts are patients per level in the atlas cohort, not population prevalence.
Query for this target: (TITLE:"MMP1" OR ABSTRACT:"MMP1" OR TITLE:"matrix metallopeptidase 1" OR ABSTRACT:"matrix metallopeptidase 1" OR TITLE:"Interstitial collagenase" OR ABSTRACT:"Interstitial collagenase") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about MMP1, not a curated reading list.