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Literature summary for 3.4.24.B4 extracted from

  • Lausch, E.; Keppler, R.; Hilbert, K.; Cormier-Daire, V.; Nikkel, S.; Nishimura, G.; Unger, S.; Spranger, J.; Superti-Furga, A.; Zabel, B.
    Mutations in MMP9 and MMP13 determine the mode of inheritance and the clinical spectrum of metaphyseal anadysplasia (2009), Am. J. Hum. Genet., 85, 168-178.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.B4

Activating Compound

Activating Compound Comment Organism Structure
additional information the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13 Mus musculus
additional information the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13 Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant MMP13 in HEK-293 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
F55S naturally occuring dominant mutation and cloning by site-directed mutagenesis, the mutation is involved in metaphyseal anadysplasia Homo sapiens
H213N naturally occuring recessive mutation and cloning by site-directed mutagenesis, the mutation is involved in metaphyseal anadysplasia Homo sapiens
M1K naturally occuring recessive mutation and cloning by site-directed mutagenesis, the mutation is involved in metaphyseal anadysplasia Homo sapiens
M72T naturally occuring dominant mutation and cloning by site-directed mutagenesis, the mutation is involved in metaphyseal anadysplasia Homo sapiens
additional information identification of mutations in MMP13 as the molecular basis of metaphyseal anadysplasia, MAD, overview. Recessive MAD is caused by homozygous loss of function of either MMP9 or MMP13, whereas dominant MAD is associated with missense mutations in the prodomain of MMP13 that determine autoactivation of MMP13 and intracellular degradation of both MMP13 and MMP9, resulting in a double enzymatic deficiency Mus musculus
additional information identification of mutations in MMP13 as the molecular basis of metaphyseal anadysplasia, MAD, overview. Recessive MAD is caused by homozygous loss of function of either MMP9 or MMP13, whereas dominant MAD is associated with missense mutations in the prodomain of MMP13 that determine autoactivation of MMP13 and intracellular degradation of both MMP13 and MMP9, resulting in a double enzymatic deficiency, phenotypes, overview Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular matrix
-
 Mus musculus 31012
-
extracellular matrix
-
 Homo sapiens 31012
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P45452
-
-
Mus musculus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13 Mus musculus
proteolytic modification the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13 Homo sapiens

Synonyms

Synonyms Comment Organism
MMP13
-
 Mus musculus
MMP13
-
 Homo sapiens

General Information

General Information Comment Organism
metabolism the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13 Mus musculus
metabolism the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13 Homo sapiens
physiological function MMP13 catalyzes the degradation of extracellular matrix components in the growth plate and at the same time cleaves and releases biologically active molecules stored in the extracellular matrix, such as the vascular endothelial growth factor A Homo sapiens
physiological function MMP13 catalyzes the degradation of extracellular matrix components in the growth plate and at the same time cleaves and releases biologically active molecules stored in the extracellular matrix, such as the vascular endothelial growth factor A. In mice, ablation of Mmp9, Mmp13, or both Mmp9 and Mmp13 causes severe distortion of the metaphyseal growth plate Mus musculus