MMP13
entrez
4322
canonical
uniprot
P45452
canonical
ensembl
ENSG00000137745
resolver
ensp
ENSP00000260302
resolver
enst
ENST00000260302
resolver
genesymbol
MMP13
resolver
hgnc
HGNC:7159
resolver
uniprot
A8K846
resolver
uniprot
B2RCZ3
resolver
uniprot
Q53H33
resolver
uniprot
Q6NWN6
resolver
uniprot_entry
MMP13_HUMAN
resolver
uniprot_entry
Q53H33_HUMAN
resolver
uniprot_sec
A8K846
resolver
uniprot_sec
B2RCZ3
resolver
uniprot_sec
Q6NWN6
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by TIMP1, TIMP2 and TIMP3. Inhibited by acetohydroxamic acid and other zinc chelators. {ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:8576151, ECO:0000269|PubMed:9065415}.
uniprot
proteins
amino_acid_sequence
MHPGVLAAFLFLSWTHCRALPLPSGGDEDDLSEEDLQFAERYLRSYYHPTNLAGILKENAASSMTERLREMQSFFGLEVTGKLDDNTLDVMKKPRCGVPDVGEYNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMIFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSHDLIFIFRGRKFWALNGYDILEGYPKKISELGLPKEVKKISAAVHFEDTGKTLLFSGNQVWRYDDTNHIMDKDYPRLIEEDFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPANSILWC
uniprot
proteins
disease_involvement
DISEASE: Spondyloepimetaphyseal dysplasia, Missouri type (SEMDM) [MIM:602111]: A bone disease characterized by moderate to severe metaphyseal changes, mild epiphyseal involvement, rhizomelic shortening of the lower limbs with bowing of the femora and/or tibiae, coxa vara, genu varum and pear-shaped vertebrae in childhood. Epimetaphyseal changes improve with age. {ECO:0000269|PubMed:16167086}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Metaphyseal anadysplasia 1 (MANDP1) [MIM:602111]: A bone development disorder characterized by skeletal anomalies that resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia. {ECO:0000269|PubMed:19615667}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Metaphyseal dysplasia, Spahr type (MDST) [MIM:250400]: An autosomal recessive, rare disease characterized by moderate short stature, mild genua vara, and radiographic signs of metaphyseal dysplasia, but no biochemical signs of rickets. {ECO:0000269|PubMed:24648384, ECO:0000269|PubMed:24781753}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion. {ECO:0000269|PubMed:16167086, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:19615667, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:8207000, ECO:0000269|PubMed:8576151, ECO:0000269|PubMed:8603731, ECO:0000269|PubMed:8663255, ECO:0000269|PubMed:9065415}.
uniprot
proteins
mass_dalton
53820
uniprot
proteins
mutagenesis
MUTAGEN 223; /note="E->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:23913860
uniprot
proteins
post_translational_modification
PTM: The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro).; PTM: N-glycosylated. {ECO:0000269|PubMed:8576151}.; PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000269|PubMed:25171405}.
uniprot
proteins
protein_family
Peptidase M10A family
uniprot
proteins
pubmed
10074939
uniprot
proteins
pubmed
10926524
uniprot
proteins
pubmed
10986126
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15734645
uniprot
proteins
pubmed
15780611
uniprot
proteins
pubmed
16167086
uniprot
proteins
pubmed
17196980
uniprot
proteins
pubmed
17623656
uniprot
proteins
pubmed
19422229
uniprot
proteins
pubmed
19615667
uniprot
proteins
pubmed
20005097
uniprot
proteins
pubmed
20726512
uniprot
proteins
pubmed
22689580
uniprot
proteins
pubmed
23810497
uniprot
proteins
pubmed
23913860
uniprot
proteins
pubmed
24648384
uniprot
proteins
pubmed
24781753
uniprot
proteins
pubmed
25171405
uniprot
proteins
pubmed
8207000
uniprot
proteins
pubmed
8576151
uniprot
proteins
pubmed
8603731
uniprot
proteins
pubmed
8663255
uniprot
proteins
pubmed
8798568
uniprot
proteins
pubmed
8969305
uniprot
proteins
pubmed
9056642
uniprot
proteins
pubmed
9065415
uniprot
proteins
pubmed
9562863
uniprot
proteins
sequence_length
471
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:8576151}. Secreted {ECO:0000269|PubMed:8576151}.
uniprot
proteins