SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P45452

- MMP13_HUMAN

UniProt

P45452 - MMP13_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Collagenase 3

Gene
MMP13
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 CTGF. 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 CTGF. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.12 Publications

Cofactori

Calcium. Can bind about 5 calcium ions per subunit.9 Publications
Binds 2 zinc ions per subunit.9 Publications

Enzyme regulationi

Inhibited by TIMP1, TIMP2 and TIMP3. Inhibited by acetohydroxamic acid and other zinc chelators.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi96 – 961Zinc 2; in inhibited form By similarity
Metal bindingi128 – 1281Calcium 1
Metal bindingi162 – 1621Calcium 2; via carbonyl oxygen
Metal bindingi172 – 1721Zinc 1; via tele nitrogen
Metal bindingi174 – 1741Zinc 1
Metal bindingi179 – 1791Calcium 3
Metal bindingi180 – 1801Calcium 3; via carbonyl oxygen
Metal bindingi182 – 1821Calcium 3; via carbonyl oxygen
Metal bindingi184 – 1841Calcium 3; via carbonyl oxygen
Metal bindingi187 – 1871Zinc 1; via tele nitrogen
Metal bindingi194 – 1941Calcium 2; via carbonyl oxygen
Metal bindingi196 – 1961Calcium 2; via carbonyl oxygen
Metal bindingi198 – 1981Calcium 2
Metal bindingi200 – 2001Zinc 1; via pros nitrogen
Metal bindingi202 – 2021Calcium 3
Metal bindingi203 – 2031Calcium 1
Metal bindingi205 – 2051Calcium 1; via carbonyl oxygen
Metal bindingi205 – 2051Calcium 3
Metal bindingi222 – 2221Zinc 2; via tele nitrogen; catalytic
Active sitei223 – 2231 Inferred
Metal bindingi226 – 2261Zinc 2; via tele nitrogen; catalytic
Metal bindingi232 – 2321Zinc 2; via tele nitrogen; catalytic
Metal bindingi240 – 2401Zinc 2; via carbonyl oxygen; catalytic
Metal bindingi291 – 2911Calcium 4; via carbonyl oxygen
Metal bindingi293 – 2931Calcium 5; via carbonyl oxygen
Metal bindingi335 – 3351Calcium 4; via carbonyl oxygen
Metal bindingi337 – 3371Calcium 5; via carbonyl oxygen
Metal bindingi383 – 3831Calcium 4; via carbonyl oxygen
Metal bindingi385 – 3851Calcium 5; via carbonyl oxygen
Metal bindingi432 – 4321Calcium 4; via carbonyl oxygen
Metal bindingi434 – 4341Calcium 5; via carbonyl oxygen

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. collagen binding Source: UniProtKB
  3. metalloendopeptidase activity Source: UniProtKB
  4. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. bone mineralization Source: Ensembl
  2. bone morphogenesis Source: UniProtKB
  3. cartilage development Source: Ensembl
  4. cellular protein metabolic process Source: Ensembl
  5. collagen catabolic process Source: UniProtKB
  6. extracellular matrix disassembly Source: UniProtKB
  7. extracellular matrix organization Source: Reactome
  8. proteolysis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.
REACT_222620. Collagen degradation.

Protein family/group databases

MEROPSiM10.013.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagenase 3 (EC:3.4.24.-)
Alternative name(s):
Matrix metalloproteinase-13
Short name:
MMP-13
Gene namesi
Name:MMP13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:7159. MMP13.

Subcellular locationi

Secretedextracellular spaceextracellular matrix Inferred. Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: ProtInc
  3. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Spondyloepimetaphyseal dysplasia Missouri type (SEMD-MO) [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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti75 – 751F → S in SEMD-MO; abnormal intracellular autoactivation and autodegradation within the ER/Golgi resulting in the secretion of small and inactive fragments. 1 Publication
VAR_032753
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti74 – 741F → S in MANDP1. 1 Publication
VAR_063432
Natural varianti91 – 911M → T in MANDP1. 1 Publication
VAR_063433
Natural varianti232 – 2321H → N in MANDP1. 1 Publication
VAR_063434

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi223 – 2231E → A: Abolishes enzyme activity. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi602111. phenotype.
Orphaneti1040. Metaphyseal anadysplasia.
93356. Spondyloepimetaphyseal dysplasia, Missouri type.
PharmGKBiPA30871.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Propeptidei20 – 10384Activation peptidePRO_0000028788Add
BLAST
Chaini104 – 471368Collagenase 3PRO_0000028789Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi117 – 1171N-linked (GlcNAc...)1 Publication
Glycosylationi152 – 1521N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi284 ↔ 4712 Publications

Post-translational modificationi

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).
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP45452.
PRIDEiP45452.

PTM databases

PhosphoSiteiP45452.

Miscellaneous databases

PMAP-CutDBP45452.

Expressioni

Tissue specificityi

Detected in fetal cartilage and calvaria, in chondrocytes of hypertrophic cartilage in vertebrae and in the dorsal end of ribs undergoing ossification, as well as in osteoblasts and periosteal cells below the inner periosteal region of ossified ribs. Detected in chondrocytes from in joint cartilage that have been treated with TNF and IL1B, but not in untreated chondrocytes. Detected in T lymphocytes. Detected in breast carcinoma tissue.4 Publications

Inductioni

Up-regulated by TNF and IL1B.5 Publications

Gene expression databases

ArrayExpressiP45452.
BgeeiP45452.
CleanExiHS_MMP13.
GenevestigatoriP45452.

Interactioni

Subunit structurei

Monomer. Interacts with TIMP1, TIMP2 and TIMP3. Binds (via the C-terminal region) to collagen.4 Publications

Protein-protein interaction databases

BioGridi110465. 1 interaction.
STRINGi9606.ENSP00000260302.

Structurei

Secondary structure

1
471
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni34 – 374
Helixi38 – 414
Beta strandi44 – 485
Beta strandi109 – 1113
Beta strandi116 – 1227
Beta strandi127 – 1293
Helixi131 – 14616
Beta strandi148 – 1503
Beta strandi152 – 1554
Beta strandi157 – 1593
Beta strandi162 – 1687
Beta strandi173 – 1753
Beta strandi180 – 1834
Beta strandi186 – 1883
Beta strandi191 – 1933
Turni194 – 1974
Beta strandi199 – 2024
Beta strandi207 – 2159
Helixi216 – 22813
Beta strandi235 – 2373
Beta strandi241 – 2433
Beta strandi249 – 2513
Helixi256 – 26611
Beta strandi291 – 2966
Beta strandi299 – 3046
Beta strandi307 – 3115
Beta strandi313 – 3164
Beta strandi319 – 3224
Helixi323 – 3264
Beta strandi335 – 3406
Helixi341 – 3433
Beta strandi345 – 3506
Beta strandi353 – 3586
Beta strandi367 – 3693
Helixi370 – 3734
Beta strandi384 – 3874
Turni389 – 3913
Beta strandi393 – 3986
Beta strandi401 – 4066
Turni407 – 4104
Helixi420 – 4234
Beta strandi432 – 4376
Beta strandi440 – 4456
Beta strandi448 – 4536
Turni454 – 4574
Beta strandi458 – 4647
Helixi465 – 4695

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EUBNMR-A104-274[»]
1FLSNMR-A104-268[»]
1FM1NMR-A104-268[»]
1PEXX-ray2.70A265-471[»]
1UC1model-A1-471[»]
1XUCX-ray1.70A/B104-274[»]
1XUDX-ray1.80A/B104-274[»]
1XURX-ray1.85A/B104-274[»]
1YOUX-ray2.30A/B104-271[»]
1ZTQX-ray2.00A/B/C/D104-268[»]
2D1NX-ray2.37A/B104-269[»]
2E2DX-ray2.00A104-268[»]
2OW9X-ray1.74A/B104-270[»]
2OZRX-ray2.30A/B/C/D/E/F/G/H104-270[»]
2PJTX-ray2.80A/B/C/D104-268[»]
2YIGX-ray1.70A/B104-274[»]
3ELMX-ray1.90A/B104-274[»]
3I7GX-ray1.95A/B104-274[»]
3I7IX-ray2.21A/B104-274[»]
3KECX-ray2.05A/B105-267[»]
3KEJX-ray2.30A/B104-270[»]
3KEKX-ray1.97A/B104-270[»]
3KRYX-ray1.90A/B/C/D104-267[»]
3LJZX-ray2.00A/B/C/D104-267[»]
3O2XX-ray1.90A/B/C/D105-267[»]
3TVCX-ray2.43A104-272[»]
3ZXHX-ray1.30A/B104-274[»]
456CX-ray2.40A/B104-271[»]
4A7BX-ray2.20A/B104-272[»]
4FU4X-ray2.85A/B104-471[»]
C/D25-50[»]
4FVLX-ray2.44A/B104-471[»]
C/D31-50[»]
4G0DX-ray2.54A/B/C/D104-471[»]
W/X/Y/Z25-50[»]
4JP4X-ray1.43A/B103-274[»]
4JPAX-ray2.00A/B103-274[»]
830CX-ray1.60A/B104-271[»]
ProteinModelPortaliP45452.
SMRiP45452. Positions 25-471.

Miscellaneous databases

EvolutionaryTraceiP45452.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati281 – 33050Hemopexin 1Add
BLAST
Repeati331 – 37747Hemopexin 2Add
BLAST
Repeati379 – 42749Hemopexin 3Add
BLAST
Repeati428 – 47144Hemopexin 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni176 – 24671Interaction with TIMP2Add
BLAST
Regioni268 – 471204Interaction with collagenAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi94 – 1018Cysteine switch By similarity

Domaini

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme By similarity.1 Publication
The C-terminal region binds to collagen.1 Publication

Sequence similaritiesi

Belongs to the peptidase M10A family.
Contains 4 hemopexin repeats.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG299356.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
KOiK07994.
OMAiELRGEKM.
PhylomeDBiP45452.
TreeFamiTF315428.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR028711. Collagenase_3.
IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF130. PTHR10201:SF130. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P45452-1 [UniParc]FASTAAdd to Basket

« Hide

MHPGVLAAFL FLSWTHCRAL PLPSGGDEDD LSEEDLQFAE RYLRSYYHPT    50
NLAGILKENA ASSMTERLRE MQSFFGLEVT GKLDDNTLDV MKKPRCGVPD 100
VGEYNVFPRT LKWSKMNLTY RIVNYTPDMT HSEVEKAFKK AFKVWSDVTP 150
LNFTRLHDGI ADIMISFGIK EHGDFYPFDG PSGLLAHAFP PGPNYGGDAH 200
FDDDETWTSS SKGYNLFLVA AHEFGHSLGL DHSKDPGALM FPIYTYTGKS 250
HFMLPDDDVQ GIQSLYGPGD EDPNPKHPKT PDKCDPSLSL DAITSLRGET 300
MIFKDRFFWR LHPQQVDAEL FLTKSFWPEL PNRIDAAYEH PSHDLIFIFR 350
GRKFWALNGY DILEGYPKKI SELGLPKEVK KISAAVHFED TGKTLLFSGN 400
QVWRYDDTNH IMDKDYPRLI EEDFPGIGDK VDAVYEKNGY IYFFNGPIQF 450
EYSIWSNRIV RVMPANSILW C 471
Length:471
Mass (Da):53,820
Last modified:November 1, 1995 - v1
Checksum:iE110F50628B57B60
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21H → L.
Corresponds to variant rs554797 [ dbSNP | Ensembl ].
VAR_011971
Natural varianti74 – 741F → S in MANDP1. 1 Publication
VAR_063432
Natural varianti75 – 751F → S in SEMD-MO; abnormal intracellular autoactivation and autodegradation within the ER/Golgi resulting in the secretion of small and inactive fragments. 1 Publication
VAR_032753
Natural varianti91 – 911M → T in MANDP1. 1 Publication
VAR_063433
Natural varianti232 – 2321H → N in MANDP1. 1 Publication
VAR_063434
Natural varianti390 – 3901D → G.1 Publication
Corresponds to variant rs17860568 [ dbSNP | Ensembl ].
VAR_020534

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471D → G in BAF84900. 1 Publication
Sequence conflicti278 – 2781P → L in AAH67523. 1 Publication
Sequence conflicti438 – 4381N → D in BAG37740. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75308 mRNA. Translation: CAA53056.1.
X81334 mRNA. Translation: CAA57108.1.
AK292211 mRNA. Translation: BAF84900.1.
AK315341 mRNA. Translation: BAG37740.1.
AY741163 Genomic DNA. Translation: AAU13907.1.
BC067522 mRNA. Translation: AAH67522.1.
BC067523 mRNA. Translation: AAH67523.1.
BC074807 mRNA. Translation: AAH74807.1.
BC074808 mRNA. Translation: AAH74808.1.
CCDSiCCDS8324.1.
PIRiA53711.
RefSeqiNP_002418.1. NM_002427.3.
UniGeneiHs.2936.

Genome annotation databases

EnsembliENST00000260302; ENSP00000260302; ENSG00000137745.
ENST00000571284; ENSP00000461440; ENSG00000262325.
GeneIDi4322.
KEGGihsa:4322.
UCSCiuc001phl.3. human.

Polymorphism databases

DMDMi1168998.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75308 mRNA. Translation: CAA53056.1 .
X81334 mRNA. Translation: CAA57108.1 .
AK292211 mRNA. Translation: BAF84900.1 .
AK315341 mRNA. Translation: BAG37740.1 .
AY741163 Genomic DNA. Translation: AAU13907.1 .
BC067522 mRNA. Translation: AAH67522.1 .
BC067523 mRNA. Translation: AAH67523.1 .
BC074807 mRNA. Translation: AAH74807.1 .
BC074808 mRNA. Translation: AAH74808.1 .
CCDSi CCDS8324.1.
PIRi A53711.
RefSeqi NP_002418.1. NM_002427.3.
UniGenei Hs.2936.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EUB NMR - A 104-274 [» ]
1FLS NMR - A 104-268 [» ]
1FM1 NMR - A 104-268 [» ]
1PEX X-ray 2.70 A 265-471 [» ]
1UC1 model - A 1-471 [» ]
1XUC X-ray 1.70 A/B 104-274 [» ]
1XUD X-ray 1.80 A/B 104-274 [» ]
1XUR X-ray 1.85 A/B 104-274 [» ]
1YOU X-ray 2.30 A/B 104-271 [» ]
1ZTQ X-ray 2.00 A/B/C/D 104-268 [» ]
2D1N X-ray 2.37 A/B 104-269 [» ]
2E2D X-ray 2.00 A 104-268 [» ]
2OW9 X-ray 1.74 A/B 104-270 [» ]
2OZR X-ray 2.30 A/B/C/D/E/F/G/H 104-270 [» ]
2PJT X-ray 2.80 A/B/C/D 104-268 [» ]
2YIG X-ray 1.70 A/B 104-274 [» ]
3ELM X-ray 1.90 A/B 104-274 [» ]
3I7G X-ray 1.95 A/B 104-274 [» ]
3I7I X-ray 2.21 A/B 104-274 [» ]
3KEC X-ray 2.05 A/B 105-267 [» ]
3KEJ X-ray 2.30 A/B 104-270 [» ]
3KEK X-ray 1.97 A/B 104-270 [» ]
3KRY X-ray 1.90 A/B/C/D 104-267 [» ]
3LJZ X-ray 2.00 A/B/C/D 104-267 [» ]
3O2X X-ray 1.90 A/B/C/D 105-267 [» ]
3TVC X-ray 2.43 A 104-272 [» ]
3ZXH X-ray 1.30 A/B 104-274 [» ]
456C X-ray 2.40 A/B 104-271 [» ]
4A7B X-ray 2.20 A/B 104-272 [» ]
4FU4 X-ray 2.85 A/B 104-471 [» ]
C/D 25-50 [» ]
4FVL X-ray 2.44 A/B 104-471 [» ]
C/D 31-50 [» ]
4G0D X-ray 2.54 A/B/C/D 104-471 [» ]
W/X/Y/Z 25-50 [» ]
4JP4 X-ray 1.43 A/B 103-274 [» ]
4JPA X-ray 2.00 A/B 103-274 [» ]
830C X-ray 1.60 A/B 104-271 [» ]
ProteinModelPortali P45452.
SMRi P45452. Positions 25-471.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110465. 1 interaction.
STRINGi 9606.ENSP00000260302.

Chemistry

BindingDBi P45452.
ChEMBLi CHEMBL2111422.
GuidetoPHARMACOLOGYi 1637.

Protein family/group databases

MEROPSi M10.013.

PTM databases

PhosphoSitei P45452.

Polymorphism databases

DMDMi 1168998.

Proteomic databases

PaxDbi P45452.
PRIDEi P45452.

Protocols and materials databases

DNASUi 4322.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260302 ; ENSP00000260302 ; ENSG00000137745 .
ENST00000571284 ; ENSP00000461440 ; ENSG00000262325 .
GeneIDi 4322.
KEGGi hsa:4322.
UCSCi uc001phl.3. human.

Organism-specific databases

CTDi 4322.
GeneCardsi GC11M102847.
HGNCi HGNC:7159. MMP13.
MIMi 600108. gene.
602111. phenotype.
neXtProti NX_P45452.
Orphaneti 1040. Metaphyseal anadysplasia.
93356. Spondyloepimetaphyseal dysplasia, Missouri type.
PharmGKBi PA30871.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG299356.
HOGENOMi HOG000217927.
HOVERGENi HBG052484.
KOi K07994.
OMAi ELRGEKM.
PhylomeDBi P45452.
TreeFami TF315428.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.
REACT_222620. Collagen degradation.

Miscellaneous databases

EvolutionaryTracei P45452.
GeneWikii Matrix_metallopeptidase_13.
GenomeRNAii 4322.
NextBioi 17005.
PMAP-CutDB P45452.
PROi P45452.
SOURCEi Search...

Gene expression databases

ArrayExpressi P45452.
Bgeei P45452.
CleanExi HS_MMP13.
Genevestigatori P45452.

Family and domain databases

Gene3Di 2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR028711. Collagenase_3.
IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view ]
PANTHERi PTHR10201:SF130. PTHR10201:SF130. 1 hit.
Pfami PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSi PR00138. MATRIXIN.
SMARTi SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas."
    Freije J.M.P., Diez-Itza I., Balbin M., Sanchez L.M., Blasco R., Tolivia J., Lopez-Otin C.
    J. Biol. Chem. 269:16766-16773(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY.
    Tissue: Mammary carcinoma.
  2. "A matrix metalloproteinase gene expressed in human T lymphocytes is identical with collagenase 3 from breast carcinomas."
    Willmroth F., Peter H.H., Conca W.
    Immunobiology 198:375-384(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Esophagus and Synovium.
  4. NIEHS SNPs program
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-390.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  6. Cited for: PROTEIN SEQUENCE OF 20-27 AND 104-118, PROPEPTIDE, AUTOCATALYTIC PROCESSING, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-117, SUBCELLULAR LOCATION, ENZYME REGULATION, INTERACTION WITH TIMP1; TIMP2 AND TIMP3.
  7. "Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme."
    Knaeuper V., Will H., Lopez-Otin C., Smith B., Atkinson S.J., Stanton H., Hembry R.M., Murphy G.
    J. Biol. Chem. 271:17124-17131(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, PROPEPTIDE, FUNCTION, CATALYTIC ACTIVITY.
  8. "Degradation of cartilage aggrecan by collagenase-3 (MMP-13)."
    Fosang A.J., Last K., Knaeuper V., Murphy G., Neame P.J.
    FEBS Lett. 380:17-20(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Cytokine control of interstitial collagenase and collagenase-3 gene expression in human chondrocytes."
    Borden P., Solymar D., Sucharczuk A., Lindman B., Cannon P., Heller R.A.
    J. Biol. Chem. 271:23577-23581(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, TISSUE SPECIFICITY.
  10. "Collagenase-3 (MMP-13) is expressed by hypertrophic chondrocytes, periosteal cells, and osteoblasts during human fetal bone development."
    Johansson N., Saarialho-Kere U., Airola K., Herva R., Nissinen L., Westermarck J., Vuorio E., Heino J., Kaehaeri V.M.
    Dev. Dyn. 208:387-397(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION BY TGFB1.
  11. "The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction."
    Knaeuper V., Cowell S., Smith B., Lopez-Otin C., O'Shea M., Morris H., Zardi L., Murphy G.
    J. Biol. Chem. 272:7608-7616(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, CATALYTIC ACTIVITY, AUTOCATALYTIC PROCESSING, FUNCTION, INTERACTION WITH TIMP1; TIMP2 AND TIMP3, ENZYME REGULATION.
  12. "The helping hand of collagenase-3 (MMP-13): 2.7 A crystal structure of its C-terminal haemopexin-like domain."
    Gomis-Rueth F.-X., Gohlke U., Betz M., Knaeuper V., Murphy G., Lopez-Otin C., Bode W.
    J. Mol. Biol. 264:556-566(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 265-471 IN COMPLEX WITH CALCIUM, DISULFIDE BOND.
  13. "Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors."
    Lovejoy B., Welch A.R., Carr S., Luong C., Broka C., Hendricks R.T., Campbell J.A., Walker K.A., Martin R., Van Wart H., Browner M.F.
    Nat. Struct. Biol. 6:217-221(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 104-271 IN COMPLEXES WITH SYNTHETIC INHIBITORS; CALCIUM AND ZINC, PROPEPTIDE, AUTOCATALYTIC PROCESSING.
  14. "Solution structure of the catalytic domain of human collagenase-3 (MMP-13) complexed to a potent non-peptidic sulfonamide inhibitor: binding comparison with stromelysin-1 and collagenase-1."
    Zhang X., Gonnella N.C., Koehn J., Pathak N., Ganu V., Melton R., Parker D., Hu S.I., Nam K.Y.
    J. Mol. Biol. 301:513-524(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 104-274 IN COMPLEX WITH CALCIUM AND ZINC.
  15. "High-resolution solution structure of the catalytic fragment of human collagenase-3 (MMP-13) complexed with a hydroxamic acid inhibitor."
    Moy F.J., Chanda P.K., Chen J.M., Cosmi S., Edris W., Levin J.I., Powers R.
    J. Mol. Biol. 302:671-689(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 104-268 IN COMPLEX WITH CALCIUM AND ZINC, CATALYTIC ACTIVITY.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 104-271 IN COMPLEX WITH CALCIUM AND ZINC, COFACTOR, CATALYTIC ACTIVITY.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 104-274 IN COMPLEX WITH CALCIUM AND ZINC, COFACTOR, CATALYTIC ACTIVITY.
  18. "Discovery and characterization of a novel inhibitor of matrix metalloprotease-13 that reduces cartilage damage in vivo without joint fibroplasia side effects."
    Johnson A.R., Pavlovsky A.G., Ortwine D.F., Prior F., Man C.F., Bornemeier D.A., Banotai C.A., Mueller W.T., McConnell P., Yan C., Baragi V., Lesch C., Roark W.H., Wilson M., Datta K., Guzman R., Han H.K., Dyer R.D.
    J. Biol. Chem. 282:27781-27791(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 104-270 IN COMPLEX WITH CALCIUM AND ZINC, COFACTOR, CATALYTIC ACTIVITY, FUNCTION IN CARTILAGE DEGRADATION.
  19. "Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2."
    Maskos K., Lang R., Tschesche H., Bode W.
    J. Mol. Biol. 366:1222-1231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 104-268 IN COMPLEX WITH TIMP2; CALCIUM AND ZINC, INTERACTION WITH TIMP2.
  20. Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 104-274 IN COMPLEX WITH CALCIUM AND ZINC, CATALYTIC ACTIVITY, COFACTOR, FUNCTION.
  21. Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 104-270 IN COMPLEX WITH CALCIUM AND ZINC, CATALYTIC ACTIVITY, COFACTOR.
  22. "Orally active MMP-1 sparing alpha-tetrahydropyranyl and alpha-piperidinyl sulfone matrix metalloproteinase (MMP) inhibitors with efficacy in cancer, arthritis, and cardiovascular disease."
    Becker D.P., Barta T.E., Bedell L.J., Boehm T.L., Bond B.R., Carroll J., Carron C.P., Decrescenzo G.A., Easton A.M., Freskos J.N., Funckes-Shippy C.L., Heron M., Hockerman S., Howard C.P., Kiefer J.R., Li M.H., Mathis K.J., McDonald J.J.
    , Mehta P.P., Munie G.E., Sunyer T., Swearingen C.A., Villamil C.I., Welsch D., Williams J.M., Yu Y., Yao J.
    J. Med. Chem. 53:6653-6680(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 104-267 IN COMPLEX WITH CALCIUM AND ZINC, CATALYTIC ACTIVITY, COFACTOR, FUNCTION.
  23. "Simple pseudo-dipeptides with a P2' glutamate: a novel inhibitor family of matrix metalloproteases and other metzincins."
    Devel L., Beau F., Amoura M., Vera L., Cassar-Lajeunesse E., Garcia S., Czarny B., Stura E.A., Dive V.
    J. Biol. Chem. 287:26647-26656(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF 104-272 IN COMPLEX WITH CALCIUM AND ZINC, COFACTOR, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION.
  24. Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 103-274 IN COMPLEX WITH CALCIUM AND ZINC, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
  25. "Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domain."
    Stura E.A., Visse R., Cuniasse P., Dive V., Nagase H.
    FASEB J. 27:4395-4405(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 104-471 OF MUTANT ALA-223 IN COMPLEX WITH CALCIUM AND ZINC, COFACTOR, DISULFIDE BOND, MUTAGENESIS OF GLU-223, ACTIVE SITE, SUBUNIT.
  26. Cited for: VARIANT SEMD-MO SER-75, CHARACTERIZATION OF VARIANT SEMD-MO SER-75, FUNCTION IN BONE DEVELOPMENT.
  27. "Mutations in MMP9 and MMP13 determine the mode of inheritance and the clinical spectrum of metaphyseal anadysplasia."
    Lausch E., Keppler R., Hilbert K., Cormier-Daire V., Nikkel S., Nishimura G., Unger S., Spranger J., Superti-Furga A., Zabel B.
    Am. J. Hum. Genet. 85:168-178(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MANDP1 SER-74; THR-91 AND ASN-232, FUNCTION IN BONE DEVELOPMENT.

Entry informationi

Entry nameiMMP13_HUMAN
AccessioniPrimary (citable) accession number: P45452
Secondary accession number(s): A8K846, B2RCZ3, Q6NWN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi