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UniProtKB - P39900 (MMP12_HUMAN)
Protein
Macrophage metalloelastase
Gene
MMP12
Organism
Homo sapiens (Human)
Status
Functioni
May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.
Catalytic activityi
- Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin. EC:3.4.24.65
Cofactori
Protein has several cofactor binding sites:Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 92 | Zinc 2; in inhibited formBy similarity | 1 | |
Metal bindingi | 124 | Calcium 1 | 1 | |
Metal bindingi | 158 | Calcium 2 | 1 | |
Metal bindingi | 168 | Zinc 1 | 1 | |
Metal bindingi | 170 | Zinc 1 | 1 | |
Metal bindingi | 175 | Calcium 3 | 1 | |
Metal bindingi | 176 | Calcium 3; via carbonyl oxygen | 1 | |
Metal bindingi | 178 | Calcium 3; via carbonyl oxygen | 1 | |
Metal bindingi | 180 | Calcium 3; via carbonyl oxygen | 1 | |
Metal bindingi | 183 | Zinc 1 | 1 | |
Metal bindingi | 190 | Calcium 2; via carbonyl oxygen | 1 | |
Metal bindingi | 192 | Calcium 2; via carbonyl oxygen | 1 | |
Metal bindingi | 194 | Calcium 2 | 1 | |
Metal bindingi | 196 | Zinc 1 | 1 | |
Metal bindingi | 198 | Calcium 3 | 1 | |
Metal bindingi | 199 | Calcium 1 | 1 | |
Metal bindingi | 201 | Calcium 1 | 1 | |
Metal bindingi | 201 | Calcium 3 | 1 | |
Metal bindingi | 218 | Zinc 2; catalytic | 1 | |
Active sitei | 219 | 1 | ||
Metal bindingi | 222 | Zinc 2; catalytic | 1 | |
Metal bindingi | 228 | Zinc 2; catalytic | 1 | |
Metal bindingi | 289 | Calcium 4; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 333 | Calcium 4; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 381 | Calcium 4; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 430 | Calcium 4; via carbonyl oxygenBy similarity | 1 |
GO - Molecular functioni
- calcium ion binding Source: CAFA
- collagen binding Source: CAFA
- core promoter sequence-specific DNA binding Source: CAFA
- endopeptidase activity Source: UniProtKB
- metalloendopeptidase activity Source: CAFA
- sequence-specific DNA binding Source: CAFA
- serine-type endopeptidase activity Source: Reactome
- zinc ion binding Source: CAFA
GO - Biological processi
- bronchiole development Source: Ensembl
- cellular response to virus Source: Ensembl
- collagen catabolic process Source: GO_Central
- elastin catabolic process Source: ARUK-UCL
- extracellular matrix disassembly Source: Reactome
- extracellular matrix organization Source: GO_Central
- lung alveolus development Source: Ensembl
- negative regulation of endothelial cell-matrix adhesion via fibronectin Source: ARUK-UCL
- negative regulation of transcription by RNA polymerase II Source: Ensembl
- negative regulation of type I interferon-mediated signaling pathway Source: Ensembl
- positive regulation of epithelial cell proliferation involved in wound healing Source: BHF-UCL
- positive regulation of interferon-alpha production Source: Ensembl
- positive regulation of transcription by RNA polymerase II Source: CAFA
- positive regulation of type I interferon-mediated signaling pathway Source: Ensembl
- protein import into nucleus Source: CAFA
- proteolysis Source: CAFA
- regulation of defense response to virus by host Source: Ensembl
- response to amyloid-beta Source: ARUK-UCL
- wound healing, spreading of epidermal cells Source: BHF-UCL
Keywordsi
Molecular function | Hydrolase, Metalloprotease, Protease |
Ligand | Calcium, Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 3.4.24.65, 2681 |
PathwayCommonsi | P39900 |
Reactomei | R-HSA-1442490, Collagen degradation R-HSA-1474228, Degradation of the extracellular matrix |
SignaLinki | P39900 |
SIGNORi | P39900 |
Protein family/group databases
MEROPSi | M10.009 |
Names & Taxonomyi
Protein namesi | Recommended name: Macrophage metalloelastase (EC:3.4.24.65)Short name: MME Alternative name(s): Macrophage elastase Short name: ME Short name: hME Matrix metalloproteinase-12 Short name: MMP-12 |
Gene namesi | Name:MMP12 Synonyms:HME |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:7158, MMP12 |
MIMi | 601046, gene |
neXtProti | NX_P39900 |
VEuPathDBi | HostDB:ENSG00000262406 |
Subcellular locationi
Extracellular region or secreted
- extracellular matrix Curated
Extracellular region or secreted
- extracellular region Source: Reactome
- extracellular space Source: CAFA
Nucleus
- nucleus Source: CAFA
Other locations
- cytoplasm Source: CAFA
- extracellular matrix Source: InterPro
Keywords - Cellular componenti
Extracellular matrix, SecretedPathology & Biotechi
Organism-specific databases
DisGeNETi | 4321 |
OpenTargetsi | ENSG00000262406 |
PharmGKBi | PA30870 |
Miscellaneous databases
Pharosi | P39900, Tchem |
Chemistry databases
ChEMBLi | CHEMBL4393 |
DrugBanki | DB07026, (1S,5S,7R)-N~7~-(BIPHENYL-4-YLMETHYL)-N~3~-HYDROXY-6,8-DIOXA-3-AZABICYCLO[3.2.1]OCTANE-3,7-DICARBOXAMIDE DB07921, 2-[(4-fluorophenyl)sulfonylamino]-N-oxo-ethanamide DB04405, 2-[2-(1,3-Dioxo-1,3-Dihydro-2h-Isoindol-2-Yl)Ethyl]-4-(4'-Ethoxy-1,1'-Biphenyl-4-Yl)-4-Oxobutanoic Acid DB00551, Acetohydroxamic acid DB05387, AE-941 DB03880, Batimastat DB07556, CGS-27023 DB02118, CP-271485 DB00786, Marimastat DB07446, N-(biphenyl-4-ylsulfonyl)-D-leucine DB07683, N-(dibenzo[b,d]thiophen-3-ylsulfonyl)-L-valine DB08599, N-[(4-methoxyphenyl)sulfonyl]-D-alanine DB08271, N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID DB07922, N-oxo-2-(phenylsulfonylamino)ethanamide DB07920, N-oxo-2-[(4-phenylphenyl)sulfonylamino]ethanamide DB03367, PF-00356231 DB00013, Urokinase |
DrugCentrali | P39900 |
GuidetoPHARMACOLOGYi | 1636 |
Genetic variation databases
BioMutai | MMP12 |
DMDMi | 729179 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 16 | CuratedAdd BLAST | 16 | |
PropeptideiPRO_0000028776 | 17 – 105 | Activation peptideBy similarityAdd BLAST | 89 | |
ChainiPRO_0000028777 | 106 – 470 | Macrophage metalloelastaseAdd BLAST | 365 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 20 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 282 ↔ 470 | By similarity | ||
Glycosylationi | 285 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Keywords - PTMi
Disulfide bond, Glycoprotein, ZymogenProteomic databases
jPOSTi | P39900 |
MassIVEi | P39900 |
PeptideAtlasi | P39900 |
PRIDEi | P39900 |
ProteomicsDBi | 55327 |
TopDownProteomicsi | P39900 |
PTM databases
GlyGeni | P39900, 2 sites |
iPTMneti | P39900 |
PhosphoSitePlusi | P39900 |
Expressioni
Tissue specificityi
Found in alveolar macrophages but not in peripheral blood monocytes.
Inductioni
By exposure to bacterial lipopolysaccharides (LPS). Inhibited by dexamethasone.
Gene expression databases
Bgeei | ENSG00000262406, Expressed in amniotic fluid and 102 other tissues |
Genevisiblei | P39900, HS |
Organism-specific databases
HPAi | ENSG00000262406, Tissue enhanced (intestine, lymphoid tissue, urinary bladder) |
Interactioni
Protein-protein interaction databases
BioGRIDi | 110464, 3 interactors |
IntActi | P39900, 2 interactors |
MINTi | P39900 |
STRINGi | 9606.ENSP00000458585 |
Chemistry databases
BindingDBi | P39900 |
Miscellaneous databases
RNActi | P39900, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P39900 |
BMRBi | P39900 |
SASBDBi | P39900 |
SMRi | P39900 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P39900 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 279 – 328 | Hemopexin 1Add BLAST | 50 | |
Repeati | 329 – 375 | Hemopexin 2Add BLAST | 47 | |
Repeati | 377 – 425 | Hemopexin 3Add BLAST | 49 | |
Repeati | 426 – 470 | Hemopexin 4Add BLAST | 45 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 90 – 97 | Cysteine switchBy similarity | 8 |
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.
Sequence similaritiesi
Belongs to the peptidase M10A family.Curated
Keywords - Domaini
Repeat, SignalPhylogenomic databases
eggNOGi | KOG1565, Eukaryota |
GeneTreei | ENSGT00940000162085 |
HOGENOMi | CLU_015489_6_0_1 |
InParanoidi | P39900 |
OMAi | VDNQYWR |
OrthoDBi | 1075463at2759 |
PhylomeDBi | P39900 |
Family and domain databases
CDDi | cd00094, HX, 1 hit cd04278, ZnMc_MMP, 1 hit |
Gene3Di | 2.110.10.10, 1 hit 3.40.390.10, 1 hit |
InterProi | View protein in InterPro IPR000585, Hemopexin-like_dom IPR036375, Hemopexin-like_dom_sf IPR018487, Hemopexin-like_repeat IPR018486, Hemopexin_CS IPR033739, M10A_MMP IPR024079, MetalloPept_cat_dom_sf IPR001818, Pept_M10_metallopeptidase IPR021190, Pept_M10A IPR021158, Pept_M10A_Zn_BS IPR006026, Peptidase_Metallo IPR002477, Peptidoglycan-bd-like IPR036365, PGBD-like_sf |
Pfami | View protein in Pfam PF00045, Hemopexin, 4 hits PF00413, Peptidase_M10, 1 hit PF01471, PG_binding_1, 1 hit |
PIRSFi | PIRSF001191, Peptidase_M10A_matrix, 1 hit |
PRINTSi | PR00138, MATRIXIN |
SMARTi | View protein in SMART SM00120, HX, 4 hits SM00235, ZnMc, 1 hit |
SUPFAMi | SSF47090, SSF47090, 1 hit SSF50923, SSF50923, 1 hit |
PROSITEi | View protein in PROSITE PS00546, CYSTEINE_SWITCH, 1 hit PS00024, HEMOPEXIN, 1 hit PS51642, HEMOPEXIN_2, 4 hits PS00142, ZINC_PROTEASE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P39900-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFGERYLEKF YGLEINKLPV
60 70 80 90 100
TKMKYSGNLM KEKIQEMQHF LGLKVTGQLD TSTLEMMHAP RCGVPDVHHF
110 120 130 140 150
REMPGGPVWR KHYITYRINN YTPDMNREDV DYAIRKAFQV WSNVTPLKFS
160 170 180 190 200
KINTGMADIL VVFARGAHGD FHAFDGKGGI LAHAFGPGSG IGGDAHFDED
210 220 230 240 250
EFWTTHSGGT NLFLTAVHEI GHSLGLGHSS DPKAVMFPTY KYVDINTFRL
260 270 280 290 300
SADDIRGIQS LYGDPKENQR LPNPDNSEPA LCDPNLSFDA VTTVGNKIFF
310 320 330 340 350
FKDRFFWLKV SERPKTSVNL ISSLWPTLPS GIEAAYEIEA RNQVFLFKDD
360 370 380 390 400
KYWLISNLRP EPNYPKSIHS FGFPNFVKKI DAAVFNPRFY RTYFFVDNQY
410 420 430 440 450
WRYDERRQMM DPGYPKLITK NFQGIGPKID AVFYSKNKYY YFFQGSNQFE
460 470
YDFLLQRITK TLKSNSWFGC
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_021343 | 357 | N → S2 PublicationsCorresponds to variant dbSNP:rs652438Ensembl. | 1 | |
Natural variantiVAR_021344 | 469 | G → R1 PublicationCorresponds to variant dbSNP:rs28381701Ensembl. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L23808 mRNA Translation: AAA58658.1 Sequence problems. AY856072 Genomic DNA Translation: AAW29944.1 AK313959 mRNA Translation: BAG36675.1 CH471065 Genomic DNA Translation: EAW67033.1 BC112301 mRNA Translation: AAI12302.1 BC143773 mRNA Translation: AAI43774.1 |
CCDSi | CCDS73375.1 |
PIRi | A49499 |
RefSeqi | NP_002417.2, NM_002426.5 |
Genome annotation databases
Ensembli | ENST00000571244.3; ENSP00000458585.1; ENSG00000262406.3 |
GeneIDi | 4321 |
KEGGi | hsa:4321 |
MANE-Selecti | ENST00000571244.3; ENSP00000458585.1; NM_002426.6; NP_002417.2 |
UCSCi | uc031yde.2, human |
Similar proteinsi
Cross-referencesi
Web resourcesi
NIEHS-SNPs |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L23808 mRNA Translation: AAA58658.1 Sequence problems. AY856072 Genomic DNA Translation: AAW29944.1 AK313959 mRNA Translation: BAG36675.1 CH471065 Genomic DNA Translation: EAW67033.1 BC112301 mRNA Translation: AAI12302.1 BC143773 mRNA Translation: AAI43774.1 |
CCDSi | CCDS73375.1 |
PIRi | A49499 |
RefSeqi | NP_002417.2, NM_002426.5 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1JIZ | X-ray | 2.60 | A/B | 100-264 | [»] | |
1JK3 | X-ray | 1.09 | A | 106-263 | [»] | |
1OS2 | X-ray | 2.15 | A/B/C/D/E/F | 106-268 | [»] | |
1OS9 | X-ray | 1.85 | A/B/C/D/E/F | 106-268 | [»] | |
1RMZ | X-ray | 1.34 | A | 106-263 | [»] | |
1ROS | X-ray | 2.00 | A/B | 106-268 | [»] | |
1UTT | X-ray | 2.20 | A | 106-264 | [»] | |
1UTZ | X-ray | 2.50 | A/B | 106-264 | [»] | |
1Y93 | X-ray | 1.03 | A | 106-263 | [»] | |
1YCM | NMR | - | A | 106-263 | [»] | |
1Z3J | NMR | - | A | 106-263 | [»] | |
2HU6 | X-ray | 1.32 | A | 106-263 | [»] | |
2JXY | NMR | - | A | 278-470 | [»] | |
2K2G | NMR | - | A | 100-263 | [»] | |
2K9C | NMR | - | A | 112-263 | [»] | |
2KRJ | NMR | - | A | 112-263 | [»] | |
2MLR | NMR | - | A | 100-263 | [»] | |
2MLS | NMR | - | A | 100-263 | [»] | |
2N8R | NMR | - | A | 100-263 | [»] | |
2OXU | X-ray | 1.24 | A | 106-263 | [»] | |
2OXW | X-ray | 1.15 | A | 106-263 | [»] | |
2OXZ | X-ray | 1.90 | A | 106-263 | [»] | |
2POJ | NMR | - | A | 100-263 | [»] | |
2W0D | X-ray | 2.00 | A/B/C/D | 106-263 | [»] | |
2WO8 | X-ray | 2.00 | A/B/C/D | 106-268 | [»] | |
2WO9 | X-ray | 1.70 | A/B/C/D | 106-268 | [»] | |
2WOA | X-ray | 2.30 | A/B/C/D | 106-268 | [»] | |
2Z2D | NMR | - | A | 100-263 | [»] | |
3BA0 | X-ray | 3.00 | A | 106-470 | [»] | |
3EHX | X-ray | 1.90 | A | 106-263 | [»] | |
3EHY | X-ray | 1.90 | A | 106-263 | [»] | |
3F15 | X-ray | 1.70 | A | 106-263 | [»] | |
3F16 | X-ray | 1.16 | A | 106-263 | [»] | |
3F17 | X-ray | 1.10 | A | 106-263 | [»] | |
3F18 | X-ray | 1.13 | A | 106-263 | [»] | |
3F19 | X-ray | 1.13 | A | 106-263 | [»] | |
3F1A | X-ray | 1.25 | A | 106-263 | [»] | |
3LIK | X-ray | 1.80 | A | 106-263 | [»] | |
3LIL | X-ray | 1.80 | A | 106-263 | [»] | |
3LIR | X-ray | 1.90 | A | 106-263 | [»] | |
3LJG | X-ray | 1.31 | A | 106-263 | [»] | |
3LK8 | X-ray | 1.80 | A | 106-263 | [»] | |
3LKA | X-ray | 1.80 | A | 106-263 | [»] | |
3N2U | X-ray | 1.81 | A | 106-263 | [»] | |
3N2V | X-ray | 1.55 | A | 106-263 | [»] | |
3NX7 | X-ray | 1.80 | A | 106-263 | [»] | |
3RTS | X-ray | 1.81 | A | 106-263 | [»] | |
3RTT | X-ray | 1.82 | A | 106-263 | [»] | |
3TS4 | X-ray | 1.59 | A | 106-263 | [»] | |
3TSK | X-ray | 2.00 | A | 106-263 | [»] | |
3UVC | X-ray | 1.30 | A/B | 106-263 | [»] | |
4EFS | X-ray | 1.63 | A | 106-263 | [»] | |
4GQL | X-ray | 1.15 | A | 106-263 | [»] | |
4GR0 | X-ray | 1.50 | A | 106-263 | [»] | |
4GR3 | X-ray | 1.49 | A | 106-263 | [»] | |
4GR8 | X-ray | 1.30 | A | 111-262 | [»] | |
4GUY | X-ray | 2.00 | A | 106-263 | [»] | |
4H30 | X-ray | 1.43 | A/B | 106-263 | [»] | |
4H49 | X-ray | 2.16 | A/B/C/D | 106-263 | [»] | |
4H76 | X-ray | 1.50 | A | 106-263 | [»] | |
4H84 | X-ray | 1.59 | A/B | 106-263 | [»] | |
4I03 | X-ray | 1.70 | A | 106-263 | [»] | |
4IJO | X-ray | 1.90 | A | 106-263 | [»] | |
5CXA | X-ray | 1.30 | A | 106-263 | [»] | |
5CZM | X-ray | 1.30 | A | 106-263 | [»] | |
5D2B | X-ray | 1.20 | A | 106-263 | [»] | |
5D3C | X-ray | 1.31 | A | 106-263 | [»] | |
5I0L | X-ray | 2.45 | A/B | 106-263 | [»] | |
5I2Z | X-ray | 2.30 | A/B/C/D | 106-263 | [»] | |
5I3M | X-ray | 2.17 | A/B/C/D | 106-263 | [»] | |
5I43 | X-ray | 1.95 | A/B/C/D | 106-263 | [»] | |
5I4O | X-ray | 2.05 | A/B/C/D | 106-263 | [»] | |
5L79 | X-ray | 2.07 | A | 106-263 | [»] | |
5L7F | X-ray | 1.80 | A/B | 106-263 | [»] | |
5LAB | X-ray | 1.34 | A | 106-263 | [»] | |
5N5J | X-ray | 1.80 | A | 106-263 | [»] | |
5N5K | X-ray | 1.80 | A | 108-263 | [»] | |
6EKN | X-ray | 1.20 | A | 106-263 | [»] | |
6ELA | X-ray | 1.49 | A/B/C/D | 106-263 | [»] | |
6ENM | X-ray | 1.59 | A/B | 106-263 | [»] | |
6EOX | X-ray | 1.30 | A | 106-263 | [»] | |
6RD0 | X-ray | 1.90 | A | 106-263 | [»] | |
6RLY | X-ray | 2.20 | A | 106-263 | [»] | |
7OVY | X-ray | 1.24 | A | 106-263 | [»] | |
AlphaFoldDBi | P39900 | |||||
BMRBi | P39900 | |||||
SASBDBi | P39900 | |||||
SMRi | P39900 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 110464, 3 interactors |
IntActi | P39900, 2 interactors |
MINTi | P39900 |
STRINGi | 9606.ENSP00000458585 |
Chemistry databases
BindingDBi | P39900 |
ChEMBLi | CHEMBL4393 |
DrugBanki | DB07026, (1S,5S,7R)-N~7~-(BIPHENYL-4-YLMETHYL)-N~3~-HYDROXY-6,8-DIOXA-3-AZABICYCLO[3.2.1]OCTANE-3,7-DICARBOXAMIDE DB07921, 2-[(4-fluorophenyl)sulfonylamino]-N-oxo-ethanamide DB04405, 2-[2-(1,3-Dioxo-1,3-Dihydro-2h-Isoindol-2-Yl)Ethyl]-4-(4'-Ethoxy-1,1'-Biphenyl-4-Yl)-4-Oxobutanoic Acid DB00551, Acetohydroxamic acid DB05387, AE-941 DB03880, Batimastat DB07556, CGS-27023 DB02118, CP-271485 DB00786, Marimastat DB07446, N-(biphenyl-4-ylsulfonyl)-D-leucine DB07683, N-(dibenzo[b,d]thiophen-3-ylsulfonyl)-L-valine DB08599, N-[(4-methoxyphenyl)sulfonyl]-D-alanine DB08271, N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID DB07922, N-oxo-2-(phenylsulfonylamino)ethanamide DB07920, N-oxo-2-[(4-phenylphenyl)sulfonylamino]ethanamide DB03367, PF-00356231 DB00013, Urokinase |
DrugCentrali | P39900 |
GuidetoPHARMACOLOGYi | 1636 |
Protein family/group databases
MEROPSi | M10.009 |
PTM databases
GlyGeni | P39900, 2 sites |
iPTMneti | P39900 |
PhosphoSitePlusi | P39900 |
Genetic variation databases
BioMutai | MMP12 |
DMDMi | 729179 |
Proteomic databases
jPOSTi | P39900 |
MassIVEi | P39900 |
PeptideAtlasi | P39900 |
PRIDEi | P39900 |
ProteomicsDBi | 55327 |
TopDownProteomicsi | P39900 |
Protocols and materials databases
ABCDi | P39900, 7 sequenced antibodies |
Antibodypediai | 61960, 640 antibodies from 41 providers |
DNASUi | 4321 |
Genome annotation databases
Ensembli | ENST00000571244.3; ENSP00000458585.1; ENSG00000262406.3 |
GeneIDi | 4321 |
KEGGi | hsa:4321 |
MANE-Selecti | ENST00000571244.3; ENSP00000458585.1; NM_002426.6; NP_002417.2 |
UCSCi | uc031yde.2, human |
Organism-specific databases
CTDi | 4321 |
DisGeNETi | 4321 |
GeneCardsi | MMP12 |
HGNCi | HGNC:7158, MMP12 |
HPAi | ENSG00000262406, Tissue enhanced (intestine, lymphoid tissue, urinary bladder) |
MIMi | 601046, gene |
neXtProti | NX_P39900 |
OpenTargetsi | ENSG00000262406 |
PharmGKBi | PA30870 |
VEuPathDBi | HostDB:ENSG00000262406 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1565, Eukaryota |
GeneTreei | ENSGT00940000162085 |
HOGENOMi | CLU_015489_6_0_1 |
InParanoidi | P39900 |
OMAi | VDNQYWR |
OrthoDBi | 1075463at2759 |
PhylomeDBi | P39900 |
Enzyme and pathway databases
BRENDAi | 3.4.24.65, 2681 |
PathwayCommonsi | P39900 |
Reactomei | R-HSA-1442490, Collagen degradation R-HSA-1474228, Degradation of the extracellular matrix |
SignaLinki | P39900 |
SIGNORi | P39900 |
Miscellaneous databases
BioGRID-ORCSi | 4321, 7 hits in 209 CRISPR screens |
ChiTaRSi | MMP12, human |
EvolutionaryTracei | P39900 |
GeneWikii | Matrix_metallopeptidase_12 |
GenomeRNAii | 4321 |
Pharosi | P39900, Tchem |
PROi | PR:P39900 |
RNActi | P39900, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000262406, Expressed in amniotic fluid and 102 other tissues |
Genevisiblei | P39900, HS |
Family and domain databases
CDDi | cd00094, HX, 1 hit cd04278, ZnMc_MMP, 1 hit |
Gene3Di | 2.110.10.10, 1 hit 3.40.390.10, 1 hit |
InterProi | View protein in InterPro IPR000585, Hemopexin-like_dom IPR036375, Hemopexin-like_dom_sf IPR018487, Hemopexin-like_repeat IPR018486, Hemopexin_CS IPR033739, M10A_MMP IPR024079, MetalloPept_cat_dom_sf IPR001818, Pept_M10_metallopeptidase IPR021190, Pept_M10A IPR021158, Pept_M10A_Zn_BS IPR006026, Peptidase_Metallo IPR002477, Peptidoglycan-bd-like IPR036365, PGBD-like_sf |
Pfami | View protein in Pfam PF00045, Hemopexin, 4 hits PF00413, Peptidase_M10, 1 hit PF01471, PG_binding_1, 1 hit |
PIRSFi | PIRSF001191, Peptidase_M10A_matrix, 1 hit |
PRINTSi | PR00138, MATRIXIN |
SMARTi | View protein in SMART SM00120, HX, 4 hits SM00235, ZnMc, 1 hit |
SUPFAMi | SSF47090, SSF47090, 1 hit SSF50923, SSF50923, 1 hit |
PROSITEi | View protein in PROSITE PS00546, CYSTEINE_SWITCH, 1 hit PS00024, HEMOPEXIN, 1 hit PS51642, HEMOPEXIN_2, 4 hits PS00142, ZINC_PROTEASE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | MMP12_HUMAN | |
Accessioni | P39900Primary (citable) accession number: P39900 Secondary accession number(s): B2R9X8, B7ZLF6, Q2M1L9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1995 |
Last sequence update: | February 1, 1995 | |
Last modified: | May 25, 2022 | |
This is version 213 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families