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P39900

- MMP12_HUMAN

UniProt

P39900 - MMP12_HUMAN

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Protein
Macrophage metalloelastase
Gene
MMP12, HME
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

Cofactori

Binds 4 calcium ions per subunit.
Binds 2 zinc ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi92 – 921Zinc 2; in inhibited form By similarity
Metal bindingi124 – 1241Calcium 1
Metal bindingi158 – 1581Calcium 2
Metal bindingi168 – 1681Zinc 1
Metal bindingi170 – 1701Zinc 1
Metal bindingi175 – 1751Calcium 3
Metal bindingi176 – 1761Calcium 3; via carbonyl oxygen
Metal bindingi178 – 1781Calcium 3; via carbonyl oxygen
Metal bindingi180 – 1801Calcium 3; via carbonyl oxygen
Metal bindingi183 – 1831Zinc 1
Metal bindingi190 – 1901Calcium 2; via carbonyl oxygen
Metal bindingi192 – 1921Calcium 2; via carbonyl oxygen
Metal bindingi194 – 1941Calcium 2
Metal bindingi196 – 1961Zinc 1
Metal bindingi198 – 1981Calcium 3
Metal bindingi199 – 1991Calcium 1
Metal bindingi201 – 2011Calcium 1
Metal bindingi201 – 2011Calcium 3
Metal bindingi218 – 2181Zinc 2; catalytic
Active sitei219 – 2191
Metal bindingi222 – 2221Zinc 2; catalytic
Metal bindingi228 – 2281Zinc 2; catalytic
Metal bindingi289 – 2891Calcium 4; via carbonyl oxygen By similarity
Metal bindingi333 – 3331Calcium 4; via carbonyl oxygen By similarity
Metal bindingi381 – 3811Calcium 4; via carbonyl oxygen By similarity
Metal bindingi430 – 4301Calcium 4; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. endopeptidase activity Source: UniProtKB
  3. metalloendopeptidase activity Source: UniProtKB
  4. zinc ion binding Source: ProtInc

GO - Biological processi

  1. collagen catabolic process Source: Reactome
  2. extracellular matrix disassembly Source: Reactome
  3. extracellular matrix organization Source: Reactome
  4. positive regulation of epithelial cell proliferation involved in wound healing Source: BHF-UCL
  5. proteolysis Source: ProtInc
  6. wound healing, spreading of epidermal cells Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_150401. Collagen degradation.

Protein family/group databases

MEROPSiM10.009.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:7158. MMP12.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30870.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616 Inferred
Add
BLAST
Propeptidei17 – 10589Activation peptide By similarity
PRO_0000028776Add
BLAST
Chaini106 – 470365Macrophage metalloelastase
PRO_0000028777Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi20 – 201N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi282 ↔ 470 By similarity
Glycosylationi285 – 2851N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP39900.
PRIDEiP39900.

PTM databases

PhosphoSiteiP39900.

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

CleanExiHS_MMP12.
GenevestigatoriP39900.

Interactioni

Protein-protein interaction databases

BioGridi110464. 1 interaction.
IntActiP39900. 1 interaction.
MINTiMINT-7709562.
STRINGi9606.ENSP00000320664.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi106 – 1083
Beta strandi110 – 1189
Beta strandi123 – 1253
Helixi127 – 14216
Beta strandi144 – 1463
Beta strandi148 – 1514
Beta strandi153 – 1553
Beta strandi158 – 1647
Beta strandi169 – 1713
Beta strandi176 – 1794
Beta strandi182 – 1843
Beta strandi187 – 1893
Turni190 – 1934
Beta strandi195 – 1984
Beta strandi203 – 2119
Helixi212 – 22312
Turni232 – 2365
Beta strandi237 – 2393
Helixi245 – 2473
Helixi252 – 2598
Beta strandi260 – 2623
Beta strandi266 – 2683
Beta strandi281 – 2844
Beta strandi291 – 2944
Beta strandi297 – 3026
Beta strandi305 – 3084
Beta strandi318 – 3203
Helixi321 – 3244
Beta strandi334 – 3385
Helixi339 – 3413
Beta strandi343 – 3486
Beta strandi351 – 3544
Beta strandi357 – 3604
Turni361 – 3633
Beta strandi365 – 3673
Turni368 – 3725
Beta strandi382 – 3865
Turni387 – 3904
Beta strandi391 – 3966
Beta strandi399 – 4046
Turni405 – 4084
Helixi418 – 4214
Beta strandi430 – 4356
Turni436 – 4383
Beta strandi439 – 4446
Beta strandi447 – 4526
Turni453 – 4564
Beta strandi457 – 4637
Turni464 – 4696

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JIZX-ray2.60A/B100-264[»]
1JK3X-ray1.09A106-263[»]
1OS2X-ray2.15A/B/C/D/E/F106-268[»]
1OS9X-ray1.85A/B/C/D/E/F106-268[»]
1RMZX-ray1.34A106-263[»]
1ROSX-ray2.00A/B106-268[»]
1UTTX-ray2.20A106-264[»]
1UTZX-ray2.50A/B106-264[»]
1Y93X-ray1.03A106-263[»]
1YCMNMR-A106-263[»]
1Z3JNMR-A106-263[»]
2HU6X-ray1.32A106-263[»]
2JXYNMR-A278-470[»]
2K2GNMR-A100-263[»]
2K9CNMR-A112-263[»]
2KRJNMR-A112-263[»]
2OXUX-ray1.24A106-263[»]
2OXWX-ray1.15A106-263[»]
2OXZX-ray1.90A106-263[»]
2POJNMR-A100-263[»]
2W0DX-ray2.00A/B/C/D106-263[»]
2WO8X-ray2.00A/B/C/D106-268[»]
2WO9X-ray1.70A/B/C/D106-268[»]
2WOAX-ray2.30A/B/C/D106-268[»]
2Z2DNMR-A100-263[»]
3BA0X-ray3.00A106-470[»]
3EHXX-ray1.90A106-263[»]
3EHYX-ray1.90A106-263[»]
3F15X-ray1.70A106-263[»]
3F16X-ray1.16A106-263[»]
3F17X-ray1.10A106-263[»]
3F18X-ray1.13A106-263[»]
3F19X-ray1.13A106-263[»]
3F1AX-ray1.25A106-263[»]
3LIKX-ray1.80A106-263[»]
3LILX-ray1.80A106-263[»]
3LIRX-ray1.90A106-263[»]
3LJGX-ray1.31A106-263[»]
3LK8X-ray1.80A106-263[»]
3LKAX-ray1.80A106-263[»]
3N2UX-ray1.81A106-263[»]
3N2VX-ray1.55A106-263[»]
3NX7X-ray1.80A106-263[»]
3RTSX-ray1.81A106-263[»]
3RTTX-ray1.82A106-263[»]
3TS4X-ray1.59A106-263[»]
3TSKX-ray2.00A106-263[»]
3UVCX-ray1.30A/B106-263[»]
4EFSX-ray1.63A106-263[»]
4GQLX-ray1.15A106-263[»]
4GR0X-ray1.50A106-263[»]
4GR3X-ray1.49A106-263[»]
4GR8X-ray1.30A111-262[»]
4GUYX-ray2.00A106-263[»]
4H30X-ray1.43A/B106-263[»]
4H49X-ray2.16A/B/C/D106-263[»]
4H76X-ray1.50A106-263[»]
4H84X-ray1.59A/B106-263[»]
4I03X-ray1.70A106-263[»]
4IJOX-ray1.90A106-263[»]
DisProtiDP00571.
ProteinModelPortaliP39900.
SMRiP39900. Positions 34-470.

Miscellaneous databases

EvolutionaryTraceiP39900.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati279 – 32850Hemopexin 1
Add
BLAST
Repeati329 – 37547Hemopexin 2
Add
BLAST
Repeati377 – 42549Hemopexin 3
Add
BLAST
Repeati426 – 47045Hemopexin 4
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi90 – 978Cysteine 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.

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG323958.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP39900.
KOiK01413.
OMAiRKHYITY.
OrthoDBiEOG7XPZ57.
PhylomeDBiP39900.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR028718. MMP12.
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:SF32. PTHR10201:SF32. 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.

P39900-1 [UniParc]FASTAAdd to Basket

« Hide

MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFGERYLEKF YGLEINKLPV    50
TKMKYSGNLM KEKIQEMQHF LGLKVTGQLD TSTLEMMHAP RCGVPDVHHF 100
REMPGGPVWR KHYITYRINN YTPDMNREDV DYAIRKAFQV WSNVTPLKFS 150
KINTGMADIL VVFARGAHGD FHAFDGKGGI LAHAFGPGSG IGGDAHFDED 200
EFWTTHSGGT NLFLTAVHEI GHSLGLGHSS DPKAVMFPTY KYVDINTFRL 250
SADDIRGIQS LYGDPKENQR LPNPDNSEPA LCDPNLSFDA VTTVGNKIFF 300
FKDRFFWLKV SERPKTSVNL ISSLWPTLPS GIEAAYEIEA RNQVFLFKDD 350
KYWLISNLRP EPNYPKSIHS FGFPNFVKKI DAAVFNPRFY RTYFFVDNQY 400
WRYDERRQMM DPGYPKLITK NFQGIGPKID AVFYSKNKYY YFFQGSNQFE 450
YDFLLQRITK TLKSNSWFGC 470
Length:470
Mass (Da):54,002
Last modified:February 1, 1995 - v1
Checksum:i8C745EEA8C0EA216
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti357 – 3571N → S.2 Publications
Corresponds to variant rs652438 [ dbSNP | Ensembl ].
VAR_021343
Natural varianti469 – 4691G → R.1 Publication
Corresponds to variant rs28381701 [ dbSNP | Ensembl ].
VAR_021344

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
PIRiA49499.
RefSeqiNP_002417.2. NM_002426.4.
UniGeneiHs.1695.
Hs.709832.

Genome annotation databases

EnsembliENST00000571244; ENSP00000458585; ENSG00000262406.
GeneIDi4321.
KEGGihsa:4321.
UCSCiuc001phk.3. human.

Polymorphism databases

DMDMi729179.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A49499.
RefSeqi NP_002417.2. NM_002426.4.
UniGenei Hs.1695.
Hs.709832.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
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 [» ]
DisProti DP00571.
ProteinModelPortali P39900.
SMRi P39900. Positions 34-470.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110464. 1 interaction.
IntActi P39900. 1 interaction.
MINTi MINT-7709562.
STRINGi 9606.ENSP00000320664.

Chemistry

BindingDBi P39900.
ChEMBLi CHEMBL4393.
DrugBanki DB00551. Acetohydroxamic Acid.

Protein family/group databases

MEROPSi M10.009.

PTM databases

PhosphoSitei P39900.

Polymorphism databases

DMDMi 729179.

Proteomic databases

PaxDbi P39900.
PRIDEi P39900.

Protocols and materials databases

DNASUi 4321.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000571244 ; ENSP00000458585 ; ENSG00000262406 .
GeneIDi 4321.
KEGGi hsa:4321.
UCSCi uc001phk.3. human.

Organism-specific databases

CTDi 4321.
GeneCardsi GC11M102767.
HGNCi HGNC:7158. MMP12.
MIMi 601046. gene.
neXtProti NX_P39900.
PharmGKBi PA30870.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG323958.
HOGENOMi HOG000217927.
HOVERGENi HBG052484.
InParanoidi P39900.
KOi K01413.
OMAi RKHYITY.
OrthoDBi EOG7XPZ57.
PhylomeDBi P39900.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_150401. Collagen degradation.

Miscellaneous databases

ChiTaRSi MMP12. human.
EvolutionaryTracei P39900.
GeneWikii Matrix_metallopeptidase_12.
GenomeRNAii 4321.
NextBioi 17001.
PROi P39900.
SOURCEi Search...

Gene expression databases

CleanExi HS_MMP12.
Genevestigatori P39900.

Family and domain databases

Gene3Di 2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR028718. MMP12.
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:SF32. PTHR10201:SF32. 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. "Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages."
    Shapiro S.D., Kobayashi D.K., Ley T.J.
    J. Biol. Chem. 268:23824-23829(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Alveolar macrophage.
  2. NIEHS SNPs program
    Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-357 AND ARG-469.
  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.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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], VARIANT SER-357.
  6. "Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase."
    Gronski T.J. Jr., Martin R.L., Kobayashi D.K., Walsh B.C., Holman M.C., Huber M., Van Wart H.E., Shapiro S.D.
    J. Biol. Chem. 272:12189-12194(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 A crystal structure."
    Lang R., Kocourek A., Braun M., Tschesche H., Huber R., Bode W., Maskos K.
    J. Mol. Biol. 312:731-742(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS) OF 106-263.
  8. "Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor."
    Nar H., Werle K., Bauer M.M.T., Dollinger H., Jung B.
    J. Mol. Biol. 312:743-751(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 100-280.

Entry informationi

Entry nameiMMP12_HUMAN
AccessioniPrimary (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: September 3, 2014
This is version 157 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, 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

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