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P50281

- MMP14_HUMAN

UniProt

P50281 - MMP14_HUMAN

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Protein

Matrix metalloproteinase-14

Gene

MMP14

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

Functioni

Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2.3 Publications

Catalytic activityi

Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • Ca2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi93 – 931Zinc; in inhibited formBy similarity
Metal bindingi239 – 2391Zinc; catalytic
Active sitei240 – 2401PROSITE-ProRule annotation
Metal bindingi243 – 2431Zinc; catalytic
Metal bindingi249 – 2491Zinc; catalytic

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. metalloendopeptidase activity Source: ProtInc
  3. peptidase activator activity Source: Ensembl
  4. sequence-specific DNA binding transcription factor activity Source: Ensembl
  5. zinc ion binding Source: ProtInc

GO - Biological processi

  1. angiogenesis Source: Ensembl
  2. astrocyte cell migration Source: Ensembl
  3. branching morphogenesis of an epithelial tube Source: Ensembl
  4. chondrocyte proliferation Source: Ensembl
  5. collagen catabolic process Source: Reactome
  6. craniofacial suture morphogenesis Source: Ensembl
  7. embryonic cranial skeleton morphogenesis Source: Ensembl
  8. endochondral ossification Source: Ensembl
  9. endodermal cell differentiation Source: UniProtKB
  10. endothelial cell proliferation Source: Ensembl
  11. extracellular matrix disassembly Source: Reactome
  12. extracellular matrix organization Source: Reactome
  13. lung development Source: Ensembl
  14. male gonad development Source: Ensembl
  15. negative regulation of focal adhesion assembly Source: Ensembl
  16. ovarian follicle development Source: Ensembl
  17. positive regulation of cell growth Source: UniProtKB
  18. positive regulation of cell migration Source: UniProtKB
  19. proteolysis Source: ProtInc
  20. response to estrogen Source: Ensembl
  21. response to hypoxia Source: Ensembl
  22. response to mechanical stimulus Source: Ensembl
  23. response to oxidative stress Source: Ensembl
  24. tissue remodeling Source: Ensembl
  25. zymogen activation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000157227-MONOMER.
BRENDAi3.4.24.7. 2681.
ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_150401. Collagen degradation.

Protein family/group databases

MEROPSiM10.014.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-14 (EC:3.4.24.80)
Short name:
MMP-14
Alternative name(s):
MMP-X1
Membrane-type matrix metalloproteinase 1
Short name:
MT-MMP 1
Short name:
MTMMP1
Membrane-type-1 matrix metalloproteinase
Short name:
MT1-MMP
Short name:
MT1MMP
Gene namesi
Name:MMP14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:7160. MMP14.

Subcellular locationi

Membrane Curated; Single-pass type I membrane protein Curated. Melanosome. Cytoplasm
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Forms a complex with BST2 and localizes to the cytoplasm.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini112 – 541430ExtracellularSequence AnalysisAdd
BLAST
Transmembranei542 – 56221HelicalSequence AnalysisAdd
BLAST
Topological domaini563 – 58220CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular matrix Source: InterPro
  2. focal adhesion Source: UniProtKB
  3. Golgi lumen Source: Reactome
  4. integral component of plasma membrane Source: ProtInc
  5. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

Winchester syndrome (WNCHRS) [MIM:277950]: A disease characterized by severe osteolysis in the hands and feet, generalized osteoporosis, bone thinning, and absence of subcutaneous nodules. Various additional features include coarse face, corneal opacities, gum hypertrophy, and EKG changes.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171T → R in WNCHRS; results in increased MMP14 proteosomal degradation and reduced protein localization to cell membrane. 1 Publication
VAR_070567

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi277950. phenotype.
Orphaneti85196. Nodulosis-arthropathy-osteolysis syndrome.
3460. Torg-Winchester syndrome.
PharmGKBiPA30872.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 11191Activation peptide1 PublicationPRO_0000028798Add
BLAST
Chaini112 – 582471Matrix metalloproteinase-14PRO_0000028799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi319 ↔ 508By similarity
Modified residuei399 – 3991Phosphotyrosine; by PKDCC1 Publication

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity
Tyrosine phosphorylated by PKDCC/VLK.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiP50281.
PaxDbiP50281.
PRIDEiP50281.

PTM databases

PhosphoSiteiP50281.

Expressioni

Tissue specificityi

Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors.1 Publication

Inductioni

Up-regulated by NANOS1.1 Publication

Gene expression databases

BgeeiP50281.
CleanExiHS_MMP14.
ExpressionAtlasiP50281. baseline and differential.
GenevestigatoriP50281.

Organism-specific databases

HPAiCAB009918.

Interactioni

Subunit structurei

Interacts (via C-terminal cytoplasmic tail) with BST2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADI1Q9BV574EBI-992788,EBI-992807
BCAR1P569453EBI-992788,EBI-702093
Gorasp2Q9R06414EBI-992788,EBI-4422912From a different organism.
LIMK1P536674EBI-992788,EBI-444403
TIMP2P160352EBI-992788,EBI-1033507

Protein-protein interaction databases

BioGridi110466. 9 interactions.
DIPiDIP-35111N.
IntActiP50281. 16 interactions.
MINTiMINT-246780.
STRINGi9606.ENSP00000308208.

Structurei

Secondary structure

1
582
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi120 – 1289Combined sources
Turni133 – 1353Combined sources
Helixi137 – 15418Combined sources
Beta strandi158 – 1614Combined sources
Helixi164 – 1685Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi176 – 1827Combined sources
Beta strandi187 – 1904Combined sources
Beta strandi194 – 2029Combined sources
Turni208 – 2114Combined sources
Beta strandi213 – 2164Combined sources
Beta strandi230 – 2323Combined sources
Helixi233 – 24412Combined sources
Beta strandi258 – 2603Combined sources
Helixi273 – 28311Combined sources
Helixi318 – 3203Combined sources
Beta strandi324 – 3296Combined sources
Beta strandi332 – 3376Combined sources
Beta strandi340 – 3456Combined sources
Beta strandi354 – 3563Combined sources
Helixi357 – 3604Combined sources
Beta strandi370 – 3734Combined sources
Beta strandi379 – 3835Combined sources
Beta strandi386 – 3916Combined sources
Beta strandi400 – 4023Combined sources
Helixi403 – 4053Combined sources
Beta strandi416 – 4205Combined sources
Turni422 – 4243Combined sources
Beta strandi427 – 4315Combined sources
Beta strandi434 – 4396Combined sources
Turni440 – 4434Combined sources
Beta strandi450 – 4523Combined sources
Helixi453 – 4553Combined sources
Beta strandi464 – 4685Combined sources
Beta strandi472 – 4798Combined sources
Beta strandi482 – 4876Combined sources
Turni488 – 4914Combined sources
Helixi501 – 5044Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BQQX-ray2.75M114-287[»]
1BUVX-ray2.75M114-287[»]
3C7XX-ray1.70A316-511[»]
3MA2X-ray2.05A/D112-292[»]
ProteinModelPortaliP50281.
SMRiP50281. Positions 65-511.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50281.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati316 – 36449Hemopexin 1Add
BLAST
Repeati365 – 41046Hemopexin 2Add
BLAST
Repeati412 – 46049Hemopexin 3Add
BLAST
Repeati461 – 50848Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi91 – 988Cysteine switchBy 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.Curated
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG295915.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiP50281.
KOiK07763.
OMAiWMGCPSG.
OrthoDBiEOG7XPZ57.
PhylomeDBiP50281.
TreeFamiTF352396.

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.
IPR028693. MMP14.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021805. Pept_M10A_metallopeptidase_C.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF24. PTHR10201:SF24. 1 hit.
PfamiPF11857. DUF3377. 1 hit.
PF00045. 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.

P50281-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSPAPRPPRC LLLPLLTLGT ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL
60 70 80 90 100
RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG
110 120 130 140 150
AEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT YEAIRKAFRV
160 170 180 190 200
WESATPLRFR EVPYAYIREG HEKQADIMIF FAEGFHGDST PFDGEGGFLA
210 220 230 240 250
HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS
260 270 280 290 300
SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGGESGFP TKMPPQPRTT
310 320 330 340 350
SRPSVPDKPK NPTYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM
360 370 380 390 400
DGYPMPIGQF WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP
410 420 430 440 450
KHIKELGRGL PTDKIDAALF WMPNGKTYFF RGNKYYRFNE ELRAVDSEYP
460 470 480 490 500
KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG NKYWKFNNQK LKVEPGYPKS
510 520 530 540 550
ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGGGAVSAA AVVLPVLLLL
560 570 580
LVLAVGLAVF FFRRHGTPRR LLYCQRSLLD KV
Length:582
Mass (Da):65,894
Last modified:January 11, 2011 - v3
Checksum:i3722DE286A4BBCDE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti338 – 3381E → K in BAA05519. (PubMed:8015608)Curated
Sequence conflicti500 – 5001S → P in CAA62432. (PubMed:8706726)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41A → T.1 Publication
Corresponds to variant rs17882219 [ dbSNP | Ensembl ].
VAR_021029
Natural varianti6 – 61R → K.1 Publication
Corresponds to variant rs17884647 [ dbSNP | Ensembl ].
VAR_021030
Natural varianti8 – 81P → S.7 Publications
Corresponds to variant rs1042703 [ dbSNP | Ensembl ].
VAR_021031
Natural varianti17 – 171T → R in WNCHRS; results in increased MMP14 proteosomal degradation and reduced protein localization to cell membrane. 1 Publication
VAR_070567
Natural varianti233 – 2331I → V.1 Publication
Corresponds to variant rs17884841 [ dbSNP | Ensembl ].
VAR_021032
Natural varianti273 – 2731D → N.1 Publication
Corresponds to variant rs1042704 [ dbSNP | Ensembl ].
VAR_021033
Natural varianti302 – 3021R → W.1 Publication
Corresponds to variant rs17884719 [ dbSNP | Ensembl ].
VAR_021034
Natural varianti355 – 3551M → I.1 Publication
Corresponds to variant rs17880989 [ dbSNP | Ensembl ].
VAR_021035
Natural varianti431 – 4311R → H.
Corresponds to variant rs3751489 [ dbSNP | Ensembl ].
VAR_031267

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26512 mRNA. Translation: BAA05519.1.
X83535 mRNA. Translation: CAA58519.1.
Z48481 mRNA. Translation: CAA88372.1.
U41078 mRNA. Translation: AAA83770.1.
X90925 mRNA. Translation: CAA62432.1.
AK291325 mRNA. Translation: BAF84014.1.
AY795074 Genomic DNA. Translation: AAV40837.1.
AL135998 Genomic DNA. No translation available.
BC064803 mRNA. Translation: AAH64803.1.
CCDSiCCDS9577.1.
PIRiI38028.
RefSeqiNP_004986.1. NM_004995.3.
UniGeneiHs.2399.

Genome annotation databases

EnsembliENST00000311852; ENSP00000308208; ENSG00000157227.
GeneIDi4323.
KEGGihsa:4323.
UCSCiuc001whc.3. human.

Polymorphism databases

DMDMi317373419.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26512 mRNA. Translation: BAA05519.1 .
X83535 mRNA. Translation: CAA58519.1 .
Z48481 mRNA. Translation: CAA88372.1 .
U41078 mRNA. Translation: AAA83770.1 .
X90925 mRNA. Translation: CAA62432.1 .
AK291325 mRNA. Translation: BAF84014.1 .
AY795074 Genomic DNA. Translation: AAV40837.1 .
AL135998 Genomic DNA. No translation available.
BC064803 mRNA. Translation: AAH64803.1 .
CCDSi CCDS9577.1.
PIRi I38028.
RefSeqi NP_004986.1. NM_004995.3.
UniGenei Hs.2399.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BQQ X-ray 2.75 M 114-287 [» ]
1BUV X-ray 2.75 M 114-287 [» ]
3C7X X-ray 1.70 A 316-511 [» ]
3MA2 X-ray 2.05 A/D 112-292 [» ]
ProteinModelPortali P50281.
SMRi P50281. Positions 65-511.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110466. 9 interactions.
DIPi DIP-35111N.
IntActi P50281. 16 interactions.
MINTi MINT-246780.
STRINGi 9606.ENSP00000308208.

Chemistry

BindingDBi P50281.
ChEMBLi CHEMBL3869.
DrugBanki DB00786. Marimastat.

Protein family/group databases

MEROPSi M10.014.

PTM databases

PhosphoSitei P50281.

Polymorphism databases

DMDMi 317373419.

Proteomic databases

MaxQBi P50281.
PaxDbi P50281.
PRIDEi P50281.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311852 ; ENSP00000308208 ; ENSG00000157227 .
GeneIDi 4323.
KEGGi hsa:4323.
UCSCi uc001whc.3. human.

Organism-specific databases

CTDi 4323.
GeneCardsi GC14P023305.
H-InvDB HIX0202102.
HGNCi HGNC:7160. MMP14.
HPAi CAB009918.
MIMi 277950. phenotype.
600754. gene.
neXtProti NX_P50281.
Orphaneti 85196. Nodulosis-arthropathy-osteolysis syndrome.
3460. Torg-Winchester syndrome.
PharmGKBi PA30872.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG295915.
GeneTreei ENSGT00760000118870.
HOGENOMi HOG000217928.
HOVERGENi HBG052484.
InParanoidi P50281.
KOi K07763.
OMAi WMGCPSG.
OrthoDBi EOG7XPZ57.
PhylomeDBi P50281.
TreeFami TF352396.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000157227-MONOMER.
BRENDAi 3.4.24.7. 2681.
Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_150401. Collagen degradation.

Miscellaneous databases

ChiTaRSi MMP14. human.
EvolutionaryTracei P50281.
GeneWikii MMP14.
GenomeRNAii 4323.
NextBioi 17009.
PROi P50281.
SOURCEi Search...

Gene expression databases

Bgeei P50281.
CleanExi HS_MMP14.
ExpressionAtlasi P50281. baseline and differential.
Genevestigatori P50281.

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.
IPR028693. MMP14.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021805. Pept_M10A_metallopeptidase_C.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view ]
PANTHERi PTHR10201:SF24. PTHR10201:SF24. 1 hit.
Pfami PF11857. DUF3377. 1 hit.
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. "A matrix metalloproteinase expressed on the surface of invasive tumour cells."
    Sato H., Takino T., Okada Y., Cao J., Shinagawa A., Yamamoto E., Seiki M.
    Nature 370:61-65(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-8.
    Tissue: Placenta.
  2. "Cloning of a human gene potentially encoding a novel matrix metalloproteinase having a C-terminal transmembrane domain."
    Takino T., Sato H., Yamamoto E., Seiki M.
    Gene 155:293-298(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-8.
    Tissue: Placenta.
  3. "Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas."
    Okada A., Bellocq J.-P., Rouyer N., Chenard M.P., Rio M.C., Chambon P., Basset P.
    Proc. Natl. Acad. Sci. U.S.A. 92:2730-2734(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-8.
  4. "cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment."
    Will H., Hinzmann B.
    Eur. J. Biochem. 231:602-608(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-8.
    Tissue: Lung.
  5. Luo G.-X., Reisfeld R.A., Strongin A.Y.
    Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. "Regulation of membrane-type matrix metalloproteinase-1 expression by growth factors and phorbol 12-myristate 13-acetate."
    Lohi J.L., Westermarck J., Kaehaeri V.M., Keski-Oja J.
    Eur. J. Biochem. 239:239-247(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  7. "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], VARIANT SER-8.
    Tissue: Tongue.
  8. NIEHS SNPs program
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-4; LYS-6; SER-8; VAL-233; ASN-273; TRP-302 AND ILE-355.
  9. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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-8.
    Tissue: Skin.
  11. "Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2."
    Sato H., Kinoshita T., Takino T., Nakayama K., Seiki M.
    FEBS Lett. 393:101-104(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 112-116.
  12. "Production and activation of matrix metalloproteinase-2 in proliferative diabetic retinopathy."
    Noda K., Ishida S., Inoue M., Obata K., Oguchi Y., Okada Y., Ikeda E.
    Invest. Ophthalmol. Vis. Sci. 44:2163-2170(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE FORMATION OF THE FIBROVASCULAR TISSUES.
  13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  14. "The E-cadherin-repressed hNanos1 gene induces tumor cell invasion by upregulating MT1-MMP expression."
    Bonnomet A., Polette M., Strumane K., Gilles C., Dalstein V., Kileztky C., Berx G., van Roy F., Birembaut P., Nawrocki-Raby B.
    Oncogene 27:3692-3699(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, TISSUE SPECIFICITY.
  15. "The Wnt/planar cell polarity protein-tyrosine kinase-7 (PTK7) is a highly efficient proteolytic target of membrane type-1 matrix metalloproteinase: implications in cancer and embryogenesis."
    Golubkov V.S., Chekanov A.V., Cieplak P., Aleshin A.E., Chernov A.V., Zhu W., Radichev I.A., Zhang D., Dong P.D., Strongin A.Y.
    J. Biol. Chem. 285:35740-35749(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "BST-2 binding with cellular MT1-MMP blocks cell growth and migration via decreasing MMP2 activity."
    Gu G., Zhao D., Yin Z., Liu P.
    J. Cell. Biochem. 113:1013-1021(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BST2.
  17. Cited for: PHOSPHORYLATION AT TYR-399.
  18. "Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor."
    Fernandez-Catalan C., Bode W., Huber R., Turk D., Calvete J.J., Lichte A., Tschesche H., Maskos K.
    EMBO J. 17:5238-5248(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 114-287 IN COMPLEX WITH TIMP2.
  19. "Mutation of membrane type-1 metalloproteinase, MT1-MMP, causes the multicentric osteolysis and arthritis disease Winchester syndrome."
    Evans B.R., Mosig R.A., Lobl M., Martignetti C.R., Camacho C., Grum-Tokars V., Glucksman M.J., Martignetti J.A.
    Am. J. Hum. Genet. 91:572-576(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT WNCHRS ARG-17, CHARACTERIZATION OF VARIANT WNCHRS ARG-17.

Entry informationi

Entry nameiMMP14_HUMAN
AccessioniPrimary (citable) accession number: P50281
Secondary accession number(s): A8K5L0, Q6GSF3, Q92678
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: November 26, 2014
This is version 155 of the entry and version 3 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 14
    Human chromosome 14: 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