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P53690

- MMP14_MOUSE

UniProt

P53690 - MMP14_MOUSE

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Protein
Matrix metalloproteinase-14
Gene
Mmp14, Mtmmp
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Endopeptidase that degrades various components of the extracellular matrix, such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development. May be involved in actin cytoskeleton reorganization by cleaving PTK7 By similarity. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues By similarity.1 Publication

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

Binds 1 zinc ion per subunit By similarity.
Calcium By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi93 – 931Zinc; in inhibited form By similarity
Metal bindingi239 – 2391Zinc; catalytic By similarity
Active sitei240 – 2401 By similarity
Metal bindingi243 – 2431Zinc; catalytic By similarity
Metal bindingi249 – 2491Zinc; catalytic By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. angiogenesis Source: Ensembl
  2. astrocyte cell migration Source: Ensembl
  3. bone development Source: MGI
  4. branching morphogenesis of an epithelial tube Source: MGI
  5. cell migration Source: MGI
  6. chondrocyte proliferation Source: MGI
  7. collagen catabolic process Source: MGI
  8. craniofacial suture morphogenesis Source: MGI
  9. embryonic cranial skeleton morphogenesis Source: MGI
  10. endochondral ossification Source: MGI
  11. endothelial cell proliferation Source: Ensembl
  12. lung development Source: MGI
  13. male gonad development Source: Ensembl
  14. negative regulation of focal adhesion assembly Source: Ensembl
  15. ossification Source: MGI
  16. ovarian follicle development Source: Ensembl
  17. positive regulation of cell growth Source: Ensembl
  18. positive regulation of cell migration Source: Ensembl
  19. regulation of transcription, DNA-templated Source: GOC
  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: MGI
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_199000. Activation of Matrix Metalloproteinases.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. 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
MT-MMP
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
Synonyms:Mtmmp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:101900. Mmp14.

Subcellular locationi

Membrane; Single-pass type I membrane protein; Extracellular side Reviewed prediction. Melanosome By similarity. Cytoplasm By similarity
Note: Forms a complex with BST2 and localizes to the cytoplasm By similarity.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini112 – 541430Extracellular Reviewed prediction
Add
BLAST
Transmembranei542 – 56221Helical; Reviewed prediction
Add
BLAST
Topological domaini563 – 58220Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. extracellular matrix Source: InterPro
  2. integral component of membrane Source: UniProtKB-KW
  3. melanosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 Reviewed prediction
Add
BLAST
Propeptidei21 – 11191 By similarity
PRO_0000028800Add
BLAST
Chaini112 – 582471Matrix metalloproteinase-14
PRO_0000028801Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi319 ↔ 508 By similarity

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase By similarity.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Zymogen

Proteomic databases

MaxQBiP53690.
PRIDEiP53690.

PTM databases

PhosphoSiteiP53690.

Expressioni

Tissue specificityi

Highly expressed in placenta, kidney, heart, lung, embryonic skeletal and periskeletal tissues.

Developmental stagei

Not detected before day 10.5. At day 12.5, prominently expressed in large arteries and the umbilical arteries, expressed at lower levels in the myocardium, craniofacial mesenchyme, nasal epithelium and liver capsule. At days 14.5 and 17.5, expressed in the musculoskeletal system, and ossification areas, with continued expression in the arterial tunica media.

Gene expression databases

ArrayExpressiP53690.
BgeeiP53690.
CleanExiMM_MMP14.
GenevestigatoriP53690.

Interactioni

Subunit structurei

Interacts (via C-terminal cytoplasmic tail) with BST2 By similarity.

Protein-protein interaction databases

IntActiP53690. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP53690.
SMRiP53690. Positions 65-511.

Family & Domainsi

Domains and Repeats

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi91 – 988Cysteine 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, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG295915.
GeneTreeiENSGT00750000117332.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ8BTX2.
KOiK07763.
OMAiWMGCPSG.
OrthoDBiEOG7XPZ57.
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.

P53690-1 [UniParc]FASTAAdd to Basket

« Hide

MSPAPRPSRS LLLPLLTLGT ALASLGWAQG SNFSPEAWLQ QYGYLPPGDL    50
RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DLATMMAMRR PRCGVPDKFG 100
TEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT FEAIRKAFRV 150
WESATPLRFR EVPYAYIREG HEKQADIMIL FAEGFHGDST PFDGEGGFLA 200
HAYFPGPNIG GDTHFDSAEP WTVQNEDLNG NDIFLVAVHE LGHALGLEHS 250
NDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGSKSGSP TKMPPQPRTT 300
SRPSVPDKPK NPAYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM 350
DGYPMPIGQF WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP 400
KHIKELGRGL PTDKIDAALF WMPNGKTYFF RGNKYYRFNE EFRAVDSEYP 450
KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG NKYWKFNNQK LKVEPGYPKS 500
ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGSGAVSAA AVVLPVLLLL 550
LVLAVGLAVF FFRRHGTPKR LLYCQRSLLD KV 582
Length:582
Mass (Da):65,919
Last modified:July 27, 2011 - v3
Checksum:i6CA95CFD5811B093
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331P → S in AAB86602. 1 Publication
Sequence conflicti255 – 2551A → D in CAA58520. 1 Publication
Sequence conflicti258 – 2581A → S in CAA58520. 1 Publication
Sequence conflicti258 – 2581A → S in AAB51753. 1 Publication
Sequence conflicti341 – 3411F → L in CAA58520. 1 Publication
Sequence conflicti346 – 3461N → P in AAB86602. 1 Publication
Sequence conflicti378 – 3781K → T in CAA58520. 1 Publication
Sequence conflicti390 – 3912FD → CV in CAA58520. 1 Publication
Sequence conflicti400 – 4012PK → AN in CAA58520. 1 Publication
Sequence conflicti407 – 4071G → V in CAA58520. 1 Publication
Sequence conflicti412 – 4121T → S in CAA58520. 1 Publication
Sequence conflicti417 – 4171A → T in CAA58520. 1 Publication
Sequence conflicti512 – 5121G → R in AAB51753. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83536 mRNA. Translation: CAA58520.2.
AF022432
, AF022424, AF022425, AF022426, AF022427, AF022428, AF022429, AF022430, AF022431 Genomic DNA. Translation: AAB86602.1.
U54984 mRNA. Translation: AAB51753.1.
DQ249870 mRNA. Translation: ABB45784.1.
AK088476 mRNA. Translation: BAC40377.1.
AK138611 mRNA. Translation: BAE23719.1.
AK149907 mRNA. Translation: BAE29158.1.
AK149988 mRNA. Translation: BAE29216.1.
AK165014 mRNA. Translation: BAE38000.1.
CH466535 Genomic DNA. Translation: EDL36348.1.
CCDSiCCDS36922.1.
PIRiI48673.
RefSeqiNP_032634.3. NM_008608.3.
UniGeneiMm.280175.
Mm.486486.

Genome annotation databases

EnsembliENSMUST00000089688; ENSMUSP00000087119; ENSMUSG00000000957.
GeneIDi17387.
KEGGimmu:17387.
UCSCiuc007twc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83536 mRNA. Translation: CAA58520.2 .
AF022432
, AF022424 , AF022425 , AF022426 , AF022427 , AF022428 , AF022429 , AF022430 , AF022431 Genomic DNA. Translation: AAB86602.1 .
U54984 mRNA. Translation: AAB51753.1 .
DQ249870 mRNA. Translation: ABB45784.1 .
AK088476 mRNA. Translation: BAC40377.1 .
AK138611 mRNA. Translation: BAE23719.1 .
AK149907 mRNA. Translation: BAE29158.1 .
AK149988 mRNA. Translation: BAE29216.1 .
AK165014 mRNA. Translation: BAE38000.1 .
CH466535 Genomic DNA. Translation: EDL36348.1 .
CCDSi CCDS36922.1.
PIRi I48673.
RefSeqi NP_032634.3. NM_008608.3.
UniGenei Mm.280175.
Mm.486486.

3D structure databases

ProteinModelPortali P53690.
SMRi P53690. Positions 65-511.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P53690. 1 interaction.

Protein family/group databases

MEROPSi M10.014.

PTM databases

PhosphoSitei P53690.

Proteomic databases

MaxQBi P53690.
PRIDEi P53690.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000089688 ; ENSMUSP00000087119 ; ENSMUSG00000000957 .
GeneIDi 17387.
KEGGi mmu:17387.
UCSCi uc007twc.2. mouse.

Organism-specific databases

CTDi 4323.
MGIi MGI:101900. Mmp14.

Phylogenomic databases

eggNOGi NOG295915.
GeneTreei ENSGT00750000117332.
HOGENOMi HOG000217928.
HOVERGENi HBG052484.
InParanoidi Q8BTX2.
KOi K07763.
OMAi WMGCPSG.
OrthoDBi EOG7XPZ57.
TreeFami TF352396.

Enzyme and pathway databases

Reactomei REACT_199000. Activation of Matrix Metalloproteinases.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

Miscellaneous databases

ChiTaRSi MMP14. mouse.
NextBioi 292000.
PROi P53690.
SOURCEi Search...

Gene expression databases

ArrayExpressi P53690.
Bgeei P53690.
CleanExi MM_MMP14.
Genevestigatori P53690.

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. "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].
  2. Odaka A.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "The matrix metalloproteinase-14 (MMP-14) gene is structurally distinct from other MMP genes and is co-expressed with the TIMP-2 gene during mouse embryogenesis."
    Apte S.S., Fukai N., Beier D.R., Olsen B.R.
    J. Biol. Chem. 272:25511-25517(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  4. "Cloning of murine membrane-type-1-matrix metalloproteinase (MT-1-MMP) and its metanephric developmental regulation with respect to MMP-2 and its inhibitor."
    Ota K., Stetler-Stevenson W.G., Yang Q., Kumar A., Wada J., Kashihara N., Wallner E.I., Kanwar Y.S.
    Kidney Int. 54:131-142(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CD-1.
    Tissue: Kidney.
  5. "Interference with the complement system by tumor cell membrane type-1 matrix metalloproteinase plays a significant role in promoting metastasis in mice."
    Rozanov D.V., Savinov A.Y., Golubkov V.S., Tomlinson S., Strongin A.Y.
    Cancer Res. 66:6258-6263(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: FVB/N.
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Eye, Spinal cord and Thymus.
  7. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover."
    Holmbeck K., Bianco P., Caterina J., Yamada S., Kromer M., Kuznetsov S.A., Mankani M., Robey P.G., Poole A.R., Pidoux I., Ward J.M., Birkedal-Hansen H.
    Cell 99:81-92(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiMMP14_MOUSE
AccessioniPrimary (citable) accession number: P53690
Secondary accession number(s): O08645, O35369, Q8BTX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi