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P50281 (MMP14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-14

Short name=MMP-14
EC=3.4.24.80
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 names
Name:MMP14
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length582 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.15 Ref.16

Catalytic activity

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.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Calcium By similarity.

Subunit structure

Interacts (via C-terminal cytoplasmic tail) with BST2. Ref.16

Subcellular location

Membrane; Single-pass type I membrane protein Potential. 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. Ref.13 Ref.16

Tissue specificity

Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors. Ref.14

Induction

Up-regulated by NANOS1. Ref.14

Domain

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.

Post-translational modification

The precursor is cleaved by a furin endopeptidase By similarity.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: Ensembl

astrocyte cell migration

Inferred from electronic annotation. Source: Ensembl

branching morphogenesis of an epithelial tube

Inferred from electronic annotation. Source: Ensembl

collagen catabolic process

Traceable author statement. Source: Reactome

endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

lung development

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from electronic annotation. Source: Ensembl

negative regulation of focal adhesion assembly

Inferred from electronic annotation. Source: Ensembl

ossification

Inferred from electronic annotation. Source: Ensembl

ovarian follicle development

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell growth

Inferred from direct assay Ref.16. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay Ref.16. Source: UniProtKB

proteolysis

Traceable author statement Ref.1. Source: ProtInc

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

tissue remodeling

Inferred from electronic annotation. Source: Ensembl

zymogen activation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

extracellular matrix

Inferred from electronic annotation. Source: InterPro

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

metalloendopeptidase activity

Traceable author statement Ref.1. Source: ProtInc

peptidase activator activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 14718544Ref.16. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 11191Activation peptide
PRO_0000028798
Chain112 – 582471Matrix metalloproteinase-14
PRO_0000028799

Regions

Topological domain112 – 541430Extracellular Potential
Transmembrane542 – 56221Helical; Potential
Topological domain563 – 58220Cytoplasmic Potential
Repeat316 – 36449Hemopexin 1
Repeat365 – 41046Hemopexin 2
Repeat412 – 46049Hemopexin 3
Repeat461 – 50848Hemopexin 4
Motif91 – 988Cysteine switch By similarity

Sites

Active site2401 By similarity
Metal binding931Zinc; in inhibited form By similarity
Metal binding2391Zinc; catalytic
Metal binding2431Zinc; catalytic
Metal binding2491Zinc; catalytic

Amino acid modifications

Disulfide bond319 ↔ 508 By similarity

Natural variations

Natural variant41A → T. Ref.8
Corresponds to variant rs17882219 [ dbSNP | Ensembl ].
VAR_021029
Natural variant61R → K. Ref.8
Corresponds to variant rs17884647 [ dbSNP | Ensembl ].
VAR_021030
Natural variant81P → S. Ref.1 Ref.2 Ref.3 Ref.4 Ref.7 Ref.8 Ref.10
Corresponds to variant rs1042703 [ dbSNP | Ensembl ].
VAR_021031
Natural variant171T → R in WNCHRS; results in increased MMP14 proteosomal degradation and reduced protein localization to cell membrane. Ref.18
VAR_070567
Natural variant2331I → V. Ref.8
Corresponds to variant rs17884841 [ dbSNP | Ensembl ].
VAR_021032
Natural variant2731D → N. Ref.8
Corresponds to variant rs1042704 [ dbSNP | Ensembl ].
VAR_021033
Natural variant3021R → W. Ref.8
Corresponds to variant rs17884719 [ dbSNP | Ensembl ].
VAR_021034
Natural variant3551M → I. Ref.8
Corresponds to variant rs17880989 [ dbSNP | Ensembl ].
VAR_021035
Natural variant4311R → H.
Corresponds to variant rs3751489 [ dbSNP | Ensembl ].
VAR_031267

Experimental info

Sequence conflict3381E → K in BAA05519. Ref.1
Sequence conflict5001S → P in CAA62432. Ref.6

Secondary structure

....................................................................... 582
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50281 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 3722DE286A4BBCDE

FASTA58265,894
        10         20         30         40         50         60 
MSPAPRPPRC LLLPLLTLGT ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL RTHTQRSPQS 

        70         80         90        100        110        120 
LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG AEIKANVRRK RYAIQGLKWQ 

       130        140        150        160        170        180 
HNEITFCIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIF 

       190        200        210        220        230        240 
FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE 

       250        260        270        280        290        300 
LGHALGLEHS SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGGESGFP TKMPPQPRTT 

       310        320        330        340        350        360 
SRPSVPDKPK NPTYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM DGYPMPIGQF 

       370        380        390        400        410        420 
WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP KHIKELGRGL PTDKIDAALF 

       430        440        450        460        470        480 
WMPNGKTYFF RGNKYYRFNE ELRAVDSEYP KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG 

       490        500        510        520        530        540 
NKYWKFNNQK LKVEPGYPKS ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGGGAVSAA 

       550        560        570        580 
AVVLPVLLLL LVLAVGLAVF FFRRHGTPRR LLYCQRSLLD KV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
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]"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.
[18]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9577.1.
PIRI38028.
RefSeqNP_004986.1. NM_004995.3.
UniGeneHs.2399.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BQQX-ray2.75M114-287[»]
1BUVX-ray2.75M114-287[»]
3C7XX-ray1.70A316-511[»]
3MA2X-ray2.05A/D112-292[»]
ProteinModelPortalP50281.
SMRP50281. Positions 65-511.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110466. 9 interactions.
DIPDIP-35111N.
IntActP50281. 16 interactions.
MINTMINT-246780.
STRING9606.ENSP00000308208.

Chemistry

BindingDBP50281.
ChEMBLCHEMBL3869.

Protein family/group databases

MEROPSM10.014.

PTM databases

PhosphoSiteP50281.

Polymorphism databases

DMDM317373419.

Proteomic databases

MaxQBP50281.
PaxDbP50281.
PRIDEP50281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311852; ENSP00000308208; ENSG00000157227.
GeneID4323.
KEGGhsa:4323.
UCSCuc001whc.3. human.

Organism-specific databases

CTD4323.
GeneCardsGC14P023305.
H-InvDBHIX0202102.
HGNCHGNC:7160. MMP14.
HPACAB009918.
MIM277950. phenotype.
600754. gene.
neXtProtNX_P50281.
Orphanet85196. Nodulosis-arthropathy-osteolysis syndrome.
3460. Torg-Winchester syndrome.
PharmGKBPA30872.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295915.
HOGENOMHOG000217928.
HOVERGENHBG052484.
InParanoidP50281.
KOK07763.
OMAWMGCPSG.
OrthoDBEOG7XPZ57.
PhylomeDBP50281.
TreeFamTF352396.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000157227-MONOMER.
BRENDA3.4.24.7. 2681.
ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP50281.
BgeeP50281.
CleanExHS_MMP14.
GenevestigatorP50281.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. 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]
PANTHERPTHR10201:SF24. PTHR10201:SF24. 1 hit.
PfamPF11857. DUF3377. 1 hit.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMMP14. human.
EvolutionaryTraceP50281.
GeneWikiMMP14.
GenomeRNAi4323.
NextBio17009.
PROP50281.
SOURCESearch...

Entry information

Entry nameMMP14_HUMAN
AccessionPrimary (citable) accession number: P50281
Secondary accession number(s): A8K5L0, Q6GSF3, Q92678
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM