P50281 (MMP14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	582 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.14 Ref.15
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.15
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.12 Ref.15
Tissue specificity	Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors. Ref.13
Induction	Up-regulated by NANOS1. Ref.13
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.
Sequence similarities	Belongs to the peptidase M10A family. Contains 4 hemopexin-like domains.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: Compara astrocyte cell migration Inferred from electronic annotation. Source: Compara branching morphogenesis of an epithelial tube Inferred from electronic annotation. Source: Compara collagen catabolic process Traceable author statement. Source: Reactome endothelial cell proliferation Inferred from electronic annotation. Source: Compara extracellular matrix disassembly Traceable author statement. Source: Reactome lung development Inferred from electronic annotation. Source: Compara negative regulation of focal adhesion assembly Inferred from electronic annotation. Source: Compara ossification Inferred from electronic annotation. Source: Compara ovarian follicle development Inferred from electronic annotation. Source: Compara positive regulation of cell growth Inferred from direct assay Ref.15. Source: UniProtKB positive regulation of cell migration Inferred from direct assay Ref.15. Source: UniProtKB proteolysis Traceable author statement Ref.1. Source: ProtInc response to estrogen stimulus Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from electronic annotation. Source: Compara tissue remodeling Inferred from electronic annotation. Source: Compara zymogen activation Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi lumen Traceable author statement. Source: Reactome extracellular matrix Inferred from electronic annotation. Source: InterPro integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium 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: Compara sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara zinc ion binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADI1	Q9BV57	4	EBI-992788,EBI-992807
LIMK1	P53667	4	EBI-992788,EBI-444403

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Potential

Propeptide

21 – 111

91

Activation peptide

PRO_0000028798

Chain

112 – 582

471

Matrix metalloproteinase-14

PRO_0000028799

Regions

Topological domain

112 – 541

430

Extracellular Potential

Transmembrane

542 – 562

21

Helical; Potential

Topological domain

563 – 582

20

Cytoplasmic Potential

Domain

323 – 366

44

Hemopexin-like 1

Domain

368 – 412

45

Hemopexin-like 2

Domain

415 – 461

47

Hemopexin-like 3

Domain

463 – 508

46

Hemopexin-like 4

Motif

91 – 98

8

Cysteine switch By similarity

Sites

Active site

240

1

By similarity

Metal binding

93

1

Zinc; in inhibited form By similarity

Metal binding

239

1

Zinc; catalytic

Metal binding

243

1

Zinc; catalytic

Metal binding

249

1

Zinc; catalytic

Amino acid modifications

Disulfide bond

319 ↔ 508

By similarity

Natural variations

Natural variant

4

1

A → T. Ref.8
Corresponds to variant rs17882219 [ dbSNP | Ensembl ].

VAR_021029

Natural variant

6

1

R → K. Ref.8
Corresponds to variant rs17884647 [ dbSNP | Ensembl ].

VAR_021030

Natural variant

8

1

P → S. Ref.1 Ref.2 Ref.3 Ref.4 Ref.7 Ref.8 Ref.10
Corresponds to variant rs1042703 [ dbSNP | Ensembl ].

VAR_021031

Natural variant

233

1

I → V. Ref.8
Corresponds to variant rs17884841 [ dbSNP | Ensembl ].

VAR_021032

Natural variant

273

1

D → N. Ref.8
Corresponds to variant rs1042704 [ dbSNP | Ensembl ].

VAR_021033

Natural variant

302

1

R → W. Ref.8
Corresponds to variant rs17884719 [ dbSNP | Ensembl ].

VAR_021034

Natural variant

355

1

M → I. Ref.8
Corresponds to variant rs17880989 [ dbSNP | Ensembl ].

VAR_021035

Natural variant

431

1

R → H.
Corresponds to variant rs3751489 [ dbSNP | Ensembl ].

VAR_031267

Experimental info

Sequence conflict

338

1

E → K in BAA05519. Ref.1

Sequence conflict

500

1

S → P in CAA62432. Ref.6

Secondary structure

1

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582

Helix Strand Turn

Details...

Beta strand

120 – 128

9

Turn

133 – 135

3

Helix

137 – 154

18

Beta strand

158 – 161

4

Helix

164 – 168

5

Beta strand

171 – 173

3

Beta strand

176 – 182

7

Beta strand

187 – 190

4

Beta strand

194 – 202

9

Turn

208 – 211

4

Beta strand

213 – 216

4

Beta strand

230 – 232

3

Helix

233 – 244

12

Beta strand

258 – 260

3

Helix

273 – 283

11

Helix

318 – 320

3

Beta strand

324 – 329

6

Beta strand

332 – 337

6

Beta strand

340 – 345

6

Beta strand

354 – 356

3

Helix

357 – 360

4

Beta strand

370 – 373

4

Beta strand

379 – 383

5

Beta strand

386 – 391

6

Beta strand

400 – 402

3

Helix

403 – 405

3

Beta strand

416 – 420

5

Turn

422 – 424

3

Beta strand

427 – 431

5

Beta strand

434 – 439

6

Turn

440 – 443

4

Beta strand

450 – 452

3

Helix

453 – 455

3

Beta strand

464 – 468

5

Beta strand

472 – 479

8

Beta strand

482 – 487

6

Turn

488 – 491

4

Helix

501 – 504

4

Sequences

	Sequence		Length	Mass (Da)
	P50281 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: 3722DE286A4BBCDE	FASTA	582	65,894
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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], MASS SPECTROMETRY. Tissue: Melanoma.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00218398.

PIR

I38028.

RefSeq

NP_004986.1. NM_004995.2.

UniGene

Hs.2399.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P50281.

SMR

P50281. Positions 65-511.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35111N.

IntAct

P50281. 5 interactions.

MINT

MINT-246780.

STRING

9606.ENSP00000308208.

Protein family/group databases

MEROPS

M10.014.

PTM databases

PhosphoSite

P50281.

Polymorphism databases

DMDM

60392771.

Proteomic databases

PaxDb

P50281.

PRIDE

P50281.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000311852; ENSP00000308208; ENSG00000157227.

GeneID

4323.

KEGG

hsa:4323.

UCSC

uc001whc.3. human.

Organism-specific databases

CTD

4323.

GeneCards

GC14P023305.

H-InvDB

HIX0202102.

HGNC

HGNC:7160. MMP14.

HPA

CAB009918.

MIM

600754. gene.

neXtProt

NX_P50281.

Orphanet

3460. Torg-Winchester syndrome.

PharmGKB

PA30872.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG295915.

HOGENOM

HOG000217928.

HOVERGEN

HBG052484.

InParanoid

P50281.

KO

K07763.

OMA

WMGCPSG.

OrthoDB

EOG4FR0RF.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000157227-MONOMER.

BRENDA

3.4.24.7. 2681.

Reactome

REACT_118779. Extracellular matrix organization.
REACT_133391. Extracellular matrix organization.

Gene expression databases

ArrayExpress

P50281.

Bgee

P50281.

CleanEx

HS_MMP14.

Genevestigator

P50281.

GermOnline

ENSG00000157227. Homo sapiens.

Family and domain databases

Gene3D

2.110.10.10. 1 hit.
3.40.390.10. 1 hit.

InterPro

IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021805. Pept_M10A_metallopeptidase_C.
IPR016293. Pept_M10A_Metazoans.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]

Pfam

PF11857. DUF3377. 1 hit.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]

PIRSF

PIRSF001191. Peptidase_M10A_matrix. 1 hit.

PRINTS

PR00138. MATRIXIN.

SMART

SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]

SUPFAM

SSF50923. Hemopexin. 1 hit.
SSF47090. PGBD_like. 1 hit.

PROSITE

PS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P50281.

ChEMBL

CHEMBL3869.

ChiTaRS

MMP14. human.

EvolutionaryTrace

P50281.

GenomeRNAi

4323.

NextBio

17009.

SOURCE

Search...

Entry information

Entry name

MMP14_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 138 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.