Reviewed, UniProtKB/Swiss-Prot P14780 (MMP9_HUMAN)

Names and origin

Protein names

Recommended name:
    Matrix metalloproteinase-9
      Short name=MMP-9
    EC=3.4.24.35
Alternative name(s):
    92 kDa type IV collagenase
    92 kDa gelatinase
    Gelatinase B
      Short name=GELB
Cleaved into the following 2 chains:
    1- Recommended name:
            67 kDa matrix metalloproteinase-9
    2- Recommended name:
            82 kDa matrix metalloproteinase-9

Gene names

Name:	MMP9
Synonyms:	CLG4B

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	707 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	May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.
Catalytic activity	Cleavage of gelatin types I and V and collagen types IV and V.
Cofactor	Binds 2 zinc ions per subunit. Binds 3 calcium ions per subunit.
Enzyme regulation	Inhibited by histatin-3 1/24 (histatin-5). Ref.19
Subunit structure	Exists as monomer, disulfide-linked homodimer, and as a heterodimer with a 25 kDa protein. Macrophages and transformed cell lines produce only the monomeric form. Ref.18 Ref.23
Subcellular location	Secreted › extracellular space › extracellular matrix Probable.
Tissue specificity	Produced by normal alveolar macrophages and granulocytes.
Induction	Activated by 4-aminophenylmercuric acetate and phorbol ester. Ref.11 Ref.12
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	Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9. N- and O-glycosylated.
Involvement in disease	Defects in MMP9 may be a cause of susceptibility to lumbar disk herniation (LDH) [MIM:603932]. LDH is the predominant cause of low-back pain and unilateral leg pain. Ref.26
Miscellaneous	In the arthritis patient this enzyme might contribute to the pathogenesis of joint destruction and might constitute a useful marker of disease status.
Sequence similarities	Belongs to the peptidase M10A family. Contains 3 fibronectin type-II domains. Contains 4 hemopexin-like domains.

Ontologies

Keywords
Biological process	Collagen degradation
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW macrophage differentiation Traceable author statement. Source: UniProtKB positive regulation of keratinocyte migration Inferred from mutant phenotype. Source: UniProtKB proteolysis Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	extracellular space Inferred from direct assay. Source: UniProtKB proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW collagen binding Traceable author statement. Source: UniProtKB metalloendopeptidase activity Ref.1 Inferred from direct assay. Source: UniProtKB zinc ion binding Traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.11 Ref.12 Ref.1 Ref.10 Ref.13

Propeptide

20 – 93

74

Activation peptide

PRO_0000028754

Chain

94 – ?

67 kDa matrix metalloproteinase-9

PRO_0000028755

Chain

107 – 707

601

82 kDa matrix metalloproteinase-9

PRO_0000028756

Propeptide

? – 707

Removed in 64 kDa matrix metalloproteinase-9 and 67 kDa matrix metalloproteinase-9

PRO_0000028757

Regions

Domain

225 – 273

49

Fibronectin type-II 1

Domain

283 – 331

49

Fibronectin type-II 2

Domain

342 – 390

49

Fibronectin type-II 3

Domain

521 – 565

45

Hemopexin-like 1

Domain

567 – 608

42

Hemopexin-like 2

Domain

613 – 659

47

Hemopexin-like 3

Domain

661 – 704

44

Hemopexin-like 4

Motif

97 – 104

8

Cysteine switch By similarity

Sites

Active site

402

1

Metal binding

99

1

Zinc 2; in inhibited form

Metal binding

131

1

Calcium 1

Metal binding

165

1

Calcium 2; via carbonyl oxygen

Metal binding

175

1

Zinc 1; structural

Metal binding

177

1

Zinc 1; structural

Metal binding

182

1

Calcium 3

Metal binding

183

1

Calcium 3; via carbonyl oxygen

Metal binding

185

1

Calcium 3; via carbonyl oxygen

Metal binding

187

1

Calcium 3; via carbonyl oxygen

Metal binding

190

1

Zinc 1; structural

Metal binding

197

1

Calcium 2; via carbonyl oxygen

Metal binding

199

1

Calcium 2; via carbonyl oxygen

Metal binding

201

1

Calcium 2

Metal binding

203

1

Zinc 1; structural

Metal binding

205

1

Calcium 3

Metal binding

206

1

Calcium 1

Metal binding

208

1

Calcium 1

Metal binding

208

1

Calcium 3

Metal binding

401

1

Zinc 2; catalytic

Metal binding

405

1

Zinc 2; catalytic

Metal binding

411

1

Zinc 2; catalytic

Site

59 – 60

2

Cleavage; by MMP3

Site

106 – 107

2

Cleavage; by MMP3

Amino acid modifications

Glycosylation

38

1

N-linked (GlcNAc...) Potential

Glycosylation

120

1

N-linked (GlcNAc...) Potential

Glycosylation

127

1

N-linked (GlcNAc...) Potential

Disulfide bond

230 ↔ 256

By similarity

Disulfide bond

244 ↔ 271

By similarity

Disulfide bond

288 ↔ 314

By similarity

Disulfide bond

302 ↔ 329

By similarity

Disulfide bond

347 ↔ 373

By similarity

Disulfide bond

361 ↔ 388

By similarity

Disulfide bond

516 ↔ 704

Natural variations

Natural variant

20

1

A → V: dbSNP rs1805088. Ref.4 Ref.25

VAR_013780

Natural variant

38

1

N → S: dbSNP rs41427445.

VAR_037004

Natural variant

82

1

E → K: dbSNP rs1805089. Ref.25

VAR_013781

Natural variant

127

1

N → K: dbSNP rs3918252.

VAR_020054

Natural variant

239

1

R → H: dbSNP rs28763886. Ref.4

VAR_025165

Natural variant

279

1

Q → R Common polymorphism; may be associated with susceptibility to LDH. dbSNP rs17576. Ref.1 Ref.25 Ref.7

VAR_013782

Natural variant

571

1

F → V: dbSNP rs35691798. Ref.4

VAR_025166

Natural variant

574

1

P → R: dbSNP rs2250889. Ref.4 Ref.6

VAR_024595

Natural variant

668

1

R → Q: dbSNP rs17577. Ref.4

VAR_014742

Experimental info

Mutagenesis

402

1

E → Q: Loss of activity.

Sequence conflict

110

1

F → L in BAG35956. Ref.3

Secondary structure

1

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707

Helix Strand Turn

Details...

Helix

41 – 51

11

Helix

68 – 78

11

Helix

88 – 94

7

Beta strand

103 – 105

3

Beta strand

119 – 125

7

Beta strand

130 – 132

3

Helix

134 – 149

16

Beta strand

151 – 153

3

Beta strand

155 – 158

4

Beta strand

164 – 171

8

Beta strand

176 – 178

3

Beta strand

183 – 186

4

Beta strand

189 – 191

3

Beta strand

194 – 196

3

Turn

197 – 200

4

Beta strand

202 – 205

4

Beta strand

213 – 219

7

Helix

220 – 231

12

Beta strand

245 – 247

3

Beta strand

255 – 261

7

Helix

262 – 265

4

Beta strand

268 – 270

3

Turn

274 – 276

3

Beta strand

279 – 283

5

Beta strand

290 – 294

5

Beta strand

297 – 301

5

Beta strand

313 – 319

7

Helix

320 – 323

4

Beta strand

326 – 328

3

Helix

333 – 335

3

Turn

340 – 344

5

Beta strand

349 – 353

5

Beta strand

356 – 358

3

Beta strand

372 – 378

7

Helix

379 – 382

4

Beta strand

385 – 387

3

Beta strand

391 – 394

4

Helix

395 – 406

12

Beta strand

420 – 422

3

Helix

433 – 442

10

Helix

515 – 517

3

Beta strand

522 – 527

6

Beta strand

530 – 535

6

Beta strand

538 – 542

5

Beta strand

545 – 547

3

Beta strand

551 – 555

5

Helix

556 – 559

4

Beta strand

568 – 572

5

Turn

574 – 576

3

Beta strand

579 – 583

5

Beta strand

586 – 591

6

Beta strand

594 – 600

7

Helix

601 – 604

4

Beta strand

615 – 618

4

Beta strand

623 – 628

6

Beta strand

631 – 636

6

Turn

637 – 640

4

Helix

644 – 646

3

Helix

650 – 653

4

Beta strand

662 – 667

6

Beta strand

670 – 675

6

Beta strand

678 – 683

6

Beta strand

690 – 696

7

Turn

697 – 700

4

Sequences

	Sequence		Length	Mass (Da)
	P14780-1 [UniParc]. Last modified September 2, 2008. Version 2. Checksum: 7B65AC8E2B47880A	FASTA	707	78,399
	10 20 30 40 50 60 MSLWQPLVLV LLVLGCCFAA PRQRQSTLVL FPGDLRTNLT DRQLAEEYLY RYGYTRVAEM 70 80 90 100 110 120 RGESKSLGPA LLLLQKQLSL PETGELDSAT LKAMRTPRCG VPDLGRFQTF EGDLKWHHHN 130 140 150 160 170 180 ITYWIQNYSE DLPRAVIDDA FARAFALWSA VTPLTFTRVY SRDADIVIQF GVAEHGDGYP 190 200 210 220 230 240 FDGKDGLLAH AFPPGPGIQG DAHFDDDELW SLGKGVVVPT RFGNADGAAC HFPFIFEGRS 250 260 270 280 290 300 YSACTTDGRS DGLPWCSTTA NYDTDDRFGF CPSERLYTQD GNADGKPCQF PFIFQGQSYS 310 320 330 340 350 360 ACTTDGRSDG YRWCATTANY DRDKLFGFCP TRADSTVMGG NSAGELCVFP FTFLGKEYST 370 380 390 400 410 420 CTSEGRGDGR LWCATTSNFD SDKKWGFCPD QGYSLFLVAA HEFGHALGLD HSSVPEALMY 430 440 450 460 470 480 PMYRFTEGPP LHKDDVNGIR HLYGPRPEPE PRPPTTTTPQ PTAPPTVCPT GPPTVHPSER 490 500 510 520 530 540 PTAGPTGPPS AGPTGPPTAG PSTATTVPLS PVDDACNVNI FDAIAEIGNQ LYLFKDGKYW 550 560 570 580 590 600 RFSEGRGSRP QGPFLIADKW PALPRKLDSV FEEPLSKKLF FFSGRQVWVY TGASVLGPRR 610 620 630 640 650 660 LDKLGLGADV AQVTGALRSG RGKMLLFSGR RLWRFDVKAQ MVDPRSASEV DRMFPGVPLD 670 680 690 700 THDVFQYREK AYFCQDRFYW RVSSRSELNQ VDQVGYVTYD ILQCPED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages." Wilhelm S.M., Collier I.E., Marmer B.L., Eisen A.Z., Grant G.A., Goldberg G.I. J. Biol. Chem. 264:17213-17221(1989) [PubMed: 2551898] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-37, VARIANT ARG-279.
[2]	"Complete structure of the human gene for 92-kDa type IV collagenase. Divergent regulation of expression for the 92- and 72-kilodalton enzyme genes in HT-1080 cells." Huhtala P., Tuuttila A., Chow L.T., Lohi J., Keski-Oja J., Tryggvason K. J. Biol. Chem. 266:16485-16490(1991) [PubMed: 1653238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[4]	SeattleSNPs variation discovery resource Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-20; LYS-127; ARG-279; ARG-574 AND GLN-668.
[5]	NIEHS SNPs program Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-20; HIS-239; VAL-571; ARG-574 AND GLN-668.
[6]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-574.
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-279. Tissue: B-cell.
[8]	"Regulatory mechanism of 92 kDa type IV collagenase gene expression which is associated with invasiveness of tumor cells." Sato H., Seiki M. Oncogene 8:395-405(1993) [PubMed: 8426746] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
[9]	"Human neutrophil gelatinase: a marker for circulating blood neutrophils. Purification and quantitation by enzyme linked immunosorbent assay." Kjeldsen L., Bjerrum O.W., Hovgaard D., Johnsen A.H., Sehested M., Borregaard N. Eur. J. Haematol. 49:180-191(1992) [PubMed: 1464361] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-39, GLYCOSYLATION. Tissue: Neutrophil.
[10]	"The cytokine-protease connection: identification of a 96-kD THP-1 gelatinase and regulation by interleukin-1 and cytokine inducers." van Ranst M., Norga K., Masure S., Proost P., Vandekerckhove F., Auwerx J., van Damme J., Opdenakker G. Cytokine 3:231-239(1991) [PubMed: 1653055] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-37.
[11]	"Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9." Ogata Y., Enghild J.J., Nagase H. J. Biol. Chem. 267:3581-3584(1992) [PubMed: 1371271] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-34; 60-71 AND 107-118, INDUCTION, PROTEOLYTIC PROCESSING BY MMP3.
[12]	"Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. Purification and activation of the precursor and enzymic properties." Okada Y., Gonoji Y., Naka K., Tomita K., Nakanishi I., Iwata K., Yamashita K., Hayakawa T. J. Biol. Chem. 267:21712-21719(1992) [PubMed: 1400481] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-32 AND 94-111, PROTEOLYTIC PROCESSING, INDUCTION. Tissue: Fibrosarcoma.
[13]	"Proteolytic and non-proteolytic activation of human neutrophil progelatinase B." Sang Q.X., Birkedal-Hansen H., Van Wart H.E. Biochim. Biophys. Acta 1251:99-108(1995) [PubMed: 7669817] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-27; 60-67; 94-101 AND 107-113.
[14]	"Purification and identification of 91-kDa neutrophil gelatinase. Release by the activating peptide interleukin-8." Masure S., Proost P., van Damme J., Opdenakker G. Eur. J. Biochem. 198:391-398(1991) [PubMed: 1645657] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-60. Tissue: Neutrophil.
[15]	"Cytokine-mediated regulation of human leukocyte gelatinases and role in arthritis." Opdenakker G., Masure S., Grillet B., Van Damme J. Lymphokine Cytokine Res. 10:317-324(1991) [PubMed: 1932376] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-37.
[16]	"Latent collagenase and gelatinase from human neutrophils and their activation." Tschesche H., Knaeuper V., Kraemer S., Michaelis J., Oberhoff R., Reinke H. Matrix Suppl. 1:245-255(1992) [PubMed: 1480034] [Abstract] Cited for: PROTEIN SEQUENCE OF 93-115, FUNCTION, CATALYTIC ACTIVITY. Tissue: Blood.
[17]	"Purification and characterization of human 92-kDa type IV collagenase (gelatinase B)." Kang K., Lee D.-H. Exp. Mol. Med. 28:161-165(1996) Cited for: CHARACTERIZATION.
[18]	"Characterization of the monomeric and dimeric forms of latent and active matrix metalloproteinase-9. Differential rates for activation by stromelysin 1." Olson M.W., Bernardo M.M., Pietila M., Gervasi D.C., Toth M., Kotra L.P., Massova I., Mobashery S., Fridman R. J. Biol. Chem. 275:2661-2668(2000) [PubMed: 10644727] [Abstract] Cited for: SUBUNIT.
[19]	"Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal disease." Gusman H., Travis J., Helmerhorst E.J., Potempa J., Troxler R.F., Oppenheim F.G. Infect. Immun. 69:1402-1408(2001) [PubMed: 11179305] [Abstract] Cited for: ENZYME REGULATION.
[20]	"Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases." Takino T., Koshikawa N., Miyamori H., Tanaka M., Sasaki T., Okada Y., Seiki M., Sato H. Oncogene 22:4617-4626(2003) [PubMed: 12879005] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF KISS1.
[21]	"Structure of the C-terminally truncated human ProMMP9, a gelatin-binding matrix metalloproteinase." Elkins P.A., Ho Y.S., Smith W.W., Janson C.A., D'Alessio K.J., McQueney M.S., Cummings M.D., Romanic A.M. Acta Crystallogr. D 58:1182-1192(2002) [PubMed: 12077439] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-444 IN COMPLEX WITH ZINC AND MAGNESIUM IONS.
[22]	"Crystal structure of human MMP9 in complex with a reverse hydroxamate inhibitor." Rowsell S., Hawtin P., Minshull C.A., Jepson H., Brockbank S.M.V., Barratt D.G., Slater A.M., McPheat W.L., Waterson D., Henney A.M., Pauptit R.A. J. Mol. Biol. 319:173-181(2002) [PubMed: 12051944] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 107-215 IN COMPLEX WITH INHIBITOR; ZINC AND CALCIUM IONS, MUTAGENESIS OF GLU-402.
[23]	"Structural basis of the adaptive molecular recognition by MMP9." Cha H., Kopetzki E., Huber R., Lanzendoerfer M., Brandstetter H. J. Mol. Biol. 320:1065-1079(2002) [PubMed: 12126625] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 513-707, SUBUNIT.
[24]	"Theoretical model of human type IV collagenase precursor." Mallena S.C., Sagajkar R.D. Submitted (APR-2002) to the PDB data bank Cited for: 3D-STRUCTURE MODELING.
[25]	"Genetic variation at the matrix metalloproteinase-9 locus on chromosome 20q12.2-13.1." Zhang B., Henney A., Eriksson P., Hamsten A., Watkins H., Ye S. Hum. Genet. 105:418-423(1999) [PubMed: 10598806] [Abstract] Cited for: VARIANTS VAL-20; LYS-82 AND ARG-279.
[26]	"A functional polymorphism in THBS2 that affects alternative splicing and MMP binding is associated with lumbar-disc herniation." Hirose Y., Chiba K., Karasugi T., Nakajima M., Kawaguchi Y., Mikami Y., Furuichi T., Mio F., Miyake A., Miyamoto T., Ozaki K., Takahashi A., Mizuta H., Kubo T., Kimura T., Tanaka T., Toyama Y., Ikegawa S. Am. J. Hum. Genet. 82:1122-1129(2008) [PubMed: 18455130] [Abstract] Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO LDH.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

SeattleSNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

J05070 mRNA. Translation: AAA51539.1.
M68343 Genomic DNA. No translation available.
M68344 Genomic DNA. No translation available.
M68345 Genomic DNA. No translation available.
M68346 Genomic DNA. No translation available.
M68347 Genomic DNA. No translation available.
M68348 Genomic DNA. No translation available.
M68349 Genomic DNA. No translation available.
M68350 Genomic DNA. No translation available.
M68351 Genomic DNA. No translation available.
M68352 Genomic DNA. No translation available.
M68353 Genomic DNA. No translation available.
M68354 Genomic DNA. No translation available.
M68355 Genomic DNA. No translation available.
AK313137 mRNA. Translation: BAG35956.1.
AF538844 Genomic DNA. Translation: AAM97934.1.
DQ194553 Genomic DNA. Translation: ABA03169.1.
AL162458 Genomic DNA. Translation: CAC10459.1.
BC006093 mRNA. Translation: AAH06093.1.
D10051 Genomic DNA. Translation: BAA20967.1.

IPI

IPI00027509.

PIR

A34458.

RefSeq

NP_004985.2.

UniGene

Hs.297413

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GKC	X-ray	2.30	A/B	107-443	[»]
1GKD	X-ray	2.10	A/B	107-443	[»]
1ITV	X-ray	1.95	A/B	513-707	[»]
1L6J	X-ray	2.50	A	20-444	[»]
1LKG	model	-	A	1-707	[»]
2OVX	X-ray	2.00	A/B	110-443	[»]
2OVZ	X-ray	2.00	A/B	110-443	[»]
2OW0	X-ray	2.00	A/B	110-443	[»]
2OW1	X-ray	2.20	A/B	110-443	[»]
2OW2	X-ray	2.90	A/B	110-443	[»]

ModBase

Search...

Protein family/group databases

MEROPS

M10.004.

PTM databases

GlycoSuiteDB

P14780.

Proteomic databases

PeptideAtlas

P14780.

PRIDE

P14780.

Genome annotation databases

Ensembl

ENSG00000100985. Homo sapiens. [Contig view]

GeneID

4318.

KEGG

hsa:4318.

Organism-specific databases

GeneCards

GC20P044070.

H-InvDB

HIX0015874.

HGNC

HGNC:7176. MMP9.

HPA

CAB000348.
HPA001238.

MIM

120361. gene.
603932. phenotype.

PharmGKB

PA30889.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P14780.

HOVERGEN

P14780.

Enzyme and pathway databases

BRENDA

3.4.24.35. 247.

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.
fgf_pathway. FGF signaling pathway.
lysophospholipid_pathway. LPA receptor mediated events.
avb3_opn_pathway. Osteopontin-mediated events.
er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.
syndecan_4_pathway. Syndecan-4-mediated signaling events.

Gene expression databases

Bgee

P14780.

CleanEx

HS_MMP9.

GermOnline

ENSG00000100985. Homo sapiens.

Family and domain databases

InterPro

IPR000562. FN_type2_col_bd.
IPR000585. Hemopexin/matrixin.
IPR018486. Hemopexin/matrixin_CS.
IPR018487. Hemopexin/matrixin_repeat.
IPR001818. Pept_M10A_M12B.
IPR006025. Pept_M_Zn_BS.
IPR006026. Peptidase_M.
IPR002477. Peptidoglycan-bd-like.
IPR006970. PT.
[Graphical view]

Gene3D

G3DSA:2.110.10.10. Hemopexin. 1 hit.

Pfam

PF00040. fn2. 3 hits.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
PF04886. PT. 1 hit.
[Graphical view]

PRINTS

PR00013. FNTYPEII.
PR00138. MATRIXIN.

ProDom

PD000995. FN_Type_II. 2 hits.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]

PROSITE

PS00546. CYSTEINE_SWITCH. 1 hit.
PS00023. FN2_1. 3 hits.
PS51092. FN2_2. 3 hits.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB01296. Glucosamine.
DB00786. Marimastat.
DB01017. Minocycline.
DB00641. Simvastatin.

NextBio

16989.

SOURCE

Search...

Entry information

Entry name

MMP9_HUMAN

Accession

Primary (citable) accession number: P14780
Secondary accession number(s): B2R7V9 , Q3LR70, Q8N725, Q9H4Z1, Q9UCJ9, Q9UCL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	September 2, 2008
Last modified:	June 16, 2009
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)