Reviewed, UniProtKB/Swiss-Prot P08253 (MMP2_HUMAN)

Names and origin

Protein names

Recommended name:
    72 kDa type IV collagenase
    EC=3.4.24.24
Alternative name(s):
    72 kDa gelatinase
    Matrix metalloproteinase-2
      Short name=MMP-2
    Gelatinase A
    TBE-1

Gene names

Name:	MMP2
Synonyms:	CLG4A

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	660 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	In addition to gelatin and collagens, it cleaves KiSS1 at a Gly-|-Leu bond.
Catalytic activity	Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.
Cofactor	Binds 4 calcium ions per subunit. Binds 2 zinc ions per subunit.
Enzyme regulation	Inhibited by histatin-3 1/24 (histatin-5). Ref.9
Subunit structure	Ligand for integrin alpha-V/beta-3.
Subcellular location	Secreted › extracellular space › extracellular matrix Probable.
Tissue specificity	Produced by normal skin fibroblasts.
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 propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3).
Involvement in disease	Defects in MMP2 are the cause of Torg-Winchester syndrome [MIM:259600]; also called multicentric osteolysis nodulosis and arthropathy (MONA). Torg-Winchester syndrome is an autosomal recessive osteolysis syndrome. It is severe with generalized osteolysis and osteopenia. Subcutaneous nodules are usually absent. Torg-Winchester syndrome has been associated with a number of additional features including coarse face, corneal opacities, patches of thickened, hyperpigmented skin, hypertrichosis and gum hypertrophy. However, these features are not always present and have occasionally been observed in other osteolysis syndromes.
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
Disease	Disease mutation
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 proteolysis Ref.7 Traceable author statement. Source: ProtInc
Cellular component	extracellular space Ref.7 Inferred from direct assay. Source: MGI intracellular membrane-bounded organelle Inferred from direct assay. Source: HPA proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Ref.7 Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Ref.7 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP90AA1	P07900	1	EBI-1033518,EBI-296047

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Potential

Propeptide

30 – 109

80

Activation peptide

PRO_0000028714

Chain

110 – 660

551

72 kDa type IV collagenase

PRO_0000028715

Regions

Domain

228 – 276

49

Fibronectin type-II 1

Domain

286 – 334

49

Fibronectin type-II 2

Domain

344 – 392

49

Fibronectin type-II 3

Domain

475 – 518

44

Hemopexin-like 1

Domain

520 – 563

44

Hemopexin-like 2

Domain

568 – 615

48

Hemopexin-like 3

Domain

617 – 660

44

Hemopexin-like 4

Region

110 – 221

112

Collagenase-like 1

Region

222 – 396

175

Collagen-binding

Region

397 – 465

69

Collagenase-like 2

Motif

100 – 107

8

Cysteine switch By similarity

Sites

Active site

404

1

By similarity

Metal binding

102

1

Zinc 2; in inhibited form By similarity

Metal binding

134

1

Calcium 1 By similarity

Metal binding

168

1

Calcium 2 By similarity

Metal binding

178

1

Zinc 1 By similarity

Metal binding

180

1

Zinc 1 By similarity

Metal binding

185

1

Calcium 3 By similarity

Metal binding

186

1

Calcium 3; via carbonyl oxygen By similarity

Metal binding

193

1

Zinc 1 By similarity

Metal binding

200

1

Calcium 2; via carbonyl oxygen By similarity

Metal binding

202

1

Calcium 2; via carbonyl oxygen By similarity

Metal binding

204

1

Calcium 2 By similarity

Metal binding

206

1

Zinc 1 By similarity

Metal binding

208

1

Calcium 3 By similarity

Metal binding

209

1

Calcium 1 By similarity

Metal binding

211

1

Calcium 3 By similarity

Metal binding

403

1

Zinc 2; catalytic By similarity

Metal binding

407

1

Zinc 2; catalytic By similarity

Metal binding

413

1

Zinc 2; catalytic By similarity

Metal binding

476

1

Calcium 4; via carbonyl oxygen

Metal binding

521

1

Calcium 4; via carbonyl oxygen

Metal binding

569

1

Calcium 4; via carbonyl oxygen

Metal binding

618

1

Calcium 4; via carbonyl oxygen

Amino acid modifications

Glycosylation

573

1

N-linked (GlcNAc...) Potential

Glycosylation

642

1

N-linked (GlcNAc...) Potential

Disulfide bond

233 ↔ 259

By similarity

Disulfide bond

247 ↔ 274

By similarity

Disulfide bond

291 ↔ 317

By similarity

Disulfide bond

305 ↔ 332

By similarity

Disulfide bond

349 ↔ 375

By similarity

Disulfide bond

363 ↔ 390

By similarity

Disulfide bond

469 ↔ 660

Natural variations

Natural variant

101

1

R → H in Torg-Winchester syndrome.

VAR_032423

Natural variant

210

1

D → Y Ref.13

VAR_032424

Natural variant

228

1

A → T in a colorectal cancer sample; somatic mutation. Ref.16

VAR_036136

Natural variant

400

1

Missing in Torg-Winchester syndrome.

VAR_054996

Natural variant

404

1

E → K in Torg-Winchester syndrome.

VAR_032425

Natural variant

447

1

A → V: dbSNP rs17859943. Ref.4

VAR_020616

Natural variant

498

1

T → M in a colorectal cancer sample; somatic mutation. Ref.16

VAR_036137

Natural variant

621

1

V → L: dbSNP rs16955280. Ref.4

VAR_020617

Natural variant

644

1

S → I in a colorectal cancer sample; somatic mutation. Ref.16

VAR_036138

Experimental info

Sequence conflict

546

1

S → G in BAG35588. Ref.3

Sequence conflict

618

1

D → G in BAG35588. Ref.3

Secondary structure

1

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660

Helix Strand Turn

Details...

Helix

46 – 57

12

Turn

62 – 64

3

Helix

67 – 81

15

Helix

91 – 96

6

Beta strand

111 – 113

3

Beta strand

122 – 128

7

Helix

137 – 152

16

Beta strand

158 – 161

4

Beta strand

163 – 165

3

Beta strand

168 – 174

7

Beta strand

179 – 181

3

Beta strand

186 – 190

5

Beta strand

192 – 194

3

Beta strand

197 – 199

3

Turn

200 – 203

4

Beta strand

205 – 208

4

Beta strand

213 – 218

6

Turn

227 – 230

4

Beta strand

235 – 239

5

Beta strand

242 – 246

5

Beta strand

258 – 264

7

Helix

265 – 268

4

Beta strand

271 – 273

3

Turn

277 – 279

3

Beta strand

282 – 286

5

Beta strand

293 – 296

4

Beta strand

301 – 304

4

Beta strand

316 – 322

7

Helix

323 – 326

4

Beta strand

329 – 331

3

Turn

342 – 346

5

Beta strand

351 – 355

5

Beta strand

358 – 362

5

Beta strand

374 – 380

7

Helix

381 – 384

4

Beta strand

387 – 389

3

Helix

397 – 409

13

Beta strand

422 – 424

3

Helix

435 – 444

10

Turn

468 – 470

3

Beta strand

476 – 481

6

Beta strand

484 – 489

6

Beta strand

492 – 498

7

Beta strand

504 – 508

5

Helix

509 – 511

3

Beta strand

521 – 526

6

Turn

527 – 530

4

Beta strand

531 – 536

6

Beta strand

539 – 544

6

Beta strand

553 – 555

3

Helix

556 – 559

4

Beta strand

569 – 573

5

Turn

575 – 577

3

Beta strand

580 – 584

5

Beta strand

587 – 592

6

Turn

593 – 596

4

Helix

606 – 609

4

Beta strand

610 – 612

3

Beta strand

618 – 622

5

Turn

624 – 626

3

Beta strand

628 – 633

6

Beta strand

636 – 641

6

Beta strand

644 – 652

9

Helix

653 – 656

4

Sequences

	Sequence		Length	Mass (Da)
	P08253-1 [UniParc]. Last modified February 1, 1991. Version 2. Checksum: BC7147DC8B49F289	FASTA	660	73,882
	10 20 30 40 50 60 MEALMARGAL TGPLRALCLL GCLLSHAAAA PSPIIKFPGD VAPKTDKELA VQYLNTFYGC 70 80 90 100 110 120 PKESCNLFVL KDTLKKMQKF FGLPQTGDLD QNTIETMRKP RCGNPDVANY NFFPRKPKWD 130 140 150 160 170 180 KNQITYRIIG YTPDLDPETV DDAFARAFQV WSDVTPLRFS RIHDGEADIM INFGRWEHGD 190 200 210 220 230 240 GYPFDGKDGL LAHAFAPGTG VGGDSHFDDD ELWTLGEGQV VRVKYGNADG EYCKFPFLFN 250 260 270 280 290 300 GKEYNSCTDT GRSDGFLWCS TTYNFEKDGK YGFCPHEALF TMGGNAEGQP CKFPFRFQGT 310 320 330 340 350 360 SYDSCTTEGR TDGYRWCGTT EDYDRDKKYG FCPETAMSTV GGNSEGAPCV FPFTFLGNKY 370 380 390 400 410 420 ESCTSAGRSD GKMWCATTAN YDDDRKWGFC PDQGYSLFLV AAHEFGHAMG LEHSQDPGAL 430 440 450 460 470 480 MAPIYTYTKN FRLSQDDIKG IQELYGASPD IDLGTGPTPT LGPVTPEICK QDIVFDGIAQ 490 500 510 520 530 540 IRGEIFFFKD RFIWRTVTPR DKPMGPLLVA TFWPELPEKI DAVYEAPQEE KAVFFAGNEY 550 560 570 580 590 600 WIYSASTLER GYPKPLTSLG LPPDVQRVDA AFNWSKNKKT YIFAGDKFWR YNEVKKKMDP 610 620 630 640 650 660 GFPKLIADAW NAIPDNLDAV VDLQGGGHSY FFKGAYYLKL ENQSLKSVKF GSIKSDWLGC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the human type IV collagenase gene." Huhtala P., Chow L.T., Tryggvason K. J. Biol. Chem. 265:11077-11082(1990) [PubMed: 2162831] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"On the structure and chromosome location of the 72- and 92-kDa human type IV collagenase genes." Collier I.E., Bruns G.A.P., Goldberg G.I., Gerhard D.S. Genomics 9:429-434(1991) [PubMed: 1851724] [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: Teratocarcinoma.
[4]	NIEHS SNPs program Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-447 AND LEU-621.
[5]	"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]. Tissue: Brain.
[6]	"Completion of the primary structure of the human type IV collagenase preproenzyme and assignment of the gene (CLG4) to the q21 region of chromosome 16." Huhtala P., Eddy R.L., Fan Y.S., Byers M.G., Shows T.B., Tryggvason K. Genomics 6:554-559(1990) [PubMed: 2158484] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
[7]	"H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen." Collier I.E., Wilhelm S.M., Eisen A.Z., Marmer B.L., Grant G.A., Seltzer J.L., Kronberger A., He C., Bauer E.A., Goldberg G.I. J. Biol. Chem. 263:6579-6587(1988) [PubMed: 2834383] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-660, PARTIAL PROTEIN SEQUENCE.
[8]	"TIMP-2: identification and characterization of a new member of the metalloproteinase inhibitor family." Stetler-Stevenson W.G., Krutzsch H.C., Liotta L.A. Matrix Suppl. 1:299-306(1992) [PubMed: 1480041] [Abstract] Cited for: PROTEIN SEQUENCE OF 30-44. Tissue: Melanoma.
[9]	"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.
[10]	"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.
[11]	"Crystal structure of the haemopexin-like C-terminal domain of gelatinase A." Libson A.M., Gittis A.G., Collier I.E., Marmer B.L., Goldberg G.I., Lattman E.E. Nat. Struct. Biol. 2:938-942(1995) [PubMed: 7583664] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 443-660.
[12]	"The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function." Gohlke U., Gomis-Rueth F.-X., Crabbe T., Murphy G., Docherty A.J., Bode W. FEBS Lett. 378:126-130(1996) [PubMed: 8549817] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 458-660.
[13]	"Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a multicentric osteolysis and arthritis syndrome." Martignetti J.A., Aqeel A.A., Sewairi W.A., Boumah C.E., Kambouris M., Mayouf S.A., Sheth K.V., Eid W.A., Dowling O., Harris J., Glucksman M.J., Bahabri S., Meyer B.F., Desnick R.J. Nat. Genet. 28:261-265(2001) [PubMed: 11431697] [Abstract] Cited for: VARIANT TORG-WINCHESTER SYNDROME HIS-101, VARIANT TYR-210.
[14]	"Winchester syndrome caused by a homozygous mutation affecting the active site of matrix metalloproteinase 2." Zankl A., Bonafe L., Calcaterra V., Di Rocco M., Superti-Furga A. Clin. Genet. 67:261-266(2005) [PubMed: 15691365] [Abstract] Cited for: VARIANT TORG-WINCHESTER SYNDROME LYS-404.
[15]	"A novel homozygous MMP2 mutation in a family with Winchester syndrome." Rouzier C., Vanatka R., Bannwarth S., Philip N., Coussement A., Paquis-Flucklinger V., Lambert J.-C. Clin. Genet. 69:271-276(2006) [PubMed: 16542393] [Abstract] Cited for: VARIANT TORG-WINCHESTER SYNDROME VAL-400 DEL.
[16]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-228; MET-498 AND ILE-644.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

M55593 , M58552, M55582, M55583, M55584, M55585, M55586, M55587, M55588, M55589, M55590, M55591, M55592 Genomic DNA. Translation: AAA52028.1.
AK312711 mRNA. Translation: BAG35588.1.
AY738117 Genomic DNA. Translation: AAU10089.1.
BC002576 mRNA. Translation: AAH02576.1.
M33789 Genomic DNA. Translation: AAA52027.1.
J03210 mRNA. Translation: AAA35701.1.

IPI

IPI00027780.

PIR

A28153.

RefSeq

NP_001121363.1.
NP_004521.1.

UniGene

Hs.513617

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CK7	X-ray	2.80	A	30-660	[»]
1CXW	NMR	-	A	278-336	[»]
1EAK	X-ray	2.66	A/B/C/D	32-452	[»]
1GEN	X-ray	2.15	A	443-660	[»]
1GXD	X-ray	3.10	A/B	30-660	[»]
1HOV	NMR	-	A	110-446	[»]
1J7M	NMR	-	A	337-394	[»]
1KS0	NMR	-	A	223-282	[»]
1QIB	X-ray	2.80	A	115-449	[»]
1RTG	X-ray	2.60	A	451-660	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:26N.

IntAct

P08253. 2 interactions.

Protein family/group databases

MEROPS

M10.003.

PTM databases

PhosphoSite

P08253.

Proteomic databases

PeptideAtlas

P08253.

PRIDE

P08253.

Genome annotation databases

Ensembl

ENSG00000087245. Homo sapiens. [Contig view]

GeneID

4313.

NMPDR

fig|9606.3.peg.12256.

Organism-specific databases

GeneCards

GC16P054070.

H-InvDB

HIX0013041.
HIX0040455.

HGNC

HGNC:7166. MMP2.

HPA

CAB002788.
HPA001939.

MIM

120360. gene.
259600. phenotype.

Orphanet

85196. Nodulosis-arthropathy-osteolysis syndrome.
3460. Winchester disease.

PharmGKB

PA30877.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P08253.

HOVERGEN

P08253.

OMA

P08253. DDDRKWG.

Enzyme and pathway databases

BRENDA

3.4.24.24. 247.

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.
foxm1pathway. FOXM1 transcription factor network.
lysophospholipid_pathway. LPA receptor mediated events.
avb3_opn_pathway. Osteopontin-mediated events.
er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.
syndecan_2_pathway. Syndecan-2-mediated signaling events.

Gene expression databases

ArrayExpress

P08253.

Bgee

P08253.

CleanEx

HS_MMP2.

GermOnline

ENSG00000087245. 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.
[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.
[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

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Other Resources

DrugBank

DB00786. Marimastat.
DB00605. Sulindac.

NextBio

16973.

PMAP-CutDB

P08253.

SOURCE

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Entry information

Entry name

MMP2_HUMAN

Accession

Primary (citable) accession number: P08253
Secondary accession number(s): B2R6U1, Q9UCJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	February 1, 1991
Last modified:	June 16, 2009
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)