SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P08253

- MMP2_HUMAN

UniProt

P08253 - MMP2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
72 kDa type IV collagenase
Gene
MMP2, CLG4A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14.8 Publications
PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.8 Publications
Isoform 2: Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.8 Publications

Catalytic activityi

Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.

Cofactori

Binds 4 calcium ions per subunit.
Binds 2 zinc ions per subunit.

Enzyme regulationi

Inhibited by histatin-3 1/24 (histatin-5).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi102 – 1021Zinc 2; in inhibited form By similarity
Metal bindingi134 – 1341Calcium 1 By similarity
Metal bindingi168 – 1681Calcium 2 By similarity
Metal bindingi178 – 1781Zinc 1 By similarity
Metal bindingi180 – 1801Zinc 1 By similarity
Metal bindingi185 – 1851Calcium 3 By similarity
Metal bindingi186 – 1861Calcium 3; via carbonyl oxygen By similarity
Metal bindingi193 – 1931Zinc 1 By similarity
Metal bindingi200 – 2001Calcium 2; via carbonyl oxygen By similarity
Metal bindingi202 – 2021Calcium 2; via carbonyl oxygen By similarity
Metal bindingi204 – 2041Calcium 2 By similarity
Metal bindingi206 – 2061Zinc 1 By similarity
Metal bindingi208 – 2081Calcium 3 By similarity
Metal bindingi209 – 2091Calcium 1 By similarity
Metal bindingi211 – 2111Calcium 3 By similarity
Metal bindingi403 – 4031Zinc 2; catalytic By similarity
Active sitei404 – 4041 By similarity
Metal bindingi407 – 4071Zinc 2; catalytic By similarity
Metal bindingi413 – 4131Zinc 2; catalytic By similarity
Metal bindingi476 – 4761Calcium 4; via carbonyl oxygen
Metal bindingi521 – 5211Calcium 4; via carbonyl oxygen
Metal bindingi569 – 5691Calcium 4; via carbonyl oxygen
Metal bindingi618 – 6181Calcium 4; via carbonyl oxygen

GO - Molecular functioni

  1. metalloendopeptidase activity Source: ProtInc
  2. protein binding Source: IntAct
  3. serine-type endopeptidase activity Source: Reactome
  4. zinc ion binding Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. blood vessel maturation Source: Ensembl
  3. bone trabecula formation Source: Ensembl
  4. cellular protein metabolic process Source: Reactome
  5. cellular response to amino acid stimulus Source: Ensembl
  6. collagen catabolic process Source: Reactome
  7. embryo implantation Source: Ensembl
  8. extracellular matrix disassembly Source: Reactome
  9. extracellular matrix organization Source: Reactome
  10. face morphogenesis Source: Ensembl
  11. intramembranous ossification Source: Ensembl
  12. proteolysis Source: ProtInc
  13. response to hypoxia Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Angiogenesis, Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS01565-MONOMER.
BRENDAi3.4.24.24. 2681.
ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_150401. Collagen degradation.
REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
REACT_197191. Collagen degradation.
REACT_222620. Collagen degradation.

Protein family/group databases

MEROPSiM10.003.

Names & Taxonomyi

Protein namesi
Recommended name:
72 kDa type IV collagenase (EC:3.4.24.24)
Alternative name(s):
72 kDa gelatinase
Gelatinase A
Matrix metalloproteinase-2
Short name:
MMP-2
TBE-1
Cleaved into the following chain:
Gene namesi
Name:MMP2
Synonyms:CLG4A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:7166. MMP2.

Subcellular locationi

Isoform 1 : Secretedextracellular spaceextracellular matrix. Membrane. Nucleus
Note: Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes.3 Publications
Isoform 2 : Cytoplasm. Mitochondrion 3 Publications

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: BHF-UCL
  3. mitochondrion Source: UniProtKB-SubCell
  4. nucleus Source: UniProtKB-SubCell
  5. plasma membrane Source: Ensembl
  6. proteinaceous extracellular matrix Source: UniProtKB-SubCell
  7. sarcomere Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Extracellular matrix, Membrane, Mitochondrion, Nucleus, Secreted

Pathology & Biotechi

Involvement in diseasei

Multicentric osteolysis, nodulosis, and arthropathy (MONA) [MIM:259600]: An autosomal recessive syndrome characterized by severe multicentric osteolysis with predominant involvement of the hands and feet. Additional features include coarse face, corneal opacities, patches of thickened, hyperpigmented skin, hypertrichosis and gum hypertrophy.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti101 – 1011R → H in MONA. 1 Publication
VAR_032423
Natural varianti400 – 4001Missing in MONA. 1 Publication
VAR_054996
Natural varianti404 – 4041E → K in MONA. 1 Publication
VAR_032425

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi259600. phenotype.
Orphaneti85196. Nodulosis-arthropathy-osteolysis syndrome.
3460. Torg-Winchester syndrome.
PharmGKBiPA30877.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929 Reviewed prediction
Add
BLAST
Propeptidei30 – 10980Activation peptide
PRO_0000028714Add
BLAST
Chaini110 – 66055172 kDa type IV collagenase
PRO_0000028715Add
BLAST
Chaini445 – 660216PEX
PRO_0000391626Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi233 ↔ 259 By similarity
Disulfide bondi247 ↔ 274 By similarity
Disulfide bondi291 ↔ 317 By similarity
Disulfide bondi305 ↔ 332 By similarity
Disulfide bondi349 ↔ 375 By similarity
Disulfide bondi363 ↔ 390 By similarity
Disulfide bondi469 ↔ 6601 Publication
Glycosylationi573 – 5731N-linked (GlcNAc...) Reviewed prediction
Glycosylationi642 – 6421N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro.1 Publication
The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3). Autocatalytic cleavage in the C-terminal produces the anti-angiogenic peptide, PEX. This processing appears to be facilitated by binding integrinv/beta3.

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiP08253.
PaxDbiP08253.
PeptideAtlasiP08253.
PRIDEiP08253.

PTM databases

PhosphoSiteiP08253.

Miscellaneous databases

PMAP-CutDBP08253.

Expressioni

Tissue specificityi

Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate.1 Publication

Inductioni

Aspirin appears to inhibit expression.2 Publications

Gene expression databases

ArrayExpressiP08253.
BgeeiP08253.
CleanExiHS_MMP2.
GenevestigatoriP08253.

Organism-specific databases

HPAiCAB002788.
HPA001939.

Interactioni

Subunit structurei

Interacts (via the C-terminal hemopexin-like domains-containing region) with the integrin alpha-V/beta-3; the interaction promotes vascular invasion in angiogenic vessels and melamoma cells. Interacts (via the C-terminal PEX domain) with TIMP2 (via the C-terminal); the interaction inhibits the degradation activity. Interacts with GSK3B.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SCUBE3Q8IX302EBI-1033518,EBI-4479975

Protein-protein interaction databases

BioGridi110457. 18 interactions.
DIPiDIP-26N.
IntActiP08253. 9 interactions.
STRINGi9606.ENSP00000219070.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi46 – 5611
Turni62 – 643
Helixi67 – 8014
Beta strandi86 – 883
Helixi91 – 977
Beta strandi111 – 1133
Beta strandi120 – 1289
Beta strandi133 – 1353
Helixi137 – 15216
Beta strandi154 – 1563
Beta strandi158 – 1614
Beta strandi163 – 1653
Beta strandi168 – 1747
Beta strandi179 – 1813
Beta strandi186 – 1894
Beta strandi192 – 1954
Beta strandi197 – 1993
Turni200 – 2034
Beta strandi205 – 2084
Beta strandi209 – 2113
Beta strandi213 – 2164
Helixi226 – 2283
Beta strandi235 – 2395
Beta strandi242 – 2465
Beta strandi258 – 2647
Turni265 – 2673
Beta strandi271 – 2733
Turni277 – 2793
Turni284 – 2885
Beta strandi293 – 2975
Beta strandi300 – 3045
Beta strandi316 – 3216
Turni323 – 3253
Beta strandi329 – 3313
Beta strandi338 – 3414
Turni342 – 3465
Beta strandi351 – 3555
Beta strandi358 – 3625
Beta strandi369 – 3713
Beta strandi374 – 3796
Helixi381 – 3844
Beta strandi387 – 3893
Beta strandi394 – 3963
Helixi397 – 40812
Beta strandi422 – 4243
Helixi435 – 44511
Turni468 – 4703
Beta strandi476 – 4816
Beta strandi484 – 4896
Beta strandi492 – 4987
Beta strandi504 – 5085
Helixi509 – 5113
Beta strandi514 – 5163
Beta strandi521 – 5266
Turni527 – 5304
Beta strandi531 – 5366
Beta strandi539 – 5446
Beta strandi553 – 5553
Helixi556 – 5594
Turni563 – 5664
Beta strandi569 – 5735
Turni575 – 5773
Beta strandi580 – 5845
Beta strandi587 – 5926
Turni593 – 5964
Helixi606 – 6094
Beta strandi610 – 6123
Beta strandi618 – 6225
Turni624 – 6263
Beta strandi628 – 6336
Beta strandi636 – 6416
Beta strandi644 – 6529
Helixi653 – 6564

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CK7X-ray2.80A30-660[»]
1CXWNMR-A278-336[»]
1EAKX-ray2.66A/B/C/D32-452[»]
1GENX-ray2.15A443-660[»]
1GXDX-ray3.10A/B30-660[»]
1HOVNMR-A110-431[»]
1J7MNMR-A337-394[»]
1KS0NMR-A223-282[»]
1QIBX-ray2.80A115-217[»]
A394-449[»]
1RTGX-ray2.60A451-660[»]
3AYUX-ray2.00A110-450[»]
ProteinModelPortaliP08253.
SMRiP08253. Positions 30-660.

Miscellaneous databases

EvolutionaryTraceiP08253.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini228 – 27649Fibronectin type-II 1
Add
BLAST
Domaini286 – 33449Fibronectin type-II 2
Add
BLAST
Domaini344 – 39249Fibronectin type-II 3
Add
BLAST
Repeati472 – 51645Hemopexin 1
Add
BLAST
Repeati517 – 56347Hemopexin 2
Add
BLAST
Repeati565 – 61349Hemopexin 3
Add
BLAST
Repeati614 – 66047Hemopexin 4
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni110 – 221112Collagenase-like 1
Add
BLAST
Regioni222 – 396175Collagen-binding
Add
BLAST
Regioni397 – 46569Collagenase-like 2
Add
BLAST
Regioni414 – 660247Required for inhibitor TIMP2 binding
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi100 – 1078Cysteine 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

Phylogenomic databases

eggNOGiNOG303159.
HOGENOMiHOG000217926.
HOVERGENiHBG052484.
InParanoidiP08253.
KOiK01398.
OMAiPCKFPFR.
OrthoDBiEOG70KGNX.
PhylomeDBiP08253.
TreeFamiTF315428.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
2.10.10.10. 3 hits.
2.110.10.10. 1 hit.
3.40.390.10. 2 hits.
InterProiIPR028708. 72kDa_collagenase.
IPR000562. FN_type2_col-bd.
IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR013806. Kringle-like.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF29. PTHR10201:SF29. 1 hit.
PfamiPF00040. fn2. 3 hits.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
SSF57440. SSF57440. 3 hits.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00023. FN2_1. 3 hits.
PS51092. FN2_2. 3 hits.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P08253-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MEALMARGAL TGPLRALCLL GCLLSHAAAA PSPIIKFPGD VAPKTDKELA    50
VQYLNTFYGC PKESCNLFVL KDTLKKMQKF FGLPQTGDLD QNTIETMRKP 100
RCGNPDVANY NFFPRKPKWD KNQITYRIIG YTPDLDPETV DDAFARAFQV 150
WSDVTPLRFS RIHDGEADIM INFGRWEHGD GYPFDGKDGL LAHAFAPGTG 200
VGGDSHFDDD ELWTLGEGQV VRVKYGNADG EYCKFPFLFN GKEYNSCTDT 250
GRSDGFLWCS TTYNFEKDGK YGFCPHEALF TMGGNAEGQP CKFPFRFQGT 300
SYDSCTTEGR TDGYRWCGTT EDYDRDKKYG FCPETAMSTV GGNSEGAPCV 350
FPFTFLGNKY ESCTSAGRSD GKMWCATTAN YDDDRKWGFC PDQGYSLFLV 400
AAHEFGHAMG LEHSQDPGAL MAPIYTYTKN FRLSQDDIKG IQELYGASPD 450
IDLGTGPTPT LGPVTPEICK QDIVFDGIAQ IRGEIFFFKD RFIWRTVTPR 500
DKPMGPLLVA TFWPELPEKI DAVYEAPQEE KAVFFAGNEY WIYSASTLER 550
GYPKPLTSLG LPPDVQRVDA AFNWSKNKKT YIFAGDKFWR YNEVKKKMDP 600
GFPKLIADAW NAIPDNLDAV VDLQGGGHSY FFKGAYYLKL ENQSLKSVKF 650
GSIKSDWLGC 660
Length:660
Mass (Da):73,882
Last modified:February 1, 1991 - v2
Checksum:iBC7147DC8B49F289
GO
Isoform 2 (identifier: P08253-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-76: Missing.

Note: Induced by oxidative stress.

Show »
Length:584
Mass (Da):65,765
Checksum:iEC1C16C91ECBC26C
GO
Isoform 3 (identifier: P08253-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAV → M

Note: No experimental confirmation available.

Show »
Length:610
Mass (Da):68,831
Checksum:iFB214CA4334DC5FC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti101 – 1011R → H in MONA. 1 Publication
VAR_032423
Natural varianti210 – 2101D → Y.1 Publication
VAR_032424
Natural varianti228 – 2281A → T in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036136
Natural varianti400 – 4001Missing in MONA. 1 Publication
VAR_054996
Natural varianti404 – 4041E → K in MONA. 1 Publication
VAR_032425
Natural varianti447 – 4471A → V.1 Publication
Corresponds to variant rs17859943 [ dbSNP | Ensembl ].
VAR_020616
Natural varianti498 – 4981T → M in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036137
Natural varianti621 – 6211V → L.1 Publication
Corresponds to variant rs16955280 [ dbSNP | Ensembl ].
VAR_020617
Natural varianti644 – 6441S → I in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036138

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7676Missing in isoform 2.
VSP_044631Add
BLAST
Alternative sequencei1 – 5151MEALM…KELAV → M in isoform 3.
VSP_045704Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti235 – 2351F → S in AK310314. 1 Publication
Sequence conflicti546 – 5461S → G in BAG35588. 1 Publication
Sequence conflicti618 – 6181D → G in BAG35588. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55593
, M58552, M55582, M55583, M55584, M55585, M55586, M55587, M55588, M55589, M55590, M55591, M55592 Genomic DNA. Translation: AAA52028.1.
AK301536 mRNA. Translation: BAG63035.1.
AK310314 mRNA. No translation available.
AK312711 mRNA. Translation: BAG35588.1.
AY738117 Genomic DNA. Translation: AAU10089.1.
AC007336 Genomic DNA. No translation available.
AC092722 Genomic DNA. No translation available.
BC002576 mRNA. Translation: AAH02576.1.
M33789 Genomic DNA. Translation: AAA52027.1.
J03210 mRNA. Translation: AAA35701.1.
CCDSiCCDS10752.1. [P08253-1]
CCDS45487.1. [P08253-3]
PIRiA28153.
RefSeqiNP_001121363.1. NM_001127891.1. [P08253-3]
NP_004521.1. NM_004530.4. [P08253-1]
UniGeneiHs.513617.

Genome annotation databases

EnsembliENST00000219070; ENSP00000219070; ENSG00000087245. [P08253-1]
ENST00000437642; ENSP00000394237; ENSG00000087245. [P08253-3]
ENST00000543485; ENSP00000444143; ENSG00000087245. [P08253-2]
ENST00000570308; ENSP00000461421; ENSG00000087245. [P08253-2]
GeneIDi4313.
KEGGihsa:4313.
UCSCiuc002ehz.4. human. [P08253-1]

Polymorphism databases

DMDMi116856.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55593
, M58552 , M55582 , M55583 , M55584 , M55585 , M55586 , M55587 , M55588 , M55589 , M55590 , M55591 , M55592 Genomic DNA. Translation: AAA52028.1 .
AK301536 mRNA. Translation: BAG63035.1 .
AK310314 mRNA. No translation available.
AK312711 mRNA. Translation: BAG35588.1 .
AY738117 Genomic DNA. Translation: AAU10089.1 .
AC007336 Genomic DNA. No translation available.
AC092722 Genomic DNA. No translation available.
BC002576 mRNA. Translation: AAH02576.1 .
M33789 Genomic DNA. Translation: AAA52027.1 .
J03210 mRNA. Translation: AAA35701.1 .
CCDSi CCDS10752.1. [P08253-1 ]
CCDS45487.1. [P08253-3 ]
PIRi A28153.
RefSeqi NP_001121363.1. NM_001127891.1. [P08253-3 ]
NP_004521.1. NM_004530.4. [P08253-1 ]
UniGenei Hs.513617.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 110-431 [» ]
1J7M NMR - A 337-394 [» ]
1KS0 NMR - A 223-282 [» ]
1QIB X-ray 2.80 A 115-217 [» ]
A 394-449 [» ]
1RTG X-ray 2.60 A 451-660 [» ]
3AYU X-ray 2.00 A 110-450 [» ]
ProteinModelPortali P08253.
SMRi P08253. Positions 30-660.
ModBasei Search...

Protein-protein interaction databases

BioGridi 110457. 18 interactions.
DIPi DIP-26N.
IntActi P08253. 9 interactions.
STRINGi 9606.ENSP00000219070.

Chemistry

BindingDBi P08253.
ChEMBLi CHEMBL2095216.
DrugBanki DB00786. Marimastat.
DB00605. Sulindac.
GuidetoPHARMACOLOGYi 1629.

Protein family/group databases

MEROPSi M10.003.

PTM databases

PhosphoSitei P08253.

Polymorphism databases

DMDMi 116856.

Proteomic databases

MaxQBi P08253.
PaxDbi P08253.
PeptideAtlasi P08253.
PRIDEi P08253.

Protocols and materials databases

DNASUi 4313.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000219070 ; ENSP00000219070 ; ENSG00000087245 . [P08253-1 ]
ENST00000437642 ; ENSP00000394237 ; ENSG00000087245 . [P08253-3 ]
ENST00000543485 ; ENSP00000444143 ; ENSG00000087245 . [P08253-2 ]
ENST00000570308 ; ENSP00000461421 ; ENSG00000087245 . [P08253-2 ]
GeneIDi 4313.
KEGGi hsa:4313.
UCSCi uc002ehz.4. human. [P08253-1 ]

Organism-specific databases

CTDi 4313.
GeneCardsi GC16P055424.
HGNCi HGNC:7166. MMP2.
HPAi CAB002788.
HPA001939.
MIMi 120360. gene.
259600. phenotype.
neXtProti NX_P08253.
Orphaneti 85196. Nodulosis-arthropathy-osteolysis syndrome.
3460. Torg-Winchester syndrome.
PharmGKBi PA30877.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG303159.
HOGENOMi HOG000217926.
HOVERGENi HBG052484.
InParanoidi P08253.
KOi K01398.
OMAi PCKFPFR.
OrthoDBi EOG70KGNX.
PhylomeDBi P08253.
TreeFami TF315428.

Enzyme and pathway databases

BioCyci MetaCyc:HS01565-MONOMER.
BRENDAi 3.4.24.24. 2681.
Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_150401. Collagen degradation.
REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
REACT_197191. Collagen degradation.
REACT_222620. Collagen degradation.

Miscellaneous databases

ChiTaRSi MMP2. human.
EvolutionaryTracei P08253.
GeneWikii MMP2.
GenomeRNAii 4313.
NextBioi 16973.
PMAP-CutDB P08253.
PROi P08253.
SOURCEi Search...

Gene expression databases

ArrayExpressi P08253.
Bgeei P08253.
CleanExi HS_MMP2.
Genevestigatori P08253.

Family and domain databases

Gene3Di 1.10.101.10. 1 hit.
2.10.10.10. 3 hits.
2.110.10.10. 1 hit.
3.40.390.10. 2 hits.
InterProi IPR028708. 72kDa_collagenase.
IPR000562. FN_type2_col-bd.
IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR013806. Kringle-like.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view ]
PANTHERi PTHR10201:SF29. PTHR10201:SF29. 1 hit.
Pfami PF00040. fn2. 3 hits.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view ]
PRINTSi PR00138. MATRIXIN.
SMARTi SM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
SSF57440. SSF57440. 3 hits.
PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
PS00023. FN2_1. 3 hits.
PS51092. FN2_2. 3 hits.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the human type IV collagenase gene."
    Huhtala P., Chow L.T., Tryggvason K.
    J. Biol. Chem. 265:11077-11082(1990) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Teratocarcinoma and Testis.
  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 sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Brain.
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
  8. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-660 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  9. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-44.
    Tissue: Melanoma.
  10. "Binding of tissue inhibitor of metalloproteinases 2 to two distinct sites on human 72-kDa gelatinase. Identification of a stabilization site."
    Howard E.W., Banda M.J.
    J. Biol. Chem. 266:17972-17977(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIMP2.
  11. "Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3."
    Brooks P.C., Stroemblad S., Sanders L.C., von Schalscha T.L., Aimes R.T., Stetler-Stevenson W.G., Quigley J.P., Cheresh D.A.
    Cell 85:683-693(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF RECEPTOR, SUBCELLULAR LOCATION.
  12. "Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases."
    Butler G.S., Will H., Atkinson S.J., Murphy G.
    Eur. J. Biochem. 244:653-657(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  13. "Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity."
    Brooks P.C., Silletti S., von Schalscha T.L., Friedlander M., Cheresh D.A.
    Cell 92:391-400(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF RECEPTOR, FUNCTION.
  14. "Vascular matrix metalloproteinase-2 cleaves big endothelin-1 yielding a novel vasoconstrictor."
    Fernandez-Patron C., Radomski M.W., Davidge S.T.
    Circ. Res. 85:906-911(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Vascular matrix metalloproteinase-2-dependent cleavage of calcitonin gene-related peptide promotes vasoconstriction."
    Fernandez-Patron C., Stewart K.G., Zhang Y., Koivunen E., Radomski M.W., Davidge S.T.
    Circ. Res. 87:670-676(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Simultaneous inhibition of glioma angiogenesis, cell proliferation, and invasion by a naturally occurring fragment of human metalloproteinase-2."
    Bello L., Lucini V., Carrabba G., Giussani C., Machluf M., Pluderi M., Nikas D., Zhang J., Tomei G., Villani R.M., Carroll R.S., Bikfalvi A., Black P.M.
    Cancer Res. 61:8730-8736(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF PEX, TISSUE SPECIFICITY, INTERACTION WITH TIMP2.
  17. "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] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  18. "Human cervical tumor cell (SiHa) surface alphavbeta3 integrin receptor has associated matrix metalloproteinase (MMP-2) activity."
    Chattopadhyay N., Mitra A., Frei E., Chatterjee A.
    J. Cancer Res. Clin. Oncol. 127:653-658(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF RECEPTOR, INTERACTION WITH TMP2, FUNCTION.
  19. "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.
  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] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF KISS1.
  21. "Matrix metalloproteinase-2 (MMP-2) is present in the nucleus of cardiac myocytes and is capable of cleaving poly (ADP-ribose) polymerase (PARP) in vitro."
    Kwan J.A., Schulze C.J., Wang W., Leon H., Sariahmetoglu M., Sung M., Sawicka J., Sims D.E., Sawicki G., Schulz R.
    FASEB J. 18:690-692(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  22. Cited for: PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
  23. "Glycogen synthase kinase-3beta is activated by matrix metalloproteinase-2 mediated proteolysis in cardiomyoblasts."
    Kandasamy A.D., Schulz R.
    Cardiovasc. Res. 83:698-706(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GSK3B, FUNCTION.
  24. "Aspirin inhibits MMP-2 and MMP-9 expressions and activities through upregulation of PPARalpha/gamma and TIMP gene expressions in ox-LDL-stimulated macrophages derived from human monocytes."
    Hua Y., Xue J., Sun F., Zhu L., Xie M.
    Pharmacology 83:18-25(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  25. "A novel intracellular isoform of matrix metalloproteinase-2 induced by oxidative stress activates innate immunity."
    Lovett D.H., Mahimkar R., Raffai R.L., Cape L., Maklashina E., Cecchini G., Karliner J.S.
    PLoS ONE 7:E34177-E34177(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION.
  26. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 443-660.
  27. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 458-660.
  28. "Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed."
    Morgunova E., Tuuttila A., Bergmann U., Isupov M., Lindqvist Y., Schneider G., Tryggvason K.
    Science 284:1667-1670(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-660 OF MUTANT ALA-404.
  29. "The second type II module from human matrix metalloproteinase 2: structure, function and dynamics."
    Briknarova K., Grishaev A., Banyai L., Tordai H., Patthy L., Llinas M.
    Structure 7:1235-1245(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 278-336, DISULFIDE BONDS.
  30. "Gelatin-binding region of human matrix metalloproteinase-2: solution structure, dynamics, and function of the COL-23 two-domain construct."
    Briknarova K., Gehrmann M., Banyai L., Tordai H., Patthy L., Llinas M.
    J. Biol. Chem. 276:27613-27621(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 337-394 OF WILD TYPE AND IN COMPLEX WITH PPG PEPTIDES.
  31. "Solution structure and backbone dynamics of the catalytic domain of matrix metalloproteinase-2 complexed with a hydroxamic acid inhibitor."
    Feng Y., Likos J.J., Zhu L., Woodward H., Munie G., McDonald J.J., Stevens A.M., Howard C.P., De Crescenzo G.A., Welsch D., Shieh H.S., Stallings W.C.
    Biochim. Biophys. Acta 1598:10-23(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 110-446 IN COMPLEX WITH A HYDROXAMIC ACID INHIBITOR.
  32. "The col-1 module of human matrix metalloproteinase-2 (MMP-2): structural/functional relatedness between gelatin-binding fibronectin type II modules and lysine-binding kringle domains."
    Gehrmann M., Briknarova K., Banyai L., Patthy L., Llinas M.
    Biol. Chem. 383:137-148(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 223-282 OF WILD TYPE AND IN COMPLEX WITH A PPG PEPTIDE.
  33. "Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2."
    Morgunova E., Tuuttila A., Bergmann U., Tryggvason K.
    Proc. Natl. Acad. Sci. U.S.A. 99:7414-7419(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 30-660 IN COMPLEX WITH INHIBITOR TIMP2.
  34. "Matrix metalloproteinase target family landscape: a chemometrical approach to ligand selectivity based on protein binding site analysis."
    Pirard B., Matter H.
    J. Med. Chem. 49:51-69(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 115-449.
  35. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT MONA HIS-101, VARIANT TYR-210.
  36. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT MONA LYS-404.
  37. Cited for: VARIANT MONA VAL-400 DEL.
  38. Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-228; MET-498 AND ILE-644.

Entry informationi

Entry nameiMMP2_HUMAN
AccessioniPrimary (citable) accession number: P08253
Secondary accession number(s): B2R6U1
, B4DWH3, E9PE45, Q9UCJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1991
Last modified: September 3, 2014
This is version 185 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi