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P08253

- MMP2_HUMAN

UniProt

P08253 - MMP2_HUMAN

Protein

72 kDa type IV collagenase

Gene

MMP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 186 (01 Oct 2014)
      Sequence version 2 (01 Feb 1991)
      Previous versions | rss
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    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.
    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.
    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.

    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 formBy similarity
    Metal bindingi134 – 1341Calcium 1By similarity
    Metal bindingi168 – 1681Calcium 2By similarity
    Metal bindingi178 – 1781Zinc 1By similarity
    Metal bindingi180 – 1801Zinc 1By similarity
    Metal bindingi185 – 1851Calcium 3By similarity
    Metal bindingi186 – 1861Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi193 – 1931Zinc 1By similarity
    Metal bindingi200 – 2001Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi202 – 2021Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi204 – 2041Calcium 2By similarity
    Metal bindingi206 – 2061Zinc 1By similarity
    Metal bindingi208 – 2081Calcium 3By similarity
    Metal bindingi209 – 2091Calcium 1By similarity
    Metal bindingi211 – 2111Calcium 3By similarity
    Metal bindingi403 – 4031Zinc 2; catalyticBy similarity
    Active sitei404 – 4041PROSITE-ProRule annotation
    Metal bindingi407 – 4071Zinc 2; catalyticBy similarity
    Metal bindingi413 – 4131Zinc 2; catalyticBy 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

    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

    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.

    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

    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 – 2929Sequence AnalysisAdd
    BLAST
    Propeptidei30 – 10980Activation peptidePRO_0000028714Add
    BLAST
    Chaini110 – 66055172 kDa type IV collagenasePRO_0000028715Add
    BLAST
    Chaini445 – 660216PEXPRO_0000391626Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi233 ↔ 259PROSITE-ProRule annotation
    Disulfide bondi247 ↔ 274PROSITE-ProRule annotation
    Disulfide bondi291 ↔ 317PROSITE-ProRule annotation
    Disulfide bondi305 ↔ 332PROSITE-ProRule annotation
    Disulfide bondi349 ↔ 375PROSITE-ProRule annotation
    Disulfide bondi363 ↔ 390PROSITE-ProRule annotation
    Disulfide bondi469 ↔ 6601 PublicationPROSITE-ProRule annotation
    Glycosylationi573 – 5731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi642 – 6421N-linked (GlcNAc...)Sequence Analysis

    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/beta3.2 Publications

    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.1 Publication

    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.8 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi110457. 18 interactions.
    DIPiDIP-26N.
    IntActiP08253. 12 interactions.
    STRINGi9606.ENSP00000219070.

    Structurei

    Secondary structure

    1
    660
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08253.

    Family & Domainsi

    Domains and Repeats

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

    Region

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

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi100 – 1078Cysteine switchBy 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.Curated
    Contains 3 fibronectin type-II domains.PROSITE-ProRule annotation
    Contains 4 hemopexin repeats.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti235 – 2351F → S in AK310314. (PubMed:14702039)Curated
    Sequence conflicti546 – 5461S → G in BAG35588. (PubMed:14702039)Curated
    Sequence conflicti618 – 6181D → G in BAG35588. (PubMed:14702039)Curated

    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. 1 PublicationVSP_044631Add
    BLAST
    Alternative sequencei1 – 5151MEALM…KELAV → M in isoform 3. 1 PublicationVSP_045704Add
    BLAST

    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...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110457. 18 interactions.
    DIPi DIP-26N.
    IntActi P08253. 12 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

    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: October 1, 2014
    This is version 186 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