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UniProtKB - P08253 (MMP2_HUMAN)

Protein

72 kDa type IV collagenase

Gene

MMP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>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. EC:3.4.24.24

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 4 Ca2+ ions per subunit.
  • Zn2+Note: Binds 2 Zn2+ ions per subunit.

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi102Zinc 2; in inhibited formBy similarity1
Metal bindingi134Calcium 1By similarity1
Metal bindingi168Calcium 2By similarity1
Metal bindingi178Zinc 1By similarity1
Metal bindingi180Zinc 1By similarity1
Metal bindingi185Calcium 3By similarity1
Metal bindingi186Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi193Zinc 1By similarity1
Metal bindingi200Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi202Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi204Calcium 2By similarity1
Metal bindingi206Zinc 1By similarity1
Metal bindingi208Calcium 3By similarity1
Metal bindingi209Calcium 1By similarity1
Metal bindingi211Calcium 3By similarity1
Metal bindingi403Zinc 2; catalyticBy similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei404PROSITE-ProRule annotation1
Metal bindingi407Zinc 2; catalyticBy similarity1
Metal bindingi413Zinc 2; catalyticBy similarity1
Metal bindingi476Calcium 4; via carbonyl oxygen1
Metal bindingi521Calcium 4; via carbonyl oxygen1
Metal bindingi569Calcium 4; via carbonyl oxygen1
Metal bindingi618Calcium 4; via carbonyl oxygen1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • metalloendopeptidase activity Source: GO_Central
  • metallopeptidase activity Source: UniProtKB
  • serine-type endopeptidase activity Source: Reactome
  • zinc ion binding Source: ProtInc
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
Biological processAngiogenesis, Collagen degradation
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS01565-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.24.24 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling

SIGNOR Signaling Network Open Resource

More...SIGNORi		P08253

Protein family/group databases

MEROPS protease database

More...MEROPSi		M10.003

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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:
PEX
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MMP2
Synonyms:CLG4A
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 16

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000087245.12

Human Gene Nomenclature Database

More...HGNCi		HGNC:7166 MMP2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		120360 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P08253

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Multicentric osteolysis, nodulosis, and arthropathy (MONA)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:259600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_032423101R → H in MONA. 1 PublicationCorresponds to variant dbSNP:rs121912953EnsemblClinVar.1
Natural variantiVAR_054996400Missing in MONA. 1 Publication1
Natural variantiVAR_032425404E → K in MONA. 1 PublicationCorresponds to variant dbSNP:rs121912955EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		4313

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		MMP2

MalaCards human disease database

More...MalaCardsi		MMP2
MIMi259600 phenotype

Open Targets

More...OpenTargetsi		ENSG00000087245

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		85196 Nodulosis-arthropathy-osteolysis syndrome
3460 Torg-Winchester syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30877

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL333

Drug and drug target database

More...DrugBanki		DB05387 AE-941
DB01197 Captopril
DB04866 Halofuginone
DB00786 Marimastat
DB01630 SC-74020

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1629

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		MMP2

Domain mapping of disease mutations (DMDM)

More...DMDMi		116856

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 29By similarityAdd BLAST29
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002871430 – 109Activation peptideAdd BLAST80
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000028715110 – 66072 kDa type IV collagenaseAdd BLAST551
ChainiPRO_0000391626445 – 660PEXAdd BLAST216

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>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 ↔ 660PROSITE-ProRule annotation1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi573N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi642N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...EPDi		P08253

MaxQB - The MaxQuant DataBase

More...MaxQBi		P08253

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P08253

PeptideAtlas

More...PeptideAtlasi		P08253

PRoteomics IDEntifications database

More...PRIDEi		P08253

ProteomicsDB human proteome resource

More...ProteomicsDBi		52101

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P08253

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P08253

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P08253

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P08253

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Aspirin appears to inhibit expression.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000087245 Expressed in 208 organ(s), highest expression level in mucosa of stomach

CleanEx database of gene expression profiles

More...CleanExi		HS_MMP2

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P08253 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P08253 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB002788
HPA001939

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		110457, 38 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P08253

Protein interaction database and analysis system

More...IntActi		P08253, 21 interactors

Molecular INTeraction database

More...MINTi		P08253

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000219070

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P08253

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1660
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P08253

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P08253

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P08253

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini228 – 276Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST49
Domaini286 – 334Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST49
Domaini344 – 392Fibronectin type-II 3PROSITE-ProRule annotationAdd BLAST49
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati472 – 516Hemopexin 1Add BLAST45
Repeati517 – 563Hemopexin 2Add BLAST47
Repeati565 – 613Hemopexin 3Add BLAST49
Repeati614 – 660Hemopexin 4Add BLAST47

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni110 – 221Collagenase-like 1Add BLAST112
Regioni222 – 396Collagen-bindingAdd BLAST175
Regioni397 – 465Collagenase-like 2Add BLAST69
Regioni414 – 660Required for inhibitor TIMP2 bindingAdd BLAST247

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi100 – 107Cysteine switchBy similarity8

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase M10A family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1565 Eukaryota
ENOG410XQ5D LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000158511

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000217926

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG052484

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P08253

KEGG Orthology (KO)

More...KOi		K01398

Identification of Orthologs from Complete Genome Data

More...OMAi		HESCTSA

Database of Orthologous Groups

More...OrthoDBi		EOG091G03DP

Database for complete collections of gene phylogenies

More...PhylomeDBi		P08253

TreeFam database of animal gene trees

More...TreeFami		TF315428

Family and domain databases

Conserved Domains Database

More...CDDi		cd00062 FN2, 3 hits
cd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.101.10, 1 hit
2.10.10.10, 3 hits
2.110.10.10, 1 hit
3.40.390.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR028708 72kDa_collagenase
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR013806 Kringle-like
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
IPR036366 PGBDSf

The PANTHER Classification System

More...PANTHERi		PTHR10201:SF29 PTHR10201:SF29, 4 hits

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00040 fn2, 3 hits
PF00045 Hemopexin, 4 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001191 Peptidase_M10A_matrix, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00138 MATRIXIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00059 FN2, 3 hits
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
SSF57440 SSF57440, 3 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

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
        10         20         30         40         50
MEALMARGAL TGPLRALCLL GCLLSHAAAA PSPIIKFPGD VAPKTDKELA 
        60         70         80         90        100
VQYLNTFYGC PKESCNLFVL KDTLKKMQKF FGLPQTGDLD QNTIETMRKP 
       110        120        130        140        150
RCGNPDVANY NFFPRKPKWD KNQITYRIIG YTPDLDPETV DDAFARAFQV 
       160        170        180        190        200
WSDVTPLRFS RIHDGEADIM INFGRWEHGD GYPFDGKDGL LAHAFAPGTG 
       210        220        230        240        250
VGGDSHFDDD ELWTLGEGQV VRVKYGNADG EYCKFPFLFN GKEYNSCTDT 
       260        270        280        290        300
GRSDGFLWCS TTYNFEKDGK YGFCPHEALF TMGGNAEGQP CKFPFRFQGT 
       310        320        330        340        350
SYDSCTTEGR TDGYRWCGTT EDYDRDKKYG FCPETAMSTV GGNSEGAPCV 
       360        370        380        390        400
FPFTFLGNKY ESCTSAGRSD GKMWCATTAN YDDDRKWGFC PDQGYSLFLV 
       410        420        430        440        450
AAHEFGHAMG LEHSQDPGAL MAPIYTYTKN FRLSQDDIKG IQELYGASPD 
       460        470        480        490        500
IDLGTGPTPT LGPVTPEICK QDIVFDGIAQ IRGEIFFFKD RFIWRTVTPR 
       510        520        530        540        550
DKPMGPLLVA TFWPELPEKI DAVYEAPQEE KAVFFAGNEY WIYSASTLER 
       560        570        580        590        600
GYPKPLTSLG LPPDVQRVDA AFNWSKNKKT YIFAGDKFWR YNEVKKKMDP 
       610        620        630        640        650
GFPKLIADAW NAIPDNLDAV VDLQGGGHSY FFKGAYYLKL ENQSLKSVKF 
       660
GSIKSDWLGC
Length:660
Mass (Da):73,882
Last modified:February 1, 1991 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BR66H3BR66_HUMAN
72 kDa type IV collagenase
MMP2
201Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BV48H3BV48_HUMAN
72 kDa type IV collagenase
MMP2
118Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BS34H3BS34_HUMAN
72 kDa type IV collagenase
MMP2
251Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3KRB7J3KRB7_HUMAN
72 kDa type IV collagenase
MMP2
22Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti235F → S in AK310314 (PubMed:14702039).Curated1
Sequence conflicti546S → G in BAG35588 (PubMed:14702039).Curated1
Sequence conflicti618D → G in BAG35588 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_032423101R → H in MONA. 1 PublicationCorresponds to variant dbSNP:rs121912953EnsemblClinVar.1
Natural variantiVAR_032424210D → Y1 Publication1
Natural variantiVAR_036136228A → T in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs759302357Ensembl.1
Natural variantiVAR_054996400Missing in MONA. 1 Publication1
Natural variantiVAR_032425404E → K in MONA. 1 PublicationCorresponds to variant dbSNP:rs121912955EnsemblClinVar.1
Natural variantiVAR_020616447A → V1 PublicationCorresponds to variant dbSNP:rs17859943EnsemblClinVar.1
Natural variantiVAR_036137498T → M in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs764961297Ensembl.1
Natural variantiVAR_020617621V → L1 PublicationCorresponds to variant dbSNP:rs16955280Ensembl.1
Natural variantiVAR_036138644S → I in a colorectal cancer sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0446311 – 76Missing in isoform 2. 1 PublicationAdd BLAST76
Alternative sequenceiVSP_0457041 – 51MEALM…KELAV → M in isoform 3. 1 PublicationAdd BLAST51

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS10752.1 [P08253-1]
CCDS45487.1 [P08253-3]
CCDS76869.1 [P08253-2]

Protein sequence database of the Protein Information Resource

More...PIRi		A28153

NCBI Reference Sequences

More...RefSeqi		NP_001121363.1, NM_001127891.2 [P08253-3]
NP_001289437.1, NM_001302508.1 [P08253-2]
NP_001289438.1, NM_001302509.1 [P08253-2]
NP_001289439.1, NM_001302510.1 [P08253-2]
NP_004521.1, NM_004530.5 [P08253-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.513617

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000219070; ENSP00000219070; ENSG00000087245 [P08253-1]
ENST00000437642; ENSP00000394237; ENSG00000087245 [P08253-3]
ENST00000543485; ENSP00000444143; ENSG00000087245 [P08253-2]
ENST00000570308; ENSP00000461421; ENSG00000087245 [P08253-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		4313

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:4313

UCSC genome browser

More...UCSCi		uc002ehz.5 human [P08253-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS76869.1 [P08253-2]
PIRiA28153
RefSeqiNP_001121363.1, NM_001127891.2 [P08253-3]
NP_001289437.1, NM_001302508.1 [P08253-2]
NP_001289438.1, NM_001302509.1 [P08253-2]
NP_001289439.1, NM_001302510.1 [P08253-2]
NP_004521.1, NM_004530.5 [P08253-1]
UniGeneiHs.513617

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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-A110-214[»]
1J7MNMR-A337-394[»]
1KS0NMR-A223-282[»]
1QIBX-ray2.80A115-213[»]
A394-449[»]
1RTGX-ray2.60A451-660[»]
3AYUX-ray2.00A110-450[»]
ProteinModelPortaliP08253
SMRiP08253
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110457, 38 interactors
CORUMiP08253
IntActiP08253, 21 interactors
MINTiP08253
STRINGi9606.ENSP00000219070

Chemistry databases

BindingDBiP08253
ChEMBLiCHEMBL333
DrugBankiDB05387 AE-941
DB01197 Captopril
DB04866 Halofuginone
DB00786 Marimastat
DB01630 SC-74020
GuidetoPHARMACOLOGYi1629

Protein family/group databases

MEROPSiM10.003

PTM databases

CarbonylDBiP08253
iPTMnetiP08253
PhosphoSitePlusiP08253

Polymorphism and mutation databases

BioMutaiMMP2
DMDMi116856

Proteomic databases

EPDiP08253
MaxQBiP08253
PaxDbiP08253
PeptideAtlasiP08253
PRIDEiP08253
ProteomicsDBi52101

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		4313
Structural Biology KnowledgebaseSearch...

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.5 human [P08253-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4313
DisGeNETi4313
EuPathDBiHostDB:ENSG00000087245.12

GeneCards: human genes, protein and diseases

More...GeneCardsi		MMP2
GeneReviewsiMMP2
HGNCiHGNC:7166 MMP2
HPAiCAB002788
HPA001939
MalaCardsiMMP2
MIMi120360 gene
259600 phenotype
neXtProtiNX_P08253
OpenTargetsiENSG00000087245
Orphaneti85196 Nodulosis-arthropathy-osteolysis syndrome
3460 Torg-Winchester syndrome
PharmGKBiPA30877

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1565 Eukaryota
ENOG410XQ5D LUCA
GeneTreeiENSGT00940000158511
HOGENOMiHOG000217926
HOVERGENiHBG052484
InParanoidiP08253
KOiK01398
OMAiHESCTSA
OrthoDBiEOG091G03DP
PhylomeDBiP08253
TreeFamiTF315428

Enzyme and pathway databases

BioCyciMetaCyc:HS01565-MONOMER
BRENDAi3.4.24.24 2681
ReactomeiR-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
SIGNORiP08253

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		MMP2 human
EvolutionaryTraceiP08253

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		MMP2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		4313
PMAP-CutDBiP08253

Protein Ontology

More...PROi		PR:P08253

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000087245 Expressed in 208 organ(s), highest expression level in mucosa of stomach
CleanExiHS_MMP2
ExpressionAtlasiP08253 baseline and differential
GenevisibleiP08253 HS

Family and domain databases

CDDicd00062 FN2, 3 hits
cd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit
Gene3Di1.10.101.10, 1 hit
2.10.10.10, 3 hits
2.110.10.10, 1 hit
3.40.390.10, 1 hit
InterProiView protein in InterPro
IPR028708 72kDa_collagenase
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR013806 Kringle-like
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
IPR036366 PGBDSf
PANTHERiPTHR10201:SF29 PTHR10201:SF29, 4 hits
PfamiView protein in Pfam
PF00040 fn2, 3 hits
PF00045 Hemopexin, 4 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PIRSFiPIRSF001191 Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138 MATRIXIN
SMARTiView protein in SMART
SM00059 FN2, 3 hits
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
SSF57440 SSF57440, 3 hits
PROSITEiView protein in PROSITE
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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMMP2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P08253
Secondary accession number(s): B2R6U1
, B4DWH3, E9PE45, Q9UCJ8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1991
Last modified: December 5, 2018
This is version 227 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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