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Protein

Matrix metalloproteinase-20

Gene

MMP20

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

Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site.2 Publications

<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:

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 bindingi100Zinc 1; in inhibited formBy similarity1
Metal bindingi164Calcium 11
Metal bindingi165Calcium 1; via carbonyl oxygen1
Metal bindingi166Calcium 1; via carbonyl oxygen1
Metal bindingi176Zinc 21
Metal bindingi178Zinc 21
Metal bindingi183Calcium 21
Metal bindingi184Calcium 2; via carbonyl oxygen1
Metal bindingi186Calcium 2; via carbonyl oxygen1
Metal bindingi188Calcium 2; via carbonyl oxygen1
Metal bindingi191Zinc 21
Metal bindingi197Calcium 1; via carbonyl oxygen1
Metal bindingi198Calcium 1; via carbonyl oxygen1
Metal bindingi200Calcium 1; via carbonyl oxygen1
Metal bindingi202Calcium 11
Metal bindingi204Zinc 21
Metal bindingi206Calcium 21
Metal bindingi209Calcium 21
Metal bindingi226Zinc 1; catalytic1
<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 sitei227PROSITE-ProRule annotation1
Metal bindingi230Zinc 1; catalytic1
Metal bindingi236Zinc 1; catalytic1

<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: CACAO
  • serine-type endopeptidase activity Source: Reactome
  • zinc ion binding Source: ProtInc

GO - Biological processi

<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
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.24.B6 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-2022090 Assembly of collagen fibrils and other multimeric structures

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M10.019

<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:
Matrix metalloproteinase-20 (EC:3.4.24.-)
Short name:
MMP-20
Alternative name(s):
Enamel metalloproteinase
Enamelysin
<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:MMP20
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000137674.3

Human Gene Nomenclature Database

More...
HGNCi
HGNC:7167 MMP20

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
604629 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O60882

<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

Extracellular matrix, 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

Amelogenesis imperfecta, hypomaturation type, 2A2 (AI2A2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA defect of enamel formation. The disorder involves both primary and secondary dentitions. The teeth have a shiny agar jelly appearance and the enamel is softer than normal. Brown pigment is present in middle layers of enamel.
See also OMIM:612529

Keywords - Diseasei

Amelogenesis imperfecta

Organism-specific databases

DisGeNET

More...
DisGeNETi
9313

MalaCards human disease database

More...
MalaCardsi
MMP20
MIMi612529 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000137674

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

More...
Orphaneti
100033 Hypomaturation amelogenesis imperfecta

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA30878

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1938226

Drug and drug target database

More...
DrugBanki
DB00786 Marimastat
DB08271 N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
MMP20

<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 – 22Sequence analysisAdd BLAST22
<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_000002883323 – 107By similarityAdd BLAST85
<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_0000028834108 – 483Matrix metalloproteinase-20Add BLAST376

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 bondi296 ↔ 483Sequence analysis

<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

Autoactivates at least at the 107-Asn-|-Tyr-108 site.By similarity

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Zymogen

Proteomic databases

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

More...
PaxDbi
O60882

PeptideAtlas

More...
PeptideAtlasi
O60882

PRoteomics IDEntifications database

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PRIDEi
O60882

ProteomicsDB human proteome resource

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ProteomicsDBi
49648

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O60882

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

More...
PhosphoSitePlusi
O60882

<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

Expressed specifically in the enamel organ.

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expression initiates prior to the onset of dentin mineralization and continues throughout the secretory stage of amelogenesis.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000137674 Expressed in 34 organ(s), highest expression level in testis

CleanEx database of gene expression profiles

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CleanExi
HS_MMP20

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O60882 HS

<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

Protein-protein interaction databases

STRING: functional protein association networks

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STRINGi
9606.ENSP00000260228

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
O60882

<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

1483
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O60882

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

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SMRi
O60882

Database of comparative protein structure models

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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
O60882

<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 ‘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>Repeati293 – 343Hemopexin 1Add BLAST51
Repeati344 – 389Hemopexin 2Add BLAST46
Repeati391 – 439Hemopexin 3Add BLAST49
Repeati440 – 483Hemopexin 4Add BLAST44

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>Motifi98 – 105Cysteine 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
ENSGT00940000161277

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000217927

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG052484

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O60882

KEGG Orthology (KO)

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KOi
K07999

Identification of Orthologs from Complete Genome Data

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OMAi
GDTHFDN

Database of Orthologous Groups

More...
OrthoDBi
EOG091G03DP

Database for complete collections of gene phylogenies

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PhylomeDBi
O60882

TreeFam database of animal gene trees

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TreeFami
TF315428

Family and domain databases

Conserved Domains Database

More...
CDDi
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
2.110.10.10, 1 hit
3.40.390.10, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028716 MMP20
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

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PANTHERi
PTHR10201:SF125 PTHR10201:SF125, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00045 Hemopexin, 3 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

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SMARTi
View protein in SMART
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00546 CYSTEINE_SWITCH, 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>Sequencei

<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.

O60882-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKVLPASGLA VFLIMALKFS TAAPSLVAAS PRTWRNNYRL AQAYLDKYYT
60 70 80 90 100
NKEGHQIGEM VARGSNSMIR KIKELQAFFG LQVTGKLDQT TMNVIKKPRC
110 120 130 140 150
GVPDVANYRL FPGEPKWKKN TLTYRISKYT PSMSSVEVDK AVEMALQAWS
160 170 180 190 200
SAVPLSFVRI NSGEADIMIS FENGDHGDSY PFDGPRGTLA HAFAPGEGLG
210 220 230 240 250
GDTHFDNAEK WTMGTNGFNL FTVAAHEFGH ALGLAHSTDP SALMYPTYKY
260 270 280 290 300
KNPYGFHLPK DDVKGIQALY GPRKVFLGKP TLPHAPHHKP SIPDLCDSSS
310 320 330 340 350
SFDAVTMLGK ELLLFKDRIF WRRQVHLRTG IRPSTITSSF PQLMSNVDAA
360 370 380 390 400
YEVAERGTAY FFKGPHYWIT RGFQMQGPPR TIYDFGFPRH VQQIDAAVYL
410 420 430 440 450
REPQKTLFFV GDEYYSYDER KRKMEKDYPK NTEEEFSGVN GQIDAAVELN
460 470 480
GYIYFFSGPK TYKYDTEKED VVSVVKSSSW IGC
Length:483
Mass (Da):54,387
Last modified:February 8, 2011 - v3
<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:i561B0A03E0BB0399
GO

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 conflicti208A → P in CAA73317 (PubMed:9398237).Curated1

Natural variant

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_02051118K → T1 PublicationCorresponds to variant dbSNP:rs2245803EnsemblClinVar.1
Natural variantiVAR_020512139D → N1 PublicationCorresponds to variant dbSNP:rs17099014EnsemblClinVar.1
Natural variantiVAR_020513169I → L1 PublicationCorresponds to variant dbSNP:rs17099008EnsemblClinVar.1
Natural variantiVAR_020514275V → A1 PublicationCorresponds to variant dbSNP:rs1784423EnsemblClinVar.1
Natural variantiVAR_057802281T → N1 PublicationCorresponds to variant dbSNP:rs1784424EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Y12779 mRNA Translation: CAA73317.1
AY673603 Genomic DNA Translation: AAT70722.1
AP000851 Genomic DNA No translation available.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS8318.1

NCBI Reference Sequences

More...
RefSeqi
NP_004762.2, NM_004771.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.591946

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000260228; ENSP00000260228; ENSG00000137674

Database of genes from NCBI RefSeq genomes

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GeneIDi
9313

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:9313

UCSC genome browser

More...
UCSCi
uc001phc.3 human

Keywords - Coding sequence diversityi

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

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12779 mRNA Translation: CAA73317.1
AY673603 Genomic DNA Translation: AAT70722.1
AP000851 Genomic DNA No translation available.
CCDSiCCDS8318.1
RefSeqiNP_004762.2, NM_004771.3
UniGeneiHs.591946

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JSDNMR-A113-272[»]
ProteinModelPortaliO60882
SMRiO60882
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000260228

Chemistry databases

BindingDBiO60882
ChEMBLiCHEMBL1938226
DrugBankiDB00786 Marimastat
DB08271 N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID

Protein family/group databases

MEROPSiM10.019

PTM databases

iPTMnetiO60882
PhosphoSitePlusiO60882

Polymorphism and mutation databases

BioMutaiMMP20

Proteomic databases

PaxDbiO60882
PeptideAtlasiO60882
PRIDEiO60882
ProteomicsDBi49648

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
9313
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260228; ENSP00000260228; ENSG00000137674
GeneIDi9313
KEGGihsa:9313
UCSCiuc001phc.3 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
9313
DisGeNETi9313
EuPathDBiHostDB:ENSG00000137674.3

GeneCards: human genes, protein and diseases

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GeneCardsi
MMP20

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0036038
HGNCiHGNC:7167 MMP20
MalaCardsiMMP20
MIMi604629 gene
612529 phenotype
neXtProtiNX_O60882
OpenTargetsiENSG00000137674
Orphaneti100033 Hypomaturation amelogenesis imperfecta
PharmGKBiPA30878

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG1565 Eukaryota
ENOG410XQ5D LUCA
GeneTreeiENSGT00940000161277
HOGENOMiHOG000217927
HOVERGENiHBG052484
InParanoidiO60882
KOiK07999
OMAiGDTHFDN
OrthoDBiEOG091G03DP
PhylomeDBiO60882
TreeFamiTF315428

Enzyme and pathway databases

BRENDAi3.4.24.B6 2681
ReactomeiR-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-2022090 Assembly of collagen fibrils and other multimeric structures

Miscellaneous databases

EvolutionaryTraceiO60882

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
MMP20

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

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GenomeRNAii
9313

Protein Ontology

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PROi
PR:O60882

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000137674 Expressed in 34 organ(s), highest expression level in testis
CleanExiHS_MMP20
GenevisibleiO60882 HS

Family and domain databases

CDDicd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit
Gene3Di1.10.101.10, 1 hit
2.110.10.10, 1 hit
3.40.390.10, 2 hits
InterProiView protein in InterPro
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028716 MMP20
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:SF125 PTHR10201:SF125, 1 hit
PfamiView protein in Pfam
PF00045 Hemopexin, 3 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PIRSFiPIRSF001191 Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138 MATRIXIN
SMARTiView protein in SMART
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
PROSITEiView protein in PROSITE
PS00546 CYSTEINE_SWITCH, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiMMP20_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: O60882
Secondary accession number(s): Q6DKT9
<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: December 1, 2000
Last sequence update: February 8, 2011
Last modified: December 5, 2018
This is version 170 of the entry and version 3 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, 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 11
    Human chromosome 11: 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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