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UniProtKB - Q9NPA2 (MMP25_HUMAN)

Entry version 177 (13 Feb 2019)
Sequence version 1 (01 Oct 2000)
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Protein

Matrix metalloproteinase-25

Gene

MMP25

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

May activate progelatinase A.

<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 bindingi90Zinc; in inhibited formBy similarity1
Metal bindingi233Zinc; catalyticPROSITE-ProRule annotation1
<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 sitei234PROSITE-ProRule annotation1
Metal bindingi237Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi243Zinc; catalyticPROSITE-ProRule annotation1

<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
  • zinc ion binding Source: InterPro
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
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-6798695 Neutrophil degranulation

Protein family/group databases

MEROPS protease database

More...MEROPSi		M10.024

<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-25 (EC:3.4.24.-)
Short name:
MMP-25
Alternative name(s):
Leukolysin
Membrane-type matrix metalloproteinase 6
Short name:
MT-MMP 6
Short name:
MTMMP6
Membrane-type-6 matrix metalloproteinase
Short name:
MT6-MMP
Short name:
MT6MMP
<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:MMP25
Synonyms:MMP20, MMPL1, MT6MMP
<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:ENSG00000008516.16

Human Gene Nomenclature Database

More...HGNCi		HGNC:14246 MMP25

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		608482 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9NPA2

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, 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

Organism-specific databases

DisGeNET

More...DisGeNETi		64386

Open Targets

More...OpenTargetsi		ENSG00000008516

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30882

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1795103

Drug and drug target database

More...DrugBanki		DB00786 Marimastat

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1647

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		MMP25

Domain mapping of disease mutations (DMDM)

More...DMDMi		12585274

<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 – 21Sequence analysisAdd BLAST21
<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_000002885222 – 107By similarityAdd BLAST86
<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_0000028853108 – 539Matrix metalloproteinase-25Add BLAST432
PropeptideiPRO_0000028854540 – 562Removed in mature formSequence analysisAdd BLAST23

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 bondi317 ↔ 508By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi539GPI-anchor amidated alanineSequence 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

The precursor is cleaved by a furin endopeptidase.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9NPA2

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

More...PaxDbi		Q9NPA2

PeptideAtlas

More...PeptideAtlasi		Q9NPA2

PRoteomics IDEntifications database

More...PRIDEi		Q9NPA2

ProteomicsDB human proteome resource

More...ProteomicsDBi		81949

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9NPA2

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

More...PhosphoSitePlusi		Q9NPA2

<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 predominantly in leukocytes, lung and spleen. Expressed also in colon carcinoma, astrocytoma and glioblastomas.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000008516 Expressed in 208 organ(s), highest expression level in blood

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9NPA2 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9NPA2 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB025177

<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

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		122149, 1 interactor

Protein interaction database and analysis system

More...IntActi		Q9NPA2, 1 interactor

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000337816

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9NPA2

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q9NPA2

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

More...SMRi		Q9NPA2

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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>Repeati314 – 363Hemopexin 1Add BLAST50
Repeati367 – 412Hemopexin 2Add BLAST46
Repeati413 – 461Hemopexin 3Add BLAST49
Repeati462 – 508Hemopexin 4Add BLAST47

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>Motifi88 – 95Cysteine switchBy similarity8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi103 – 107Poly-Arg5
Compositional biasi549 – 555Poly-Leu7

<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		ENSGT00940000159799

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000217928

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG052484

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9NPA2

KEGG Orthology (KO)

More...KOi		K08003

Identification of Orthologs from Complete Genome Data

More...OMAi		TGDTYFF

Database of Orthologous Groups

More...OrthoDBi		1517160at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9NPA2

TreeFam database of animal gene trees

More...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		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
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028733 MMP25
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like

The PANTHER Classification System

More...PANTHERi		PTHR10201:SF142 PTHR10201:SF142, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
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
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50923 SSF50923, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
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>Sequence (1+)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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q9NPA2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRLRLRLLAL LLLLLAPPAR APKPSAQDVS LGVDWLTRYG YLPPPHPAQA 
        60         70         80         90        100
QLQSPEKLRD AIKVMQRFAG LPETGRMDPG TVATMRKPRC SLPDVLGVAG 
       110        120        130        140        150
LVRRRRRYAL SGSVWKKRTL TWRVRSFPQS SQLSQETVRV LMSYALMAWG 
       160        170        180        190        200
MESGLTFHEV DSPQGQEPDI LIDFARAFHQ DSYPFDGLGG TLAHAFFPGE 
       210        220        230        240        250
HPISGDTHFD DEETWTFGSK DGEGTDLFAV AVHEFGHALG LGHSSAPNSI 
       260        270        280        290        300
MRPFYQGPVG DPDKYRLSQD DRDGLQQLYG KAPQTPYDKP TRKPLAPPPQ 
       310        320        330        340        350
PPASPTHSPS FPIPDRCEGN FDAIANIRGE TFFFKGPWFW RLQPSGQLVS 
       360        370        380        390        400
PRPARLHRFW EGLPAQVRVV QAAYARHRDG RILLFSGPQF WVFQDRQLEG 
       410        420        430        440        450
GARPLTELGL PPGEEVDAVF SWPQNGKTYL VRGRQYWRYD EAAARPDPGY 
       460        470        480        490        500
PRDLSLWEGA PPSPDDVTVS NAGDTYFFKG AHYWRFPKNS IKTEPDAPQP 
       510        520        530        540        550
MGPNWLDCPA PSSGPRAPRP PKATPVSETC DCQCELNQAA GRWPAPIPLL 
       560 
LLPLLVGGVA SR
Length:562
Mass (Da):62,554
Last modified:October 1, 2000 - v1
<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:iA6A50AE05D969C64
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
O43923O43923_HUMAN
Matrix metalloproteinase-25
MMP25 MMP20, mmp20
183Annotation score:

Annotation score:2 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 conflicti47P → R in BAB20584 (PubMed:11034316).Curated1

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
AJ239053 mRNA Translation: CAB94713.1
AF145442 mRNA Translation: AAF66697.2
AF185270 mRNA Translation: AAG17007.1
AB042328 mRNA Translation: BAB20584.1
AJ272137 mRNA Translation: CAC03490.1
CH471112 Genomic DNA Translation: EAW85413.1
CH471112 Genomic DNA Translation: EAW85415.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS10492.1

NCBI Reference Sequences

More...RefSeqi		NP_071913.1, NM_022468.4

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.654979

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000336577; ENSP00000337816; ENSG00000008516

Database of genes from NCBI RefSeq genomes

More...GeneIDi		64386

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:64386

UCSC genome browser

More...UCSCi		uc002cth.4 human

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ239053 mRNA Translation: CAB94713.1
AF145442 mRNA Translation: AAF66697.2
AF185270 mRNA Translation: AAG17007.1
AB042328 mRNA Translation: BAB20584.1
AJ272137 mRNA Translation: CAC03490.1
CH471112 Genomic DNA Translation: EAW85413.1
CH471112 Genomic DNA Translation: EAW85415.1
CCDSiCCDS10492.1
RefSeqiNP_071913.1, NM_022468.4
UniGeneiHs.654979

3D structure databases

ProteinModelPortaliQ9NPA2
SMRiQ9NPA2
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122149, 1 interactor
IntActiQ9NPA2, 1 interactor
STRINGi9606.ENSP00000337816

Chemistry databases

BindingDBiQ9NPA2
ChEMBLiCHEMBL1795103
DrugBankiDB00786 Marimastat
GuidetoPHARMACOLOGYi1647

Protein family/group databases

MEROPSiM10.024

PTM databases

iPTMnetiQ9NPA2
PhosphoSitePlusiQ9NPA2

Polymorphism and mutation databases

BioMutaiMMP25
DMDMi12585274

Proteomic databases

EPDiQ9NPA2
PaxDbiQ9NPA2
PeptideAtlasiQ9NPA2
PRIDEiQ9NPA2
ProteomicsDBi81949

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		64386
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336577; ENSP00000337816; ENSG00000008516
GeneIDi64386
KEGGihsa:64386
UCSCiuc002cth.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		64386
DisGeNETi64386
EuPathDBiHostDB:ENSG00000008516.16

GeneCards: human genes, protein and diseases

More...GeneCardsi		MMP25
HGNCiHGNC:14246 MMP25
HPAiCAB025177
MIMi608482 gene
neXtProtiNX_Q9NPA2
OpenTargetsiENSG00000008516
PharmGKBiPA30882

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1565 Eukaryota
ENOG410XQ5D LUCA
GeneTreeiENSGT00940000159799
HOGENOMiHOG000217928
HOVERGENiHBG052484
InParanoidiQ9NPA2
KOiK08003
OMAiTGDTYFF
OrthoDBi1517160at2759
PhylomeDBiQ9NPA2
TreeFamiTF315428

Enzyme and pathway databases

ReactomeiR-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-6798695 Neutrophil degranulation

Miscellaneous databases

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

More...ChiTaRSi		MMP25 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		MMP25

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

More...GenomeRNAii		64386

Protein Ontology

More...PROi		PR:Q9NPA2

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000008516 Expressed in 208 organ(s), highest expression level in blood
ExpressionAtlasiQ9NPA2 baseline and differential
GenevisibleiQ9NPA2 HS

Family and domain databases

CDDicd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit
Gene3Di2.110.10.10, 1 hit
3.40.390.10, 1 hit
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
IPR028733 MMP25
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
PANTHERiPTHR10201:SF142 PTHR10201:SF142, 1 hit
PfamiView protein in Pfam
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
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF50923 SSF50923, 1 hit
PROSITEiView protein in PROSITE
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 nameiMMP25_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: Q9NPA2
Secondary accession number(s): D3DUA8, Q9H3Q0
<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: January 24, 2001
Last sequence update: October 1, 2000
Last modified: February 13, 2019
This is version 177 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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