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Protein

Neutrophil collagenase

Gene

MMP8

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

Can degrade fibrillar type I, II, and III collagens.

<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 interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I. EC:3.4.24.34

<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 3 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

Cannot be activated without removal of the activation peptide.

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 bindingi91Zinc 2; in inhibited form1
Metal bindingi157Calcium 11
Metal bindingi167Zinc 11 Publication1
Metal bindingi169Zinc 11 Publication1
Metal bindingi174Calcium 21 Publication1
Metal bindingi175Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi177Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi179Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi182Zinc 11 Publication1
Metal bindingi189Calcium 1; via carbonyl oxygen1
Metal bindingi191Calcium 1; via carbonyl oxygen1
Metal bindingi193Calcium 11
Metal bindingi195Zinc 11 Publication1
Metal bindingi197Calcium 21 Publication1
Metal bindingi200Calcium 21 Publication1
Metal bindingi217Zinc 2; catalytic1 Publication1
<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 sitei2181
Metal bindingi221Zinc 2; catalytic1 Publication1
Metal bindingi227Zinc 2; catalytic1 Publication1
Metal bindingi286Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi378Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi425Calcium 3; via carbonyl oxygenBy similarity1

<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

  • endopeptidase activity Source: ARUK-UCL
  • metalloendopeptidase activity Source: Reactome
  • serine-type endopeptidase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

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
Biological processCollagen degradation
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.24.34 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-6798695 Neutrophil degranulation

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M10.002

<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:
Neutrophil collagenase (EC:3.4.24.34)
Alternative name(s):
Matrix metalloproteinase-8
Short name:
MMP-8
PMNL collagenase
Short name:
PMNL-CL
<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:MMP8
Synonyms:CLG1
<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:ENSG00000118113.11

Human Gene Nomenclature Database

More...
HGNCi
HGNC:7175 MMP8

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
120355 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P22894

<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

Organism-specific databases

DisGeNET

More...
DisGeNETi
4317

MalaCards human disease database

More...
MalaCardsi
MMP8

Open Targets

More...
OpenTargetsi
ENSG00000118113

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA30888

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4588

Drug and drug target database

More...
DrugBanki
DB02326 1-Hydroxyamine-2-Isobutylmalonic Acid
DB02953 2-Thiomethyl-3-Phenylpropanoic Acid
DB08476 3-AMINO-AZACYCLOTRIDECAN-2-ONE
DB07900 3-FORMYL-2-HYDROXY-5-METHYL-HEXANOIC ACID HYDROXYAMIDE
DB03880 Batimastat
DB03636 Glycinamid
DB00786 Marimastat
DB08403 METHYLAMINO-PHENYLALANYL-LEUCYL-HYDROXAMIC ACID

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1632

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
MMP8

Domain mapping of disease mutations (DMDM)

More...
DMDMi
116862

<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 – 202 PublicationsAdd BLAST20
<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_000002874421 – 100Activation 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_0000028745101 – 467Neutrophil collagenaseAdd BLAST367

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi54N-linked (GlcNAc...) asparagineCurated1
Glycosylationi73N-linked (GlcNAc...) asparagineCurated1
Glycosylationi112N-linked (GlcNAc...) asparagine1
Glycosylationi204N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi246N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi279 ↔ 464Curated

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

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

More...
PaxDbi
P22894

PeptideAtlas

More...
PeptideAtlasi
P22894

PRoteomics IDEntifications database

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PRIDEi
P22894

ProteomicsDB human proteome resource

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ProteomicsDBi
54047

Consortium for Top Down Proteomics

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TopDownProteomicsi
P22894

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P22894

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

More...
PhosphoSitePlusi
P22894

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P22894

<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

Neutrophils.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000118113 Expressed in 79 organ(s), highest expression level in bone marrow

CleanEx database of gene expression profiles

More...
CleanExi
HS_MMP8

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P22894 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P22894 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA021221
HPA022935

<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
110460, 2 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000236826

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P22894

<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

1467
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
P22894

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

More...
SMRi
P22894

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
P22894

<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>Repeati276 – 325Hemopexin 1Add BLAST50
Repeati326 – 372Hemopexin 2Add BLAST47
Repeati374 – 420Hemopexin 3Add BLAST47
Repeati421 – 464Hemopexin 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>Motifi89 – 96Cysteine 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
ENSGT00940000161871

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

More...
InParanoidi
P22894

KEGG Orthology (KO)

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KOi
K01402

Identification of Orthologs from Complete Genome Data

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OMAi
EETWTKT

Database of Orthologous Groups

More...
OrthoDBi
EOG091G03DP

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P22894

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
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

More...
InterProi
View protein in InterPro
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028709 MMP8
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:SF137 PTHR10201:SF137, 1 hit

Pfam protein domain database

More...
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

More...
SMARTi
View protein in SMART
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

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00546 CYSTEINE_SWITCH, 1 hit
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>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 4 potential isoforms that are computationally mapped.Show allAlign All

P22894-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFSLKTLPFL LLLHVQISKA FPVSSKEKNT KTVQDYLEKF YQLPSNQYQS
60 70 80 90 100
TRKNGTNVIV EKLKEMQRFF GLNVTGKPNE ETLDMMKKPR CGVPDSGGFM
110 120 130 140 150
LTPGNPKWER TNLTYRIRNY TPQLSEAEVE RAIKDAFELW SVASPLIFTR
160 170 180 190 200
ISQGEADINI AFYQRDHGDN SPFDGPNGIL AHAFQPGQGI GGDAHFDAEE
210 220 230 240 250
TWTNTSANYN LFLVAAHEFG HSLGLAHSSD PGALMYPNYA FRETSNYSLP
260 270 280 290 300
QDDIDGIQAI YGLSSNPIQP TGPSTPKPCD PSLTFDAITT LRGEILFFKD
310 320 330 340 350
RYFWRRHPQL QRVEMNFISL FWPSLPTGIQ AAYEDFDRDL IFLFKGNQYW
360 370 380 390 400
ALSGYDILQG YPKDISNYGF PSSVQAIDAA VFYRSKTYFF VNDQFWRYDN
410 420 430 440 450
QRQFMEPGYP KSISGAFPGI ESKVDAVFQQ EHFFHVFSGP RYYAFDLIAQ
460
RVTRVARGNK WLNCRYG
Length:467
Mass (Da):53,412
Last modified:August 1, 1991 - 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:i4D4602A53AD7F8BC
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
H7C1M3H7C1M3_HUMAN
Matrix metalloproteinase
MMP8
344Annotation 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>
E9PJB3E9PJB3_HUMAN
Matrix metalloproteinase
MMP8
56Annotation 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>
E9PIY7E9PIY7_HUMAN
Matrix metalloproteinase
MMP8
43Annotation 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>
E9PL87E9PL87_HUMAN
Matrix metalloproteinase
MMP8
36Annotation 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 conflicti40F → I AA sequence (PubMed:2159879).Curated1
Sequence conflicti48Y → V AA sequence (PubMed:2159879).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_0250363S → C1 PublicationCorresponds to variant dbSNP:rs17099450Ensembl.1
Natural variantiVAR_02503732T → I2 PublicationsCorresponds to variant dbSNP:rs3765620EnsemblClinVar.1
Natural variantiVAR_00673087K → E1 PublicationCorresponds to variant dbSNP:rs1940475EnsemblClinVar.1
Natural variantiVAR_025038154G → E1 PublicationCorresponds to variant dbSNP:rs35056226Ensembl.1
Natural variantiVAR_025039193D → V1 PublicationCorresponds to variant dbSNP:rs34428739Ensembl.1
Natural variantiVAR_025040246N → Y1 PublicationCorresponds to variant dbSNP:rs35243553Ensembl.1
Natural variantiVAR_025041436V → A1 PublicationCorresponds to variant dbSNP:rs34009635Ensembl.1
Natural variantiVAR_025042460K → T1 PublicationCorresponds to variant dbSNP:rs35866072Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
J05556 mRNA Translation: AAA88021.1
DQ141306 Genomic DNA Translation: AAZ38714.1
BC074988 mRNA Translation: AAH74988.1
BC074989 mRNA Translation: AAH74989.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS8320.1

Protein sequence database of the Protein Information Resource

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PIRi
A37073 KCHUN

NCBI Reference Sequences

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RefSeqi
NP_001291370.1, NM_001304441.1
NP_001291371.1, NM_001304442.1
NP_002415.1, NM_002424.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.161839

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000236826; ENSP00000236826; ENSG00000118113

Database of genes from NCBI RefSeq genomes

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GeneIDi
4317

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:4317

UCSC genome browser

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UCSCi
uc001phe.2 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
J05556 mRNA Translation: AAA88021.1
DQ141306 Genomic DNA Translation: AAZ38714.1
BC074988 mRNA Translation: AAH74988.1
BC074989 mRNA Translation: AAH74989.1
CCDSiCCDS8320.1
PIRiA37073 KCHUN
RefSeqiNP_001291370.1, NM_001304441.1
NP_001291371.1, NM_001304442.1
NP_002415.1, NM_002424.2
UniGeneiHs.161839

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
1A85X-ray2.00A105-262[»]
1A86X-ray2.00A105-262[»]
1BZSX-ray1.70A99-262[»]
1I73X-ray1.40A100-262[»]
1I76X-ray1.20A100-262[»]
1JANX-ray2.50A99-262[»]
1JAOX-ray2.40A100-262[»]
1JAPX-ray1.82A100-262[»]
1JAQX-ray2.40A100-262[»]
1JH1X-ray2.70A105-262[»]
1JJ9X-ray2.00A100-262[»]
1KBCX-ray1.80A/B99-262[»]
1MMBX-ray2.10A100-262[»]
1MNCX-ray2.10A101-263[»]
1ZP5X-ray1.80A100-262[»]
1ZS0X-ray1.56A100-262[»]
1ZVXX-ray1.87A100-262[»]
2OY2X-ray1.50A/F105-262[»]
2OY4X-ray1.70A/F105-262[»]
3DNGX-ray2.00A/B100-262[»]
3DPEX-ray1.60A100-262[»]
3DPFX-ray2.10A/B100-262[»]
3TT4X-ray1.88A104-262[»]
4QKZX-ray1.20A100-262[»]
5H8XX-ray1.30A100-262[»]
ProteinModelPortaliP22894
SMRiP22894
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110460, 2 interactors
STRINGi9606.ENSP00000236826

Chemistry databases

BindingDBiP22894
ChEMBLiCHEMBL4588
DrugBankiDB02326 1-Hydroxyamine-2-Isobutylmalonic Acid
DB02953 2-Thiomethyl-3-Phenylpropanoic Acid
DB08476 3-AMINO-AZACYCLOTRIDECAN-2-ONE
DB07900 3-FORMYL-2-HYDROXY-5-METHYL-HEXANOIC ACID HYDROXYAMIDE
DB03880 Batimastat
DB03636 Glycinamid
DB00786 Marimastat
DB08403 METHYLAMINO-PHENYLALANYL-LEUCYL-HYDROXAMIC ACID
GuidetoPHARMACOLOGYi1632

Protein family/group databases

MEROPSiM10.002

PTM databases

iPTMnetiP22894
PhosphoSitePlusiP22894

Polymorphism and mutation databases

BioMutaiMMP8
DMDMi116862

Proteomic databases

PaxDbiP22894
PeptideAtlasiP22894
PRIDEiP22894
ProteomicsDBi54047
TopDownProteomicsiP22894

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000236826; ENSP00000236826; ENSG00000118113
GeneIDi4317
KEGGihsa:4317
UCSCiuc001phe.2 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
4317
DisGeNETi4317
EuPathDBiHostDB:ENSG00000118113.11

GeneCards: human genes, protein and diseases

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GeneCardsi
MMP8
HGNCiHGNC:7175 MMP8
HPAiHPA021221
HPA022935
MalaCardsiMMP8
MIMi120355 gene
neXtProtiNX_P22894
OpenTargetsiENSG00000118113
PharmGKBiPA30888

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1565 Eukaryota
ENOG410XQ5D LUCA
GeneTreeiENSGT00940000161871
HOGENOMiHOG000217927
HOVERGENiHBG052484
InParanoidiP22894
KOiK01402
OMAiEETWTKT
OrthoDBiEOG091G03DP
PhylomeDBiP22894
TreeFamiTF315428

Enzyme and pathway databases

BRENDAi3.4.24.34 2681
ReactomeiR-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-6798695 Neutrophil degranulation

Miscellaneous databases

EvolutionaryTraceiP22894

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
MMP8

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

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GenomeRNAii
4317
PMAP-CutDBiP22894

Protein Ontology

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PROi
PR:P22894

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000118113 Expressed in 79 organ(s), highest expression level in bone marrow
CleanExiHS_MMP8
ExpressionAtlasiP22894 baseline and differential
GenevisibleiP22894 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
IPR018486 Hemopexin_CS
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028709 MMP8
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:SF137 PTHR10201:SF137, 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
PS00024 HEMOPEXIN, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiMMP8_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: P22894
Secondary accession number(s): Q45F99
<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, 1991
Last sequence update: August 1, 1991
Last modified: December 5, 2018
This is version 191 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

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 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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