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Protein

Matrix metalloproteinase-9

Gene

MMP9

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 play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.1 Publication

Miscellaneous

In the arthritis patient this enzyme might contribute to the pathogenesis of joint destruction and might constitute a useful marker of disease status.

<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

<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:

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

Inhibited by histatin-3 1/24 (histatin-5). Inhibited by ECM1.2 Publications

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 bindingi99Zinc 2; in inhibited form2 Publications1
Metal bindingi131Calcium 11
Metal bindingi165Calcium 2; via carbonyl oxygen1
Metal bindingi175Zinc 1; structural2 Publications1
Metal bindingi177Zinc 1; structural2 Publications1
Metal bindingi182Calcium 31
Metal bindingi183Calcium 3; via carbonyl oxygen1
Metal bindingi185Calcium 3; via carbonyl oxygen1
Metal bindingi187Calcium 3; via carbonyl oxygen1
Metal bindingi190Zinc 1; structural2 Publications1
Metal bindingi197Calcium 2; via carbonyl oxygen1
Metal bindingi199Calcium 2; via carbonyl oxygen1
Metal bindingi201Calcium 21
Metal bindingi203Zinc 1; structural2 Publications1
Metal bindingi205Calcium 31
Metal bindingi206Calcium 11
Metal bindingi208Calcium 11
Metal bindingi208Calcium 31
Metal bindingi401Zinc 2; catalytic2 Publications1
<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 sitei4021
Metal bindingi405Zinc 2; catalytic2 Publications1
Metal bindingi411Zinc 2; catalytic2 Publications1

<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

  • collagen binding Source: UniProtKB
  • endopeptidase activity Source: ParkinsonsUK-UCL
  • identical protein binding Source: IntAct
  • metalloendopeptidase activity Source: UniProtKB
  • metallopeptidase activity Source: UniProtKB
  • serine-type endopeptidase activity Source: Reactome
  • 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
3.4.24.35 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1433557 Signaling by SCF-KIT
R-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-2022090 Assembly of collagen fibrils and other multimeric structures
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-6798695 Neutrophil degranulation

SIGNOR Signaling Network Open Resource

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SIGNORi
P14780

Protein family/group databases

MEROPS protease database

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MEROPSi
M10.004

<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-9 (EC:3.4.24.35)
Short name:
MMP-9
Alternative name(s):
92 kDa gelatinase
92 kDa type IV collagenase1 Publication
Gelatinase B
Short name:
GELB
Cleaved into the following 2 chains:
<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:MMP9
Synonyms:CLG4B
<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 20

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000100985.7

Human Gene Nomenclature Database

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HGNCi
HGNC:7176 MMP9

Online Mendelian Inheritance in Man (OMIM)

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MIMi
120361 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P14780

<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

Intervertebral disc disease (IDD)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain.
See also OMIM:603932
Metaphyseal anadysplasia 2 (MANDP2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA bone development disorder characterized by skeletal anomalies that resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia.
See also OMIM:613073

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi402E → Q: Loss of activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
4318

MalaCards human disease database

More...
MalaCardsi
MMP9
MIMi603932 phenotype
613073 phenotype

Open Targets

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OpenTargetsi
ENSG00000100985

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

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Orphaneti
1040 Metaphyseal anadysplasia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30889

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL321

Drug and drug target database

More...
DrugBanki
DB03683 2-{[Formyl(Hydroxy)Amino]Methyl}-4-Methylpentanoic Acid
DB05387 AE-941
DB01197 Captopril
DB01296 Glucosamine
DB00786 Marimastat
DB01017 Minocycline
DB05495 PG-530742

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1633

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
MMP9

Domain mapping of disease mutations (DMDM)

More...
DMDMi
269849668

<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 <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_0000028757? – 707Removed in 64 kDa matrix metalloproteinase-9 and 67 kDa matrix metalloproteinase-9
<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 – 196 PublicationsAdd BLAST19
PropeptideiPRO_000002875420 – 93Activation peptideAdd BLAST74
<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_000002875594 – ?67 kDa matrix metalloproteinase-9
ChainiPRO_0000028756107 – 70782 kDa matrix metalloproteinase-9Add BLAST601

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>Glycosylationi38N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi120N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi127N-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 bondi230 ↔ 256PROSITE-ProRule annotation
Disulfide bondi244 ↔ 271PROSITE-ProRule annotation
Disulfide bondi288 ↔ 314PROSITE-ProRule annotation
Disulfide bondi302 ↔ 329PROSITE-ProRule annotation
Disulfide bondi347 ↔ 373PROSITE-ProRule annotation
Disulfide bondi361 ↔ 388PROSITE-ProRule annotation
Disulfide bondi516 ↔ 704

<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

Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9.3 Publications
N- and O-glycosylated.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei59 – 60Cleavage; by MMP32
Sitei106 – 107Cleavage; by MMP32

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P14780

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P14780

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

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PaxDbi
P14780

PeptideAtlas

More...
PeptideAtlasi
P14780

PRoteomics IDEntifications database

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PRIDEi
P14780

ProteomicsDB human proteome resource

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ProteomicsDBi
53082

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
6

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P14780

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

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PhosphoSitePlusi
P14780

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P14780

<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

Detected in neutrophils (at protein level) (PubMed:7683678). Produced by normal alveolar macrophages and granulocytes.1 Publication

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

Activated by 4-aminophenylmercuric acetate and phorbol ester. Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells.3 Publications
(Microbial infection) Expression induced by M.bovis MPB83 (at protein level) (PubMed:20800577).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000100985 Expressed in 154 organ(s), highest expression level in tibia

CleanEx database of gene expression profiles

More...
CleanExi
HS_MMP9

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P14780 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB000348
CAB068199
CAB068200
CAB068201
HPA001238
HPA063909

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

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

Exists as monomer or homodimer; disulfide-linked (PubMed:1281792, PubMed:7683678). Exists also as heterodimer with LCN2 (PubMed:1281792, PubMed:7683678). Macrophages and transformed cell lines produce only the monomeric form. Interacts with ECM1 (PubMed:16512877).7 Publications

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
110461, 18 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P14780

Database of interacting proteins

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DIPi
DIP-29518N

Protein interaction database and analysis system

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IntActi
P14780, 11 interactors

Molecular INTeraction database

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MINTi
P14780

STRING: functional protein association networks

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STRINGi
9606.ENSP00000361405

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P14780

<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

1707
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1GKCX-ray2.30A/B107-443[»]
1GKDX-ray2.10A/B107-443[»]
1ITVX-ray1.95A/B513-707[»]
1L6JX-ray2.50A20-444[»]
1LKGmodel-A1-707[»]
2OVXX-ray2.00A/B110-443[»]
2OVZX-ray2.00A/B110-443[»]
2OW0X-ray2.00A/B110-443[»]
2OW1X-ray2.20A/B110-443[»]
2OW2X-ray2.90A/B110-443[»]
4H1QX-ray1.59A/B110-214[»]
A/B391-444[»]
4H2EX-ray2.90A/B107-216[»]
A/B392-444[»]
4H3XX-ray1.76A/B107-216[»]
A/B392-444[»]
4H82X-ray1.90A/B/C/D110-444[»]
4HMAX-ray1.94A/B110-214[»]
A/B391-444[»]
4JIJX-ray1.70A/B107-444[»]
4JQGX-ray1.85A/B107-444[»]
4WZVX-ray1.65A/B110-444[»]
4XCTX-ray1.30A113-444[»]
5CUHX-ray1.83A/B107-444[»]
5I12X-ray1.59A113-444[»]
5TH6X-ray1.70A/B/C/D40-443[»]
5TH9X-ray3.00A/B/C40-443[»]
5UE3X-ray1.60A/B35-445[»]
5UE4X-ray1.80A/B35-445[»]
6ESMX-ray1.10A110-227[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P14780

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

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SMRi
P14780

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P14780

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini225 – 273Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST49
Domaini283 – 331Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST49
Domaini342 – 390Fibronectin type-II 3PROSITE-ProRule annotationAdd BLAST49
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati518 – 563Hemopexin 1Add BLAST46
Repeati564 – 608Hemopexin 2Add BLAST45
Repeati610 – 657Hemopexin 3Add BLAST48
Repeati658 – 704Hemopexin 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>Motifi97 – 104Cysteine 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

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GeneTreei
ENSGT00940000157415

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG052484

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P14780

KEGG Orthology (KO)

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KOi
K01403

Identification of Orthologs from Complete Genome Data

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OMAi
GFCPSER

Database of Orthologous Groups

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OrthoDBi
1072976at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P14780

TreeFam database of animal gene trees

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TreeFami
TF315428

Family and domain databases

Conserved Domains Database

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

Gene3D Structural and Functional Annotation of Protein Families

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

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR013806 Kringle-like
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028688 MMP9
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
IPR036366 PGBDSf

The PANTHER Classification System

More...
PANTHERi
PTHR10201:SF30 PTHR10201:SF30, 1 hit

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001191 Peptidase_M10A_matrix, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00138 MATRIXIN

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00546 CYSTEINE_SWITCH, 1 hit
PS00023 FN2_1, 3 hits
PS51092 FN2_2, 3 hits
PS00024 HEMOPEXIN, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit

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

P14780-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLWQPLVLV LLVLGCCFAA PRQRQSTLVL FPGDLRTNLT DRQLAEEYLY
60 70 80 90 100
RYGYTRVAEM RGESKSLGPA LLLLQKQLSL PETGELDSAT LKAMRTPRCG
110 120 130 140 150
VPDLGRFQTF EGDLKWHHHN ITYWIQNYSE DLPRAVIDDA FARAFALWSA
160 170 180 190 200
VTPLTFTRVY SRDADIVIQF GVAEHGDGYP FDGKDGLLAH AFPPGPGIQG
210 220 230 240 250
DAHFDDDELW SLGKGVVVPT RFGNADGAAC HFPFIFEGRS YSACTTDGRS
260 270 280 290 300
DGLPWCSTTA NYDTDDRFGF CPSERLYTQD GNADGKPCQF PFIFQGQSYS
310 320 330 340 350
ACTTDGRSDG YRWCATTANY DRDKLFGFCP TRADSTVMGG NSAGELCVFP
360 370 380 390 400
FTFLGKEYST CTSEGRGDGR LWCATTSNFD SDKKWGFCPD QGYSLFLVAA
410 420 430 440 450
HEFGHALGLD HSSVPEALMY PMYRFTEGPP LHKDDVNGIR HLYGPRPEPE
460 470 480 490 500
PRPPTTTTPQ PTAPPTVCPT GPPTVHPSER PTAGPTGPPS AGPTGPPTAG
510 520 530 540 550
PSTATTVPLS PVDDACNVNI FDAIAEIGNQ LYLFKDGKYW RFSEGRGSRP
560 570 580 590 600
QGPFLIADKW PALPRKLDSV FEERLSKKLF FFSGRQVWVY TGASVLGPRR
610 620 630 640 650
LDKLGLGADV AQVTGALRSG RGKMLLFSGR RLWRFDVKAQ MVDPRSASEV
660 670 680 690 700
DRMFPGVPLD THDVFQYREK AYFCQDRFYW RVSSRSELNQ VDQVGYVTYD

ILQCPED
Length:707
Mass (Da):78,458
Last modified:November 24, 2009 - 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:i2165AC8CA1466209
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 conflicti110F → L in BAG35956 (PubMed:14702039).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_01378020A → V3 PublicationsCorresponds to variant dbSNP:rs1805088EnsemblClinVar.1
Natural variantiVAR_03700438N → S. Corresponds to variant dbSNP:rs41427445Ensembl.1
Natural variantiVAR_01378182E → K1 PublicationCorresponds to variant dbSNP:rs1805089Ensembl.1
Natural variantiVAR_020054127N → K1 PublicationCorresponds to variant dbSNP:rs3918252Ensembl.1
Natural variantiVAR_025165239R → H1 PublicationCorresponds to variant dbSNP:rs28763886EnsemblClinVar.1
Natural variantiVAR_013782279Q → R Common polymorphism; may be associated with susceptibility to IDD. 4 PublicationsCorresponds to variant dbSNP:rs17576EnsemblClinVar.1
Natural variantiVAR_025166571F → V1 PublicationCorresponds to variant dbSNP:rs35691798Ensembl.1
Natural variantiVAR_024595574R → P5 PublicationsCorresponds to variant dbSNP:rs2250889EnsemblClinVar.1
Natural variantiVAR_014742668R → Q2 PublicationsCorresponds to variant dbSNP:rs17577EnsemblClinVar.1

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
J05070 mRNA Translation: AAA51539.1
M68343 Genomic DNA No translation available.
M68344 Genomic DNA No translation available.
M68345 Genomic DNA No translation available.
M68346 Genomic DNA No translation available.
M68347 Genomic DNA No translation available.
M68348 Genomic DNA No translation available.
M68349 Genomic DNA No translation available.
M68350 Genomic DNA No translation available.
M68351 Genomic DNA No translation available.
M68352 Genomic DNA No translation available.
M68353 Genomic DNA No translation available.
M68354 Genomic DNA No translation available.
M68355 Genomic DNA No translation available.
AK313137 mRNA Translation: BAG35956.1
AF538844 Genomic DNA Translation: AAM97934.1
DQ194553 Genomic DNA Translation: ABA03169.1
AL162458 Genomic DNA No translation available.
BC006093 mRNA Translation: AAH06093.1
D10051 Genomic DNA Translation: BAA20967.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS13390.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A34458

NCBI Reference Sequences

More...
RefSeqi
NP_004985.2, NM_004994.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.297413

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000372330; ENSP00000361405; ENSG00000100985

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4318

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:4318

UCSC genome browser

More...
UCSCi
uc002xqz.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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05070 mRNA Translation: AAA51539.1
M68343 Genomic DNA No translation available.
M68344 Genomic DNA No translation available.
M68345 Genomic DNA No translation available.
M68346 Genomic DNA No translation available.
M68347 Genomic DNA No translation available.
M68348 Genomic DNA No translation available.
M68349 Genomic DNA No translation available.
M68350 Genomic DNA No translation available.
M68351 Genomic DNA No translation available.
M68352 Genomic DNA No translation available.
M68353 Genomic DNA No translation available.
M68354 Genomic DNA No translation available.
M68355 Genomic DNA No translation available.
AK313137 mRNA Translation: BAG35956.1
AF538844 Genomic DNA Translation: AAM97934.1
DQ194553 Genomic DNA Translation: ABA03169.1
AL162458 Genomic DNA No translation available.
BC006093 mRNA Translation: AAH06093.1
D10051 Genomic DNA Translation: BAA20967.1
CCDSiCCDS13390.1
PIRiA34458
RefSeqiNP_004985.2, NM_004994.2
UniGeneiHs.297413

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GKCX-ray2.30A/B107-443[»]
1GKDX-ray2.10A/B107-443[»]
1ITVX-ray1.95A/B513-707[»]
1L6JX-ray2.50A20-444[»]
1LKGmodel-A1-707[»]
2OVXX-ray2.00A/B110-443[»]
2OVZX-ray2.00A/B110-443[»]
2OW0X-ray2.00A/B110-443[»]
2OW1X-ray2.20A/B110-443[»]
2OW2X-ray2.90A/B110-443[»]
4H1QX-ray1.59A/B110-214[»]
A/B391-444[»]
4H2EX-ray2.90A/B107-216[»]
A/B392-444[»]
4H3XX-ray1.76A/B107-216[»]
A/B392-444[»]
4H82X-ray1.90A/B/C/D110-444[»]
4HMAX-ray1.94A/B110-214[»]
A/B391-444[»]
4JIJX-ray1.70A/B107-444[»]
4JQGX-ray1.85A/B107-444[»]
4WZVX-ray1.65A/B110-444[»]
4XCTX-ray1.30A113-444[»]
5CUHX-ray1.83A/B107-444[»]
5I12X-ray1.59A113-444[»]
5TH6X-ray1.70A/B/C/D40-443[»]
5TH9X-ray3.00A/B/C40-443[»]
5UE3X-ray1.60A/B35-445[»]
5UE4X-ray1.80A/B35-445[»]
6ESMX-ray1.10A110-227[»]
ProteinModelPortaliP14780
SMRiP14780
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110461, 18 interactors
CORUMiP14780
DIPiDIP-29518N
IntActiP14780, 11 interactors
MINTiP14780
STRINGi9606.ENSP00000361405

Chemistry databases

BindingDBiP14780
ChEMBLiCHEMBL321
DrugBankiDB03683 2-{[Formyl(Hydroxy)Amino]Methyl}-4-Methylpentanoic Acid
DB05387 AE-941
DB01197 Captopril
DB01296 Glucosamine
DB00786 Marimastat
DB01017 Minocycline
DB05495 PG-530742
GuidetoPHARMACOLOGYi1633

Protein family/group databases

MEROPSiM10.004

PTM databases

GlyConnecti6
iPTMnetiP14780
PhosphoSitePlusiP14780
UniCarbKBiP14780

Polymorphism and mutation databases

BioMutaiMMP9
DMDMi269849668

Proteomic databases

EPDiP14780
jPOSTiP14780
PaxDbiP14780
PeptideAtlasiP14780
PRIDEiP14780
ProteomicsDBi53082

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4318
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372330; ENSP00000361405; ENSG00000100985
GeneIDi4318
KEGGihsa:4318
UCSCiuc002xqz.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4318
DisGeNETi4318
EuPathDBiHostDB:ENSG00000100985.7

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MMP9

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0015874
HGNCiHGNC:7176 MMP9
HPAiCAB000348
CAB068199
CAB068200
CAB068201
HPA001238
HPA063909
MalaCardsiMMP9
MIMi120361 gene
603932 phenotype
613073 phenotype
neXtProtiNX_P14780
OpenTargetsiENSG00000100985
Orphaneti1040 Metaphyseal anadysplasia
PharmGKBiPA30889

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1565 Eukaryota
ENOG410XQ5D LUCA
GeneTreeiENSGT00940000157415
HOVERGENiHBG052484
InParanoidiP14780
KOiK01403
OMAiGFCPSER
OrthoDBi1072976at2759
PhylomeDBiP14780
TreeFamiTF315428

Enzyme and pathway databases

BRENDAi3.4.24.35 2681
ReactomeiR-HSA-1433557 Signaling by SCF-KIT
R-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-2022090 Assembly of collagen fibrils and other multimeric structures
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-6798695 Neutrophil degranulation
SIGNORiP14780

Miscellaneous databases

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

More...
ChiTaRSi
MMP9 human
EvolutionaryTraceiP14780

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
MMP9

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

More...
GenomeRNAii
4318

Protein Ontology

More...
PROi
PR:P14780

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000100985 Expressed in 154 organ(s), highest expression level in tibia
CleanExiHS_MMP9
GenevisibleiP14780 HS

Family and domain databases

CDDicd00062 FN2, 3 hits
cd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit
Gene3Di1.10.101.10, 1 hit
2.10.10.10, 3 hits
2.110.10.10, 1 hit
3.40.390.10, 1 hit
InterProiView protein in InterPro
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR013806 Kringle-like
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028688 MMP9
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:SF30 PTHR10201:SF30, 1 hit
PfamiView protein in Pfam
PF00040 fn2, 3 hits
PF00045 Hemopexin, 4 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PIRSFiPIRSF001191 Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138 MATRIXIN
SMARTiView protein in SMART
SM00059 FN2, 3 hits
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
SSF57440 SSF57440, 3 hits
PROSITEiView protein in PROSITE
PS00546 CYSTEINE_SWITCH, 1 hit
PS00023 FN2_1, 3 hits
PS51092 FN2_2, 3 hits
PS00024 HEMOPEXIN, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMMP9_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: P14780
Secondary accession number(s): B2R7V9
, Q3LR70, Q8N725, Q9H4Z1, Q9UCJ9, Q9UCL1, Q9UDK2
<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: April 1, 1990
Last sequence update: November 24, 2009
Last modified: January 16, 2019
This is version 235 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, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
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