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Entry version 183 (13 Feb 2019)
Sequence version 2 (11 Jan 2011)
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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 5

Gene

ADAMTS5

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

Metalloproteinase that plays an important role in connective tissue organization, development, inflammation, arthritis, and cell migration. ADAMTS5 is an extracellular matrix (ECM) degrading enzyme that show proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including aggrecan, versican, brevican and neurocan (PubMed:16133547, PubMed:18992360). Cleavage within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a role in embryonic development, including limb and cardiac morphogenesis, and skeletal muscle development through its versican remodeling properties. Participates in development of brown adipose tissue and browning of white adipose tissue. Plays an important role for T-lymphocyte migration from draining lymph nodes following viral infection.By similarity2 Publications

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

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi209Zinc; in inhibited formBy similarity1
<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>Sitei261Cleveage; by furin and PCSK71 Publication1
Metal bindingi410Zinc; 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 sitei411PROSITE-ProRule annotation1 Publication1
Metal bindingi414Zinc; catalytic1 Publication1
Metal bindingi420Zinc; catalytic1 Publication1

<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

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
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.4.24.B12 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-5083635 Defective B3GALTL causes Peters-plus syndrome (PpS)
R-HSA-5173214 O-glycosylation of TSR domain-containing proteins

SIGNOR Signaling Network Open Resource

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SIGNORi
Q9UNA0

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M12.225

<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:
A disintegrin and metalloproteinase with thrombospondin motifs 5 (EC:3.4.24.-)
Short name:
ADAM-TS 5
Short name:
ADAM-TS5
Short name:
ADAMTS-5
Alternative name(s):
A disintegrin and metalloproteinase with thrombospondin motifs 11
Short name:
ADAM-TS 11
Short name:
ADAMTS-11
ADMP-2
Aggrecanase-2
<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:ADAMTS5
Synonyms:ADAMTS11, ADMP2
<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 21

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000154736.5

Human Gene Nomenclature Database

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HGNCi
HGNC:221 ADAMTS5

Online Mendelian Inheritance in Man (OMIM)

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MIMi
605007 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q9UNA0

<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

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

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>Mutagenesisi411E → A: Complete loss of catalytic activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
11096

Open Targets

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OpenTargetsi
ENSG00000154736

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2285

Drug and drug target database

More...
DrugBanki
DB03880 Batimastat
DB06945 N-hydroxy-4-({4-[4-(trifluoromethyl)phenoxy]phenyl}sulfonyl)tetrahydro-2H-pyran-4-carboxamide

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1678

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ADAMTS5

Domain mapping of disease mutations (DMDM)

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DMDMi
317373326

<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 – 16Sequence analysisAdd BLAST16
<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_000002917017 – 2611 PublicationAdd BLAST245
<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_0000029171262 – 930A disintegrin and metalloproteinase with thrombospondin motifs 5Add BLAST669

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 bondi342 ↔ 3941 Publication
Disulfide bondi371 ↔ 3761 Publication
Disulfide bondi388 ↔ 4711 Publication
Disulfide bondi426 ↔ 4551 Publication
Disulfide bondi497 ↔ 5191 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi498N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi508 ↔ 5291 Publication
Disulfide bondi514 ↔ 5481 Publication
Disulfide bondi542 ↔ 5531 Publication
Glycosylationi570C-linked (Man) tryptophan1 Publication1
Glycosylationi573C-linked (Man) tryptophan1 Publication1
Disulfide bondi579 ↔ 616By similarity
Glycosylationi582O-linked (Fuc...) serine1 Publication1
Disulfide bondi583 ↔ 621By similarity
Disulfide bondi594 ↔ 606By similarity
Glycosylationi728N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi802N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi807N-linked (GlcNAc...) asparagineSequence analysis1

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

The precursor is cleaved by furin and PCSK7 outside of the cell.1 Publication
C- and O-glycosylated. O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X2-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation can mediate the efficient secretion of ADAMTS family members. Can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity).By similarity
Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X2-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity).By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9UNA0

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

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PaxDbi
Q9UNA0

PeptideAtlas

More...
PeptideAtlasi
Q9UNA0

PRoteomics IDEntifications database

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PRIDEi
Q9UNA0

ProteomicsDB human proteome resource

More...
ProteomicsDBi
85273

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9UNA0

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

More...
PhosphoSitePlusi
Q9UNA0

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
Q9UNA0

<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 at low level in placenta primarily but also detected in heart and brain, cervix, uterus, bladder, esophagus, rib cartilage, chondroblastoma, fibrous tissue and a joint capsule from an arthritic patient.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000154736 Expressed in 209 organ(s), highest expression level in decidua

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9UNA0 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB025996
HPA005661
HPA030906
HPA030908

<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%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

WithEntry#Exp.IntActNotes
ACANP136082EBI-2808663,EBI-6259246From Bos taurus.

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

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IntActi
Q9UNA0, 3 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000284987

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q9UNA0

<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

1930
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
2RJQX-ray2.60A262-628[»]
3B8ZX-ray1.40A/B264-480[»]
3HY7X-ray1.69A/B262-480[»]
3HY9X-ray2.02A/B262-480[»]
3HYGX-ray1.40A/B262-480[»]
3LJTX-ray1.60A264-480[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q9UNA0

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

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SMRi
Q9UNA0

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

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EvolutionaryTracei
Q9UNA0

<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>Domaini267 – 476Peptidase M12BPROSITE-ProRule annotationAdd BLAST210
Domaini485 – 566DisintegrinAdd BLAST82
Domaini567 – 622TSP type-1 1PROSITE-ProRule annotationAdd BLAST56
Domaini875 – 929TSP type-1 2PROSITE-ProRule annotationAdd BLAST55

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni732 – 874SpacerAdd BLAST143

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>Motifi207 – 214Cysteine 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 biasi37 – 41Poly-Ala5
Compositional biasi257 – 261Poly-Arg5
Compositional biasi624 – 731Cys-richAdd BLAST108

<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 spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
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.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IND8 Eukaryota
ENOG410ZQPN LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159090

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000004799

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG004313

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9UNA0

KEGG Orthology (KO)

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KOi
K08620

Identification of Orthologs from Complete Genome Data

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OMAi
TVCPGMD

Database of Orthologous Groups

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OrthoDBi
1593287at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9UNA0

TreeFam database of animal gene trees

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TreeFami
TF331949

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.20.100.10, 2 hits
3.40.390.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR006586 ADAM_Cys-rich
IPR010294 ADAM_spacer1
IPR013273 ADAMTS/ADAMTS-like
IPR024079 MetalloPept_cat_dom_sf
IPR013276 Pept_M12B_ADAM-TS5
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N
IPR000884 TSP1_rpt
IPR036383 TSP1_rpt_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05986 ADAM_spacer1, 1 hit
PF01562 Pep_M12B_propep, 1 hit
PF01421 Reprolysin, 1 hit
PF00090 TSP_1, 2 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01860 ADAMTS5
PR01857 ADAMTSFAMILY

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00608 ACR, 1 hit
SM00209 TSP1, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF82895 SSF82895, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50215 ADAM_MEPRO, 1 hit
PS50092 TSP1, 2 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.

Q9UNA0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLLGWASLLL CAFRLPLAAV GPAATPAQDK AGQPPTAAAA AQPRRRQGEE
60 70 80 90 100
VQERAEPPGH PHPLAQRRRS KGLVQNIDQL YSGGGKVGYL VYAGGRRFLL
110 120 130 140 150
DLERDGSVGI AGFVPAGGGT SAPWRHRSHC FYRGTVDGSP RSLAVFDLCG
160 170 180 190 200
GLDGFFAVKH ARYTLKPLLR GPWAEEEKGR VYGDGSARIL HVYTREGFSF
210 220 230 240 250
EALPPRASCE TPASTPEAHE HAPAHSNPSG RAALASQLLD QSALSPAGGS
260 270 280 290 300
GPQTWWRRRR RSISRARQVE LLLVADASMA RLYGRGLQHY LLTLASIANR
310 320 330 340 350
LYSHASIENH IRLAVVKVVV LGDKDKSLEV SKNAATTLKN FCKWQHQHNQ
360 370 380 390 400
LGDDHEEHYD AAILFTREDL CGHHSCDTLG MADVGTICSP ERSCAVIEDD
410 420 430 440 450
GLHAAFTVAH EIGHLLGLSH DDSKFCEETF GSTEDKRLMS SILTSIDASK
460 470 480 490 500
PWSKCTSATI TEFLDDGHGN CLLDLPRKQI LGPEELPGQT YDATQQCNLT
510 520 530 540 550
FGPEYSVCPG MDVCARLWCA VVRQGQMVCL TKKLPAVEGT PCGKGRICLQ
560 570 580 590 600
GKCVDKTKKK YYSTSSHGNW GSWGSWGQCS RSCGGGVQFA YRHCNNPAPR
610 620 630 640 650
NNGRYCTGKR AIYRSCSLMP CPPNGKSFRH EQCEAKNGYQ SDAKGVKTFV
660 670 680 690 700
EWVPKYAGVL PADVCKLTCR AKGTGYYVVF SPKVTDGTEC RLYSNSVCVR
710 720 730 740 750
GKCVRTGCDG IIGSKLQYDK CGVCGGDNSS CTKIVGTFNK KSKGYTDVVR
760 770 780 790 800
IPEGATHIKV RQFKAKDQTR FTAYLALKKK NGEYLINGKY MISTSETIID
810 820 830 840 850
INGTVMNYSG WSHRDDFLHG MGYSATKEIL IVQILATDPT KPLDVRYSFF
860 870 880 890 900
VPKKSTPKVN SVTSHGSNKV GSHTSQPQWV TGPWLACSRT CDTGWHTRTV
910 920 930
QCQDGNRKLA KGCPLSQRPS AFKQCLLKKC
Length:930
Mass (Da):101,718
Last modified:January 11, 2011 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8CCE448A15A29CE8
GO

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_028199138G → A2 PublicationsCorresponds to variant dbSNP:rs457947Ensembl.1
Natural variantiVAR_021849614R → H1 PublicationCorresponds to variant dbSNP:rs2830585Ensembl.1
Natural variantiVAR_028200692L → P3 PublicationsCorresponds to variant dbSNP:rs226794Ensembl.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

More...
DDBJi
Links Updated
AF142099 mRNA Translation: AAD49577.1
AP001698 Genomic DNA Translation: BAA95504.1
AP001697 Genomic DNA Translation: BAA95503.1
BC093775 mRNA Translation: AAH93775.1
BC093777 mRNA Translation: AAH93777.1
AF141293 mRNA Translation: AAF02493.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS13579.1

NCBI Reference Sequences

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RefSeqi
NP_008969.2, NM_007038.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.58324

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000284987; ENSP00000284987; ENSG00000154736

Database of genes from NCBI RefSeq genomes

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GeneIDi
11096

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:11096

UCSC genome browser

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UCSCi
uc002ymg.4 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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF142099 mRNA Translation: AAD49577.1
AP001698 Genomic DNA Translation: BAA95504.1
AP001697 Genomic DNA Translation: BAA95503.1
BC093775 mRNA Translation: AAH93775.1
BC093777 mRNA Translation: AAH93777.1
AF141293 mRNA Translation: AAF02493.1
CCDSiCCDS13579.1
RefSeqiNP_008969.2, NM_007038.4
UniGeneiHs.58324

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RJQX-ray2.60A262-628[»]
3B8ZX-ray1.40A/B264-480[»]
3HY7X-ray1.69A/B262-480[»]
3HY9X-ray2.02A/B262-480[»]
3HYGX-ray1.40A/B262-480[»]
3LJTX-ray1.60A264-480[»]
ProteinModelPortaliQ9UNA0
SMRiQ9UNA0
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9UNA0, 3 interactors
STRINGi9606.ENSP00000284987

Chemistry databases

BindingDBiQ9UNA0
ChEMBLiCHEMBL2285
DrugBankiDB03880 Batimastat
DB06945 N-hydroxy-4-({4-[4-(trifluoromethyl)phenoxy]phenyl}sulfonyl)tetrahydro-2H-pyran-4-carboxamide
GuidetoPHARMACOLOGYi1678

Protein family/group databases

MEROPSiM12.225

PTM databases

iPTMnetiQ9UNA0
PhosphoSitePlusiQ9UNA0

Polymorphism and mutation databases

BioMutaiADAMTS5
DMDMi317373326

Proteomic databases

jPOSTiQ9UNA0
PaxDbiQ9UNA0
PeptideAtlasiQ9UNA0
PRIDEiQ9UNA0
ProteomicsDBi85273

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000284987; ENSP00000284987; ENSG00000154736
GeneIDi11096
KEGGihsa:11096
UCSCiuc002ymg.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
11096
DisGeNETi11096
EuPathDBiHostDB:ENSG00000154736.5

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ADAMTS5

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0016044
HGNCiHGNC:221 ADAMTS5
HPAiCAB025996
HPA005661
HPA030906
HPA030908
MIMi605007 gene
neXtProtiNX_Q9UNA0
OpenTargetsiENSG00000154736

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IND8 Eukaryota
ENOG410ZQPN LUCA
GeneTreeiENSGT00940000159090
HOGENOMiHOG000004799
HOVERGENiHBG004313
InParanoidiQ9UNA0
KOiK08620
OMAiTVCPGMD
OrthoDBi1593287at2759
PhylomeDBiQ9UNA0
TreeFamiTF331949

Enzyme and pathway databases

BRENDAi3.4.24.B12 2681
ReactomeiR-HSA-1474228 Degradation of the extracellular matrix
R-HSA-5083635 Defective B3GALTL causes Peters-plus syndrome (PpS)
R-HSA-5173214 O-glycosylation of TSR domain-containing proteins
SIGNORiQ9UNA0

Miscellaneous databases

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

More...
ChiTaRSi
ADAMTS5 human
EvolutionaryTraceiQ9UNA0

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
ADAMTS5

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

More...
GenomeRNAii
11096
PMAP-CutDBiQ9UNA0

Protein Ontology

More...
PROi
PR:Q9UNA0

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000154736 Expressed in 209 organ(s), highest expression level in decidua
GenevisibleiQ9UNA0 HS

Family and domain databases

Gene3Di2.20.100.10, 2 hits
3.40.390.10, 1 hit
InterProiView protein in InterPro
IPR006586 ADAM_Cys-rich
IPR010294 ADAM_spacer1
IPR013273 ADAMTS/ADAMTS-like
IPR024079 MetalloPept_cat_dom_sf
IPR013276 Pept_M12B_ADAM-TS5
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N
IPR000884 TSP1_rpt
IPR036383 TSP1_rpt_sf
PfamiView protein in Pfam
PF05986 ADAM_spacer1, 1 hit
PF01562 Pep_M12B_propep, 1 hit
PF01421 Reprolysin, 1 hit
PF00090 TSP_1, 2 hits
PRINTSiPR01860 ADAMTS5
PR01857 ADAMTSFAMILY
SMARTiView protein in SMART
SM00608 ACR, 1 hit
SM00209 TSP1, 2 hits
SUPFAMiSSF82895 SSF82895, 2 hits
PROSITEiView protein in PROSITE
PS50215 ADAM_MEPRO, 1 hit
PS50092 TSP1, 2 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 nameiATS5_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: Q9UNA0
Secondary accession number(s): Q52LV4, Q9UKP2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 11, 2011
Last modified: February 13, 2019
This is version 183 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
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