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UniProtKB - Q9UHI8 (ATS1_HUMAN)

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 1

Gene

ADAMTS1

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

Cleaves aggrecan, a cartilage proteoglycan, at the '1938-Glu-|-Leu-1939' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover (By similarity). Has angiogenic inhibitor activity. Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture.By similarity1 Publication

<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 bindingi198Zinc; in inhibited formBy similarity1
Metal bindingi261Calcium 11 Publication1
Metal bindingi261Calcium 21 Publication1
Metal bindingi344Calcium 11 Publication1
Metal bindingi344Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi351Calcium 11 Publication1
Metal bindingi401Zinc; 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 sitei402PROSITE-ProRule annotation1 Publication1
Metal bindingi405Zinc; catalytic1 Publication1
Metal bindingi411Zinc; catalytic1 Publication1
Metal bindingi462Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi465Calcium 11 Publication1
Metal bindingi465Calcium 21 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

  • heparin binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: Ensembl
  • metallopeptidase activity Source: ProtInc
  • zinc ion binding Source: InterPro
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHeparin-binding, Hydrolase, Metalloprotease, Protease
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.24.B11 2681
3.4.24.B12 2681

Reactome - a knowledgebase of biological pathways and processes

More...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

More...SIGNORi		Q9UHI8

Protein family/group databases

MEROPS protease database

More...MEROPSi		M12.222

Transport Classification Database

More...TCDBi		8.A.77.1.6 the sheddase (sheddase) family

<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 1 (EC:3.4.24.-)
Short name:
ADAM-TS 1
Short name:
ADAM-TS1
Short name:
ADAMTS-1
Alternative name(s):
METH-1
<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:ADAMTS1
Synonyms:KIAA1346, METH1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 21

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000154734.14

Human Gene Nomenclature Database

More...HGNCi		HGNC:217 ADAMTS1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		605174 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9UHI8

<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		9510

Open Targets

More...OpenTargetsi		ENSG00000154734

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA24536

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5133

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1674

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ADAMTS1

Domain mapping of disease mutations (DMDM)

More...DMDMi		124053460

<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 – 49Sequence analysisAdd BLAST49
<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_000002915050 – 252By similarityAdd BLAST203
<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_0000029151253 – 967A disintegrin and metalloproteinase with thrombospondin motifs 1Add BLAST715

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 bondi333 ↔ 3851 Publication
Disulfide bondi362 ↔ 3671 Publication
Disulfide bondi379 ↔ 4621 Publication
Disulfide bondi417 ↔ 4461 Publication
Disulfide bondi488 ↔ 5111 Publication
Disulfide bondi499 ↔ 5211 Publication
Disulfide bondi506 ↔ 5401 Publication
Disulfide bondi534 ↔ 5451 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>Glycosylationi547N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi571 ↔ 608By similarity
Disulfide bondi575 ↔ 613By similarity
Disulfide bondi586 ↔ 598By similarity
Glycosylationi720N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi764N-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 a furin endopeptidase.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

Encyclopedia of Proteome Dynamics

More...EPDi		Q9UHI8

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9UHI8

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9UHI8

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

More...PaxDbi		Q9UHI8

PeptideAtlas

More...PeptideAtlasi		Q9UHI8

PRoteomics IDEntifications database

More...PRIDEi		Q9UHI8

ProteomicsDB human proteome resource

More...ProteomicsDBi		84361

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		Q9UHI8

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9UHI8

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

More...PhosphoSitePlusi		Q9UHI8

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		Q9UHI8

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000154734 Expressed in 224 organ(s), highest expression level in female gonad

CleanEx database of gene expression profiles

More...CleanExi		HS_ADAMTS1

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9UHI8 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9UHI8 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB016394

<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		114888, 37 interactors

Protein interaction database and analysis system

More...IntActi		Q9UHI8, 4 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000284984

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9UHI8

<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

1967
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JIHX-ray2.10A/B253-548[»]
2V4BX-ray2.00A/B253-548[»]
3Q2GX-ray2.30A/B256-548[»]
3Q2HX-ray2.33A/B256-548[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q9UHI8

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

More...SMRi		Q9UHI8

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		Q9UHI8

<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>Domaini258 – 467Peptidase M12BPROSITE-ProRule annotationAdd BLAST210
Domaini476 – 559DisintegrinAdd BLAST84
Domaini559 – 614TSP type-1 1PROSITE-ProRule annotationAdd BLAST56
Domaini854 – 905TSP type-1 2PROSITE-ProRule annotationAdd BLAST52
Domaini908 – 967TSP type-1 3PROSITE-ProRule annotationAdd BLAST60

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>Regioni725 – 849SpacerAdd BLAST125

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>Motifi196 – 203Cysteine 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 biasi617 – 724Cys-richAdd BLAST108
Compositional biasi843 – 846Poly-Lys4

<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		KOG3538 Eukaryota
ENOG410XPKZ LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156815

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000004799

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG004313

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9UHI8

KEGG Orthology (KO)

More...KOi		K08617

Identification of Orthologs from Complete Genome Data

More...OMAi		GPAVEWT

Database of Orthologous Groups

More...OrthoDBi		655109at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9UHI8

TreeFam database of animal gene trees

More...TreeFami		TF331949

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.20.100.10, 3 hits
3.40.390.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006586 ADAM_Cys-rich
IPR010294 ADAM_spacer1
IPR013273 ADAMTS/ADAMTS-like
IPR024079 MetalloPept_cat_dom_sf
IPR013274 Pept_M12B_ADAM-TS1
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, 3 hits

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01858 ADAMTS1
PR01857 ADAMTSFAMILY

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00608 ACR, 1 hit
SM00209 TSP1, 3 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF82895 SSF82895, 3 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50215 ADAM_MEPRO, 1 hit
PS50092 TSP1, 3 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 3 potential isoforms that are computationally mapped.Show allAlign All

Q9UHI8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQRAVPEGFG RRKLGSDMGN AERAPGSRSF GPVPTLLLLA AALLAVSDAL 
        60         70         80         90        100
GRPSEEDEEL VVPELERAPG HGTTRLRLHA FDQQLDLELR PDSSFLAPGF 
       110        120        130        140        150
TLQNVGRKSG SETPLPETDL AHCFYSGTVN GDPSSAAALS LCEGVRGAFY 
       160        170        180        190        200
LLGEAYFIQP LPAASERLAT AAPGEKPPAP LQFHLLRRNR QGDVGGTCGV 
       210        220        230        240        250
VDDEPRPTGK AETEDEDEGT EGEDEGAQWS PQDPALQGVG QPTGTGSIRK 
       260        270        280        290        300
KRFVSSHRYV ETMLVADQSM AEFHGSGLKH YLLTLFSVAA RLYKHPSIRN 
       310        320        330        340        350
SVSLVVVKIL VIHDEQKGPE VTSNAALTLR NFCNWQKQHN PPSDRDAEHY 
       360        370        380        390        400
DTAILFTRQD LCGSQTCDTL GMADVGTVCD PSRSCSVIED DGLQAAFTTA 
       410        420        430        440        450
HELGHVFNMP HDDAKQCASL NGVNQDSHMM ASMLSNLDHS QPWSPCSAYM 
       460        470        480        490        500
ITSFLDNGHG ECLMDKPQNP IQLPGDLPGT SYDANRQCQF TFGEDSKHCP 
       510        520        530        540        550
DAASTCSTLW CTGTSGGVLV CQTKHFPWAD GTSCGEGKWC INGKCVNKTD 
       560        570        580        590        600
RKHFDTPFHG SWGMWGPWGD CSRTCGGGVQ YTMRECDNPV PKNGGKYCEG 
       610        620        630        640        650
KRVRYRSCNL EDCPDNNGKT FREEQCEAHN EFSKASFGSG PAVEWIPKYA 
       660        670        680        690        700
GVSPKDRCKL ICQAKGIGYF FVLQPKVVDG TPCSPDSTSV CVQGQCVKAG 
       710        720        730        740        750
CDRIIDSKKK FDKCGVCGGN GSTCKKISGS VTSAKPGYHD IITIPTGATN 
       760        770        780        790        800
IEVKQRNQRG SRNNGSFLAI KAADGTYILN GDYTLSTLEQ DIMYKGVVLR 
       810        820        830        840        850
YSGSSAALER IRSFSPLKEP LTIQVLTVGN ALRPKIKYTY FVKKKKESFN 
       860        870        880        890        900
AIPTFSAWVI EEWGECSKSC ELGWQRRLVE CRDINGQPAS ECAKEVKPAS 
       910        920        930        940        950
TRPCADHPCP QWQLGEWSSC SKTCGKGYKK RSLKCLSHDG GVLSHESCDP 
       960 
LKKPKHFIDF CTMAECS
Length:967
Mass (Da):105,358
Last modified:January 23, 2007 - v4
<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:i334119D6310A05A7
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7C206H7C206_HUMAN
A disintegrin and metalloproteinase...
ADAMTS1
200Annotation score:

Annotation score:1 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>
E5RI60E5RI60_HUMAN
A disintegrin and metalloproteinase...
ADAMTS1
171Annotation score:

Annotation score:1 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>
E5RJR7E5RJR7_HUMAN
A disintegrin and metalloproteinase...
ADAMTS1
128Annotation score:

Annotation score:1 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAD48080 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA92584 differs from that shown. Reason: Erroneous initiation.Curated

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 conflicti468Q → H in AAF15317 (Ref. 1) Curated1
Sequence conflicti561S → N in AAF15317 (Ref. 1) 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_030001227A → P3 PublicationsCorresponds to variant dbSNP:rs428785Ensembl.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
AF170084 mRNA Translation: AAF15317.1
AF060152 mRNA Translation: AAD48080.1 Different initiation.
AF207664 mRNA Translation: AAF23772.1
AB037767 mRNA Translation: BAA92584.1 Different initiation.
AP001697 Genomic DNA Translation: BAA95502.1
CH471079 Genomic DNA Translation: EAX09951.1
CH471079 Genomic DNA Translation: EAX09952.1
AL162080 mRNA Translation: CAB82413.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS33524.1

Protein sequence database of the Protein Information Resource

More...PIRi		T47158

NCBI Reference Sequences

More...RefSeqi		NP_008919.3, NM_006988.4

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.643357

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000284984; ENSP00000284984; ENSG00000154734

Database of genes from NCBI RefSeq genomes

More...GeneIDi		9510

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:9510

UCSC genome browser

More...UCSCi		uc002ymf.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

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170084 mRNA Translation: AAF15317.1
AF060152 mRNA Translation: AAD48080.1 Different initiation.
AF207664 mRNA Translation: AAF23772.1
AB037767 mRNA Translation: BAA92584.1 Different initiation.
AP001697 Genomic DNA Translation: BAA95502.1
CH471079 Genomic DNA Translation: EAX09951.1
CH471079 Genomic DNA Translation: EAX09952.1
AL162080 mRNA Translation: CAB82413.1
CCDSiCCDS33524.1
PIRiT47158
RefSeqiNP_008919.3, NM_006988.4
UniGeneiHs.643357

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JIHX-ray2.10A/B253-548[»]
2V4BX-ray2.00A/B253-548[»]
3Q2GX-ray2.30A/B256-548[»]
3Q2HX-ray2.33A/B256-548[»]
ProteinModelPortaliQ9UHI8
SMRiQ9UHI8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114888, 37 interactors
IntActiQ9UHI8, 4 interactors
STRINGi9606.ENSP00000284984

Chemistry databases

BindingDBiQ9UHI8
ChEMBLiCHEMBL5133
GuidetoPHARMACOLOGYi1674

Protein family/group databases

MEROPSiM12.222
TCDBi8.A.77.1.6 the sheddase (sheddase) family

PTM databases

CarbonylDBiQ9UHI8
iPTMnetiQ9UHI8
PhosphoSitePlusiQ9UHI8

Polymorphism and mutation databases

BioMutaiADAMTS1
DMDMi124053460

Proteomic databases

EPDiQ9UHI8
jPOSTiQ9UHI8
MaxQBiQ9UHI8
PaxDbiQ9UHI8
PeptideAtlasiQ9UHI8
PRIDEiQ9UHI8
ProteomicsDBi84361

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		9510
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000284984; ENSP00000284984; ENSG00000154734
GeneIDi9510
KEGGihsa:9510
UCSCiuc002ymf.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		9510
DisGeNETi9510
EuPathDBiHostDB:ENSG00000154734.14

GeneCards: human genes, protein and diseases

More...GeneCardsi		ADAMTS1
HGNCiHGNC:217 ADAMTS1
HPAiCAB016394
MIMi605174 gene
neXtProtiNX_Q9UHI8
OpenTargetsiENSG00000154734
PharmGKBiPA24536

Human Unidentified Gene-Encoded large proteins database

More...HUGEi		Search...

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3538 Eukaryota
ENOG410XPKZ LUCA
GeneTreeiENSGT00940000156815
HOGENOMiHOG000004799
HOVERGENiHBG004313
InParanoidiQ9UHI8
KOiK08617
OMAiGPAVEWT
OrthoDBi655109at2759
PhylomeDBiQ9UHI8
TreeFamiTF331949

Enzyme and pathway databases

BRENDAi3.4.24.B11 2681
3.4.24.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
SIGNORiQ9UHI8

Miscellaneous databases

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

More...ChiTaRSi		ADAMTS1 human
EvolutionaryTraceiQ9UHI8

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		ADAMTS1

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

More...GenomeRNAii		9510
PMAP-CutDBiQ9UHI8

Protein Ontology

More...PROi		PR:Q9UHI8

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000154734 Expressed in 224 organ(s), highest expression level in female gonad
CleanExiHS_ADAMTS1
ExpressionAtlasiQ9UHI8 baseline and differential
GenevisibleiQ9UHI8 HS

Family and domain databases

Gene3Di2.20.100.10, 3 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
IPR013274 Pept_M12B_ADAM-TS1
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, 3 hits
PRINTSiPR01858 ADAMTS1
PR01857 ADAMTSFAMILY
SMARTiView protein in SMART
SM00608 ACR, 1 hit
SM00209 TSP1, 3 hits
SUPFAMiSSF82895 SSF82895, 3 hits
PROSITEiView protein in PROSITE
PS50215 ADAM_MEPRO, 1 hit
PS50092 TSP1, 3 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 nameiATS1_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: Q9UHI8
Secondary accession number(s): D3DSD5
, Q9NSJ8, Q9P2K0, Q9UH83, Q9UP80
<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: May 30, 2000
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 183 of the entry and version 4 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. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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