Protein detail
ATS1
A disintegrin and metalloproteinase with thrombospondin motifs 1 (ADAM-TS 1) (ADAM-TS1) (ADAMTS-1) (EC 3.4.24.-) (METH-1)
Entry name ATS1 | UniProt ID | EVMP score 0.38 |
Frequency 1 | Transmembrane count | Protein classification Cancer-related genesPlasma proteinsPredicted intracellular proteinsPredicted secreted proteinsTransporters |
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
A disintegrin and metalloproteinase with thrombospondin motifs 1 (ADAM-TS 1) (ADAM-TS1) (ADAMTS-1) (EC 3.4.24.-) (METH-1)
Protein Class
Cancer-related genesPlasma proteinsPredicted intracellular proteinsPredicted secreted proteinsTransporters
Protein Function
- Predicted intracellular proteins
- Cancer-related genes:Candidate cancer biomarkers
- Predicted secreted proteins
- Transporters:Accessory Factors Involved in Transport
Ensembl
Entrez Gene Symbol
Gene Synonym
C3-C5KIAA1346METH1
Gene Description
ADAM metallopeptidase with thrombospondin type 1 motif 1
Chromosome
21
Position
26835755-26845409
Frequency
1
EVMP Score
0.38
Fluorescence & Localization
Cell SpecificCardiomyocytesBlood Lineage Specificdendritic cells
Function & Pathway
Protein Function
- Predicted intracellular proteins
- Cancer-related genes:Candidate cancer biomarkers
- Predicted secreted proteins
- Transporters:Accessory Factors Involved in Transport
Cellular Component
Molecular Function
Biological Process
Reactome
- R-hsa-1474228 degradation of the extracellular matrix
- R-hsa-3906995 diseases associated with o glycosylation of proteins
- R-hsa-3781865 diseases of glycosylation
- R-hsa-5668914 diseases of metabolism
- R-hsa-1474244 extracellular matrix organization
- R-hsa-5173214 o glycosylation of tsr domain containing proteins
- R-hsa-5173105 o linked glycosylation
- R-hsa-597592 post translational protein modification
Canonical Pathways
- M193 Pid nephrin neph1 pathway
- M16 Pid insulin pathway
- M12 Pid rhoa pathway
Mediation Categories
Clinical-translation mediationMetabolism mediation
Relations & Evidence
Enzyme-Mediated Modification
1 record.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| ADAMTS1 | FURIN | P09958 | F | 253 | cleavage | HPRD | HPRD:10373500 |
Ligand-Receptor Signaling
21 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| receptor | receptor | scConnect | No | Yes | Yes | No | No |
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Regulatory Interaction Network
0 records.
Protein Complex Composition
0 records.
Isolation & Detection Technology
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Differential Ultracentrifugation | Mass spectrometry | 1 | 37505422 |
Sequence, Structure & Domains
Sequences
Length
967
Mass
105,358
Sequence
MQRAVPEGFGRRKLGSDMGNAERAPGSRSFGPVPTLLLLAAALLAVSDALGRPSEEDEELVVPELERAPGHGTTRLRLHAFDQQLDLELRPDSSFLAPGFTLQNVGRKSGSETPLPETDLAHCFYSGTVNGDPSSAAALSLCEGVRGAFYLLGEAYFIQPLPAASERLATAAPGEKPPAPLQFHLLRRNRQGDVGGTCGVVDDEPRPTGKAETEDEDEGTEGEDEGAQWSPQDPALQGVGQPTGTGSIRKKRFVSSHRYVETMLVADQSMAEFHGSGLKHYLLTLFSVAARLYKHPSIRNSVSLVVVKILVIHDEQKGPEVTSNAALTLRNFCNWQKQHNPPSDRDAEHYDTAILFTRQDLCGSQTCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDAKQCASLNGVNQDSHMMASMLSNLDHSQPWSPCSAYMITSFLDNGHGECLMDKPQNPIQLPGDLPGTSYDANRQCQFTFGEDSKHCPDAASTCSTLWCTGTSGGVLVCQTKHFPWADGTSCGEGKWCINGKCVNKTDRKHFDTPFHGSWGMWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNLEDCPDNNGKTFREEQCEAHNEFSKASFGSGPAVEWIPKYAGVSPKDRCKLICQAKGIGYFFVLQPKVVDGTPCSPDSTSVCVQGQCVKAGCDRIIDSKKKFDKCGVCGGNGSTCKKISGSVTSAKPGYHDIITIPTGATNIEVKQRNQRGSRNNGSFLAIKAADGTYILNGDYTLSTLEQDIMYKGVVLRYSGSSAALERIRSFSPLKEPLTIQVLTVGNALRPKIKYTYFVKKKKESFNAIPTFSAWVIEEWGECSKSCELGWQRRLVECRDINGQPASECAKEVKPASTRPCADHPCPQWQLGEWSSCSKTCGKGYKKRSLKCLSHDGGVLSHESCDPLKKPKHFIDFCTMAECS
3D Structural Models
Turn
381..383; 418..420; 457..460
Helix
268..274; 275..277; 278..293; 296..298; 315..317; 325..336; 337..339; 395..406; 415..417; 445..456; 461..464; 478..481; 484..492
Beta Strand
258..266; 302..311; 351..359; 371..373; 385..389; 510..513; 520..523; 538..541; 544..548
3D Structure
X-ray crystallography (4)
Domain & Motif Annotations
Compositional Bias
203..212; Basic and acidic residues; 213..226; Acidic residues
Motif
196..203; Cysteine switch
Domain (CC)
The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.; DOMAIN: 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.
Domain (FT)
258..467; Peptidase M12B; 476..559; Disintegrin; 559..614; TSP type-1 1; 854..905; TSP type-1 2; 908..967; TSP type-1 3
Region
1..27; Disordered; 192..250; Disordered; 725..849; Spacer