Protein detail
PPTC7
Protein phosphatase PTC7 homolog (EC 3.1.3.16) (T-cell activation protein phosphatase 2C) (TA-PP2C) (T-cell activation protein phosphatase 2C-like)
Entry name PPTC7 | UniProt ID | EVMP confidence score 0.40 |
Supporting publications (n) 2 | Transmembrane count | Protein classification EnzymesPredicted intracellular proteins |
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.70High >= 0.60Medium >= 0.40Low >= 0.30Basic Information
Protein Names
Protein phosphatase PTC7 homolog (EC 3.1.3.16) (T-cell activation protein phosphatase 2C) (TA-PP2C) (T-cell activation protein phosphatase 2C-like)
Protein Class (2)
EnzymesPredicted intracellular proteins
Protein Function (3)
- Enzymes
- Predicted intracellular proteins
- ENZYME proteins:Hydrolases
Ensembl
Entrez Gene Symbol
Gene Synonym
TA-PP2C
Gene Description
Protein phosphatase targeting COQ7
Chromosome
12
Position
110533245-110583318
Supporting publications (n)
2
EVMP confidence score
0.40
Fluorescence & Localization
Tissue SpecificepididymisCell SpecificAlveolar cells type 2Single-Nuclei Brain Specificdeep-layer corticothalamic and 6bBlood Cell Specificclassical monocyteBlood Lineage Specificdendritic cells
Function & Pathway
Protein Function (3)
- Enzymes
- Predicted intracellular proteins
- ENZYME proteins:Hydrolases
Cellular Component (2)
Molecular Function (4)
Biological Process (3)
Mediation Categories
Metabolism mediation
Relations & Evidence12
Ligand-Receptor Signaling (4)
4 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | ComPPI | |||||
| intracellular | intracellular | GO_Intercell | |||||
| intracellular | intracellular | UniProt_location | |||||
| intracellular | intracellular | OmniPath |
Protein Complex Composition (7)
7 records.
| Component Name | Component Gene Symbols | Component UniProt ID | Stoichiometry | Database | Database IDs | References |
|---|---|---|---|---|---|---|
| PPTC7SEC14L2SEC14L4TRIB3UBC | O76054P0CG48Q8NI37Q96RU7Q9UDX3 | 1:1:1:1:1 | NetworkBlastCompleat | Compleat:HC5087 | ||
| PPTC7SEC14L2SEC14L4SLC2A8UBC | O76054P0CG48Q8NI37Q9NY64Q9UDX3 | 1:1:1:1:1 | NetworkBlastCompleat | Compleat:HC6073 | ||
| BLVRAPPTC7RRAGBRTN4IP1TRMT2B | P53004Q5VZM2Q8NI37Q8WWV3Q96GJ1 | 0:0:0:0:0 | hu.MAP2 | |||
| FMC1MOCS1OXLD1PPTC7TRMT2B | Q5BKU9Q8NI37Q96GJ1Q96HJ9Q9NZB8 | 0:0:0:0:0 | hu.MAP2 | |||
| PPTC7RTN4IP1 | Q8NI37Q8WWV3 | 0:0 | hu.MAP2 | |||
| FOXRED1PPTC7RTN4IP1 | Q8NI37Q8WWV3Q96CU9 | 0:0:0 | hu.MAP2 | |||
| FOXRED1PPTC7RTN4IP1TRMT2B | Q8NI37Q8WWV3Q96CU9Q96GJ1 | 0:0:0:0 | hu.MAP2 |
Isolation & Detection Technology (1)
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Differential UltracentrifugationUltrafiltration / Tangential Flow FiltrationSize Exclusion ChromatographyMicrofluidics-Based Methods | Mass spectrometry | 34 | 33718342364064913786238139949490315085003468166338225453398737264054596338644352327954143873186825950383268019192688484127723984282428433035349230550287306087003370951034202855273124283097589437686366384909582839651130760538313205914121688440311616400914553045137141315767 |
Sequence, Structure & Domains
Sequences
Length
304
Mass
32,646
Sequence
MFSVLSYGRLVARAVLGGLSQTDPRAGGGGGGDYGLVTAGCGFGKDFRKGLLKKGACYGDDACFVARHRSADVLGVADGVGGWRDYGVDPSQFSGTLMRTCERLVKEGRFVPSNPIGILTTSYCELLQNKVPLLGSSTACIVVLDRTSHRLHTANLGDSGFLVVRGGEVVHRSDEQQHYFNTPFQLSIAPPEAEGVVLSDSPDAADSTSFDVQLGDIILTATDGLFDNMPDYMILQELKKLKNSNYESIQQTARSIAEQAHELAYDPNYMSPFAQFACDNGLNVRGGKPDDITVLLSIVAEYTD
Domain & Motif Annotations
Domain (FT)
69..299; PPM-type phosphatase
Protein Families
PP2C family
Sequence Similarities
Belongs to the PP2C family.
Clinical Relevance
Supporting Publications2
| PMID | Title | Related sentences |
|---|---|---|
| 34265469 | Proteomic Landscape of Exosomes Reveals the Functional Contributions of CD151 in Triple-Negative Breast Cancer. | Furthermore, utilizing quantitative proteomics approach to reveal the proteomes of CD151-deleted exosomes and cells, we found that exosomal CD151 facilitated secretion of ribosomal proteins via exosomes while inhibiting exosome secretion of complement proteins. Moreover, we proved that CD151-deleted exosomes significantly decreased the migration and invasion of TNBC cells. Most importantly, we found that the tetraspanin CD151 expression levels in TNBC-derived serum exosomes were significantly higher than those exosomes from healthy subjects, and we validated our findings with samples from 16 additional donors. This is the first comparative study of the proteomes of TNBC patient-derived and CD151-deleted exosomes. |
| 36573687 | Proteomic and phosphoproteomic landscape of salivary extracellular vesicles to assess OSCC therapeutical outcomes. | No related sentences available |