Q68CZ2 · TENS3_HUMAN
- ProteinTensin-3
- GeneTNS3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1445 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May act as a protein phosphatase and/or a lipid phosphatase (Probable). Involved in the dissociation of the integrin-tensin-actin complex (PubMed:17643115).
EGF activates TNS4 and down-regulates TNS3 which results in capping the tail of ITGB1 (PubMed:17643115).
Increases DOCK5 guanine nucleotide exchange activity towards Rac and plays a role in osteoclast podosome organization (By similarity).
Enhances RHOA activation in the presence of DLC1 (PubMed:26427649).
Required for growth factor-induced epithelial cell migration; growth factor stimulation induces TNS3 phosphorylation which changes its binding preference from DLC1 to the p85 regulatory subunit of the PI3K kinase complex, displacing PI3K inhibitor PTEN and resulting in translocation of the TNS3-p85 complex to the leading edge of migrating cells to promote RAC1 activation (PubMed:26166433).
Meanwhile, PTEN switches binding preference from p85 to DLC1 and the PTEN-DLC1 complex translocates to the posterior of migrating cells to activate RHOA (PubMed:26166433).
Acts as an adapter protein by bridging the association of scaffolding protein PEAK1 with integrins ITGB1, ITGB3 and ITGB5 which contributes to the promotion of cell migration (PubMed:35687021).
Controls tonsil-derived mesenchymal stem cell proliferation and differentiation by regulating the activity of integrin ITGB1 (PubMed:31905841).
EGF activates TNS4 and down-regulates TNS3 which results in capping the tail of ITGB1 (PubMed:17643115).
Increases DOCK5 guanine nucleotide exchange activity towards Rac and plays a role in osteoclast podosome organization (By similarity).
Enhances RHOA activation in the presence of DLC1 (PubMed:26427649).
Required for growth factor-induced epithelial cell migration; growth factor stimulation induces TNS3 phosphorylation which changes its binding preference from DLC1 to the p85 regulatory subunit of the PI3K kinase complex, displacing PI3K inhibitor PTEN and resulting in translocation of the TNS3-p85 complex to the leading edge of migrating cells to promote RAC1 activation (PubMed:26166433).
Meanwhile, PTEN switches binding preference from p85 to DLC1 and the PTEN-DLC1 complex translocates to the posterior of migrating cells to activate RHOA (PubMed:26166433).
Acts as an adapter protein by bridging the association of scaffolding protein PEAK1 with integrins ITGB1, ITGB3 and ITGB5 which contributes to the promotion of cell migration (PubMed:35687021).
Controls tonsil-derived mesenchymal stem cell proliferation and differentiation by regulating the activity of integrin ITGB1 (PubMed:31905841).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell projection | |
Cellular Component | cytosol | |
Cellular Component | focal adhesion | |
Cellular Component | podosome | |
Molecular Function | phosphoprotein phosphatase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTensin-3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ68CZ2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to both focal and fibrillar adhesions but is mostly found in fibrillar adhesions.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 321 | Constitutive interaction with p85 and interaction with DLC1 after EGF stimulation. | ||||
Sequence: Y → T | ||||||
Mutagenesis | 323 | Abolishes phosphorylation. Abolishes interaction with DLC1 and p85. | ||||
Sequence: T → A | ||||||
Mutagenesis | 323 | Constitutive interaction with p85. | ||||
Sequence: T → E | ||||||
Natural variant | VAR_034593 | 600 | in dbSNP:rs2293362 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_034594 | 679 | in dbSNP:rs7808646 | |||
Sequence: G → S | ||||||
Natural variant | VAR_052548 | 1034 | in dbSNP:rs3807590 | |||
Sequence: E → K | ||||||
Mutagenesis | 1173 | Significantly reduced interaction with PEAK1; when associated with F-1206 and F-1256. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 1206 | Significantly reduced interaction with PEAK1; when associated with F-1173 and F-1256. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 1256 | Significantly reduced interaction with PEAK1; when associated with F-1173 and F-1206. | ||||
Sequence: Y → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,651 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000295915 | 1-1445 | UniProt | Tensin-3 | |||
Sequence: MEEGHGLDLTYITERIIAVSFPAGCSEESYLHNLQEVTRMLKSKHGDNYLVLNLSEKRYDLTKLNPKIMDVGWPELHAPPLDKMCTICKAQESWLNSNLQHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKKFYDDKVSALMQPSQKRYVQFLSGLLSGSVKMNASPLFLHFVILHGTPNFDTGGVCRPFLKLYQAMQPVYTSGIYNVGPENPSRICIVIEPAQLLKGDVMVKCYHKKYRSATRDVIFRLQFHTGAVQGYGLVFGKEDLDNASKDDRFPDYGKVELVFSATPEKIQGSEHLYNDHGVIVDYNTTDPLIRWDSYENLSADGEVLHTQGPVDGSLYAKVRKKSSSDPGIPGGPQAIPATNSPDHSDHTLSVSSDSGHSTASARTDKTEERLAPGTRRGLSAQEKAELDQLLSGFGLEDPGSSLKEMTDARSKYSGTRHVVPAQVHVNGDAALKDRETDILDDEMPHHDLHSVDSLGTLSSSEGPQSAHLGPFTCHKSSQNSLLSDGFGSNVGEDPQGTLVPDLGLGMDGPYERERTFGSREPKQPQPLLRKPSVSAQMQAYGQSSYSTQTWVRQQQMVVAHQYSFAPDGEARLVSRCPADNPGLVQAQPRVPLTPTRGTSSRVAVQRGVGSGPHPPDTQQPSPSKAFKPRFPGDQVVNGAGPELSTGPSPGSPTLDIDQSIEQLNRLILELDPTFEPIPTHMNALGSQANGSVSPDSVGGGLRASSRLPDTGEGPSRATGRQGSSAEQPLGGRLRKLSLGQYDNDAGGQLPFSKCAWGKAGVDYAPNLPPFPSPADVKETMTPGYPQDLDIIDGRILSSKESMCSTPAFPVSPETPYVKTALRHPPFSPPEPPLSSPASQHKGGREPRSCPETLTHAVGMSESPIGPKSTMLRADASSTPSFQQAFASSCTISSNGPGQRRESSSSAERQWVESSPKPMVSLLGSGRPTGSPLSAEFSGTRKDSPVLSCFPPSELQAPFHSHELSLAEPPDSLAPPSSQAFLGFGTAPVGSGLPPEEDLGALLANSHGASPTPSIPLTATGAADNGFLSHNFLTVAPGHSSHHSPGLQGQGVTLPGQPPLPEKKRASEGDRSLGSVSPSSSGFSSPHSGSTISIPFPNVLPDFSKASEAASPLPDSPGDKLVIVKFVQDTSKFWYKADISREQAIAMLKDKEPGSFIVRDSHSFRGAYGLAMKVATPPPSVLQLNKKAGDLANELVRHFLIECTPKGVRLKGCSNEPYFGSLTALVCQHSITPLALPCKLLIPERDPLEEIAESSPQTAANSAAELLKQGAACNVWYLNSVEMESLTGHQAIQKALSITLVQEPPPVSTVVHFKVSAQGITLTDNQRKLFFRRHYPVNSVIFCALDPQDRKWIKDGPSSKVFGFVARKQGSATDNVCHLFAEHDPEQPASAIVNFVSKVMIGSPKKV | |||||||
Modified residue (large scale data) | 321 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 323 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 332 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 332 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 333 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 337 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 352 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 354 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 361 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 379 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 440 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 440 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 516 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 549 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 571 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 571 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 584 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 601 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 632 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 632 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 637 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 649 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 649 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 660 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 660 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 662 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 687 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 687 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 690 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 690 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 692 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 698 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 732 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 735 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 735 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 762 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 776 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 776 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 780 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 780 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 802 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 811 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 811 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 820 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 823 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 840 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 844 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 850 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 853 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 855 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 866 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 866 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 873 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 874 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 877 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 887 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 899 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 901 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 901 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 941 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 944 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 952 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 953 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 963 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 967 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 969 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 972 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 976 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1105 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1115 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1117 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1145 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1149 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1149 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1154 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1154 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1199 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1201 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1214 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1256 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1293 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1293 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1441 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on Ser/Thr and Tyr residues (PubMed:26166433).
Phosphorylated on Thr-323 in the C2-type tensin domain following EGF stimulation which changes its binding preference from DLC1 to the p85 regulatory subunit of the PI3K kinase complex (PubMed:26166433).
EGF induces tyrosine phosphorylation in a time- and dose-dependent manner (PubMed:15140944).
Phosphorylation of the SH2 domain enhances interaction with PEAK1 (PubMed:35687021).
Phosphorylated on Thr-323 in the C2-type tensin domain following EGF stimulation which changes its binding preference from DLC1 to the p85 regulatory subunit of the PI3K kinase complex (PubMed:26166433).
EGF induces tyrosine phosphorylation in a time- and dose-dependent manner (PubMed:15140944).
Phosphorylation of the SH2 domain enhances interaction with PEAK1 (PubMed:35687021).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in umbilical vein endothelial cells, epithelial cells, and fibroblasts cells (at protein level). Highly expressed in thyroid, kidney and placenta. Low expression in heart, skeletal muscle, spleen, liver, and lung. Expressed at higher levels in tonsil-derived mesenchymal stem cells (MSCs) than in adipose tissue-derived MSCs or bone marrow-derived MSCs (PubMed:31905841).
Expressed in tumor endothelial cells. Expression seems to be down-regulated in thyroid tumor tissues and in anaplastic carcinomas
Expressed in tumor endothelial cells. Expression seems to be down-regulated in thyroid tumor tissues and in anaplastic carcinomas
Induction
Down-regulated by EGF.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with EGFR; EGF promotes the interaction with EGFR (PubMed:15140944).
Interacts with PTK2/FAK1 and BCAR1 (PubMed:15140944).
Tyrosine phosphorylation is critical for these interactions (PubMed:15140944).
Interacts with Rho GTPase-activating protein DLC1 and with the regulatory p85 subunit of the PI3K kinase complex; in resting cells, interacts (via C2 tensin-type domain) with DLC1 but, following growth factor stimulation, TNS3 is phosphorylated which leads to weakened interaction with DLC1 and enhanced interaction (via C2 tensin-type domain) with p85 while DLC1 interaction with PTEN increases (PubMed:26166433).
Interacts (when phosphorylated on the SH2 domain) with integrins ITGB1, ITGB3 and ITGB5 and with scaffolding protein PEAK1 (phosphorylated on 'Tyr-635'); mediates the association of PEAK1 with ITGB1, ITGB3 and ITGB5 (PubMed:35687021).
Interacts (via N-terminus) with DOCK5 (via N-terminus); the interaction increases DOCK5 guanine nucleotide exchange activity towards Rac (By similarity).
Interacts with receptor tyrosine kinase MET (PubMed:24814316).
Interacts with PTK2/FAK1 and BCAR1 (PubMed:15140944).
Tyrosine phosphorylation is critical for these interactions (PubMed:15140944).
Interacts with Rho GTPase-activating protein DLC1 and with the regulatory p85 subunit of the PI3K kinase complex; in resting cells, interacts (via C2 tensin-type domain) with DLC1 but, following growth factor stimulation, TNS3 is phosphorylated which leads to weakened interaction with DLC1 and enhanced interaction (via C2 tensin-type domain) with p85 while DLC1 interaction with PTEN increases (PubMed:26166433).
Interacts (when phosphorylated on the SH2 domain) with integrins ITGB1, ITGB3 and ITGB5 and with scaffolding protein PEAK1 (phosphorylated on 'Tyr-635'); mediates the association of PEAK1 with ITGB1, ITGB3 and ITGB5 (PubMed:35687021).
Interacts (via N-terminus) with DOCK5 (via N-terminus); the interaction increases DOCK5 guanine nucleotide exchange activity towards Rac (By similarity).
Interacts with receptor tyrosine kinase MET (PubMed:24814316).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q68CZ2 | BCAR1 P56945 | 8 | EBI-1220488, EBI-702093 | |
BINARY | Q68CZ2 | CDH1 P12830 | 2 | EBI-1220488, EBI-727477 | |
BINARY | Q68CZ2 | EGFR P00533 | 5 | EBI-1220488, EBI-297353 | |
BINARY | Q68CZ2 | ERBB2 P04626 | 2 | EBI-1220488, EBI-641062 | |
BINARY | Q68CZ2 | ERBB3 P21860 | 2 | EBI-1220488, EBI-720706 | |
BINARY | Q68CZ2 | KIT P10721 | 5 | EBI-1220488, EBI-1379503 | |
BINARY | Q68CZ2 | MET P08581 | 3 | EBI-1220488, EBI-1039152 | |
BINARY | Q68CZ2 | PTK2 Q05397 | 3 | EBI-1220488, EBI-702142 | |
BINARY | Q68CZ2 | SRC P12931 | 13 | EBI-1220488, EBI-621482 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-170 | Phosphatase tensin-type | ||||
Sequence: MEEGHGLDLTYITERIIAVSFPAGCSEESYLHNLQEVTRMLKSKHGDNYLVLNLSEKRYDLTKLNPKIMDVGWPELHAPPLDKMCTICKAQESWLNSNLQHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKKFYDDKVSALMQPSQKRYVQFLSGLLSGS | ||||||
Domain | 175-301 | C2 tensin-type | ||||
Sequence: ASPLFLHFVILHGTPNFDTGGVCRPFLKLYQAMQPVYTSGIYNVGPENPSRICIVIEPAQLLKGDVMVKCYHKKYRSATRDVIFRLQFHTGAVQGYGLVFGKEDLDNASKDDRFPDYGKVELVFSAT | ||||||
Region | 358-421 | Disordered | ||||
Sequence: RKKSSSDPGIPGGPQAIPATNSPDHSDHTLSVSSDSGHSTASARTDKTEERLAPGTRRGLSAQE | ||||||
Compositional bias | 376-398 | Polar residues | ||||
Sequence: ATNSPDHSDHTLSVSSDSGHSTA | ||||||
Region | 538-568 | Disordered | ||||
Sequence: VPDLGLGMDGPYERERTFGSREPKQPQPLLR | ||||||
Region | 618-695 | Disordered | ||||
Sequence: DNPGLVQAQPRVPLTPTRGTSSRVAVQRGVGSGPHPPDTQQPSPSKAFKPRFPGDQVVNGAGPELSTGPSPGSPTLDI | ||||||
Compositional bias | 630-644 | Polar residues | ||||
Sequence: PLTPTRGTSSRVAVQ | ||||||
Region | 717-769 | Disordered | ||||
Sequence: PTHMNALGSQANGSVSPDSVGGGLRASSRLPDTGEGPSRATGRQGSSAEQPLG | ||||||
Compositional bias | 719-733 | Polar residues | ||||
Sequence: HMNALGSQANGSVSP | ||||||
Region | 859-981 | Disordered | ||||
Sequence: ALRHPPFSPPEPPLSSPASQHKGGREPRSCPETLTHAVGMSESPIGPKSTMLRADASSTPSFQQAFASSCTISSNGPGQRRESSSSAERQWVESSPKPMVSLLGSGRPTGSPLSAEFSGTRKD | ||||||
Compositional bias | 910-950 | Polar residues | ||||
Sequence: LRADASSTPSFQQAFASSCTISSNGPGQRRESSSSAERQWV | ||||||
Region | 1076-1127 | Disordered | ||||
Sequence: GHSSHHSPGLQGQGVTLPGQPPLPEKKRASEGDRSLGSVSPSSSGFSSPHSG | ||||||
Compositional bias | 1110-1127 | Polar residues | ||||
Sequence: SLGSVSPSSSGFSSPHSG | ||||||
Domain | 1172-1282 | SH2 | ||||
Sequence: WYKADISREQAIAMLKDKEPGSFIVRDSHSFRGAYGLAMKVATPPPSVLQLNKKAGDLANELVRHFLIECTPKGVRLKGCSNEPYFGSLTALVCQHSITPLALPCKLLIPE | ||||||
Domain | 1310-1444 | PTB | ||||
Sequence: ACNVWYLNSVEMESLTGHQAIQKALSITLVQEPPPVSTVVHFKVSAQGITLTDNQRKLFFRRHYPVNSVIFCALDPQDRKWIKDGPSSKVFGFVARKQGSATDNVCHLFAEHDPEQPASAIVNFVSKVMIGSPKK |
Sequence similarities
Belongs to the PTEN phosphatase protein family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q68CZ2-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,445
- Mass (Da)155,266
- Last updated2007-07-24 v2
- Checksum40B02C6269899320
Q68CZ2-2
- Name2
- Differences from canonical
- 241-480: Missing
Q68CZ2-3
- Name3
Q68CZ2-4
- Name4
Computationally mapped potential isoform sequences
There are 10 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9JWN9 | C9JWN9_HUMAN | TNS3 | 108 | ||
C9JTD0 | C9JTD0_HUMAN | TNS3 | 138 | ||
C9JUW5 | C9JUW5_HUMAN | TNS3 | 114 | ||
C9JHU5 | C9JHU5_HUMAN | TNS3 | 1534 | ||
H7BZ64 | H7BZ64_HUMAN | TNS3 | 21 | ||
E9PCX8 | E9PCX8_HUMAN | TNS3 | 1548 | ||
A0A994J7T8 | A0A994J7T8_HUMAN | TNS3 | 501 | ||
A0A994J7F3 | A0A994J7F3_HUMAN | TNS3 | 1002 | ||
A0A994J4W0 | A0A994J4W0_HUMAN | TNS3 | 548 | ||
A0A994J537 | A0A994J537_HUMAN | TNS3 | 1559 |
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 31 | in Ref. 2; AAN32667 | ||||
Sequence: L → P | ||||||
Alternative sequence | VSP_027123 | 241-480 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_027124 | 243-250 | in isoform 4 | |||
Sequence: KCYHKKYR → MNYNIANI | ||||||
Alternative sequence | VSP_027125 | 251-1445 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 376-398 | Polar residues | ||||
Sequence: ATNSPDHSDHTLSVSSDSGHSTA | ||||||
Alternative sequence | VSP_027126 | 381-391 | in isoform 3 | |||
Sequence: DHSDHTLSVSS → ANVLFELIGQV | ||||||
Alternative sequence | VSP_027127 | 392-1445 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 458 | in Ref. 4; CAH18438 | ||||
Sequence: V → A | ||||||
Sequence conflict | 505 | in Ref. 2; AAN32667 | ||||
Sequence: A → V | ||||||
Compositional bias | 630-644 | Polar residues | ||||
Sequence: PLTPTRGTSSRVAVQ | ||||||
Compositional bias | 719-733 | Polar residues | ||||
Sequence: HMNALGSQANGSVSP | ||||||
Compositional bias | 910-950 | Polar residues | ||||
Sequence: LRADASSTPSFQQAFASSCTISSNGPGQRRESSSSAERQWV | ||||||
Sequence conflict | 917 | in Ref. 4; CAH18438 | ||||
Sequence: T → A | ||||||
Sequence conflict | 1047 | in Ref. 4; CAH18438 | ||||
Sequence: A → T | ||||||
Compositional bias | 1110-1127 | Polar residues | ||||
Sequence: SLGSVSPSSSGFSSPHSG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF378756 EMBL· GenBank· DDBJ | AAL11993.1 EMBL· GenBank· DDBJ | mRNA | ||
AF417489 EMBL· GenBank· DDBJ | AAN32667.1 EMBL· GenBank· DDBJ | mRNA | ||
AK092864 EMBL· GenBank· DDBJ | BAC03993.1 EMBL· GenBank· DDBJ | mRNA | ||
CR749644 EMBL· GenBank· DDBJ | CAH18438.1 EMBL· GenBank· DDBJ | mRNA | ||
AC073341 EMBL· GenBank· DDBJ | AAQ96841.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471128 EMBL· GenBank· DDBJ | EAW61011.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC071791 EMBL· GenBank· DDBJ | AAH71791.1 EMBL· GenBank· DDBJ | mRNA | ||
BC137133 EMBL· GenBank· DDBJ | AAI37134.1 EMBL· GenBank· DDBJ | mRNA | ||
BC137134 EMBL· GenBank· DDBJ | AAI37135.1 EMBL· GenBank· DDBJ | mRNA | ||
AB062750 EMBL· GenBank· DDBJ | BAB60681.1 EMBL· GenBank· DDBJ | mRNA |