TNS3
entrez
64759
canonical
uniprot
Q68CZ2
canonical
ensembl
ENSG00000136205
resolver
ensp
ENSP00000312143
resolver
ensp
ENSP00000396914
resolver
ensp
ENSP00000414358
resolver
ensp
ENSP00000516118
resolver
ensp
ENSP00000516130
resolver
ensp
ENSP00000557146
resolver
ensp
ENSP00000557147
resolver
ensp
ENSP00000609460
resolver
ensp
ENSP00000609461
resolver
enst
ENST00000450444
resolver
enst
ENST00000457718
resolver
enst
ENST00000705350
resolver
enst
ENST00000705474
resolver
genesymbol
TNS3
resolver
genesymbol_syn
TEM6
resolver
genesymbol_syn
TENS1
resolver
genesymbol_syn
TPP
resolver
hgnc
HGNC:21616
resolver
uniprot
A0A994J537
resolver
uniprot
A0A994J7F3
resolver
uniprot
B2RNV1
resolver
uniprot
C9JHU5
resolver
uniprot
E9PCX8
resolver
uniprot
Q6IPQ2
resolver
uniprot
Q8IZW7
resolver
uniprot
Q8NAD0
resolver
uniprot
Q96PE0
resolver
uniprot
Q96S48
resolver
uniprot_entry
A0A994J537_HUMAN
resolver
uniprot_entry
A0A994J7F3_HUMAN
resolver
uniprot_entry
C9JHU5_HUMAN
resolver
uniprot_entry
E9PCX8_HUMAN
resolver
uniprot_entry
TENS3_HUMAN
resolver
uniprot_sec
B2RNV1
resolver
uniprot_sec
Q6IPQ2
resolver
uniprot_sec
Q8IZW7
resolver
uniprot_sec
Q8NAD0
resolver
uniprot_sec
Q96PE0
resolver
uniprot_sec
Q96S48
resolver
amino_acid_sequence
MEEGHGLDLTYITERIIAVSFPAGCSEESYLHNLQEVTRMLKSKHGDNYLVLNLSEKRYDLTKLNPKIMDVGWPELHAPPLDKMCTICKAQESWLNSNLQHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKKFYDDKVSALMQPSQKRYVQFLSGLLSGSVKMNASPLFLHFVILHGTPNFDTGGVCRPFLKLYQAMQPVYTSGIYNVGPENPSRICIVIEPAQLLKGDVMVKCYHKKYRSATRDVIFRLQFHTGAVQGYGLVFGKEDLDNASKDDRFPDYGKVELVFSATPEKIQGSEHLYNDHGVIVDYNTTDPLIRWDSYENLSADGEVLHTQGPVDGSLYAKVRKKSSSDPGIPGGPQAIPATNSPDHSDHTLSVSSDSGHSTASARTDKTEERLAPGTRRGLSAQEKAELDQLLSGFGLEDPGSSLKEMTDARSKYSGTRHVVPAQVHVNGDAALKDRETDILDDEMPHHDLHSVDSLGTLSSSEGPQSAHLGPFTCHKSSQNSLLSDGFGSNVGEDPQGTLVPDLGLGMDGPYERERTFGSREPKQPQPLLRKPSVSAQMQAYGQSSYSTQTWVRQQQMVVAHQYSFAPDGEARLVSRCPADNPGLVQAQPRVPLTPTRGTSSRVAVQRGVGSGPHPPDTQQPSPSKAFKPRFPGDQVVNGAGPELSTGPSPGSPTLDIDQSIEQLNRLILELDPTFEPIPTHMNALGSQANGSVSPDSVGGGLRASSRLPDTGEGPSRATGRQGSSAEQPLGGRLRKLSLGQYDNDAGGQLPFSKCAWGKAGVDYAPNLPPFPSPADVKETMTPGYPQDLDIIDGRILSSKESMCSTPAFPVSPETPYVKTALRHPPFSPPEPPLSSPASQHKGGREPRSCPETLTHAVGMSESPIGPKSTMLRADASSTPSFQQAFASSCTISSNGPGQRRESSSSAERQWVESSPKPMVSLLGSGRPTGSPLSAEFSGTRKDSPVLSCFPPSELQAPFHSHELSLAEPPDSLAPPSSQAFLGFGTAPVGSGLPPEEDLGALLANSHGASPTPSIPLTATGAADNGFLSHNFLTVAPGHSSHHSPGLQGQGVTLPGQPPLPEKKRASEGDRSLGSVSPSSSGFSSPHSGSTISIPFPNVLPDFSKASEAASPLPDSPGDKLVIVKFVQDTSKFWYKADISREQAIAMLKDKEPGSFIVRDSHSFRGAYGLAMKVATPPPSVLQLNKKAGDLANELVRHFLIECTPKGVRLKGCSNEPYFGSLTALVCQHSITPLALPCKLLIPERDPLEEIAESSPQTAANSAAELLKQGAACNVWYLNSVEMESLTGHQAIQKALSITLVQEPPPVSTVVHFKVSAQGITLTDNQRKLFFRRHYPVNSVIFCALDPQDRKWIKDGPSSKVFGFVARKQGSATDNVCHLFAEHDPEQPASAIVNFVSKVMIGSPKKV
uniprot
proteins
ec_number
3.1.3.-
uniprot
proteins
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). {ECO:0000250|UniProtKB:Q5SSZ5, ECO:0000269|PubMed:17643115, ECO:0000269|PubMed:26166433, ECO:0000269|PubMed:26427649, ECO:0000269|PubMed:31905841, ECO:0000269|PubMed:35687021, ECO:0000305}.
uniprot
proteins
mass_dalton
155266
uniprot
proteins
mutagenesis
MUTAGEN 321; /note="Y->T: Constitutive interaction with p85 and interaction with DLC1 after EGF stimulation."; /evidence="ECO:0000269|PubMed:26166433"; MUTAGEN 323; /note="T->A: Abolishes phosphorylation. Abolishes interaction with DLC1 and p85."; /evidence="ECO:0000269|PubMed:26166433"; MUTAGEN 323; /note="T->E: Constitutive interaction with p85."; /evidence="ECO:0000269|PubMed:26166433"; MUTAGEN 1173; /note="Y->F: Significantly reduced interaction with PEAK1; when associated with F-1206 and F-1256."; /evidence="ECO:0000269|PubMed:35687021"; MUTAGEN 1206; /note="Y->F: Significantly reduced interaction with PEAK1; when associated with F-1173 and F-1256."; /evidence="ECO:0000269|PubMed:35687021"; MUTAGEN 1256; /note="Y->F: Significantly reduced interaction with PEAK1; when associated with F-1173 and F-1206."; /evidence="ECO:0000269|PubMed:35687021
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000269|PubMed:15140944, ECO:0000269|PubMed:26166433, ECO:0000269|PubMed:35687021}.
uniprot
proteins
protein_family
PTEN phosphatase protein family
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
11559528
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15140944
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16461921
uniprot
proteins
pubmed
17643115
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20069572
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24814316
uniprot
proteins
pubmed
26166433
uniprot
proteins
pubmed
26427649
uniprot
proteins
pubmed
29866430
uniprot
proteins
pubmed
31905841
uniprot
proteins
pubmed
35687021
uniprot
proteins
sequence_length
1445
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:15140944, ECO:0000269|PubMed:17643115, ECO:0000269|PubMed:20069572, ECO:0000269|PubMed:35687021}. Cell projection, podosome {ECO:0000250|UniProtKB:Q5SSZ5}. Note=Localizes to both focal and fibrillar adhesions but is mostly found in fibrillar adhesions. {ECO:0000269|PubMed:20069572}.
uniprot
proteins