TNS1
entrez
7145
canonical
uniprot
Q9HBL0
canonical
ensembl
ENSG00000079308
resolver
ensp
ENSP00000171887
resolver
ensp
ENSP00000408724
resolver
ensp
ENSP00000480559
resolver
ensp
ENSP00000493967
resolver
ensp
ENSP00000506917
resolver
enst
ENST00000419504
resolver
enst
ENST00000615025
resolver
enst
ENST00000646520
resolver
genesymbol
TNS1
resolver
genesymbol_syn
TNS
resolver
hgnc
HGNC:11973
resolver
uniprot
A0A087WWW7
resolver
uniprot
A0A2R8Y4T1
resolver
uniprot
A0A804HI61
resolver
uniprot
A1L0S7
resolver
uniprot
B2RU35
resolver
uniprot
B7Z6H8
resolver
uniprot
E9PF55
resolver
uniprot
E9PGF5
resolver
uniprot
Q0VG54
resolver
uniprot
Q0VG55
resolver
uniprot
Q4ZG71
resolver
uniprot
Q59G71
resolver
uniprot
Q6IPI5
resolver
uniprot
Q86VB0
resolver
uniprot_entry
A0A2R8Y4T1_HUMAN
resolver
uniprot_entry
A1L0S7_HUMAN
resolver
uniprot_entry
B2RU35_HUMAN
resolver
uniprot_entry
B7Z6H8_HUMAN
resolver
uniprot_entry
E9PF55_HUMAN
resolver
uniprot_entry
E9PGF5_HUMAN
resolver
uniprot_entry
Q0VG54_HUMAN
resolver
uniprot_entry
Q0VG55_HUMAN
resolver
uniprot_entry
Q59G71_HUMAN
resolver
uniprot_entry
Q86VB0_HUMAN
resolver
uniprot_entry
TENS1_HUMAN
resolver
uniprot_sec
A0A087WWW7
resolver
uniprot_sec
A0A804HI61
resolver
uniprot_sec
Q4ZG71
resolver
uniprot_sec
Q6IPI5
resolver
amino_acid_sequence
MTWICLSCMLWPEDLEAPKTHRFKVKTFKKVKPCGICRQVITQEGCTCKVCSFSCHRKCQAKVAAPCVPPSNHELVPITTENAPKNVVDKGEGASRGGNTRKSLEDNGSTRVTPSVQPHLQPIRNMSVSRTMEDSCELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKICSICKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPVYTSGIYNIPGDSQTSVCITIEPGLLLKGDILLKCYHKKFRSPARDVIFRVQFHTCAIHDLGVVFGKEDLDDAFKDDRFPEYGKVEFVFSYGPEKIQGMEHLENGPSVSVDYNTSDPLIRWDSYDNFSGHRDDGMEEVVGHTQGPLDGSLYAKVKKKDSLHGSTGAVNATRPTLSATPNHVEHTLSVSSDSGNSTASTKTDKTDEPVPGASSATAALSPQEKRELDRLLSGFGLEREKQGAMYHTQHLRSRPAGGSAVPSSGRHVVPAQVHVNGGALASERETDILDDELPNQDGHSAGSMGTLSSLDGVTNTSEGGYPEALSPLTNGLDKSYPMEPMVNGGGYPYESASRAGPAHAGHTAPMRPSYSAQEGLAGYQREGPHPAWPQPVTTSHYAHDPSGMFRSQSFSEAEPQLPPAPVRGGSSREAVQRGLNSWQQQQQQQQQPRPPPRQQERAHLESLVASRPSPQPLAETPIPSLPEFPRAASQQEIEQSIETLNMLMLDLEPASAAAPLHKSQSVPGAWPGASPLSSQPLSGSSRQSHPLTQSRSGYIPSGHSLGTPEPAPRASLESVPPGRSYSPYDYQPCLAGPNQDFHSKSPASSSLPAFLPTTHSPPGPQQPPASLPGLTAQPLLSPKEATSDPSRTPEEEPLNLEGLVAHRVAGVQAREKQPAEPPAPLRRRAASDGQYENQSPEATSPRSPGVRSPVQCVSPELALTIALNPGGRPKEPHLHSYKEAFEEMEGTSPSSPPPSGVRSPPGLAKTPLSALGLKPHNPADILLHPTGEPRSYVESVARTAVAGPRAQDSEPKSFSAPATQAYGHEIPLRNGTLGGSFVSPSPLSTSSPILSADSTSVGSFPSGESSDQGPRTPTQPLLESGFRSGSLGQPSPSAQRNYQSSSPLPTVGSSYSSPDYSLQHFSSSPESQARAQFSVAGVHTVPGSPQARHRTVGTNTPPSPGFGWRAINPSMAAPSSPSLSHHQMMGPPGTGFHGSTVSSPQSSAATTPGSPSLCRHPAGVYQVSGLHNKVATTPGSPSLGRHPGAHQGNLASGLHSNAIASPGSPSLGRHLGGSGSVVPGSPCLDRHVAYGGYSTPEDRRPTLSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEKRRMSVGDRAGSLPNYATINGKVSSPVASGMSSPSGGSTVSFSHTLPDFSKYSMPDNSPETRAKVKFVQDTSKYWYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPPPTIMQQNKKGDMTHELVRHFLIETGPRGVKLKGCPNEPNFGSLSALVYQHSIIPLALPCKLVIPNRDPTDESKDSSGPANSTADLLKQGAACNVLFVNSVDMESLTGPQAISKATSETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFRRHYPLNTVTFCDLDPQERKWMKTEGGAPAKLFGFVARKQGSTTDNACHLFAELDPNQPASAIVNFVSKVMLNAGQKR
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 fibrillar adhesion formation (PubMed:21768292, PubMed:28005397). Essential for myofibroblast differentiation and myofibroblast-mediated extracellular matrix deposition (PubMed:28005397). Enhances RHOA activation in the presence of DLC1 (PubMed:26427649). Plays a role in cell polarization and migration (PubMed:19826001). May be involved in cartilage development and in linking signal transduction pathways to the cytoskeleton (PubMed:21768292). {ECO:0000269|PubMed:19826001, ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:26427649, ECO:0000269|PubMed:28005397, ECO:0000305}.
uniprot
proteins
mass_dalton
197023
uniprot
proteins
mutagenesis
MUTAGEN 369..370; /note="GD->AA: Reduces interaction with DLC1."; /evidence="ECO:0000269|PubMed:26427649"; MUTAGEN 377..378; /note="HK->AA: No effect on interaction with DLC1."; /evidence="ECO:0000269|PubMed:26427649"; MUTAGEN 427; /note="F->A: Abolishes interaction with PPP1CA. Reduces interaction with DLC1. Increases phosphorylation of some Ser/Thr residues. Reduced rate of cell spreading and impaired cell polarization. Reduced phosphorylation of MYL12B."; /evidence="ECO:0000269|PubMed:19826001, ECO:0000269|PubMed:20798394"; MUTAGEN 1592; /note="R->A: Reduces interaction with DLC1 but does not affect interaction with PPP1CA. Impaired cell polarization. Reduced phosphorylation of MYL12B."; /evidence="ECO:0000269|PubMed:19826001, ECO:0000269|PubMed:26427649
uniprot
proteins
post_translational_modification
PTM: Extensively phosphorylated on serine and threonine residues in a p38 MAPK-dependent manner which reduces interaction with DLC1 and increases interaction with tyrosine-phosphorylated proteins including BCAR1/p130cas and PTK2/FAK. The majority of the phosphorylated Ser/Thr residues are immediately adjacent to a proline residue. Also phosphorylated on tyrosine residues. {ECO:0000269|PubMed:20798394}.; PTM: Rapidly cleaved by calpain II. {ECO:0000269|PubMed:11023826}.
uniprot
proteins
protein_family
PTEN phosphatase protein family
uniprot
proteins
pubmed
11023826
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17517630
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19826001
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20069572
uniprot
proteins
pubmed
20798394
uniprot
proteins
pubmed
21768292
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26427649
uniprot
proteins
pubmed
28005397
uniprot
proteins
pubmed
29866430
uniprot
proteins
sequence_length
1839
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:21768292}. Cell junction, focal adhesion {ECO:0000269|PubMed:19826001, ECO:0000269|PubMed:20069572, ECO:0000269|PubMed:21768292}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21768292}. Note=Localizes to both focal adhesions and fibrillar adhesions (PubMed:20069572). Localized at the cell periphery preferentially to fibrillar adhesions rather than to focal adhesions. Translocates from the cell edge to the cell center in an ITGB1BP1-dependent manner (PubMed:21768292). {ECO:0000269|PubMed:20069572, ECO:0000269|PubMed:21768292}.
uniprot
proteins