TNS2
entrez
23371
canonical
uniprot
Q63HR2
canonical
ensembl
ENSG00000111077
resolver
ensp
ENSP00000319684
resolver
ensp
ENSP00000319756
resolver
ensp
ENSP00000369232
resolver
genesymbol
TNS2
resolver
genesymbol_syn
KIAA1075
resolver
genesymbol_syn
TENC1
resolver
hgnc
HGNC:19737
resolver
uniprot
A2VDF2
resolver
uniprot
A2VDF3
resolver
uniprot
A2VDI8
resolver
uniprot
A5PKY4
resolver
uniprot
Q2NL80
resolver
uniprot
Q76MW6
resolver
uniprot
Q7Z5T9
resolver
uniprot
Q8NFF9
resolver
uniprot
Q8NFG0
resolver
uniprot
Q96P25
resolver
uniprot
Q9NT29
resolver
uniprot
Q9UPS7
resolver
uniprot_entry
TENS2_HUMAN
resolver
uniprot_sec
A2VDF2
resolver
uniprot_sec
A2VDF3
resolver
uniprot_sec
A2VDI8
resolver
uniprot_sec
A5PKY4
resolver
uniprot_sec
Q2NL80
resolver
uniprot_sec
Q76MW6
resolver
uniprot_sec
Q7Z5T9
resolver
uniprot_sec
Q8NFF9
resolver
uniprot_sec
Q8NFG0
resolver
uniprot_sec
Q96P25
resolver
uniprot_sec
Q9NT29
resolver
uniprot_sec
Q9UPS7
resolver
amino_acid_sequence
MKSSGPVERLLRALGRRDSSRAASRPRKAEPHSFREKVFRKKPPVCAVCKVTIDGTGVSCRVCKVATHRKCEAKVTSACQALPPVELRRNTAPVRRIEHLGSTKSLNHSKQRSTLPRSFSLDPLMERRWDLDLTYVTERILAAAFPARPDEQRHRGHLRELAHVLQSKHRDKYLLFNLSEKRHDLTRLNPKVQDFGWPELHAPPLDKLCSICKAMETWLSADPQHVVVLYCKGNKGKLGVIVSAYMHYSKISAGADQALATLTMRKFCEDKVATELQPSQRRYISYFSGLLSGSIRMNSSPLFLHYVLIPMLPAFEPGTGFQPFLKIYQSMQLVYTSGVYHIAGPGPQQLCISLEPALLLKGDVMVTCYHKGGRGTDRTLVFRVQFHTCTIHGPQLTFPKDQLDEAWTDERFPFQASVEFVFSSSPEKIKGSTPRNDPSVSVDYNTTEPAVRWDSYENFNQHHEDSVDGSLTHTRGPLDGSPYAQVQRPPRQTPPAPSPEPPPPPMLSVSSDSGHSSTLTTEPAAESPGRPPPTAAERQELDRLLGGCGVASGGRGAGRETAILDDEEQPTVGGGPHLGVYPGHRPGLSRHCSCRQGYREPCGVPNGGYYRPEGTLERRRLAYGGYEGSPQGYAEASMEKRRLCRSLSEGLYPYPPEMGKPATGDFGYRAPGYREVVILEDPGLPALYPCPACEEKLALPTAALYGLRLEREAGEGWASEAGKPLLHPVRPGHPLPLLLPACGHHHAPMPDYSCLKPPKAGEEGHEGCSYTMCPEGRYGHPGYPALVTYSYGGAVPSYCPAYGRVPHSCGSPGEGRGYPSPGAHSPRAGSISPGSPPYPQSRKLSYEIPTEEGGDRYPLPGHLASAGPLASAESLEPVSWREGPSGHSTLPRSPRDAPCSASSELSGPSTPLHTSSPVQGKESTRRQDTRSPTSAPTQRLSPGEALPPVSQAGTGKAPELPSGSGPEPLAPSPVSPTFPPSSPSDWPQERSPGGHSDGASPRSPVPTTLPGLRHAPWQGPRGPPDSPDGSPLTPVPSQMPWLVASPEPPQSSPTPAFPLAASYDTNGLSQPPLPEKRHLPGPGQQPGPWGPEQASSPARGISHHVTFAPLLSDNVPQTPEPPTQESQSNVKFVQDTSKFWYKPHLSRDQAIALLKDKDPGAFLIRDSHSFQGAYGLALKVATPPPSAQPWKGDPVEQLVRHFLIETGPKGVKIKGCPSEPYFGSLSALVSQHSISPISLPCCLRIPSKDPLEETPEAPVPTNMSTAADLLRQGAACSVLYLTSVETESLTGPQAVARASSAALSCSPRPTPAVVHFKVSAQGITLTDNQRKLFFRRHYPVNSITFSSTDPQDRRWTNPDGTTSKIFGFVAKKPGSPWENVCHLFAELDPDQPAGAIVTFITKVLLGQRK
uniprot
proteins
ec_number
3.1.3.48
uniprot
proteins
function
FUNCTION: Tyrosine-protein phosphatase which regulates cell motility, proliferation and muscle-response to insulin (PubMed:15817639, PubMed:23401856). Phosphatase activity is mediated by binding to phosphatidylinositol-3,4,5-triphosphate (PtdIns(3,4,5)P3) via the SH2 domain (PubMed:30092354). In muscles and under catabolic conditions, dephosphorylates IRS1 leading to its degradation and muscle atrophy (PubMed:23401856, PubMed:30092354). Negatively regulates PI3K-AKT pathway activation (PubMed:15817639, PubMed:23401856, PubMed:30092354). Dephosphorylates nephrin NPHS1 in podocytes which regulates activity of the mTORC1 complex (PubMed:28955049). Under normal glucose conditions, NPHS1 outcompetes IRS1 for binding to phosphatidylinositol 3-kinase (PI3K) which balances mTORC1 activity but high glucose conditions lead to up-regulation of TNS2, increased NPHS1 dephosphorylation and activation of mTORC1, contributing to podocyte hypertrophy and proteinuria (PubMed:28955049). Required for correct podocyte morphology, podocyte-glomerular basement membrane interaction and integrity of the glomerular filtration barrier (By similarity). Enhances RHOA activation in the presence of DLC1 (PubMed:26427649). Plays a role in promoting DLC1-dependent remodeling of the extracellular matrix (PubMed:20069572). {ECO:0000250|UniProtKB:Q8CGB6, ECO:0000269|PubMed:15817639, ECO:0000269|PubMed:20069572, ECO:0000269|PubMed:23401856, ECO:0000269|PubMed:26427649, ECO:0000269|PubMed:28955049, ECO:0000269|PubMed:30092354}.
uniprot
proteins
mass_dalton
152580
uniprot
proteins
mutagenesis
MUTAGEN 231; /note="C->S: Loss of tyrosine-protein phosphatase activity. Reduced IRS1 degradation under catabolic conditions. Abolishes inhibition of AKT1 kinase activity. Does not affect disruption of SQSTM1-IRS1 interaction by TNS2. Reduced mTORC1 complex activation."; /evidence="ECO:0000269|PubMed:15817639, ECO:0000269|PubMed:23401856, ECO:0000269|PubMed:25101860, ECO:0000269|PubMed:28955049"; MUTAGEN 1142; /note="K->Q: 6-fold reduction in affinity for PtdIns(3,4,5)P3 and reduced IRS1 dephosphorylation but does not affect cell membrane localization or affinity for a tyrosine-phosphorylated peptide; when associated with Q-1155 and Q-1157."; /evidence="ECO:0000269|PubMed:30092354"; MUTAGEN 1155; /note="K->Q: 6-fold reduction in affinity for PtdIns(3,4,5)P3 and reduced IRS1 dephosphorylation but does not affect cell membrane localization or affinity for a tyrosine-phosphorylated peptide; when associated with Q-1142 and Q-1157."; /evidence="ECO:0000269|PubMed:30092354"; MUTAGEN 1157; /note="K->Q: 6-fold reduction in affinity for PtdIns(3,4,5)P3 and reduced IRS1 dephosphorylation but does not affect cell membrane localization or affinity for a tyrosine-phosphorylated peptide; when associated with Q-1142 and Q-1155."; /evidence="ECO:0000269|PubMed:30092354"; MUTAGEN 1165; /note="R->A: Does not affect affinity for PtdIns(3,4,5)P3. Reduced affinity for tyrosine-phosphorylated peptide."; /evidence="ECO:0000269|PubMed:30092354"; MUTAGEN 1209; /note="K->Q: Does not affect affinity for PtdIns(3,4,5)P3; when associated with Q-1212 and Q-1214."; /evidence="ECO:0000269|PubMed:30092354"; MUTAGEN 1212; /note="K->Q: Does not affect affinity for PtdIns(3,4,5)P3; when associated with Q-1209 and Q-1214."; /evidence="ECO:0000269|PubMed:30092354"; MUTAGEN 1214; /note="K->Q: Does not affect affinity for PtdIns(3,4,5)P3; when associated with Q-1209 and Q-1212."; /evidence="ECO:0000269|PubMed:30092354
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated following sequestration in cytoplasmic aggregates with SQSTM1, leading to proteasomal degradation. {ECO:0000269|PubMed:25101860}.
uniprot
proteins
protein_family
PTEN phosphatase protein family
uniprot
proteins
pubmed
10470851
uniprot
proteins
pubmed
11792844
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
12470648
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15817639
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
20069572
uniprot
proteins
pubmed
22019427
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23401856
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25101860
uniprot
proteins
pubmed
26427649
uniprot
proteins
pubmed
28955049
uniprot
proteins
pubmed
29866430
uniprot
proteins
pubmed
30092354
uniprot
proteins
sequence_length
1409
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:11792844, ECO:0000269|PubMed:20069572, ECO:0000269|PubMed:22019427}. Cell membrane {ECO:0000269|PubMed:11792844, ECO:0000269|PubMed:30092354}; Peripheral membrane protein {ECO:0000269|PubMed:11792844}; Cytoplasmic side {ECO:0000269|PubMed:11792844}. Cytoplasm {ECO:0000269|PubMed:22019427, ECO:0000269|PubMed:25101860}. Note=Detected at the end of actin stress fibers. Detected in cytoplasmic punctate bodies (PubMed:22019427, PubMed:25101860). Localizes to both focal adhesions and fibrillar adhesions but is found mainly in focal adhesions (PubMed:20069572). Enriched in dynamic focal adhesions at the leading edge of the cell and is found only rarely in fibrillar adhesions on the ventral surface of cells (PubMed:20069572). {ECO:0000269|PubMed:20069572, ECO:0000269|PubMed:22019427, ECO:0000269|PubMed:25101860}.
uniprot
proteins