Tns2
entrez
209039
canonical
uniprot
Q8CGB6
canonical
ensembl
ENSMUSG00000037003
resolver
ensp
ENSMUSP00000041087
resolver
ensp
ENSMUSP00000129146
resolver
ensp
ENSMUSP00000155309
resolver
ensp
ENSMUSP00000155830
resolver
genesymbol
Tns2
resolver
genesymbol_syn
Tenc1
resolver
uniprot
Q3TZ93
resolver
uniprot
Q3UGR8
resolver
uniprot
Q8CJ95
resolver
uniprot
Q8R122
resolver
uniprot_entry
TENS2_MOUSE
resolver
uniprot_sec
Q3TZ93
resolver
uniprot_sec
Q3UGR8
resolver
uniprot_sec
Q8CJ95
resolver
uniprot_sec
Q8R122
resolver
amino_acid_sequence
MKSSGPVERLLRALGRRDSSRATSRPRKAEPHSFREKVFRKKTPVCAVCKVTIDGTGVSCRVCKVATHRKCEAKVTSSCQALPPAELRRSTAPVRRIEHLGSTKSLNHSKQRSTLPRSFSLDPLMERRWDLDLTYVTERILAAAFPARPDEQRHRGHLRELAHVLQSKHRDKYLLFNLSEKRHDLTRLNPKVQDFGWPELHAPPLDKLCSICKAMETWLSADPQHVVVLYCKGSKGKLGVIVSAYMHYSKISAGADQALATLTMRKFCEDKVATELQPSQRRYVSYFSGLLSGSIRMNSSPLFLHYVFVPVLPAFEPNTGFQPFLKIYQSMQLVYTSGVYRIAGPGPQQLCISLEPALLLKGDVMVTCYHKGGQGTDRTLVFRVQFHTCTIHGSRLTFPKDQLDEAWADERFPFQASVEFVFSSSPEKVKGNTPRNDPSVSVDYNTTEPAVRWDSYENFNQHHEDSVDGALAHTRGPLDGSPYAQVQRVPRQTPPAPSPELPPPPMLSVSSDSGHSSTLTTEHTAESPGRPPPTAAERQELDRLLGGCGVASAGRGAGRETAILDDEEQPSVGGGLHLGMYSGHRPGLSRRCSCRQGFREPCGVPNGSYYRPEGTLERRRPPYGGYEGHPQGYAEASVEKRRLCRSLSEGPYPYAPELGKPANGDFGYRPAGYREVVILEDPGVPALCSCPACEEKLALPTAALYGLRLEREAAEGWSSEVGKPLLHPVRPGHPLPLLVPACGHHHAPMPDYGCLKPPKVGEEGHEGCSYAVCSEGRYGHSGYPALVTYGYGGAVPSYCPAYGRAPHSCGSPSEGRGYPSPGAHSPRAGSVSPGSPPYLQPRKLGYEISAEDGRDKYPLSGHLASTGPLASTESPEPSWRDGSSGHSTLPRSPRDPQCSASSELSGPSTPLHTSSPVQGKESNRRQDTTRSPSLAPTQRLSPGEALPSVVQGVAEKTPELLTSSRPEQLDPSPFSQTSAPGSPNGWPQERSPGGHTNSASPRSPVPTTLPGLRHAPWQGPRGTSDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPAFPLATSYDANGPIQPPLPEKRHLPGSGQQPSPPARSTNQHVTFASPLPDVTQPPEHPLQENQSNVKFVQDTSKFWYKPHLSRDQAIALLKDKDPGAFLIRDSHSFQGAYGLALKVATPPPSAQPWKGDPSEQLVRHFLIETGPKGVKIKGCPTEPYFGSLSALVSQHSISPISLPCCLRIPSKDPLEETPEAPVPTNMSTAADLLRQGAACSVLYLTSVETESLTGPQAVAKASSAALSCSPVPVPAIVHFKVSAQGITLTDNQRKLFFRRHYPVNSITFSSTDPQDRRWTNPDGATSKIFGFVAKKPGSPWENVCHLFAELDPDQPASAIVTFITKVLLGQRK
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 (By similarity). Phosphatase activity is mediated by binding to phosphatidylinositol-3,4,5-triphosphate (PtdIns(3,4,5)P3) via the SH2 domain (By similarity). In muscles and under catabolic conditions, dephosphorylates IRS1 leading to its degradation and muscle atrophy. Negatively regulates PI3K-AKT pathway activation (By similarity). Dephosphorylates nephrin NPHS1 in podocytes which affects mTORC1 complex activity (By similarity). 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 (By similarity). Required for correct podocyte morphology, podocyte-glomerular basement membrane interaction and integrity of the glomerular filtration barrier (PubMed:27246398, PubMed:31723089, PubMed:32390516). Enhances RHOA activation in the presence of DLC1 (By similarity). Plays a role in promoting DLC1-dependent remodeling of the extracellular matrix (By similarity). {ECO:0000250|UniProtKB:Q63HR2, ECO:0000269|PubMed:27246398, ECO:0000269|PubMed:31723089, ECO:0000269|PubMed:32390516}.
uniprot
proteins
mass_dalton
152013
uniprot
proteins
mutagenesis
MUTAGEN 231; /note="C->S: No abnormalities in glomerular morphology."; /evidence="ECO:0000269|PubMed:31723089
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated following sequestration in cytoplasmic aggregates with SQSTM1, leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q63HR2}.
uniprot
proteins
protein_family
PTEN phosphatase protein family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23401856
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
27246398
uniprot
proteins
pubmed
28955049
uniprot
proteins
pubmed
31723089
uniprot
proteins
pubmed
32390516
uniprot
proteins
sequence_length
1400
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:31723089}. Cell membrane {ECO:0000250|UniProtKB:Q63HR2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q63HR2}; Cytoplasmic side {ECO:0000250|UniProtKB:Q63HR2}. Cytoplasm {ECO:0000250|UniProtKB:Q63HR2}. Note=Detected at the end of actin stress fibers. Detected in cytoplasmic punctate bodies. Localizes to both focal adhesions and fibrillar adhesions but is found mainly in focal adhesions. 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. {ECO:0000250|UniProtKB:Q63HR2}.
uniprot
proteins