TNS2_HUMAN
ID TNS2_HUMAN Reviewed; 1409 AA.
AC Q63HR2; A2VDF2; A2VDF3; A2VDI8; A5PKY4; Q2NL80; Q76MW6; Q7Z5T9; Q8NFF9;
AC Q8NFG0; Q96P25; Q9NT29; Q9UPS7;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Tensin-2;
DE EC=3.1.3.48 {ECO:0000269|PubMed:23401856};
DE AltName: Full=C1 domain-containing phosphatase and tensin homolog;
DE Short=C1-TEN;
DE AltName: Full=Tensin-like C1 domain-containing phosphatase;
GN Name=TNS2; Synonyms=KIAA1075, TENC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), INTERACTION WITH AXL, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=12470648; DOI=10.1016/s0006-291x(02)02718-3;
RA Hafizi S., Alindri F., Karlsson R., Dahlbaeck B.;
RT "Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1
RT domain-containing protein with homology to tensin.";
RL Biochem. Biophys. Res. Commun. 299:793-800(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11792844; DOI=10.1073/pnas.022518699;
RA Chen H., Duncan I.C., Bozorgchami H., Lo S.H.;
RT "Tensin1 and a previously undocumented family member, tensin2, positively
RT regulate cell migration.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:733-738(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 759-1409 (ISOFORM 6).
RC TISSUE=Colon endothelium, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 364-1398 (ISOFORM 2).
RC TISSUE=Brain, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF CYS-231.
RX PubMed=15817639; DOI=10.1096/fj.04-2532fje;
RA Hafizi S., Ibraimi F., Dahlbaeck B.;
RT "C1-TEN is a negative regulator of the Akt/PKB signal transduction pathway
RT and inhibits cell survival, proliferation, and migration.";
RL FASEB J. 19:971-973(2005).
RN [8]
RP INTERACTION WITH SYK, AND SUBCELLULAR LOCATION.
RX PubMed=22019427; DOI=10.1016/j.bbamcr.2011.10.001;
RA Moon K.D., Zhang X., Zhou Q., Geahlen R.L.;
RT "The protein-tyrosine kinase Syk interacts with the C-terminal region of
RT tensin2.";
RL Biochim. Biophys. Acta 1823:199-205(2012).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-835 AND SER-1003,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-231.
RX PubMed=23401856; DOI=10.1128/mcb.01447-12;
RA Koh A., Lee M.N., Yang Y.R., Jeong H., Ghim J., Noh J., Kim J., Ryu D.,
RA Park S., Song P., Koo S.H., Leslie N.R., Berggren P.O., Choi J.H.,
RA Suh P.G., Ryu S.H.;
RT "C1-Ten is a protein tyrosine phosphatase of insulin receptor substrate 1
RT (IRS-1), regulating IRS-1 stability and muscle atrophy.";
RL Mol. Cell. Biol. 33:1608-1620(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91; SER-120; SER-455;
RP TYR-456; SER-466; THR-474; SER-820; SER-825; SER-830; SER-832; SER-845;
RP SER-931; SER-941; SER-972; THR-977; SER-991; SER-1003; THR-1182 AND
RP SER-1247, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP STRUCTURE BY NMR OF 1263-1409.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PTB domain of KIAA1075 protein from human.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Tyrosine-protein phosphatase which regulates cell motility
CC proliferation and muscle-response to insulin (PubMed:15817639,
CC PubMed:23401856). In muscles and under catabolic conditions,
CC dephosphorylates IRS1 leading to its degradation and muscle atrophy
CC (PubMed:23401856). Negatively regulates PI3K-AKT pathway activation
CC (PubMed:15817639, PubMed:23401856). {ECO:0000269|PubMed:15817639,
CC ECO:0000269|PubMed:23401856}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000269|PubMed:23401856};
CC -!- SUBUNIT: Interacts with AXL. Interacts with SYK; leading to its
CC phosphorylation (PubMed:22019427). {ECO:0000269|PubMed:12470648,
CC ECO:0000269|PubMed:22019427}.
CC -!- INTERACTION:
CC Q63HR2; Q9Y4X0-3: AMMECR1; NbExp=3; IntAct=EBI-949753, EBI-12823597;
CC Q63HR2; P29972: AQP1; NbExp=3; IntAct=EBI-949753, EBI-745213;
CC Q63HR2; Q03989: ARID5A; NbExp=3; IntAct=EBI-949753, EBI-948603;
CC Q63HR2; P30049: ATP5F1D; NbExp=3; IntAct=EBI-949753, EBI-1049505;
CC Q63HR2; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-949753, EBI-742750;
CC Q63HR2; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-949753, EBI-2548012;
CC Q63HR2; J3KQ12: BSCL2; NbExp=3; IntAct=EBI-949753, EBI-11532900;
CC Q63HR2; Q6NUJ2: C11orf87; NbExp=3; IntAct=EBI-949753, EBI-6660291;
CC Q63HR2; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-949753, EBI-946029;
CC Q63HR2; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-949753, EBI-7317823;
CC Q63HR2; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-949753, EBI-744545;
CC Q63HR2; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-949753, EBI-741032;
CC Q63HR2; Q8N684-3: CPSF7; NbExp=3; IntAct=EBI-949753, EBI-11523759;
CC Q63HR2; O43186: CRX; NbExp=3; IntAct=EBI-949753, EBI-748171;
CC Q63HR2; Q9UBR2: CTSZ; NbExp=3; IntAct=EBI-949753, EBI-8636823;
CC Q63HR2; Q86YF9: DZIP1; NbExp=3; IntAct=EBI-949753, EBI-998108;
CC Q63HR2; Q86Y13: DZIP3; NbExp=3; IntAct=EBI-949753, EBI-948630;
CC Q63HR2; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-949753, EBI-744099;
CC Q63HR2; Q9UM22: EPDR1; NbExp=3; IntAct=EBI-949753, EBI-946972;
CC Q63HR2; P04626: ERBB2; NbExp=4; IntAct=EBI-949753, EBI-641062;
CC Q63HR2; P21860: ERBB3; NbExp=3; IntAct=EBI-949753, EBI-720706;
CC Q63HR2; Q8N9I5: FADS6; NbExp=3; IntAct=EBI-949753, EBI-3943864;
CC Q63HR2; Q86W67: FAM228A; NbExp=3; IntAct=EBI-949753, EBI-12958227;
CC Q63HR2; P48023: FASLG; NbExp=3; IntAct=EBI-949753, EBI-495538;
CC Q63HR2; P49639: HOXA1; NbExp=3; IntAct=EBI-949753, EBI-740785;
CC Q63HR2; P17482: HOXB9; NbExp=3; IntAct=EBI-949753, EBI-745290;
CC Q63HR2; P31273: HOXC8; NbExp=3; IntAct=EBI-949753, EBI-1752118;
CC Q63HR2; Q9C086: INO80B; NbExp=3; IntAct=EBI-949753, EBI-715611;
CC Q63HR2; Q7L273: KCTD9; NbExp=3; IntAct=EBI-949753, EBI-4397613;
CC Q63HR2; P10721: KIT; NbExp=2; IntAct=EBI-949753, EBI-1379503;
CC Q63HR2; Q5T749: KPRP; NbExp=5; IntAct=EBI-949753, EBI-10981970;
CC Q63HR2; Q01546: KRT76; NbExp=3; IntAct=EBI-949753, EBI-2952745;
CC Q63HR2; Q8IUG1: KRTAP1-3; NbExp=5; IntAct=EBI-949753, EBI-11749135;
CC Q63HR2; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-949753, EBI-10172150;
CC Q63HR2; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-949753, EBI-10172290;
CC Q63HR2; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-949753, EBI-10171774;
CC Q63HR2; Q8IUC1: KRTAP11-1; NbExp=5; IntAct=EBI-949753, EBI-1052037;
CC Q63HR2; P59991: KRTAP12-2; NbExp=6; IntAct=EBI-949753, EBI-10176379;
CC Q63HR2; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-949753, EBI-11953334;
CC Q63HR2; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-949753, EBI-11953846;
CC Q63HR2; Q9BYR3: KRTAP4-4; NbExp=3; IntAct=EBI-949753, EBI-11958132;
CC Q63HR2; Q14847-2: LASP1; NbExp=3; IntAct=EBI-949753, EBI-9088686;
CC Q63HR2; Q8IXW0: LMNTD2; NbExp=3; IntAct=EBI-949753, EBI-12028858;
CC Q63HR2; O60711: LPXN; NbExp=3; IntAct=EBI-949753, EBI-744222;
CC Q63HR2; Q9P127: LUZP4; NbExp=3; IntAct=EBI-949753, EBI-10198848;
CC Q63HR2; P08581: MET; NbExp=2; IntAct=EBI-949753, EBI-1039152;
CC Q63HR2; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-949753, EBI-2858213;
CC Q63HR2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-949753, EBI-22310682;
CC Q63HR2; Q9Y5Y2: NUBP2; NbExp=3; IntAct=EBI-949753, EBI-1048886;
CC Q63HR2; P32242: OTX1; NbExp=5; IntAct=EBI-949753, EBI-740446;
CC Q63HR2; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-949753, EBI-11022007;
CC Q63HR2; O43189: PHF1; NbExp=3; IntAct=EBI-949753, EBI-530034;
CC Q63HR2; Q13526: PIN1; NbExp=3; IntAct=EBI-949753, EBI-714158;
CC Q63HR2; Q13835: PKP1; NbExp=3; IntAct=EBI-949753, EBI-2513407;
CC Q63HR2; Q9NRY6: PLSCR3; NbExp=3; IntAct=EBI-949753, EBI-750734;
CC Q63HR2; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-949753, EBI-744023;
CC Q63HR2; Q9NYW8: RBAK; NbExp=3; IntAct=EBI-949753, EBI-1210429;
CC Q63HR2; Q96HR9: REEP6; NbExp=3; IntAct=EBI-949753, EBI-750345;
CC Q63HR2; Q04864: REL; NbExp=3; IntAct=EBI-949753, EBI-307352;
CC Q63HR2; A0A0S2Z4G9: RNF6; NbExp=3; IntAct=EBI-949753, EBI-16428950;
CC Q63HR2; Q14140: SERTAD2; NbExp=3; IntAct=EBI-949753, EBI-2822051;
CC Q63HR2; Q9NUL5: SHFL; NbExp=4; IntAct=EBI-949753, EBI-10313866;
CC Q63HR2; Q6ZT89-3: SLC25A48; NbExp=3; IntAct=EBI-949753, EBI-12065614;
CC Q63HR2; O14512: SOCS7; NbExp=3; IntAct=EBI-949753, EBI-1539606;
CC Q63HR2; O60504: SORBS3; NbExp=3; IntAct=EBI-949753, EBI-741237;
CC Q63HR2; Q9UGT4: SUSD2; NbExp=3; IntAct=EBI-949753, EBI-1054721;
CC Q63HR2; Q5T7P8-2: SYT6; NbExp=3; IntAct=EBI-949753, EBI-10246152;
CC Q63HR2; Q9BXF9: TEKT3; NbExp=3; IntAct=EBI-949753, EBI-8644516;
CC Q63HR2; Q96M29: TEKT5; NbExp=6; IntAct=EBI-949753, EBI-10239812;
CC Q63HR2; Q96A09: TENT5B; NbExp=3; IntAct=EBI-949753, EBI-752030;
CC Q63HR2; Q7Z6R9: TFAP2D; NbExp=3; IntAct=EBI-949753, EBI-11952651;
CC Q63HR2; Q63HR2: TNS2; NbExp=3; IntAct=EBI-949753, EBI-949753;
CC Q63HR2; Q9BZR9: TRIM8; NbExp=3; IntAct=EBI-949753, EBI-2340370;
CC Q63HR2; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-949753, EBI-11975223;
CC Q63HR2; Q8WYQ9: ZCCHC14; NbExp=3; IntAct=EBI-949753, EBI-3937908;
CC Q63HR2; Q9NZV7: ZIM2; NbExp=3; IntAct=EBI-949753, EBI-11962760;
CC Q63HR2; P52741: ZNF134; NbExp=3; IntAct=EBI-949753, EBI-18054945;
CC Q63HR2; O95201: ZNF205; NbExp=3; IntAct=EBI-949753, EBI-747343;
CC Q63HR2; P15622-3: ZNF250; NbExp=3; IntAct=EBI-949753, EBI-10177272;
CC Q63HR2; Q8TAU3: ZNF417; NbExp=9; IntAct=EBI-949753, EBI-740727;
CC Q63HR2; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-949753, EBI-10486136;
CC Q63HR2; Q86XF7: ZNF575; NbExp=3; IntAct=EBI-949753, EBI-14069183;
CC Q63HR2; Q96SQ5: ZNF587; NbExp=6; IntAct=EBI-949753, EBI-6427977;
CC Q63HR2; Q5T619: ZNF648; NbExp=3; IntAct=EBI-949753, EBI-11985915;
CC Q63HR2; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-949753, EBI-16429014;
CC Q63HR2; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-949753, EBI-11962574;
CC Q63HR2; Q9NWL9; NbExp=3; IntAct=EBI-949753, EBI-10315054;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000269|PubMed:11792844, ECO:0000269|PubMed:22019427}. Cell
CC membrane {ECO:0000269|PubMed:11792844}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11792844}; Cytoplasmic side
CC {ECO:0000269|PubMed:11792844}. Note=Detected at the end of actin stress
CC fibers. Detected in cytoplasmic punctate bodies (PubMed:22019427).
CC {ECO:0000269|PubMed:22019427}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q63HR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q63HR2-2; Sequence=VSP_026460;
CC Name=4;
CC IsoId=Q63HR2-4; Sequence=VSP_026458;
CC Name=5;
CC IsoId=Q63HR2-5; Sequence=VSP_026457;
CC Name=6;
CC IsoId=Q63HR2-6; Sequence=VSP_026461;
CC -!- TISSUE SPECIFICITY: Detected in heart, kidney, brain, thymus, spleen,
CC liver, placenta, lung, skeletal muscle and small intestine.
CC {ECO:0000269|PubMed:11792844, ECO:0000269|PubMed:12470648}.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI29829.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI29830.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI31504.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA83027.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH56176.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF518729; AAM74225.1; -; mRNA.
DR EMBL; AF518728; AAN03866.1; -; mRNA.
DR EMBL; AF417490; AAL14641.1; -; mRNA.
DR EMBL; AB028998; BAA83027.2; ALT_INIT; mRNA.
DR EMBL; AL137564; CAB70815.1; -; mRNA.
DR EMBL; BX647126; CAH56176.1; ALT_SEQ; mRNA.
DR EMBL; BC054099; AAH54099.1; -; mRNA.
DR EMBL; BC110854; AAI10855.1; -; mRNA.
DR EMBL; BC129828; AAI29829.1; ALT_INIT; mRNA.
DR EMBL; BC129829; AAI29830.1; ALT_INIT; mRNA.
DR EMBL; BC131503; AAI31504.1; ALT_INIT; mRNA.
DR EMBL; BC142668; AAI42669.1; -; mRNA.
DR EMBL; BC142712; AAI42713.1; -; mRNA.
DR CCDS; CCDS8842.1; -. [Q63HR2-4]
DR CCDS; CCDS8843.1; -. [Q63HR2-1]
DR CCDS; CCDS8844.1; -. [Q63HR2-5]
DR PIR; T46500; T46500.
DR RefSeq; NP_056134.2; NM_015319.2. [Q63HR2-4]
DR RefSeq; NP_736610.2; NM_170754.2. [Q63HR2-1]
DR RefSeq; NP_938072.1; NM_198316.1. [Q63HR2-5]
DR PDB; 2DKQ; NMR; -; A=1263-1409.
DR PDB; 2KNO; NMR; -; A=1135-1249.
DR PDB; 2L6K; NMR; -; A=1135-1248.
DR PDB; 2LOZ; NMR; -; A=1263-1409.
DR PDB; 3HQC; X-ray; 1.80 A; A=1264-1409.
DR PDBsum; 2DKQ; -.
DR PDBsum; 2KNO; -.
DR PDBsum; 2L6K; -.
DR PDBsum; 2LOZ; -.
DR PDBsum; 3HQC; -.
DR AlphaFoldDB; Q63HR2; -.
DR BMRB; Q63HR2; -.
DR SMR; Q63HR2; -.
DR BioGRID; 116951; 232.
DR IntAct; Q63HR2; 194.
DR MINT; Q63HR2; -.
DR STRING; 9606.ENSP00000319756; -.
DR MoonDB; Q63HR2; Predicted.
DR DEPOD; TNS2; -.
DR GlyConnect; 2083; 1 N-Linked glycan (1 site).
DR GlyGen; Q63HR2; 3 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (2 sites).
DR iPTMnet; Q63HR2; -.
DR PhosphoSitePlus; Q63HR2; -.
DR BioMuta; TNS2; -.
DR DMDM; 150416153; -.
DR EPD; Q63HR2; -.
DR jPOST; Q63HR2; -.
DR MassIVE; Q63HR2; -.
DR MaxQB; Q63HR2; -.
DR PaxDb; Q63HR2; -.
DR PeptideAtlas; Q63HR2; -.
DR PRIDE; Q63HR2; -.
DR ProteomicsDB; 65895; -. [Q63HR2-1]
DR ProteomicsDB; 65896; -. [Q63HR2-2]
DR ProteomicsDB; 65897; -. [Q63HR2-4]
DR ProteomicsDB; 65898; -. [Q63HR2-5]
DR ProteomicsDB; 65899; -. [Q63HR2-6]
DR Antibodypedia; 26823; 87 antibodies from 23 providers.
DR DNASU; 23371; -.
DR Ensembl; ENST00000314250.11; ENSP00000319684.7; ENSG00000111077.18. [Q63HR2-1]
DR Ensembl; ENST00000314276.7; ENSP00000319756.3; ENSG00000111077.18. [Q63HR2-4]
DR Ensembl; ENST00000379902.7; ENSP00000369232.3; ENSG00000111077.18. [Q63HR2-5]
DR Ensembl; ENST00000546602.5; ENSP00000449363.1; ENSG00000111077.18. [Q63HR2-2]
DR Ensembl; ENST00000552570.5; ENSP00000447021.1; ENSG00000111077.18. [Q63HR2-6]
DR GeneID; 23371; -.
DR KEGG; hsa:23371; -.
DR MANE-Select; ENST00000314250.11; ENSP00000319684.7; NM_170754.4; NP_736610.2.
DR UCSC; uc001sbl.4; human. [Q63HR2-1]
DR CTD; 23371; -.
DR DisGeNET; 23371; -.
DR GeneCards; TNS2; -.
DR HGNC; HGNC:19737; TNS2.
DR HPA; ENSG00000111077; Low tissue specificity.
DR MIM; 607717; gene.
DR neXtProt; NX_Q63HR2; -.
DR OpenTargets; ENSG00000111077; -.
DR PharmGKB; PA134976096; -.
DR VEuPathDB; HostDB:ENSG00000111077; -.
DR eggNOG; KOG1930; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000161535; -.
DR HOGENOM; CLU_002189_0_0_1; -.
DR InParanoid; Q63HR2; -.
DR OMA; RCKTATH; -.
DR OrthoDB; 172407at2759; -.
DR PhylomeDB; Q63HR2; -.
DR TreeFam; TF315996; -.
DR PathwayCommons; Q63HR2; -.
DR SignaLink; Q63HR2; -.
DR BioGRID-ORCS; 23371; 28 hits in 1066 CRISPR screens.
DR ChiTaRS; TNS2; human.
DR EvolutionaryTrace; Q63HR2; -.
DR GeneWiki; TENC1; -.
DR GenomeRNAi; 23371; -.
DR Pharos; Q63HR2; Tbio.
DR PRO; PR:Q63HR2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q63HR2; protein.
DR Bgee; ENSG00000111077; Expressed in apex of heart and 186 other tissues.
DR ExpressionAtlas; Q63HR2; baseline and differential.
DR Genevisible; Q63HR2; HS.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0019725; P:cellular homeostasis; IEA:Ensembl.
DR GO; GO:0032963; P:collagen metabolic process; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0048871; P:multicellular organismal homeostasis; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
DR GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
DR CDD; cd00029; C1; 1.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd09927; SH2_Tensin_like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR IDEAL; IID00673; -.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR013625; PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035012; Tensin-like_SH2.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR033929; Tensin_PTB.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Hydrolase; Membrane; Metal-binding; Methylation; Phosphoprotein;
KW Protein phosphatase; Reference proteome; SH2 domain; Zinc; Zinc-finger.
FT CHAIN 1..1409
FT /note="Tensin-2"
FT /id="PRO_0000292987"
FT DOMAIN 122..294
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 299..425
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT DOMAIN 1140..1247
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT ZN_FING 31..79
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..508
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..986
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1034
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1055
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 231
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000305|PubMed:23401856"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGB6"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 456
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 474
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGB6"
FT MOD_RES 483
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGB6"
FT MOD_RES 555
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGB6"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 835
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 910
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGB6"
FT MOD_RES 931
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 972
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 977
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1182
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..124
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11792844,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_026457"
FT VAR_SEQ 1..25
FT /note="MKSSGPVERLLRALGRRDSSRAASR -> MDGGGVCVGRGDLLSSPQALGQL
FT LRKESRPRRAMK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12470648"
FT /id="VSP_026458"
FT VAR_SEQ 776..872
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026460"
FT VAR_SEQ 1273..1274
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_026461"
FT VARIANT 353
FT /note="S -> T (in dbSNP:rs11170389)"
FT /id="VAR_033043"
FT VARIANT 670
FT /note="A -> T (in dbSNP:rs11558984)"
FT /id="VAR_052547"
FT MUTAGEN 231
FT /note="C->S: Loss of tyrosine-protein phosphatase activity.
FT Reduced IRS1 degradation under catabolic conditions.
FT Abolishes inhibition of AKT1 kinase activity."
FT /evidence="ECO:0000269|PubMed:15817639,
FT ECO:0000269|PubMed:23401856"
FT CONFLICT 702
FT /note="A -> V (in Ref. 6; AAH54099)"
FT /evidence="ECO:0000305"
FT CONFLICT 898
FT /note="P -> Q (in Ref. 6; AAH54099)"
FT /evidence="ECO:0000305"
FT CONFLICT 1036
FT /note="P -> L (in Ref. 5; CAB70815)"
FT /evidence="ECO:0000305"
FT CONFLICT 1083
FT /note="G -> E (in Ref. 6; AAI29830)"
FT /evidence="ECO:0000305"
FT CONFLICT 1119
FT /note="P -> S (in Ref. 6; AAH54099)"
FT /evidence="ECO:0000305"
FT CONFLICT 1148
FT /note="D -> G (in Ref. 6; AAH54099)"
FT /evidence="ECO:0000305"
FT CONFLICT 1236
FT /note="P -> L (in Ref. 5; CAH56176)"
FT /evidence="ECO:0000305"
FT CONFLICT 1246
FT /note="P -> L (in Ref. 1; AAM74225/AAN03866, 2; AAL14641
FT and 3; BAA83027)"
FT /evidence="ECO:0000305"
FT HELIX 1137..1140
FT /evidence="ECO:0007829|PDB:2KNO"
FT STRAND 1141..1144
FT /evidence="ECO:0007829|PDB:2L6K"
FT HELIX 1147..1154
FT /evidence="ECO:0007829|PDB:2KNO"
FT STRAND 1161..1166
FT /evidence="ECO:0007829|PDB:2KNO"
FT STRAND 1168..1170
FT /evidence="ECO:0007829|PDB:2KNO"
FT STRAND 1173..1179
FT /evidence="ECO:0007829|PDB:2KNO"
FT STRAND 1184..1189
FT /evidence="ECO:0007829|PDB:2KNO"
FT STRAND 1190..1192
FT /evidence="ECO:0007829|PDB:2L6K"
FT HELIX 1194..1198
FT /evidence="ECO:0007829|PDB:2KNO"
FT STRAND 1199..1205
FT /evidence="ECO:0007829|PDB:2KNO"
FT STRAND 1210..1213
FT /evidence="ECO:0007829|PDB:2L6K"
FT STRAND 1222..1224
FT /evidence="ECO:0007829|PDB:2L6K"
FT HELIX 1225..1230
FT /evidence="ECO:0007829|PDB:2KNO"
FT TURN 1231..1234
FT /evidence="ECO:0007829|PDB:2KNO"
FT STRAND 1237..1241
FT /evidence="ECO:0007829|PDB:2L6K"
FT HELIX 1266..1272
FT /evidence="ECO:0007829|PDB:3HQC"
FT STRAND 1274..1285
FT /evidence="ECO:0007829|PDB:3HQC"
FT HELIX 1291..1304
FT /evidence="ECO:0007829|PDB:3HQC"
FT STRAND 1305..1307
FT /evidence="ECO:0007829|PDB:2DKQ"
FT STRAND 1312..1319
FT /evidence="ECO:0007829|PDB:3HQC"
FT STRAND 1322..1329
FT /evidence="ECO:0007829|PDB:3HQC"
FT STRAND 1332..1339
FT /evidence="ECO:0007829|PDB:3HQC"
FT HELIX 1340..1342
FT /evidence="ECO:0007829|PDB:3HQC"
FT STRAND 1343..1348
FT /evidence="ECO:0007829|PDB:3HQC"
FT STRAND 1350..1352
FT /evidence="ECO:0007829|PDB:2LOZ"
FT STRAND 1354..1356
FT /evidence="ECO:0007829|PDB:3HQC"
FT TURN 1358..1360
FT /evidence="ECO:0007829|PDB:2DKQ"
FT STRAND 1362..1372
FT /evidence="ECO:0007829|PDB:3HQC"
FT STRAND 1375..1385
FT /evidence="ECO:0007829|PDB:3HQC"
FT STRAND 1389..1391
FT /evidence="ECO:0007829|PDB:2DKQ"
FT HELIX 1393..1405
FT /evidence="ECO:0007829|PDB:3HQC"
SQ SEQUENCE 1409 AA; 152580 MW; 67824299A1382140 CRC64;
MKSSGPVERL LRALGRRDSS RAASRPRKAE PHSFREKVFR KKPPVCAVCK VTIDGTGVSC
RVCKVATHRK CEAKVTSACQ ALPPVELRRN TAPVRRIEHL GSTKSLNHSK QRSTLPRSFS
LDPLMERRWD LDLTYVTERI LAAAFPARPD EQRHRGHLRE LAHVLQSKHR DKYLLFNLSE
KRHDLTRLNP KVQDFGWPEL HAPPLDKLCS ICKAMETWLS ADPQHVVVLY CKGNKGKLGV
IVSAYMHYSK ISAGADQALA TLTMRKFCED KVATELQPSQ RRYISYFSGL LSGSIRMNSS
PLFLHYVLIP MLPAFEPGTG FQPFLKIYQS MQLVYTSGVY HIAGPGPQQL CISLEPALLL
KGDVMVTCYH KGGRGTDRTL VFRVQFHTCT IHGPQLTFPK DQLDEAWTDE RFPFQASVEF
VFSSSPEKIK GSTPRNDPSV SVDYNTTEPA VRWDSYENFN QHHEDSVDGS LTHTRGPLDG
SPYAQVQRPP RQTPPAPSPE PPPPPMLSVS SDSGHSSTLT TEPAAESPGR PPPTAAERQE
LDRLLGGCGV ASGGRGAGRE TAILDDEEQP TVGGGPHLGV YPGHRPGLSR HCSCRQGYRE
PCGVPNGGYY RPEGTLERRR LAYGGYEGSP QGYAEASMEK RRLCRSLSEG LYPYPPEMGK
PATGDFGYRA PGYREVVILE DPGLPALYPC PACEEKLALP TAALYGLRLE REAGEGWASE
AGKPLLHPVR PGHPLPLLLP ACGHHHAPMP DYSCLKPPKA GEEGHEGCSY TMCPEGRYGH
PGYPALVTYS YGGAVPSYCP AYGRVPHSCG SPGEGRGYPS PGAHSPRAGS ISPGSPPYPQ
SRKLSYEIPT EEGGDRYPLP GHLASAGPLA SAESLEPVSW REGPSGHSTL PRSPRDAPCS
ASSELSGPST PLHTSSPVQG KESTRRQDTR SPTSAPTQRL SPGEALPPVS QAGTGKAPEL
PSGSGPEPLA PSPVSPTFPP SSPSDWPQER SPGGHSDGAS PRSPVPTTLP GLRHAPWQGP
RGPPDSPDGS PLTPVPSQMP WLVASPEPPQ SSPTPAFPLA ASYDTNGLSQ PPLPEKRHLP
GPGQQPGPWG PEQASSPARG ISHHVTFAPL LSDNVPQTPE PPTQESQSNV KFVQDTSKFW
YKPHLSRDQA IALLKDKDPG AFLIRDSHSF QGAYGLALKV ATPPPSAQPW KGDPVEQLVR
HFLIETGPKG VKIKGCPSEP YFGSLSALVS QHSISPISLP CCLRIPSKDP LEETPEAPVP
TNMSTAADLL RQGAACSVLY LTSVETESLT GPQAVARASS AALSCSPRPT PAVVHFKVSA
QGITLTDNQR KLFFRRHYPV NSITFSSTDP QDRRWTNPDG TTSKIFGFVA KKPGSPWENV
CHLFAELDPD QPAGAIVTFI TKVLLGQRK
