TENS3_HUMAN
ID TENS3_HUMAN Reviewed; 1445 AA.
AC Q68CZ2; B2RNV1; Q6IPQ2; Q8IZW7; Q8NAD0; Q96PE0; Q96S48;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Tensin-3;
DE AltName: Full=Tensin-like SH2 domain-containing protein 1;
DE AltName: Full=Tumor endothelial marker 6;
GN Name=TNS3; Synonyms=TEM6, TENS1, TPP;
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] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=11559528;
RA Carson-Walter E.B., Watkins D.N., Nanda A., Vogelstein B., Kinzler K.W.,
RA St Croix B.;
RT "Cell surface tumor endothelial markers are conserved in mice and humans.";
RL Cancer Res. 61:6649-6655(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, AND INTERACTION WITH EGFR; PTK2/FAK1 AND BCAR1.
RX PubMed=15140944;
RA Cui Y., Liao Y.-C., Lo S.H.;
RT "Epidermal growth factor modulates tyrosine phosphorylation of a novel
RT tensin family member, tensin3.";
RL Mol. Cancer Res. 2:225-232(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain, and Kidney;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 749-1445, AND TISSUE SPECIFICITY.
RX PubMed=16461921; DOI=10.1677/jme.1.01913;
RA Maeda I., Takano T., Yoshida H., Matsuzuka F., Amino N., Miyauchi A.;
RT "Tensin3 is a novel thyroid-specific gene.";
RL J. Mol. Endocrinol. 36:R1-R8(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND KNOCKDOWN IN MCF10A CELLS.
RX PubMed=17643115; DOI=10.1038/ncb1622;
RA Katz M., Amit I., Citri A., Shay T., Carvalho S., Lavi S., Milanezi F.,
RA Lyass L., Amariglio N., Jacob-Hirsch J., Ben-Chetrit N., Tarcic G.,
RA Lindzen M., Avraham R., Liao Y.C., Trusk P., Lyass A., Rechavi G.,
RA Spector N.L., Lo S.H., Schmitt F., Bacus S.S., Yarden Y.;
RT "A reciprocal tensin-3-cten switch mediates EGF-driven mammary cell
RT migration.";
RL Nat. Cell Biol. 9:961-969(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; THR-632; SER-660;
RP SER-776; SER-866; SER-901; SER-1149; SER-1154 AND SER-1293, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; SER-660; SER-735;
RP SER-776; TYR-780; SER-811; SER-1149 AND SER-1154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660; SER-776; SER-1149 AND
RP SER-1441, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361; SER-440; SER-516;
RP SER-776; SER-811; SER-901; SER-1149 AND SER-1154, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: May play a role in actin remodeling. Involved in the
CC dissociation of the integrin-tensin-actin complex. EGF activates TNS4
CC and down-regulates TNS3 which results in capping the tail of ITGB1.
CC Seems to be involved in mammary cell migration. May be involved in cell
CC migration and bone development (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:17643115}.
CC -!- SUBUNIT: EGF promotes the interaction with EGFR. Interacts with
CC PTK2/FAK1 and BCAR1. Tyrosine phosphorylation is critical for these
CC interactions. {ECO:0000269|PubMed:15140944}.
CC -!- INTERACTION:
CC Q68CZ2; P56945: BCAR1; NbExp=8; IntAct=EBI-1220488, EBI-702093;
CC Q68CZ2; P12830: CDH1; NbExp=2; IntAct=EBI-1220488, EBI-727477;
CC Q68CZ2; P00533: EGFR; NbExp=5; IntAct=EBI-1220488, EBI-297353;
CC Q68CZ2; P04626: ERBB2; NbExp=2; IntAct=EBI-1220488, EBI-641062;
CC Q68CZ2; P21860: ERBB3; NbExp=2; IntAct=EBI-1220488, EBI-720706;
CC Q68CZ2; P10721: KIT; NbExp=5; IntAct=EBI-1220488, EBI-1379503;
CC Q68CZ2; P08581: MET; NbExp=3; IntAct=EBI-1220488, EBI-1039152;
CC Q68CZ2; Q05397: PTK2; NbExp=3; IntAct=EBI-1220488, EBI-702142;
CC Q68CZ2; P12931: SRC; NbExp=13; IntAct=EBI-1220488, EBI-621482;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000269|PubMed:15140944, ECO:0000269|PubMed:17643115}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q68CZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68CZ2-2; Sequence=VSP_027123;
CC Name=3;
CC IsoId=Q68CZ2-3; Sequence=VSP_027126, VSP_027127;
CC Name=4;
CC IsoId=Q68CZ2-4; Sequence=VSP_027124, VSP_027125;
CC -!- TISSUE SPECIFICITY: Expressed in umbilical vein endothelial cells,
CC epithelial cells, and fibroblasts cells (at protein level). Highly
CC expressed in thyroid, kidney and placenta. Low expression in heart,
CC skeletal muscle, spleen, liver, and lung. Expressed in tumor
CC endothelial cells. Expression seems to be down-regulated in thyroid
CC tumor tissues and in anaplastic carcinomas.
CC {ECO:0000269|PubMed:11559528, ECO:0000269|PubMed:15140944,
CC ECO:0000269|PubMed:16461921}.
CC -!- INDUCTION: Down-regulated by EGF. {ECO:0000269|PubMed:15140944,
CC ECO:0000269|PubMed:17643115}.
CC -!- PTM: EGF/epidermal growth factor induces tyrosine phosphorylation in a
CC time- and dose-dependent manner.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000305}.
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DR EMBL; AF378756; AAL11993.1; -; mRNA.
DR EMBL; AF417489; AAN32667.1; -; mRNA.
DR EMBL; AK092864; BAC03993.1; -; mRNA.
DR EMBL; CR749644; CAH18438.1; -; mRNA.
DR EMBL; AC073341; AAQ96841.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61011.1; -; Genomic_DNA.
DR EMBL; BC071791; AAH71791.1; -; mRNA.
DR EMBL; BC137133; AAI37134.1; -; mRNA.
DR EMBL; BC137134; AAI37135.1; -; mRNA.
DR EMBL; AB062750; BAB60681.1; -; mRNA.
DR CCDS; CCDS5506.2; -. [Q68CZ2-1]
DR RefSeq; NP_073585.8; NM_022748.11. [Q68CZ2-1]
DR RefSeq; XP_011513782.1; XM_011515480.2. [Q68CZ2-1]
DR RefSeq; XP_011513783.1; XM_011515481.2. [Q68CZ2-1]
DR RefSeq; XP_011513784.1; XM_011515482.2.
DR RefSeq; XP_011513785.1; XM_011515483.2. [Q68CZ2-1]
DR RefSeq; XP_016868028.1; XM_017012539.1.
DR AlphaFoldDB; Q68CZ2; -.
DR SMR; Q68CZ2; -.
DR BioGRID; 122272; 61.
DR IntAct; Q68CZ2; 140.
DR MINT; Q68CZ2; -.
DR STRING; 9606.ENSP00000312143; -.
DR ChEMBL; CHEMBL4295861; -.
DR DEPOD; TNS3; -.
DR GlyGen; Q68CZ2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q68CZ2; -.
DR MetOSite; Q68CZ2; -.
DR PhosphoSitePlus; Q68CZ2; -.
DR BioMuta; TNS3; -.
DR DMDM; 156637424; -.
DR EPD; Q68CZ2; -.
DR jPOST; Q68CZ2; -.
DR MassIVE; Q68CZ2; -.
DR MaxQB; Q68CZ2; -.
DR PaxDb; Q68CZ2; -.
DR PeptideAtlas; Q68CZ2; -.
DR PRIDE; Q68CZ2; -.
DR ProteomicsDB; 66036; -. [Q68CZ2-1]
DR ProteomicsDB; 66037; -. [Q68CZ2-2]
DR ProteomicsDB; 66038; -. [Q68CZ2-3]
DR ProteomicsDB; 66039; -. [Q68CZ2-4]
DR Antibodypedia; 1019; 146 antibodies from 26 providers.
DR DNASU; 64759; -.
DR Ensembl; ENST00000311160.14; ENSP00000312143.9; ENSG00000136205.17. [Q68CZ2-1]
DR Ensembl; ENST00000442536.6; ENSP00000389285.2; ENSG00000136205.17. [Q68CZ2-4]
DR Ensembl; ENST00000458317.6; ENSP00000388318.2; ENSG00000136205.17. [Q68CZ2-4]
DR GeneID; 64759; -.
DR KEGG; hsa:64759; -.
DR MANE-Select; ENST00000311160.14; ENSP00000312143.9; NM_022748.12; NP_073585.8.
DR UCSC; uc003tnw.3; human. [Q68CZ2-1]
DR CTD; 64759; -.
DR DisGeNET; 64759; -.
DR GeneCards; TNS3; -.
DR HGNC; HGNC:21616; TNS3.
DR HPA; ENSG00000136205; Low tissue specificity.
DR MIM; 606825; gene.
DR neXtProt; NX_Q68CZ2; -.
DR OpenTargets; ENSG00000136205; -.
DR PharmGKB; PA134888115; -.
DR VEuPathDB; HostDB:ENSG00000136205; -.
DR eggNOG; KOG1930; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000156328; -.
DR HOGENOM; CLU_002189_1_0_1; -.
DR InParanoid; Q68CZ2; -.
DR OMA; STHTWVC; -.
DR OrthoDB; 172407at2759; -.
DR PhylomeDB; Q68CZ2; -.
DR TreeFam; TF315996; -.
DR PathwayCommons; Q68CZ2; -.
DR Reactome; R-HSA-8875513; MET interacts with TNS proteins.
DR SignaLink; Q68CZ2; -.
DR SIGNOR; Q68CZ2; -.
DR BioGRID-ORCS; 64759; 81 hits in 1077 CRISPR screens.
DR ChiTaRS; TNS3; human.
DR GenomeRNAi; 64759; -.
DR Pharos; Q68CZ2; Tbio.
DR PRO; PR:Q68CZ2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q68CZ2; protein.
DR Bgee; ENSG00000136205; Expressed in renal glomerulus and 202 other tissues.
DR ExpressionAtlas; Q68CZ2; baseline and differential.
DR Genevisible; Q68CZ2; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
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 InterPro; IPR035892; C2_domain_sf.
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 InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Phosphoprotein; Reference proteome;
KW SH2 domain.
FT CHAIN 1..1445
FT /note="Tensin-3"
FT /id="PRO_0000295915"
FT DOMAIN 1..170
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 175..301
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT DOMAIN 1172..1282
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 358..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSZ5"
FT MOD_RES 632
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSZ5"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSZ5"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 780
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 811
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 1293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 241..480
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11559528"
FT /id="VSP_027123"
FT VAR_SEQ 243..250
FT /note="KCYHKKYR -> MNYNIANI (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027124"
FT VAR_SEQ 251..1445
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027125"
FT VAR_SEQ 381..391
FT /note="DHSDHTLSVSS -> ANVLFELIGQV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027126"
FT VAR_SEQ 392..1445
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027127"
FT VARIANT 600
FT /note="Q -> H (in dbSNP:rs2293362)"
FT /id="VAR_034593"
FT VARIANT 679
FT /note="G -> S (in dbSNP:rs7808646)"
FT /id="VAR_034594"
FT VARIANT 1034
FT /note="E -> K (in dbSNP:rs3807590)"
FT /id="VAR_052548"
FT CONFLICT 31
FT /note="L -> P (in Ref. 2; AAN32667)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="V -> A (in Ref. 4; CAH18438)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="A -> V (in Ref. 2; AAN32667)"
FT /evidence="ECO:0000305"
FT CONFLICT 917
FT /note="T -> A (in Ref. 4; CAH18438)"
FT /evidence="ECO:0000305"
FT CONFLICT 1047
FT /note="A -> T (in Ref. 4; CAH18438)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1445 AA; 155266 MW; 40B02C6269899320 CRC64;
MEEGHGLDLT YITERIIAVS FPAGCSEESY LHNLQEVTRM LKSKHGDNYL VLNLSEKRYD
LTKLNPKIMD VGWPELHAPP LDKMCTICKA QESWLNSNLQ HVVVIHCRGG KGRIGVVISS
YMHFTNVSAS ADQALDRFAM KKFYDDKVSA LMQPSQKRYV QFLSGLLSGS VKMNASPLFL
HFVILHGTPN FDTGGVCRPF LKLYQAMQPV YTSGIYNVGP ENPSRICIVI EPAQLLKGDV
MVKCYHKKYR SATRDVIFRL QFHTGAVQGY GLVFGKEDLD NASKDDRFPD YGKVELVFSA
TPEKIQGSEH LYNDHGVIVD YNTTDPLIRW DSYENLSADG EVLHTQGPVD GSLYAKVRKK
SSSDPGIPGG PQAIPATNSP DHSDHTLSVS SDSGHSTASA RTDKTEERLA PGTRRGLSAQ
EKAELDQLLS GFGLEDPGSS LKEMTDARSK YSGTRHVVPA QVHVNGDAAL KDRETDILDD
EMPHHDLHSV DSLGTLSSSE GPQSAHLGPF TCHKSSQNSL LSDGFGSNVG EDPQGTLVPD
LGLGMDGPYE RERTFGSREP KQPQPLLRKP SVSAQMQAYG QSSYSTQTWV RQQQMVVAHQ
YSFAPDGEAR LVSRCPADNP GLVQAQPRVP LTPTRGTSSR VAVQRGVGSG PHPPDTQQPS
PSKAFKPRFP GDQVVNGAGP ELSTGPSPGS PTLDIDQSIE QLNRLILELD PTFEPIPTHM
NALGSQANGS VSPDSVGGGL RASSRLPDTG EGPSRATGRQ GSSAEQPLGG RLRKLSLGQY
DNDAGGQLPF SKCAWGKAGV DYAPNLPPFP SPADVKETMT PGYPQDLDII DGRILSSKES
MCSTPAFPVS PETPYVKTAL RHPPFSPPEP PLSSPASQHK GGREPRSCPE TLTHAVGMSE
SPIGPKSTML RADASSTPSF QQAFASSCTI SSNGPGQRRE SSSSAERQWV ESSPKPMVSL
LGSGRPTGSP LSAEFSGTRK DSPVLSCFPP SELQAPFHSH ELSLAEPPDS LAPPSSQAFL
GFGTAPVGSG LPPEEDLGAL LANSHGASPT PSIPLTATGA ADNGFLSHNF LTVAPGHSSH
HSPGLQGQGV TLPGQPPLPE KKRASEGDRS LGSVSPSSSG FSSPHSGSTI SIPFPNVLPD
FSKASEAASP LPDSPGDKLV IVKFVQDTSK FWYKADISRE QAIAMLKDKE PGSFIVRDSH
SFRGAYGLAM KVATPPPSVL QLNKKAGDLA NELVRHFLIE CTPKGVRLKG CSNEPYFGSL
TALVCQHSIT PLALPCKLLI PERDPLEEIA ESSPQTAANS AAELLKQGAA CNVWYLNSVE
MESLTGHQAI QKALSITLVQ EPPPVSTVVH FKVSAQGITL TDNQRKLFFR RHYPVNSVIF
CALDPQDRKW IKDGPSSKVF GFVARKQGSA TDNVCHLFAE HDPEQPASAI VNFVSKVMIG
SPKKV
