Full text data of TNS1
TNS1
(TNS)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Tensin-1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Tensin-1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9HBL0
ID TENS1_HUMAN Reviewed; 1735 AA.
AC Q9HBL0; Q4ZG71;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-NOV-2008, sequence version 2.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Tensin-1;
GN Name=TNS1; Synonyms=TNS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANTS ARG-1197
RP AND ILE-1604.
RC TISSUE=Heart;
RX PubMed=11023826; DOI=10.1042/0264-6021:3510403;
RA Chen H., Ishii A., Wong W.K., Chen L.B., Lo S.H.;
RT "Molecular characterization of human tensin.";
RL Biochem. J. 351:403-411(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
RP PROTEIN SEQUENCE OF 764-781; 1105-1129; 1164-1181; 1440-1450;
RP 1621-1653 AND 1689-1695, PHOSPHORYLATION AT SER-1177, AND MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lempens A., Norman J.C.;
RL Submitted (OCT-2009) to UniProtKB.
RN [4]
RP INTERACTION WITH STARD8.
RX PubMed=17517630; DOI=10.1073/pnas.0703033104;
RA Qian X., Li G., Asmussen H.K., Asnaghi L., Vass W.C., Braverman R.,
RA Yamada K.M., Popescu N.C., Papageorge A.G., Lowy D.R.;
RT "Oncogenic inhibition by a deleted in liver cancer gene requires
RT cooperation between tensin binding and Rho-specific GTPase-activating
RT protein activities.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:9012-9017(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1192 AND SER-1314,
RP VARIANT [LARGE SCALE ANALYSIS] ARG-1197, AND MASS SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1192 AND SER-1314,
RP VARIANT [LARGE SCALE ANALYSIS] ARG-1197, AND MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1177; SER-1192;
RP THR-1266; SER-1269; SER-1381 AND SER-1446, VARIANT [LARGE SCALE
RP ANALYSIS] ARG-1197, AND MASS SPECTROMETRY.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-701; SER-1177; THR-1189;
RP SER-1192; SER-1269; SER-1294 AND SER-1314, VARIANT [LARGE SCALE
RP ANALYSIS] ARG-1197, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21768292; DOI=10.1083/jcb.201007108;
RA Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A.,
RA Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.;
RT "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
RT fibronectin deposition.";
RL J. Cell Biol. 194:307-322(2011).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-1093.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Involved in fibrillar adhesion formation. May be
CC involved in cell migration, cartilage development and in linking
CC signal transduction pathways to the cytoskeleton.
CC -!- SUBUNIT: Binds to actin filaments and interacts with
CC phosphotyrosine-containing proteins. Interacts with STARD8.
CC -!- SUBCELLULAR LOCATION: Cell surface. Cell junction, focal adhesion.
CC Cytoplasm, cytoskeleton. Note=Localized at cell periphery
CC preferentially to fibrillar adhesions than focal adhesions.
CC Translocates from the cell edge to cell center in an ITGB1BP1-
CC dependent manner.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Rapidly cleaved by calpain II.
CC -!- SIMILARITY: Contains 1 C2 tensin-type domain.
CC -!- SIMILARITY: Contains 1 phosphatase tensin-type domain.
CC -!- SIMILARITY: Contains 1 SH2 domain.
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DR EMBL; AF225896; AAG33700.1; -; mRNA.
DR EMBL; AC009469; AAX88952.1; -; Genomic_DNA.
DR RefSeq; NP_072174.3; NM_022648.4.
DR UniGene; Hs.471381; -.
DR ProteinModelPortal; Q9HBL0; -.
DR SMR; Q9HBL0; 5-305, 1458-1574, 1597-1729.
DR IntAct; Q9HBL0; 5.
DR STRING; 9606.ENSP00000171887; -.
DR PhosphoSite; Q9HBL0; -.
DR DMDM; 212276466; -.
DR PaxDb; Q9HBL0; -.
DR PRIDE; Q9HBL0; -.
DR Ensembl; ENST00000171887; ENSP00000171887; ENSG00000079308.
DR GeneID; 7145; -.
DR KEGG; hsa:7145; -.
DR UCSC; uc002vgt.2; human.
DR CTD; 7145; -.
DR GeneCards; GC02M218664; -.
DR H-InvDB; HIX0002818; -.
DR HGNC; HGNC:11973; TNS1.
DR HPA; CAB018774; -.
DR HPA; HPA036089; -.
DR HPA; HPA036090; -.
DR MIM; 600076; gene.
DR neXtProt; NX_Q9HBL0; -.
DR PharmGKB; PA36660; -.
DR eggNOG; COG2453; -.
DR HOGENOM; HOG000060090; -.
DR HOVERGEN; HBG060186; -.
DR InParanoid; Q9HBL0; -.
DR OMA; GAHQGNL; -.
DR OrthoDB; EOG7QG43J; -.
DR PhylomeDB; Q9HBL0; -.
DR SignaLink; Q9HBL0; -.
DR ChiTaRS; TNS1; human.
DR GeneWiki; TNS1; -.
DR GenomeRNAi; 7145; -.
DR NextBio; 27967; -.
DR PMAP-CutDB; Q9HBL0; -.
DR PRO; PR:Q9HBL0; -.
DR ArrayExpress; Q9HBL0; -.
DR Bgee; Q9HBL0; -.
DR CleanEx; HS_TNS1; -.
DR Genevestigator; Q9HBL0; -.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0007044; P:cell-substrate junction assembly; IEA:Ensembl.
DR GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR014019; Phosphatase_tensin-typ.
DR InterPro; IPR013625; PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR014020; Tensin_phosphatase_C2-dom.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF49562; SSF49562; 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 Actin-binding; Cell junction; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; SH2 domain.
FT CHAIN 1 1735 Tensin-1.
FT /FTId=PRO_0000215900.
FT DOMAIN 4 176 Phosphatase tensin-type.
FT DOMAIN 181 307 C2 tensin-type.
FT DOMAIN 1463 1572 SH2.
FT COMPBIAS 651 667 Gln-rich.
FT COMPBIAS 1069 1160 Ser-rich.
FT MOD_RES 701 701 Phosphoserine.
FT MOD_RES 1177 1177 Phosphoserine.
FT MOD_RES 1189 1189 Phosphothreonine.
FT MOD_RES 1192 1192 Phosphoserine.
FT MOD_RES 1266 1266 Phosphothreonine.
FT MOD_RES 1269 1269 Phosphoserine.
FT MOD_RES 1294 1294 Phosphoserine.
FT MOD_RES 1314 1314 Phosphoserine.
FT MOD_RES 1381 1381 Phosphoserine.
FT MOD_RES 1446 1446 Phosphoserine.
FT VARIANT 311 311 I -> M (in dbSNP:rs11680854).
FT /FTId=VAR_047066.
FT VARIANT 466 466 R -> C (in dbSNP:rs3815849).
FT /FTId=VAR_047067.
FT VARIANT 528 528 T -> I (in dbSNP:rs3796033).
FT /FTId=VAR_047068.
FT VARIANT 1004 1004 R -> W (in dbSNP:rs3796028).
FT /FTId=VAR_047069.
FT VARIANT 1093 1093 F -> L (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_048004.
FT VARIANT 1197 1197 W -> R (in dbSNP:rs2571445).
FT /FTId=VAR_047070.
FT VARIANT 1604 1604 V -> I (in dbSNP:rs918949).
FT /FTId=VAR_047071.
FT CONFLICT 179 179 M -> I (in Ref. 1; AAG33700).
FT CONFLICT 1412 1412 S -> A (in Ref. 1; AAG33700).
FT CONFLICT 1416 1416 A -> P (in Ref. 1; AAG33700).
SQ SEQUENCE 1735 AA; 185701 MW; 90C173D5E371EF3E CRC64;
MSVSRTMEDS CELDLVYVTE RIIAVSFPST ANEENFRSNL REVAQMLKSK HGGNYLLFNL
SERRPDITKL HAKVLEFGWP DLHTPALEKI CSICKAMDTW LNADPHNVVV LHNKGNRGRI
GVVIAAYMHY SNISASADQA LDRFAMKRFY EDKIVPIGQP SQRRYVHYFS GLLSGSIKMN
NKPLFLHHVI MHGIPNFESK GGCRPFLRIY QAMQPVYTSG IYNIPGDSQT SVCITIEPGL
LLKGDILLKC YHKKFRSPAR DVIFRVQFHT CAIHDLGVVF GKEDLDDAFK DDRFPEYGKV
EFVFSYGPEK IQGMEHLENG PSVSVDYNTS DPLIRWDSYD NFSGHRDDGM EEVVGHTQGP
LDGSLYAKVK KKDSLHGSTG AVNATRPTLS ATPNHVEHTL SVSSDSGNST ASTKTDKTDE
PVPGASSATA ALSPQEKREL DRLLSGFGLE REKQGAMYHT QHLRSRPAGG SAVPSSGRHV
VPAQVHVNGG ALASERETDI LDDELPNQDG HSAGSMGTLS SLDGVTNTSE GGYPEALSPL
TNGLDKSYPM EPMVNGGGYP YESASRAGPA HAGHTAPMRP SYSAQEGLAG YQREGPHPAW
PQPVTTSHYA HDPSGMFRSQ SFSEAEPQLP PAPVRGGSSR EAVQRGLNSW QQQQQQQQQP
RPPPRQQERA HLESLVASRP SPQPLAETPI PSLPEFPRAA SQQEIEQSIE TLNMLMLDLE
PASAAAPLHK SQSVPGAWPG ASPLSSQPLS GSSRQSHPLT QSRSGYIPSG HSLGTPEPAP
RASLESVPPG RSYSPYDYQP CLAGPNQDFH SKSPASSSLP AFLPTTHSPP GPQQPPASLP
GLTAQPLLSP KEATSDPSRT PEEEPLNLEG LVAHRVAGVQ AREKQPAEPP APLRRRAASD
GQYENQSPEA TSPRSPGVRS PVQCVSPELA LTIALNPGGR PKEPHLHSYK EAFEEMEGTS
PSSPPPSGVR SPPGLAKTPL SALGLKPHNP ADILLHPTGV TRRRIQPEED EGKVVVRLSE
EPRSYVESVA RTAVAGPRAQ DSEPKSFSAP ATQAYGHEIP LRNGTLGGSF VSPSPLSTSS
PILSADSTSV GSFPSGESSD QGPRTPTQPL LESGFRSGSL GQPSPSAQRN YQSSSPLPTV
GSSYSSPDYS LQHFSSSPES QARAQFSVAG VHTVPGSPQA RHRTVGTNTP PSPGFGWRAI
NPSMAAPSSP SLSHHQMMGP PGTGFHGSTV SSPQSSAATT PGSPSLCRHP AGVYQVSGLH
NKVATTPGSP SLGRHPGAHQ GNLASGLHSN AIASPGSPSL GRHLGGSGSV VPGSPCLDRH
VAYGGYSTPE DRRPTLSRQS SASGYQAPST PSFPVSPAYY PGLSSPATSP SPDSAAFRQG
SPTPALPEKR RMSVGDRAGS LPNYATINGK VSSPVASGMS SPSGGSTVSF SHTLPDFSKY
SMPDNSPETR AKVKFVQDTS KYWYKPEISR EQAIALLKDQ EPGAFIIRDS HSFRGAYGLA
MKVSSPPPTI MQQNKKGDMT HELVRHFLIE TGPRGVKLKG CPNEPNFGSL SALVYQHSII
PLALPCKLVI PNRDPTDESK DSSGPANSTA DLLKQGAACN VLFVNSVDME SLTGPQAISK
ATSETLAADP TPAATIVHFK VSAQGITLTD NQRKLFFRRH YPLNTVTFCD LDPQERKWMK
TEGGAPAKLF GFVARKQGST TDNACHLFAE LDPNQPASAI VNFVSKVMLN AGQKR
//
ID TENS1_HUMAN Reviewed; 1735 AA.
AC Q9HBL0; Q4ZG71;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-NOV-2008, sequence version 2.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Tensin-1;
GN Name=TNS1; Synonyms=TNS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANTS ARG-1197
RP AND ILE-1604.
RC TISSUE=Heart;
RX PubMed=11023826; DOI=10.1042/0264-6021:3510403;
RA Chen H., Ishii A., Wong W.K., Chen L.B., Lo S.H.;
RT "Molecular characterization of human tensin.";
RL Biochem. J. 351:403-411(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
RP PROTEIN SEQUENCE OF 764-781; 1105-1129; 1164-1181; 1440-1450;
RP 1621-1653 AND 1689-1695, PHOSPHORYLATION AT SER-1177, AND MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lempens A., Norman J.C.;
RL Submitted (OCT-2009) to UniProtKB.
RN [4]
RP INTERACTION WITH STARD8.
RX PubMed=17517630; DOI=10.1073/pnas.0703033104;
RA Qian X., Li G., Asmussen H.K., Asnaghi L., Vass W.C., Braverman R.,
RA Yamada K.M., Popescu N.C., Papageorge A.G., Lowy D.R.;
RT "Oncogenic inhibition by a deleted in liver cancer gene requires
RT cooperation between tensin binding and Rho-specific GTPase-activating
RT protein activities.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:9012-9017(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1192 AND SER-1314,
RP VARIANT [LARGE SCALE ANALYSIS] ARG-1197, AND MASS SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1192 AND SER-1314,
RP VARIANT [LARGE SCALE ANALYSIS] ARG-1197, AND MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1177; SER-1192;
RP THR-1266; SER-1269; SER-1381 AND SER-1446, VARIANT [LARGE SCALE
RP ANALYSIS] ARG-1197, AND MASS SPECTROMETRY.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-701; SER-1177; THR-1189;
RP SER-1192; SER-1269; SER-1294 AND SER-1314, VARIANT [LARGE SCALE
RP ANALYSIS] ARG-1197, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21768292; DOI=10.1083/jcb.201007108;
RA Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A.,
RA Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.;
RT "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
RT fibronectin deposition.";
RL J. Cell Biol. 194:307-322(2011).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-1093.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Involved in fibrillar adhesion formation. May be
CC involved in cell migration, cartilage development and in linking
CC signal transduction pathways to the cytoskeleton.
CC -!- SUBUNIT: Binds to actin filaments and interacts with
CC phosphotyrosine-containing proteins. Interacts with STARD8.
CC -!- SUBCELLULAR LOCATION: Cell surface. Cell junction, focal adhesion.
CC Cytoplasm, cytoskeleton. Note=Localized at cell periphery
CC preferentially to fibrillar adhesions than focal adhesions.
CC Translocates from the cell edge to cell center in an ITGB1BP1-
CC dependent manner.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Rapidly cleaved by calpain II.
CC -!- SIMILARITY: Contains 1 C2 tensin-type domain.
CC -!- SIMILARITY: Contains 1 phosphatase tensin-type domain.
CC -!- SIMILARITY: Contains 1 SH2 domain.
CC -----------------------------------------------------------------------
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DR EMBL; AF225896; AAG33700.1; -; mRNA.
DR EMBL; AC009469; AAX88952.1; -; Genomic_DNA.
DR RefSeq; NP_072174.3; NM_022648.4.
DR UniGene; Hs.471381; -.
DR ProteinModelPortal; Q9HBL0; -.
DR SMR; Q9HBL0; 5-305, 1458-1574, 1597-1729.
DR IntAct; Q9HBL0; 5.
DR STRING; 9606.ENSP00000171887; -.
DR PhosphoSite; Q9HBL0; -.
DR DMDM; 212276466; -.
DR PaxDb; Q9HBL0; -.
DR PRIDE; Q9HBL0; -.
DR Ensembl; ENST00000171887; ENSP00000171887; ENSG00000079308.
DR GeneID; 7145; -.
DR KEGG; hsa:7145; -.
DR UCSC; uc002vgt.2; human.
DR CTD; 7145; -.
DR GeneCards; GC02M218664; -.
DR H-InvDB; HIX0002818; -.
DR HGNC; HGNC:11973; TNS1.
DR HPA; CAB018774; -.
DR HPA; HPA036089; -.
DR HPA; HPA036090; -.
DR MIM; 600076; gene.
DR neXtProt; NX_Q9HBL0; -.
DR PharmGKB; PA36660; -.
DR eggNOG; COG2453; -.
DR HOGENOM; HOG000060090; -.
DR HOVERGEN; HBG060186; -.
DR InParanoid; Q9HBL0; -.
DR OMA; GAHQGNL; -.
DR OrthoDB; EOG7QG43J; -.
DR PhylomeDB; Q9HBL0; -.
DR SignaLink; Q9HBL0; -.
DR ChiTaRS; TNS1; human.
DR GeneWiki; TNS1; -.
DR GenomeRNAi; 7145; -.
DR NextBio; 27967; -.
DR PMAP-CutDB; Q9HBL0; -.
DR PRO; PR:Q9HBL0; -.
DR ArrayExpress; Q9HBL0; -.
DR Bgee; Q9HBL0; -.
DR CleanEx; HS_TNS1; -.
DR Genevestigator; Q9HBL0; -.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0007044; P:cell-substrate junction assembly; IEA:Ensembl.
DR GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR014019; Phosphatase_tensin-typ.
DR InterPro; IPR013625; PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR014020; Tensin_phosphatase_C2-dom.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF49562; SSF49562; 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 Actin-binding; Cell junction; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; SH2 domain.
FT CHAIN 1 1735 Tensin-1.
FT /FTId=PRO_0000215900.
FT DOMAIN 4 176 Phosphatase tensin-type.
FT DOMAIN 181 307 C2 tensin-type.
FT DOMAIN 1463 1572 SH2.
FT COMPBIAS 651 667 Gln-rich.
FT COMPBIAS 1069 1160 Ser-rich.
FT MOD_RES 701 701 Phosphoserine.
FT MOD_RES 1177 1177 Phosphoserine.
FT MOD_RES 1189 1189 Phosphothreonine.
FT MOD_RES 1192 1192 Phosphoserine.
FT MOD_RES 1266 1266 Phosphothreonine.
FT MOD_RES 1269 1269 Phosphoserine.
FT MOD_RES 1294 1294 Phosphoserine.
FT MOD_RES 1314 1314 Phosphoserine.
FT MOD_RES 1381 1381 Phosphoserine.
FT MOD_RES 1446 1446 Phosphoserine.
FT VARIANT 311 311 I -> M (in dbSNP:rs11680854).
FT /FTId=VAR_047066.
FT VARIANT 466 466 R -> C (in dbSNP:rs3815849).
FT /FTId=VAR_047067.
FT VARIANT 528 528 T -> I (in dbSNP:rs3796033).
FT /FTId=VAR_047068.
FT VARIANT 1004 1004 R -> W (in dbSNP:rs3796028).
FT /FTId=VAR_047069.
FT VARIANT 1093 1093 F -> L (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_048004.
FT VARIANT 1197 1197 W -> R (in dbSNP:rs2571445).
FT /FTId=VAR_047070.
FT VARIANT 1604 1604 V -> I (in dbSNP:rs918949).
FT /FTId=VAR_047071.
FT CONFLICT 179 179 M -> I (in Ref. 1; AAG33700).
FT CONFLICT 1412 1412 S -> A (in Ref. 1; AAG33700).
FT CONFLICT 1416 1416 A -> P (in Ref. 1; AAG33700).
SQ SEQUENCE 1735 AA; 185701 MW; 90C173D5E371EF3E CRC64;
MSVSRTMEDS CELDLVYVTE RIIAVSFPST ANEENFRSNL REVAQMLKSK HGGNYLLFNL
SERRPDITKL HAKVLEFGWP DLHTPALEKI CSICKAMDTW LNADPHNVVV LHNKGNRGRI
GVVIAAYMHY SNISASADQA LDRFAMKRFY EDKIVPIGQP SQRRYVHYFS GLLSGSIKMN
NKPLFLHHVI MHGIPNFESK GGCRPFLRIY QAMQPVYTSG IYNIPGDSQT SVCITIEPGL
LLKGDILLKC YHKKFRSPAR DVIFRVQFHT CAIHDLGVVF GKEDLDDAFK DDRFPEYGKV
EFVFSYGPEK IQGMEHLENG PSVSVDYNTS DPLIRWDSYD NFSGHRDDGM EEVVGHTQGP
LDGSLYAKVK KKDSLHGSTG AVNATRPTLS ATPNHVEHTL SVSSDSGNST ASTKTDKTDE
PVPGASSATA ALSPQEKREL DRLLSGFGLE REKQGAMYHT QHLRSRPAGG SAVPSSGRHV
VPAQVHVNGG ALASERETDI LDDELPNQDG HSAGSMGTLS SLDGVTNTSE GGYPEALSPL
TNGLDKSYPM EPMVNGGGYP YESASRAGPA HAGHTAPMRP SYSAQEGLAG YQREGPHPAW
PQPVTTSHYA HDPSGMFRSQ SFSEAEPQLP PAPVRGGSSR EAVQRGLNSW QQQQQQQQQP
RPPPRQQERA HLESLVASRP SPQPLAETPI PSLPEFPRAA SQQEIEQSIE TLNMLMLDLE
PASAAAPLHK SQSVPGAWPG ASPLSSQPLS GSSRQSHPLT QSRSGYIPSG HSLGTPEPAP
RASLESVPPG RSYSPYDYQP CLAGPNQDFH SKSPASSSLP AFLPTTHSPP GPQQPPASLP
GLTAQPLLSP KEATSDPSRT PEEEPLNLEG LVAHRVAGVQ AREKQPAEPP APLRRRAASD
GQYENQSPEA TSPRSPGVRS PVQCVSPELA LTIALNPGGR PKEPHLHSYK EAFEEMEGTS
PSSPPPSGVR SPPGLAKTPL SALGLKPHNP ADILLHPTGV TRRRIQPEED EGKVVVRLSE
EPRSYVESVA RTAVAGPRAQ DSEPKSFSAP ATQAYGHEIP LRNGTLGGSF VSPSPLSTSS
PILSADSTSV GSFPSGESSD QGPRTPTQPL LESGFRSGSL GQPSPSAQRN YQSSSPLPTV
GSSYSSPDYS LQHFSSSPES QARAQFSVAG VHTVPGSPQA RHRTVGTNTP PSPGFGWRAI
NPSMAAPSSP SLSHHQMMGP PGTGFHGSTV SSPQSSAATT PGSPSLCRHP AGVYQVSGLH
NKVATTPGSP SLGRHPGAHQ GNLASGLHSN AIASPGSPSL GRHLGGSGSV VPGSPCLDRH
VAYGGYSTPE DRRPTLSRQS SASGYQAPST PSFPVSPAYY PGLSSPATSP SPDSAAFRQG
SPTPALPEKR RMSVGDRAGS LPNYATINGK VSSPVASGMS SPSGGSTVSF SHTLPDFSKY
SMPDNSPETR AKVKFVQDTS KYWYKPEISR EQAIALLKDQ EPGAFIIRDS HSFRGAYGLA
MKVSSPPPTI MQQNKKGDMT HELVRHFLIE TGPRGVKLKG CPNEPNFGSL SALVYQHSII
PLALPCKLVI PNRDPTDESK DSSGPANSTA DLLKQGAACN VLFVNSVDME SLTGPQAISK
ATSETLAADP TPAATIVHFK VSAQGITLTD NQRKLFFRRH YPLNTVTFCD LDPQERKWMK
TEGGAPAKLF GFVARKQGST TDNACHLFAE LDPNQPASAI VNFVSKVMLN AGQKR
//
MIM
600076
*RECORD*
*FIELD* NO
600076
*FIELD* TI
*600076 TENSIN 1; TNS1
;;TENSIN; TNS
*FIELD* TX
DESCRIPTION
Tensin is an actin-binding protein that is concentrated in some
read moresubmembranous cytoskeletal focal contacts (Weigt et al., 1992). In
addition to its 3 actin-binding domains, the 200-kD tensin protein
contains an Src homology 2 (SH2) motif that mediates protein-protein
contacts and is shared by a variety of signal transduction molecules. In
addition, tensin can bind to phosphotyrosine-containing proteins and can
itself be phosphorylated, suggesting that tensin may be a link between
the cytoskeleton and a signal transduction pathway. Tensin
phosphorylation occurs during cell adhesion to extracellular matrix
proteins.
CLONING
Using avian tensin as probe, Chen et al. (2000) obtained overlapping
clones of tensin from human heart and bovine pericyte cDNA libraries.
The deduced 1,735-amino acid protein has a calculated molecular mass of
185 kD. Human and bovine tensins share 82% amino acid identity. In
addition to the actin-binding domains and SH2 domain, tensin contains a
region similar to PTEN (601728) and a 9-amino acid sequence that is
repeated 4 times. Northern blot analysis revealed a major 10-kb
transcript expressed in most tissues, with highest levels in heart,
skeletal muscle, kidney, and lung. Heart and skeletal muscle also
expressed a 9-kb transcript. Western blot analysis revealed an apparent
molecular mass of 220 kD, and mutation analysis revealed that the
discrepancy between the calculated and the apparent molecular masses was
due to the reduced electrophoretic mobility of the central region of the
tensin polypeptide. Expression of tensin in mouse fibroblasts resulted
in staining at focal adhesions.
GENE FUNCTION
Katz et al. (2000) presented evidence that overexpression of mammalian
tensin activates both the JNK (601158) and p38 MAPK (600289) pathways.
Tensin-mediated JNK activation was independent of the activities of Rac
(602048) and Cdc42 (116952), but did depend on Sek (601335).
Chen et al. (2002) determined that stable overexpression of both
tensin-1 and -2 (TENC1; 607717) in HEK293 cells promoted cell migration
on fibronectin (135600) in a cell migration assay. Fibroblasts from
tensin-1-null mice migrated significantly slower than their normal
counterparts in the cell migration assay, and tensin-2 expression was
not upregulated to compensate for loss of tensin-1 function.
Chen et al. (2000) found that tensin expression was reduced or absent in
several prostate and breast cancer cell lines, while the levels of talin
(186745) and focal adhesion kinase (600758) remained at normal levels.
They also found that tensin is a substrate for a focal adhesion
protease, calpain II (114230), and that incubation of cells with a
calpain inhibitor prevented tensin cleavage and induced morphologic
change. Chen et al. (2002) hypothesized that cleavage of tensin and
other focal adhesion constituents by calpain disrupts maintenance of
normal cell shape.
GENE STRUCTURE
Chen et al. (2002) determined that the tensin gene contains 33 exons and
spans about 150 kb. Exon 6 contains the putative start codon.
MAPPING
Jankowski and Gumucio (1995) demonstrated that, in the mouse, genes for
tensin, villin (193040), and desmin (125660) are closely linked on
chromosome 1. This region is homologous to human chromosome 2; in the
human, the desmin gene maps to 2q35 and the villin-1 gene to 2q35-q36.
Jankowski and Gumucio (1995) used a rat DNA probe to study human/rodent
somatic cell hybrids and obtained results consistent with location of
the human TNS gene on chromosome 2. Homology of synteny would suggest
that it is located in the 2q35-q36 region.
ANIMAL MODEL
Lo et al. (1997) generated tensin-null mice. These mice appeared normal
and healthy for several months, but eventually developed cystic kidneys.
Progressive cyst formation led to kidney degeneration and death from
renal failure. The authors concluded that tensin is not necessary for
mouse embryogenesis, but it is required for the maintenance of normal
renal function.
*FIELD* RF
1. Chen, H.; Duncan, I. C.; Bozorgchami, H.; Lo, S. H.: Tensin1 and
a previously undocumented family member, tensin2, positively regulate
cell migration. Proc. Nat. Acad. Sci. 99: 733-738, 2002.
2. Chen, H.; Ishii, A.; Wong, W. K; Chen, L. B.; Lo, S. H.: Molecular
characterization of human tensin. Biochem J. 351: 403-411, 2000.
3. Jankowski, S. A.; Gumucio, D. L.: Genes for tensin, villin and
desmin are linked on mouse chromosome 1. Mammalian Genome 6: 744-745,
1995.
4. Katz, B. Z.; Zohar, M.; Teramoto, H.; Matsumoto, K.; Gutkind, J.
S.; Lin, D. C.; Lin, S.; Yamada, K. M.: Tensin can induce JNK and
p38 activation. Biochem. Biophys. Res. Commun. 16: 717-720, 2000.
5. Lo, S. H.; Yu, Q.-C.; Degenstein, L.; Chen, L. B.; Fuchs, E.:
Progressive kidney degeneration in mice lacking tensin. J. Cell Biol. 136:
1349-1361, 1997.
6. Weigt, C.; Gaertner, A.; Wegner, A.; Korte, H.; Meyer, H. E.:
Occurrence of an actin-inserting domain in tensin. J. Molec. Biol. 227:
593-595, 1992.
*FIELD* CN
Patricia A. Hartz - updated: 5/7/2003
Patricia A. Hartz - updated: 4/23/2003
*FIELD* CD
Victor A. McKusick: 12/1/1995
*FIELD* ED
mgross: 02/18/2008
alopez: 2/21/2007
terry: 4/4/2005
terry: 7/28/2003
cwells: 5/21/2003
cwells: 5/7/2003
mgross: 4/24/2003
terry: 4/23/2003
dholmes: 6/8/1998
*RECORD*
*FIELD* NO
600076
*FIELD* TI
*600076 TENSIN 1; TNS1
;;TENSIN; TNS
*FIELD* TX
DESCRIPTION
Tensin is an actin-binding protein that is concentrated in some
read moresubmembranous cytoskeletal focal contacts (Weigt et al., 1992). In
addition to its 3 actin-binding domains, the 200-kD tensin protein
contains an Src homology 2 (SH2) motif that mediates protein-protein
contacts and is shared by a variety of signal transduction molecules. In
addition, tensin can bind to phosphotyrosine-containing proteins and can
itself be phosphorylated, suggesting that tensin may be a link between
the cytoskeleton and a signal transduction pathway. Tensin
phosphorylation occurs during cell adhesion to extracellular matrix
proteins.
CLONING
Using avian tensin as probe, Chen et al. (2000) obtained overlapping
clones of tensin from human heart and bovine pericyte cDNA libraries.
The deduced 1,735-amino acid protein has a calculated molecular mass of
185 kD. Human and bovine tensins share 82% amino acid identity. In
addition to the actin-binding domains and SH2 domain, tensin contains a
region similar to PTEN (601728) and a 9-amino acid sequence that is
repeated 4 times. Northern blot analysis revealed a major 10-kb
transcript expressed in most tissues, with highest levels in heart,
skeletal muscle, kidney, and lung. Heart and skeletal muscle also
expressed a 9-kb transcript. Western blot analysis revealed an apparent
molecular mass of 220 kD, and mutation analysis revealed that the
discrepancy between the calculated and the apparent molecular masses was
due to the reduced electrophoretic mobility of the central region of the
tensin polypeptide. Expression of tensin in mouse fibroblasts resulted
in staining at focal adhesions.
GENE FUNCTION
Katz et al. (2000) presented evidence that overexpression of mammalian
tensin activates both the JNK (601158) and p38 MAPK (600289) pathways.
Tensin-mediated JNK activation was independent of the activities of Rac
(602048) and Cdc42 (116952), but did depend on Sek (601335).
Chen et al. (2002) determined that stable overexpression of both
tensin-1 and -2 (TENC1; 607717) in HEK293 cells promoted cell migration
on fibronectin (135600) in a cell migration assay. Fibroblasts from
tensin-1-null mice migrated significantly slower than their normal
counterparts in the cell migration assay, and tensin-2 expression was
not upregulated to compensate for loss of tensin-1 function.
Chen et al. (2000) found that tensin expression was reduced or absent in
several prostate and breast cancer cell lines, while the levels of talin
(186745) and focal adhesion kinase (600758) remained at normal levels.
They also found that tensin is a substrate for a focal adhesion
protease, calpain II (114230), and that incubation of cells with a
calpain inhibitor prevented tensin cleavage and induced morphologic
change. Chen et al. (2002) hypothesized that cleavage of tensin and
other focal adhesion constituents by calpain disrupts maintenance of
normal cell shape.
GENE STRUCTURE
Chen et al. (2002) determined that the tensin gene contains 33 exons and
spans about 150 kb. Exon 6 contains the putative start codon.
MAPPING
Jankowski and Gumucio (1995) demonstrated that, in the mouse, genes for
tensin, villin (193040), and desmin (125660) are closely linked on
chromosome 1. This region is homologous to human chromosome 2; in the
human, the desmin gene maps to 2q35 and the villin-1 gene to 2q35-q36.
Jankowski and Gumucio (1995) used a rat DNA probe to study human/rodent
somatic cell hybrids and obtained results consistent with location of
the human TNS gene on chromosome 2. Homology of synteny would suggest
that it is located in the 2q35-q36 region.
ANIMAL MODEL
Lo et al. (1997) generated tensin-null mice. These mice appeared normal
and healthy for several months, but eventually developed cystic kidneys.
Progressive cyst formation led to kidney degeneration and death from
renal failure. The authors concluded that tensin is not necessary for
mouse embryogenesis, but it is required for the maintenance of normal
renal function.
*FIELD* RF
1. Chen, H.; Duncan, I. C.; Bozorgchami, H.; Lo, S. H.: Tensin1 and
a previously undocumented family member, tensin2, positively regulate
cell migration. Proc. Nat. Acad. Sci. 99: 733-738, 2002.
2. Chen, H.; Ishii, A.; Wong, W. K; Chen, L. B.; Lo, S. H.: Molecular
characterization of human tensin. Biochem J. 351: 403-411, 2000.
3. Jankowski, S. A.; Gumucio, D. L.: Genes for tensin, villin and
desmin are linked on mouse chromosome 1. Mammalian Genome 6: 744-745,
1995.
4. Katz, B. Z.; Zohar, M.; Teramoto, H.; Matsumoto, K.; Gutkind, J.
S.; Lin, D. C.; Lin, S.; Yamada, K. M.: Tensin can induce JNK and
p38 activation. Biochem. Biophys. Res. Commun. 16: 717-720, 2000.
5. Lo, S. H.; Yu, Q.-C.; Degenstein, L.; Chen, L. B.; Fuchs, E.:
Progressive kidney degeneration in mice lacking tensin. J. Cell Biol. 136:
1349-1361, 1997.
6. Weigt, C.; Gaertner, A.; Wegner, A.; Korte, H.; Meyer, H. E.:
Occurrence of an actin-inserting domain in tensin. J. Molec. Biol. 227:
593-595, 1992.
*FIELD* CN
Patricia A. Hartz - updated: 5/7/2003
Patricia A. Hartz - updated: 4/23/2003
*FIELD* CD
Victor A. McKusick: 12/1/1995
*FIELD* ED
mgross: 02/18/2008
alopez: 2/21/2007
terry: 4/4/2005
terry: 7/28/2003
cwells: 5/21/2003
cwells: 5/7/2003
mgross: 4/24/2003
terry: 4/23/2003
dholmes: 6/8/1998