Full text data of TES
TES
[Confidence: low (only semi-automatic identification from reviews)]
Testin (TESS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Testin (TESS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UGI8
ID TES_HUMAN Reviewed; 421 AA.
AC Q9UGI8; A4D0U6; Q9GZQ1; Q9HAJ9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=Testin;
DE AltName: Full=TESS;
GN Name=TES;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RX PubMed=10950921; DOI=10.1006/geno.2000.6272;
RA Tatarelli C., Linnenbach A., Mimori K., Croce C.M.;
RT "Characterization of the human TESTIN gene localized in the FRA7G
RT region at 7q31.2.";
RL Genomics 68:1-12(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11420696; DOI=10.1038/sj.onc.1204433;
RA Tobias E.S., Hurlstone A.F.L., MacKenzie E., McFarlane R., Black D.M.;
RT "The TES gene at 7q31.1 is methylated in tumours and encodes a novel
RT growth-suppressing LIM domain protein.";
RL Oncogene 20:2844-2853(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Prostate;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF CYS-391, AND
RP INTERACTION WITH ENAH; ZYX; VASP; ACTIN FIBERS; ALPHA-ACTININ AND PXN.
RX PubMed=12695497; DOI=10.1083/jcb.200211015;
RA Garvalov B.K., Higgins T.E., Sutherland J.D., Zettl M., Scaplehorn N.,
RA Koecher T., Piddini E., Griffiths G., Way M.;
RT "The conformational state of Tes regulates its zyxin-dependent
RT recruitment to focal adhesions.";
RL J. Cell Biol. 161:33-39(2003).
RN [8]
RP FUNCTION, INTERACTION WITH ZYX; GRIP1; ENAH AND TALIN, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12571287; DOI=10.1242/jcs.00278;
RA Coutts A.S., MacKenzie E., Griffith E., Black D.M.;
RT "TES is a novel focal adhesion protein with a role in cell
RT spreading.";
RL J. Cell Sci. 116:897-906(2003).
RN [9]
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.,
RA Buerckstuemmer T., 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 [10]
RP INTERACTION WITH ALKBH4.
RX PubMed=23145062; DOI=10.1371/journal.pone.0049045;
RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M.,
RA Meza-Zepeda L.A., Falnes P.O.;
RT "Human ALKBH4 interacts with proteins associated with transcription.";
RL PLoS ONE 7:E49045-E49045(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 357-421 IN COMPLEX WITH ZINC
RP IONS AND ENAH.
RX PubMed=18158903; DOI=10.1016/j.molcel.2007.10.033;
RA Boeda B., Briggs D.C., Higgins T., Garvalov B.K., Fadden A.J.,
RA McDonald N.Q., Way M.;
RT "Tes, a specific Mena interacting partner, breaks the rules for EVH1
RT binding.";
RL Mol. Cell 28:1071-1082(2007).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 296-421 IN COMPLEX WITH ZINC
RP IONS; ENAH AND ACTL7A, MUTAGENESIS OF CYS-328, AND SUBUNIT.
RX PubMed=21278383; DOI=10.1074/jbc.M110.171264;
RA Boeda B., Knowles P.P., Briggs D.C., Murray-Rust J., Soriano E.,
RA Garvalov B.K., McDonald N.Q., Way M.;
RT "Molecular recognition of the Tes LIM2-3 domains by the actin-related
RT protein Arp7A.";
RL J. Biol. Chem. 286:11543-11554(2011).
CC -!- FUNCTION: Scaffold protein that may play a role in cell adhesion,
CC cell spreading and in the reorganization of the actin
CC cytoskeleton. Plays a role in the regulation of cell
CC proliferation. May act as a tumor suppressor. Inhibits tumor cell
CC growth.
CC -!- SUBUNIT: Interacts via LIM domain 1 with ZYX. Interacts (via LIM
CC domain 3) with ENAH and VASP. Interacts with ALKBH4, talin, actin,
CC alpha-actinin, GRIP1 and PXN. Interacts (via LIM domain 2) with
CC ACTL7A (via N-terminus). Heterodimer with ACTL7A; the heterodimer
CC interacts with ENAH to form a heterotrimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion.
CC Note=Detected along actin stress fibers.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UGI8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UGI8-2; Sequence=VSP_003122;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The N-terminal and the C-terminal halves of the protein
CC can associate with each other, thereby hindering interactions with
CC ZYX.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC -!- SIMILARITY: Contains 3 LIM zinc-binding domains.
CC -!- SIMILARITY: Contains 1 PET domain.
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DR EMBL; AF260225; AAG17635.1; -; Genomic_DNA.
DR EMBL; AF260225; AAG17636.1; -; Genomic_DNA.
DR EMBL; AF245356; AAG17612.1; -; mRNA.
DR EMBL; AF245357; AAG17613.1; -; mRNA.
DR EMBL; AJ250865; CAB65119.1; -; mRNA.
DR EMBL; AK021575; BAB13846.1; -; mRNA.
DR EMBL; AK291802; BAF84491.1; -; mRNA.
DR EMBL; AC073130; AAQ93367.1; -; Genomic_DNA.
DR EMBL; CH236947; EAL24365.1; -; Genomic_DNA.
DR EMBL; BC001451; AAH01451.1; -; mRNA.
DR RefSeq; NP_056456.1; NM_015641.3.
DR RefSeq; NP_690042.1; NM_152829.2.
DR UniGene; Hs.592286; -.
DR UniGene; Hs.664957; -.
DR PDB; 2IYB; X-ray; 2.35 A; E/F/G/H=357-421.
DR PDB; 2XQN; X-ray; 2.62 A; T=296-421.
DR PDBsum; 2IYB; -.
DR PDBsum; 2XQN; -.
DR ProteinModelPortal; Q9UGI8; -.
DR SMR; Q9UGI8; 258-421.
DR IntAct; Q9UGI8; 18.
DR MINT; MINT-2821159; -.
DR STRING; 9606.ENSP00000350937; -.
DR PhosphoSite; Q9UGI8; -.
DR DMDM; 17380320; -.
DR PaxDb; Q9UGI8; -.
DR PeptideAtlas; Q9UGI8; -.
DR PRIDE; Q9UGI8; -.
DR DNASU; 26136; -.
DR Ensembl; ENST00000358204; ENSP00000350937; ENSG00000135269.
DR Ensembl; ENST00000393481; ENSP00000377121; ENSG00000135269.
DR GeneID; 26136; -.
DR KEGG; hsa:26136; -.
DR UCSC; uc003vho.3; human.
DR CTD; 26136; -.
DR GeneCards; GC07P115850; -.
DR HGNC; HGNC:14620; TES.
DR HPA; CAB003690; -.
DR HPA; HPA015269; -.
DR HPA; HPA018123; -.
DR MIM; 606085; gene.
DR neXtProt; NX_Q9UGI8; -.
DR PharmGKB; PA37906; -.
DR eggNOG; NOG272178; -.
DR HOGENOM; HOG000231628; -.
DR HOVERGEN; HBG001038; -.
DR InParanoid; Q9UGI8; -.
DR OMA; VKLPREM; -.
DR OrthoDB; EOG7P8P7M; -.
DR PhylomeDB; Q9UGI8; -.
DR ChiTaRS; TES; human.
DR EvolutionaryTrace; Q9UGI8; -.
DR GeneWiki; Testin; -.
DR GenomeRNAi; 26136; -.
DR NextBio; 48175; -.
DR PRO; PR:Q9UGI8; -.
DR ArrayExpress; Q9UGI8; -.
DR Bgee; Q9UGI8; -.
DR CleanEx; HS_TES; -.
DR Genevestigator; Q9UGI8; -.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0043234; C:protein complex; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
DR Gene3D; 2.10.110.10; -; 3.
DR InterPro; IPR010442; PET_domain.
DR InterPro; IPR027683; Testin.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24211:SF1; PTHR24211:SF1; 1.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF06297; PET; 1.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS51303; PET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Complete proteome;
KW Cytoplasm; LIM domain; Metal-binding; Polymorphism;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1 421 Testin.
FT /FTId=PRO_0000075906.
FT DOMAIN 92 199 PET.
FT DOMAIN 234 297 LIM zinc-binding 1.
FT DOMAIN 299 359 LIM zinc-binding 2.
FT DOMAIN 362 421 LIM zinc-binding 3.
FT COMPBIAS 22 46 Cys-rich.
FT VAR_SEQ 1 9 Missing (in isoform 2).
FT /FTId=VSP_003122.
FT VARIANT 221 221 A -> V (in dbSNP:rs2272193).
FT /FTId=VAR_050170.
FT MUTAGEN 328 328 C->A: Abolishes interaction with ACTL7A.
FT MUTAGEN 391 391 C->A: Abolishes localization at focal
FT adhesions.
FT CONFLICT 132 132 K -> E (in Ref. 3; BAB13846).
FT TURN 302 304
FT STRAND 305 307
FT STRAND 313 316
FT STRAND 319 321
FT HELIX 323 325
FT TURN 329 331
FT STRAND 338 343
FT STRAND 346 349
FT HELIX 350 356
FT TURN 362 364
FT STRAND 365 368
FT STRAND 374 377
FT STRAND 380 383
FT TURN 384 387
FT TURN 392 394
FT STRAND 404 406
FT STRAND 409 413
FT HELIX 414 418
SQ SEQUENCE 421 AA; 47996 MW; AB9FF6669C50D492 CRC64;
MDLENKVKKM GLGHEQGFGA PCLKCKEKCE GFELHFWRKI CRNCKCGQEE HDVLLSNEED
RKVGKLFEDT KYTTLIAKLK SDGIPMYKRN VMILTNPVAA KKNVSINTVT YEWAPPVQNQ
ALARQYMQML PKEKQPVAGS EGAQYRKKQL AKQLPAHDQD PSKCHELSPR EVKEMEQFVK
KYKSEALGVG DVKLPCEMDA QGPKQMNIPG GDRSTPAAVG AMEDKSAEHK RTQYSCYCCK
LSMKEGDPAI YAERAGYDKL WHPACFVCST CHELLVDMIY FWKNEKLYCG RHYCDSEKPR
CAGCDELIFS NEYTQAENQN WHLKHFCCFD CDSILAGEIY VMVNDKPVCK PCYVKNHAVV
CQGCHNAIDP EVQRVTYNNF SWHASTECFL CSCCSKCLIG QKFMPVEGMV FCSVECKKRM
S
//
ID TES_HUMAN Reviewed; 421 AA.
AC Q9UGI8; A4D0U6; Q9GZQ1; Q9HAJ9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=Testin;
DE AltName: Full=TESS;
GN Name=TES;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RX PubMed=10950921; DOI=10.1006/geno.2000.6272;
RA Tatarelli C., Linnenbach A., Mimori K., Croce C.M.;
RT "Characterization of the human TESTIN gene localized in the FRA7G
RT region at 7q31.2.";
RL Genomics 68:1-12(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11420696; DOI=10.1038/sj.onc.1204433;
RA Tobias E.S., Hurlstone A.F.L., MacKenzie E., McFarlane R., Black D.M.;
RT "The TES gene at 7q31.1 is methylated in tumours and encodes a novel
RT growth-suppressing LIM domain protein.";
RL Oncogene 20:2844-2853(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Prostate;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF CYS-391, AND
RP INTERACTION WITH ENAH; ZYX; VASP; ACTIN FIBERS; ALPHA-ACTININ AND PXN.
RX PubMed=12695497; DOI=10.1083/jcb.200211015;
RA Garvalov B.K., Higgins T.E., Sutherland J.D., Zettl M., Scaplehorn N.,
RA Koecher T., Piddini E., Griffiths G., Way M.;
RT "The conformational state of Tes regulates its zyxin-dependent
RT recruitment to focal adhesions.";
RL J. Cell Biol. 161:33-39(2003).
RN [8]
RP FUNCTION, INTERACTION WITH ZYX; GRIP1; ENAH AND TALIN, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12571287; DOI=10.1242/jcs.00278;
RA Coutts A.S., MacKenzie E., Griffith E., Black D.M.;
RT "TES is a novel focal adhesion protein with a role in cell
RT spreading.";
RL J. Cell Sci. 116:897-906(2003).
RN [9]
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.,
RA Buerckstuemmer T., 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 [10]
RP INTERACTION WITH ALKBH4.
RX PubMed=23145062; DOI=10.1371/journal.pone.0049045;
RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M.,
RA Meza-Zepeda L.A., Falnes P.O.;
RT "Human ALKBH4 interacts with proteins associated with transcription.";
RL PLoS ONE 7:E49045-E49045(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 357-421 IN COMPLEX WITH ZINC
RP IONS AND ENAH.
RX PubMed=18158903; DOI=10.1016/j.molcel.2007.10.033;
RA Boeda B., Briggs D.C., Higgins T., Garvalov B.K., Fadden A.J.,
RA McDonald N.Q., Way M.;
RT "Tes, a specific Mena interacting partner, breaks the rules for EVH1
RT binding.";
RL Mol. Cell 28:1071-1082(2007).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 296-421 IN COMPLEX WITH ZINC
RP IONS; ENAH AND ACTL7A, MUTAGENESIS OF CYS-328, AND SUBUNIT.
RX PubMed=21278383; DOI=10.1074/jbc.M110.171264;
RA Boeda B., Knowles P.P., Briggs D.C., Murray-Rust J., Soriano E.,
RA Garvalov B.K., McDonald N.Q., Way M.;
RT "Molecular recognition of the Tes LIM2-3 domains by the actin-related
RT protein Arp7A.";
RL J. Biol. Chem. 286:11543-11554(2011).
CC -!- FUNCTION: Scaffold protein that may play a role in cell adhesion,
CC cell spreading and in the reorganization of the actin
CC cytoskeleton. Plays a role in the regulation of cell
CC proliferation. May act as a tumor suppressor. Inhibits tumor cell
CC growth.
CC -!- SUBUNIT: Interacts via LIM domain 1 with ZYX. Interacts (via LIM
CC domain 3) with ENAH and VASP. Interacts with ALKBH4, talin, actin,
CC alpha-actinin, GRIP1 and PXN. Interacts (via LIM domain 2) with
CC ACTL7A (via N-terminus). Heterodimer with ACTL7A; the heterodimer
CC interacts with ENAH to form a heterotrimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion.
CC Note=Detected along actin stress fibers.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UGI8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UGI8-2; Sequence=VSP_003122;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The N-terminal and the C-terminal halves of the protein
CC can associate with each other, thereby hindering interactions with
CC ZYX.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC -!- SIMILARITY: Contains 3 LIM zinc-binding domains.
CC -!- SIMILARITY: Contains 1 PET domain.
CC -----------------------------------------------------------------------
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DR EMBL; AF260225; AAG17635.1; -; Genomic_DNA.
DR EMBL; AF260225; AAG17636.1; -; Genomic_DNA.
DR EMBL; AF245356; AAG17612.1; -; mRNA.
DR EMBL; AF245357; AAG17613.1; -; mRNA.
DR EMBL; AJ250865; CAB65119.1; -; mRNA.
DR EMBL; AK021575; BAB13846.1; -; mRNA.
DR EMBL; AK291802; BAF84491.1; -; mRNA.
DR EMBL; AC073130; AAQ93367.1; -; Genomic_DNA.
DR EMBL; CH236947; EAL24365.1; -; Genomic_DNA.
DR EMBL; BC001451; AAH01451.1; -; mRNA.
DR RefSeq; NP_056456.1; NM_015641.3.
DR RefSeq; NP_690042.1; NM_152829.2.
DR UniGene; Hs.592286; -.
DR UniGene; Hs.664957; -.
DR PDB; 2IYB; X-ray; 2.35 A; E/F/G/H=357-421.
DR PDB; 2XQN; X-ray; 2.62 A; T=296-421.
DR PDBsum; 2IYB; -.
DR PDBsum; 2XQN; -.
DR ProteinModelPortal; Q9UGI8; -.
DR SMR; Q9UGI8; 258-421.
DR IntAct; Q9UGI8; 18.
DR MINT; MINT-2821159; -.
DR STRING; 9606.ENSP00000350937; -.
DR PhosphoSite; Q9UGI8; -.
DR DMDM; 17380320; -.
DR PaxDb; Q9UGI8; -.
DR PeptideAtlas; Q9UGI8; -.
DR PRIDE; Q9UGI8; -.
DR DNASU; 26136; -.
DR Ensembl; ENST00000358204; ENSP00000350937; ENSG00000135269.
DR Ensembl; ENST00000393481; ENSP00000377121; ENSG00000135269.
DR GeneID; 26136; -.
DR KEGG; hsa:26136; -.
DR UCSC; uc003vho.3; human.
DR CTD; 26136; -.
DR GeneCards; GC07P115850; -.
DR HGNC; HGNC:14620; TES.
DR HPA; CAB003690; -.
DR HPA; HPA015269; -.
DR HPA; HPA018123; -.
DR MIM; 606085; gene.
DR neXtProt; NX_Q9UGI8; -.
DR PharmGKB; PA37906; -.
DR eggNOG; NOG272178; -.
DR HOGENOM; HOG000231628; -.
DR HOVERGEN; HBG001038; -.
DR InParanoid; Q9UGI8; -.
DR OMA; VKLPREM; -.
DR OrthoDB; EOG7P8P7M; -.
DR PhylomeDB; Q9UGI8; -.
DR ChiTaRS; TES; human.
DR EvolutionaryTrace; Q9UGI8; -.
DR GeneWiki; Testin; -.
DR GenomeRNAi; 26136; -.
DR NextBio; 48175; -.
DR PRO; PR:Q9UGI8; -.
DR ArrayExpress; Q9UGI8; -.
DR Bgee; Q9UGI8; -.
DR CleanEx; HS_TES; -.
DR Genevestigator; Q9UGI8; -.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0043234; C:protein complex; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
DR Gene3D; 2.10.110.10; -; 3.
DR InterPro; IPR010442; PET_domain.
DR InterPro; IPR027683; Testin.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24211:SF1; PTHR24211:SF1; 1.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF06297; PET; 1.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS51303; PET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Complete proteome;
KW Cytoplasm; LIM domain; Metal-binding; Polymorphism;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1 421 Testin.
FT /FTId=PRO_0000075906.
FT DOMAIN 92 199 PET.
FT DOMAIN 234 297 LIM zinc-binding 1.
FT DOMAIN 299 359 LIM zinc-binding 2.
FT DOMAIN 362 421 LIM zinc-binding 3.
FT COMPBIAS 22 46 Cys-rich.
FT VAR_SEQ 1 9 Missing (in isoform 2).
FT /FTId=VSP_003122.
FT VARIANT 221 221 A -> V (in dbSNP:rs2272193).
FT /FTId=VAR_050170.
FT MUTAGEN 328 328 C->A: Abolishes interaction with ACTL7A.
FT MUTAGEN 391 391 C->A: Abolishes localization at focal
FT adhesions.
FT CONFLICT 132 132 K -> E (in Ref. 3; BAB13846).
FT TURN 302 304
FT STRAND 305 307
FT STRAND 313 316
FT STRAND 319 321
FT HELIX 323 325
FT TURN 329 331
FT STRAND 338 343
FT STRAND 346 349
FT HELIX 350 356
FT TURN 362 364
FT STRAND 365 368
FT STRAND 374 377
FT STRAND 380 383
FT TURN 384 387
FT TURN 392 394
FT STRAND 404 406
FT STRAND 409 413
FT HELIX 414 418
SQ SEQUENCE 421 AA; 47996 MW; AB9FF6669C50D492 CRC64;
MDLENKVKKM GLGHEQGFGA PCLKCKEKCE GFELHFWRKI CRNCKCGQEE HDVLLSNEED
RKVGKLFEDT KYTTLIAKLK SDGIPMYKRN VMILTNPVAA KKNVSINTVT YEWAPPVQNQ
ALARQYMQML PKEKQPVAGS EGAQYRKKQL AKQLPAHDQD PSKCHELSPR EVKEMEQFVK
KYKSEALGVG DVKLPCEMDA QGPKQMNIPG GDRSTPAAVG AMEDKSAEHK RTQYSCYCCK
LSMKEGDPAI YAERAGYDKL WHPACFVCST CHELLVDMIY FWKNEKLYCG RHYCDSEKPR
CAGCDELIFS NEYTQAENQN WHLKHFCCFD CDSILAGEIY VMVNDKPVCK PCYVKNHAVV
CQGCHNAIDP EVQRVTYNNF SWHASTECFL CSCCSKCLIG QKFMPVEGMV FCSVECKKRM
S
//
MIM
606085
*RECORD*
*FIELD* NO
606085
*FIELD* TI
*606085 TESTIS-DERIVED TRANSCRIPT; TES
;;TESTIN
*FIELD* TX
DESCRIPTION
TES belongs to a subgroup of LIM-only proteins that contain 3 C-terminal
read moreLIM domains and an N-terminal proline-rich region. Members of this
subfamily include mediators of intracellular signaling and determinants
of cytoskeletal and adhesion complex organization. TES is thought to be
a tumor suppressor gene that is inactivated primarily by transcriptional
silencing resulting from CpG island methylation (Tobias et al., 2001).
CLONING
By construction and sequencing of a BAC contig within the FRA7G region
at 7q31.2, Tatarelli et al. (2000) identified a novel gene which they
called TESTIN because of its homology to mouse testin. They isolated 3
human isoforms. Isoforms 1 and 2, which use exon 1a and differ in their
3-prime UTR, contain 7 exons and encode a deduced 421-amino acid protein
with a calculated molecular mass of 48 kD. Isoform 3, which uses exon
1b, encodes a deduced 412-amino acid protein with a calculated molecular
mass of 47 kD. Each of the isoforms contains 3 LIM domains in the C
terminus and shows 89% and 35% sequence identity with the mouse and C.
elegans homologs, respectively. Human TESTIN contains 7 putative
functional sites: 4 phosphorylation sites, a glycosylation site, a
myristylation site, and a cytochrome C heme-binding site. Northern blot
analysis of normal human tissues demonstrated ubiquitous expression of
an approximately 2.8-kb TESTIN transcript, which apparently corresponded
to isoforms 2 and 3. An approximately 1.5-kb transcript, corresponding
to isoform 1, was expressed at significantly higher levels in testis
than in other tissues.
FRA7G is a common aphidicolin-inducible fragile site at 7q31.2 showing
loss of heterozygosity in human malignancies. Tatarelli et al. (2000)
noted that a relationship between LIM proteins and cancer had been
observed in several studies. By RT-PCR analysis, they found lack of
TESTIN expression in 22% of cancer cell lines and 44% of the cell lines
derived from hematologic malignancies. They determined that in most of
these cases the inactivation of TESTIN expression was due to methylation
of a CpG island. Analysis of the TESTIN coding region in 26 tumor cell
lines revealed 3 missense mutations. The authors thus suggested that
TESTIN may represent a tumor suppressor gene.
Tobias et al. (2001) also cloned and characterized human TESTIN, which
they called TES. Mutation analysis of the coding TES exons in 21
human-derived cell lines revealed the presence of a frameshift mutation
in 1 allele in a breast cancer cell line. Methylation of the CpG island
at the 5-prime end of TES appeared to be a remarkably frequent finding,
occurring in 7 of 10 ovarian carcinomas and in each of 30 tumor-derived
cell lines tested. Moreover, forced expression of TES in HeLa or OVCAR5
cells resulted in a profound reduction in growth potential, as
determined by the colony formation assay. Tobias et al. (2001) suggested
that TES is a tumor suppressor gene that is inactivated primarily by
transcriptional silencing resulting from CpG island methylation.
GENE STRUCTURE
The TES gene contains 7 exons (Tatarelli et al., 2000, Tobias et al.,
2001).
MAPPING
Tatarelli et al. (2000) and Tobias et al. (2001) identified the TES gene
within the fragile site FRA7G at chromosome 7q31.2.
*FIELD* RF
1. Tatarelli, C.; Linnenbach, A.; Mimori, K.; Croce, C. M.: Characterization
of the human TESTIN gene localized in the FRA7G region at 7q31.2. Genomics 68:
1-12, 2000.
2. Tobias, E. S.; Hurlstone, A. F. L.; MacKenzie, E.; McFarlane, R.;
Black, D. M.: The TES gene at 7q31.1 is methylated in tumours and
encodes a novel growth-suppressing LIM domain protein. Oncogene 20:
2844-2853, 2001.
*FIELD* CN
Victor A. McKusick - updated: 7/20/2001
*FIELD* CD
Carol A. Bocchini: 7/6/2001
*FIELD* ED
alopez: 04/04/2012
alopez: 11/4/2003
cwells: 11/30/2001
cwells: 8/2/2001
carol: 7/20/2001
cwells: 7/9/2001
carol: 7/6/2001
*RECORD*
*FIELD* NO
606085
*FIELD* TI
*606085 TESTIS-DERIVED TRANSCRIPT; TES
;;TESTIN
*FIELD* TX
DESCRIPTION
TES belongs to a subgroup of LIM-only proteins that contain 3 C-terminal
read moreLIM domains and an N-terminal proline-rich region. Members of this
subfamily include mediators of intracellular signaling and determinants
of cytoskeletal and adhesion complex organization. TES is thought to be
a tumor suppressor gene that is inactivated primarily by transcriptional
silencing resulting from CpG island methylation (Tobias et al., 2001).
CLONING
By construction and sequencing of a BAC contig within the FRA7G region
at 7q31.2, Tatarelli et al. (2000) identified a novel gene which they
called TESTIN because of its homology to mouse testin. They isolated 3
human isoforms. Isoforms 1 and 2, which use exon 1a and differ in their
3-prime UTR, contain 7 exons and encode a deduced 421-amino acid protein
with a calculated molecular mass of 48 kD. Isoform 3, which uses exon
1b, encodes a deduced 412-amino acid protein with a calculated molecular
mass of 47 kD. Each of the isoforms contains 3 LIM domains in the C
terminus and shows 89% and 35% sequence identity with the mouse and C.
elegans homologs, respectively. Human TESTIN contains 7 putative
functional sites: 4 phosphorylation sites, a glycosylation site, a
myristylation site, and a cytochrome C heme-binding site. Northern blot
analysis of normal human tissues demonstrated ubiquitous expression of
an approximately 2.8-kb TESTIN transcript, which apparently corresponded
to isoforms 2 and 3. An approximately 1.5-kb transcript, corresponding
to isoform 1, was expressed at significantly higher levels in testis
than in other tissues.
FRA7G is a common aphidicolin-inducible fragile site at 7q31.2 showing
loss of heterozygosity in human malignancies. Tatarelli et al. (2000)
noted that a relationship between LIM proteins and cancer had been
observed in several studies. By RT-PCR analysis, they found lack of
TESTIN expression in 22% of cancer cell lines and 44% of the cell lines
derived from hematologic malignancies. They determined that in most of
these cases the inactivation of TESTIN expression was due to methylation
of a CpG island. Analysis of the TESTIN coding region in 26 tumor cell
lines revealed 3 missense mutations. The authors thus suggested that
TESTIN may represent a tumor suppressor gene.
Tobias et al. (2001) also cloned and characterized human TESTIN, which
they called TES. Mutation analysis of the coding TES exons in 21
human-derived cell lines revealed the presence of a frameshift mutation
in 1 allele in a breast cancer cell line. Methylation of the CpG island
at the 5-prime end of TES appeared to be a remarkably frequent finding,
occurring in 7 of 10 ovarian carcinomas and in each of 30 tumor-derived
cell lines tested. Moreover, forced expression of TES in HeLa or OVCAR5
cells resulted in a profound reduction in growth potential, as
determined by the colony formation assay. Tobias et al. (2001) suggested
that TES is a tumor suppressor gene that is inactivated primarily by
transcriptional silencing resulting from CpG island methylation.
GENE STRUCTURE
The TES gene contains 7 exons (Tatarelli et al., 2000, Tobias et al.,
2001).
MAPPING
Tatarelli et al. (2000) and Tobias et al. (2001) identified the TES gene
within the fragile site FRA7G at chromosome 7q31.2.
*FIELD* RF
1. Tatarelli, C.; Linnenbach, A.; Mimori, K.; Croce, C. M.: Characterization
of the human TESTIN gene localized in the FRA7G region at 7q31.2. Genomics 68:
1-12, 2000.
2. Tobias, E. S.; Hurlstone, A. F. L.; MacKenzie, E.; McFarlane, R.;
Black, D. M.: The TES gene at 7q31.1 is methylated in tumours and
encodes a novel growth-suppressing LIM domain protein. Oncogene 20:
2844-2853, 2001.
*FIELD* CN
Victor A. McKusick - updated: 7/20/2001
*FIELD* CD
Carol A. Bocchini: 7/6/2001
*FIELD* ED
alopez: 04/04/2012
alopez: 11/4/2003
cwells: 11/30/2001
cwells: 8/2/2001
carol: 7/20/2001
cwells: 7/9/2001
carol: 7/6/2001