Full text data of TSN
TSN
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Translin; 3.1.-.- (Component 3 of promoter of RISC; C3PO)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Translin; 3.1.-.- (Component 3 of promoter of RISC; C3PO)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15631
ID TSN_HUMAN Reviewed; 228 AA.
AC Q15631; B7Z3X8; Q5U0K7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Translin;
DE EC=3.1.-.-;
DE AltName: Full=Component 3 of promoter of RISC;
DE Short=C3PO;
GN Name=TSN;
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] (ISOFORM 1).
RX PubMed=7663511; DOI=10.1038/ng0695-167;
RA Aoki K., Suzuki K., Sugano T., Tasaka T., Nakahara K., Kuge O.,
RA Omori A., Kasai M.;
RT "A novel gene, Translin, encodes a recombination hotspot binding
RT protein associated with chromosomal translocations.";
RL Nat. Genet. 10:167-174(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thalamus;
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=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-215.
RX PubMed=9244443; DOI=10.1006/geno.1997.4796;
RA Aoki K., Inazawa J., Takahashi T., Nakahara K., Kasai M.;
RT "Genomic structure and chromosomal localization of the gene encoding
RT translin, a recombination hotspot binding protein.";
RL Genomics 43:237-241(1997).
RN [7]
RP FUNCTION.
RX PubMed=9111049; DOI=10.1074/jbc.272.17.11402;
RA Kasai M., Matsuzaki T., Katayanagi K., Omori A., Maziarz R.T.,
RA Strominger J.L., Aoki K., Suzuki K.;
RT "The translin ring specifically recognizes DNA ends at recombination
RT hot spots in the human genome.";
RL J. Biol. Chem. 272:11402-11407(1997).
RN [8]
RP DNA/RNA-BINDING REGION.
RX PubMed=10025964; DOI=10.1016/S0014-5793(99)00010-1;
RA Aoki K., Suzuki K., Ishida R., Kasai M.;
RT "The DNA binding activity of Translin is mediated by a basic region in
RT the ring-shaped structure conserved in evolution.";
RL FEBS Lett. 443:363-366(1999).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TSNAX.
RX PubMed=11801738;
RA Erdemir T., Bilican B., Oncel D., Goding C.R., Yavuzer U.;
RT "DNA damage-dependent interaction of the nuclear matrix protein C1D
RT with Translin-associated factor X (TRAX).";
RL J. Cell Sci. 115:207-216(2002).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-187 AND LYS-199, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TSNAX, FUNCTION
RP IN RISC ACTIVATION, AND SUBUNIT.
RX PubMed=21552258; DOI=10.1038/nsmb.2032;
RA Ye X., Huang N., Liu Y., Paroo Z., Huerta C., Li P., Chen S., Liu Q.,
RA Zhang H.;
RT "Structure of C3PO and mechanism of human RISC activation.";
RL Nat. Struct. Mol. Biol. 18:650-657(2011).
CC -!- FUNCTION: DNA-binding protein that specifically recognizes
CC consensus sequences at the breakpoint junctions in chromosomal
CC translocations, mostly involving immunoglobulin (Ig)/T-cell
CC receptor gene segments. Seems to recognize single-stranded DNA
CC ends generated by staggered breaks occurring at recombination hot
CC spots.
CC -!- FUNCTION: Exhibits both single-stranded and double-stranded
CC endoribonuclease activity. May act as an activator of RNA-induced
CC silencing complex (RISC) by facilitating endonucleolytic cleavage
CC of the siRNA passenger strand.
CC -!- SUBUNIT: Ring-shaped heterooctamer of six TSN and two TSNAX
CC subunits, DNA/RNA binding occurs inside the ring.
CC -!- INTERACTION:
CC Q14161:GIT2; NbExp=2; IntAct=EBI-1044160, EBI-1046878;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15631-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15631-2; Sequence=VSP_044937, VSP_044938;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the translin family.
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DR EMBL; X78627; CAA55341.1; -; mRNA.
DR EMBL; BT019490; AAV38297.1; -; mRNA.
DR EMBL; BT019491; AAV38298.1; -; mRNA.
DR EMBL; AK296469; BAH12364.1; -; mRNA.
DR EMBL; AC018737; AAY14831.1; -; Genomic_DNA.
DR EMBL; BC002359; AAH02359.1; -; mRNA.
DR EMBL; Y12563; CAA73150.1; -; Genomic_DNA.
DR EMBL; Y12564; CAA73150.1; JOINED; Genomic_DNA.
DR EMBL; Y12565; CAA73150.1; JOINED; Genomic_DNA.
DR EMBL; Y12566; CAA73150.1; JOINED; Genomic_DNA.
DR EMBL; Y12567; CAA73150.1; JOINED; Genomic_DNA.
DR PIR; S51738; S51738.
DR RefSeq; NP_001248330.1; NM_001261401.1.
DR RefSeq; NP_004613.1; NM_004622.2.
DR UniGene; Hs.75066; -.
DR PDB; 1J1J; X-ray; 2.20 A; A/B/C/D=1-228.
DR PDB; 3PJA; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I=1-228.
DR PDB; 3QB5; X-ray; 2.95 A; A/B/C=1-228.
DR PDBsum; 1J1J; -.
DR PDBsum; 3PJA; -.
DR PDBsum; 3QB5; -.
DR ProteinModelPortal; Q15631; -.
DR SMR; Q15631; 1-217.
DR DIP; DIP-42216N; -.
DR IntAct; Q15631; 2.
DR MINT; MINT-5002843; -.
DR STRING; 9606.ENSP00000374332; -.
DR PhosphoSite; Q15631; -.
DR DMDM; 6136060; -.
DR PaxDb; Q15631; -.
DR PeptideAtlas; Q15631; -.
DR PRIDE; Q15631; -.
DR DNASU; 7247; -.
DR Ensembl; ENST00000389682; ENSP00000374332; ENSG00000211460.
DR Ensembl; ENST00000536142; ENSP00000437728; ENSG00000211460.
DR GeneID; 7247; -.
DR KEGG; hsa:7247; -.
DR UCSC; uc010yze.2; human.
DR CTD; 7247; -.
DR GeneCards; GC02P122419; -.
DR HGNC; HGNC:12379; TSN.
DR MIM; 600575; gene.
DR neXtProt; NX_Q15631; -.
DR PharmGKB; PA37047; -.
DR eggNOG; NOG268068; -.
DR HOGENOM; HOG000198374; -.
DR HOVERGEN; HBG000373; -.
DR InParanoid; Q15631; -.
DR OMA; NQFWRWK; -.
DR PhylomeDB; Q15631; -.
DR ChiTaRS; TSN; human.
DR EvolutionaryTrace; Q15631; -.
DR GeneWiki; TSN_(gene); -.
DR GenomeRNAi; 7247; -.
DR NextBio; 28337; -.
DR PRO; PR:Q15631; -.
DR ArrayExpress; Q15631; -.
DR Bgee; Q15631; -.
DR CleanEx; HS_TSN; -.
DR Genevestigator; Q15631; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR Gene3D; 1.20.58.190; -; 1.
DR Gene3D; 1.20.58.200; -; 1.
DR InterPro; IPR002848; Translin.
DR InterPro; IPR016069; Translin_C.
DR InterPro; IPR016068; Translin_N.
DR PANTHER; PTHR10741; PTHR10741; 1.
DR Pfam; PF01997; Translin; 1.
DR SUPFAM; SSF74784; SSF74784; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; DNA-binding; Endonuclease; Hydrolase; Nuclease; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1 228 Translin.
FT /FTId=PRO_0000191683.
FT REGION 86 90 DNA/RNA binding.
FT REGION 177 198 Leucine-zipper (Potential).
FT MOD_RES 187 187 N6-acetyllysine.
FT MOD_RES 199 199 N6-acetyllysine.
FT VAR_SEQ 127 148 PDREKGFHLDVEDYLSGVLILA -> AVCQQRDCWRLLPTP
FT PHLHLHQ (in isoform 2).
FT /FTId=VSP_044937.
FT VAR_SEQ 149 228 Missing (in isoform 2).
FT /FTId=VSP_044938.
FT HELIX 3 42
FT HELIX 43 46
FT STRAND 47 51
FT HELIX 54 77
FT HELIX 81 83
FT HELIX 84 87
FT HELIX 88 90
FT HELIX 92 110
FT HELIX 116 123
FT STRAND 128 133
FT HELIX 137 160
FT HELIX 166 181
FT HELIX 189 195
FT HELIX 198 213
FT TURN 214 216
SQ SEQUENCE 228 AA; 26183 MW; 3CAAF20BED7C4939 CRC64;
MSVSEIFVEL QGFLAAEQDI REEIRKVVQS LEQTAREILT LLQGVHQGAG FQDIPKRCLK
AREHFGTVKT HLTSLKTKFP AEQYYRFHEH WRFVLQRLVF LAAFVVYLET ETLVTREAVT
EILGIEPDRE KGFHLDVEDY LSGVLILASE LSRLSVNSVT AGDYSRPLHI STFINELDSG
FRLLNLKNDS LRKRYDGLKY DVKKVEEVVY DLSIRGFNKE TAAACVEK
//
ID TSN_HUMAN Reviewed; 228 AA.
AC Q15631; B7Z3X8; Q5U0K7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Translin;
DE EC=3.1.-.-;
DE AltName: Full=Component 3 of promoter of RISC;
DE Short=C3PO;
GN Name=TSN;
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] (ISOFORM 1).
RX PubMed=7663511; DOI=10.1038/ng0695-167;
RA Aoki K., Suzuki K., Sugano T., Tasaka T., Nakahara K., Kuge O.,
RA Omori A., Kasai M.;
RT "A novel gene, Translin, encodes a recombination hotspot binding
RT protein associated with chromosomal translocations.";
RL Nat. Genet. 10:167-174(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thalamus;
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=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-215.
RX PubMed=9244443; DOI=10.1006/geno.1997.4796;
RA Aoki K., Inazawa J., Takahashi T., Nakahara K., Kasai M.;
RT "Genomic structure and chromosomal localization of the gene encoding
RT translin, a recombination hotspot binding protein.";
RL Genomics 43:237-241(1997).
RN [7]
RP FUNCTION.
RX PubMed=9111049; DOI=10.1074/jbc.272.17.11402;
RA Kasai M., Matsuzaki T., Katayanagi K., Omori A., Maziarz R.T.,
RA Strominger J.L., Aoki K., Suzuki K.;
RT "The translin ring specifically recognizes DNA ends at recombination
RT hot spots in the human genome.";
RL J. Biol. Chem. 272:11402-11407(1997).
RN [8]
RP DNA/RNA-BINDING REGION.
RX PubMed=10025964; DOI=10.1016/S0014-5793(99)00010-1;
RA Aoki K., Suzuki K., Ishida R., Kasai M.;
RT "The DNA binding activity of Translin is mediated by a basic region in
RT the ring-shaped structure conserved in evolution.";
RL FEBS Lett. 443:363-366(1999).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TSNAX.
RX PubMed=11801738;
RA Erdemir T., Bilican B., Oncel D., Goding C.R., Yavuzer U.;
RT "DNA damage-dependent interaction of the nuclear matrix protein C1D
RT with Translin-associated factor X (TRAX).";
RL J. Cell Sci. 115:207-216(2002).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-187 AND LYS-199, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TSNAX, FUNCTION
RP IN RISC ACTIVATION, AND SUBUNIT.
RX PubMed=21552258; DOI=10.1038/nsmb.2032;
RA Ye X., Huang N., Liu Y., Paroo Z., Huerta C., Li P., Chen S., Liu Q.,
RA Zhang H.;
RT "Structure of C3PO and mechanism of human RISC activation.";
RL Nat. Struct. Mol. Biol. 18:650-657(2011).
CC -!- FUNCTION: DNA-binding protein that specifically recognizes
CC consensus sequences at the breakpoint junctions in chromosomal
CC translocations, mostly involving immunoglobulin (Ig)/T-cell
CC receptor gene segments. Seems to recognize single-stranded DNA
CC ends generated by staggered breaks occurring at recombination hot
CC spots.
CC -!- FUNCTION: Exhibits both single-stranded and double-stranded
CC endoribonuclease activity. May act as an activator of RNA-induced
CC silencing complex (RISC) by facilitating endonucleolytic cleavage
CC of the siRNA passenger strand.
CC -!- SUBUNIT: Ring-shaped heterooctamer of six TSN and two TSNAX
CC subunits, DNA/RNA binding occurs inside the ring.
CC -!- INTERACTION:
CC Q14161:GIT2; NbExp=2; IntAct=EBI-1044160, EBI-1046878;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15631-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15631-2; Sequence=VSP_044937, VSP_044938;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the translin family.
CC -----------------------------------------------------------------------
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DR EMBL; X78627; CAA55341.1; -; mRNA.
DR EMBL; BT019490; AAV38297.1; -; mRNA.
DR EMBL; BT019491; AAV38298.1; -; mRNA.
DR EMBL; AK296469; BAH12364.1; -; mRNA.
DR EMBL; AC018737; AAY14831.1; -; Genomic_DNA.
DR EMBL; BC002359; AAH02359.1; -; mRNA.
DR EMBL; Y12563; CAA73150.1; -; Genomic_DNA.
DR EMBL; Y12564; CAA73150.1; JOINED; Genomic_DNA.
DR EMBL; Y12565; CAA73150.1; JOINED; Genomic_DNA.
DR EMBL; Y12566; CAA73150.1; JOINED; Genomic_DNA.
DR EMBL; Y12567; CAA73150.1; JOINED; Genomic_DNA.
DR PIR; S51738; S51738.
DR RefSeq; NP_001248330.1; NM_001261401.1.
DR RefSeq; NP_004613.1; NM_004622.2.
DR UniGene; Hs.75066; -.
DR PDB; 1J1J; X-ray; 2.20 A; A/B/C/D=1-228.
DR PDB; 3PJA; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I=1-228.
DR PDB; 3QB5; X-ray; 2.95 A; A/B/C=1-228.
DR PDBsum; 1J1J; -.
DR PDBsum; 3PJA; -.
DR PDBsum; 3QB5; -.
DR ProteinModelPortal; Q15631; -.
DR SMR; Q15631; 1-217.
DR DIP; DIP-42216N; -.
DR IntAct; Q15631; 2.
DR MINT; MINT-5002843; -.
DR STRING; 9606.ENSP00000374332; -.
DR PhosphoSite; Q15631; -.
DR DMDM; 6136060; -.
DR PaxDb; Q15631; -.
DR PeptideAtlas; Q15631; -.
DR PRIDE; Q15631; -.
DR DNASU; 7247; -.
DR Ensembl; ENST00000389682; ENSP00000374332; ENSG00000211460.
DR Ensembl; ENST00000536142; ENSP00000437728; ENSG00000211460.
DR GeneID; 7247; -.
DR KEGG; hsa:7247; -.
DR UCSC; uc010yze.2; human.
DR CTD; 7247; -.
DR GeneCards; GC02P122419; -.
DR HGNC; HGNC:12379; TSN.
DR MIM; 600575; gene.
DR neXtProt; NX_Q15631; -.
DR PharmGKB; PA37047; -.
DR eggNOG; NOG268068; -.
DR HOGENOM; HOG000198374; -.
DR HOVERGEN; HBG000373; -.
DR InParanoid; Q15631; -.
DR OMA; NQFWRWK; -.
DR PhylomeDB; Q15631; -.
DR ChiTaRS; TSN; human.
DR EvolutionaryTrace; Q15631; -.
DR GeneWiki; TSN_(gene); -.
DR GenomeRNAi; 7247; -.
DR NextBio; 28337; -.
DR PRO; PR:Q15631; -.
DR ArrayExpress; Q15631; -.
DR Bgee; Q15631; -.
DR CleanEx; HS_TSN; -.
DR Genevestigator; Q15631; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR Gene3D; 1.20.58.190; -; 1.
DR Gene3D; 1.20.58.200; -; 1.
DR InterPro; IPR002848; Translin.
DR InterPro; IPR016069; Translin_C.
DR InterPro; IPR016068; Translin_N.
DR PANTHER; PTHR10741; PTHR10741; 1.
DR Pfam; PF01997; Translin; 1.
DR SUPFAM; SSF74784; SSF74784; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; DNA-binding; Endonuclease; Hydrolase; Nuclease; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1 228 Translin.
FT /FTId=PRO_0000191683.
FT REGION 86 90 DNA/RNA binding.
FT REGION 177 198 Leucine-zipper (Potential).
FT MOD_RES 187 187 N6-acetyllysine.
FT MOD_RES 199 199 N6-acetyllysine.
FT VAR_SEQ 127 148 PDREKGFHLDVEDYLSGVLILA -> AVCQQRDCWRLLPTP
FT PHLHLHQ (in isoform 2).
FT /FTId=VSP_044937.
FT VAR_SEQ 149 228 Missing (in isoform 2).
FT /FTId=VSP_044938.
FT HELIX 3 42
FT HELIX 43 46
FT STRAND 47 51
FT HELIX 54 77
FT HELIX 81 83
FT HELIX 84 87
FT HELIX 88 90
FT HELIX 92 110
FT HELIX 116 123
FT STRAND 128 133
FT HELIX 137 160
FT HELIX 166 181
FT HELIX 189 195
FT HELIX 198 213
FT TURN 214 216
SQ SEQUENCE 228 AA; 26183 MW; 3CAAF20BED7C4939 CRC64;
MSVSEIFVEL QGFLAAEQDI REEIRKVVQS LEQTAREILT LLQGVHQGAG FQDIPKRCLK
AREHFGTVKT HLTSLKTKFP AEQYYRFHEH WRFVLQRLVF LAAFVVYLET ETLVTREAVT
EILGIEPDRE KGFHLDVEDY LSGVLILASE LSRLSVNSVT AGDYSRPLHI STFINELDSG
FRLLNLKNDS LRKRYDGLKY DVKKVEEVVY DLSIRGFNKE TAAACVEK
//
MIM
600575
*RECORD*
*FIELD* NO
600575
*FIELD* TI
*600575 TRANSLIN; TSN
;;RECOMBINATION HOTSPOT-ASSOCIATED FACTOR 1; RCHF1;;
TESTIS-BRAIN RNA-BINDING PROTEIN; TBRBP
read more*FIELD* TX
CLONING
Kasai et al. (1994) identified a protein they termed recombination
hotspot-associated factor (RcHF1), which specifically binds to the
signal-like sequences at the breakpoint junction of 8q24 and 1p32 in
acute lymphoblastic leukemia (ALL) patients carrying t(8;14)(q24;q11)
and t(1;14)(p32;q11) translocations involving the TCR delta-chain locus
(TCRD; see 186810). Aoki et al. (1994) showed that an analogous protein,
which they designated BCLF1, specifically binds to a target sequence
within the clustered breakpoint region of the BCL2 oncogene (151430) in
follicular lymphoma patients carrying t(14;18)(q32;q21) translocations.
It was proposed that these binding activities at recombination hotspot
regions may play a crucial role in chromosomal translocations in
lymphoid neoplasms. Aoki et al. (1995) purified the BCLF1 protein to
homogeneity and determined that it is identical to RcHF1. Molecular gene
cloning experiments revealed that the purified protein, which they named
translin (TSN), is a previously undescribed DNA-binding protein with no
significant similarity to known proteins. (The designation 'translin'
came from selected letters in 'translocation.') In addition, Aoki et al.
(1995) found that nuclear localization of translin was limited to
lymphoid cell lines with rearranged Ig and processes such as DNA repair,
replication, or recombination. In their native form, translin
polypeptides form a multimeric structure that is responsible for its DNA
binding activity.
GENE STRUCTURE
Aoki et al. (1997) found that the human and mouse translin genes have
identical genomic structures consisting of 6 exons, 5 introns, and a
GC-rich upstream region.
GENE FUNCTION
Badge et al. (2000) studied a subtelomeric region at 16p13.3 that
displays a 300-fold increase in crossovers compared to the genomic
average rate. Segregation analysis of CEPH and other pedigrees yielded 6
paternal crossover breakpoints in the approximately 85-kb interval
between the minisatellite loci D16S309 (MS205) and D16S83 (EKMDA2).
Three crossovers were mapped to within the same small (less than 3 kb)
interval, which did not colocalize with any tandem repeat array or
expressed sequence. Sequence analysis revealed the presence of
recombination-associated motifs and binding sites for translin. The
authors concluded that this locus represents an intense male-specific
recombination hotspot.
Hosaka et al. (2000) demonstrated that the presence of the translin
binding motif may be one of the important determinants for the location
of breakpoints in the TLS (137070) and CHOP (126337) genes which are
fused by translocation t(12;16) in liposarcomas.
Liu et al. (2009) reconstituted long double-stranded RNA- and duplex
siRNA-initiated RNA-induced silencing complex (RISC) activities with the
use of recombinant Drosophila Dicer-2 (see 606241), R2D2, and Ago2
(606229) proteins. They used this core reconstitution system to purify
an RNAi regulator that they termed C3PO (component 3 promoter of RISC),
a complex of translin and TRAX (602964). C3PO is a magnesium
ion-dependent endoribonuclease that promotes RISC activation by removing
siRNA passenger strand cleavage products. Liu et al. (2009) showed that
TRAX is unstable without translin and that TRAX is the catalytic subunit
of C3PO. Liu et al. (2009) concluded that their study established an in
vitro RNAi reconstitution system and identified C3PO as a key activator
of the core RNAi machinery.
MAPPING
By in situ hybridization and analysis of somatic cell hybrids, Aoki et
al. (1997) mapped the human TSN gene to 2q21.1.
*FIELD* RF
1. Aoki, K.; Inazawa, J.; Takahashi, T.; Nakahara, K.; Kasai, M.:
Genomic structure and chromosomal localization of the gene encoding
translin, a recombination hotspot binding protein. Genomics 43:
237-241, 1997.
2. Aoki, K.; Nakahara, K.; Ikegawa, C.; Seto, M.; Takahashi, T.; Minowada,
J.; Strominger, J. L.; Maziarz, R. T.; Kasai, M.: Nuclear proteins
binding to a novel target sequence within the recombination hotspot
regions of Bcl-2 and the immunoglobulin D(H) gene family. Oncogene 9:
1109-1115, 1994.
3. Aoki, K.; Suzuki, K.; Sugano, T.; Tasaka, T.; Nakahara, K.; Kuge,
O.; Omori, A.; Kasai, M.: A novel gene, 'Translin,' encodes a recombination
hotspot binding protein associated with chromosomal translocations. Nature
Genet. 10: 167-174, 1995.
4. Badge, R. M.; Yardley, J.; Jeffreys, A. J.; Armour, J. A. L.:
Crossover breakpoint mapping identifies a subtelomeric hotspot for
male meiotic recombination. Hum. Molec. Genet. 9: 1239-1244, 2000.
5. Hosaka, T.; Kanoe, H.; Nakayama, T.; Murakami, H.; Yamamoto, H.;
Nakamata, T.; Tsuboyama, T.; Oka, M.; Kasai, M.; Sasaki, M. S.; Nakamura,
T.; Toguchida, J.: Translin binds to the sequences adjacent to the
breakpoints of the TLS and CHOP genes in liposarcomas with translocation
t(12;16). Oncogene 19: 5821-5825, 2000.
6. Kasai, M.; Aoki, K.; Matsuo, Y.; Minowada, J.; Maziarz, R. T.;
Strominger, J. L.: Recombination hotspot associated factors specifically
recognize novel target sequences at the site of interchromosomal rearrangements
in T-ALL patients with t(8;14)(q24;q11)and (t(1;14)(p32;q11). Int.
Immun. 6: 1017-1025, 1994.
7. Liu, Y.; Ye, X.; Jiang, F.; Liang, C.; Chen, D.; Peng, J.; Kinch,
L. N.; Grishin, N. V.; Liu, Q.: C3PO, an endoribonuclease that promotes
RNAi by facilitating RISC activation. Science 325: 750-753, 2009.
*FIELD* CN
Ada Hamosh - updated: 9/1/2009
Victor A. McKusick - updated: 2/26/2001
George E. Tiller - updated: 7/10/2000
Carol A. Bocchini - updated: 2/28/1999
*FIELD* CD
Victor A. McKusick: 6/1/1995
*FIELD* ED
mgross: 10/07/2013
alopez: 9/10/2009
terry: 9/1/2009
cwells: 3/2/2001
terry: 2/26/2001
alopez: 7/10/2000
terry: 3/1/1999
carol: 2/28/1999
alopez: 5/21/1998
mark: 5/30/1997
terry: 6/8/1995
mark: 6/1/1995
*RECORD*
*FIELD* NO
600575
*FIELD* TI
*600575 TRANSLIN; TSN
;;RECOMBINATION HOTSPOT-ASSOCIATED FACTOR 1; RCHF1;;
TESTIS-BRAIN RNA-BINDING PROTEIN; TBRBP
read more*FIELD* TX
CLONING
Kasai et al. (1994) identified a protein they termed recombination
hotspot-associated factor (RcHF1), which specifically binds to the
signal-like sequences at the breakpoint junction of 8q24 and 1p32 in
acute lymphoblastic leukemia (ALL) patients carrying t(8;14)(q24;q11)
and t(1;14)(p32;q11) translocations involving the TCR delta-chain locus
(TCRD; see 186810). Aoki et al. (1994) showed that an analogous protein,
which they designated BCLF1, specifically binds to a target sequence
within the clustered breakpoint region of the BCL2 oncogene (151430) in
follicular lymphoma patients carrying t(14;18)(q32;q21) translocations.
It was proposed that these binding activities at recombination hotspot
regions may play a crucial role in chromosomal translocations in
lymphoid neoplasms. Aoki et al. (1995) purified the BCLF1 protein to
homogeneity and determined that it is identical to RcHF1. Molecular gene
cloning experiments revealed that the purified protein, which they named
translin (TSN), is a previously undescribed DNA-binding protein with no
significant similarity to known proteins. (The designation 'translin'
came from selected letters in 'translocation.') In addition, Aoki et al.
(1995) found that nuclear localization of translin was limited to
lymphoid cell lines with rearranged Ig and processes such as DNA repair,
replication, or recombination. In their native form, translin
polypeptides form a multimeric structure that is responsible for its DNA
binding activity.
GENE STRUCTURE
Aoki et al. (1997) found that the human and mouse translin genes have
identical genomic structures consisting of 6 exons, 5 introns, and a
GC-rich upstream region.
GENE FUNCTION
Badge et al. (2000) studied a subtelomeric region at 16p13.3 that
displays a 300-fold increase in crossovers compared to the genomic
average rate. Segregation analysis of CEPH and other pedigrees yielded 6
paternal crossover breakpoints in the approximately 85-kb interval
between the minisatellite loci D16S309 (MS205) and D16S83 (EKMDA2).
Three crossovers were mapped to within the same small (less than 3 kb)
interval, which did not colocalize with any tandem repeat array or
expressed sequence. Sequence analysis revealed the presence of
recombination-associated motifs and binding sites for translin. The
authors concluded that this locus represents an intense male-specific
recombination hotspot.
Hosaka et al. (2000) demonstrated that the presence of the translin
binding motif may be one of the important determinants for the location
of breakpoints in the TLS (137070) and CHOP (126337) genes which are
fused by translocation t(12;16) in liposarcomas.
Liu et al. (2009) reconstituted long double-stranded RNA- and duplex
siRNA-initiated RNA-induced silencing complex (RISC) activities with the
use of recombinant Drosophila Dicer-2 (see 606241), R2D2, and Ago2
(606229) proteins. They used this core reconstitution system to purify
an RNAi regulator that they termed C3PO (component 3 promoter of RISC),
a complex of translin and TRAX (602964). C3PO is a magnesium
ion-dependent endoribonuclease that promotes RISC activation by removing
siRNA passenger strand cleavage products. Liu et al. (2009) showed that
TRAX is unstable without translin and that TRAX is the catalytic subunit
of C3PO. Liu et al. (2009) concluded that their study established an in
vitro RNAi reconstitution system and identified C3PO as a key activator
of the core RNAi machinery.
MAPPING
By in situ hybridization and analysis of somatic cell hybrids, Aoki et
al. (1997) mapped the human TSN gene to 2q21.1.
*FIELD* RF
1. Aoki, K.; Inazawa, J.; Takahashi, T.; Nakahara, K.; Kasai, M.:
Genomic structure and chromosomal localization of the gene encoding
translin, a recombination hotspot binding protein. Genomics 43:
237-241, 1997.
2. Aoki, K.; Nakahara, K.; Ikegawa, C.; Seto, M.; Takahashi, T.; Minowada,
J.; Strominger, J. L.; Maziarz, R. T.; Kasai, M.: Nuclear proteins
binding to a novel target sequence within the recombination hotspot
regions of Bcl-2 and the immunoglobulin D(H) gene family. Oncogene 9:
1109-1115, 1994.
3. Aoki, K.; Suzuki, K.; Sugano, T.; Tasaka, T.; Nakahara, K.; Kuge,
O.; Omori, A.; Kasai, M.: A novel gene, 'Translin,' encodes a recombination
hotspot binding protein associated with chromosomal translocations. Nature
Genet. 10: 167-174, 1995.
4. Badge, R. M.; Yardley, J.; Jeffreys, A. J.; Armour, J. A. L.:
Crossover breakpoint mapping identifies a subtelomeric hotspot for
male meiotic recombination. Hum. Molec. Genet. 9: 1239-1244, 2000.
5. Hosaka, T.; Kanoe, H.; Nakayama, T.; Murakami, H.; Yamamoto, H.;
Nakamata, T.; Tsuboyama, T.; Oka, M.; Kasai, M.; Sasaki, M. S.; Nakamura,
T.; Toguchida, J.: Translin binds to the sequences adjacent to the
breakpoints of the TLS and CHOP genes in liposarcomas with translocation
t(12;16). Oncogene 19: 5821-5825, 2000.
6. Kasai, M.; Aoki, K.; Matsuo, Y.; Minowada, J.; Maziarz, R. T.;
Strominger, J. L.: Recombination hotspot associated factors specifically
recognize novel target sequences at the site of interchromosomal rearrangements
in T-ALL patients with t(8;14)(q24;q11)and (t(1;14)(p32;q11). Int.
Immun. 6: 1017-1025, 1994.
7. Liu, Y.; Ye, X.; Jiang, F.; Liang, C.; Chen, D.; Peng, J.; Kinch,
L. N.; Grishin, N. V.; Liu, Q.: C3PO, an endoribonuclease that promotes
RNAi by facilitating RISC activation. Science 325: 750-753, 2009.
*FIELD* CN
Ada Hamosh - updated: 9/1/2009
Victor A. McKusick - updated: 2/26/2001
George E. Tiller - updated: 7/10/2000
Carol A. Bocchini - updated: 2/28/1999
*FIELD* CD
Victor A. McKusick: 6/1/1995
*FIELD* ED
mgross: 10/07/2013
alopez: 9/10/2009
terry: 9/1/2009
cwells: 3/2/2001
terry: 2/26/2001
alopez: 7/10/2000
terry: 3/1/1999
carol: 2/28/1999
alopez: 5/21/1998
mark: 5/30/1997
terry: 6/8/1995
mark: 6/1/1995