TSNAX_MOUSE
ID TSNAX_MOUSE Reviewed; 290 AA.
AC Q9QZE7; Q3UJR2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Translin-associated protein X;
DE AltName: Full=Translin-associated factor X;
GN Name=Tsnax; Synonyms=Trax;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10790540; DOI=10.1007/s003350010074;
RA Devon R.S., Taylor M.S., Millar J.K., Porteous D.J.;
RT "Isolation and characterization of the mouse translin-associated protein X
RT (Trax) gene.";
RL Mamm. Genome 11:395-398(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GOLGA3.
RX PubMed=15314092; DOI=10.1369/jhc.4b6304.2004;
RA Matsuda M., Kondo M., Kashiwabara S., Yoshihara M., Sutou S., Matsukuma S.;
RT "Co-localization of Trax and Mea2 in Golgi complex of pachytene
RT spermatocytes in the mouse.";
RL J. Histochem. Cytochem. 52:1245-1248(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts in combination with TSN as an endonuclease involved in
CC the activation of the RNA-induced silencing complex (RISC). Possible
CC role in spermatogenesis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Ring-shaped heterooctamer of six TSN and two TSNAX subunits.
CC Interacts with GOLGA3, TSNAXIP1, SUN1 and AKAP9. Interacts with the
CC homodimeric form of C1D following gamma-radiation. Interacts with TSN
CC and C1D in a mutually exclusive manner (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9QZE7; P30543: Adora2a; Xeno; NbExp=6; IntAct=EBI-2910751, EBI-2902822;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC Golgi apparatus {ECO:0000269|PubMed:15314092}. Nucleus {ECO:0000250}.
CC Note=Expressed in the cytoplasm in the presence of TSN (By similarity).
CC Accumulate in the Golgi complex of mid-late pachytene spermatocytes.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, lung, liver, kidney and
CC testis. {ECO:0000269|PubMed:10790540}.
CC -!- PTM: Sumoylated with SUMO1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the translin family. {ECO:0000305}.
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DR EMBL; AF187040; AAF05529.1; -; mRNA.
DR EMBL; AK030407; BAC26948.1; -; mRNA.
DR EMBL; AK146339; BAE27093.1; -; mRNA.
DR EMBL; BC004611; AAH04611.1; -; mRNA.
DR CCDS; CCDS22778.1; -.
DR RefSeq; NP_058605.1; NM_016909.2.
DR AlphaFoldDB; Q9QZE7; -.
DR SMR; Q9QZE7; -.
DR BioGRID; 207317; 25.
DR ComplexPortal; CPX-4629; C3PO endoribonuclease complex.
DR IntAct; Q9QZE7; 2.
DR STRING; 10090.ENSMUSP00000075290; -.
DR iPTMnet; Q9QZE7; -.
DR PhosphoSitePlus; Q9QZE7; -.
DR EPD; Q9QZE7; -.
DR jPOST; Q9QZE7; -.
DR MaxQB; Q9QZE7; -.
DR PaxDb; Q9QZE7; -.
DR PeptideAtlas; Q9QZE7; -.
DR PRIDE; Q9QZE7; -.
DR ProteomicsDB; 297727; -.
DR DNASU; 53424; -.
DR Ensembl; ENSMUST00000075896; ENSMUSP00000075290; ENSMUSG00000056820.
DR GeneID; 53424; -.
DR KEGG; mmu:53424; -.
DR UCSC; uc009nxz.1; mouse.
DR CTD; 7257; -.
DR MGI; MGI:1855672; Tsnax.
DR VEuPathDB; HostDB:ENSMUSG00000056820; -.
DR eggNOG; KOG3066; Eukaryota.
DR GeneTree; ENSGT00940000153568; -.
DR HOGENOM; CLU_067225_1_0_1; -.
DR InParanoid; Q9QZE7; -.
DR OMA; DTCMETC; -.
DR OrthoDB; 1213910at2759; -.
DR PhylomeDB; Q9QZE7; -.
DR TreeFam; TF323633; -.
DR Reactome; R-MMU-426486; Small interfering RNA (siRNA) biogenesis.
DR BioGRID-ORCS; 53424; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Tsnax; mouse.
DR PRO; PR:Q9QZE7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9QZE7; protein.
DR Bgee; ENSMUSG00000056820; Expressed in superior frontal gyrus and 260 other tissues.
DR ExpressionAtlas; Q9QZE7; baseline and differential.
DR Genevisible; Q9QZE7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:1902555; C:endoribonuclease complex; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031687; F:A2A adenosine receptor binding; ISO:MGI.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030422; P:siRNA processing; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.190; -; 1.
DR Gene3D; 1.20.58.200; -; 1.
DR InterPro; IPR016069; Translin_C.
DR InterPro; IPR002848; Translin_fam.
DR InterPro; IPR016068; Translin_N.
DR InterPro; IPR036081; Translin_sf.
DR PANTHER; PTHR10741; PTHR10741; 1.
DR Pfam; PF01997; Translin; 1.
DR SUPFAM; SSF74784; SSF74784; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW Golgi apparatus; Isopeptide bond; Magnesium; Metal-binding; Nucleus;
KW Reference proteome; Spermatogenesis; Ubl conjugation.
FT CHAIN 1..290
FT /note="Translin-associated protein X"
FT /id="PRO_0000191687"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..208
FT /note="Interaction with C1D"
FT /evidence="ECO:0000250"
FT COMPBIAS 7..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99598"
SQ SEQUENCE 290 AA; 32926 MW; 62038133C46B7952 CRC64;
MNGKEGPGGF RKRKHDTFPH NQRREGKDAS LSSPVMLAFK SFQQELDARH DKYERLVKLS
RDITVESKRT IFLLHRITSA PDMEEILTES ESKLDGVRQK ILQVAQELSG EDMHQFHRAV
TTGLQEYVEA VSFQHFIKTR SLISMEEINK QLTFTAEDSG KESKTPPAEG QEKQLVTWRL
KLTPVDYLLG VADLTGELMR MCINSVGNGD IDTPFEVSQF LRQVYDGFSF IGNTGPYEVS
KKLYTLKQSL AKVENACYAL KVRGSEIPKH MLADVFSVKT DMIDQEESIS
