TSNAX_HUMAN
ID TSNAX_HUMAN Reviewed; 290 AA.
AC Q99598; B1APC6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Translin-associated protein X;
DE AltName: Full=Translin-associated factor X;
GN Name=TSNAX; Synonyms=TRAX;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH TSN.
RC TISSUE=Spleen;
RX PubMed=9013868; DOI=10.1016/s0014-5793(96)01444-5;
RA Aoki K., Ishida R., Kasai M.;
RT "Isolation and characterization of a cDNA encoding a translin-like protein,
RT TRAX.";
RL FEBS Lett. 401:109-112(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Guyonnet Duperat V., Dupuy D., Stef M., Arveiler B.;
RT "Genomic structure of human translin-associated factor X (TRAX) gene.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Muscle;
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TSN; GOLGA3; TSNAXIP1;
RP SUN1 AND AKAP9.
RC TISSUE=Testis;
RX PubMed=12036294; DOI=10.1006/geno.2002.6779;
RA Bray J.D., Chennathukuzhi V.M., Hecht N.B.;
RT "Identification and characterization of cDNAs encoding four novel proteins
RT that interact with translin associated factor-X.";
RL Genomics 79:799-808(2002).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH C1D AND TSN.
RX PubMed=11801738; DOI=10.1242/jcs.115.1.207;
RA Erdemir T., Bilican B., Oncel D., Goding C.R., Yavuzer U.;
RT "DNA damage-dependent interaction of the nuclear matrix protein C1D with
RT Translin-associated factor X (TRAX).";
RL J. Cell Sci. 115:207-216(2002).
RN [9]
RP DNA-BINDING, AND SUBUNIT.
RX PubMed=15919079; DOI=10.1016/j.febslet.2005.05.007;
RA Gupta G.D., Makde R.D., Kamdar R.P., D'Souza J.S., Kulkarni M.G., Kumar V.,
RA Rao B.J.;
RT "Co-expressed recombinant human Translin-Trax complex binds DNA.";
RL FEBS Lett. 579:3141-3146(2005).
RN [10]
RP SUMOYLATION.
RX PubMed=15561718; DOI=10.1074/jbc.m411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-like
RT modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-279, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS), SUBUNIT, MAGNESIUM-BINDING SITES,
RP AND FUNCTION.
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: 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. {ECO:0000269|PubMed:12036294,
CC ECO:0000269|PubMed:21552258}.
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. {ECO:0000269|PubMed:11801738,
CC ECO:0000269|PubMed:12036294, ECO:0000269|PubMed:15919079,
CC ECO:0000269|PubMed:21552258, ECO:0000269|PubMed:9013868}.
CC -!- INTERACTION:
CC Q99598; Q12904: AIMP1; NbExp=3; IntAct=EBI-742638, EBI-1045802;
CC Q99598; P46379-2: BAG6; NbExp=3; IntAct=EBI-742638, EBI-10988864;
CC Q99598; Q00994: BEX3; NbExp=3; IntAct=EBI-742638, EBI-741753;
CC Q99598; Q8TDH9: BLOC1S5; NbExp=6; IntAct=EBI-742638, EBI-465861;
CC Q99598; Q9H257: CARD9; NbExp=5; IntAct=EBI-742638, EBI-751319;
CC Q99598; Q76N32-2: CEP68; NbExp=3; IntAct=EBI-742638, EBI-11975967;
CC Q99598; P28329-3: CHAT; NbExp=3; IntAct=EBI-742638, EBI-25837549;
CC Q99598; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-742638, EBI-3866319;
CC Q99598; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-742638, EBI-12593112;
CC Q99598; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-742638, EBI-11748557;
CC Q99598; P22607: FGFR3; NbExp=3; IntAct=EBI-742638, EBI-348399;
CC Q99598; O95257: GADD45G; NbExp=4; IntAct=EBI-742638, EBI-448202;
CC Q99598; P14136: GFAP; NbExp=3; IntAct=EBI-742638, EBI-744302;
CC Q99598; Q53GS7: GLE1; NbExp=3; IntAct=EBI-742638, EBI-1955541;
CC Q99598; Q9NW75-2: GPATCH2; NbExp=3; IntAct=EBI-742638, EBI-12068108;
CC Q99598; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-742638, EBI-717919;
CC Q99598; P06396: GSN; NbExp=3; IntAct=EBI-742638, EBI-351506;
CC Q99598; P26583: HMGB2; NbExp=3; IntAct=EBI-742638, EBI-1057009;
CC Q99598; P01112: HRAS; NbExp=3; IntAct=EBI-742638, EBI-350145;
CC Q99598; Q92993: KAT5; NbExp=3; IntAct=EBI-742638, EBI-399080;
CC Q99598; Q6P597: KLC3; NbExp=5; IntAct=EBI-742638, EBI-1643885;
CC Q99598; Q6P597-3: KLC3; NbExp=7; IntAct=EBI-742638, EBI-12076930;
CC Q99598; O14901: KLF11; NbExp=3; IntAct=EBI-742638, EBI-948266;
CC Q99598; Q15323: KRT31; NbExp=3; IntAct=EBI-742638, EBI-948001;
CC Q99598; O43679: LDB2; NbExp=4; IntAct=EBI-742638, EBI-2865580;
CC Q99598; O95751: LDOC1; NbExp=3; IntAct=EBI-742638, EBI-740738;
CC Q99598; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-742638, EBI-11742507;
CC Q99598; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-742638, EBI-741037;
CC Q99598; P35240: NF2; NbExp=3; IntAct=EBI-742638, EBI-1014472;
CC Q99598; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-742638, EBI-741158;
CC Q99598; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-742638, EBI-2811583;
CC Q99598; Q6P1K2: PMF1; NbExp=4; IntAct=EBI-742638, EBI-713832;
CC Q99598; Q99633: PRPF18; NbExp=3; IntAct=EBI-742638, EBI-2798416;
CC Q99598; P40937: RFC5; NbExp=3; IntAct=EBI-742638, EBI-712376;
CC Q99598; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-742638, EBI-9090795;
CC Q99598; Q16637: SMN2; NbExp=3; IntAct=EBI-742638, EBI-395421;
CC Q99598; O94964-4: SOGA1; NbExp=3; IntAct=EBI-742638, EBI-14083835;
CC Q99598; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-742638, EBI-5235340;
CC Q99598; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-742638, EBI-7082156;
CC Q99598; Q6PIF2: SYCE2; NbExp=3; IntAct=EBI-742638, EBI-11958386;
CC Q99598; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-742638, EBI-745392;
CC Q99598; Q99081: TCF12; NbExp=3; IntAct=EBI-742638, EBI-722877;
CC Q99598; Q99081-3: TCF12; NbExp=3; IntAct=EBI-742638, EBI-11952764;
CC Q99598; Q9NUJ3: TCP11L1; NbExp=3; IntAct=EBI-742638, EBI-2555179;
CC Q99598; Q15631: TSN; NbExp=14; IntAct=EBI-742638, EBI-1044160;
CC Q99598; Q9UK41-2: VPS28; NbExp=6; IntAct=EBI-742638, EBI-12146727;
CC Q99598; P61981: YWHAG; NbExp=3; IntAct=EBI-742638, EBI-359832;
CC Q99598; Q9Y649; NbExp=3; IntAct=EBI-742638, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Golgi apparatus
CC {ECO:0000250}. Nucleus. Note=Accumulate in the Golgi complex of mid-
CC late pachytene spermatocytes (By similarity). Expressed in the
CC cytoplasm in the presence of TSN. {ECO:0000250}.
CC -!- PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:15561718}.
CC -!- SIMILARITY: Belongs to the translin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X95073; CAA64469.1; -; mRNA.
DR EMBL; AF271269; AAK58640.1; -; Genomic_DNA.
DR EMBL; AF271267; AAK58640.1; JOINED; Genomic_DNA.
DR EMBL; AF271268; AAK58640.1; JOINED; Genomic_DNA.
DR EMBL; AK313068; BAG35896.1; -; mRNA.
DR EMBL; AL626763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471098; EAW69963.1; -; Genomic_DNA.
DR EMBL; BC010376; AAH10376.1; -; mRNA.
DR EMBL; BC011797; AAH11797.1; -; mRNA.
DR CCDS; CCDS1596.1; -.
DR RefSeq; NP_005990.1; NM_005999.2.
DR PDB; 3PJA; X-ray; 3.00 A; J/K/L=1-290.
DR PDB; 3QB5; X-ray; 2.95 A; K=1-290.
DR PDBsum; 3PJA; -.
DR PDBsum; 3QB5; -.
DR AlphaFoldDB; Q99598; -.
DR SMR; Q99598; -.
DR BioGRID; 113108; 133.
DR ComplexPortal; CPX-890; C3PO endoribonuclease complex.
DR DIP; DIP-29463N; -.
DR IntAct; Q99598; 132.
DR MINT; Q99598; -.
DR STRING; 9606.ENSP00000355599; -.
DR ChEMBL; CHEMBL4524025; -.
DR GlyGen; Q99598; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99598; -.
DR MetOSite; Q99598; -.
DR PhosphoSitePlus; Q99598; -.
DR BioMuta; TSNAX; -.
DR DMDM; 6136057; -.
DR EPD; Q99598; -.
DR jPOST; Q99598; -.
DR MassIVE; Q99598; -.
DR MaxQB; Q99598; -.
DR PaxDb; Q99598; -.
DR PeptideAtlas; Q99598; -.
DR PRIDE; Q99598; -.
DR ProteomicsDB; 78351; -.
DR Antibodypedia; 34686; 155 antibodies from 26 providers.
DR DNASU; 7257; -.
DR Ensembl; ENST00000366639.9; ENSP00000355599.3; ENSG00000116918.15.
DR GeneID; 7257; -.
DR KEGG; hsa:7257; -.
DR MANE-Select; ENST00000366639.9; ENSP00000355599.3; NM_005999.3; NP_005990.1.
DR UCSC; uc001huw.4; human.
DR CTD; 7257; -.
DR DisGeNET; 7257; -.
DR GeneCards; TSNAX; -.
DR HGNC; HGNC:12380; TSNAX.
DR HPA; ENSG00000116918; Low tissue specificity.
DR MIM; 602964; gene.
DR neXtProt; NX_Q99598; -.
DR OpenTargets; ENSG00000116918; -.
DR PharmGKB; PA37048; -.
DR VEuPathDB; HostDB:ENSG00000116918; -.
DR eggNOG; KOG3066; Eukaryota.
DR GeneTree; ENSGT00940000153568; -.
DR HOGENOM; CLU_067225_1_0_1; -.
DR InParanoid; Q99598; -.
DR OMA; DTCMETC; -.
DR OrthoDB; 1213910at2759; -.
DR PhylomeDB; Q99598; -.
DR TreeFam; TF323633; -.
DR PathwayCommons; Q99598; -.
DR Reactome; R-HSA-426486; Small interfering RNA (siRNA) biogenesis.
DR SignaLink; Q99598; -.
DR BioGRID-ORCS; 7257; 13 hits in 1081 CRISPR screens.
DR GeneWiki; TSNAX; -.
DR GenomeRNAi; 7257; -.
DR Pharos; Q99598; Tbio.
DR PRO; PR:Q99598; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q99598; protein.
DR Bgee; ENSG00000116918; Expressed in adrenal tissue and 211 other tissues.
DR ExpressionAtlas; Q99598; baseline and differential.
DR Genevisible; Q99598; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:1902555; C:endoribonuclease complex; IPI:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
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; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030422; P:siRNA processing; IDA:ComplexPortal.
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 3D-structure; Cytoplasm; Developmental protein; Differentiation;
KW DNA-binding; Golgi apparatus; Isopeptide bond; Magnesium; Metal-binding;
KW Nucleus; Reference proteome; Spermatogenesis; Ubl conjugation.
FT CHAIN 1..290
FT /note="Translin-associated protein X"
FT /id="PRO_0000191686"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..208
FT /note="Interaction with C1D"
FT /evidence="ECO:0000269|PubMed:11801738"
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 BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT HELIX 34..75
FT /evidence="ECO:0007829|PDB:3QB5"
FT HELIX 83..108
FT /evidence="ECO:0007829|PDB:3QB5"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3QB5"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3QB5"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3QB5"
FT HELIX 121..139
FT /evidence="ECO:0007829|PDB:3QB5"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:3QB5"
FT HELIX 184..207
FT /evidence="ECO:0007829|PDB:3QB5"
FT HELIX 213..231
FT /evidence="ECO:0007829|PDB:3QB5"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:3QB5"
FT HELIX 237..263
FT /evidence="ECO:0007829|PDB:3QB5"
SQ SEQUENCE 290 AA; 33112 MW; D38B0DD96B50C0B9 CRC64;
MSNKEGSGGF RKRKHDNFPH NQRREGKDVN SSSPVMLAFK SFQQELDARH DKYERLVKLS
RDITVESKRT IFLLHRITSA PDMEDILTES EIKLDGVRQK IFQVAQELSG EDMHQFHRAI
TTGLQEYVEA VSFQHFIKTR SLISMDEINK QLIFTTEDNG KENKTPSSDA QDKQFGTWRL
RVTPVDYLLG VADLTGELMR MCINSVGNGD IDTPFEVSQF LRQVYDGFSF IGNTGPYEVS
KKLYTLKQSL AKVENACYAL KVRGSEIPKH MLADVFSVKT EMIDQEEGIS
