Full text data of TSNAX
TSNAX
(TRAX)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Translin-associated protein X (Translin-associated factor X)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Translin-associated protein X (Translin-associated factor X)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q99598
ID TSNAX_HUMAN Reviewed; 290 AA.
AC Q99598; B1APC6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1997, sequence version 1.
DT 22-JAN-2014, entry version 114.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT protein, 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)
RT 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.,
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TSN; GOLGA3;
RP TSNAXIP1; 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
RT proteins 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;
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 [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.,
RA Kumar V., 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-
RT like 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.,
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 [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.,
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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS), SUBUNIT, MAGNESIUM-BINDING
RP SITES, 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
CC in the activation of the RNA-induced silencing complex (RISC).
CC Possible role in spermatogenesis.
CC -!- SUBUNIT: Ring-shaped heterooctamer of six TSN and two TSNAX
CC subunits. Interacts with GOLGA3, TSNAXIP1, SUN1 and AKAP9.
CC Interacts with the homodimeric form of C1D following gamma-
CC radiation. Interacts with TSN and C1D in a mutually exclusive
CC manner.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Golgi
CC apparatus (By similarity). Nucleus. Note=Accumulate in the Golgi
CC complex of mid-late pachytene spermatocytes (By similarity).
CC Expressed in the cytoplasm in the presence of TSN.
CC -!- PTM: Sumoylated with SUMO1.
CC -!- SIMILARITY: Belongs to the translin family.
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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; CAH70959.1; -; Genomic_DNA.
DR EMBL; AL445524; CAH70959.1; JOINED; Genomic_DNA.
DR EMBL; AL445524; CAH72107.1; -; Genomic_DNA.
DR EMBL; AL626763; CAH72107.1; JOINED; Genomic_DNA.
DR EMBL; CH471098; EAW69963.1; -; Genomic_DNA.
DR EMBL; BC010376; AAH10376.1; -; mRNA.
DR EMBL; BC011797; AAH11797.1; -; mRNA.
DR RefSeq; NP_005990.1; NM_005999.2.
DR UniGene; Hs.13318; -.
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 ProteinModelPortal; Q99598; -.
DR SMR; Q99598; 31-272.
DR DIP; DIP-29463N; -.
DR IntAct; Q99598; 19.
DR MINT; MINT-1347706; -.
DR STRING; 9606.ENSP00000355599; -.
DR PhosphoSite; Q99598; -.
DR DMDM; 6136057; -.
DR PaxDb; Q99598; -.
DR PeptideAtlas; Q99598; -.
DR PRIDE; Q99598; -.
DR DNASU; 7257; -.
DR Ensembl; ENST00000366639; ENSP00000355599; ENSG00000116918.
DR GeneID; 7257; -.
DR KEGG; hsa:7257; -.
DR UCSC; uc001huw.3; human.
DR CTD; 7257; -.
DR GeneCards; GC01P231664; -.
DR HGNC; HGNC:12380; TSNAX.
DR HPA; CAB034263; -.
DR HPA; HPA031054; -.
DR HPA; HPA031055; -.
DR MIM; 602964; gene.
DR neXtProt; NX_Q99598; -.
DR PharmGKB; PA37048; -.
DR eggNOG; COG2178; -.
DR HOGENOM; HOG000008075; -.
DR HOVERGEN; HBG059067; -.
DR InParanoid; Q99598; -.
DR OMA; CISSVGN; -.
DR OrthoDB; EOG7XWPPR; -.
DR PhylomeDB; Q99598; -.
DR ChiTaRS; TSNAX; human.
DR GeneWiki; TSNAX; -.
DR GenomeRNAi; 7257; -.
DR NextBio; 28373; -.
DR PRO; PR:Q99598; -.
DR ArrayExpress; Q99598; -.
DR Bgee; Q99598; -.
DR CleanEx; HS_TSNAX; -.
DR Genevestigator; Q99598; -.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008565; F:protein transporter activity; TAS:ProtInc.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
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; 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; Complete proteome; Cytoplasm; Developmental protein;
KW Differentiation; DNA-binding; Golgi apparatus; Magnesium;
KW Metal-binding; Nucleus; Reference proteome; Spermatogenesis;
KW Ubl conjugation.
FT CHAIN 1 290 Translin-associated protein X.
FT /FTId=PRO_0000191686.
FT REGION 73 208 Interaction with C1D.
FT METAL 129 129 Magnesium.
FT METAL 197 197 Magnesium.
FT HELIX 34 75
FT HELIX 83 108
FT STRAND 109 111
FT TURN 114 116
FT HELIX 117 119
FT HELIX 121 139
FT HELIX 145 150
FT HELIX 184 207
FT HELIX 213 231
FT HELIX 232 234
FT HELIX 237 263
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
//
ID TSNAX_HUMAN Reviewed; 290 AA.
AC Q99598; B1APC6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1997, sequence version 1.
DT 22-JAN-2014, entry version 114.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT protein, 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)
RT 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.,
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TSN; GOLGA3;
RP TSNAXIP1; 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
RT proteins 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;
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 [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.,
RA Kumar V., 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-
RT like 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.,
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 [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.,
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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS), SUBUNIT, MAGNESIUM-BINDING
RP SITES, 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
CC in the activation of the RNA-induced silencing complex (RISC).
CC Possible role in spermatogenesis.
CC -!- SUBUNIT: Ring-shaped heterooctamer of six TSN and two TSNAX
CC subunits. Interacts with GOLGA3, TSNAXIP1, SUN1 and AKAP9.
CC Interacts with the homodimeric form of C1D following gamma-
CC radiation. Interacts with TSN and C1D in a mutually exclusive
CC manner.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Golgi
CC apparatus (By similarity). Nucleus. Note=Accumulate in the Golgi
CC complex of mid-late pachytene spermatocytes (By similarity).
CC Expressed in the cytoplasm in the presence of TSN.
CC -!- PTM: Sumoylated with SUMO1.
CC -!- SIMILARITY: Belongs to the translin family.
CC -----------------------------------------------------------------------
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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; CAH70959.1; -; Genomic_DNA.
DR EMBL; AL445524; CAH70959.1; JOINED; Genomic_DNA.
DR EMBL; AL445524; CAH72107.1; -; Genomic_DNA.
DR EMBL; AL626763; CAH72107.1; JOINED; Genomic_DNA.
DR EMBL; CH471098; EAW69963.1; -; Genomic_DNA.
DR EMBL; BC010376; AAH10376.1; -; mRNA.
DR EMBL; BC011797; AAH11797.1; -; mRNA.
DR RefSeq; NP_005990.1; NM_005999.2.
DR UniGene; Hs.13318; -.
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 ProteinModelPortal; Q99598; -.
DR SMR; Q99598; 31-272.
DR DIP; DIP-29463N; -.
DR IntAct; Q99598; 19.
DR MINT; MINT-1347706; -.
DR STRING; 9606.ENSP00000355599; -.
DR PhosphoSite; Q99598; -.
DR DMDM; 6136057; -.
DR PaxDb; Q99598; -.
DR PeptideAtlas; Q99598; -.
DR PRIDE; Q99598; -.
DR DNASU; 7257; -.
DR Ensembl; ENST00000366639; ENSP00000355599; ENSG00000116918.
DR GeneID; 7257; -.
DR KEGG; hsa:7257; -.
DR UCSC; uc001huw.3; human.
DR CTD; 7257; -.
DR GeneCards; GC01P231664; -.
DR HGNC; HGNC:12380; TSNAX.
DR HPA; CAB034263; -.
DR HPA; HPA031054; -.
DR HPA; HPA031055; -.
DR MIM; 602964; gene.
DR neXtProt; NX_Q99598; -.
DR PharmGKB; PA37048; -.
DR eggNOG; COG2178; -.
DR HOGENOM; HOG000008075; -.
DR HOVERGEN; HBG059067; -.
DR InParanoid; Q99598; -.
DR OMA; CISSVGN; -.
DR OrthoDB; EOG7XWPPR; -.
DR PhylomeDB; Q99598; -.
DR ChiTaRS; TSNAX; human.
DR GeneWiki; TSNAX; -.
DR GenomeRNAi; 7257; -.
DR NextBio; 28373; -.
DR PRO; PR:Q99598; -.
DR ArrayExpress; Q99598; -.
DR Bgee; Q99598; -.
DR CleanEx; HS_TSNAX; -.
DR Genevestigator; Q99598; -.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008565; F:protein transporter activity; TAS:ProtInc.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
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; 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; Complete proteome; Cytoplasm; Developmental protein;
KW Differentiation; DNA-binding; Golgi apparatus; Magnesium;
KW Metal-binding; Nucleus; Reference proteome; Spermatogenesis;
KW Ubl conjugation.
FT CHAIN 1 290 Translin-associated protein X.
FT /FTId=PRO_0000191686.
FT REGION 73 208 Interaction with C1D.
FT METAL 129 129 Magnesium.
FT METAL 197 197 Magnesium.
FT HELIX 34 75
FT HELIX 83 108
FT STRAND 109 111
FT TURN 114 116
FT HELIX 117 119
FT HELIX 121 139
FT HELIX 145 150
FT HELIX 184 207
FT HELIX 213 231
FT HELIX 232 234
FT HELIX 237 263
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
//
MIM
602964
*RECORD*
*FIELD* NO
602964
*FIELD* TI
*602964 TRANSLIN-ASSOCIATED FACTOR X; TSNAX
;;TRAX
*FIELD* TX
CLONING
Translin (TSN; 600575) is a DNA-binding protein that specifically binds
read moreto consensus sequences at breakpoint junctions of chromosomal
translocations in many cases of lymphoid malignancies. Aoki et al.
(1997) used a yeast 2-hybrid system to screen a human spleen cDNA
library for potential interactions of TSN with other proteins. They
isolated a TSNAX cDNA, termed TRAX (translin-associated factor X) by the
authors, whose product specifically interacted with TSN in
cotransformation and in vitro interaction assays. The cDNA encodes a
putative 290-amino acid protein with a predicted molecular mass of 33
kD. The protein contains a heptad repeat of hydrophobic amino acids
consistent with the hypothetical leucine zipper structure. The authors
found 28% amino acid sequence identity between TSNAX and TSN, with 38%
identity in the C-terminal regions. Northern blot analysis revealed a
single TSNAX transcript of 2.7 kb, with a tissue distribution similar to
that of the TSN transcript.
GENE FUNCTION
Liu et al. (2009) reconstituted long double-stranded RNA- and duplex
siRNA-initiated RISC (RNA-induced silencing complex) 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. 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.
GENE STRUCTURE
Meng et al. (2000) determined that the genomic structure of TSNAX is
similar to that of TSN, consisting of 6 exons encompassing approximately
27 kb of genomic DNA.
MAPPING
By fluorescence in situ hybridization, Meng et al. (2000) mapped the
TSNAX gene to chromosome 1q41.
MOLECULAR GENETICS
Cannon et al. (2005) conducted a population-based twin cohort study in
Finland to examine the association of SNPs of DISC1 (605210) and TRAX
with schizophrenia (SCZD9; 604906) and several endophenotypic traits
thought to be involved in the disease pathogenesis. Two hundred and
thirty-six subjects consisting of 7 pairs concordant for schizophrenia
(6 monozygotic, 1 dizygotic), 52 pairs discordant for schizophrenia (20
monozygotic, 32 dizygotic), and 59 demographically balanced normal pairs
(28 monozygotic, 31 dizygotic) were drawn from a twin cohort consisting
of all same-sex twins born in Finland from 1940 through 1957. Diagnosis
was confirmed, and performance measurements on neurocognitive tests of
short- and long-term memory as well as gray matter volume measurements
as assessed on MRI images were recorded. A common haplotype
incorporating 3 SNPs near the translocation breakpoint of DISC1 (HEP1;
odds ratio, 2.6, p = 0.02) and a rare haplotype incorporating 4 markers
from the DISC1 and TRAX genes (combined HEP2/HEP3; odds ratio, 13.0, p =
0.001) were significantly overrepresented among individuals with
schizophrenia. These haplotypes were also associated with several
quantitative and endophenotypic traits including impairments in short-
and long-term memory, functioning, and reduced gray matter density in
the prefrontal cortex.
*FIELD* RF
1. Aoki, K.; Ishida, R.; Kasai, M.: Isolation and characterization
of a cDNA encoding a translin-like protein, TRAX. FEBS Lett. 401:
109-112, 1997.
2. Cannon, T. D.; Hennah, W.; van Erp, T. G. M.; Thompson, P. M.;
Lonnqvist, J.; Huttenen, M.; Gasperoni, T.; Tuulio-Henriksson, A.;
Pirkola, T.; Toga, A. W.; Kaprio, J.; Mazziotta, J.; Peltonen, L.
: Association of DISC1/TRAX haplotypes with schizophrenia, reduced
prefrontal gray matter, and impaired short- and long-term memory. Arch.
Gen. Psychiat. 62: 1205-1213, 2005.
3. 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.
4. Meng, G.; Aoki, K.; Tokura, K.; Nakahara, K.; Inazawa, J.; Kasai,
M.: Genomic structure and chromosomal localization of the gene encoding
TRAX, a translin-associated factor X. J. Hum. Genet. 45: 305-308,
2000.
*FIELD* CN
Ada Hamosh - updated: 9/1/2009
John Logan Black, III - updated: 11/30/2007
Victor A. McKusick - updated: 12/6/2000
*FIELD* CD
Sheryl A. Jankowski: 8/12/1998
*FIELD* ED
alopez: 09/10/2009
terry: 9/1/2009
carol: 11/30/2007
carol: 12/6/2000
carol: 8/13/1998
*RECORD*
*FIELD* NO
602964
*FIELD* TI
*602964 TRANSLIN-ASSOCIATED FACTOR X; TSNAX
;;TRAX
*FIELD* TX
CLONING
Translin (TSN; 600575) is a DNA-binding protein that specifically binds
read moreto consensus sequences at breakpoint junctions of chromosomal
translocations in many cases of lymphoid malignancies. Aoki et al.
(1997) used a yeast 2-hybrid system to screen a human spleen cDNA
library for potential interactions of TSN with other proteins. They
isolated a TSNAX cDNA, termed TRAX (translin-associated factor X) by the
authors, whose product specifically interacted with TSN in
cotransformation and in vitro interaction assays. The cDNA encodes a
putative 290-amino acid protein with a predicted molecular mass of 33
kD. The protein contains a heptad repeat of hydrophobic amino acids
consistent with the hypothetical leucine zipper structure. The authors
found 28% amino acid sequence identity between TSNAX and TSN, with 38%
identity in the C-terminal regions. Northern blot analysis revealed a
single TSNAX transcript of 2.7 kb, with a tissue distribution similar to
that of the TSN transcript.
GENE FUNCTION
Liu et al. (2009) reconstituted long double-stranded RNA- and duplex
siRNA-initiated RISC (RNA-induced silencing complex) 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. 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.
GENE STRUCTURE
Meng et al. (2000) determined that the genomic structure of TSNAX is
similar to that of TSN, consisting of 6 exons encompassing approximately
27 kb of genomic DNA.
MAPPING
By fluorescence in situ hybridization, Meng et al. (2000) mapped the
TSNAX gene to chromosome 1q41.
MOLECULAR GENETICS
Cannon et al. (2005) conducted a population-based twin cohort study in
Finland to examine the association of SNPs of DISC1 (605210) and TRAX
with schizophrenia (SCZD9; 604906) and several endophenotypic traits
thought to be involved in the disease pathogenesis. Two hundred and
thirty-six subjects consisting of 7 pairs concordant for schizophrenia
(6 monozygotic, 1 dizygotic), 52 pairs discordant for schizophrenia (20
monozygotic, 32 dizygotic), and 59 demographically balanced normal pairs
(28 monozygotic, 31 dizygotic) were drawn from a twin cohort consisting
of all same-sex twins born in Finland from 1940 through 1957. Diagnosis
was confirmed, and performance measurements on neurocognitive tests of
short- and long-term memory as well as gray matter volume measurements
as assessed on MRI images were recorded. A common haplotype
incorporating 3 SNPs near the translocation breakpoint of DISC1 (HEP1;
odds ratio, 2.6, p = 0.02) and a rare haplotype incorporating 4 markers
from the DISC1 and TRAX genes (combined HEP2/HEP3; odds ratio, 13.0, p =
0.001) were significantly overrepresented among individuals with
schizophrenia. These haplotypes were also associated with several
quantitative and endophenotypic traits including impairments in short-
and long-term memory, functioning, and reduced gray matter density in
the prefrontal cortex.
*FIELD* RF
1. Aoki, K.; Ishida, R.; Kasai, M.: Isolation and characterization
of a cDNA encoding a translin-like protein, TRAX. FEBS Lett. 401:
109-112, 1997.
2. Cannon, T. D.; Hennah, W.; van Erp, T. G. M.; Thompson, P. M.;
Lonnqvist, J.; Huttenen, M.; Gasperoni, T.; Tuulio-Henriksson, A.;
Pirkola, T.; Toga, A. W.; Kaprio, J.; Mazziotta, J.; Peltonen, L.
: Association of DISC1/TRAX haplotypes with schizophrenia, reduced
prefrontal gray matter, and impaired short- and long-term memory. Arch.
Gen. Psychiat. 62: 1205-1213, 2005.
3. 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.
4. Meng, G.; Aoki, K.; Tokura, K.; Nakahara, K.; Inazawa, J.; Kasai,
M.: Genomic structure and chromosomal localization of the gene encoding
TRAX, a translin-associated factor X. J. Hum. Genet. 45: 305-308,
2000.
*FIELD* CN
Ada Hamosh - updated: 9/1/2009
John Logan Black, III - updated: 11/30/2007
Victor A. McKusick - updated: 12/6/2000
*FIELD* CD
Sheryl A. Jankowski: 8/12/1998
*FIELD* ED
alopez: 09/10/2009
terry: 9/1/2009
carol: 11/30/2007
carol: 12/6/2000
carol: 8/13/1998