Full text data of FTSJ1
FTSJ1
[Confidence: low (only semi-automatic identification from reviews)]
Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase; 2.1.1.205 (2'-O-ribose RNA methyltransferase TRM7 homolog; Protein ftsJ homolog 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase; 2.1.1.205 (2'-O-ribose RNA methyltransferase TRM7 homolog; Protein ftsJ homolog 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UET6
ID TRM7_HUMAN Reviewed; 329 AA.
AC Q9UET6; B2RCJ0; O75670;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2000, sequence version 2.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase;
DE EC=2.1.1.205;
DE AltName: Full=2'-O-ribose RNA methyltransferase TRM7 homolog;
DE AltName: Full=Protein ftsJ homolog 1;
GN Name=FTSJ1; ORFNames=JM23;
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 2).
RA Pengue G., Lutfiyya L.L., Mazzarella R.;
RT "A human and yeast gene involved in cell division.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A.,
RA Meindl A.;
RT "Transcription map in Xp11.23.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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] (ISOFORM 1).
RC TISSUE=Lymph;
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 INVOLVEMENT IN MRX44, AND TISSUE SPECIFICITY.
RX PubMed=15162322; DOI=10.1086/422507;
RA Freude K., Hoffmann K., Jensen L.-R., Delatycki M.B., des Portes V.,
RA Moser B., Hamel B.C.J., van Bokhoven H., Moraine C., Fryns J.-P.,
RA Chelly J., Gecz J., Lenzner S., Kalscheuer V.M., Ropers H.-H.;
RT "Mutations in the FTSJ1 gene coding for a novel S-adenosylmethionine-
RT binding protein cause nonsyndromic X-linked mental retardation.";
RL Am. J. Hum. Genet. 75:305-309(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(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).
CC -!- FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions
CC 32 and 34 of the tRNA anticodon loop of substrate tRNAs (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine +
CC cytidine(32)/guanosine(34) in tRNA = S-adenosyl-L-homocysteine +
CC 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UET6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UET6-2; Sequence=VSP_041419;
CC -!- TISSUE SPECIFICITY: Found in fetal brain, lung, liver and kidney.
CC In the adult brain, expressed in amygdala, caudate nucleus, corpus
CC callosum, hippocampus and thalamus.
CC -!- DISEASE: Mental retardation, X-linked 44 (MRX44) [MIM:309549]: A
CC disorder characterized by significantly below average general
CC intellectual functioning associated with impairments in adaptive
CC behavior and manifested during the developmental period.
CC Intellectual deficiency is the only primary symptom of non-
CC syndromic X-linked mental retardation, while syndromic mental
CC retardation presents with associated physical, neurological and/or
CC psychiatric manifestations. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmE
CC family. TRM7 subfamily.
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/FTSJ1";
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DR EMBL; AF063015; AAC33734.1; -; mRNA.
DR EMBL; AJ005892; CAA06749.1; -; mRNA.
DR EMBL; AK315138; BAG37587.1; -; mRNA.
DR EMBL; AF196972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471224; EAW50782.1; -; Genomic_DNA.
DR EMBL; BC023584; AAH23584.1; -; mRNA.
DR RefSeq; NP_001269086.1; NM_001282157.1.
DR RefSeq; NP_036412.1; NM_012280.3.
DR RefSeq; NP_803188.1; NM_177439.2.
DR RefSeq; XP_005272652.1; XM_005272595.1.
DR RefSeq; XP_005278087.1; XM_005278030.1.
DR UniGene; Hs.23170; -.
DR ProteinModelPortal; Q9UET6; -.
DR SMR; Q9UET6; 20-201.
DR IntAct; Q9UET6; 1.
DR STRING; 9606.ENSP00000326948; -.
DR PhosphoSite; Q9UET6; -.
DR DMDM; 12643879; -.
DR PaxDb; Q9UET6; -.
DR PRIDE; Q9UET6; -.
DR DNASU; 24140; -.
DR Ensembl; ENST00000019019; ENSP00000019019; ENSG00000068438.
DR Ensembl; ENST00000348411; ENSP00000326948; ENSG00000068438.
DR Ensembl; ENST00000456787; ENSP00000415457; ENSG00000068438.
DR Ensembl; ENST00000594571; ENSP00000471790; ENSG00000269875.
DR Ensembl; ENST00000597753; ENSP00000472739; ENSG00000269875.
DR Ensembl; ENST00000601551; ENSP00000470732; ENSG00000269875.
DR GeneID; 24140; -.
DR KEGG; hsa:24140; -.
DR UCSC; uc004djo.1; human.
DR CTD; 24140; -.
DR GeneCards; GC0XP048334; -.
DR HGNC; HGNC:13254; FTSJ1.
DR HPA; HPA002718; -.
DR MIM; 300499; gene.
DR MIM; 309549; phenotype.
DR neXtProt; NX_Q9UET6; -.
DR Orphanet; 777; X-linked non-syndromic intellectual deficit.
DR PharmGKB; PA28417; -.
DR eggNOG; COG0293; -.
DR HOGENOM; HOG000162368; -.
DR HOVERGEN; HBG017749; -.
DR InParanoid; Q9UET6; -.
DR KO; K14864; -.
DR OMA; IIRHFEG; -.
DR PhylomeDB; Q9UET6; -.
DR ChiTaRS; FTSJ1; human.
DR GeneWiki; FTSJ1; -.
DR GenomeRNAi; 24140; -.
DR NextBio; 46813; -.
DR PRO; PR:Q9UET6; -.
DR ArrayExpress; Q9UET6; -.
DR Bgee; Q9UET6; -.
DR CleanEx; HS_FTSJ1; -.
DR Genevestigator; Q9UET6; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR HAMAP; MF_01547; RNA_methyltr_E; 1; -.
DR HAMAP; MF_03162; RNA_methyltr_E_TRM7; 1; -.
DR InterPro; IPR028590; RNA_methyltr_E_Trm7.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
DR PANTHER; PTHR10920; PTHR10920; 1.
DR Pfam; PF01728; FtsJ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Mental retardation; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1 329 Putative tRNA
FT (cytidine(32)/guanosine(34)-2'-O)-
FT methyltransferase.
FT /FTId=PRO_0000155575.
FT ACT_SITE 156 156 Proton acceptor (By similarity).
FT BINDING 53 53 S-adenosyl-L-methionine; via amide
FT nitrogen (By similarity).
FT BINDING 55 55 S-adenosyl-L-methionine; via amide
FT nitrogen (By similarity).
FT BINDING 75 75 S-adenosyl-L-methionine (By similarity).
FT BINDING 91 91 S-adenosyl-L-methionine (By similarity).
FT BINDING 116 116 S-adenosyl-L-methionine (By similarity).
FT VAR_SEQ 219 220 Missing (in isoform 2).
FT /FTId=VSP_041419.
SQ SEQUENCE 329 AA; 36079 MW; 9A85D63A4FA80615 CRC64;
MGRTSKDKRD VYYRLAKENG WRARSAFKLL QLDKEFQLFQ GVTRAVDLCA APGSWSQVLS
QKIGGQGSGH VVAVDLQAMA PLPGVVQIQG DITQLSTAKE IIQHFKGCPA DLVVCDGAPD
VTGLHDVDEY MQAQLLLAAL NIATHVLKPG GCFVAKIFRG RDVTLLYSQL QVFFSSVLCA
KPRSSRNSSI EAFAVCQGYD PPEGFIPDLS KPLLDHSYDP DFNQLDGPTR IIVPFVTCGD
LSSYDSDRSY PLDLEGGSEY KYTPPTQPPI SPPYQEACTL KRKGQLAKEI RPQDCPISRV
DTFPQPLAAP QCHTLLAPEM EDNEMSCSP
//
ID TRM7_HUMAN Reviewed; 329 AA.
AC Q9UET6; B2RCJ0; O75670;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2000, sequence version 2.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase;
DE EC=2.1.1.205;
DE AltName: Full=2'-O-ribose RNA methyltransferase TRM7 homolog;
DE AltName: Full=Protein ftsJ homolog 1;
GN Name=FTSJ1; ORFNames=JM23;
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 2).
RA Pengue G., Lutfiyya L.L., Mazzarella R.;
RT "A human and yeast gene involved in cell division.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A.,
RA Meindl A.;
RT "Transcription map in Xp11.23.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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] (ISOFORM 1).
RC TISSUE=Lymph;
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 INVOLVEMENT IN MRX44, AND TISSUE SPECIFICITY.
RX PubMed=15162322; DOI=10.1086/422507;
RA Freude K., Hoffmann K., Jensen L.-R., Delatycki M.B., des Portes V.,
RA Moser B., Hamel B.C.J., van Bokhoven H., Moraine C., Fryns J.-P.,
RA Chelly J., Gecz J., Lenzner S., Kalscheuer V.M., Ropers H.-H.;
RT "Mutations in the FTSJ1 gene coding for a novel S-adenosylmethionine-
RT binding protein cause nonsyndromic X-linked mental retardation.";
RL Am. J. Hum. Genet. 75:305-309(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(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).
CC -!- FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions
CC 32 and 34 of the tRNA anticodon loop of substrate tRNAs (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine +
CC cytidine(32)/guanosine(34) in tRNA = S-adenosyl-L-homocysteine +
CC 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UET6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UET6-2; Sequence=VSP_041419;
CC -!- TISSUE SPECIFICITY: Found in fetal brain, lung, liver and kidney.
CC In the adult brain, expressed in amygdala, caudate nucleus, corpus
CC callosum, hippocampus and thalamus.
CC -!- DISEASE: Mental retardation, X-linked 44 (MRX44) [MIM:309549]: A
CC disorder characterized by significantly below average general
CC intellectual functioning associated with impairments in adaptive
CC behavior and manifested during the developmental period.
CC Intellectual deficiency is the only primary symptom of non-
CC syndromic X-linked mental retardation, while syndromic mental
CC retardation presents with associated physical, neurological and/or
CC psychiatric manifestations. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmE
CC family. TRM7 subfamily.
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/FTSJ1";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF063015; AAC33734.1; -; mRNA.
DR EMBL; AJ005892; CAA06749.1; -; mRNA.
DR EMBL; AK315138; BAG37587.1; -; mRNA.
DR EMBL; AF196972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471224; EAW50782.1; -; Genomic_DNA.
DR EMBL; BC023584; AAH23584.1; -; mRNA.
DR RefSeq; NP_001269086.1; NM_001282157.1.
DR RefSeq; NP_036412.1; NM_012280.3.
DR RefSeq; NP_803188.1; NM_177439.2.
DR RefSeq; XP_005272652.1; XM_005272595.1.
DR RefSeq; XP_005278087.1; XM_005278030.1.
DR UniGene; Hs.23170; -.
DR ProteinModelPortal; Q9UET6; -.
DR SMR; Q9UET6; 20-201.
DR IntAct; Q9UET6; 1.
DR STRING; 9606.ENSP00000326948; -.
DR PhosphoSite; Q9UET6; -.
DR DMDM; 12643879; -.
DR PaxDb; Q9UET6; -.
DR PRIDE; Q9UET6; -.
DR DNASU; 24140; -.
DR Ensembl; ENST00000019019; ENSP00000019019; ENSG00000068438.
DR Ensembl; ENST00000348411; ENSP00000326948; ENSG00000068438.
DR Ensembl; ENST00000456787; ENSP00000415457; ENSG00000068438.
DR Ensembl; ENST00000594571; ENSP00000471790; ENSG00000269875.
DR Ensembl; ENST00000597753; ENSP00000472739; ENSG00000269875.
DR Ensembl; ENST00000601551; ENSP00000470732; ENSG00000269875.
DR GeneID; 24140; -.
DR KEGG; hsa:24140; -.
DR UCSC; uc004djo.1; human.
DR CTD; 24140; -.
DR GeneCards; GC0XP048334; -.
DR HGNC; HGNC:13254; FTSJ1.
DR HPA; HPA002718; -.
DR MIM; 300499; gene.
DR MIM; 309549; phenotype.
DR neXtProt; NX_Q9UET6; -.
DR Orphanet; 777; X-linked non-syndromic intellectual deficit.
DR PharmGKB; PA28417; -.
DR eggNOG; COG0293; -.
DR HOGENOM; HOG000162368; -.
DR HOVERGEN; HBG017749; -.
DR InParanoid; Q9UET6; -.
DR KO; K14864; -.
DR OMA; IIRHFEG; -.
DR PhylomeDB; Q9UET6; -.
DR ChiTaRS; FTSJ1; human.
DR GeneWiki; FTSJ1; -.
DR GenomeRNAi; 24140; -.
DR NextBio; 46813; -.
DR PRO; PR:Q9UET6; -.
DR ArrayExpress; Q9UET6; -.
DR Bgee; Q9UET6; -.
DR CleanEx; HS_FTSJ1; -.
DR Genevestigator; Q9UET6; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR HAMAP; MF_01547; RNA_methyltr_E; 1; -.
DR HAMAP; MF_03162; RNA_methyltr_E_TRM7; 1; -.
DR InterPro; IPR028590; RNA_methyltr_E_Trm7.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
DR PANTHER; PTHR10920; PTHR10920; 1.
DR Pfam; PF01728; FtsJ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Mental retardation; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1 329 Putative tRNA
FT (cytidine(32)/guanosine(34)-2'-O)-
FT methyltransferase.
FT /FTId=PRO_0000155575.
FT ACT_SITE 156 156 Proton acceptor (By similarity).
FT BINDING 53 53 S-adenosyl-L-methionine; via amide
FT nitrogen (By similarity).
FT BINDING 55 55 S-adenosyl-L-methionine; via amide
FT nitrogen (By similarity).
FT BINDING 75 75 S-adenosyl-L-methionine (By similarity).
FT BINDING 91 91 S-adenosyl-L-methionine (By similarity).
FT BINDING 116 116 S-adenosyl-L-methionine (By similarity).
FT VAR_SEQ 219 220 Missing (in isoform 2).
FT /FTId=VSP_041419.
SQ SEQUENCE 329 AA; 36079 MW; 9A85D63A4FA80615 CRC64;
MGRTSKDKRD VYYRLAKENG WRARSAFKLL QLDKEFQLFQ GVTRAVDLCA APGSWSQVLS
QKIGGQGSGH VVAVDLQAMA PLPGVVQIQG DITQLSTAKE IIQHFKGCPA DLVVCDGAPD
VTGLHDVDEY MQAQLLLAAL NIATHVLKPG GCFVAKIFRG RDVTLLYSQL QVFFSSVLCA
KPRSSRNSSI EAFAVCQGYD PPEGFIPDLS KPLLDHSYDP DFNQLDGPTR IIVPFVTCGD
LSSYDSDRSY PLDLEGGSEY KYTPPTQPPI SPPYQEACTL KRKGQLAKEI RPQDCPISRV
DTFPQPLAAP QCHTLLAPEM EDNEMSCSP
//
MIM
300499
*RECORD*
*FIELD* NO
300499
*FIELD* TI
*300499 FTSJ HOMOLOG 1; FTSJ1
;;SPB1, S. CEREVISIAE, HOMOLOG OF;;
JM23
*FIELD* TX
read moreCLONING
Pintard et al. (2000) cloned and characterized Spb1, the S. cerevisiae
homolog of E. coli FTSJ1. The deduced 842-amino acid protein contains a
221-amino acid N-terminal S-adenosyl-L-methionine (AdoMet)-binding
domain found in AdoMet-dependent methyltransferases. The Spb1 protein
localized to the nucleolus. By database analysis, Pintard et al. (2000)
identified a human homolog of FTSJ1, which encodes a protein with
significant similarity to Spb1 in the AdoMet-binding domain.
GENE FUNCTION
Pintard et al. (2000) confirmed that yeast Spb1 binds AdoMet, suggesting
that it is a methylase. They found that temperature-sensitive mutant
alleles of Spb1 could suppress the deletion of the poly(A)-binding
protein gene (Pab1; 604679). The mutant alleles were also associated
with reduced 60S ribosome subunit content and abnormalities in the
processing of other ribosomal subunits.
FTSJ1 protein is a homolog of Escherichia coli RNA methyltransferase
FtsJ/RrmJ and may play a role in the regulation of translation (Freude
et al., 2004).
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the FTSJ1
gene to the X chromosome (TMAP WI-13805).
MOLECULAR GENETICS
As could be concluded from the distribution of linkage intervals in 125
families with nonsyndromic X-linked mental retardation, approximately
30% of all relevant mutations cluster on the proximal short arm of the X
chromosome (Ropers et al., 2003). PQBP1 (300463) and ZNF41 (314995) are
2 of the genes located in that region in which mutations causing
X-linked mental retardation have been found. Freude et al. (2004) found
that FTSJ1 is a third such gene. In a family reported by Hamel et al.
(1999), and designated MRX44 (309549), Freude et al. (2004) found a
mutation in the FTSJ1 gene (300499.0001). Other mutations in this gene
were found in 2 other families.
In a large Belgian family with nonsyndromic X-linked mental retardation
designated MRX9 (309549), Ramser et al. (2004) identified a splice site
mutation in the FTSJ1 gene (300499.0004). The findings indicated that
the FTSJ1 protein, which may be associated with ribosomal stability, is
associated with X-linked mental retardation.
*FIELD* AV
.0001
MENTAL RETARDATION, X-LINKED 44
FTSJ1, EX9DEL
In the family reported by Hamel et al. (1999) and designated MRX44
(309549), affected males had mild to moderate mental retardation. Freude
et al. (2004) found a single-nucleotide substitution (655G-A) at the
last nucleotide of exon 9 in this family. Subsequent amplification of
patient cDNA resulted in a fragment that was smaller than expected;
direct sequencing of this specific product showed that exon 9 was
absent. The absence introduced no frameshift in the FTSJ1 open reading
frame, but the resulting FTSJ1 protein lacked 28 amino acids, which
altered its structure and probably also its function.
.0002
MENTAL RETARDATION, X-LINKED 44
FTSJ1, 196C-T
After the finding of the FTSJ1 mutation in the original MRX44 family
(309549), Freude et al. (2004) searched for mutations in this gene in
215 individuals from unrelated families with putative X-linked metal
retardation for which no linkage data were available. This analysis
resulted in detection of a single-nucleotide substitution (196C-T) in
exon 4, resulting in a predicted truncated protein of 65 amino acids.
.0003
MENTAL RETARDATION, X-LINKED 44
FTSJ1, IVS2, G DEL, +1
In 1 family with presumed nonsyndromic X-linked mental retardation
(MRX44; 309549), Freude et al. (2004) found a single-nucleotide
deletion, IVS2+1delG. The deletion affected 1 of the 2 guanine
nucleotides of the exon 2/intron 2 boundary. Direct sequencing of mutant
RT-PCR products from the patient showed that, at the boundary between
exon 2 and exon 3, the transcript carried an insertion of a 10-bp
sequence of intron 2, which indicated that the IVS2+1delG deletion
affected splicing by cryptic splice site activation. The incorporation
of intronic sequence led to a frameshift in the FTSJ1 mRNA that resulted
in the use of a premature stop codon in exon 3 at position 138,
presumably producing a truncated protein of 49 amino acids.
.0004
MENTAL RETARDATION, X-LINKED 9
FTSJ1, IVS3AS, A-G, -2
In a Belgian family with nonsyndromic X-linked mental retardation
(309549) previously described by Willems et al. (1993), Ramser et al.
(2004) identified an A-to-G transition in the conserved acceptor splice
site of intron 3 (IVS3-2A-G) of the FTSJ1 gene. The mutation resulted in
skipping of exon 4 and introduced a premature stop codon in exon 5,
leading to a severely truncated protein.
*FIELD* RF
1. Freude, K.; Hoffmann, K.; Jensen, L.-R.; Delatycki, M. B.; des
Portes, V.; Moser, B.; Hamel, B.; van Bokhoven, H.; Moraine, C.; Fryns,
J.-P.; Chelly, J.; Gecz, J.; Lenzner, S.; Kalscheuer, V. M.; Ropers,
H.-H.: Mutations in the FTSJ1 gene coding for a novel S-adenosylmethionine-binding
protein cause nonsyndromic X-linked mental retardation. Am. J. Hum.
Genet. 75: 305-309, 2004.
2. Hamel, B. C. J.; Smits, A. P. T.; van den Helm, B.; Smeets, D.
F. C. M.; Knoers, N. V. A. M.; van Roosmalen, T.; Thoonen, G. H. J.;
Assman-Hulsmans, C. F. C. H.; Ropers, H.-H.; Mariman, E. C. M.; Kremer,
H.: Four families (MRX43, MRX44, MRX45, MRX52) with nonspecific X-linked
mental retardation: clinical and psychometric data and results of
linkage analysis. Am. J. Med. Genet. 85: 290-304, 1999.
3. Pintard, L.; Kressler, D.; Lapeyre, B.: Spb1p is a yeast nucleolar
protein associated with Nop1p and Nop58p that is able to bind S-adenosyl-L-methionine
in vitro. Molec. Cell. Biol. 20: 1370-1381, 2000.
4. Ramser, J.; Winnepenninckx, B.; Lenski, C.; Errijgers, V.; Platzer,
M.; Schwartz, C. E.; Meindl, A.; Kooy, R. F.: A splice site mutation
in the methyltransferase gene FTSJ1 in Xp11.23 is associated with
non-syndromic mental retardation in a large Belgian family (MRX9). J.
Med. Genet. 41: 679-683, 2004.
5. Ropers, H. H.; Hoeltzenbein, M.; Kalscheuer, V.; Yntema, H.; Hamel,
B.; Fryns, J. P.; Chelly, J.; Partington, M.; Gecz, J.; Moraine, C.
: Nonsyndromic X-linked mental retardation: where are the missing
mutations? Trends Genet. 19: 316-320, 2003.
6. Willems, P.; Vits, L.; Buntinx, I.; Raeymaekers, P.; Van Broeckhoven,
C.; Ceulemans, B.: Localization of a gene responsible for nonspecific
mental retardation (MRX9) to the pericentromeric region of the X chromosome. Genomics 18:
290-294, 1993.
*FIELD* CN
Victor A. McKusick - updated: 10/12/2004
Victor A. McKusick - updated: 7/12/2004
*FIELD* CD
Patricia A. Hartz: 7/2/2004
*FIELD* ED
carol: 02/01/2007
tkritzer: 10/14/2004
terry: 10/12/2004
alopez: 7/14/2004
terry: 7/12/2004
carol: 7/2/2004
*RECORD*
*FIELD* NO
300499
*FIELD* TI
*300499 FTSJ HOMOLOG 1; FTSJ1
;;SPB1, S. CEREVISIAE, HOMOLOG OF;;
JM23
*FIELD* TX
read moreCLONING
Pintard et al. (2000) cloned and characterized Spb1, the S. cerevisiae
homolog of E. coli FTSJ1. The deduced 842-amino acid protein contains a
221-amino acid N-terminal S-adenosyl-L-methionine (AdoMet)-binding
domain found in AdoMet-dependent methyltransferases. The Spb1 protein
localized to the nucleolus. By database analysis, Pintard et al. (2000)
identified a human homolog of FTSJ1, which encodes a protein with
significant similarity to Spb1 in the AdoMet-binding domain.
GENE FUNCTION
Pintard et al. (2000) confirmed that yeast Spb1 binds AdoMet, suggesting
that it is a methylase. They found that temperature-sensitive mutant
alleles of Spb1 could suppress the deletion of the poly(A)-binding
protein gene (Pab1; 604679). The mutant alleles were also associated
with reduced 60S ribosome subunit content and abnormalities in the
processing of other ribosomal subunits.
FTSJ1 protein is a homolog of Escherichia coli RNA methyltransferase
FtsJ/RrmJ and may play a role in the regulation of translation (Freude
et al., 2004).
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the FTSJ1
gene to the X chromosome (TMAP WI-13805).
MOLECULAR GENETICS
As could be concluded from the distribution of linkage intervals in 125
families with nonsyndromic X-linked mental retardation, approximately
30% of all relevant mutations cluster on the proximal short arm of the X
chromosome (Ropers et al., 2003). PQBP1 (300463) and ZNF41 (314995) are
2 of the genes located in that region in which mutations causing
X-linked mental retardation have been found. Freude et al. (2004) found
that FTSJ1 is a third such gene. In a family reported by Hamel et al.
(1999), and designated MRX44 (309549), Freude et al. (2004) found a
mutation in the FTSJ1 gene (300499.0001). Other mutations in this gene
were found in 2 other families.
In a large Belgian family with nonsyndromic X-linked mental retardation
designated MRX9 (309549), Ramser et al. (2004) identified a splice site
mutation in the FTSJ1 gene (300499.0004). The findings indicated that
the FTSJ1 protein, which may be associated with ribosomal stability, is
associated with X-linked mental retardation.
*FIELD* AV
.0001
MENTAL RETARDATION, X-LINKED 44
FTSJ1, EX9DEL
In the family reported by Hamel et al. (1999) and designated MRX44
(309549), affected males had mild to moderate mental retardation. Freude
et al. (2004) found a single-nucleotide substitution (655G-A) at the
last nucleotide of exon 9 in this family. Subsequent amplification of
patient cDNA resulted in a fragment that was smaller than expected;
direct sequencing of this specific product showed that exon 9 was
absent. The absence introduced no frameshift in the FTSJ1 open reading
frame, but the resulting FTSJ1 protein lacked 28 amino acids, which
altered its structure and probably also its function.
.0002
MENTAL RETARDATION, X-LINKED 44
FTSJ1, 196C-T
After the finding of the FTSJ1 mutation in the original MRX44 family
(309549), Freude et al. (2004) searched for mutations in this gene in
215 individuals from unrelated families with putative X-linked metal
retardation for which no linkage data were available. This analysis
resulted in detection of a single-nucleotide substitution (196C-T) in
exon 4, resulting in a predicted truncated protein of 65 amino acids.
.0003
MENTAL RETARDATION, X-LINKED 44
FTSJ1, IVS2, G DEL, +1
In 1 family with presumed nonsyndromic X-linked mental retardation
(MRX44; 309549), Freude et al. (2004) found a single-nucleotide
deletion, IVS2+1delG. The deletion affected 1 of the 2 guanine
nucleotides of the exon 2/intron 2 boundary. Direct sequencing of mutant
RT-PCR products from the patient showed that, at the boundary between
exon 2 and exon 3, the transcript carried an insertion of a 10-bp
sequence of intron 2, which indicated that the IVS2+1delG deletion
affected splicing by cryptic splice site activation. The incorporation
of intronic sequence led to a frameshift in the FTSJ1 mRNA that resulted
in the use of a premature stop codon in exon 3 at position 138,
presumably producing a truncated protein of 49 amino acids.
.0004
MENTAL RETARDATION, X-LINKED 9
FTSJ1, IVS3AS, A-G, -2
In a Belgian family with nonsyndromic X-linked mental retardation
(309549) previously described by Willems et al. (1993), Ramser et al.
(2004) identified an A-to-G transition in the conserved acceptor splice
site of intron 3 (IVS3-2A-G) of the FTSJ1 gene. The mutation resulted in
skipping of exon 4 and introduced a premature stop codon in exon 5,
leading to a severely truncated protein.
*FIELD* RF
1. Freude, K.; Hoffmann, K.; Jensen, L.-R.; Delatycki, M. B.; des
Portes, V.; Moser, B.; Hamel, B.; van Bokhoven, H.; Moraine, C.; Fryns,
J.-P.; Chelly, J.; Gecz, J.; Lenzner, S.; Kalscheuer, V. M.; Ropers,
H.-H.: Mutations in the FTSJ1 gene coding for a novel S-adenosylmethionine-binding
protein cause nonsyndromic X-linked mental retardation. Am. J. Hum.
Genet. 75: 305-309, 2004.
2. Hamel, B. C. J.; Smits, A. P. T.; van den Helm, B.; Smeets, D.
F. C. M.; Knoers, N. V. A. M.; van Roosmalen, T.; Thoonen, G. H. J.;
Assman-Hulsmans, C. F. C. H.; Ropers, H.-H.; Mariman, E. C. M.; Kremer,
H.: Four families (MRX43, MRX44, MRX45, MRX52) with nonspecific X-linked
mental retardation: clinical and psychometric data and results of
linkage analysis. Am. J. Med. Genet. 85: 290-304, 1999.
3. Pintard, L.; Kressler, D.; Lapeyre, B.: Spb1p is a yeast nucleolar
protein associated with Nop1p and Nop58p that is able to bind S-adenosyl-L-methionine
in vitro. Molec. Cell. Biol. 20: 1370-1381, 2000.
4. Ramser, J.; Winnepenninckx, B.; Lenski, C.; Errijgers, V.; Platzer,
M.; Schwartz, C. E.; Meindl, A.; Kooy, R. F.: A splice site mutation
in the methyltransferase gene FTSJ1 in Xp11.23 is associated with
non-syndromic mental retardation in a large Belgian family (MRX9). J.
Med. Genet. 41: 679-683, 2004.
5. Ropers, H. H.; Hoeltzenbein, M.; Kalscheuer, V.; Yntema, H.; Hamel,
B.; Fryns, J. P.; Chelly, J.; Partington, M.; Gecz, J.; Moraine, C.
: Nonsyndromic X-linked mental retardation: where are the missing
mutations? Trends Genet. 19: 316-320, 2003.
6. Willems, P.; Vits, L.; Buntinx, I.; Raeymaekers, P.; Van Broeckhoven,
C.; Ceulemans, B.: Localization of a gene responsible for nonspecific
mental retardation (MRX9) to the pericentromeric region of the X chromosome. Genomics 18:
290-294, 1993.
*FIELD* CN
Victor A. McKusick - updated: 10/12/2004
Victor A. McKusick - updated: 7/12/2004
*FIELD* CD
Patricia A. Hartz: 7/2/2004
*FIELD* ED
carol: 02/01/2007
tkritzer: 10/14/2004
terry: 10/12/2004
alopez: 7/14/2004
terry: 7/12/2004
carol: 7/2/2004
MIM
309549
*RECORD*
*FIELD* NO
309549
*FIELD* TI
#309549 MENTAL RETARDATION, X-LINKED 9; MRX9
;;MENTAL RETARDATION, X-LINKED 44; MRX44
read more*FIELD* TX
A number sign (#) is used with this entry because this form of
nonspecific X-linked mental retardation is caused by mutation in the
FTSJ1 gene (300499).
CLINICAL FEATURES
Nonspecific X-linked mental retardation (MRX) includes several distinct
entities with mental retardation but without additional distinguishing
features.
Hamel et al. (1999) described a 4-generation family segregating X-linked
mental retardation. Affected members had nonprogressive mental
retardation noted during childhood, and several demonstrated aggressive
behavior. The mental retardation in tested members of the family was
moderate to severe; none of the patients was able to read, write, or
solve simple arithmetic problems.
Froyen et al. (2007) reported 3 Caucasian brothers with nonsyndromic
X-linked mental retardation. Two had moderate and 1 had severe
intellectual handicap. The oldest patient had autistic behavior that
lessened after age 5 years, as well as delayed speech and motor
development. The 2 younger brothers also had seizures; 1 had flat nasal
bridge and shortened distal phalanges. High-resolution array CGH
identified a 50-kb microdeletion at Xp11.23 involving the FTSJ1 and
SLC38A5 (300649) genes. Detailed mapping studies suggested that the
deletion breakpoints involved the repeat region of the SSX1 gene
(312820). The unaffected mother also carried the deletion, but showed
complete inactivation of the aberrant X chromosome. Froyen et al. (2007)
concluded that the cognitive impairment in this family was most likely
due to absence of the FTSJ1 gene.
MAPPING
Willems et al. (1993) described linkage studies in a family classified
as MRX9 in the nomenclature proposed by Mulley et al. (1992) and
reviewed by Neri et al. (1992). The studies suggested localization in
the pericentromeric region, namely, Xp21-q13. Winnepenninckx et al.
(2002) restudied the Belgian family reported by Willems et al. (1993)
and refined the mapping of the MRX9 gene to Xp11.4-p11.22.
Hamel et al. (1999) performed linkage analysis in family MRX44 and
obtained a maximum lod score of 2.90 (theta = 0.0) with marker DXS1204.
Haplotype construction defined the region to Xp11.3-p11.21, spanning an
approximately 10-cM interval flanked by markers DXS1003 and ALAS2.
MOLECULAR GENETICS
The MRX44 family of Hamel et al. (1999) was shown by Freude et al.
(2004) to carry a mutation in the FTSJ1 gene (300499.0001), resulting in
deletion of exon 9.
In the Belgian MRX9 family reported by Willems et al. (1993), Ramser et
al. (2004) established a gene catalog for the candidate region defined
by Winnepenninckx et al. (2002). Comprehensive mutation analysis by
direct sequencing identified an alteration in the conserved acceptor
splice site of intron 3 of the FTSJ1 gene (300499.0004).
*FIELD* RF
1. Freude, K.; Hoffmann, K.; Jensen, L.-R.; Delatycki, M. B.; des
Portes, V.; Moser, B.; Hamel, B.; van Bokhoven, H.; Moraine, C.; Fryns,
J.-P.; Chelly, J.; Gecz, J.; Lenzner, S.; Kalscheuer, V. M.; Ropers,
H.-H.: Mutations in the FTSJ1 gene coding for a novel S-adenosylmethionine-binding
protein cause nonsyndromic X-linked mental retardation. Am. J. Hum.
Genet. 75: 305-309, 2004.
2. Froyen, G.; Bauters, M.; Boyle, J.; van Esch, H.; Govaerts, K.;
van Bokhoven, H.; Ropers, H.-H.; Moraine, C.; Chelly, J.; Fryns, J.-P.;
Marynen, P.; Gecz, J.; Turner, G.: Loss of SLC38A5 and FTSJ1 at Xp11.23
in three brothers with non-syndromic mental retardation due to a microdeletion
in an unstable genomic region. Hum. Genet. 121: 539-547, 2007.
3. Hamel, B. C. J.; Smits, A. P. T.; van den Helm, B.; Smeets, D.
F. C. M.; Knoers, N. V. A. M.; van Roosmalen, T.; Thoonen, G. H. J.;
Assman-Hulsmans, C. F. C. H.; Ropers, H.-H.; Mariman, E. C. M.; Kremer,
H.: Four families (MRX43, MRX44, MRX45, MRX52) with nonspecific X-linked
mental retardation: clinical and psychometric data and results of
linkage analysis. Am. J. Med. Genet. 85: 290-304, 1999.
4. Mulley, J. C.; Kerr, B.; Stevenson, R.; Lubs, H.: Nomenclature
guidelines for X-linked mental retardation. Am. J. Med. Genet. 43:
383-391, 1992.
5. Neri, G.; Chiurazzi, P.; Arena, F.; Lubs, H. A.; Glass, I. A.:
XLMR genes: update 1992. Am. J. Med. Genet. 43: 373-382, 1992.
6. Ramser, J.; Winnepenninckx, B.; Lenski, C.; Errijgers, V.; Platzer,
M.; Schwartz, C. E.; Meindl, A.; Kooy, R. F.: A splice site mutation
in the methyltransferase gene FTSJ1 in Xp11.23 is associated with
non-syndromic mental retardation in a large Belgian family (MRX9). J.
Med. Genet. 41: 679-683, 2004.
7. Willems, P.; Vits, L.; Buntinx, I.; Raeymaekers, P.; Van Broeckhoven,
C.; Ceulemans, B.: Localization of a gene responsible for nonspecific
mental retardation (MRX9) to the pericentromeric region of the X chromosome. Genomics 18:
290-294, 1993.
8. Winnepenninckx, B.; Errijgers, V.; Reyniers, E.; De Deyn, P. P.;
Abidi, F. E.; Schwartz, C. E.; Kooy, R. F.: Family MRX9 revisited:
further evidence for locus heterogeneity in MRX. Am. J. Med. Genet. 112:
17-22, 2002.
*FIELD* CN
Cassandra L. Kniffin - updated: 6/12/2007
Victor A. McKusick - updated: 10/12/2004
Victor A. McKusick - updated: 10/7/2002
Victor A. McKusick - updated: 3/25/1998
*FIELD* CD
Victor A. McKusick: 11/30/1993
*FIELD* ED
terry: 03/16/2012
wwang: 6/14/2007
ckniffin: 6/12/2007
carol: 2/1/2007
tkritzer: 10/14/2004
terry: 10/12/2004
carol: 3/18/2004
terry: 4/28/2003
tkritzer: 10/9/2002
tkritzer: 10/8/2002
terry: 10/7/2002
alopez: 3/25/1998
terry: 3/17/1998
carol: 10/3/1995
carol: 11/30/1993
*RECORD*
*FIELD* NO
309549
*FIELD* TI
#309549 MENTAL RETARDATION, X-LINKED 9; MRX9
;;MENTAL RETARDATION, X-LINKED 44; MRX44
read more*FIELD* TX
A number sign (#) is used with this entry because this form of
nonspecific X-linked mental retardation is caused by mutation in the
FTSJ1 gene (300499).
CLINICAL FEATURES
Nonspecific X-linked mental retardation (MRX) includes several distinct
entities with mental retardation but without additional distinguishing
features.
Hamel et al. (1999) described a 4-generation family segregating X-linked
mental retardation. Affected members had nonprogressive mental
retardation noted during childhood, and several demonstrated aggressive
behavior. The mental retardation in tested members of the family was
moderate to severe; none of the patients was able to read, write, or
solve simple arithmetic problems.
Froyen et al. (2007) reported 3 Caucasian brothers with nonsyndromic
X-linked mental retardation. Two had moderate and 1 had severe
intellectual handicap. The oldest patient had autistic behavior that
lessened after age 5 years, as well as delayed speech and motor
development. The 2 younger brothers also had seizures; 1 had flat nasal
bridge and shortened distal phalanges. High-resolution array CGH
identified a 50-kb microdeletion at Xp11.23 involving the FTSJ1 and
SLC38A5 (300649) genes. Detailed mapping studies suggested that the
deletion breakpoints involved the repeat region of the SSX1 gene
(312820). The unaffected mother also carried the deletion, but showed
complete inactivation of the aberrant X chromosome. Froyen et al. (2007)
concluded that the cognitive impairment in this family was most likely
due to absence of the FTSJ1 gene.
MAPPING
Willems et al. (1993) described linkage studies in a family classified
as MRX9 in the nomenclature proposed by Mulley et al. (1992) and
reviewed by Neri et al. (1992). The studies suggested localization in
the pericentromeric region, namely, Xp21-q13. Winnepenninckx et al.
(2002) restudied the Belgian family reported by Willems et al. (1993)
and refined the mapping of the MRX9 gene to Xp11.4-p11.22.
Hamel et al. (1999) performed linkage analysis in family MRX44 and
obtained a maximum lod score of 2.90 (theta = 0.0) with marker DXS1204.
Haplotype construction defined the region to Xp11.3-p11.21, spanning an
approximately 10-cM interval flanked by markers DXS1003 and ALAS2.
MOLECULAR GENETICS
The MRX44 family of Hamel et al. (1999) was shown by Freude et al.
(2004) to carry a mutation in the FTSJ1 gene (300499.0001), resulting in
deletion of exon 9.
In the Belgian MRX9 family reported by Willems et al. (1993), Ramser et
al. (2004) established a gene catalog for the candidate region defined
by Winnepenninckx et al. (2002). Comprehensive mutation analysis by
direct sequencing identified an alteration in the conserved acceptor
splice site of intron 3 of the FTSJ1 gene (300499.0004).
*FIELD* RF
1. Freude, K.; Hoffmann, K.; Jensen, L.-R.; Delatycki, M. B.; des
Portes, V.; Moser, B.; Hamel, B.; van Bokhoven, H.; Moraine, C.; Fryns,
J.-P.; Chelly, J.; Gecz, J.; Lenzner, S.; Kalscheuer, V. M.; Ropers,
H.-H.: Mutations in the FTSJ1 gene coding for a novel S-adenosylmethionine-binding
protein cause nonsyndromic X-linked mental retardation. Am. J. Hum.
Genet. 75: 305-309, 2004.
2. Froyen, G.; Bauters, M.; Boyle, J.; van Esch, H.; Govaerts, K.;
van Bokhoven, H.; Ropers, H.-H.; Moraine, C.; Chelly, J.; Fryns, J.-P.;
Marynen, P.; Gecz, J.; Turner, G.: Loss of SLC38A5 and FTSJ1 at Xp11.23
in three brothers with non-syndromic mental retardation due to a microdeletion
in an unstable genomic region. Hum. Genet. 121: 539-547, 2007.
3. Hamel, B. C. J.; Smits, A. P. T.; van den Helm, B.; Smeets, D.
F. C. M.; Knoers, N. V. A. M.; van Roosmalen, T.; Thoonen, G. H. J.;
Assman-Hulsmans, C. F. C. H.; Ropers, H.-H.; Mariman, E. C. M.; Kremer,
H.: Four families (MRX43, MRX44, MRX45, MRX52) with nonspecific X-linked
mental retardation: clinical and psychometric data and results of
linkage analysis. Am. J. Med. Genet. 85: 290-304, 1999.
4. Mulley, J. C.; Kerr, B.; Stevenson, R.; Lubs, H.: Nomenclature
guidelines for X-linked mental retardation. Am. J. Med. Genet. 43:
383-391, 1992.
5. Neri, G.; Chiurazzi, P.; Arena, F.; Lubs, H. A.; Glass, I. A.:
XLMR genes: update 1992. Am. J. Med. Genet. 43: 373-382, 1992.
6. Ramser, J.; Winnepenninckx, B.; Lenski, C.; Errijgers, V.; Platzer,
M.; Schwartz, C. E.; Meindl, A.; Kooy, R. F.: A splice site mutation
in the methyltransferase gene FTSJ1 in Xp11.23 is associated with
non-syndromic mental retardation in a large Belgian family (MRX9). J.
Med. Genet. 41: 679-683, 2004.
7. Willems, P.; Vits, L.; Buntinx, I.; Raeymaekers, P.; Van Broeckhoven,
C.; Ceulemans, B.: Localization of a gene responsible for nonspecific
mental retardation (MRX9) to the pericentromeric region of the X chromosome. Genomics 18:
290-294, 1993.
8. Winnepenninckx, B.; Errijgers, V.; Reyniers, E.; De Deyn, P. P.;
Abidi, F. E.; Schwartz, C. E.; Kooy, R. F.: Family MRX9 revisited:
further evidence for locus heterogeneity in MRX. Am. J. Med. Genet. 112:
17-22, 2002.
*FIELD* CN
Cassandra L. Kniffin - updated: 6/12/2007
Victor A. McKusick - updated: 10/12/2004
Victor A. McKusick - updated: 10/7/2002
Victor A. McKusick - updated: 3/25/1998
*FIELD* CD
Victor A. McKusick: 11/30/1993
*FIELD* ED
terry: 03/16/2012
wwang: 6/14/2007
ckniffin: 6/12/2007
carol: 2/1/2007
tkritzer: 10/14/2004
terry: 10/12/2004
carol: 3/18/2004
terry: 4/28/2003
tkritzer: 10/9/2002
tkritzer: 10/8/2002
terry: 10/7/2002
alopez: 3/25/1998
terry: 3/17/1998
carol: 10/3/1995
carol: 11/30/1993