Q9UET6 (TRM7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase
EC=2.1.1.205

Alternative name(s):
2'-O-ribose RNA methyltransferase TRM7 homolog
Protein ftsJ homolog 1

Gene names

Name:	FTSJ1
ORF Names:	JM23

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs By similarity. HAMAP-Rule MF_03162
Catalytic activity	S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O-methylguanosine34 in tRNA. HAMAP-Rule MF_03162
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Found in fetal brain, lung, liver and kidney. In the adult brain, expressed in amygdala, caudate nucleus, corpus callosum, hippocampus and thalamus. Ref.7
Involvement in disease	Mental retardation, X-linked 44 (MRX44) [MIM:309549]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7
Sequence similarities	Belongs to the methyltransferase superfamily. RlmE family. TRM7 subfamily.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Disease	Mental retardation
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA methylation Inferred from electronic annotation. Source: InterPro tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	methyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UET6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UET6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     219-220: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 329	329	Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase HAMAP-Rule MF_03162		PRO_0000155575
Sites
	Active site	156	1	Proton acceptor By similarity
	Binding site	53	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	55	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	75	1	S-adenosyl-L-methionine By similarity
	Binding site	91	1	S-adenosyl-L-methionine By similarity
	Binding site	116	1	S-adenosyl-L-methionine By similarity
Natural variations
	Alternative sequence	219 – 220	2	Missing in isoform 2.		VSP_041419

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 9A85D63A4FA80615	FASTA	329	36,079
	10 20 30 40 50 60 MGRTSKDKRD VYYRLAKENG WRARSAFKLL QLDKEFQLFQ GVTRAVDLCA APGSWSQVLS 70 80 90 100 110 120 QKIGGQGSGH VVAVDLQAMA PLPGVVQIQG DITQLSTAKE IIQHFKGCPA DLVVCDGAPD 130 140 150 160 170 180 VTGLHDVDEY MQAQLLLAAL NIATHVLKPG GCFVAKIFRG RDVTLLYSQL QVFFSSVLCA 190 200 210 220 230 240 KPRSSRNSSI EAFAVCQGYD PPEGFIPDLS KPLLDHSYDP DFNQLDGPTR IIVPFVTCGD 250 260 270 280 290 300 LSSYDSDRSY PLDLEGGSEY KYTPPTQPPI SPPYQEACTL KRKGQLAKEI RPQDCPISRV 310 320 DTFPQPLAAP QCHTLLAPEM EDNEMSCSP
	Isoform 2 [UniParc]. Checksum: 54417CCDEB515C55	FASTA	327	35,867
	10 20 30 40 50 60 MGRTSKDKRD VYYRLAKENG WRARSAFKLL QLDKEFQLFQ GVTRAVDLCA APGSWSQVLS 70 80 90 100 110 120 QKIGGQGSGH VVAVDLQAMA PLPGVVQIQG DITQLSTAKE IIQHFKGCPA DLVVCDGAPD 130 140 150 160 170 180 VTGLHDVDEY MQAQLLLAAL NIATHVLKPG GCFVAKIFRG RDVTLLYSQL QVFFSSVLCA 190 200 210 220 230 240 KPRSSRNSSI EAFAVCQGYD PPEGFIPDLS KPLLDHSYDF NQLDGPTRII VPFVTCGDLS 250 260 270 280 290 300 SYDSDRSYPL DLEGGSEYKY TPPTQPPISP PYQEACTLKR KGQLAKEIRP QDCPISRVDT 310 320 FPQPLAAPQC HTLLAPEMED NEMSCSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human and yeast gene involved in cell division." Pengue G., Lutfiyya L.L., Mazzarella R. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"Transcription map in Xp11.23." Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A., Meindl A. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lymph.
[7]	"Mutations in the FTSJ1 gene coding for a novel S-adenosylmethionine-binding protein cause nonsyndromic X-linked mental retardation." Freude K., Hoffmann K., Jensen L.-R., Delatycki M.B., des Portes V., Moser B., Hamel B.C.J., van Bokhoven H., Moraine C., Fryns J.-P., Chelly J., Gecz J., Lenzner S., Kalscheuer V.M., Ropers H.-H. Am. J. Hum. Genet. 75:305-309(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MRX44, TISSUE SPECIFICITY.
[8]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF063015 mRNA. Translation: AAC33734.1. AJ005892 mRNA. Translation: CAA06749.1. AK315138 mRNA. Translation: BAG37587.1. AF196972 Genomic DNA. No translation available. CH471224 Genomic DNA. Translation: EAW50782.1. BC023584 mRNA. Translation: AAH23584.1.
IPI	IPI00004308. IPI00219764.
RefSeq	NP_036412.1. NM_012280.2. NP_803183.1. NM_177434.1. NP_803188.1. NM_177439.1.
UniGene	Hs.23170.
3D structure databases
ProteinModelPortal	Q9UET6.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UET6. 1 interaction.
STRING	9606.ENSP00000326948.
PTM databases
PhosphoSite	Q9UET6.
Polymorphism databases
DMDM	12643879.
Proteomic databases
PaxDb	Q9UET6.
PRIDE	Q9UET6.
Protocols and materials databases
DNASU	24140.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000019019; ENSP00000019019; ENSG00000068438. ENST00000348411; ENSP00000326948; ENSG00000068438. ENST00000456787; ENSP00000415457; ENSG00000068438. ENST00000594571; ENSP00000471790; ENSG00000269875. ENST00000597753; ENSP00000472739; ENSG00000269875. ENST00000601551; ENSP00000470732; ENSG00000269875.
GeneID	24140.
KEGG	hsa:24140.
UCSC	uc004djn.1. human. uc004djo.1. human.
Organism-specific databases
CTD	24140.
GeneCards	GC0XP048334.
HGNC	HGNC:13254. FTSJ1.
HPA	HPA002718.
MIM	300499. gene. 309549. phenotype.
neXtProt	NX_Q9UET6.
Orphanet	777. X-linked nonsyndromic intellectual deficit.
PharmGKB	PA28417.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0293.
HOGENOM	HOG000162368.
HOVERGEN	HBG017749.
InParanoid	Q9UET6.
KO	K14864.
OMA	IIRHFEG.
OrthoDB	EOG43JC53.
PhylomeDB	Q9UET6.
Gene expression databases
ArrayExpress	Q9UET6.
Bgee	Q9UET6.
CleanEx	HS_FTSJ1.
Genevestigator	Q9UET6.
GermOnline	ENSG00000068438. Homo sapiens.
Family and domain databases
HAMAP	MF_01547. RNA_methyltr_E. MF_03162. RNA_methyltr_E_TRM7.
InterPro	IPR015507. rRNA-MeTfrase_E. IPR002877. rRNA_MeTrfase_FtsJ_dom. [Graphical view]
PANTHER	PTHR10920. PTHR10920. 1 hit.
Pfam	PF01728. FtsJ. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	FTSJ1. human.
GenomeRNAi	24140.
NextBio	46813.
SOURCE	Search...

Entry information

Entry name

TRM7_HUMAN

Accession

Primary (citable) accession number: Q9UET6
Secondary accession number(s): B2RCJ0, O75670

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.