Q9NX74 (DUS2L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
tRNA-dihydrouridine(20) synthase [NAD(P)+]-like
EC=1.3.1.-

Alternative name(s):
Up-regulated in lung cancer protein 8
Short name=URLC8
tRNA-dihydrouridine synthase 2-like
Short name=hDUS2

Gene names

Name:	DUS2L
Synonyms:	DUS2

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	493 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dihydrouridine synthase. Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Ref.1
Cofactor	FAD By similarity.
Subunit structure	Interacts with EPRS. Ref.1
Subcellular location	Cytoplasm. Endoplasmic reticulum. Note: Mainly at the endoplasmic reticulum. Ref.1
Tissue specificity	Weak expression in heart, placenta and skeletal muscle. Up-regulated in most lung cancer cells (at protein level). Ref.1
Sequence similarities	Belongs to the dus family. Dus2 subfamily. Contains 1 DRBM (double-stranded RNA-binding) domain.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Cytoplasm Endoplasmic reticulum
Ligand	FAD Flavoprotein RNA-binding
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	tRNA dihydrouridine synthesis Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	double-stranded RNA binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro tRNA dihydrouridine synthase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 493	493	tRNA-dihydrouridine(20) synthase [NAD(P)+]-like		PRO_0000162157
Regions
	Domain	369 – 436	68	DRBM
Amino acid modifications
	Modified residue	488	1	Phosphoserine Ref.5 Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q9NX74 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 8CFE5046CCF79DCD	FASTA	493	55,050
	10 20 30 40 50 60 MILNSLSLCY HNKLILAPMV RVGTLPMRLL ALDYGADIVY CEELIDLKMI QCKRVVNEVL 70 80 90 100 110 120 STVDFVAPDD RVVFRTCERE QNRVVFQMGT SDAERALAVA RLVENDVAGI DVNMGCPKQY 130 140 150 160 170 180 STKGGMGAAL LSDPDKIEKI LSTLVKGTRR PVTCKIRILP SLEDTLSLVK RIERTGIAAI 190 200 210 220 230 240 AVHGRKREER PQHPVSCEVI KAIADTLSIP VIANGGSHDH IQQYSDIEDF RQATAASSVM 250 260 270 280 290 300 VARAAMWNPS IFLKEGLRPL EEVMQKYIRY AVQYDNHYTN TKYCLCQMLR EQLESPQGRL 310 320 330 340 350 360 LHAAQSSREI CEAFGLGAFY EETTQELDAQ QARLSAKTSE QTGEPAEDTS GVIKMAVKFD 370 380 390 400 410 420 RRAYPAQITP KMCLLEWCRR EKLAQPVYET VQRPLDRLFS SIVTVAEQKY QSTLWDKSKK 430 440 450 460 470 480 LAEQAAAIVC LRSQGLPEGR LGEESPSLHK RKREAPDQDP GGPRAQELAQ PGDLCKKPFV 490 ALGSGEESPL EGW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis." Kato T., Daigo Y., Hayama S., Ishikawa N., Yamabuki T., Ito T., Miyamoto M., Kondo S., Nakamura Y. Cancer Res. 65:5638-5646(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH EPRS.
[2]	"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]. Tissue: Gastric carcinoma.
[3]	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].
[4]	"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]. Tissue: Colon.
[5]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB101210 mRNA. Translation: BAE07219.1. AK000406 mRNA. Translation: BAA91143.1. AK290578 mRNA. Translation: BAF83267.1. CH471092 Genomic DNA. Translation: EAW83207.1. BC006527 mRNA. Translation: AAH06527.1.
IPI	IPI00015804.
RefSeq	NP_001258691.1. NM_001271762.1. NP_001258692.1. NM_001271763.1. NP_060273.1. NM_017803.4.
UniGene	Hs.534460.
3D structure databases
ProteinModelPortal	Q9NX74.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NX74. 1 interaction.
STRING	9606.ENSP00000351769.
PTM databases
PhosphoSite	Q9NX74.
Polymorphism databases
DMDM	73620832.
Proteomic databases
PaxDb	Q9NX74.
PRIDE	Q9NX74.
Protocols and materials databases
DNASU	54920.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000358896; ENSP00000351769; ENSG00000167264. ENST00000565263; ENSP00000455229; ENSG00000167264.
GeneID	54920.
KEGG	hsa:54920.
UCSC	uc002evi.3. human.
Organism-specific databases
CTD	54920.
GeneCards	GC16P068058.
HGNC	HGNC:26014. DUS2L.
HPA	HPA042560. HPA043528.
MIM	609707. gene.
neXtProt	NX_Q9NX74.
PharmGKB	PA142671937.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0042.
HOGENOM	HOG000195580.
HOVERGEN	HBG079551.
InParanoid	Q9NX74.
KO	K05543.
OMA	YHNKLIL.
OrthoDB	EOG4MW85W.
PhylomeDB	Q9NX74.
Gene expression databases
ArrayExpress	Q9NX74.
Bgee	Q9NX74.
CleanEx	HS_DUS2L.
Genevestigator	Q9NX74.
Family and domain databases
Gene3D	3.20.20.70. 1 hit. 3.30.160.20. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR001159. Ds-RNA-bd. IPR014720. dsRNA-bd-like_dom. IPR001269. tRNA_hU_synthase. IPR018517. tRNA_hU_synthase_CS. [Graphical view]
PANTHER	PTHR11082. PTHR11082. 1 hit.
Pfam	PF00035. dsrm. 1 hit. PF01207. Dus. 1 hit. [Graphical view]
SMART	SM00358. DSRM. 1 hit. [Graphical view]
PROSITE	PS50137. DS_RBD. False negative. PS01136. UPF0034. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	54920.
NextBio	57992.
SOURCE	Search...

Entry information

Entry name

DUS2L_HUMAN

Accession

Primary (citable) accession number: Q9NX74
Secondary accession number(s): A8K3G3, Q4H4D9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 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.