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Protein

tRNA-dihydrouridine(20) synthase [NAD(P)+]-like

Gene

DUS2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Dihydrouridine synthase. Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Negatively regulates the activation of EIF2AK2/PKR.2 Publications

Cofactori

FMNBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei87 – 871FMNBy similarity
Active sitei116 – 1161Proton donorBy similarity
Binding sitei155 – 1551FMNBy similarity
Binding sitei183 – 1831FMNBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 203FMNBy similarity
Nucleotide bindingi214 – 2163FMNBy similarity
Nucleotide bindingi242 – 2432FMNBy similarity

GO - Molecular functioni

  • double-stranded RNA binding Source: UniProtKB
  • flavin adenine dinucleotide binding Source: InterPro
  • protein kinase inhibitor activity Source: UniProtKB
  • tRNA dihydrouridine synthase activity Source: InterPro

GO - Biological processi

  • negative regulation of cell death Source: UniProtKB
  • negative regulation of protein kinase activity Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Flavoprotein, FMN, RNA-binding

Enzyme and pathway databases

BRENDAi1.3.1.91. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (EC:1.3.1.-)
Alternative name(s):
Dihydrouridine synthase 2
Up-regulated in lung cancer protein 8
Short name:
URLC8
tRNA-dihydrouridine synthase 2-like
Short name:
hDUS2
Gene namesi
Name:DUS2
Synonyms:DUS2L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:26014. DUS2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671937.

Polymorphism and mutation databases

DMDMi73620832.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 493493tRNA-dihydrouridine(20) synthase [NAD(P)+]-likePRO_0000162157Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei488 – 4881Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NX74.
PaxDbiQ9NX74.
PRIDEiQ9NX74.

PTM databases

PhosphoSiteiQ9NX74.

Expressioni

Tissue specificityi

Weak expression in heart, placenta and skeletal muscle. Up-regulated in most lung cancer cells (at protein level).1 Publication

Gene expression databases

BgeeiQ9NX74.
CleanExiHS_DUS2L.
ExpressionAtlasiQ9NX74. baseline and differential.
GenevisibleiQ9NX74. HS.

Organism-specific databases

HPAiHPA042560.
HPA043528.

Interactioni

Subunit structurei

Interacts with EPRS. Interacts (via DRBM domain) with PRKRA and EIF2AK2/PKR (via DRBM 1 domain).2 Publications

Protein-protein interaction databases

BioGridi120261. 3 interactions.
IntActiQ9NX74. 3 interactions.
MINTiMINT-3076069.
STRINGi9606.ENSP00000351769.

Structurei

Secondary structure

1
493
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 163Combined sources
Turni20 – 234Combined sources
Helixi25 – 339Combined sources
Beta strandi37 – 404Combined sources
Helixi46 – 494Combined sources
Beta strandi53 – 575Combined sources
Turni58 – 614Combined sources
Beta strandi62 – 665Combined sources
Beta strandi72 – 765Combined sources
Helixi78 – 803Combined sources
Turni81 – 833Combined sources
Beta strandi84 – 896Combined sources
Helixi93 – 10311Combined sources
Helixi104 – 1063Combined sources
Beta strandi108 – 1136Combined sources
Helixi130 – 1323Combined sources
Helixi134 – 14714Combined sources
Beta strandi152 – 1587Combined sources
Helixi162 – 17312Combined sources
Turni174 – 1763Combined sources
Beta strandi178 – 1869Combined sources
Helixi197 – 20610Combined sources
Beta strandi211 – 2144Combined sources
Turni218 – 2203Combined sources
Beta strandi221 – 2233Combined sources
Helixi224 – 23411Combined sources
Beta strandi237 – 2426Combined sources
Helixi243 – 2475Combined sources
Helixi249 – 2524Combined sources
Helixi260 – 27314Combined sources
Helixi278 – 28811Combined sources
Turni289 – 2913Combined sources
Helixi296 – 3038Combined sources
Helixi307 – 3137Combined sources
Helixi317 – 33317Combined sources
Helixi336 – 3383Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XP7X-ray1.90A1-340[»]
ProteinModelPortaliQ9NX74.
SMRiQ9NX74. Positions 7-339, 352-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini369 – 43668DRBMAdd
BLAST

Sequence similaritiesi

Belongs to the Dus family. Dus2 subfamily.Curated

Phylogenomic databases

eggNOGiCOG0042.
GeneTreeiENSGT00550000075019.
HOGENOMiHOG000195580.
HOVERGENiHBG079551.
InParanoidiQ9NX74.
KOiK05543.
OMAiTSGVIKM.
PhylomeDBiQ9NX74.
TreeFamiTF106151.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.30.160.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR014720. dsRNA-bd_dom.
IPR001269. tRNA_hU_synthase.
IPR018517. tRNA_hU_synthase_CS.
[Graphical view]
PANTHERiPTHR11082. PTHR11082. 1 hit.
PfamiPF00035. dsrm. 1 hit.
PF01207. Dus. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 1 hit.
[Graphical view]
PROSITEiPS01136. UPF0034. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NX74-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILNSLSLCY HNKLILAPMV RVGTLPMRLL ALDYGADIVY CEELIDLKMI
60 70 80 90 100
QCKRVVNEVL STVDFVAPDD RVVFRTCERE QNRVVFQMGT SDAERALAVA
110 120 130 140 150
RLVENDVAGI DVNMGCPKQY STKGGMGAAL LSDPDKIEKI LSTLVKGTRR
160 170 180 190 200
PVTCKIRILP SLEDTLSLVK RIERTGIAAI AVHGRKREER PQHPVSCEVI
210 220 230 240 250
KAIADTLSIP VIANGGSHDH IQQYSDIEDF RQATAASSVM VARAAMWNPS
260 270 280 290 300
IFLKEGLRPL EEVMQKYIRY AVQYDNHYTN TKYCLCQMLR EQLESPQGRL
310 320 330 340 350
LHAAQSSREI CEAFGLGAFY EETTQELDAQ QARLSAKTSE QTGEPAEDTS
360 370 380 390 400
GVIKMAVKFD RRAYPAQITP KMCLLEWCRR EKLAQPVYET VQRPLDRLFS
410 420 430 440 450
SIVTVAEQKY QSTLWDKSKK LAEQAAAIVC LRSQGLPEGR LGEESPSLHK
460 470 480 490
RKREAPDQDP GGPRAQELAQ PGDLCKKPFV ALGSGEESPL EGW
Length:493
Mass (Da):55,050
Last modified:October 1, 2000 - v1
Checksum:i8CFE5046CCF79DCD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB101210 mRNA. Translation: BAE07219.1.
AK000406 mRNA. Translation: BAA91143.1.
AK290578 mRNA. Translation: BAF83267.1.
AC130462 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83207.1.
BC006527 mRNA. Translation: AAH06527.1.
CCDSiCCDS10859.1.
RefSeqiNP_001258691.1. NM_001271762.1.
NP_001258692.1. NM_001271763.1.
NP_060273.1. NM_017803.4.
UniGeneiHs.534460.
Hs.744492.

Genome annotation databases

EnsembliENST00000358896; ENSP00000351769; ENSG00000167264.
ENST00000565263; ENSP00000455229; ENSG00000167264.
GeneIDi54920.
KEGGihsa:54920.
UCSCiuc002evi.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB101210 mRNA. Translation: BAE07219.1.
AK000406 mRNA. Translation: BAA91143.1.
AK290578 mRNA. Translation: BAF83267.1.
AC130462 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83207.1.
BC006527 mRNA. Translation: AAH06527.1.
CCDSiCCDS10859.1.
RefSeqiNP_001258691.1. NM_001271762.1.
NP_001258692.1. NM_001271763.1.
NP_060273.1. NM_017803.4.
UniGeneiHs.534460.
Hs.744492.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XP7X-ray1.90A1-340[»]
ProteinModelPortaliQ9NX74.
SMRiQ9NX74. Positions 7-339, 352-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120261. 3 interactions.
IntActiQ9NX74. 3 interactions.
MINTiMINT-3076069.
STRINGi9606.ENSP00000351769.

PTM databases

PhosphoSiteiQ9NX74.

Polymorphism and mutation databases

DMDMi73620832.

Proteomic databases

MaxQBiQ9NX74.
PaxDbiQ9NX74.
PRIDEiQ9NX74.

Protocols and materials databases

DNASUi54920.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358896; ENSP00000351769; ENSG00000167264.
ENST00000565263; ENSP00000455229; ENSG00000167264.
GeneIDi54920.
KEGGihsa:54920.
UCSCiuc002evi.4. human.

Organism-specific databases

CTDi54920.
GeneCardsiGC16P068021.
HGNCiHGNC:26014. DUS2.
HPAiHPA042560.
HPA043528.
MIMi609707. gene.
neXtProtiNX_Q9NX74.
PharmGKBiPA142671937.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0042.
GeneTreeiENSGT00550000075019.
HOGENOMiHOG000195580.
HOVERGENiHBG079551.
InParanoidiQ9NX74.
KOiK05543.
OMAiTSGVIKM.
PhylomeDBiQ9NX74.
TreeFamiTF106151.

Enzyme and pathway databases

BRENDAi1.3.1.91. 2681.

Miscellaneous databases

GenomeRNAii54920.
NextBioi57992.
PROiQ9NX74.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NX74.
CleanExiHS_DUS2L.
ExpressionAtlasiQ9NX74. baseline and differential.
GenevisibleiQ9NX74. HS.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.30.160.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR014720. dsRNA-bd_dom.
IPR001269. tRNA_hU_synthase.
IPR018517. tRNA_hU_synthase_CS.
[Graphical view]
PANTHERiPTHR11082. PTHR11082. 1 hit.
PfamiPF00035. dsrm. 1 hit.
PF01207. Dus. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 1 hit.
[Graphical view]
PROSITEiPS01136. UPF0034. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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.
  6. "Interaction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKR."
    Mittelstadt M., Frump A., Khuu T., Fowlkes V., Handy I., Patel C.V., Patel R.C.
    Nucleic Acids Res. 36:998-1008(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRKRA AND EIF2AK2.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDUS2L_HUMAN
AccessioniPrimary (citable) accession number: Q9NX74
Secondary accession number(s): A8K3G3, Q4H4D9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.