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Protein

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

Gene

Dus2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity). Negatively regulates the activation of EIF2AK2/PKR (By similarity).By similarity

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Flavoprotein, FMN, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (EC:1.3.1.-)
Alternative name(s):
Dihydrouridine synthase 2
tRNA-dihydrouridine synthase 2-like
Gene namesi
Name:Dus2
Synonyms:Dus2l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1913619. Dus2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 493493tRNA-dihydrouridine(20) synthase [NAD(P)+]-likePRO_0000162158Add
BLAST

Proteomic databases

EPDiQ9D7B1.
MaxQBiQ9D7B1.
PaxDbiQ9D7B1.
PRIDEiQ9D7B1.

PTM databases

PhosphoSiteiQ9D7B1.

Expressioni

Gene expression databases

BgeeiQ9D7B1.
ExpressionAtlasiQ9D7B1. baseline and differential.
GenevisibleiQ9D7B1. MM.

Interactioni

Subunit structurei

Interacts with EPRS. Interacts (via DRBM domain) with PRKRA and EIF2AK2/PKR (via DRBM 1 domain).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034375.

Structurei

Secondary structure

1
493
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi350 – 3556Combined sources
Helixi361 – 3633Combined sources
Helixi370 – 38011Combined sources
Beta strandi390 – 3923Combined sources
Beta strandi394 – 3963Combined sources
Beta strandi399 – 4057Combined sources
Beta strandi408 – 4147Combined sources
Beta strandi416 – 4183Combined sources
Helixi419 – 43416Combined sources
Beta strandi437 – 4393Combined sources
Turni440 – 4423Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WHNNMR-A350-464[»]
ProteinModelPortaliQ9D7B1.
SMRiQ9D7B1. Positions 7-338, 352-464.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9D7B1.

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

eggNOGiKOG2334. Eukaryota.
COG0042. LUCA.
GeneTreeiENSGT00550000075019.
HOGENOMiHOG000195580.
HOVERGENiHBG079551.
InParanoidiQ9D7B1.
KOiK05543.
OMAiTSGVIKM.
PhylomeDBiQ9D7B1.
TreeFamiTF106151.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.30.160.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR014720. dsRBD_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.

Q9D7B1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVNSLSLCY HNKLILAPMV RVGTLPMRLL ALDYGADIVY CEELIDLKML
60 70 80 90 100
QCKRVVNEVL STVDFVAPDD RVVFRTCERE QSRVVFQMGT SDAERALAVA
110 120 130 140 150
RLVENDVAGI DVNMGCPKEY STKGGMGAAL LSDPDKIEKI LSTLVKGTHR
160 170 180 190 200
PVTCKIRILP SLEDTLNLVK RIERTGISAI AVHGRNRDER PQHPVSCEVI
210 220 230 240 250
RAIAETLSIP VIANGGSHDH IQQHVDIEDF RQATAASSVM VARAAMWNPS
260 270 280 290 300
IFLKDGLRPL EEVMQKYIRY AVQYDNHYTN TKYCLCQMLR EQLESPQGRL
310 320 330 340 350
LHAAQSSQEI CEAFGLGAFY EETIRELDAR RADLLAKTPE AVEEPAEDTS
360 370 380 390 400
GIIKMAIRFD RRAYPPQITP KMCLLEWCRR EKLPQPVYET VQRTIDRMFC
410 420 430 440 450
SVVTVAEQKY QSTLWDKSKK LAEQTAAIVC LRSQGLPEGR LGEESPSLNK
460 470 480 490
RKREAPDQDP GGPRVQEPAL PGEICKKPFV TLDSSEENLL EGC
Length:493
Mass (Da):55,325
Last modified:June 1, 2001 - v1
Checksum:iB66BDCB06B096299
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009391 mRNA. Translation: BAB26260.1.
BC058431 mRNA. Translation: AAH58431.1.
CCDSiCCDS22627.1.
RefSeqiNP_001288105.1. NM_001301176.1.
NP_079794.1. NM_025518.4.
XP_006531341.1. XM_006531278.2.
UniGeneiMm.287500.

Genome annotation databases

EnsembliENSMUST00000034375; ENSMUSP00000034375; ENSMUSG00000031901.
GeneIDi66369.
KEGGimmu:66369.
UCSCiuc009nfa.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009391 mRNA. Translation: BAB26260.1.
BC058431 mRNA. Translation: AAH58431.1.
CCDSiCCDS22627.1.
RefSeqiNP_001288105.1. NM_001301176.1.
NP_079794.1. NM_025518.4.
XP_006531341.1. XM_006531278.2.
UniGeneiMm.287500.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WHNNMR-A350-464[»]
ProteinModelPortaliQ9D7B1.
SMRiQ9D7B1. Positions 7-338, 352-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034375.

PTM databases

PhosphoSiteiQ9D7B1.

Proteomic databases

EPDiQ9D7B1.
MaxQBiQ9D7B1.
PaxDbiQ9D7B1.
PRIDEiQ9D7B1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034375; ENSMUSP00000034375; ENSMUSG00000031901.
GeneIDi66369.
KEGGimmu:66369.
UCSCiuc009nfa.2. mouse.

Organism-specific databases

CTDi54920.
MGIiMGI:1913619. Dus2.

Phylogenomic databases

eggNOGiKOG2334. Eukaryota.
COG0042. LUCA.
GeneTreeiENSGT00550000075019.
HOGENOMiHOG000195580.
HOVERGENiHBG079551.
InParanoidiQ9D7B1.
KOiK05543.
OMAiTSGVIKM.
PhylomeDBiQ9D7B1.
TreeFamiTF106151.

Miscellaneous databases

EvolutionaryTraceiQ9D7B1.
NextBioi321469.
PROiQ9D7B1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D7B1.
ExpressionAtlasiQ9D7B1. baseline and differential.
GenevisibleiQ9D7B1. MM.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.30.160.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR014720. dsRBD_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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Tongue.
  2. "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] OF 205-493.
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.
  4. "Solution structure of the DSRBD from hypothetical protein BAB26260."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 350-464.

Entry informationi

Entry nameiDUS2L_MOUSE
AccessioniPrimary (citable) accession number: Q9D7B1
Secondary accession number(s): Q6PDX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2001
Last modified: May 11, 2016
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

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.