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Protein

tRNA pseudouridine synthase A, mitochondrial

Gene

Pus1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts specific uridines to PSI in a number of tRNA substrates. Acts on positions 27/28 in the anticodon stem and also positions 34 and 36 in the anticodon of an intron containing tRNA. Involved in regulation of nuclear receptor activity possibly through pseudouridylation of SRA1 RNA. Isoforms 3 and 4 do not form pseudouridine when expressed in vitro.3 Publications

Catalytic activityi

tRNA uridine(38-40) = tRNA pseudouridine(38-40).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei142 – 1421NucleophileBy similarity
Binding sitei197 – 1971SubstrateBy similarity

GO - Molecular functioni

  • ligand-dependent nuclear receptor transcription coactivator activity Source: MGI
  • poly(A) RNA binding Source: MGI
  • pseudouridine synthase activity Source: MGI

GO - Biological processi

  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • tRNA pseudouridine synthesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

tRNA processing

Enzyme and pathway databases

BRENDAi4.2.1.70. 3474.
5.4.99.B22. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA pseudouridine synthase A, mitochondrial (EC:5.4.99.12)
Alternative name(s):
tRNA pseudouridine(38-40) synthase
tRNA pseudouridylate synthase I
tRNA-uridine isomerase I
Gene namesi
Name:Pus1
ORF Names:MNCb-0873
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1929237. Pus1.

Subcellular locationi

Isoform 1 :
Isoform 2 :

GO - Cellular componenti

  • mitochondrion Source: MGI
  • nucleolus Source: MGI
  • nucleus Source: MGI
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 423tRNA pseudouridine synthase A, mitochondrialPRO_0000057518
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei411 – 4111PhosphoserineBy similarity
Modified residuei416 – 4161PhosphoserineCombined sources
Modified residuei422 – 4221PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9WU56.
MaxQBiQ9WU56.
PaxDbiQ9WU56.
PRIDEiQ9WU56.

PTM databases

PhosphoSiteiQ9WU56.

Expressioni

Gene expression databases

BgeeiQ9WU56.
CleanExiMM_PUS1.
ExpressionAtlasiQ9WU56. baseline and differential.
GenevisibleiQ9WU56. MM.

Interactioni

Subunit structurei

Forms a complex with RARG and the SRA1 RNA in the nucleus.1 Publication

Protein-protein interaction databases

BioGridi207924. 1 interaction.
STRINGi10090.ENSMUSP00000083844.

Structurei

3D structure databases

ProteinModelPortaliQ9WU56.
SMRiQ9WU56. Positions 79-390.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2553. Eukaryota.
COG0101. LUCA.
GeneTreeiENSGT00510000047706.
HOVERGENiHBG000489.
InParanoidiQ9WU56.
KOiK06173.
OrthoDBiEOG79KPFG.
PhylomeDBiQ9WU56.

Family and domain databases

Gene3Di3.30.70.580. 1 hit.
3.30.70.660. 1 hit.
InterProiIPR020103. PsdUridine_synth_cat_dom.
IPR001406. PsdUridine_synth_TruA.
IPR020097. PsdUridine_synth_TruA_a/b_dom.
IPR020095. PsdUridine_synth_TruA_C.
IPR020094. PsdUridine_synth_TruA_N.
[Graphical view]
PANTHERiPTHR11142. PTHR11142. 1 hit.
PfamiPF01416. PseudoU_synth_1. 1 hit.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 1 hit.
TIGRFAMsiTIGR00071. hisT_truA. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9WU56-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGFPRLWAAL LRNWGRWTAR PGPRVPGLPP MAGNKVPPAL ASHQPDRKGR
60 70 80 90 100
GGWVWEETEH PAKRVKGGED EEPPRKLPKR KIVLLMAYSG KGYHGMQRNL
110 120 130 140 150
GSSQFRTIED DLVSALVQAG CIPENHGTDM RKMSFQRCAR TDKGVSAAGQ
160 170 180 190 200
VVSLKVWLID DILDKINSHL PSHIRILGLK RVTGGFNSKN KCDARTYCYM
210 220 230 240 250
LPTFAFAHKD RDVQDESYRL SAETLQQVNR LLACYKGTHN FHNFTSQKGP
260 270 280 290 300
REPSARRYIL EMYCEEPFVR EGLEFAVIKV KGQSFMMHQI RKMVGLVVAI
310 320 330 340 350
VKGYAPESVL ERSWGEEKVD VPKAPGLGLV LERVHFEKYN QRFGGDGLHE
360 370 380 390 400
PLDWTQEEGK VTAFKEQYIY PTIVSTERDE RSMAQWLNTL PIHNFSGTAL
410 420
GAADTGAKVP SSLEGSEGDG DTD
Length:423
Mass (Da):47,502
Last modified:September 5, 2006 - v2
Checksum:iC71FDBF60F29295A
GO
Isoform 2 (identifier: Q9WU56-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.

Show »
Length:393
Mass (Da):44,093
Checksum:i4CE2BD836B15A54A
GO
Isoform 3 (identifier: Q9WU56-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.
     143-143: K → KPLRTSACFCLYTGFLFHW

Show »
Length:411
Mass (Da):46,238
Checksum:i152A6D10552F88FA
GO
Isoform 4 (identifier: Q9WU56-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.
     98-143: Missing.

Note: No experimental confirmation available.
Show »
Length:347
Mass (Da):38,927
Checksum:i326246638DFAD35F
GO

Sequence cautioni

The sequence BAA95047.1 differs from that shown. Reason: Frameshift at position 230. Curated
The sequence BAC40817.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481K → E in BAC40817 (PubMed:16141072).Curated
Sequence conflicti52 – 521G → D in BAC40817 (PubMed:16141072).Curated
Sequence conflicti406 – 4061G → V in AAH21446 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3030Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_020114Add
BLAST
Alternative sequencei98 – 14346Missing in isoform 4. 1 PublicationVSP_021791Add
BLAST
Alternative sequencei143 – 1431K → KPLRTSACFCLYTGFLFHW in isoform 3. 1 PublicationVSP_021792

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF116237 mRNA. Translation: AAD21041.1.
AF269250 Genomic DNA. Translation: AAG35307.1.
AF269250 Genomic DNA. Translation: AAG35308.1.
AB041563 mRNA. Translation: BAA95047.1. Frameshift.
AK089258 mRNA. Translation: BAC40817.1. Different initiation.
AK138570 mRNA. Translation: BAE23701.1.
BC021446 mRNA. Translation: AAH21446.2.
BC034359 mRNA. Translation: AAH34359.2.
CCDSiCCDS19531.1. [Q9WU56-1]
CCDS39212.1. [Q9WU56-2]
RefSeqiNP_001020733.1. NM_001025562.2. [Q9WU56-2]
NP_062674.2. NM_019700.4. [Q9WU56-1]
XP_006535208.1. XM_006535145.2. [Q9WU56-3]
XP_006535209.1. XM_006535146.2. [Q9WU56-3]
XP_006535212.1. XM_006535149.2. [Q9WU56-4]
XP_011247847.1. XM_011249545.1. [Q9WU56-2]
UniGeneiMm.23528.

Genome annotation databases

EnsembliENSMUST00000031481; ENSMUSP00000031481; ENSMUSG00000029507. [Q9WU56-2]
ENSMUST00000031483; ENSMUSP00000031483; ENSMUSG00000029507. [Q9WU56-1]
ENSMUST00000112426; ENSMUSP00000108045; ENSMUSG00000029507. [Q9WU56-4]
ENSMUST00000170468; ENSMUSP00000130814; ENSMUSG00000029507. [Q9WU56-2]
GeneIDi56361.
KEGGimmu:56361.
UCSCiuc008yrm.1. mouse. [Q9WU56-4]
uc008yrn.1. mouse. [Q9WU56-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF116237 mRNA. Translation: AAD21041.1.
AF269250 Genomic DNA. Translation: AAG35307.1.
AF269250 Genomic DNA. Translation: AAG35308.1.
AB041563 mRNA. Translation: BAA95047.1. Frameshift.
AK089258 mRNA. Translation: BAC40817.1. Different initiation.
AK138570 mRNA. Translation: BAE23701.1.
BC021446 mRNA. Translation: AAH21446.2.
BC034359 mRNA. Translation: AAH34359.2.
CCDSiCCDS19531.1. [Q9WU56-1]
CCDS39212.1. [Q9WU56-2]
RefSeqiNP_001020733.1. NM_001025562.2. [Q9WU56-2]
NP_062674.2. NM_019700.4. [Q9WU56-1]
XP_006535208.1. XM_006535145.2. [Q9WU56-3]
XP_006535209.1. XM_006535146.2. [Q9WU56-3]
XP_006535212.1. XM_006535149.2. [Q9WU56-4]
XP_011247847.1. XM_011249545.1. [Q9WU56-2]
UniGeneiMm.23528.

3D structure databases

ProteinModelPortaliQ9WU56.
SMRiQ9WU56. Positions 79-390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207924. 1 interaction.
STRINGi10090.ENSMUSP00000083844.

PTM databases

PhosphoSiteiQ9WU56.

Proteomic databases

EPDiQ9WU56.
MaxQBiQ9WU56.
PaxDbiQ9WU56.
PRIDEiQ9WU56.

Protocols and materials databases

DNASUi56361.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031481; ENSMUSP00000031481; ENSMUSG00000029507. [Q9WU56-2]
ENSMUST00000031483; ENSMUSP00000031483; ENSMUSG00000029507. [Q9WU56-1]
ENSMUST00000112426; ENSMUSP00000108045; ENSMUSG00000029507. [Q9WU56-4]
ENSMUST00000170468; ENSMUSP00000130814; ENSMUSG00000029507. [Q9WU56-2]
GeneIDi56361.
KEGGimmu:56361.
UCSCiuc008yrm.1. mouse. [Q9WU56-4]
uc008yrn.1. mouse. [Q9WU56-1]

Organism-specific databases

CTDi80324.
MGIiMGI:1929237. Pus1.

Phylogenomic databases

eggNOGiKOG2553. Eukaryota.
COG0101. LUCA.
GeneTreeiENSGT00510000047706.
HOVERGENiHBG000489.
InParanoidiQ9WU56.
KOiK06173.
OrthoDBiEOG79KPFG.
PhylomeDBiQ9WU56.

Enzyme and pathway databases

BRENDAi4.2.1.70. 3474.
5.4.99.B22. 3474.

Miscellaneous databases

NextBioi312382.
PROiQ9WU56.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WU56.
CleanExiMM_PUS1.
ExpressionAtlasiQ9WU56. baseline and differential.
GenevisibleiQ9WU56. MM.

Family and domain databases

Gene3Di3.30.70.580. 1 hit.
3.30.70.660. 1 hit.
InterProiIPR020103. PsdUridine_synth_cat_dom.
IPR001406. PsdUridine_synth_TruA.
IPR020097. PsdUridine_synth_TruA_a/b_dom.
IPR020095. PsdUridine_synth_TruA_C.
IPR020094. PsdUridine_synth_TruA_N.
[Graphical view]
PANTHERiPTHR11142. PTHR11142. 1 hit.
PfamiPF01416. PseudoU_synth_1. 1 hit.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 1 hit.
TIGRFAMsiTIGR00071. hisT_truA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a mammalian pseudouridine synthase."
    Chen J., Patton J.R.
    RNA 5:409-419(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY.
  2. "Mouse pseudouridine synthase 1: gene structure and alternative splicing of pre-mRNA."
    Chen J., Patton J.R.
    Biochem. J. 352:465-473(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2 AND 3), FUNCTION, ALTERNATIVE SPLICING (ISOFORM 4).
    Strain: 129/SvJ.
  3. "Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
    Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "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] (ISOFORMS 1 AND 4).
    Strain: C57BL/6J and NOD.
    Tissue: Dendritic cell and Spinal cord.
  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] (ISOFORM 1).
    Strain: Czech II and FVB/N.
    Tissue: Mammary gland.
  6. "Regulation of nuclear receptor activity by a pseudouridine synthase through posttranscriptional modification of steroid receptor RNA activator."
    Zhao X., Patton J.R., Davis S.L., Florence B., Ames S.J., Spanjaard R.A.
    Mol. Cell 15:549-558(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH RARG AND SRA1.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416 AND THR-422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney and Lung.

Entry informationi

Entry nameiTRUA_MOUSE
AccessioniPrimary (citable) accession number: Q9WU56
Secondary accession number(s): Q3UUC6
, Q791J1, Q8C250, Q8VDQ3, Q9EQD1, Q9JJE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 5, 2006
Last modified: May 11, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.