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Reviewed, UniProtKB/Swiss-Prot Q8R2Y8 (PTH2_MOUSE)

Last modified November 3, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-tRNA hydrolase 2, mitochondrial
      Short name=PTH 2
    EC=3.1.1.29
Gene names
Name: Ptrh2
Synonyms: Pth2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length181 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis By similarity.

Catalytic activity

N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA.

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the PTH2 family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionHydrolase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processtranslation

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

   Molecular functionaminoacyl-tRNA hydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6464Mitochondrion Potential
Chain65 – 181117Peptidyl-tRNA hydrolase 2, mitochondrial
PRO_0000029863

Amino acid modifications

Modified residue591Phosphoserine By similarity

Experimental info

Sequence conflict1711I → T in BAC30159. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8R2Y8-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: C341176DE560C2B8

FASTA18119,527
        10         20         30         40         50         60 
MLSKFLTMEY LVHPGTLSLA AGVACGMCLG WGLRSHLGMF PQNSTSEANR DTETGTEASI 

        70         80         90        100        110        120 
LGESGEYKMI LVVRTDLKMG KGKVAAQCSH AAVSAYKQTQ RRSPQVLKEW EYCGQPKVVV 

       130        140        150        160        170        180 
KAPDEDTLIQ LLTHAKTLGL TVSLIQDAGR TQIEPGSRTV LGIGPGPVEL IDEVTGHLKL 


Y 

« Hide

References

[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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Hypothalamus, Skin and Testis.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

AK028555 mRNA. Translation: BAC26006.1. Different initiation.
AK031620 mRNA. Translation: BAC27482.1.
AK038888 mRNA. Translation: BAC30159.1.
BC026947 mRNA. Translation: AAH26947.1.
IPIIPI00853967.
RefSeqNP_001092280.1.
NP_778169.1.
UniGeneMm.24868

3D structure databases

SMRQ8R2Y8. Positions 65-181.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8R2Y8.

PTM databases

PhosphoSiteQ8R2Y8.

Proteomic databases

PRIDEQ8R2Y8.

Genome annotation databases

EnsemblENSMUST00000100665; ENSMUSP00000098230; ENSMUSG00000072582; Mus musculus. [Genome view]
ENSMUST00000108021; ENSMUSP00000103656; ENSMUSG00000072582; Mus musculus. [Genome view]
ENSMUST00000108022; ENSMUSP00000103657; ENSMUSG00000072582; Mus musculus. [Genome view]
GeneID217057.
KEGGmmu:217057.
UCSCuc007ksz.1. mouse.

Organism-specific databases

CTD217057.
MGIMGI:2444848. Ptrh2.

Phylogenomic databases

HOGENOMQ8R2Y8.
HOVERGENQ8R2Y8.
OMAMEYLVHP.

Enzyme and pathway databases

BRENDA3.1.1.29. 244.

Gene expression databases

ArrayExpressQ8R2Y8.
BgeeQ8R2Y8.
CleanExMM_PTH2.
MM_PTRH2.
GenevestigatorQ8R2Y8.
GermOnlineENSMUSG00000072582. Mus musculus.

Family and domain databases

InterProIPR002833. Pep_tRNA_hydro_PTH2.
[Graphical view]
PfamPF01981. PTH2. 1 hit.
[Graphical view]
ProDomPD010667. UPF0099. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00283. Pep_tRNA_hydro_PTH2. 1 hit.
ProtoNetSearch...

Other Resources

NextBio375534.
SOURCESearch...

Entry information

Entry namePTH2_MOUSE
AccessionPrimary (citable) accession number: Q8R2Y8
Secondary accession number(s): Q8BI01, Q8BI31
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: June 1, 2002
Last modified: November 3, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents