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Reviewed, UniProtKB/Swiss-Prot Q9Y3E5 (PTH2_HUMAN)

Last modified February 9, 2010. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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
Alternative name(s):
    Bcl-2 inhibitor of transcription 1
Gene names
Name: PTRH2
Synonyms: BIT1, PTH2
ORF Names: CGI-147
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length179 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.6

Promotes caspase-independent apoptosis by regulating the function of two transcriptional regulators, AES and TLE1. Ref.6

Catalytic activity

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

Subunit structure

Monomer.

Subcellular location

Mitochondrion.

Sequence similarities

Belongs to the PTH2 family.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processapoptosis

Inferred from electronic annotation. Source: UniProtKB-KW

translation

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion

Inferred from direct assay. Source: HPA

   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 – 6262Mitochondrion Potential
Chain63 – 179117Peptidyl-tRNA hydrolase 2, mitochondrial
PRO_0000029862

Amino acid modifications

Modified residue571Phosphoserine Ref.7

Secondary structure

.................. 179
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y3E5-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 11A0BA9ECF6B5E46

FASTA17919,194
        10         20         30         40         50         60 
MPSKSLVMEY LAHPSTLGLA VGVACGMCLG WSLRVCFGML PKSKTSKTHT DTESEASILG 

        70         80         90        100        110        120 
DSGEYKMILV VRNDLKMGKG KVAAQCSHAA VSAYKQIQRR NPEMLKQWEY CGQPKVVVKA 

       130        140        150        160        170 
PDEETLIALL AHAKMLGLTV SLIQDAGRTQ IAPGSQTVLG IGPGPADLID KVTGHLKLY 

« Hide

References

« Hide 'large scale' references
[1]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed: 10810093] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Uterus.
[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. expand/collapse author list , 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 (SEP-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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-179.
Tissue: Testis.
[6]"A mitochondrial protein, Bit1, mediates apoptosis regulated by integrins and Groucho/TLE corepressors."
Jan Y., Matter M., Pai J.-T., Chen Y.-L., Pilch J., Komatsu M., Ong E., Fukuda M., Ruoslahti E.
Cell 116:751-762(2004) [PubMed: 15006356] [Abstract]
Cited for: FUNCTION IN APOPTOSIS.
[7]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, MASS SPECTROMETRY.
[8]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]"Crystal structure of a human peptidyl-tRNA hydrolase reveals a new fold and suggests basis for a bifunctional activity."
De Pereda J.M., Waas W.F., Jan Y., Ruoslahti E., Schimmel P., Pascual J.
J. Biol. Chem. 279:8111-8115(2004) [PubMed: 14660562] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 63-179.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF151905 mRNA. Translation: AAD34142.1.
AK098219 mRNA. Translation: BAG53596.1.
CH471109 Genomic DNA. Translation: EAW94394.1.
BC006807 mRNA. Translation: AAH06807.1.
AL137322 mRNA. Translation: CAB70696.1.
IPIIPI00032903.
PIRT46479.
RefSeqNP_057161.1.
UniGeneHs.12677

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q7SX-ray2.00A/B63-179[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Y3E5. 1 interaction.
STRINGQ9Y3E5.

PTM databases

PhosphoSiteQ9Y3E5.

Proteomic databases

PRIDEQ9Y3E5.

Genome annotation databases

EnsemblENST00000393038; ENSP00000376758; ENSG00000141378; Homo sapiens. [Genome view]
ENST00000409433; ENSP00000387180; ENSG00000141378; Homo sapiens. [Genome view]
GeneID51651.
KEGGhsa:51651.
UCSCuc002ixt.1. human.

Organism-specific databases

CTD51651.
GeneCardsGC17M055131.
H-InvDBHIX0019799.
HGNCHGNC:24265. PTRH2.
HPAHPA012897.
MIM608625. gene.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG526257.
HOVERGENQ9Y3E5.
InParanoidQ9Y3E5.
OMAIQRRNPE.
OrthoDBEOG969TF4.
PhylomeDBQ9Y3E5.

Enzyme and pathway databases

BRENDA3.1.1.29. 247.

Gene expression databases

ArrayExpressQ9Y3E5.
BgeeQ9Y3E5.
CleanExHS_PTH2.
HS_PTRH2.
GenevestigatorQ9Y3E5.
GermOnlineENSG00000141378. Homo sapiens.

Family and domain databases

InterProIPR002833. Pep_tRNA_hydro_PTH2.
[Graphical view]
PfamPF01981. PTH2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00283. Pep_tRNA_hydro_PTH2. 1 hit.
ProtoNetSearch...

Other Resources

NextBio55610.
SOURCESearch...

Entry information

Entry namePTH2_HUMAN
AccessionPrimary (citable) accession number: Q9Y3E5
Secondary accession number(s): B3KUY4, Q9NTE5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: February 9, 2010
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Uncharacterized protein families (UPF)

List of uncharacterized protein family (UPF) entries

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