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Q9Y3E5

- PTH2_HUMAN

UniProt

Q9Y3E5 - PTH2_HUMAN

Protein

Peptidyl-tRNA hydrolase 2, mitochondrial

Gene

PTRH2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.By similarity
    Promotes caspase-independent apoptosis by regulating the function of two transcriptional regulators, AES and TLE1.1 Publication

    Catalytic activityi

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

    GO - Molecular functioni

    1. aminoacyl-tRNA hydrolase activity Source: UniProtKB-EC
    2. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. negative regulation of anoikis Source: UniProtKB
    3. negative regulation of gene expression Source: UniProtKB
    4. positive regulation of anoikis Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    BRENDAi3.1.1.29. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-tRNA hydrolase 2, mitochondrial (EC:3.1.1.29)
    Short name:
    PTH 2
    Alternative name(s):
    Bcl-2 inhibitor of transcription 1
    Gene namesi
    Name:PTRH2
    Synonyms:BIT1, PTH2
    ORF Names:CGI-147
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:24265. PTRH2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB
    3. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA143485586.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6262MitochondrionSequence AnalysisAdd
    BLAST
    Chaini63 – 179117Peptidyl-tRNA hydrolase 2, mitochondrialPRO_0000029862Add
    BLAST

    Proteomic databases

    MaxQBiQ9Y3E5.
    PaxDbiQ9Y3E5.
    PRIDEiQ9Y3E5.

    PTM databases

    PhosphoSiteiQ9Y3E5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y3E5.
    BgeeiQ9Y3E5.
    CleanExiHS_PTH2.
    HS_PTRH2.
    GenevestigatoriQ9Y3E5.

    Organism-specific databases

    HPAiHPA012897.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AESQ081177EBI-1056751,EBI-717810
    PTK2Q053972EBI-1056751,EBI-702142

    Protein-protein interaction databases

    BioGridi119659. 17 interactions.
    IntActiQ9Y3E5. 3 interactions.
    MINTiMINT-4657346.
    STRINGi9606.ENSP00000376758.

    Structurei

    Secondary structure

    1
    179
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi65 – 728
    Helixi73 – 753
    Helixi79 – 10022
    Helixi102 – 1109
    Beta strandi115 – 1228
    Helixi123 – 13513
    Beta strandi140 – 1456
    Beta strandi147 – 1515
    Beta strandi153 – 16513
    Helixi166 – 1738

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Q7SX-ray2.00A/B63-179[»]
    ProteinModelPortaliQ9Y3E5.
    SMRiQ9Y3E5. Positions 63-179.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y3E5.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PTH2 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1990.
    HOGENOMiHOG000227349.
    HOVERGENiHBG049458.
    InParanoidiQ9Y3E5.
    KOiK04794.
    OMAiCGVCLGW.
    OrthoDBiEOG7PCJJ2.
    PhylomeDBiQ9Y3E5.
    TreeFamiTF324583.

    Family and domain databases

    Gene3Di3.40.1490.10. 1 hit.
    InterProiIPR023476. Pep_tRNA_hydro_II_dom.
    IPR002833. PTH2.
    [Graphical view]
    PfamiPF01981. PTH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF102462. SSF102462. 1 hit.
    TIGRFAMsiTIGR00283. arch_pth2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9Y3E5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSKSLVMEY LAHPSTLGLA VGVACGMCLG WSLRVCFGML PKSKTSKTHT    50
    DTESEASILG DSGEYKMILV VRNDLKMGKG KVAAQCSHAA VSAYKQIQRR 100
    NPEMLKQWEY CGQPKVVVKA PDEETLIALL AHAKMLGLTV SLIQDAGRTQ 150
    IAPGSQTVLG IGPGPADLID KVTGHLKLY 179
    Length:179
    Mass (Da):19,194
    Last modified:November 1, 1999 - v1
    Checksum:i11A0BA9ECF6B5E46
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS11618.1.
    PIRiT46479.
    RefSeqiNP_057161.1. NM_016077.3.
    XP_005257504.2. XM_005257447.2.
    UniGeneiHs.12677.

    Genome annotation databases

    EnsembliENST00000393038; ENSP00000376758; ENSG00000141378.
    ENST00000470557; ENSP00000464327; ENSG00000141378.
    GeneIDi51651.
    KEGGihsa:51651.
    UCSCiuc002ixt.3. human.

    Polymorphism databases

    DMDMi6686183.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS11618.1.
    PIRi T46479.
    RefSeqi NP_057161.1. NM_016077.3.
    XP_005257504.2. XM_005257447.2.
    UniGenei Hs.12677.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Q7S X-ray 2.00 A/B 63-179 [» ]
    ProteinModelPortali Q9Y3E5.
    SMRi Q9Y3E5. Positions 63-179.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119659. 17 interactions.
    IntActi Q9Y3E5. 3 interactions.
    MINTi MINT-4657346.
    STRINGi 9606.ENSP00000376758.

    PTM databases

    PhosphoSitei Q9Y3E5.

    Polymorphism databases

    DMDMi 6686183.

    Proteomic databases

    MaxQBi Q9Y3E5.
    PaxDbi Q9Y3E5.
    PRIDEi Q9Y3E5.

    Protocols and materials databases

    DNASUi 51651.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000393038 ; ENSP00000376758 ; ENSG00000141378 .
    ENST00000470557 ; ENSP00000464327 ; ENSG00000141378 .
    GeneIDi 51651.
    KEGGi hsa:51651.
    UCSCi uc002ixt.3. human.

    Organism-specific databases

    CTDi 51651.
    GeneCardsi GC17M057774.
    HGNCi HGNC:24265. PTRH2.
    HPAi HPA012897.
    MIMi 608625. gene.
    neXtProti NX_Q9Y3E5.
    PharmGKBi PA143485586.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1990.
    HOGENOMi HOG000227349.
    HOVERGENi HBG049458.
    InParanoidi Q9Y3E5.
    KOi K04794.
    OMAi CGVCLGW.
    OrthoDBi EOG7PCJJ2.
    PhylomeDBi Q9Y3E5.
    TreeFami TF324583.

    Enzyme and pathway databases

    BRENDAi 3.1.1.29. 2681.

    Miscellaneous databases

    ChiTaRSi PTRH2. human.
    EvolutionaryTracei Q9Y3E5.
    GenomeRNAii 51651.
    NextBioi 55610.
    PROi Q9Y3E5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y3E5.
    Bgeei Q9Y3E5.
    CleanExi HS_PTH2.
    HS_PTRH2.
    Genevestigatori Q9Y3E5.

    Family and domain databases

    Gene3Di 3.40.1490.10. 1 hit.
    InterProi IPR023476. Pep_tRNA_hydro_II_dom.
    IPR002833. PTH2.
    [Graphical view ]
    Pfami PF01981. PTH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF102462. SSF102462. 1 hit.
    TIGRFAMsi TIGR00283. arch_pth2. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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.
      , 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: Uterus.
    3. 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    5. 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] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOSIS.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 63-179.

    Entry informationi

    Entry nameiPTH2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y3E5
    Secondary accession number(s): B3KUY4, Q9NTE5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 131 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 17
      Human chromosome 17: 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
    5. Uncharacterized protein families (UPF)
      List of uncharacterized protein family (UPF) entries

    External Data

    Dasty 3