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Protein

Peptidyl-tRNA hydrolase 2, mitochondrial

Gene

PTRH2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • metabolic process Source: GOC
  • negative regulation of anoikis Source: UniProtKB
  • negative regulation of gene expression Source: UniProtKB
  • positive regulation of anoikis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BRENDAi3.1.1.29. 2681.

Protein family/group databases

MoonProtiQ9Y3E5.

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 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:24265. PTRH2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Neurologic, endocrine, and pancreatic disease, multisystem, infantile-onset (IMNEPD)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA progressive multisystem disease characterized by a variety of neurologic, endocrine, and, in some patients, pancreatic features. Variable clinical symptoms include global developmental delay, hypotonia, hearing loss, ataxia, hyporeflexia, facial dysmorphism, hypothyroidism, and pancreatic insufficiency.

See also OMIM:616263
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti85 – 851Q → P in IMNEPD. 1 Publication
VAR_073386

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi616263. phenotype.
PharmGKBiPA143485586.

Polymorphism and mutation databases

BioMutaiPTRH2.
DMDMi6686183.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki47 – 47Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki76 – 76Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki81 – 81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki95 – 95Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki106 – 106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki115 – 115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki171 – 171Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki177 – 177Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Ubiquitinated by PARK2 during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ9Y3E5.
PaxDbiQ9Y3E5.
PRIDEiQ9Y3E5.

PTM databases

PhosphoSiteiQ9Y3E5.

Expressioni

Gene expression databases

BgeeiQ9Y3E5.
CleanExiHS_PTH2.
HS_PTRH2.
ExpressionAtlasiQ9Y3E5. baseline and differential.
GenevisibleiQ9Y3E5. HS.

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. 27 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 – 728Combined sources
Helixi73 – 753Combined sources
Helixi79 – 10022Combined sources
Helixi102 – 1109Combined sources
Beta strandi115 – 1228Combined sources
Helixi123 – 13513Combined sources
Beta strandi140 – 1456Combined sources
Beta strandi147 – 1515Combined sources
Beta strandi153 – 16513Combined sources
Helixi166 – 1738Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000015991.
HOGENOMiHOG000227349.
HOVERGENiHBG049458.
InParanoidiQ9Y3E5.
KOiK04794.
OMAiKQVIVVR.
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

        10         20         30         40         50
MPSKSLVMEY LAHPSTLGLA VGVACGMCLG WSLRVCFGML PKSKTSKTHT
60 70 80 90 100
DTESEASILG DSGEYKMILV VRNDLKMGKG KVAAQCSHAA VSAYKQIQRR
110 120 130 140 150
NPEMLKQWEY CGQPKVVVKA PDEETLIALL AHAKMLGLTV SLIQDAGRTQ
160 170
IAPGSQTVLG IGPGPADLID KVTGHLKLY
Length:179
Mass (Da):19,194
Last modified:November 1, 1999 - v1
Checksum:i11A0BA9ECF6B5E46
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti85 – 851Q → P in IMNEPD. 1 Publication
VAR_073386

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001015509.1. NM_001015509.2.
NP_057161.1. NM_016077.4.
XP_011523189.1. XM_011524887.1.
UniGeneiHs.12677.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001015509.1. NM_001015509.2.
NP_057161.1. NM_016077.4.
XP_011523189.1. XM_011524887.1.
UniGeneiHs.12677.

3D structure databases

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

Protein-protein interaction databases

BioGridi119659. 27 interactions.
IntActiQ9Y3E5. 3 interactions.
MINTiMINT-4657346.
STRINGi9606.ENSP00000376758.

Protein family/group databases

MoonProtiQ9Y3E5.

PTM databases

PhosphoSiteiQ9Y3E5.

Polymorphism and mutation databases

BioMutaiPTRH2.
DMDMi6686183.

Proteomic databases

MaxQBiQ9Y3E5.
PaxDbiQ9Y3E5.
PRIDEiQ9Y3E5.

Protocols and materials databases

DNASUi51651.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51651.
GeneCardsiGC17M057774.
HGNCiHGNC:24265. PTRH2.
HPAiHPA012897.
MIMi608625. gene.
616263. phenotype.
neXtProtiNX_Q9Y3E5.
PharmGKBiPA143485586.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1990.
GeneTreeiENSGT00390000015991.
HOGENOMiHOG000227349.
HOVERGENiHBG049458.
InParanoidiQ9Y3E5.
KOiK04794.
OMAiKQVIVVR.
OrthoDBiEOG7PCJJ2.
PhylomeDBiQ9Y3E5.
TreeFamiTF324583.

Enzyme and pathway databases

BRENDAi3.1.1.29. 2681.

Miscellaneous databases

ChiTaRSiPTRH2. human.
EvolutionaryTraceiQ9Y3E5.
GenomeRNAii51651.
NextBioi55610.
PROiQ9Y3E5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y3E5.
CleanExiHS_PTH2.
HS_PTRH2.
ExpressionAtlasiQ9Y3E5. baseline and differential.
GenevisibleiQ9Y3E5. HS.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: INVOLVEMENT IN IMNEPD.
  10. "Accelerating novel candidate gene discovery in neurogenetic disorders via whole-exome sequencing of prescreened multiplex consanguineous families."
    Alazami A.M., Patel N., Shamseldin H.E., Anazi S., Al-Dosari M.S., Alzahrani F., Hijazi H., Alshammari M., Aldahmesh M.A., Salih M.A., Faqeih E., Alhashem A., Bashiri F.A., Al-Owain M., Kentab A.Y., Sogaty S., Al Tala S., Temsah M.H.
    , Tulbah M., Aljelaify R.F., Alshahwan S.A., Seidahmed M.Z., Alhadid A.A., Aldhalaan H., AlQallaf F., Kurdi W., Alfadhel M., Babay Z., Alsogheer M., Kaya N., Al-Hassnan Z.N., Abdel-Salam G.M., Al-Sannaa N., Al Mutairi F., El Khashab H.Y., Bohlega S., Jia X., Nguyen H.C., Hammami R., Adly N., Mohamed J.Y., Abdulwahab F., Ibrahim N., Naim E.A., Al-Younes B., Meyer B.F., Hashem M., Shaheen R., Xiong Y., Abouelhoda M., Aldeeri A.A., Monies D.M., Alkuraya F.S.
    Cell Rep. 10:148-161(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN IMNEPD, VARIANT IMNEPD PRO-85.
  11. "USP30 and parkin homeostatically regulate atypical ubiquitin chains on mitochondria."
    Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M., Kirkpatrick D.S., Bingol B., Corn J.E.
    Nat. Cell Biol. 17:160-169(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-47; LYS-76; LYS-81; LYS-95; LYS-106; LYS-115; LYS-171 AND LYS-177.
  12. "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: July 22, 2015
This is version 140 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
  7. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

External Data

Dasty 3

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 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.