Q9Y3E5 (PTH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	179 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Apoptosis
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of anoikis Inferred from mutant phenotype PubMed 21383007. Source: UniProtKB negative regulation of gene expression Inferred from mutant phenotype Ref.6. Source: UniProtKB positive regulation of anoikis Inferred from mutant phenotype Ref.6PubMed 22952044. Source: UniProtKB
Cellular_component	cytosol Inferred from mutant phenotype Ref.6PubMed 22952044. Source: UniProtKB mitochondrion Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	aminoacyl-tRNA hydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AES	Q08117	7	EBI-1056751,EBI-717810
PTK2	Q05397	2	EBI-1056751,EBI-702142

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 62

62

Mitochondrion Potential

Chain

63 – 179

117

Peptidyl-tRNA hydrolase 2, mitochondrial

PRO_0000029862

Amino acid modifications

Modified residue

57

1

Phosphoserine Ref.7

Secondary structure

1

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179

Helix Strand Turn

Details...

Beta strand

65 – 72

8

Helix

73 – 75

3

Helix

79 – 100

22

Helix

102 – 110

9

Beta strand

115 – 122

8

Helix

123 – 135

13

Beta strand

140 – 145

6

Beta strand

147 – 151

5

Beta strand

153 – 165

13

Helix

166 – 173

8

Sequences

	Sequence		Length	Mass (Da)
	Q9Y3E5 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 11A0BA9ECF6B5E46	FASTA	179	19,194
	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

References

	« Hide 'large scale' referencesShow '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] [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]	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. , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	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.

IPI

IPI00032903.

PIR

T46479.

RefSeq

NP_057161.1. NM_016077.3.

UniGene

Hs.12677.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q7S	X-ray	2.00	A/B	63-179	[»]

ProteinModelPortal

Q9Y3E5.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y3E5. 3 interactions.

STRING

9606.ENSP00000376758.

PTM databases

PhosphoSite

Q9Y3E5.

Polymorphism databases

DMDM

6686183.

Proteomic databases

PaxDb

Q9Y3E5.

PRIDE

Q9Y3E5.

Protocols and materials databases

DNASU

51651.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000393038; ENSP00000376758; ENSG00000141378.
ENST00000470557; ENSP00000464327; ENSG00000141378.
ENST00000537860; ENSP00000437690; ENSG00000141378.

GeneID

51651.

KEGG

hsa:51651.

UCSC

uc002ixt.3. human.

Organism-specific databases

CTD

51651.

GeneCards

GC17M057774.

HGNC

HGNC:24265. PTRH2.

HPA

HPA012897.

MIM

608625. gene.

neXtProt

NX_Q9Y3E5.

PharmGKB

PA143485586.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1990.

HOGENOM

HOG000227349.

HOVERGEN

HBG049458.

InParanoid

Q9Y3E5.

KO

K04794.

OMA

KQVIVVR.

OrthoDB

EOG40VVR0.

Enzyme and pathway databases

BRENDA

3.1.1.29. 2681.

Gene expression databases

Bgee

Q9Y3E5.

CleanEx

HS_PTH2.
HS_PTRH2.

Genevestigator

Q9Y3E5.

GermOnline

ENSG00000141378. Homo sapiens.

Family and domain databases

Gene3D

3.40.1490.10. 1 hit.

InterPro

IPR023476. Pep_tRNA_hydro_II_dom.
IPR002833. Pep_tRNA_hydro_PTH2.
[Graphical view]

PANTHER

PTHR12649:SF6. PTHR12649:SF6. 1 hit.

Pfam

PF01981. PTH2. 1 hit.
[Graphical view]

SUPFAM

SSF102462. SSF102462. 1 hit.

TIGRFAMs

TIGR00283. arch_pth2. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

PTRH2. human.

EvolutionaryTrace

Q9Y3E5.

GenomeRNAi

51651.

NextBio

55610.

SOURCE

Search...

Entry information

Entry name

PTH2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.