Reviewed, UniProtKB/Swiss-Prot Q9Y3E5 (PTH2_HUMAN)

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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW translation Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from direct assay. Source: HPA
Molecular function	aminoacyl-tRNA hydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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)
	Q9Y3E5-1 [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: 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. , 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. , 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.

IPI

IPI00032903.

PIR

T46479.

RefSeq

NP_057161.1.

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y3E5. 1 interaction.

STRING

Q9Y3E5.

PTM databases

PhosphoSite

Q9Y3E5.

Proteomic databases

PRIDE

Q9Y3E5.

Genome annotation databases

Ensembl

ENST00000393038; ENSP00000376758; ENSG00000141378; Homo sapiens. [Genome view]
ENST00000409433; ENSP00000387180; ENSG00000141378; Homo sapiens. [Genome view]

GeneID

51651.

KEGG

hsa:51651.

UCSC

uc002ixt.1. human.

Organism-specific databases

CTD

51651.

GeneCards

GC17M055131.

H-InvDB

HIX0019799.

HGNC

HGNC:24265. PTRH2.

HPA

HPA012897.

MIM

608625. gene.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG526257.

HOVERGEN

Q9Y3E5.

InParanoid

Q9Y3E5.

OMA

IQRRNPE.

OrthoDB

EOG969TF4.

PhylomeDB

Q9Y3E5.

Enzyme and pathway databases

BRENDA

3.1.1.29. 247.

Gene expression databases

ArrayExpress

Q9Y3E5.

Bgee

Q9Y3E5.

CleanEx

HS_PTH2.
HS_PTRH2.

Genevestigator

Q9Y3E5.

GermOnline

ENSG00000141378. Homo sapiens.

Family and domain databases

InterPro

IPR002833. Pep_tRNA_hydro_PTH2.
[Graphical view]

Pfam

PF01981. PTH2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00283. Pep_tRNA_hydro_PTH2. 1 hit.

ProtoNet

Search...

Other Resources

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:	February 9, 2010
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.