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Protein Page:
PTRH2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PTRH2 The natural substrate for this enzyme may be peptidyl- tRNAs which drop off the ribosome during protein synthesis. Monomer. Belongs to the PTH2 family. Note: This description may include information from UniProtKB.
Protein type: Hydrolase; Mitochondrial; EC 3.1.1.29
Cellular Component: mitochondrion; cytosol
Molecular Function: protein binding; aminoacyl-tRNA hydrolase activity
Biological Process: metabolic process; apoptosis
Reference #:  Q9Y3E5 (UniProtKB)
Alt. Names/Synonyms: Bcl-2 inhibitor of transcription 1; BIT1; CGI-147; FLJ32471; peptidyl-tRNA hydrolase 2; Peptidyl-tRNA hydrolase 2, mitochondrial; PTH 2; PTH2; PTRH2
Gene Symbols: PTRH2
Molecular weight: 19,194 Da
Basal Isoelectric point: 8.95  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PTRH2

Protein Structure Not Found.


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Sites Implicated In
apoptosis, altered: S5‑p, S87‑p
cell adhesion, altered: S5‑p, S87‑p
intracellular localization: S5‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 0 S5-p ___MPSKsLVMEYLA
0 1 V35 CLGWSLRVCFGMLPK
0 1 T45-p GMLPKSKtSktHtDt
0 48 K47-ub LPKSKtSktHtDtEs
0 1 T48-p PKSKtSktHtDtEsE
0 1 T50-p SKtSktHtDtEsEAs
0 1 T52-p tSktHtDtEsEAsIL
0 3 S54-p ktHtDtEsEAsILGD
0 7 S57-p tDtEsEAsILGDSGE
0 1 S62 EAsILGDSGEYKMIL
0 1 K76-ub LVVRNDLkMGkGKVA
0 1 K79-ub RNDLkMGkGKVAAQC
0 1 K81 DLkMGkGKVAAQCsH
1 0 S87-p GKVAAQCsHAAVSAy
0 1 Y94-p sHAAVSAykQIQRRN
0 1 K95-ub HAAVSAykQIQRRNP
0 1 K119-ub GQPKVVVkAPDEETL
0 8 K134-ub IALLAHAkMLGLTVS
0 7 K171-ub GPADLIDkVTGHLkL
0 25 K177-ub DkVTGHLkLY_____
  mouse

 
F5 ___MLSKFLTMEYLV
S35 CLGWGLRSHLGMFPQ
T45 GMFPQNSTSEANRDT
E47 FPQNSTSEANRDTET
A48 PQNSTSEANRDTETG
R50 NSTSEANRDTETGTE
T52 TSEANRDTETGTEAs
T56 NRDTETGTEAsILGE
S59-p TETGTEAsILGESGE
S64 EAsILGESGEYKMIL
K78 LVVRTDLKMGKGkVA
K81 RTDLKMGKGkVAAQC
K83-ub DLKMGKGkVAAQCSH
S89 GkVAAQCSHAAVSAY
Y96 SHAAVSAYKQTQRRS
K97 HAAVSAYKQTQRRSP
K121 GQPKVVVKAPDEDTL
K136-ub IQLLTHAkTLGLTVS
E173 GPVELIDEVTGHLkL
K179-ub DEVTGHLkLY_____
  rat

 
L5 ___MLSKLLTMEYLV
S35-p CLGWGLRsHLGIFPQ
T45 GIFPQNSTSETNRDT
E47 FPQNSTSETNRDTEM
T48 PQNSTSETNRDTEMG
- gap
T52 TSETNRDTEMGtEAS
T56-p NRDTEMGtEASILGE
S59 TEMGtEASILGEsGE
S64-p EASILGEsGEYKMIL
K78 LVVRTDLKMGKGKVA
K81 RTDLKMGKGKVAAQC
K83 DLKMGKGKVAAQCSH
S89 GKVAAQCSHAAVSAY
Y96 SHAAVSAYKQIQRRN
K97 HAAVSAYKQIQRRNP
K121 GQPKVVVKAPDEDSL
K136 IQLLTHAKALGLTVS
E173 GPVELIDEVTGHLKL
K179 DEVTGHLKLY_____
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