dbPTM

PTH2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTH2_HUMAN
UniProt AC	Q9Y3E5
Protein Name	Peptidyl-tRNA hydrolase 2, mitochondrial
Gene Name	PTRH2
Organism	Homo sapiens (Human).
Sequence Length	179
Subcellular Localization	Mitochondrion.
Protein Description	The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.; Promotes caspase-independent apoptosis by regulating the function of two transcriptional regulators, AES and TLE1..
Protein Sequence	MPSKSLVMEYLAHPSTLGLAVGVACGMCLGWSLRVCFGMLPKSKTSKTHTDTESEASILGDSGEYKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQDAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MPSKSLVMEY -----CCCHHHHHHH	33.31	22210691
5	Phosphorylation	---MPSKSLVMEYLA ---CCCHHHHHHHHC	30.45	18703509
16	Phosphorylation	EYLAHPSTLGLAVGV HHHCCHHHHHHHHHH	29.33	22210691
32	Phosphorylation	CGMCLGWSLRVCFGM HHHHHHHHHHHHHHC	12.42	24719451
39	Sulfoxidation	SLRVCFGMLPKSKTS HHHHHHHCCCCCCCC	2.65	21406390
45	Phosphorylation	GMLPKSKTSKTHTDT HCCCCCCCCCCCCCC	42.41	23312004
46	Phosphorylation	MLPKSKTSKTHTDTE CCCCCCCCCCCCCCH	39.01	23312004
47	2-Hydroxyisobutyrylation	LPKSKTSKTHTDTES CCCCCCCCCCCCCHH	49.94	-
47	Ubiquitination	LPKSKTSKTHTDTES CCCCCCCCCCCCCHH	49.94	21890473
48	Ubiquitination	PKSKTSKTHTDTESE CCCCCCCCCCCCHHH	29.76	-
48	Phosphorylation	PKSKTSKTHTDTESE CCCCCCCCCCCCHHH	29.76	23403867
50	Phosphorylation	SKTSKTHTDTESEAS CCCCCCCCCCHHHHH	50.26	23403867
51	Phosphorylation	KTSKTHTDTESEASI CCCCCCCCCHHHHHH	40.65	-
52	Phosphorylation	TSKTHTDTESEASIL CCCCCCCCHHHHHHC	42.43	23403867
53	Phosphorylation	SKTHTDTESEASILG CCCCCCCHHHHHHCC	49.76	-
54	Phosphorylation	KTHTDTESEASILGD CCCCCCHHHHHHCCC	40.32	25159151
55	Phosphorylation	THTDTESEASILGDS CCCCCHHHHHHCCCC	39.96	-
57	Phosphorylation	TDTESEASILGDSGE CCCHHHHHHCCCCCC	17.81	23401153
58	Phosphorylation	DTESEASILGDSGEY CCHHHHHHCCCCCCE	6.85	18669648
62	Phosphorylation	EASILGDSGEYKMIL HHHHCCCCCCEEEEE	31.55	25849741
63	Phosphorylation	ASILGDSGEYKMILV HHHCCCCCCEEEEEE	47.17	-
65	Phosphorylation	ILGDSGEYKMILVVR HCCCCCCEEEEEEEE	14.91	23403867
76	Ubiquitination	LVVRNDLKMGKGKVA EEEECCCCCCCCCHH	48.77	21890473
77	Ubiquitination	VVRNDLKMGKGKVAA EEECCCCCCCCCHHH	9.73	-
79	Ubiquitination	RNDLKMGKGKVAAQC ECCCCCCCCCHHHHH	52.65	21906983
80	Ubiquitination	NDLKMGKGKVAAQCS CCCCCCCCCHHHHHH	24.76	-
81	Ubiquitination	DLKMGKGKVAAQCSH CCCCCCCCHHHHHHH	31.99	25621951
82	Ubiquitination	LKMGKGKVAAQCSHA CCCCCCCHHHHHHHH	7.91	-
87	Phosphorylation	GKVAAQCSHAAVSAY CCHHHHHHHHHHHHH	12.23	18703509
88	Phosphorylation	KVAAQCSHAAVSAYK CHHHHHHHHHHHHHH	25.90	-
94	Phosphorylation	SHAAVSAYKQIQRRN HHHHHHHHHHHHHHC	8.91	-
95	Acetylation	HAAVSAYKQIQRRNP HHHHHHHHHHHHHCH	40.41	26051181
95	Ubiquitination	HAAVSAYKQIQRRNP HHHHHHHHHHHHHCH	40.41	21890473
96	Ubiquitination	AAVSAYKQIQRRNPE HHHHHHHHHHHHCHH	25.11	-
106	Acetylation	RRNPEMLKQWEYCGQ HHCHHHHHHHEECCC	52.64	25825284
106	Ubiquitination	RRNPEMLKQWEYCGQ HHCHHHHHHHEECCC	52.64	25621951
107	Ubiquitination	RNPEMLKQWEYCGQP HCHHHHHHHEECCCC	33.98	-
107	Acetylation	RNPEMLKQWEYCGQP HCHHHHHHHEECCCC	33.98	-
115	Ubiquitination	WEYCGQPKVVVKAPD HEECCCCEEEEECCC	39.51	25621951
119	Ubiquitination	GQPKVVVKAPDEETL CCCEEEEECCCHHHH	42.46	21906983
119	Acetylation	GQPKVVVKAPDEETL CCCEEEEECCCHHHH	42.46	26051181
120	Ubiquitination	QPKVVVKAPDEETLI CCEEEEECCCHHHHH	12.74	-
134	Ubiquitination	IALLAHAKMLGLTVS HHHHHHHHHHCCHHH	25.45	-
135	Ubiquitination	ALLAHAKMLGLTVSL HHHHHHHHHCCHHHH	3.58	-
139	Phosphorylation	HAKMLGLTVSLIQDA HHHHHCCHHHHHHHC	13.27	20068231
141	Phosphorylation	KMLGLTVSLIQDAGR HHHCCHHHHHHHCCC	17.96	20068231
171	Ubiquitination	GPADLIDKVTGHLKL CHHHHHHHHCCCEEE	34.40	2190698
172	Ubiquitination	PADLIDKVTGHLKLY HHHHHHHHCCCEEEC	7.41	-
177	Ubiquitination	DKVTGHLKLY----- HHHCCCEEEC-----	39.81	21890473
178	Ubiquitination	KVTGHLKLY------ HHCCCEEEC------	8.47	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
5	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
87	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PTH2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PTH2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AES_HUMAN	AES	physical	15006356
VPP1_HUMAN	ATP6V0A1	physical	22939629
VPP2_HUMAN	ATP6V0A2	physical	22939629
VATD_HUMAN	ATP6V1D	physical	22939629
STT3B_HUMAN	STT3B	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS15_HUMAN	RPS15	physical	22939629
FAK1_HUMAN	PTK2	physical	21383007

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616263	Neurologic, endocrine, and pancreatic disease, multisystem, infantile-onset (IMNEPD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PTH2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND MASSSPECTROMETRY.	18669648 [Abstract]