TRPT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRPT1_HUMAN
• UniProt AC: Q86TN4
• Protein Name: tRNA 2'-phosphotransferase 1
• Gene Name: TRPT1
• Organism: Homo sapiens (Human).
• Sequence Length: 253
• Protein Description: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate..
• Protein Sequence: MNFSGGGRQEAAGSRGRRAPRPREQDRDVQLSKALSYALRHGALKLGLPMGADGFVPLGTLLQLPQFRGFSAEDVQRVVDTNRKQRFALQLGDPSTGLLIRANQGHSLQVPKLELMPLETPQALPPMLVHGTFWKHWPSILLKGLSCQGRTHIHLAPGLPGDPGIISGMRSHCEIAVFIDGPLALADGIPFFRSANGVILTPGNTDGFLLPKYFKEALQLRPTRKPLSLAGDEETECQSSPKHSSRERRRIQQ

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNFSGGGR -------CCCCCCCC	11.73	22814378
33	Ubiquitination	DRDVQLSKALSYALR CHHHHHHHHHHHHHH	63.04	-
37	Phosphorylation	QLSKALSYALRHGAL HHHHHHHHHHHCCHH	15.54	29496907
139	Phosphorylation	TFWKHWPSILLKGLS CCHHHHHHHHHHCCC	22.22	20873877
202 (in isoform 3)	Phosphorylation	-	30.50	28787133
203 (in isoform 3)	Phosphorylation	-	44.42	28787133
215	Ubiquitination	FLLPKYFKEALQLRP CCCCHHHHHHHHHCC	38.70	-
223	Phosphorylation	EALQLRPTRKPLSLA HHHHHCCCCCCCCCC	44.91	23312004
225	Ubiquitination	LQLRPTRKPLSLAGD HHHCCCCCCCCCCCC	53.43	-
228	Phosphorylation	RPTRKPLSLAGDEET CCCCCCCCCCCCCCC	25.38	23403867
235	Phosphorylation	SLAGDEETECQSSPK CCCCCCCCCCCCCCC	39.76	23401153
237	Phosphorylation	AGDEETECQSSPKHS CCCCCCCCCCCCCCC	6.58	27251275
239	Phosphorylation	DEETECQSSPKHSSR CCCCCCCCCCCCCHH	61.33	29255136
240	Phosphorylation	EETECQSSPKHSSRE CCCCCCCCCCCCHHH	16.46	29255136
241	Phosphorylation	ETECQSSPKHSSRER CCCCCCCCCCCHHHH	43.56	24719451
242	Phosphorylation	TECQSSPKHSSRERR CCCCCCCCCCHHHHH	59.05	24719451
244	Phosphorylation	CQSSPKHSSRERRRI CCCCCCCCHHHHHHH	36.90	28450419
245	Phosphorylation	QSSPKHSSRERRRIQ CCCCCCCHHHHHHHC	37.57	28450419
246	Phosphorylation	SSPKHSSRERRRIQQ CCCCCCHHHHHHHCC	44.44	24719451

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

Oops, there are no upstream regulatory protein records of TRPT1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRPT1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TRPT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
DC1L1_HUMAN	DYNC1LI1	physical	28514442
STRP1_HUMAN	STRIP1	physical	28514442
ZY11B_HUMAN	ZYG11B	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND MASSSPECTROMETRY.
PubMed: 19690332

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-240, ANDMASS SPECTROMETRY.
PubMed: 19413330