TRM61_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRM61_HUMAN
• UniProt AC: Q96FX7
• Protein Name: tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRMT61A
• Gene Name: TRMT61A
• Organism: Homo sapiens (Human).
• Sequence Length: 289
• Subcellular Localization: Nucleus .
• Protein Description: Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. [PubMed: 16043508 Catalytic subunit of mRNA N(1)-methyltransferase complex, which mediates methylation of adenosine residues at the N(1) position of a small subset of mRNAs: N(1) methylation takes place in tRNA T-loop-like structures of mRNAs and is only present at low stoichiometries]
• Protein Sequence: MSFVAYEELIKEGDTAILSLGHGAMVAVRVQRGAQTQTRHGVLRHSVDLIGRPFGSKVTCGRGGWVYVLHPTPELWTLNLPHRTQILYSTDIALITMMLELRPGSVVCESGTGSGSVSHAIIRTIAPTGHLHTVEFHQQRAEKAREEFQEHRVGRWVTVRTQDVCRSGFGVSHVADAVFLDIPSPWEAVGHAWDALKVEGGRFCSFSPCIEQVQRTCQALAARGFSELSTLEVLPQVYNVRTVSLPPPDLGTGTDGPAGSDTSPFRSGTPMKEAVGHTGYLTFATKTPG

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
2	Acetylation	------MSFVAYEEL ------CCCCCHHHH	28.55	22223895
2	Phosphorylation	------MSFVAYEEL ------CCCCCHHHH	28.55	18187866
19	Phosphorylation	EGDTAILSLGHGAMV HCCEEEEEECCCEEE	26.62	19060867
32	Methylation	MVAVRVQRGAQTQTR EEEEEEECCCCCCCC	39.29	115919021
46	Phosphorylation	RHGVLRHSVDLIGRP CCCCHHCCEEECCCC	15.76	27422710
56	Phosphorylation	LIGRPFGSKVTCGRG ECCCCCCCEEEECCC	25.08	27794612
57	Acetylation	IGRPFGSKVTCGRGG CCCCCCCEEEECCCC	41.78	23749302
57	Ubiquitination	IGRPFGSKVTCGRGG CCCCCCCEEEECCCC	41.78	-
62	Methylation	GSKVTCGRGGWVYVL CCEEEECCCCEEEEE	42.47	54560347
67	Phosphorylation	CGRGGWVYVLHPTPE ECCCCEEEEEECCCC	7.26	20090780
242	Phosphorylation	PQVYNVRTVSLPPPD CCEECEEEEECCCCC	15.34	-
252	Phosphorylation	LPPPDLGTGTDGPAG CCCCCCCCCCCCCCC	44.18	26074081
254	Phosphorylation	PPDLGTGTDGPAGSD CCCCCCCCCCCCCCC	37.31	26074081
260	Phosphorylation	GTDGPAGSDTSPFRS CCCCCCCCCCCCCCC	39.56	26074081
262	Phosphorylation	DGPAGSDTSPFRSGT CCCCCCCCCCCCCCC	39.74	25159151
263	Phosphorylation	GPAGSDTSPFRSGTP CCCCCCCCCCCCCCC	27.34	25159151
267	Phosphorylation	SDTSPFRSGTPMKEA CCCCCCCCCCCCHHC	47.61	21949786
269	Phosphorylation	TSPFRSGTPMKEAVG CCCCCCCCCCHHCCC	22.81	21949786
278	Phosphorylation	MKEAVGHTGYLTFAT CHHCCCCCCEEEEEE	22.92	24719451
280	Phosphorylation	EAVGHTGYLTFATKT HCCCCCCEEEEEECC	12.06	29759185
286	Ubiquitination	GYLTFATKTPG---- CEEEEEECCCC----	49.66	-

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

Oops, there are no upstream regulatory protein records of TRM61_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRM61_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 TRM61_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRM6_HUMAN	TRMT6	physical	22939629
VPS36_HUMAN	VPS36	physical	22939629
VPS35_HUMAN	VPS35	physical	22939629
TRM6_HUMAN	TRMT6	physical	26186194
ARHGC_HUMAN	ARHGEF12	physical	26186194
ARHGB_HUMAN	ARHGEF11	physical	26186194
RFOX2_HUMAN	RBFOX2	physical	26186194
PBLD_HUMAN	PBLD	physical	26186194
FHL2_HUMAN	FHL2	physical	26186194
SK2L2_HUMAN	SKIV2L2	physical	26344197
TLN2_HUMAN	TLN2	physical	26344197
TRM6_HUMAN	TRMT6	physical	26344197
TRM6_HUMAN	TRMT6	physical	28514442
RFOX2_HUMAN	RBFOX2	physical	28514442
ARHGC_HUMAN	ARHGEF12	physical	28514442
ARHGB_HUMAN	ARHGEF11	physical	28514442
PBLD_HUMAN	PBLD	physical	28514442
FHL2_HUMAN	FHL2	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-263, AND MASSSPECTROMETRY.
PubMed: 19690332

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-19, AND MASSSPECTROMETRY.
PubMed: 18187866