dbPTM

TRM6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRM6_HUMAN
UniProt AC	Q9UJA5
Protein Name	tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6
Gene Name	TRMT6
Organism	Homo sapiens (Human).
Sequence Length	497
Subcellular Localization	Nucleus .
Protein Description	Substrate-binding 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 Together with the TRMT61A catalytic subunit, part of a mRNA N(1)-methyltransferase complex that 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	MEGSGEQPGPQPQHPGDHRIRDGDFVVLKREDVFKAVQVQRRKKVTFEKQWFYLDNVIGHSYGTAFEVTSGGSLQPKKKREEPTAETKEAGTDNRNIVDDGKSQKLTQDDIKALKDKGIKGEEIVQQLIENSTTFRDKTEFAQDKYIKKKKKKYEAIITVVKPSTRILSIMYYAREPGKINHMRYDTLAQMLTLGNIRAGNKMIVMETCAGLVLGAMMERMGGFGSIIQLYPGGGPVRAATACFGFPKSFLSGLYEFPLNKVDSLLHGTFSAKMLSSEPKDSALVEESNGTLEEKQASEQENEDSMAEAPESNHPEDQETMETISQDPEHKGPKERGSKKDYIQEKQRRQEEQRKRHLEAAALLSERNADGLIVASRFHPTPLLLSLLDFVAPSRPFVVYCQYKEPLLECYTKLRERGGVINLRLSETWLRNYQVLPDRSHPKLLMSGGGGYLLSGFTVAMDNLKADTSLKSNASTLESHETEEPAAKKRKCPESDS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEGSGEQP -------CCCCCCCC	13.69	-
4	Phosphorylation	----MEGSGEQPGPQ ----CCCCCCCCCCC	26.33	26714015
29	Ubiquitination	DGDFVVLKREDVFKA CCCEEEEEHHHHHHH	41.97	24816145
35	Ubiquitination	LKREDVFKAVQVQRR EEHHHHHHHHHCCCC	47.71	29967540
87	Phosphorylation	REEPTAETKEAGTDN CCCCCCCHHCCCCCC	31.55	-
88	Ubiquitination	EEPTAETKEAGTDNR CCCCCCHHCCCCCCC	36.75	21906983
88 (in isoform 1)	Ubiquitination	-	36.75	21890473
88 (in isoform 2)	Ubiquitination	-	36.75	21890473
88 (in isoform 3)	Ubiquitination	-	36.75	21890473
91	Ubiquitination	TAETKEAGTDNRNIV CCCHHCCCCCCCCCC	34.39	21890473
92	Phosphorylation	AETKEAGTDNRNIVD CCHHCCCCCCCCCCC	36.83	-
102	Acetylation	RNIVDDGKSQKLTQD CCCCCCCCCCCCCHH	57.62	25953088
103	Ubiquitination	NIVDDGKSQKLTQDD CCCCCCCCCCCCHHH	37.77	-
103	Ubiquitination	NIVDDGKSQKLTQDD CCCCCCCCCCCCHHH	37.77	21890473
103	Phosphorylation	NIVDDGKSQKLTQDD CCCCCCCCCCCCHHH	37.77	-
105	Ubiquitination	VDDGKSQKLTQDDIK CCCCCCCCCCHHHHH	61.67	33845483
107	Phosphorylation	DGKSQKLTQDDIKAL CCCCCCCCHHHHHHH	36.67	17525332
112	Ubiquitination	KLTQDDIKALKDKGI CCCHHHHHHHHHCCC	55.45	21890473
112	Ubiquitination	KLTQDDIKALKDKGI CCCHHHHHHHHHCCC	55.45	22817900
112 (in isoform 2)	Ubiquitination	-	55.45	21890473
112 (in isoform 1)	Ubiquitination	-	55.45	21890473
112 (in isoform 3)	Ubiquitination	-	55.45	21890473
115	Ubiquitination	QDDIKALKDKGIKGE HHHHHHHHHCCCCHH	63.35	22817900
117	Ubiquitination	DIKALKDKGIKGEEI HHHHHHHCCCCHHHH	62.03	22817900
120	Ubiquitination	ALKDKGIKGEEIVQQ HHHHCCCCHHHHHHH	69.78	30230243
138	Ubiquitination	NSTTFRDKTEFAQDK CCCCCCCHHHHHHHH	45.78	33845483
145	Methylation	KTEFAQDKYIKKKKK HHHHHHHHHHHHHHH	36.47	-
145	Ubiquitination	KTEFAQDKYIKKKKK HHHHHHHHHHHHHHH	36.47	29967540
154	Phosphorylation	IKKKKKKYEAIITVV HHHHHHCEEEEEEEE	21.33	24719451
158	Ubiquitination	KKKYEAIITVVKPST HHCEEEEEEEECCCH	2.85	24816145
159	Phosphorylation	KKYEAIITVVKPSTR HCEEEEEEEECCCHH	17.09	24719451
164	Phosphorylation	IITVVKPSTRILSIM EEEEECCCHHHEEEE	25.30	20068231
165	Phosphorylation	ITVVKPSTRILSIMY EEEECCCHHHEEEEE	30.20	20068231
169	Phosphorylation	KPSTRILSIMYYARE CCCHHHEEEEECCCC	11.70	20068231
170	Ubiquitination	PSTRILSIMYYAREP CCHHHEEEEECCCCC	1.52	24816145
172	Phosphorylation	TRILSIMYYAREPGK HHHEEEEECCCCCCC	7.72	20068231
173	Phosphorylation	RILSIMYYAREPGKI HHEEEEECCCCCCCC	5.04	20068231
176	Ubiquitination	SIMYYAREPGKINHM EEEECCCCCCCCCCC	50.67	29967540
176	Ubiquitination	SIMYYAREPGKINHM EEEECCCCCCCCCCC	50.67	-
185	Phosphorylation	GKINHMRYDTLAQML CCCCCCCHHHHHHHH	13.00	21406692
187	Phosphorylation	INHMRYDTLAQMLTL CCCCCHHHHHHHHHH	18.30	21406692
193	Phosphorylation	DTLAQMLTLGNIRAG HHHHHHHHHCCCCCC	27.55	21406692
208	Phosphorylation	NKMIVMETCAGLVLG CEEEEEEHHHHHHHH	6.91	22210691
226	Phosphorylation	ERMGGFGSIIQLYPG HHCCCCCCEEEEECC	17.79	25867546
231	Phosphorylation	FGSIIQLYPGGGPVR CCCEEEEECCCCCHH	5.39	25867546
273 (in isoform 1)	Ubiquitination	-	38.89	21890473
273 (in isoform 3)	Ubiquitination	-	38.89	21890473
273	Ubiquitination	LHGTFSAKMLSSEPK HHCCCCCHHCCCCCC	38.89	21890473
273 (in isoform 2)	Ubiquitination	-	38.89	21890473
273	Ubiquitination	LHGTFSAKMLSSEPK HHCCCCCHHCCCCCC	38.89	22817900
282	Phosphorylation	LSSEPKDSALVEESN CCCCCCCCCCEECCC	29.63	23663014
288	Phosphorylation	DSALVEESNGTLEEK CCCCEECCCCCHHHH	27.36	23663014
289	Ubiquitination	SALVEESNGTLEEKQ CCCEECCCCCHHHHH	51.23	22505724
291	Phosphorylation	LVEESNGTLEEKQAS CEECCCCCHHHHHHH	34.93	23663014
298	Phosphorylation	TLEEKQASEQENEDS CHHHHHHHHHHCHHH	37.00	30278072
301	Ubiquitination	EKQASEQENEDSMAE HHHHHHHHCHHHHHC	59.54	32015554
301	Ubiquitination	EKQASEQENEDSMAE HHHHHHHHCHHHHHC	59.54	-
305	Phosphorylation	SEQENEDSMAEAPES HHHHCHHHHHCCCCC	17.45	10810093
312	Phosphorylation	SMAEAPESNHPEDQE HHHCCCCCCCCCCHH	39.10	30576142
320	Phosphorylation	NHPEDQETMETISQD CCCCCHHHHHHHHCC	18.06	29496963
323	Phosphorylation	EDQETMETISQDPEH CCHHHHHHHHCCCCC	18.33	26074081
325	Phosphorylation	QETMETISQDPEHKG HHHHHHHHCCCCCCC	35.63	26074081
340	Ubiquitination	PKERGSKKDYIQEKQ CCCCCCHHHHHHHHH	58.42	24816145
342	Phosphorylation	ERGSKKDYIQEKQRR CCCCHHHHHHHHHHH	17.24	-
346	Ubiquitination	KKDYIQEKQRRQEEQ HHHHHHHHHHHHHHH	32.50	29967540
417	Methylation	CYTKLRERGGVINLR HHHHHHHCCCEEEEE	40.51	-
452	Phosphorylation	LMSGGGGYLLSGFTV EEECCCCEECCCEEE	14.03	23532336
468	Phosphorylation	MDNLKADTSLKSNAS ECCCCCCCCCCCCCH	40.60	21712546
469	Phosphorylation	DNLKADTSLKSNAST CCCCCCCCCCCCCHH	34.05	29214152
471	Ubiquitination	LKADTSLKSNASTLE CCCCCCCCCCCHHHH	41.24	33845483
472	Phosphorylation	KADTSLKSNASTLES CCCCCCCCCCHHHHC	42.81	24043423
475	Phosphorylation	TSLKSNASTLESHET CCCCCCCHHHHCCCC	37.46	25159151
476	Phosphorylation	SLKSNASTLESHETE CCCCCCHHHHCCCCC	31.94	25159151
479	Phosphorylation	SNASTLESHETEEPA CCCHHHHCCCCCCCH	29.72	23312004
482	Phosphorylation	STLESHETEEPAAKK HHHHCCCCCCCHHHH	39.98	23312004
488	Acetylation	ETEEPAAKKRKCPES CCCCCHHHHCCCCCC	56.04	25953088
495	Phosphorylation	KKRKCPESDS----- HHCCCCCCCC-----	28.44	24719451
497	Phosphorylation	RKCPESDS------- CCCCCCCC-------	51.94	24719451

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
Oops, there are no upstream regulatory protein records of TRM6_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TRM6_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 TRM6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VPS35_HUMAN	VPS35	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
SHOT1_HUMAN	KIAA1598	physical	22863883
OGFR_HUMAN	OGFR	physical	22863883
DDX5_HUMAN	DDX5	physical	26344197
DJC17_HUMAN	DNAJC17	physical	26344197
EI2BA_HUMAN	EIF2B1	physical	26344197
NH2L1_HUMAN	NHP2L1	physical	26344197
TRUA_HUMAN	PUS1	physical	26344197
RADI_HUMAN	RDX	physical	26344197
SNW1_HUMAN	SNW1	physical	26344197
STK24_HUMAN	STK24	physical	26344197
TLN2_HUMAN	TLN2	physical	26344197
TTC4_HUMAN	TTC4	physical	26344197
UT14A_HUMAN	UTP14A	physical	26344197

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.

Regulatory Network of TRM6_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107, AND MASSSPECTROMETRY.	17525332 [Abstract]