dbPTM

TRMB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRMB_HUMAN
UniProt AC	Q9UBP6
Protein Name	tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255\|HAMAP-Rule:MF_03055}
Gene Name	METTL1 {ECO:0000255\|HAMAP-Rule:MF_03055}
Organism	Homo sapiens (Human).
Sequence Length	276
Subcellular Localization	Nucleus .
Protein Description	Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA..
Protein Sequence	MAAETRNVAGAEAPPPQKRYYRQRAHSNPMADHTLRYPVKPEEMDWSELYPEFFAPLTQNQSHDDPKDKKEKRAQAQVEFADIGCGYGGLLVELSPLFPDTLILGLEIRVKVSDYVQDRIRALRAAPAGGFQNIACLRSNAMKHLPNFFYKGQLTKMFFLFPDPHFKRTKHKWRIISPTLLAEYAYVLRVGGLVYTITDVLELHDWMCTHFEEHPLFERVPLEDLSEDPVVGHLGTSTEEGKKVLRNGGKNFPAIFRRIQDPVLQAVTSQTSLPGH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAETRNVA ------CCCCCCCCC	17.63	19413330
5	Phosphorylation	---MAAETRNVAGAE ---CCCCCCCCCCCC	23.87	20068231
18	Ubiquitination	AEAPPPQKRYYRQRA CCCCCCCHHHHHHHH	48.41	21906983
24	Methylation	QKRYYRQRAHSNPMA CHHHHHHHHHCCCCC	25.85	24388179
27	Phosphorylation	YYRQRAHSNPMADHT HHHHHHHCCCCCCCC	41.46	29255136
34	Phosphorylation	SNPMADHTLRYPVKP CCCCCCCCCCCCCCH	17.30	23403867
87 (in isoform 2)	Phosphorylation	-	16.46	22210691
111	Ubiquitination	LGLEIRVKVSDYVQD EEEEEEEEHHHHHHH	26.60	-
128	Phosphorylation	RALRAAPAGGFQNIA HHHHHCCCCCCCHHH	26.47	27251275
128 (in isoform 2)	Phosphorylation	-	26.47	28348404
148 (in isoform 2)	Phosphorylation	-	7.17	25003641
177	Phosphorylation	KHKWRIISPTLLAEY CCCEEEECHHHHHHH	14.95	-
207	Ubiquitination	VLELHDWMCTHFEEH HHHHHHHHHHHCHHC	2.05	21890473
242	Ubiquitination	GTSTEEGKKVLRNGG CCCHHHHHHHHHCCC	42.88	21906983
242	Acetylation	GTSTEEGKKVLRNGG CCCHHHHHHHHHCCC	42.88	26051181
243	Ubiquitination	TSTEEGKKVLRNGGK CCHHHHHHHHHCCCC	58.31	-
250	Ubiquitination	KVLRNGGKNFPAIFR HHHHCCCCCCHHHHH	57.73	23000965
250	Acetylation	KVLRNGGKNFPAIFR HHHHCCCCCCHHHHH	57.73	88403
268	Phosphorylation	DPVLQAVTSQTSLPG CHHHHHHHHCCCCCC	20.38	28857561
269	Phosphorylation	PVLQAVTSQTSLPGH HHHHHHHHCCCCCCC	25.51	29978859
271	Phosphorylation	LQAVTSQTSLPGH-- HHHHHHCCCCCCC--	31.81	29978859
272	Phosphorylation	QAVTSQTSLPGH--- HHHHHCCCCCCC---	25.57	29978859

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
27	S	Phosphorylation	Kinase	AKT1	P31749	PSP
27	S	Phosphorylation	Kinase	RPS6KA1	Q15418	GPS
27	S	Phosphorylation	Kinase	RPS6KA3	P51812	Uniprot
27	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
27	S	Phosphorylation		15861136
Phosphorylation at Ser-27 inactivates its catalytic activity but does not affect the interaction with WDR4.

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 TRMB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WDR4_HUMAN	WDR4	physical	16189514
WDR4_HUMAN	WDR4	physical	22939629
SYAC_HUMAN	AARS	physical	22863883
ARC1B_HUMAN	ARPC1B	physical	22863883
ARPC2_HUMAN	ARPC2	physical	22863883
ARPC4_HUMAN	ARPC4	physical	22863883
ARPC5_HUMAN	ARPC5	physical	22863883
CYBP_HUMAN	CACYBP	physical	22863883
PYRG2_HUMAN	CTPS2	physical	22863883
NC2B_HUMAN	DR1	physical	22863883
GTF2I_HUMAN	GTF2I	physical	22863883
DAAF5_HUMAN	DNAAF5	physical	22863883
IPO11_HUMAN	IPO11	physical	22863883
KBP_HUMAN	KIAA1279	physical	22863883
NIF3L_HUMAN	NIF3L1	physical	22863883
NUCB1_HUMAN	NUCB1	physical	22863883
PAF15_HUMAN	KIAA0101	physical	22863883
PRDX1_HUMAN	PRDX1	physical	22863883
PRDX2_HUMAN	PRDX2	physical	22863883
PRKDC_HUMAN	PRKDC	physical	22863883
TM1L1_HUMAN	TOM1L1	physical	22863883
TPD54_HUMAN	TPD52L2	physical	22863883
UBE3A_HUMAN	UBE3A	physical	22863883
TRMB_YEAST	TRM8	genetic	15861136
WDR4_HUMAN	WDR4	physical	15861136
WDR4_HUMAN	WDR4	physical	25416956
WDR4_HUMAN	WDR4	physical	26186194
APEX1_HUMAN	APEX1	physical	26344197
CO040_HUMAN	C15orf40	physical	26344197
NH2L1_HUMAN	NHP2L1	physical	26344197
IPYR2_HUMAN	PPA2	physical	26344197
TPD54_HUMAN	TPD52L2	physical	26344197
TRM61_HUMAN	TRMT61A	physical	26344197
TSNAX_HUMAN	TSNAX	physical	26344197
WDR4_HUMAN	WDR4	physical	26344197
WDR4_HUMAN	WDR4	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.

Regulatory Network of TRMB_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 ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"The tRNA methylase METTL1 is phosphorylated and inactivated by PKBand RSK in vitro and in cells."; Cartlidge R.A., Knebel A., Peggie M., Alexandrov A., Phizicky E.M.,Cohen P.; EMBO J. 24:1696-1705(2005). Cited for: SUBCELLULAR LOCATION, INTERACTION WITH WDR4, PHOSPHORYLATION ATSER-27, AND MUTAGENESIS OF SER-27.	15861136 [Abstract]