dbPTM

MOD5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MOD5_HUMAN
UniProt AC	Q9H3H1
Protein Name	tRNA dimethylallyltransferase
Gene Name	TRIT1
Organism	Homo sapiens (Human).
Sequence Length	467
Subcellular Localization	Isoform 1: Mitochondrion . Isoform 4: Mitochondrion . Isoform 2: Cytoplasm . Isoform 3: Cytoplasm . Isoform 5: Cytoplasm .
Protein Description	Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 of both cytosolic and mitochondrial tRNAs, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A)..
Protein Sequence	MASVAAARAVPVGSGLRGLQRTLPLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQRICRHHMISFVDPLVTNYTVVDFRNRATALIEDIFARDKIPIVVGGTNYYIESLLWKVLVNTKPQEMGTEKVIDRKVELEKEDGLVLHKRLSQVDPEMAAKLHPHDKRKVARSLQVFEETGISHSEFLHRQHTEEGGGPLGGPLKFSNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELRDFHRRYNQKNVSENSQDYQHGIFQSIGFKEFHEYLITEGKCTLETSNQLLKKGIEALKQVTKRYARKQNRWVKNRFLSRPGPIVPPVYGLEVSDVSKWEESVLEPALEIVQSFIQGHKPTATPIKMPYNEAENKRSYHLCDLCDRIIIGDREWAAHIKSKSHLNQLKKRRRLDSDAVNTIESQSVSPDHNKEPKEKGSPGQNDQELKCSV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MASVAAARAV -----CCCHHHHHCC	15.81	-
14	Phosphorylation	ARAVPVGSGLRGLQR HHCCCCCCCHHHHHH	34.58	-
103	Phosphorylation	VDFRNRATALIEDIF EECCHHHHHHHHHHH	20.82	19060867
137	Phosphorylation	LWKVLVNTKPQEMGT HHHHHCCCCCHHCCC	36.30	28464451
138	Ubiquitination	WKVLVNTKPQEMGTE HHHHCCCCCHHCCCH	39.23	-
142	Sulfoxidation	VNTKPQEMGTEKVID CCCCCHHCCCHHEEC	7.29	21406390
146	Ubiquitination	PQEMGTEKVIDRKVE CHHCCCHHEECEEEE	44.31	-
164	Ubiquitination	EDGLVLHKRLSQVDP CCCEEEEEHHHHCCH	51.37	-
167	Phosphorylation	LVLHKRLSQVDPEMA EEEEEHHHHCCHHHH	31.99	28985074
173	Sulfoxidation	LSQVDPEMAAKLHPH HHHCCHHHHHHCCCC	5.52	21406390
176	Ubiquitination	VDPEMAAKLHPHDKR CCHHHHHHCCCCCHH	37.48	-
272	Phosphorylation	QKNVSENSQDYQHGI CCCCCCCCHHHCCCH	22.00	-
297	Ubiquitination	EYLITEGKCTLETSN HHHHCCCCEEHHHHH	20.15	-
315	Ubiquitination	KKGIEALKQVTKRYA HHHHHHHHHHHHHHH	50.17	-
315	Acetylation	KKGIEALKQVTKRYA HHHHHHHHHHHHHHH	50.17	30593099
391	Ubiquitination	PYNEAENKRSYHLCD CCCHHCCCCCHHHHH	33.94	-
431	Phosphorylation	KKRRRLDSDAVNTIE HHHHCCCHHHHHHHH	31.87	28176443
436	Phosphorylation	LDSDAVNTIESQSVS CCHHHHHHHHHCCCC	21.37	28176443
439	Phosphorylation	DAVNTIESQSVSPDH HHHHHHHHCCCCCCC	24.73	23401153
441	Phosphorylation	VNTIESQSVSPDHNK HHHHHHCCCCCCCCC	33.57	30266825
443	Phosphorylation	TIESQSVSPDHNKEP HHHHCCCCCCCCCCC	29.83	29255136
455	Phosphorylation	KEPKEKGSPGQNDQE CCCCCCCCCCCCCCC	36.60	23401153

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 MOD5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MOD5_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 MOD5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SMYD3_HUMAN	SMYD3	physical	23455924

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 MOD5_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-103, AND MASSSPECTROMETRY.	17693683 [Abstract]