DUS1L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DUS1L_HUMAN
• UniProt AC: Q6P1R4
• Protein Name: tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like
• Gene Name: DUS1L
• Organism: Homo sapiens (Human).
• Sequence Length: 473
• Protein Description: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs..
• Protein Sequence: MPKLQGFEFWSRTLRGARHVVAPMVDQSELAWRLLSRRHGAQLCYTPMLHAQVFVRDANYRKENLYCEVCPEDRPLIVQFCANDPEVFVQAALLAQDYCDAIDLNLGCPQMIAKRGHYGAFLQDEWDLLQRMILLAHEKLSVPVTCKIRVFPEIDKTVRYAQMLEKAGCQLLTVHGRTKEQKGPLSGAASWEHIKAVRKAVAIPVFANGNIQCLQDVERCLRDTGVQGVMSAEGNLHNPALFEGRSPAVWELAEEYLDIVREHPCPLSYVRAHLFKLWHHTLQVHQELREELAKVKTLEGIAAVSQELKLRCQEEISRQEGAKPTGDLPFHWICQPYIRPGPREGSKEKAGARSKRALEEEEGGTEVLSKNKQKKQLRNPHKTFDPSLKPKYAKCDQCGNPKGNRCVFSLCRGCCKKRASKETADCPGHGLLFKTKLEKSLAWKEAQPELQEPQPAAPGTPGGFSEVMGSALA

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
3	Sumoylation	-----MPKLQGFEFW -----CCCCCCHHHH	52.74	-
3	Sumoylation	-----MPKLQGFEFW -----CCCCCCHHHH	52.74	-
11	Phosphorylation	LQGFEFWSRTLRGAR CCCHHHHHHHHCCCC	22.25	30631047
13	Phosphorylation	GFEFWSRTLRGARHV CHHHHHHHHCCCCCE	18.45	30631047
45	Phosphorylation	RHGAQLCYTPMLHAQ HCCCEEEECCCEEEE	23.59	-
139	Ubiquitination	MILLAHEKLSVPVTC HHHHHHHCCCCCEEE	35.87	-
147	Ubiquitination	LSVPVTCKIRVFPEI CCCCEEEEEEECCCH	24.96	29967540
156	Ubiquitination	RVFPEIDKTVRYAQM EECCCHHHHHHHHHH	55.36	-
166	Ubiquitination	RYAQMLEKAGCQLLT HHHHHHHHHCCEEEE	46.23	29967540
195	Ubiquitination	AASWEHIKAVRKAVA CCCHHHHHHHHHHCE	42.61	29967540
296	Ubiquitination	REELAKVKTLEGIAA HHHHHHCCCHHHHHH	46.84	29967540
309	Ubiquitination	AAVSQELKLRCQEEI HHHHHHHHHHHHHHH	32.88	29967540
317	Phosphorylation	LRCQEEISRQEGAKP HHHHHHHHHHCCCCC	31.06	22617229
323	Ubiquitination	ISRQEGAKPTGDLPF HHHHCCCCCCCCCCC	54.70	-
372	Ubiquitination	TEVLSKNKQKKQLRN CCHHCCHHHHHHHCC	68.20	-
423	Phosphorylation	KKRASKETADCPGHG HHHCCCCCCCCCCCC	31.37	28555341
460	Phosphorylation	PQPAAPGTPGGFSEV CCCCCCCCCCCHHHH	20.08	29978859
465	Phosphorylation	PGTPGGFSEVMGSAL CCCCCCHHHHCCHHC	32.34	29978859
470	Phosphorylation	GFSEVMGSALA---- CHHHHCCHHCC----	11.30	28555341

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

Oops, there are no upstream regulatory protein records of DUS1L_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DUS1L_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 DUS1L_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of DUS1L_HUMAN !!

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

"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 THR-460 AND SER-465, ANDMASS SPECTROMETRY.
PubMed: 19413330