dbPTM

DUS2L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DUS2L_HUMAN
UniProt AC	Q9NX74
Protein Name	tRNA-dihydrouridine(20) synthase [NAD(P)+]-like
Gene Name	DUS2
Organism	Homo sapiens (Human).
Sequence Length	493
Subcellular Localization	Cytoplasm . Endoplasmic reticulum . Mainly at the endoplasmic reticulum.
Protein Description	Dihydrouridine synthase. Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Negatively regulates the activation of EIF2AK2/PKR..
Protein Sequence	MILNSLSLCYHNKLILAPMVRVGTLPMRLLALDYGADIVYCEELIDLKMIQCKRVVNEVLSTVDFVAPDDRVVFRTCEREQNRVVFQMGTSDAERALAVARLVENDVAGIDVNMGCPKQYSTKGGMGAALLSDPDKIEKILSTLVKGTRRPVTCKIRILPSLEDTLSLVKRIERTGIAAIAVHGRKREERPQHPVSCEVIKAIADTLSIPVIANGGSHDHIQQYSDIEDFRQATAASSVMVARAAMWNPSIFLKEGLRPLEEVMQKYIRYAVQYDNHYTNTKYCLCQMLREQLESPQGRLLHAAQSSREICEAFGLGAFYEETTQELDAQQARLSAKTSEQTGEPAEDTSGVIKMAVKFDRRAYPAQITPKMCLLEWCRREKLAQPVYETVQRPLDRLFSSIVTVAEQKYQSTLWDKSKKLAEQAAAIVCLRSQGLPEGRLGEESPSLHKRKREAPDQDPGGPRAQELAQPGDLCKKPFVALGSGEESPLEGW

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MILNSLSLCYHN ---CCCCHHHHHHCC	18.85	20068231
7	Phosphorylation	-MILNSLSLCYHNKL -CCCCHHHHHHCCHH	19.06	20068231
10	Phosphorylation	LNSLSLCYHNKLILA CCHHHHHHCCHHHHH	17.45	20068231
24	Phosphorylation	APMVRVGTLPMRLLA HCCCCCCCCCHHHHH	25.49	20068231
118	Ubiquitination	DVNMGCPKQYSTKGG CCCCCCCCCCCCCCC	66.98	-
120	Phosphorylation	NMGCPKQYSTKGGMG CCCCCCCCCCCCCCC	25.16	24275569
121	Phosphorylation	MGCPKQYSTKGGMGA CCCCCCCCCCCCCCH	22.58	24275569
122	Phosphorylation	GCPKQYSTKGGMGAA CCCCCCCCCCCCCHH	28.86	24275569
123	Ubiquitination	CPKQYSTKGGMGAAL CCCCCCCCCCCCHHH	47.75	-
126	Sulfoxidation	QYSTKGGMGAALLSD CCCCCCCCCHHHHCC	4.50	21406390
142	Phosphorylation	DKIEKILSTLVKGTR HHHHHHHHHHHCCCC	24.14	22468782
143	Phosphorylation	KIEKILSTLVKGTRR HHHHHHHHHHCCCCC	31.93	22468782
146	Ubiquitination	KILSTLVKGTRRPVT HHHHHHHCCCCCCEE	58.64	-
148	Phosphorylation	LSTLVKGTRRPVTCK HHHHHCCCCCCEEEE	20.14	22468782
155	Ubiquitination	TRRPVTCKIRILPSL CCCCEEEEEEECCCH	26.17	-
165	Phosphorylation	ILPSLEDTLSLVKRI ECCCHHHHHHHHHHH	14.63	26699800
167	Phosphorylation	PSLEDTLSLVKRIER CCHHHHHHHHHHHHH	32.96	26699800
170	Ubiquitination	EDTLSLVKRIERTGI HHHHHHHHHHHHHCC	53.61	21890473
175	Phosphorylation	LVKRIERTGIAAIAV HHHHHHHHCCEEEEE	21.83	19413330
234	Phosphorylation	IEDFRQATAASSVMV HHHHHHHHHHHHHHH	17.89	-
266	Ubiquitination	PLEEVMQKYIRYAVQ CHHHHHHHHHHHHHH	25.25	-
274	Phosphorylation	YIRYAVQYDNHYTNT HHHHHHHCCCCCCCH	16.47	-
283	Phosphorylation	NHYTNTKYCLCQMLR CCCCCHHHHHHHHHH	6.66	-
337	Ubiquitination	QQARLSAKTSEQTGE HHHHHHHHCCCCCCC	49.56	21890473
342	Phosphorylation	SAKTSEQTGEPAEDT HHHCCCCCCCCCCCC	39.19	25278378
349	Phosphorylation	TGEPAEDTSGVIKMA CCCCCCCCCCCCEEE	20.91	25278378
350	Phosphorylation	GEPAEDTSGVIKMAV CCCCCCCCCCCEEEE	43.30	25278378
388	Phosphorylation	EKLAQPVYETVQRPL HHCCCHHHHHHHHHH	16.74	28796482
417	Ubiquitination	YQSTLWDKSKKLAEQ HHHHHHHHHHHHHHH	53.22	-
445	Phosphorylation	EGRLGEESPSLHKRK CCCCCCCCCCHHHHH	18.58	29255136
447	Phosphorylation	RLGEESPSLHKRKRE CCCCCCCCHHHHHHC	53.00	29255136
477	Ubiquitination	QPGDLCKKPFVALGS CCCCCCCCCEEEECC	42.57	-
484	Phosphorylation	KPFVALGSGEESPLE CCEEEECCCCCCCCC	43.83	30183078
488	Phosphorylation	ALGSGEESPLEGW-- EECCCCCCCCCCC--	30.40	25159151

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 DUS2L_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DUS2L_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 DUS2L_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
NECT2_HUMAN	PVRL2	physical	21988832

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 DUS2L_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND MASSSPECTROMETRY.	18669648 [Abstract]