dbPTM

DUS3L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DUS3L_HUMAN
UniProt AC	Q96G46
Protein Name	tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like
Gene Name	DUS3L
Organism	Homo sapiens (Human).
Sequence Length	650
Subcellular Localization
Protein Description	Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs..
Protein Sequence	MAEGTAEAPLENGGGGDSGAGALERGVAPIKRQYLTTKEQFHQFLEAKGQEKTCRETEVGDPAGNELAEPEAKRIRLEDGQTADGQTEEAAEPGEQLQTQKRARGQNKGRPHVKPTNYDKNRLCPSLIQESAAKCFFGDRCRFLHDVGRYLETKPADLGPRCVLFETFGRCPYGVTCRFAGAHLRPEGQNLVQEELAARGTQPPSIRNGLDKALQQQLRKREVRFERAEQALRRFSQGPTPAAAVPEGTAAEGAPRQENCGAQQVPAGPGTSTPPSSPVRTCGPLTDEDVVRLRPCEKKRLDIRGKLYLAPLTTCGNLPFRRICKRFGADVTCGEMAVCTNLLQGQMSEWALLKRHQCEDIFGVQLEGAFPDTMTKCAELLSRTVEVDFVDINVGCPIDLVYKKGGGCALMNRSTKFQQIVRGMNQVLDVPLTVKIRTGVQERVNLAHRLLPELRDWGVALVTLHGRSREQRYTKLADWQYIEECVQAASPMPLFGNGDILSFEDANRAMQTGVTGIMIARGALLKPWLFTEIKEQRHWDISSSERLDILRDFTNYGLEHWGSDTQGVEKTRRFLLEWLSFLCRYVPVGLLERLPQRINERPPYYLGRDYLETLMASQKAADWIRISEMLLGPVPPSFAFLPKHKANAYK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEGTAEAP ------CCCCCCCCC	24.75	22814378
31	Acetylation	ERGVAPIKRQYLTTK HCCCCCCCCCCCCCH	32.18	25953088
34	Phosphorylation	VAPIKRQYLTTKEQF CCCCCCCCCCCHHHH	15.28	29759185
36	Phosphorylation	PIKRQYLTTKEQFHQ CCCCCCCCCHHHHHH	30.78	29759185
37	Phosphorylation	IKRQYLTTKEQFHQF CCCCCCCCHHHHHHH	29.95	29759185
38	Ubiquitination	KRQYLTTKEQFHQFL CCCCCCCHHHHHHHH	44.26	-
48	Acetylation	FHQFLEAKGQEKTCR HHHHHHHCCCCCCCC	52.32	7677919
48	Ubiquitination	FHQFLEAKGQEKTCR HHHHHHHCCCCCCCC	52.32	-
73	Acetylation	ELAEPEAKRIRLEDG CCCCCCCCEEECCCC	46.85	23954790
73	Ubiquitination	ELAEPEAKRIRLEDG CCCCCCCCEEECCCC	46.85	21906983
73 (in isoform 2)	Ubiquitination	-	46.85	21890473
73 (in isoform 1)	Ubiquitination	-	46.85	21890473
101	Acetylation	GEQLQTQKRARGQNK CHHHHHHHHHCCCCC	51.95	26051181
101	Ubiquitination	GEQLQTQKRARGQNK CHHHHHHHHHCCCCC	51.95	21906983
101 (in isoform 1)	Ubiquitination	-	51.95	21890473
101 (in isoform 2)	Ubiquitination	-	51.95	21890473
114	Ubiquitination	NKGRPHVKPTNYDKN CCCCCCCCCCCCCCC	42.99	-
120	Ubiquitination	VKPTNYDKNRLCPSL CCCCCCCCCCCCHHH	33.34	-
134	Ubiquitination	LIQESAAKCFFGDRC HHHHHHHHHHHCCHH	31.15	-
154 (in isoform 2)	Ubiquitination	-	28.91	21890473
154 (in isoform 1)	Ubiquitination	-	28.91	21890473
154	Ubiquitination	VGRYLETKPADLGPR HHHHHCCCCCCCCCC	28.91	21906983
174 (in isoform 3)	Ubiquitination	-	8.06	21890473
193 (in isoform 3)	Ubiquitination	-	41.43	21890473
212	Ubiquitination	SIRNGLDKALQQQLR HHHCHHHHHHHHHHH	56.91	-
212	Acetylation	SIRNGLDKALQQQLR HHHCHHHHHHHHHHH	56.91	25953088
236	Phosphorylation	EQALRRFSQGPTPAA HHHHHHHHCCCCCCC	32.20	25159151
240	Phosphorylation	RRFSQGPTPAAAVPE HHHHCCCCCCCCCCC	32.17	21712546
249	Phosphorylation	AAAVPEGTAAEGAPR CCCCCCCCCCCCCCC	22.49	20068231
271	Phosphorylation	QVPAGPGTSTPPSSP CCCCCCCCCCCCCCC	32.34	29255136
272	Phosphorylation	VPAGPGTSTPPSSPV CCCCCCCCCCCCCCC	44.85	29255136
273	Phosphorylation	PAGPGTSTPPSSPVR CCCCCCCCCCCCCCC	38.77	29255136
276	Phosphorylation	PGTSTPPSSPVRTCG CCCCCCCCCCCCCCC	48.77	29255136
277	Phosphorylation	GTSTPPSSPVRTCGP CCCCCCCCCCCCCCC	32.94	29255136
281	Phosphorylation	PPSSPVRTCGPLTDE CCCCCCCCCCCCCCH	23.27	30576142
284 (in isoform 3)	Ubiquitination	-	33.94	21890473
286	Phosphorylation	VRTCGPLTDEDVVRL CCCCCCCCCHHHEEC	40.24	21815630
306	Ubiquitination	KRLDIRGKLYLAPLT CCCCCCCEEEEECCC	24.90	-
308	Phosphorylation	LDIRGKLYLAPLTTC CCCCCEEEEECCCCC	12.33	22817900
354	Methylation	MSEWALLKRHQCEDI CHHHHHHHHHCCCCC	49.00	-
377 (in isoform 3)	Ubiquitination	-	2.33	21890473
382	Phosphorylation	TKCAELLSRTVEVDF HHHHHHHHCCEEEEE	38.23	24719451
403	Ubiquitination	CPIDLVYKKGGGCAL CCEEEEEECCCCEEE	37.15	-
404	Ubiquitination	PIDLVYKKGGGCALM CEEEEEECCCCEEEC	45.13	-
416	Ubiquitination	ALMNRSTKFQQIVRG EECCCCHHHHHHHHC	42.28	21890473
416	Acetylation	ALMNRSTKFQQIVRG EECCCCHHHHHHHHC	42.28	25953088
416	Sumoylation	ALMNRSTKFQQIVRG EECCCCHHHHHHHHC	42.28	28112733
416 (in isoform 2)	Ubiquitination	-	42.28	21890473
416 (in isoform 1)	Ubiquitination	-	42.28	21890473
435 (in isoform 1)	Ubiquitination	-	22.64	21890473
435	Ubiquitination	LDVPLTVKIRTGVQE CCCCEEEEECCCHHH	22.64	21890473
435 (in isoform 2)	Ubiquitination	-	22.64	21890473
526 (in isoform 1)	Ubiquitination	-	34.69	21890473
526	Ubiquitination	IARGALLKPWLFTEI EECCHHHCHHHHHHH	34.69	21890473
534	Ubiquitination	PWLFTEIKEQRHWDI HHHHHHHHHHCCCCC	41.38	-
542	Phosphorylation	EQRHWDISSSERLDI HHCCCCCCHHHHHHH	25.91	-
543	Phosphorylation	QRHWDISSSERLDIL HCCCCCCHHHHHHHH	36.23	-
544	Phosphorylation	RHWDISSSERLDILR CCCCCCHHHHHHHHH	21.68	-
580	Phosphorylation	RFLLEWLSFLCRYVP HHHHHHHHHHHHHCC	19.76	24719451
610	Phosphorylation	PYYLGRDYLETLMAS CCCCCHHHHHHHHHH	12.70	-
619 (in isoform 1)	Ubiquitination	-	42.94	21890473
619	Ubiquitination	ETLMASQKAADWIRI HHHHHHHHHHHHHHH	42.94	2190698
643	Ubiquitination	PSFAFLPKHKANAYK CHHHCCHHHHCCCCC	60.94	-
645	Ubiquitination	FAFLPKHKANAYK-- HHCCHHHHCCCCC--	49.84	-

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 DUS3L_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DUS3L_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 DUS3L_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
BCAT1_HUMAN	BCAT1	physical	22863883
CALU_HUMAN	CALU	physical	22863883
DPP9_HUMAN	DPP9	physical	22863883
U5S1_HUMAN	EFTUD2	physical	22863883
T2FA_HUMAN	GTF2F1	physical	22863883
KAP1_HUMAN	PRKAR1B	physical	22863883
RPR1B_HUMAN	RPRD1B	physical	22863883
SYSC_HUMAN	SARS	physical	22863883
SC23A_HUMAN	SEC23A	physical	22863883
GDN_HUMAN	SERPINE2	physical	22863883
SNF8_HUMAN	SNF8	physical	22863883
XPO5_HUMAN	XPO5	physical	22863883
EIF2A_HUMAN	EIF2A	physical	26344197
TRM6_HUMAN	TRMT6	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 DUS3L_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-273; SER-276 AND SER-277, AND MASSSPECTROMETRY.	19413330 [Abstract]
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-273; SER-276 AND SER-277, 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-236, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273, AND MASSSPECTROMETRY.	19690332 [Abstract]