DUS1_YEAST - dbPTM
DUS1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DUS1_YEAST
UniProt AC P53759
Protein Name tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]
Gene Name DUS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 423
Subcellular Localization
Protein Description Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U16 and U17 in cytoplasmic tRNAs..
Protein Sequence MTEPALSSANNALMQKLTGRQLFDKIGRPTRIVAPMVDQSELAWRILSRRYGATLAYTPMLHAKLFATSKKYREDNWSSLDGSSVDRPLVVQFCANDPEYLLAAAKLVEDKCDAVDLNLGCPQGIAKKGHYGSFLMEEWDLIHNLINTLHKNLKVPVTAKIRIFDDCEKSLNYAKMVLDAGAQFLTVHGRVREQKGQKTGLANWETIKYLRDNLPKETVFFANGNILYPEDISRCMEHIGADAVMSAEGNLYNPGVFNVGQTKNKEKIFPRVDKIIREYFQIVKECQESKASKTAMKSHFFKILRPFLPHHTDIRSTLATMNAKATWEEWEEQVVKPVEKVVQEIFEQPDIAIKDEITIGEKQSWGGSYRTVPYWRCQPYFRPVNGITGDKRVMQGLIDESVNKKRKADVPLESADKKKDVKA
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 Orthologous
Protein Cluster
2Acetylation------MTEPALSSA
------CCHHHHHHH
51.1522814378
7Phosphorylation-MTEPALSSANNALM
-CCHHHHHHHHHHHH
29.5230377154
8PhosphorylationMTEPALSSANNALMQ
CCHHHHHHHHHHHHH
35.5519779198
18PhosphorylationNALMQKLTGRQLFDK
HHHHHHHHHHHHHHH
37.0419779198
25AcetylationTGRQLFDKIGRPTRI
HHHHHHHHHCCCEEE
39.4624489116
169UbiquitinationRIFDDCEKSLNYAKM
EEECCHHHHCCHHHH
67.5823749301
391AcetylationVNGITGDKRVMQGLI
CCCCCCCHHHHHHHC
48.5124489116

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 DUS1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DUS1_YEAST !!

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 DUS1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PML39_YEASTPML39genetic
19061648
NCBP1_YEASTSTO1genetic
19061648
LSM7_YEASTLSM7genetic
19061648
EIF3J_YEASTHCR1genetic
19061648
COA4_YEASTCOA4genetic
27708008
KPC1_YEASTPKC1genetic
27708008
PRP5_YEASTPRP5genetic
27708008
CDC10_YEASTCDC10genetic
27708008
CDC48_YEASTCDC48genetic
27708008
TIM22_YEASTTIM22genetic
27708008
DAD1_YEASTDAD1genetic
27708008
TAF12_YEASTTAF12genetic
27708008
MOB2_YEASTMOB2genetic
27708008
SMD1_YEASTSMD1genetic
27708008
MPPA_YEASTMAS2genetic
27708008
BIG1_YEASTBIG1genetic
27708008
EXO70_YEASTEXO70genetic
27708008
DPB11_YEASTDPB11genetic
27708008
PRP21_YEASTPRP21genetic
27708008
KTHY_YEASTCDC8genetic
27708008
CDC11_YEASTCDC11genetic
27708008
RU1C_YEASTYHC1genetic
27708008
SEC12_YEASTSEC12genetic
27708008
SEC63_YEASTSEC63genetic
27708008
HRR25_YEASTHRR25genetic
27708008
MED10_YEASTNUT2genetic
27708008
IMG2_YEASTIMG2genetic
27708008
RPN4_YEASTRPN4genetic
27708008
RS27B_YEASTRPS27Bgenetic
27708008
FLX1_YEASTFLX1genetic
27708008
IF4A_YEASTTIF2genetic
27708008
VPS24_YEASTVPS24genetic
27708008
ELM1_YEASTELM1genetic
27708008
UBI4P_YEASTUBI4genetic
27708008
SIC1_YEASTSIC1genetic
27708008
ACE2_YEASTACE2genetic
27708008
RL37A_YEASTRPL37Agenetic
27708008
COQ11_YEASTYLR290Cgenetic
27708008
ROM2_YEASTROM2genetic
27708008
YNO0_YEASTYNL140Cgenetic
27708008
IDH2_YEASTIDH2genetic
27708008
LIS1_YEASTPAC1genetic
27708008
YP066_YEASTRGL1genetic
27708008
COX10_YEASTCOX10genetic
27708008
WDR6_YEASTRTT10genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DUS1_YEAST

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Related Literatures of Post-Translational Modification

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