WDR6_YEAST - dbPTM
WDR6_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR6_YEAST
UniProt AC Q08924
Protein Name Regulator of Ty1 transposition protein 10
Gene Name RTT10
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1013
Subcellular Localization Cytoplasm. Endosome. Recruited to endosomes in cells in which increased recycling of internalized plasma membrane proteins occurs.
Protein Description Involved in regulation of Ty1 transposition. Plays also a role in the regulation of the retromer complex and is required for the recycling from endosomes of plasma membrane proteins like CAN1 and MUP1. Required together with TRM7 for the methylation of the 2'-O-ribose of nucleotides at position 34 of the tRNA anticodon loop of tRNA(Phe) and tRNA(Leu(UAA))..
Protein Sequence MKDLSHYGPALCVKFYNDYVLAGYGPFIHVYDYHSATLINKCRLFHYNKVHGLSLSSEGKILAYGARSVTIVELEDVLKKESLVDFERINSDWITGATFSFDNLQIYLLTCYNKVLICDLNCEVLFRKSLGGERSILYSGIIKVFGPDKVYVNAGTVMGGVIIWDLFSETKIHNLLGHEGSIFYVNLSNNGRYVASCSDDRSIRLWDLETGKQLSVGWSHTARIWNLMFFDNDSKLISVSEDCTCRVWNIIESRENVAELSISNVYEVHLIKSIWGVDVKDDEMIAVTSGNDGRLKLIDLLQLKRHGDEETSFSLDDIAKQCGDIFEKNESIKGFQWFSFGVIAITSLGKILKYSDVTKQWKLLLTNEKFNSYPITNGIQTQNIAVFSNNKSDILLIKFSKDSADIIETEEFHLDELSKTNNCLVTEYDDDSFLLTLQSPNPREKFVCLEISLQNLKIKSKHCFNKPENFSSSCLTSFRNHILVGSRFSTLVIYNLLDESEEPFIIRRLSPGDTTTSIEFVEDKDNSAVFSVTNRDGYYVFIELTKNSLEEGPYRLSYKVLHSNKMMKGFLEGAFFNSKGEYITYGFKSSLFYLYNETNCYELASEVCGGSHRLWNLAKITDGHVLMYIKASRFHLRKIYNSIVPETLENGVHGREIRDISICPVSNTNTNDNFKDGHIFCTASEDTTIKLGYFNNRTGKVQNFWTQRKHVSGLQRCQFINHKLMISSSAREELFLWELNDKYNKRPYMTIRQALPVSTNNSDLRIMDFDVKFISQSGDFLLVTVYSDSTIKIWHYRENQNKFDLIMQGRYKTCCLFNVVFIALKEELLVVISPTDGHLVVYNITEYVPFSVDPISGDLVDHKLDATISNLPAPVAQLPVHQSGVKSLDYVANATRTSATILTGGDDNGLGLSNLKLDDSNKVTLKTSDFIAAAASSTITSGMLINGGKEVITTSVDQVIRAWEITAGKLSLVDKKRTTVADTGSLEIISNDEDADSEKTLLIGGVGLSIWKK
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
219PhosphorylationKQLSVGWSHTARIWN
CEEEEECCCHHEEEE		12.6728889911
304AcetylationLIDLLQLKRHGDEET
EEEEECHHHHCCCCC		29.4124489116
392PhosphorylationAVFSNNKSDILLIKF
EEEECCCCCEEEEEE		31.8221126336
420PhosphorylationHLDELSKTNNCLVTE
CHHHHHHCCCEEEEE		28.4327017623
436PhosphorylationDDDSFLLTLQSPNPR
CCCCEEEEECCCCHH		25.5427017623
439PhosphorylationSFLLTLQSPNPREKF
CEEEEECCCCHHHCE		29.7427017623
477PhosphorylationFSSSCLTSFRNHILV
CCHHHHHHHCCCEEC		14.8425371407
514PhosphorylationRRLSPGDTTTSIEFV
EECCCCCCCCEEEEE		37.5828889911
897PhosphorylationYVANATRTSATILTG
HHHCCCCCCEEEEEC		20.5422369663
898PhosphorylationVANATRTSATILTGG
HHCCCCCCEEEEECC		21.8122369663
900PhosphorylationNATRTSATILTGGDD
CCCCCCEEEEECCCC		19.1122369663
903PhosphorylationRTSATILTGGDDNGL
CCCEEEEECCCCCCC		34.9622369663
913PhosphorylationDDNGLGLSNLKLDDS
CCCCCCCCCCEECCC		38.0122369663
927PhosphorylationSNKVTLKTSDFIAAA
CCCEEEEHHHHHHHH		36.3229688323
928PhosphorylationNKVTLKTSDFIAAAA
CCEEEEHHHHHHHHH		29.0128132839
936PhosphorylationDFIAAAASSTITSGM
HHHHHHHCCCCCCCC		24.2428132839
937PhosphorylationFIAAAASSTITSGML
HHHHHHCCCCCCCCE		21.0729688323
938PhosphorylationIAAAASSTITSGMLI
HHHHHCCCCCCCCEE		26.2729688323
940PhosphorylationAAASSTITSGMLING
HHHCCCCCCCCEECC		21.2229688323
941PhosphorylationAASSTITSGMLINGG
HHCCCCCCCCEECCC		20.5329688323
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 WDR6_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR6_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 WDR6_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRM7_YEASTTRM7physical
14759368
WDR6_YEASTRTT10physical
14759368
TRM7_YEASTTRM7physical
16554755
HSP7F_YEASTSSE1physical
19536198
SSB1_YEASTSSB1physical
19536198
TRM1_YEASTTRM1genetic
22912484
TR732_YEASTTRM732genetic
22912484
PEX32_YEASTPEX32genetic
27708008
SWC5_YEASTSWC5genetic
27708008
TRM1_YEASTTRM1genetic
27708008
INO2_YEASTINO2genetic
27708008
UBP3_YEASTUBP3genetic
27708008
BUD27_YEASTBUD27genetic
27708008
SGF73_YEASTSGF73genetic
27708008
AAKG_YEASTSNF4genetic
27708008
VAM7_YEASTVAM7genetic
27708008
GAT4_YEASTGAT4genetic
27708008
VPS24_YEASTVPS24genetic
27708008
SAC1_YEASTSAC1genetic
27708008
IRS4_YEASTIRS4genetic
27708008
LDB18_YEASTLDB18genetic
27708008
ENV10_YEASTENV10genetic
27708008
STM1_YEASTSTM1genetic
27708008
SRC1_YEASTSRC1genetic
27708008
MSC1_YEASTMSC1genetic
27708008
PFKA2_YEASTPFK2genetic
27708008
SWS2_YEASTSWS2genetic
27708008
BRE5_YEASTBRE5genetic
27708008
SIN3_YEASTSIN3genetic
27708008
YO036_YEASTYOL036Wgenetic
27708008
TRM11_YEASTTRM11genetic
27708008
TYW4_YEASTPPM2genetic
27708008
ESS1_YEASTESS1genetic
29674565
TYW4_YEASTPPM2genetic
29674565
VPS51_YEASTVPS51genetic
29674565
EF1A_YEASTTEF2genetic
29674565
TRM1_YEASTTRM1genetic
29674565
UBP3_YEASTUBP3genetic
29674565
ATC1_YEASTPMR1genetic
29674565
XPOT_YEASTLOS1genetic
29674565
SIC1_YEASTSIC1genetic
29674565
YPT6_YEASTYPT6genetic
29674565
SRC1_YEASTSRC1genetic
29674565
ERG5_YEASTERG5genetic
29674565
SCS7_YEASTSCS7genetic
29674565
EAF7_YEASTEAF7genetic
29674565
TPT1_YEASTTPT1genetic
29674565
TYSY_YEASTCDC21genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WDR6_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-514, AND MASSSPECTROMETRY.

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