FUI1_YEAST - dbPTM
FUI1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FUI1_YEAST
UniProt AC P38196
Protein Name Uridine permease
Gene Name FUI1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 639
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description High-affinity transport of uridine..
Protein Sequence MPVSDSGFDNSSKTMKDDTIPTEDYEEITKESEMGDATKITSKIDANVIEKKDTDSENNITIAQDDEKVSWLQRVVEFFEVKNDSTDLADHKPENPIRTFKDLQESLRSTYLYNTDLRPVEAKRRTWTWKQYIFFWISGSFNVNTWQISATGLQLGLNWWQTWICIWVGYTFVAFFLILGSKVGNNYHISFPISSRVSFGIYFSIWIVINRVVMACVWNSTLAYIGSQCVQLMLKAIFGTNLNTRIKDTIKNPNLTNFEFMCFMVFWVACLPFLWFPPDKLRHIFALKSAITPFAAFGFLIWTLCKAKGHLALGSLNDNGGAISKTVLAWSVIRAIMSALDNFSTLILNAPDFTRFGKTYKSSVYSQLIALPVCYAIISLIGILSVSAAYTLYGVNYWSPLDILNRYLDNYTSGNRAGVFLISFIFAFDQLGANLSGNSIPAGTDLTALLPKFINIRRGSYICALISLAICPWDLLSSSSKFTTALAAYAVFLSAIAGVISADYFIVRKGYVNIFHCYTDKPGSYYMYNKYGTNWRAVVAYIFGIAPNFAGFLGSVGVSVPIGAMKVYYLNYFVGYLLAALSYCILVYFYPIKGIPGDAKITDRKWLEEWVEVEEFGTEREAFEEYGGVSTGYEKIRYI
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
4Phosphorylation----MPVSDSGFDNS
----CCCCCCCCCCC		21.8625005228
6Phosphorylation--MPVSDSGFDNSSK
--CCCCCCCCCCCCC		33.5819823750
11PhosphorylationSDSGFDNSSKTMKDD
CCCCCCCCCCCCCCC		34.7522369663
12PhosphorylationDSGFDNSSKTMKDDT
CCCCCCCCCCCCCCC		38.1024909858
14PhosphorylationGFDNSSKTMKDDTIP
CCCCCCCCCCCCCCC		31.2519823750
16UbiquitinationDNSSKTMKDDTIPTE
CCCCCCCCCCCCCCC		58.6523749301
19PhosphorylationSKTMKDDTIPTEDYE
CCCCCCCCCCCCCHH		38.7021440633
22PhosphorylationMKDDTIPTEDYEEIT
CCCCCCCCCCHHHHH		37.3221440633
25PhosphorylationDTIPTEDYEEITKES
CCCCCCCHHHHHCHH		14.8319823750
29PhosphorylationTEDYEEITKESEMGD
CCCHHHHHCHHHCCC		31.8519823750
30UbiquitinationEDYEEITKESEMGDA
CCHHHHHCHHHCCCH		65.9722817900
32PhosphorylationYEEITKESEMGDATK
HHHHHCHHHCCCHHH		34.1425521595
38PhosphorylationESEMGDATKITSKID
HHHCCCHHHCCCCCC		27.9320377248
39UbiquitinationSEMGDATKITSKIDA
HHCCCHHHCCCCCCC		45.7923749301
41PhosphorylationMGDATKITSKIDANV
CCCHHHCCCCCCCHH		26.0623749301
42PhosphorylationGDATKITSKIDANVI
CCHHHCCCCCCCHHE		30.9617330950
43UbiquitinationDATKITSKIDANVIE
CHHHCCCCCCCHHEE		35.6423749301
51UbiquitinationIDANVIEKKDTDSEN
CCCHHEECCCCCCCC		44.8423749301
52UbiquitinationDANVIEKKDTDSENN
CCHHEECCCCCCCCC		53.7423749301
54PhosphorylationNVIEKKDTDSENNIT
HHEECCCCCCCCCEE		50.7525521595
56PhosphorylationIEKKDTDSENNITIA
EECCCCCCCCCEEEE		44.2925521595
61PhosphorylationTDSENNITIAQDDEK
CCCCCCEEEECCHHH		16.6321440633
92UbiquitinationSTDLADHKPENPIRT
CCCCCCCCCCCCCCC		55.3522817900
101AcetylationENPIRTFKDLQESLR
CCCCCCHHHHHHHHH		57.8424489116
338PhosphorylationSVIRAIMSALDNFST
HHHHHHHHHHHHCCH		21.4027017623
344PhosphorylationMSALDNFSTLILNAP
HHHHHHCCHHHHCCC		28.6727017623
345PhosphorylationSALDNFSTLILNAPD
HHHHHCCHHHHCCCC		17.4327017623
354PhosphorylationILNAPDFTRFGKTYK
HHCCCCCCCCCCHHH		32.2527017623
635UbiquitinationGVSTGYEKIRYI---
CCCCCCCEEECC---		24.8123749301
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 FUI1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FUI1_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 FUI1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPN3_YEASTRPN3physical
10688190
YG3A_YEASTYGR130Cphysical
18467557
PDR12_YEASTPDR12physical
18467557
MUP1_YEASTMUP1physical
18467557
FMP45_YEASTFMP45physical
18467557
RFS1_YEASTRFS1physical
18467557
YG3A_YEASTYGR130Cphysical
22615397
EF1A_YEASTTEF2genetic
27708008
ARO1_YEASTARO1genetic
27708008
MON1_YEASTMON1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
ELM1_YEASTELM1genetic
27708008
ZRC1_YEASTZRC1genetic
27708008
RNH2A_YEASTRNH201genetic
27708008
VAM3_YEASTVAM3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FUI1_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 SER-4, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54 AND SER-56, AND MASSSPECTROMETRY.

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