FUR4_YEAST - dbPTM
FUR4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FUR4_YEAST
UniProt AC P05316
Protein Name Uracil permease
Gene Name FUR4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 633
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Transport of uracil..
Protein Sequence MPDNLSLHLSGSSKRLNSRQLMESSNETFAPNNVDLEKEYKSSQSNITTEVYEASSFEEKVSSEKPQYSSFWKKIYYEYVVVDKSILGVSILDSFMYNQDLKPVEKERRVWSWYNYCYFWLAECFNINTWQIAATGLQLGLNWWQCWITIWIGYGFVGAFVVLASRVGSAYHLSFPISSRASFGIFFSLWPVINRVVMAIVWYSVQAYIAATPVSLMLKSIFGKDLQDKIPDHFGSPNATTYEFMCFFIFWAASLPFLLVPPHKIRHLFTVKAVLVPFASFGFLIWAIRRAHGRIALGSLTDVQPHGSAFSWAFLRSLMGCMANFSTMVINAPDFSRFSKNPNSALWSQLVCIPFLFSITCLIGILVTAAGYEIYGINYWSPLDVLEKFLQTTYNKGTRAGVFLISFVFAVAQLGTNISANSLSCGTDMSAIFPKFINIKRGSLFCAAMALCICPWNLMATSSKFTMALSAYAIFLSSIAGVVCSDYFVVRRGYIKLTHIYSHQKGSFYMYGNRFGINWRALAAYLCGVAPCLPGFIAEVGAPAIKVSDGAMKLYYLSYWVGYGLSFSSYTALCYFFPVPGCPVNNIIKDKGWFQRWANVDDFEEEWKDTIERDDLVDDNISVYEHEHEKTFI
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
6Phosphorylation--MPDNLSLHLSGSS
--CCCCCEEECCCCC
21.7228152593
10PhosphorylationDNLSLHLSGSSKRLN
CCCEEECCCCCCCCC
26.3619823750
12PhosphorylationLSLHLSGSSKRLNSR
CEEECCCCCCCCCHH
29.3419823750
13PhosphorylationSLHLSGSSKRLNSRQ
EEECCCCCCCCCHHH
25.8919823750
38UbiquitinationPNNVDLEKEYKSSQS
CCCCCHHHHHHHCCC
73.8923749301
41UbiquitinationVDLEKEYKSSQSNIT
CCHHHHHHHCCCCCE
44.7322817900
43PhosphorylationLEKEYKSSQSNITTE
HHHHHHHCCCCCEEE
33.2110811641
45PhosphorylationKEYKSSQSNITTEVY
HHHHHCCCCCEEEEE
31.9510811641
55PhosphorylationTTEVYEASSFEEKVS
EEEEEHHHCHHHHHC
24.5010811641
56PhosphorylationTEVYEASSFEEKVSS
EEEEHHHCHHHHHCC
43.6610811641
62PhosphorylationSSFEEKVSSEKPQYS
HCHHHHHCCCCCCCH
43.7928889911
65UbiquitinationEEKVSSEKPQYSSFW
HHHHCCCCCCCHHHH
39.0923749301
501PhosphorylationYIKLTHIYSHQKGSF
EEEEEEEEEECCCEE
7.7827017623
507PhosphorylationIYSHQKGSFYMYGNR
EEEECCCEEEEECCC
21.9027017623
509PhosphorylationSHQKGSFYMYGNRFG
EECCCEEEEECCCCC
7.3627017623
511PhosphorylationQKGSFYMYGNRFGIN
CCCEEEEECCCCCCC
10.4027017623
622PhosphorylationDLVDDNISVYEHEHE
HCCCCCCEEEEECCH
25.5425521595
624PhosphorylationVDDNISVYEHEHEKT
CCCCCEEEEECCHHC
12.5529688323

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
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FUR4_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 FUR4_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAN1_YEASTCAN1physical
15536122
SUR7_YEASTSUR7physical
15536122
FUI1_YEASTFUI1genetic
9485596

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FUR4_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-6 AND SER-622, AND MASSSPECTROMETRY.

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