QDR2_YEAST - dbPTM
QDR2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID QDR2_YEAST
UniProt AC P40474
Protein Name Quinidine resistance protein 2
Gene Name QDR2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 542
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Multidrug resistance transporter involved in resistance and adaptation to quinidine and to the herbicide barban (4-chloro-2-butynyl [3-chlorophenyl] carbamate). Implicated in potassium uptake..
Protein Sequence MAGATSSIIRENDFEDELAESMQSYNRETADKLALTRTESVKPEPEITAPPHSRFSRSFKTVLIAQCAFTGFFSTIAGAIYYPVLSVIERKFDIDEELVNVTVVVYFVFQGLAPTFMGGFADSLGRRPVVLVAIVIYFGACIGLACAQTYAQIIVLRCLQAAGISPVIAINSGIMGDVTTRAERGGYVGYVAGFQVLGSAFGALIGAGLSSRWGWRAIFWFLAIGSGICFLASFLILPETKRNISGNGSVTPKSYLNRAPILVLPTVRKSLHLDNPDYETLELPTQLNLLAPFKILKAYEICILMLVAGLQFAMYTTHLTALSTALSKQYHLTVAKVGLCYLPSGICTLCSIVIAGRYLNWNYRRRLKYYQNWLGKKRSKLLEEHDNDLNLVQRIIENDPKYTFNIFKARLQPAFVTLLLSSSGFCAYGWCITVKAPLAAVLCMSGFASLFSNCILTFSTTLIVDLFPTKTSTATGCLNLFRCILSAVFIAALSKMVEKMKFGGVFTFLGALTSSSSILLFILLRKGKELAFKRKKQELGVN
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
5Phosphorylation---MAGATSSIIREN
---CCCCCCHHHCCC		23.3028889911
6Phosphorylation--MAGATSSIIREND
--CCCCCCHHHCCCC		21.0022369663
7Phosphorylation-MAGATSSIIRENDF
-CCCCCCHHHCCCCC		20.0622369663
21PhosphorylationFEDELAESMQSYNRE
CHHHHHHHHHHCCHH		19.2622369663
24PhosphorylationELAESMQSYNRETAD
HHHHHHHHCCHHHHH		18.7422369663
25PhosphorylationLAESMQSYNRETADK
HHHHHHHCCHHHHHH		11.0122369663
29PhosphorylationMQSYNRETADKLALT
HHHCCHHHHHHHHHH		36.6022369663
32UbiquitinationYNRETADKLALTRTE
CCHHHHHHHHHHCCC		32.9423749301
36PhosphorylationTADKLALTRTESVKP
HHHHHHHHCCCCCCC		29.9128152593
38PhosphorylationDKLALTRTESVKPEP
HHHHHHCCCCCCCCC		27.6321082442
40PhosphorylationLALTRTESVKPEPEI
HHHHCCCCCCCCCCC		34.5221082442
42UbiquitinationLTRTESVKPEPEITA
HHCCCCCCCCCCCCC		53.6023749301
53PhosphorylationEITAPPHSRFSRSFK
CCCCCCCCCCCHHHH		40.5730377154
245PhosphorylationPETKRNISGNGSVTP
CCCCCCCCCCCCCCC		29.7421126336
251PhosphorylationISGNGSVTPKSYLNR
CCCCCCCCCHHHHCC		27.0525704821
253UbiquitinationGNGSVTPKSYLNRAP
CCCCCCCHHHHCCCC		42.2223749301
380AcetylationWLGKKRSKLLEEHDN
HHCHHHHHHHHHCCC		62.2124489116
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 QDR2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of QDR2_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 QDR2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCB3_YEASTTCB3physical
18467557
TPO1_YEASTTPO1physical
18467557
MID2_YEASTMID2physical
18467557
PDR5_YEASTPDR5physical
18467557
QDR2_YEASTQDR2physical
18467557
PDR12_YEASTPDR12physical
18467557
YL413_YEASTINA1physical
18467557
SFK1_YEASTSFK1physical
18467557
VMA21_YEASTVMA21genetic
20093466
SLH1_YEASTSLH1genetic
20093466
RIM4_YEASTRIM4genetic
20093466
PEX18_YEASTPEX18genetic
20093466
ALN_YEASTDAL1genetic
20093466
YJU6_YEASTYJL206Cgenetic
20093466
TCB1_YEASTTCB1genetic
20093466
SERC_YEASTSER1genetic
20093466
CUP9_YEASTCUP9genetic
20093466
SPO19_YEASTSPO19genetic
20093466
CSR2_YEASTCSR2genetic
20093466
TCB3_YEASTTCB3physical
22615397
VMA21_YEASTVMA21genetic
27708008
CDC10_YEASTCDC10genetic
27708008
NSE4_YEASTNSE4genetic
27708008
RSP5_YEASTRSP5genetic
27708008
SMD1_YEASTSMD1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
FDFT_YEASTERG9genetic
27708008
CDC11_YEASTCDC11genetic
27708008
MED14_YEASTRGR1genetic
27708008
MED4_YEASTMED4genetic
27708008
ODO2_YEASTKGD2genetic
27708008
SHE9_YEASTSHE9genetic
27708008
SLH1_YEASTSLH1genetic
27708008
MND2_YEASTMND2genetic
27708008
ALN_YEASTDAL1genetic
27708008
YJ24_YEASTKCH1genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
JEN1_YEASTJEN1genetic
27708008
CUP9_YEASTCUP9genetic
27708008
ERV14_YEASTERV14physical
28723420
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of QDR2_YEAST

loading...

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-40, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory