PDR5_YEAST - dbPTM
PDR5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDR5_YEAST
UniProt AC P33302
Protein Name Pleiotropic ABC efflux transporter of multiple drugs
Gene Name PDR5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1511
Subcellular Localization Cell membrane
Multi-pass membrane protein . The ERAD mutants 'Pro-183' and 'Tyr-1427' fail to reach the plasma membrane. The mutant 'Pro-183' accumulates into ER-associated compartments.
Protein Description Active efflux of weakly charged organic compounds of 90 cubic Angstroms to 300 cubic Angstroms surface volume. Confers resistance to numerous chemicals including cycloheximide, sulfomethuron methyl, steroids, antiseptics, antibiotics, anticancer, herbicides, mycotoxins, insecticides, ionophores, alkaloids, flavonoids, phenothiazines, organotin compounds, carbazoles, lysosomotropic aminoesters, detergents, rhodamines and other fluorophores, azoles and other antifungals. Exhibits nucleoside triphosphatase activity..
Protein Sequence MPEAKLNNNVNDVTSYSSASSSTENAADLHNYNGFDEHTEARIQKLARTLTAQSMQNSTQSAPNKSDAQSIFSSGVEGVNPIFSDPEAPGYDPKLDPNSENFSSAAWVKNMAHLSAADPDFYKPYSLGCAWKNLSASGASADVAYQSTVVNIPYKILKSGLRKFQRSKETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTHGFDLGADTKISYSGYSGDDIKKHFRGEVVYNAEADVHLPHLTVFETLVTVARLKTPQNRIKGVDRESYANHLAEVAMATYGLSHTRNTKVGNDIVRGVSGGERKRVSIAEVSICGSKFQCWDNATRGLDSATALEFIRALKTQADISNTSATVAIYQCSQDAYDLFNKVCVLDDGYQIYYGPADKAKKYFEDMGYVCPSRQTTADFLTSVTSPSERTLNKDMLKKGIHIPQTPKEMNDYWVKSPNYKELMKEVDQRLLNDDEASREAIKEAHIAKQSKRARPSSPYTVSYMMQVKYLLIRNMWRLRNNIGFTLFMILGNCSMALILGSMFFKIMKKGDTSTFYFRGSAMFFAILFNAFSSLLEIFSLYEARPITEKHRTYSLYHPSADAFASVLSEIPSKLIIAVCFNIIFYFLVDFRRNGGVFFFYLLINIVAVFSMSHLFRCVGSLTKTLSEAMVPASMLLLALSMYTGFAIPKKKILRWSKWIWYINPLAYLFESLLINEFHGIKFPCAEYVPRGPAYANISSTESVCTVVGAVPGQDYVLGDDFIRGTYQYYHKDKWRGFGIGMAYVVFFFFVYLFLCEYNEGAKQKGEILVFPRSIVKRMKKRGVLTEKNANDPENVGERSDLSSDRKMLQESSEEESDTYGEIGLSKSEAIFHWRNLCYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGDILVNGIPRDKSFPRSIGYCQQQDLHLKTATVRESLRFSAYLRQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVFLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILMQEFDRLLFMQRGGKTVYFGDLGEGCKTMIDYFESHGAHKCPADANPAEWMLEVVGAAPGSHANQDYYEVWRNSEEYRAVQSELDWMERELPKKGSITAAEDKHEFSQSIIYQTKLVSIRLFQQYWRSPDYLWSKFILTIFNQLFIGFTFFKAGTSLQGLQNQMLAVFMFTVIFNPILQQYLPSFVQQRDLYEARERPSRTFSWISFIFAQIFVEVPWNILAGTIAYFIYYYPIGFYSNASAAGQLHERGALFWLFSCAFYVYVGSMGLLVISFNQVAESAANLASLLFTMSLSFCGVMTTPSAMPRFWIFMYRVSPLTYFIQALLAVGVANVDVKCADYELLEFTPPSGMTCGQYMEPYLQLAKTGYLTDENATDTCSFCQISTTNDYLANVNSFYSERWRNYGIFICYIAFNYIAGVFFYWLARVPKKNGKLSKK
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
14PhosphorylationNNNVNDVTSYSSASS
CCCCCCHHHCCCCCC		25.4720377248
15PhosphorylationNNVNDVTSYSSASSS
CCCCCHHHCCCCCCC		23.9020377248
16PhosphorylationNVNDVTSYSSASSST
CCCCHHHCCCCCCCC		9.4020377248
17PhosphorylationVNDVTSYSSASSSTE
CCCHHHCCCCCCCCC		21.1320377248
18PhosphorylationNDVTSYSSASSSTEN
CCHHHCCCCCCCCCC		24.7620377248
20PhosphorylationVTSYSSASSSTENAA
HHHCCCCCCCCCCHH		27.1120377248
21PhosphorylationTSYSSASSSTENAAD
HHCCCCCCCCCCHHH		40.7820377248
22PhosphorylationSYSSASSSTENAADL
HCCCCCCCCCCHHHH		36.9320377248
23PhosphorylationYSSASSSTENAADLH
CCCCCCCCCCHHHHC		34.9020377248
32PhosphorylationNAADLHNYNGFDEHT
CHHHHCCCCCCCHHH		13.1020377248
39PhosphorylationYNGFDEHTEARIQKL
CCCCCHHHHHHHHHH		29.3221440633
49PhosphorylationRIQKLARTLTAQSMQ
HHHHHHHHHHHHHHH		23.8922369663
51PhosphorylationQKLARTLTAQSMQNS
HHHHHHHHHHHHHHC		23.2625521595
54PhosphorylationARTLTAQSMQNSTQS
HHHHHHHHHHHCCCC		21.6322369663
58PhosphorylationTAQSMQNSTQSAPNK
HHHHHHHCCCCCCCH		15.7822369663
59PhosphorylationAQSMQNSTQSAPNKS
HHHHHHCCCCCCCHH		33.8122369663
61PhosphorylationSMQNSTQSAPNKSDA
HHHHCCCCCCCHHHH		45.8722369663
65UbiquitinationSTQSAPNKSDAQSIF
CCCCCCCHHHHHHHH		48.9623749301
66PhosphorylationTQSAPNKSDAQSIFS
CCCCCCHHHHHHHHH		44.8322890988
70PhosphorylationPNKSDAQSIFSSGVE
CCHHHHHHHHHCCCC		27.5922890988
73PhosphorylationSDAQSIFSSGVEGVN
HHHHHHHHCCCCCCC		25.2222890988
74PhosphorylationDAQSIFSSGVEGVNP
HHHHHHHCCCCCCCC		35.7922890988
84PhosphorylationEGVNPIFSDPEAPGY
CCCCCCCCCCCCCCC		53.6422890988
103PhosphorylationDPNSENFSSAAWVKN
CCCCCCCCHHHHHHH		30.5628889911
104PhosphorylationPNSENFSSAAWVKNM
CCCCCCCHHHHHHHH		20.1919779198
159PhosphorylationIPYKILKSGLRKFQR
CCHHHHHHHHHHHHH		39.3528889911
205PhosphorylationGCTTLLKSISSNTHG
CHHHHHHHHCCCCCC		27.8921440633
207PhosphorylationTTLLKSISSNTHGFD
HHHHHHHCCCCCCCC		25.3222369663
208PhosphorylationTLLKSISSNTHGFDL
HHHHHHCCCCCCCCC		44.0422369663
210PhosphorylationLKSISSNTHGFDLGA
HHHHCCCCCCCCCCC		25.8922369663
219PhosphorylationGFDLGADTKISYSGY
CCCCCCCCEEEECCC		29.7322369663
220UbiquitinationFDLGADTKISYSGYS
CCCCCCCEEEECCCC		30.1515699485
227PhosphorylationKISYSGYSGDDIKKH
EEEECCCCCHHHHHH		38.9919779198
232UbiquitinationGYSGDDIKKHFRGEV
CCCCHHHHHHHCCEE		47.3815699485
232AcetylationGYSGDDIKKHFRGEV
CCCCHHHHHHHCCEE		47.3824489116
232SuccinylationGYSGDDIKKHFRGEV
CCCCHHHHHHHCCEE		47.3823954790
233UbiquitinationYSGDDIKKHFRGEVV
CCCHHHHHHHCCEEE		48.5915699485
291PhosphorylationAEVAMATYGLSHTRN
HHHHHHHHCCCCCCC		13.4128889911
310PhosphorylationNDIVRGVSGGERKRV
CCHHCCCCCCCCCCE		43.8620377248
327PhosphorylationAEVSICGSKFQCWDN
EEEEECCCEECCCCC		26.3627017623
341PhosphorylationNATRGLDSATALEFI
CCCCCCCHHHHHHHH		32.3428152593
358PhosphorylationLKTQADISNTSATVA
HHHHHCCCCCCCEEE		34.3027017623
367PhosphorylationTSATVAIYQCSQDAY
CCCEEEEEEECHHHH		8.1727017623
374PhosphorylationYQCSQDAYDLFNKVC
EEECHHHHHHHHCEE		22.8227017623
399UbiquitinationGPADKAKKYFEDMGY
ECHHHHHHHHHHCCC		61.0915699485
431UbiquitinationPSERTLNKDMLKKGI
CCCCCCCHHHHHCCC		47.8522817900
435UbiquitinationTLNKDMLKKGIHIPQ
CCCHHHHHCCCCCCC		42.1722817900
436UbiquitinationLNKDMLKKGIHIPQT
CCHHHHHCCCCCCCC		60.1722817900
443PhosphorylationKGIHIPQTPKEMNDY
CCCCCCCCCHHHCCC		30.8521440633
450PhosphorylationTPKEMNDYWVKSPNY
CCHHHCCCCCCCCCH		13.7019795423
453UbiquitinationEMNDYWVKSPNYKEL
HHCCCCCCCCCHHHH		46.1524961812
453AcetylationEMNDYWVKSPNYKEL
HHCCCCCCCCCHHHH		46.1524489116
454PhosphorylationMNDYWVKSPNYKELM
HCCCCCCCCCHHHHH		14.5719795423
457PhosphorylationYWVKSPNYKELMKEV
CCCCCCCHHHHHHHH		14.8219795423
475PhosphorylationLLNDDEASREAIKEA
HHCCHHHHHHHHHHH		28.7120377248
494PhosphorylationQSKRARPSSPYTVSY
HCCCCCCCCCCHHHH		38.0920377248
495PhosphorylationSKRARPSSPYTVSYM
CCCCCCCCCCHHHHH		25.3020377248
500PhosphorylationPSSPYTVSYMMQVKY
CCCCCHHHHHHHHHH		10.2627017623
501PhosphorylationSSPYTVSYMMQVKYL
CCCCHHHHHHHHHHH		7.7127017623
550PhosphorylationKIMKKGDTSTFYFRG
HHHCCCCCCEEEECH		38.0327017623
551PhosphorylationIMKKGDTSTFYFRGS
HHCCCCCCEEEECHH		22.6627017623
554PhosphorylationKGDTSTFYFRGSAMF
CCCCCEEEECHHHHH		7.7727017623
590PhosphorylationPITEKHRTYSLYHPS
CCCHHCCEEECCCCC		19.7220377248
591PhosphorylationITEKHRTYSLYHPSA
CCHHCCEEECCCCCH		9.1620377248
592PhosphorylationTEKHRTYSLYHPSAD
CHHCCEEECCCCCHH		23.1020377248
594PhosphorylationKHRTYSLYHPSADAF
HCCEEECCCCCHHHH		13.0220377248
664PhosphorylationGSLTKTLSEAMVPAS
HHHHHHHHHHCCCHH		28.6527017623
671PhosphorylationSEAMVPASMLLLALS
HHHCCCHHHHHHHHH		12.1427017623
678PhosphorylationSMLLLALSMYTGFAI
HHHHHHHHHHHCCCC		12.2527017623
734N-linked_GlycosylationPRGPAYANISSTESV
CCCCCCCCCCCCCCE		23.23-
825AcetylationKRGVLTEKNANDPEN
HCCCCCCCCCCCCCC		57.0024489116
825UbiquitinationKRGVLTEKNANDPEN
HCCCCCCCCCCCCCC		57.0023749301
837PhosphorylationPENVGERSDLSSDRK
CCCCCCCCCCHHHHH		38.3022369663
840PhosphorylationVGERSDLSSDRKMLQ
CCCCCCCHHHHHHHH		34.8725521595
841PhosphorylationGERSDLSSDRKMLQE
CCCCCCHHHHHHHHH		49.0525521595
844UbiquitinationSDLSSDRKMLQESSE
CCCHHHHHHHHHCCH		49.2923749301
849PhosphorylationDRKMLQESSEEESDT
HHHHHHHCCHHHHCC		30.0422369663
850PhosphorylationRKMLQESSEEESDTY
HHHHHHCCHHHHCCC		48.5522369663
854PhosphorylationQESSEEESDTYGEIG
HHCCHHHHCCCCCCC		38.2322369663
856PhosphorylationSSEEESDTYGEIGLS
CCHHHHCCCCCCCCC		42.5822369663
857PhosphorylationSEEESDTYGEIGLSK
CHHHHCCCCCCCCCH		20.1122369663
863PhosphorylationTYGEIGLSKSEAIFH
CCCCCCCCHHHHHHH		28.9922890988
911UbiquitinationMGASGAGKTTLLDCL
HCCCCCCHHHHHHHH		37.4915699485
1045PhosphorylationTSGLDSQTAWSICQL
CCCCCHHHHHHHHHH		33.7620377248
1048PhosphorylationLDSQTAWSICQLMKK
CCHHHHHHHHHHHHH		15.8320377248
1101UbiquitinationGDLGEGCKTMIDYFE
CCCCCCHHHHHHHHH		52.5724961812
1156PhosphorylationEEYRAVQSELDWMER
HHHHHHHHHHHHHHH		33.2627017623
1170PhosphorylationRELPKKGSITAAEDK
HHCCCCCCCCCCCCC		26.1628889911
1172PhosphorylationLPKKGSITAAEDKHE
CCCCCCCCCCCCCCH		22.8527717283
1414PhosphorylationVDVKCADYELLEFTP
CCCEECCHHHEECCC		7.0227017623
1426PhosphorylationFTPPSGMTCGQYMEP
CCCCCCCCCCHHCHH		19.6027017623
1430PhosphorylationSGMTCGQYMEPYLQL
CCCCCCHHCHHHHHH		6.6927017623
1434PhosphorylationCGQYMEPYLQLAKTG
CCHHCHHHHHHHHHC		8.1827017623
1447N-linked_GlycosylationTGYLTDENATDTCSF
HCCCCCCCCCCCCCC		51.45-
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 ligaseHRD1Q08109
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDR5_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 PDR5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ECM27_YEASTECM27physical
11957110
HKR1_YEASTHKR1physical
11957110
PDR5_YEASTPDR5physical
11957110
PRY3_YEASTPRY3physical
11957110
RAX2_YEASTRAX2physical
11957110
TMS1_YEASTTMS1physical
11957110
OTU1_YEASTOTU1physical
11957110
YAP3_YEASTYAP3physical
11957110
SC160_YEASTSCP160physical
11957110
UTP10_YEASTUTP10physical
11957110
NRT1_YEASTNRT1physical
11957110
SNQ2_YEASTSNQ2physical
12469340
PMA1_YEASTPMA1physical
12469340
HXT7_YEASTHXT7physical
12469340
MRH1_YEASTMRH1physical
12469340
FET4_YEASTFET4physical
12469340
PTR2_YEASTPTR2physical
12469340
NCE2_YEASTNCE102physical
12469340
KC12_YEASTYCK2physical
12469340
SUR7_YEASTSUR7physical
12469340
YG5L_YEASTYGR266Wphysical
12469340
PDR3_YEASTPDR3genetic
8007969
PDR1_YEASTPDR1genetic
7629127
YOR1_YEASTYOR1genetic
9890948
YOR1_YEASTYOR1genetic
15342785
RSB1_YEASTRSB1genetic
15342785
SNQ2_YEASTSNQ2genetic
15985442
YOR1_YEASTYOR1genetic
15985442
ERG6_YEASTERG6genetic
15985442
PDR15_YEASTPDR15genetic
17881724
PDR5_YEASTPDR5physical
18467557
PDR12_YEASTPDR12physical
18467557
DIP5_YEASTDIP5physical
18467557
DSE2_YEASTDSE2genetic
20093466
YJ24_YEASTKCH1genetic
20093466
YMF3_YEASTYML053Cgenetic
20093466
SNQ2_YEASTSNQ2genetic
8810273
GEP3_YEASTGEP3genetic
21987634
PDR5_YEASTPDR5physical
22615397
SSB1_YEASTSSB1physical
22940862
HSP71_YEASTSSA1physical
22940862
YPT7_YEASTYPT7genetic
22999853
YPT32_YEASTYPT32genetic
22999853
YPT31_YEASTYPT31genetic
22999853
SNQ2_YEASTSNQ2genetic
19884123
YOR1_YEASTYOR1genetic
19884123
AIM41_YEASTAIM41physical
23831759
PDR5_YEASTPDR5physical
23831759
ORM2_YEASTORM2physical
23831759
SEO1_YEASTSEO1physical
23831759
YO075_YEASTYOL075Cphysical
23831759
MCH5_YEASTMCH5physical
23831759
SMF2_YEASTSMF2physical
23831759
NPC1_YEASTNCR1physical
23831759
ZRT1_YEASTZRT1physical
23831759
SNQ2_YEASTSNQ2genetic
23831759
ZRT1_YEASTZRT1genetic
23831759
CCW12_YEASTCCW12physical
23831759
COS1_YEASTCOS1physical
23831759
IF2P_YEASTFUN12physical
23831759
FUN26_YEASTFUN26physical
23831759
GLE1_YEASTGLE1physical
23831759
OST2_YEASTOST2physical
23831759
PMA1_YEASTPMA1physical
23831759
RAS2_YEASTRAS2physical
23831759
RTN1_YEASTRTN1physical
23831759
SERC_YEASTSER1physical
23831759
SNQ2_YEASTSNQ2physical
23831759
ELO3_YEASTELO3physical
23831759
TMN3_YEASTTMN3physical
23831759
YG1I_YEASTYGR026Wphysical
23831759
POM33_YEASTPOM33physical
23831759
YL050_YEASTYLR050Cphysical
23831759
YND1_YEASTYND1physical
23831759
YNU8_YEASTYNL208Wphysical
23831759
RPD3_YEASTRPD3genetic
25263705
PP11_YEASTSIT4genetic
25263705
GCN4_YEASTGCN4genetic
25724885
GET1_YEASTGET1genetic
27708008
DSE2_YEASTDSE2genetic
27708008
YJ24_YEASTKCH1genetic
27708008
YMF3_YEASTYML053Cgenetic
27708008
COX10_YEASTCOX10genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PDR5_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-54; SER-58; THR-59;SER-837; SER-840; SER-849; SER-850 AND SER-854, AND MASS SPECTROMETRY.
"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-837; SER-840 ANDSER-841, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-837; SER-840 ANDSER-841, AND MASS SPECTROMETRY.
"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-49; SER-54; SER-61;SER-837; SER-840; SER-841; SER-849; SER-850 AND SER-854, AND MASSSPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-849; TYR-857 ANDSER-863, UBIQUITINATION AT LYS-825, AND MASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-61, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery.";
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-825, AND MASSSPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-849; TYR-857 ANDSER-863, UBIQUITINATION AT LYS-825, AND MASS SPECTROMETRY.

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