PDR12_YEAST - dbPTM
PDR12_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDR12_YEAST
UniProt AC Q02785
Protein Name ATP-dependent permease PDR12
Gene Name PDR12
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1511
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Plasma membrane transporter which mediates resistance to water-soluble, monocarboxylic acids with chain lengths of from C1 to C7 by active extrusion of the preservative anions from the cytosol. Also involved in the export of aromatic and branched-chain organic acids produced in amino acid catabolism..
Protein Sequence MSSTDEHIEKDISSRSNHDDDYANSVQSYAASEGQVDNEDLAATSQLSRHLSNILSNEEGIERLESMARVISHKTKKEMDSFEINDLDFDLRSLLHYLRSRQLEQGIEPGDSGIAFKNLTAVGVDASAAYGPSVEEMFRNIASIPAHLISKFTKKSDVPLRNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGETSELVDVQGEFSYDGLDQSEMMSKYKGYVIYCPELDFHFPKITVKETIDFALKCKTPRVRIDKMTRKQYVDNIRDMWCTVFGLRHTYATKVGNDFVRGVSGGERKRVSLVEAQAMNASIYSWDNATRGLDASTALEFAQAIRTATNMVNNSAIVAIYQAGENIYELFDKTTVLYNGRQIYFGPADKAVGYFQRMGWVKPNRMTSAEFLTSVTVDFENRTLDIKPGYEDKVPKSSSEFEEYWLNSEDYQELLRTYDDYQSRHPVNETRDRLDVAKKQRLQQGQRENSQYVVNYWTQVYYCMIRGFQRVKGDSTYTKVYLSSFLIKALIIGSMFHKIDDKSQSTTAGAYSRGGMLFYVLLFASVTSLAEIGNSFSSRPVIVKHKSYSMYHLSAESLQEIITEFPTKFVAIVILCLITYWIPFMKYEAGAFFQYILYLLTVQQCTSFIFKFVATMSKSGVDAHAVGGLWVLMLCVYAGFVLPIGEMHHWIRWLHFINPLTYAFESLVSTEFHHREMLCSALVPSGPGYEGISIANQVCDAAGAVKGNLYVSGDSYILHQYHFAYKHAWRNWGVNIVWTFGYIVFNVILSEYLKPVEGGGDLLLYKRGHMPELGTENADARTASREEMMEALNGPNVDLEKVIAEKDVFTWNHLDYTIPYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINMGVITGDMLVNAKPLPASFNRSCGYVAQADNHMAELSVRESLRFAAELRQQSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLFLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSATLFEQFDRLLLLKKGGKMVYFGDIGPNSETLLKYFERQSGMKCGVSENPAEYILNCIGAGATASVNSDWHDLWLASPECAAARAEVEELHRTLPGRAVNDDPELATRFAASYMTQIKCVLRRTALQFWRSPVYIRAKFFECVACALFVGLSYVGVNHSVGGAIEAFSSIFMLLLIALAMINQLHVFAYDSRELYEVREAASNTFHWSVLLLCHAAVENFWSTLCQFMCFICYYWPAQFSGRASHAGFFFFFYVLIFPLYFVTYGLWILYMSPDVPSASMINSNLFAAMLLFCGILQPREKMPAFWRRLMYNVSPFTYVVQALVTPLVHNKKVVCNPHEYNIMDPPSGKTCGEFLSTYMDNNTGYLVNPTATENCQYCPYTVQDQVVAKYNVKWDHRWRNFGFMWAYICFNIAAMLICYYVVRVKVWSLKSVLNFKKWFNGPRKERHEKDTNIFQTVPGDENKITKK
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
2Acetylation------MSSTDEHIE
------CCCHHHHHH		53.9322814378
2Phosphorylation------MSSTDEHIE
------CCCHHHHHH		53.9322369663
3Phosphorylation-----MSSTDEHIEK
-----CCCHHHHHHH		52.3022369663
4Phosphorylation----MSSTDEHIEKD
----CCCHHHHHHHH		55.4822369663
10AcetylationSTDEHIEKDISSRSN
CHHHHHHHHHHHCCC		60.8124489116
16PhosphorylationEKDISSRSNHDDDYA
HHHHHHCCCCCHHHH		40.2322369663
22PhosphorylationRSNHDDDYANSVQSY
CCCCCHHHHHHHHHH		18.0622369663
25PhosphorylationHDDDYANSVQSYAAS
CCHHHHHHHHHHHHH		17.2322369663
28PhosphorylationDYANSVQSYAASEGQ
HHHHHHHHHHHHCCC		18.0022369663
29PhosphorylationYANSVQSYAASEGQV
HHHHHHHHHHHCCCC		6.7922369663
32PhosphorylationSVQSYAASEGQVDNE
HHHHHHHHCCCCCHH		33.8022369663
44PhosphorylationDNEDLAATSQLSRHL
CHHHHHHHHHHHHHH		16.0522369663
45PhosphorylationNEDLAATSQLSRHLS
HHHHHHHHHHHHHHH		25.1322369663
48PhosphorylationLAATSQLSRHLSNIL
HHHHHHHHHHHHHHH		15.2622369663
52PhosphorylationSQLSRHLSNILSNEE
HHHHHHHHHHHCCHH		18.7222369663
56PhosphorylationRHLSNILSNEEGIER
HHHHHHHCCHHHHHH		38.1022369663
66PhosphorylationEGIERLESMARVISH
HHHHHHHHHHHHHHH		23.4922369663
81PhosphorylationKTKKEMDSFEINDLD
CCHHHCCCCCCCCCC		24.3822369663
93PhosphorylationDLDFDLRSLLHYLRS
CCCHHHHHHHHHHHH		42.4524603354
97PhosphorylationDLRSLLHYLRSRQLE
HHHHHHHHHHHHHHH		12.0926447709
117UbiquitinationGDSGIAFKNLTAVGV
CCCCEEEECCEEEEC		41.8617644757
151AcetylationIPAHLISKFTKKSDV
HCHHHHHHHCCCCCC		50.4924489116
151UbiquitinationIPAHLISKFTKKSDV
HCHHHHHHHCCCCCC		50.4917644757
195PhosphorylationSTFLKCLSGETSELV
HHHHHHHCCCCCEEE		44.0127017623
210PhosphorylationDVQGEFSYDGLDQSE
ECCCCCCCCCCCHHH		21.2527017623
297PhosphorylationNDFVRGVSGGERKRV
CCHHCCCCCCCCCCE		43.8628889911
420UbiquitinationENRTLDIKPGYEDKV
CCCEEECCCCCCCCC		31.8623749301
426UbiquitinationIKPGYEDKVPKSSSE
CCCCCCCCCCCCCHH		48.7923749301
516PhosphorylationTYTKVYLSSFLIKAL
CCCHHHHHHHHHHHH		11.0128152593
834UbiquitinationGPNVDLEKVIAEKDV
CCCCCHHHHHCCCCC		46.3623749301
859UbiquitinationPYDGATRKLLSDVFG
CCCHHHHHHHHHHHC		49.8017644757
869UbiquitinationSDVFGYVKPGKMTAL
HHHHCCCCCCCEEEE		39.3017644757
872UbiquitinationFGYVKPGKMTALMGE
HCCCCCCCEEEEECC		41.4217644757
884UbiquitinationMGESGAGKTTLLNVL
ECCCCCCHHHHHHHH		37.4917644757
961UbiquitinationEKYEYVEKIITLLGM
HHHHHHHHHHHHHCC		29.3917644757
978UbiquitinationYAEALVGKTGRGLNV
HHHHHHCCCCCCCCH		40.0817644757
1405N-linked_GlycosylationFLSTYMDNNTGYLVN
HHHHHCCCCCCEEEC		31.28-
1493AcetylationPRKERHEKDTNIFQT
CCCHHCCCCCCCCCC		64.8224489116
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 PDR12_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDR12_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 PDR12_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DIP5_YEASTDIP5physical
18467557
MEP3_YEASTMEP3physical
18467557
SSBP1_YEASTSBP1genetic
20093466
YUR1_YEASTYUR1genetic
20093466
SSH4_YEASTSSH4genetic
20093466
UBI4P_YEASTUBI4genetic
20093466
SSO2_YEASTSSO2genetic
20093466
CIK1_YEASTCIK1genetic
20093466
BRE5_YEASTBRE5genetic
20093466
YO036_YEASTYOL036Wgenetic
20093466
TPO1_YEASTTPO1genetic
20851956
SLT2_YEASTSLT2genetic
20526336
YDC1_YEASTYDC1genetic
20526336
SCS7_YEASTSCS7genetic
20526336
HSP71_YEASTSSA1physical
22940862
ILV5_YEASTILV5physical
22940862
HSP72_YEASTSSA2physical
22940862
SSB1_YEASTSSB1physical
22940862
YBQ6_YEASTYBR056Wphysical
23831759
GST1_YEASTGTT1physical
23831759
PDR5_YEASTPDR5physical
23831759
COS8_YEASTCOS8physical
23831759
PDR10_YEASTPDR10physical
23831759
PDR11_YEASTPDR11physical
23831759
TMA7_YEASTTMA7physical
23831759
TBB_YEASTTUB2physical
23831759
CMR1_YEASTCMR1physical
23831759
POM33_YEASTPOM33physical
23831759
VAM7_YEASTVAM7genetic
27708008
YJ24_YEASTKCH1genetic
27708008
GPR1_YEASTGPR1genetic
27708008
TPS2_YEASTTPS2genetic
27708008
RV167_YEASTRVS167genetic
27708008
UBP3_YEASTUBP3genetic
27708008
ASK10_YEASTASK10genetic
27708008
SSBP1_YEASTSBP1genetic
27708008
BZZ1_YEASTBZZ1genetic
27708008
DAL81_YEASTDAL81genetic
27708008
YET1_YEASTYET1genetic
27708008
EF1G2_YEASTTEF4genetic
27708008
SSH4_YEASTSSH4genetic
27708008
SSO2_YEASTSSO2genetic
27708008
VHS3_YEASTVHS3genetic
27708008
VPS17_YEASTVPS17genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PDR12_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-32; SER-52 AND SER-56,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-52, 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 SER-52 AND SER-56, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-56, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"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: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-426, AND MASSSPECTROMETRY.

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