TPO1_YEAST - dbPTM
TPO1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPO1_YEAST
UniProt AC Q07824
Protein Name Polyamine transporter 1
Gene Name TPO1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 586
Subcellular Localization Cell membrane
Multi-pass membrane protein . Enriched on the cell membrane of growing buds.
Protein Description Cell membrane polyamine/proton antiporter, involved in the detoxification of excess polyamines in the cytoplasm. Catalyzes polyamine uptake at alkaline pH and excretion at acidic pH. Recognizes spermidine, spermine and putrescine, the polyamine analogs methylglyoxal bis(guanylhydrazone) (MGBG) and paraquat, the antimalarial drug quinidine, and cycloheximide. Confers resistance to the non-steroidal anti-inflammatory drug indomethacin..
Protein Sequence MSDHSPISNKENHLLPSDSSRSSSSDMHSTGTTGTTGVEPVDFTGEGAKYTTATEGNGGADLAIQRTTTMNSAAESEVNITRRLTKILTGSVNEPDRVEVDYTNCAPMGGDRPYPPSLPSRDLYEVTFDGPNDPLHPFNWPMKKKVLLCLVLCLDSIAIAMCSSIFASAVPQICEIYHVIEVVAILGITLFVLGFAASPVIYAPLSELYGRKGVLVLSAFGFALFQFAVATAENLQTIFICRFFGGFIGAAPMAVVPAAFADMFDTNVRGKAIALFSLGVFVGPILSPVMGSYIAQRTTWRWLEYVVGCFASAVFVAIVLFFEETHHPTILVNKAKQMRKQSNNWGIHAAHEDVELSIKDIVQKTVTRPIIMLFVEPLLLFVTIYNSFVYGILYLLLEAYPLVFVEGYGFTENGELPYIALIIGMMVCAAFIWYMDNDYLKRCRAKGKLVPEARLYAMVIAGTVFPIGILWFCWTGYYPHKIHWMVPTVGGAFIGFGLMGIFLPCLNYIIESYLLLAASAVAANTFMRSAFGACFPLFAGYMFRGMGIGWAGLLLGLFAAAMIPVPLLFLKYGESIRKKSKYAYAA
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
2Phosphorylation------MSDHSPISN
------CCCCCCCCC		43.9928889911
5Phosphorylation---MSDHSPISNKEN
---CCCCCCCCCCCC		28.9930377154
8PhosphorylationMSDHSPISNKENHLL
CCCCCCCCCCCCCCC		45.2827717283
17PhosphorylationKENHLLPSDSSRSSS
CCCCCCCCCCCCCCC		50.5220377248
19PhosphorylationNHLLPSDSSRSSSSD
CCCCCCCCCCCCCCC		31.8020377248
20PhosphorylationHLLPSDSSRSSSSDM
CCCCCCCCCCCCCCC		40.9729688323
25PhosphorylationDSSRSSSSDMHSTGT
CCCCCCCCCCCCCCC		40.6823749301
29PhosphorylationSSSSDMHSTGTTGTT
CCCCCCCCCCCCCCC		23.1520377248
30PhosphorylationSSSDMHSTGTTGTTG
CCCCCCCCCCCCCCC		24.7020377248
32PhosphorylationSDMHSTGTTGTTGVE
CCCCCCCCCCCCCCC		23.3423749301
35PhosphorylationHSTGTTGTTGVEPVD
CCCCCCCCCCCCCCC		20.4823749301
49UbiquitinationDFTGEGAKYTTATEG
CCCCCCCEEEECCCC		54.7217644757
51PhosphorylationTGEGAKYTTATEGNG
CCCCCEEEECCCCCC		14.8428889911
52PhosphorylationGEGAKYTTATEGNGG
CCCCEEEECCCCCCC		28.6125752575
54PhosphorylationGAKYTTATEGNGGAD
CCEEEECCCCCCCCC		42.1919779198
67PhosphorylationADLAIQRTTTMNSAA
CCEEEEEECCCCHHH		15.3922890988
68PhosphorylationDLAIQRTTTMNSAAE
CEEEEEECCCCHHHH		26.6622369663
69PhosphorylationLAIQRTTTMNSAAES
EEEEEECCCCHHHHH		17.4722369663
72PhosphorylationQRTTTMNSAAESEVN
EEECCCCHHHHHHHH		20.3122369663
76PhosphorylationTMNSAAESEVNITRR
CCCHHHHHHHHHHHH		41.9622369663
81PhosphorylationAESEVNITRRLTKIL
HHHHHHHHHHHHHHH		12.4421440633
85PhosphorylationVNITRRLTKILTGSV
HHHHHHHHHHHHCCC		17.7724961812
89PhosphorylationRRLTKILTGSVNEPD
HHHHHHHHCCCCCCC		30.7717330950
91PhosphorylationLTKILTGSVNEPDRV
HHHHHHCCCCCCCCE		19.2817330950
102PhosphorylationPDRVEVDYTNCAPMG
CCCEEECCCCCCCCC		12.6719779198
103PhosphorylationDRVEVDYTNCAPMGG
CCEEECCCCCCCCCC		21.2519779198
114PhosphorylationPMGGDRPYPPSLPSR
CCCCCCCCCCCCCCC		28.7719779198
117PhosphorylationGDRPYPPSLPSRDLY
CCCCCCCCCCCCCEE		48.7019779198
342PhosphorylationAKQMRKQSNNWGIHA
HHHHHHHCCCCCCCC		34.8628889911
357PhosphorylationAHEDVELSIKDIVQK
CHHCCEECHHHHHHH		17.6828889911
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
19SPhosphorylationKinasePKC-FAMILY-GPS
19SPhosphorylationKinasePKC-Uniprot
52TPhosphorylationKinaseCK1-FAMILY-GPS
52TPhosphorylationKinaseCK1-Uniprot
342SPhosphorylationKinasePKA-FAMILY-GPS
342SPhosphorylationKinasePKA-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPO1_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 TPO1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUP2_YEASTCUP2physical
10688190
YCT1_YEASTYCT1genetic
16269340
PFD2_YEASTGIM4genetic
16269340
MTC4_YEASTMTC4genetic
16269340
ORM2_YEASTORM2genetic
16269340
UBX2_YEASTUBX2genetic
16269340
SWA2_YEASTSWA2genetic
16269340
PLMT_YEASTOPI3genetic
16269340
PDR5_YEASTPDR5physical
18467557
MSC3_YEASTMSC3physical
18467557
YL326_YEASTYLR326Wphysical
18467557
PDR12_YEASTPDR12physical
18467557
YL413_YEASTINA1physical
18467557
TCB3_YEASTTCB3physical
18467557
TPO3_YEASTTPO3physical
18467557
DIP5_YEASTDIP5physical
18467557
TCB2_YEASTTCB2physical
18467557
MEP3_YEASTMEP3physical
18467557
MID2_YEASTMID2physical
18467557
RSA3_YEASTRSA3physical
18467557
TPO1_YEASTTPO1physical
18467557
LDS1_YEASTLDS1physical
16093310
PRM9_YEASTPRM9physical
16093310
MST28_YEASTMST28physical
16093310
PHO88_YEASTPHO88physical
16093310
ALG1_YEASTALG1physical
16093310
MKAR_YEASTIFA38physical
16093310
PHO89_YEASTPHO89physical
16093310
ELO2_YEASTELO2physical
16093310
SHR3_YEASTSHR3physical
16093310
OST4_YEASTOST4physical
16093310
SUR2_YEASTSUR2physical
16093310
ITR1_YEASTITR1physical
16093310
OSTB_YEASTWBP1physical
16093310
VATL1_YEASTVMA3physical
16093310
FET5_YEASTFET5physical
16093310
MST27_YEASTMST27physical
16093310
MSMO_YEASTERG25physical
16093310
CBP4_YEASTCBP4physical
16093310
VATO_YEASTVMA16physical
16093310
YHU0_YEASTYHR140Wphysical
16093310
GPI16_YEASTGPI16physical
16093310
SNL1_YEASTSNL1physical
16093310
YET1_YEASTYET1physical
16093310
POM34_YEASTPOM34physical
16093310
ERG3_YEASTERG3physical
16093310
ELO3_YEASTELO3physical
16093310
GSF2_YEASTGSF2physical
16093310
OSTD_YEASTSWP1physical
16093310
GAS3_YEASTGAS3physical
16093310
CUE1_YEASTCUE1physical
16093310
YTP1_YEASTYTP1physical
16093310
ERP4_YEASTERP4physical
16093310
SEC63_YEASTSEC63physical
16093310
VATL2_YEASTVMA11physical
16093310
PDR5_YEASTPDR5physical
22615397
SHG1_YEASTSHG1genetic
27708008
SNF5_YEASTSNF5genetic
27708008
GPR1_YEASTGPR1genetic
27708008
CYK3_YEASTCYK3genetic
27708008
VPS41_YEASTVPS41genetic
27708008
SDC1_YEASTSDC1genetic
27708008
IES1_YEASTIES1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
INM1_YEASTINM1genetic
27708008
VPS53_YEASTVPS53genetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
PET8_YEASTPET8genetic
27708008
RU2A_YEASTLEA1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPO1_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-72, 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-72; SER-76; THR-89 ANDSER-91, 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-72 AND SER-76, AND MASSSPECTROMETRY.

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