TPO4_YEAST - dbPTM
TPO4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPO4_YEAST
UniProt AC Q12256
Protein Name Polyamine transporter 4
Gene Name TPO4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 659
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Cell membrane polyamine/proton antiporter, involved in the detoxification of excess polyamines in the cytoplasm. Recognizes spermidine, spermine and the antimalarial drug quinidine, but not quinine, chloroquine and mefloquine..
Protein Sequence MPSSLTKTESNSDPRTNIQQVPKALDKNVTNSGNLDSTSSSTGSITEDEKRSEPNADSNNMTGGEPIDPRDLDWDGPDDPDNPHNWSSLKKWYTTMTSAFLCLVVTMGSSLYVSSVPELVERYHVSQTLALAGLTFYLLGLSTVIGAPLSEVFGRKPVYLFSLPVSMLFTMGVGLSNGHMRIILPLRFLSGVFASPALSVGSGTILDIFDVDQVSVAMTYFVLSPFLGPVLSPIMAGFATEAKGWRWSEWIQLIAGGLILPFIALMPETHKGIILRKRAKKRNIALKKFSREAQKEFLKTTVTITILRPLKMLVVEPIVFVFSVYVAFIFAILFGFFEAYAVIYRGVYHMSMGISGLPFIGIGVGLWIGAFFYLYIDRKYLFPKPPAGTQPLTEKERTSKRTTPYRGARDAETGELLPVVPEKFLIACKFGSVALPIGLFWQAWTARSDVHWMAPVAAGVPFGFGLILIFFSVLMYFSTCYPPLTVASCLAANNLLRYVMSSVFPLFTIQMYTKMKIKWASTLFALVCVVMIPIPWVFEKWGSKLRHKSQFGYAAMEKEAETEGGIDDVNAVDGELNLTRMTTLRTMETDPSTREKPGERLSLRRTHTQPVPASFDREDGQHAQNRNEPISNSLYSAIKDNEDGYSYTEMATDASARMV
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
3Phosphorylation-----MPSSLTKTES
-----CCCCCCCCCC		36.3622369663
4Phosphorylation----MPSSLTKTESN
----CCCCCCCCCCC		33.9022369663
6Phosphorylation--MPSSLTKTESNSD
--CCCCCCCCCCCCC		37.5622369663
8PhosphorylationMPSSLTKTESNSDPR
CCCCCCCCCCCCCCC		39.1422369663
10PhosphorylationSSLTKTESNSDPRTN
CCCCCCCCCCCCCCC		47.0322369663
12PhosphorylationLTKTESNSDPRTNIQ
CCCCCCCCCCCCCHH		59.2722369663
16PhosphorylationESNSDPRTNIQQVPK
CCCCCCCCCHHHHCH		41.9022369663
23UbiquitinationTNIQQVPKALDKNVT
CCHHHHCHHHCCCCC		63.8323749301
27UbiquitinationQVPKALDKNVTNSGN
HHCHHHCCCCCCCCC		54.9217644757
30PhosphorylationKALDKNVTNSGNLDS
HHHCCCCCCCCCCCC		32.8222369663
32PhosphorylationLDKNVTNSGNLDSTS
HCCCCCCCCCCCCCC		21.4922369663
37PhosphorylationTNSGNLDSTSSSTGS
CCCCCCCCCCCCCCC		33.1022369663
38PhosphorylationNSGNLDSTSSSTGSI
CCCCCCCCCCCCCCC		32.0922369663
39PhosphorylationSGNLDSTSSSTGSIT
CCCCCCCCCCCCCCC		26.6622369663
40PhosphorylationGNLDSTSSSTGSITE
CCCCCCCCCCCCCCC		31.8220377248
41PhosphorylationNLDSTSSSTGSITED
CCCCCCCCCCCCCCC		36.2320377248
42PhosphorylationLDSTSSSTGSITEDE
CCCCCCCCCCCCCCC		36.5823749301
44PhosphorylationSTSSSTGSITEDEKR
CCCCCCCCCCCCCCC		26.8222369663
46PhosphorylationSSSTGSITEDEKRSE
CCCCCCCCCCCCCCC		38.8022369663
50UbiquitinationGSITEDEKRSEPNAD
CCCCCCCCCCCCCCC		73.8123749301
52PhosphorylationITEDEKRSEPNADSN
CCCCCCCCCCCCCCC		69.3522369663
58PhosphorylationRSEPNADSNNMTGGE
CCCCCCCCCCCCCCC		27.9122369663
62PhosphorylationNADSNNMTGGEPIDP
CCCCCCCCCCCCCCH		44.1322369663
300PhosphorylationAQKEFLKTTVTITIL
HHHHHHHHCHHHCCC		28.7528889911
305PhosphorylationLKTTVTITILRPLKM
HHHCHHHCCCCCHHH		12.4728889911
549PhosphorylationGSKLRHKSQFGYAAM
CCHHHHHHHHCHHHH		25.3125704821
558UbiquitinationFGYAAMEKEAETEGG
HCHHHHHHHHHHCCC		49.4917644757
562PhosphorylationAMEKEAETEGGIDDV
HHHHHHHHCCCCCCH		47.1528152593
579PhosphorylationVDGELNLTRMTTLRT
CCCCEEEEEEEEEEE		19.8128889911
582PhosphorylationELNLTRMTTLRTMET
CEEEEEEEEEEEECC		21.2722369663
583PhosphorylationLNLTRMTTLRTMETD
EEEEEEEEEEEECCC		12.6122369663
586PhosphorylationTRMTTLRTMETDPST
EEEEEEEEECCCCCC		23.5922369663
589PhosphorylationTTLRTMETDPSTREK
EEEEEECCCCCCCCC		42.2522369663
592PhosphorylationRTMETDPSTREKPGE
EEECCCCCCCCCCCC		42.7922369663
593PhosphorylationTMETDPSTREKPGER
EECCCCCCCCCCCCC		48.5122369663
596UbiquitinationTDPSTREKPGERLSL
CCCCCCCCCCCCCCC		55.8423749301
602PhosphorylationEKPGERLSLRRTHTQ
CCCCCCCCCCCCCCC		26.5028889911
606PhosphorylationERLSLRRTHTQPVPA
CCCCCCCCCCCCCCC		23.8817330950
608PhosphorylationLSLRRTHTQPVPASF
CCCCCCCCCCCCCCC		33.6717330950
614PhosphorylationHTQPVPASFDREDGQ
CCCCCCCCCCCCCCC		22.9322369663
631PhosphorylationQNRNEPISNSLYSAI
CCCCCCCCHHHHHHH		30.9522890988
633PhosphorylationRNEPISNSLYSAIKD
CCCCCCHHHHHHHHC		23.1522890988
635PhosphorylationEPISNSLYSAIKDNE
CCCCHHHHHHHHCCC		8.9022890988
636PhosphorylationPISNSLYSAIKDNED
CCCHHHHHHHHCCCC		28.8922890988
639UbiquitinationNSLYSAIKDNEDGYS
HHHHHHHHCCCCCCC		54.9723749301
645PhosphorylationIKDNEDGYSYTEMAT
HHCCCCCCCHHHCCC		15.7222369663
646PhosphorylationKDNEDGYSYTEMATD
HCCCCCCCHHHCCCC		30.9822369663
647PhosphorylationDNEDGYSYTEMATDA
CCCCCCCHHHCCCCC		9.7620377248
648PhosphorylationNEDGYSYTEMATDAS
CCCCCCHHHCCCCCC		17.2222369663
652PhosphorylationYSYTEMATDASARMV
CCHHHCCCCCCCCCC		30.6822369663
655PhosphorylationTEMATDASARMV---
HHCCCCCCCCCC---		21.1522369663
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 TPO4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPO4_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 TPO4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FLC1_YEASTFLC1physical
18467557
LSP1_YEASTLSP1physical
18467557
PDR12_YEASTPDR12physical
18467557
GIP4_YEASTGIP4genetic
20093466
VPS8_YEASTVPS8genetic
20093466
CSG2_YEASTCSG2genetic
20093466
MBA1_YEASTMBA1genetic
20093466
BEM1_YEASTBEM1genetic
20093466
FUB1_YEASTFUB1genetic
20093466
BRE1_YEASTBRE1genetic
20093466
MTU1_YEASTSLM3genetic
20093466
TPA1_YEASTTPA1genetic
20093466
RIM15_YEASTRIM15genetic
20093466
YGY5_YEASTYGL235Wgenetic
20093466
MHP1_YEASTMHP1genetic
20093466
FOLC_YEASTRMA1genetic
20093466
MSS1_YEASTMSS1genetic
20093466
ATP23_YEASTATP23genetic
20093466
MDL2_YEASTMDL2genetic
20093466
NIP80_YEASTNIP100genetic
20093466
COX10_YEASTCOX10genetic
20093466
UBA3_YEASTUBA3genetic
20093466
QCR2_YEASTQCR2genetic
20093466
HSP71_YEASTSSA1physical
22940862
RIM15_YEASTRIM15genetic
22282571
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPO4_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 THR-589 AND SER-646, ANDMASS 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-10, AND MASSSPECTROMETRY.
"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 THR-589 AND SER-592, ANDMASS 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-606 AND THR-608, ANDMASS SPECTROMETRY.

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