TPO3_YEAST - dbPTM
TPO3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPO3_YEAST
UniProt AC Q06451
Protein Name Polyamine transporter 3
Gene Name TPO3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 622
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 spermine, but not spermidine..
Protein Sequence MNRQESINSFNSDETSSLSDVESQQPQQYIPSESGSKSNMAPNQLKLTRTETVKSLQDMGVSSKAPVPDVNAPQSSKNKIFPEEYTLETPTGLVPVATLHSIGRTSTAISRTRTRQIDGASSPSSNEDALESDNNEKGKEGDSSGANDEAPDLDPEIEFVTFVTGDPENPHNWPAWIRWSYTVLLSILVICVAYGSACISGGLGTVEKKYHVGMEAAILSVSLMVIGFSLGPLIWSPVSDLYGRRVAYFVSMGLYVIFNIPCALAPNLGSLLACRFLCGVWSSSGLCLVGGSIADMFPSETRGKAIAFFAFAPYVGPVVGPLVNGFISVSTGRMDLIFWVNMAFAGVMWIISSAIPETYAPVILKRKAARLRKETGNPKIMTEQEAQGVSMGEMMRACLLRPLYFSVTEPVLVATCFYVCLIYSLLYAFFFAFPVIFGELYGYKDNLVGLMFIPIVIGALWALATTFYCENKYLQIVKQRKPTPEDRLLGAKIGAPFAAIALWILGATAYKHIIWVGPASAGLAFGFGMVLIYYSLNNYIIDCYVQYASSALATKVFLRSAGGAAFPLFTIQMYHKLNLHWGSWLLAFISTAMIALPFAFSYWGKGLRHKLSKKDYSIDSIE
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
37UbiquitinationIPSESGSKSNMAPNQ
CCCCCCCCCCCCCCC		49.7417644757
38PhosphorylationPSESGSKSNMAPNQL
CCCCCCCCCCCCCCE		33.2722369663
46UbiquitinationNMAPNQLKLTRTETV
CCCCCCEEECCHHHH		37.7423749301
48PhosphorylationAPNQLKLTRTETVKS
CCCCEEECCHHHHHH		33.6821440633
50PhosphorylationNQLKLTRTETVKSLQ
CCEEECCHHHHHHHH		30.6725005228
52PhosphorylationLKLTRTETVKSLQDM
EEECCHHHHHHHHHC		32.4011875433
54UbiquitinationLTRTETVKSLQDMGV
ECCHHHHHHHHHCCC		53.5223749301
55PhosphorylationTRTETVKSLQDMGVS
CCHHHHHHHHHCCCC		27.2522369663
62PhosphorylationSLQDMGVSSKAPVPD
HHHHCCCCCCCCCCC		22.0122890988
63PhosphorylationLQDMGVSSKAPVPDV
HHHCCCCCCCCCCCC		30.3621440633
64UbiquitinationQDMGVSSKAPVPDVN
HHCCCCCCCCCCCCC		49.5623749301
75PhosphorylationPDVNAPQSSKNKIFP
CCCCCCCHHCCCCCC		42.0728889911
76PhosphorylationDVNAPQSSKNKIFPE
CCCCCCHHCCCCCCC		34.6920377248
77UbiquitinationVNAPQSSKNKIFPEE
CCCCCHHCCCCCCCC		68.4617644757
79UbiquitinationAPQSSKNKIFPEEYT
CCCHHCCCCCCCCCC		49.8424961812
85PhosphorylationNKIFPEEYTLETPTG
CCCCCCCCCCCCCCC		18.2419779198
86PhosphorylationKIFPEEYTLETPTGL
CCCCCCCCCCCCCCC		22.7719779198
89PhosphorylationPEEYTLETPTGLVPV
CCCCCCCCCCCCEEH		29.3022890988
91PhosphorylationEYTLETPTGLVPVAT
CCCCCCCCCCEEHHH		51.0422890988
98PhosphorylationTGLVPVATLHSIGRT
CCCEEHHHHHHCCCC		25.8222369663
101PhosphorylationVPVATLHSIGRTSTA
EEHHHHHHCCCCCCC		29.8322369663
105PhosphorylationTLHSIGRTSTAISRT
HHHHCCCCCCCCCCC		25.8021440633
106PhosphorylationLHSIGRTSTAISRTR
HHHCCCCCCCCCCCC		17.9319779198
107PhosphorylationHSIGRTSTAISRTRT
HHCCCCCCCCCCCCC		27.6516445868
110PhosphorylationGRTSTAISRTRTRQI
CCCCCCCCCCCCEEC		25.7416445868
121PhosphorylationTRQIDGASSPSSNED
CEECCCCCCCCCCHH		48.5922369663
122PhosphorylationRQIDGASSPSSNEDA
EECCCCCCCCCCHHH		28.4122369663
124PhosphorylationIDGASSPSSNEDALE
CCCCCCCCCCHHHHH		47.9822369663
125PhosphorylationDGASSPSSNEDALES
CCCCCCCCCHHHHHC		47.8522369663
132PhosphorylationSNEDALESDNNEKGK
CCHHHHHCCCCCCCC		46.6322369663
137UbiquitinationLESDNNEKGKEGDSS
HHCCCCCCCCCCCCC		76.9123749301
143PhosphorylationEKGKEGDSSGANDEA
CCCCCCCCCCCCCCC		41.3428747907
379UbiquitinationRKETGNPKIMTEQEA
HHHHCCCCCCCHHHH		49.4623749301
478UbiquitinationNKYLQIVKQRKPTPE
HHHHHHHHCCCCCHH		46.1222817900
481UbiquitinationLQIVKQRKPTPEDRL
HHHHHCCCCCHHHHH		51.2323749301
620PhosphorylationKKDYSIDSIE-----
CCCCCCCCCC-----		27.2627214570
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 TPO3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPO3_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 TPO3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERD2_YEASTERD2physical
16093310
PHO88_YEASTPHO88physical
16093310
ALG1_YEASTALG1physical
16093310
MKAR_YEASTIFA38physical
16093310
ELO2_YEASTELO2physical
16093310
SHR3_YEASTSHR3physical
16093310
FET5_YEASTFET5physical
16093310
MST27_YEASTMST27physical
16093310
ERV29_YEASTERV29physical
16093310
YET1_YEASTYET1physical
16093310
ELO3_YEASTELO3physical
16093310
GSF2_YEASTGSF2physical
16093310
ERP4_YEASTERP4physical
16093310
AQY1_YEASTAQY1physical
16093310
SSB1_YEASTSSB1physical
22940862
HSP7F_YEASTSSE1physical
22940862
HSP72_YEASTSSA2physical
22940862
HSP71_YEASTSSA1physical
22940862
ENO2_YEASTENO2physical
22940862
EXO84_YEASTEXO84genetic
27708008
MCES_YEASTABD1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
SMD1_YEASTSMD1genetic
27708008
BIG1_YEASTBIG1genetic
27708008
NU192_YEASTNUP192genetic
27708008
KTHY_YEASTCDC8genetic
27708008
ROT1_YEASTROT1genetic
27708008
CAP_YEASTSRV2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPO3_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-55; THR-98 AND SER-110,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-101 AND SER-132, 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 SER-55, 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-52; SER-55; THR-107 ANDSER-110, AND MASS SPECTROMETRY.

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