TPO2_YEAST - dbPTM
TPO2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPO2_YEAST
UniProt AC P53283
Protein Name Polyamine transporter 2
Gene Name TPO2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 614
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 MSDQESVVSFNSQNTSMVDVEGQQPQQYVPSKTNSRANQLKLTKTETVKSLQDLGVTSAAPVPDINAPQTAKNNIFPEEYTMETPSGLVPVATLQSMGRTASALSRTRTKQLNRTATNSSSTGKEEMEEEETEEREDQSGENELDPEIEFVTFVTGDPENPHNWPSWVRWSYTVLLSILVICVAYGSACISGGLGTVEKKYHVGMEAAILSCSLMVIGFSLGPLIWSPVSDLYGRRVAYFVSMGLYVIFNIPCALAPNLGCLLACRFLCGVWSSSGLCLVGGSIADMFPSETRGKAIAFFAFAPYVGPVVGPLVNGFISVSTGRMDLIFWVNMAFAGVMWIISSAIPETYAPVILKRKAARLRKETGNPKIMTEQEAQGVSMSEMMRACLLRPLYFAVTEPVLVATCFYVCLIYSLLYAFFFAFPVIFGELYGYKDNLVGLMFIPIVIGALWALATTFYCENKYLQIVKQRKPTPEDRLLGAKIGAPFAAIALWILGATAYKHIIWVGPASAGLAFGFGMVLIYYSLNNYIIDCYVQYASSALATKVFLRSAGGAAFPLFTIQMYHKLNLHWGSWLLAFISTAMIALPFAFSYWGKGLRHKLSKKDYSIDSVEM
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
35PhosphorylationYVPSKTNSRANQLKL
CCCCCCCCCHHCCCC		37.6927738172
43PhosphorylationRANQLKLTKTETVKS
CHHCCCCCCCHHHHH		34.0428889911
44UbiquitinationANQLKLTKTETVKSL
HHCCCCCCCHHHHHH		55.5922817900
45PhosphorylationNQLKLTKTETVKSLQ
HCCCCCCCHHHHHHH		31.4911875433
47PhosphorylationLKLTKTETVKSLQDL
CCCCCCHHHHHHHHC		38.1711875433
49UbiquitinationLTKTETVKSLQDLGV
CCCCHHHHHHHHCCC		53.5223749301
50PhosphorylationTKTETVKSLQDLGVT
CCCHHHHHHHHCCCC		27.2517330950
57PhosphorylationSLQDLGVTSAAPVPD
HHHHCCCCCCCCCCC		15.7323749301
58PhosphorylationLQDLGVTSAAPVPDI
HHHCCCCCCCCCCCC		21.7428889911
93PhosphorylationSGLVPVATLQSMGRT
CCCEEHHHHHHCCCH		26.0921440633
96PhosphorylationVPVATLQSMGRTASA
EEHHHHHHCCCHHHH		26.7321440633
100PhosphorylationTLQSMGRTASALSRT
HHHHCCCHHHHHHHH		21.1620377248
102PhosphorylationQSMGRTASALSRTRT
HHCCCHHHHHHHHHH		29.1822369663
105PhosphorylationGRTASALSRTRTKQL
CCHHHHHHHHHHHHH		31.1822369663
107PhosphorylationTASALSRTRTKQLNR
HHHHHHHHHHHHHCC		39.0422369663
109PhosphorylationSALSRTRTKQLNRTA
HHHHHHHHHHHCCCC		23.6421440633
115PhosphorylationRTKQLNRTATNSSST
HHHHHCCCCCCCCCC		36.4423749301
117PhosphorylationKQLNRTATNSSSTGK
HHHCCCCCCCCCCCH		34.7123749301
119PhosphorylationLNRTATNSSSTGKEE
HCCCCCCCCCCCHHH		22.7028889911
120PhosphorylationNRTATNSSSTGKEEM
CCCCCCCCCCCHHHH		33.7123749301
121PhosphorylationRTATNSSSTGKEEME
CCCCCCCCCCHHHHH		40.7923749301
122PhosphorylationTATNSSSTGKEEMEE
CCCCCCCCCHHHHHH		54.9723749301
124UbiquitinationTNSSSTGKEEMEEEE
CCCCCCCHHHHHHHH		51.0623749301
132PhosphorylationEEMEEEETEEREDQS
HHHHHHHHHHHHCCC		46.5628889911
139PhosphorylationTEEREDQSGENELDP
HHHHHCCCCCCCCCC		61.4728747907
201PhosphorylationLGTVEKKYHVGMEAA
CCHHCHHHCCCHHHH		16.8930377154
211PhosphorylationGMEAAILSCSLMVIG
CHHHHHHHHHHHHHC		8.7830377154
213PhosphorylationEAAILSCSLMVIGFS
HHHHHHHHHHHHCCC		19.0030377154
220PhosphorylationSLMVIGFSLGPLIWS
HHHHHCCCCCHHCCC		27.4830377154
227PhosphorylationSLGPLIWSPVSDLYG
CCCHHCCCCHHHHHH		14.3930377154
230PhosphorylationPLIWSPVSDLYGRRV
HHCCCCHHHHHHHHH		25.8630377154
370UbiquitinationRKETGNPKIMTEQEA
HHHHCCCCCCCHHHH		49.4623749301
381PhosphorylationEQEAQGVSMSEMMRA
HHHHCCCCHHHHHHH		24.3429650682
383PhosphorylationEAQGVSMSEMMRACL
HHCCCCHHHHHHHHH		18.1629650682
469UbiquitinationNKYLQIVKQRKPTPE
HHHHHHHHCCCCCHH		46.1222817900
472UbiquitinationLQIVKQRKPTPEDRL
HHHHHCCCCCHHHHH		51.2323749301
605UbiquitinationLRHKLSKKDYSIDSV
HHHHHCCCCCCCCCC		59.5323749301
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 TPO2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPO2_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 TPO2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MID2_YEASTMID2physical
18467557
HXT5_YEASTHXT5physical
18467557
HXT1_YEASTHXT1physical
18467557
PDR12_YEASTPDR12physical
18467557
YL413_YEASTINA1physical
18467557
TCB3_YEASTTCB3physical
18467557
SLM1_YEASTSLM1physical
18467557
TPO3_YEASTTPO3physical
18467557
TPO1_YEASTTPO1physical
18467557
SFK1_YEASTSFK1physical
18467557
PDR5_YEASTPDR5physical
18467557
EMP24_YEASTEMP24physical
16093310
FCY22_YEASTFCY22genetic
18192430
ATP11_YEASTATP11genetic
18192430
RXT2_YEASTRXT2genetic
18192430
CGR1_YEASTCGR1genetic
18192430
PP11_YEASTSIT4genetic
18192430
PP4R2_YEASTPSY4genetic
18192430
SWI6_YEASTSWI6genetic
27708008
LCF1_YEASTFAA1genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
CSG2_YEASTCSG2genetic
27708008
VPS41_YEASTVPS41genetic
27708008
MAC1_YEASTMAC1genetic
27708008
MKS1_YEASTMKS1genetic
27708008
CTU2_YEASTNCS2genetic
27708008
LGE1_YEASTLGE1genetic
27708008
SUR1_YEASTSUR1genetic
27708008
ELP3_YEASTELP3genetic
27708008
NAA30_YEASTMAK3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPO2_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-50 AND SER-96, AND MASSSPECTROMETRY.
"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-50, 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-45; THR-47; SER-102 ANDSER-105, AND MASS SPECTROMETRY.

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