Basic Information
Name | ATP-dependent permease PDR15 |
Uniprot ID | Q04182 |
Systematic gene name | YDR406W |
Standard gene name | PDR15 |
Gene names | PDR15 YDR406W D9509.24 |
Description from SGD | YDR406W PDR15 SGDID:S000002814, Chr IV from 1279210-1283799, Genome Release 64-3-1, Verified ORF, "Plasma membrane ATP binding cassette (ABC) transporter; multidrug transporter and general stress response factor implicated in cellular detoxification; regulated by Pdr1p, Pdr3p and Pdr8p; promoter contains a PDR responsive element; PDR15 has a paralog, PDR5, that arose from the whole genome duplication" |
Protein length | 1529 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MSSDIRDVEE RNSRSSSSSS SSNSAAQSIG QHPYRGFDSE AAERVHELAR
TLTSQSLLYT ANSNNSSSSN HNAHNADSRS VFSTDMEGVN PVFTNPDTPG
YNPKLDPNSD QFSSTAWVQN MANICTSDPD FYKPYSLGCV WKNLSASGDS
ADVSYQSTFA NIVPKLLTKG LRLLKPSKEE DTFQILKPMD GCLNPGELLV
VLGRPGSGCT TLLKSISSNS HGFKIAKDSI VSYNGLSSSD IRKHYRGEVV
YNAESDIHLP HLTVYQTLFT VARMKTPQNR IKGVDREAYA NHVTEVAMAT
YGLSHTRDTK VGNDLVRGVS GGERKRVSIA EVAICGARFQ CWDNATRGLD
SATALEFIRA LKTQADIGKT AATVAIYQCS QDAYDLFDKV CVLDDGYQLY
FGPAKDAKKY FQDMGYYCPP RQTTADFLTS ITSPTERIIS KEFIEKGTRV
PQTPKDMAEY WLQSESYKNL IKDIDSTLEK NTDEARNIIR DAHHAKQAKR
APPSSPYVVN YGMQVKYLLI RNFWRMKQSA SVTLWQVIGN SVMAFILGSM
FYKVMKKNDT STFYFRGAAM FFAILFNAFS CLLEIFSLYE TRPITEKHRT
YSLYHPSADA FASVLSEMPP KLITAVCFNI IFYFLVDFRR NGGVFFFYFL
INVIATFTLS HLFRCVGSLT KTLQEAMVPA SMLLLAISMY TGFAIPKTKI
LGWSIWIWYI NPLAYLFESL MINEFHDRRF PCAQYIPAGP AYQNITGTQR
VCSAVGAYPG NDYVLGDDFL KESYDYEHKH KWRGFGIGMA YVVFFFFVYL
ILCEYNEGAK QKGEMVVFLR SKIKQLKKEG KLQEKHRPGD IENNAGSSPD
SATTEKKILD DSSEGSDSSS DNAGLGLSKS EAIFHWRDLC YDVPIKGGQR
RILNNVDGWV KPGTLTALMG ASGAGKTTLL DCLAERVTMG VITGNIFVDG
RLRDESFPRS IGYCQQQDLH LKTATVRESL RFSAYLRQPS SVSIEEKNRY
VEEVIKILEM QQYSDAVVGV AGEGLNVEQR KRLTIGVELA ARPKLLVFLD
EPTSGLDSQT AWDTCQLMRK LATHGQAILC TIHQPSAILM QQFDRLLFLQ
KGGQTVYFGD LGEGCKTMID YFESKGAHKC PPDANPAEWM LEVVGAAPGS
HATQDYNEVW RNSDEYKAVQ EELDWMEKNL PGRSKEPTAE EHKPFAASLY
YQFKMVTIRL FQQYWRSPDY LWSKFILTIF NQVFIGFTFF KADRSLQGLQ
NQMLSIFMYT VIFNPILQQY LPSFVQQRDL YEARERPSRT FSWLAFFLSQ
IIVEIPWNIL AGTIAYCIYY YAVGFYANAS AAGQLHERGA LFWLFSIAFY
VYIGSMGLLM ISFNEVAETA AHMGTLLFTM ALSFCGVMAT PKVMPRFWIF
MYRVSPLTYM IDALLALGVA NVDVKCSNYE MVKFTPPSGT TCGDYMASYI
KLAGTGYLSD PSATDICSFC AVSTTNAFLA TFSSHYYRRW RNYGIFICYI
AFDYIAATFL YWLSRVPKKN GKISEKPKK
TLTSQSLLYT ANSNNSSSSN HNAHNADSRS VFSTDMEGVN PVFTNPDTPG
YNPKLDPNSD QFSSTAWVQN MANICTSDPD FYKPYSLGCV WKNLSASGDS
ADVSYQSTFA NIVPKLLTKG LRLLKPSKEE DTFQILKPMD GCLNPGELLV
VLGRPGSGCT TLLKSISSNS HGFKIAKDSI VSYNGLSSSD IRKHYRGEVV
YNAESDIHLP HLTVYQTLFT VARMKTPQNR IKGVDREAYA NHVTEVAMAT
YGLSHTRDTK VGNDLVRGVS GGERKRVSIA EVAICGARFQ CWDNATRGLD
SATALEFIRA LKTQADIGKT AATVAIYQCS QDAYDLFDKV CVLDDGYQLY
FGPAKDAKKY FQDMGYYCPP RQTTADFLTS ITSPTERIIS KEFIEKGTRV
PQTPKDMAEY WLQSESYKNL IKDIDSTLEK NTDEARNIIR DAHHAKQAKR
APPSSPYVVN YGMQVKYLLI RNFWRMKQSA SVTLWQVIGN SVMAFILGSM
FYKVMKKNDT STFYFRGAAM FFAILFNAFS CLLEIFSLYE TRPITEKHRT
YSLYHPSADA FASVLSEMPP KLITAVCFNI IFYFLVDFRR NGGVFFFYFL
INVIATFTLS HLFRCVGSLT KTLQEAMVPA SMLLLAISMY TGFAIPKTKI
LGWSIWIWYI NPLAYLFESL MINEFHDRRF PCAQYIPAGP AYQNITGTQR
VCSAVGAYPG NDYVLGDDFL KESYDYEHKH KWRGFGIGMA YVVFFFFVYL
ILCEYNEGAK QKGEMVVFLR SKIKQLKKEG KLQEKHRPGD IENNAGSSPD
SATTEKKILD DSSEGSDSSS DNAGLGLSKS EAIFHWRDLC YDVPIKGGQR
RILNNVDGWV KPGTLTALMG ASGAGKTTLL DCLAERVTMG VITGNIFVDG
RLRDESFPRS IGYCQQQDLH LKTATVRESL RFSAYLRQPS SVSIEEKNRY
VEEVIKILEM QQYSDAVVGV AGEGLNVEQR KRLTIGVELA ARPKLLVFLD
EPTSGLDSQT AWDTCQLMRK LATHGQAILC TIHQPSAILM QQFDRLLFLQ
KGGQTVYFGD LGEGCKTMID YFESKGAHKC PPDANPAEWM LEVVGAAPGS
HATQDYNEVW RNSDEYKAVQ EELDWMEKNL PGRSKEPTAE EHKPFAASLY
YQFKMVTIRL FQQYWRSPDY LWSKFILTIF NQVFIGFTFF KADRSLQGLQ
NQMLSIFMYT VIFNPILQQY LPSFVQQRDL YEARERPSRT FSWLAFFLSQ
IIVEIPWNIL AGTIAYCIYY YAVGFYANAS AAGQLHERGA LFWLFSIAFY
VYIGSMGLLM ISFNEVAETA AHMGTLLFTM ALSFCGVMAT PKVMPRFWIF
MYRVSPLTYM IDALLALGVA NVDVKCSNYE MVKFTPPSGT TCGDYMASYI
KLAGTGYLSD PSATDICSFC AVSTTNAFLA TFSSHYYRRW RNYGIFICYI
AFDYIAATFL YWLSRVPKKN GKISEKPKK
Legend
- X Phoshorylation
- X Ubiquitination
- X K-benzoylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[2, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[2, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[80, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[80, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[80, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[94, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[94, Phos] | Studer RA, Rodriguez-Mias RA, Haas KM, et al (2016) Evolution of protein phosphorylation across 18 fungal species. Science 354:229–232. (Publication) (All modifications) |
[94, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[94, Phos] | Albuquerque, C.P., Smolka, M.B., Payne, S.H., Bafna, V., Eng, J., Zhou, H. (2008). A multidimensional chromatography technology for in-depth phosphoproteome analysis. Molecular and Cellular Proteomics 7(7):1389-1396. (Publication) (All modifications) |
[94, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[98, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[98, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[232, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[232, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[233, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[233, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[238, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[238, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[238, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[239, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[239, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[320, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[320, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[320, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[351, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[441, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[472, K-bz] | Wang, D., Yan, F., Wu, P., Ge, K., Li, M., Li, T., Gao, Y., Peng, C., Chen, Y. (2022). Global profiling of regulatory elements in the histone benzoylation pathway. Nature Communications 13(1):1369 (Publication) (All modifications) |
[480, K-bz] | Wang, D., Yan, F., Wu, P., Ge, K., Li, M., Li, T., Gao, Y., Peng, C., Chen, Y. (2022). Global profiling of regulatory elements in the histone benzoylation pathway. Nature Communications 13(1):1369 (Publication) (All modifications) |
[853, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[853, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[853, Phos] | MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications) |
[853, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[854, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[854, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[857, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[866, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[866, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[868, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[868, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[869, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[869, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1034, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |