Basic Information
Name | Vacuolar morphogenesis protein 6 (Vacuolar protein sorting-associated protein 39) |
Uniprot ID | Q07468 |
Systematic gene name | YDL077C |
Standard gene name | VAM6 |
Gene names | VAM6 CVT4 VPL18 VPL22 VPS39 YDL077C |
Description from SGD | YDL077C VAM6 SGDID:S000002235, Chr IV from 320120-316971, Genome Release 64-3-1, reverse complement, Verified ORF, "Guanine nucleotide exchange factor for the GTPase Gtr1p; subunit of the HOPS endocytic tethering complex; vacuole membrane protein; functions as a Rab GTPase effector, interacting with both GTP- and GDP-bound conformations of Ypt7p; facilitates tethering and promotes membrane fusion events at the late endosome and vacuole; required for both membrane and protein trafficking; component of vacuole-mitochondrion contacts (vCLAMPs) important for lipid transfer between organelles" |
Protein length | 1049 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MLRAQKLHSL KSSDITAILP TEQSQKLVLA KKNGDVEVYS RDGNTLKLFQ
VYPDLLQNAK NDPLPPVIEN FYFANELSTI FAQCKETLIL LSTTNLHEYD
RIIDRRGINH CWLFERSHKN KEEKNTYLIY STINTAKMRV LIWEGRTYKN
MMEASLSYRK ETIRSIYPGE TGITLATDLG IYHWPYNKPS LIRIEKTVKN
KFPKDMISAL TELKEQAEKV IEKKPKKNSH FDAQSFSSMD RMSRKSSMSS
LWYRTIRNER GNKIRYTFEL DGNDATPMII DGATKKIFKV ELMHNNEEPF
LIATDHATFS ESNSEFDHMQ YLSSNLLMLY NSSTIKFVDY ENGFTFLQQK
IPEGIKWVKN LSGTYFLVWT SNDEVQLFSY HVDDGSEDDD QESICGDIND
PDFYQLWRKV LFYKFFIDSP HSKELCVSDN PEESLDICAM KLRDLTVMWC
LRIFDKFQNY MVQLERSRNS RMIRSKCEEM IIKSIFDLFI KFWAPPQLVI
LKVFPSAISS LVLEITGQEH HCLLKEAEEV KETYDIPPHL LNRWCLPYLT
DTRRHLQNLL SKENDDESRI TWCYRDREIK QSFDFFLISN HDDVDLNTML
TLIDTVLFKC YLYYNPPMVG PFIRVENHCD SHVIVTELKI RHMFKDLIDF
YYKRGNHEEA LKFLTDLVDE LENDNTDQKQ RQKIDHGVKI LVIYYLKKLS
NPQLDVIFTY TDWLLNRHND SIKEILSSIF FYDSQACSSR DHLKVYGYIK
KFDKLLAIQY LEFAISTFRL EGNKLHTVLI KLYLENLDIP STRIKLKSLL
ETTSVYEPRT ILKLLNDAIE SGSDQLPTNQ LNFVKYLKIF PLSKLENHKE
AVHILLDEID DYKAATSYCN DVYQSDSTKG EELLLYLYSK LVSIYDSNRN
SKLILNFLQD HGSKLNSAEI YKNLPQDISL YDIGRVVSQL LKKHTSKMDE
TRLEKALLQV ELVATTYKLN ERMSSYGVLS DSHKCPICKK VISNFGTDSI
SWFTREGRNI ITHYNCGKVL QERFNAKNEK SSRIKQKTLG EVINELNNK
VYPDLLQNAK NDPLPPVIEN FYFANELSTI FAQCKETLIL LSTTNLHEYD
RIIDRRGINH CWLFERSHKN KEEKNTYLIY STINTAKMRV LIWEGRTYKN
MMEASLSYRK ETIRSIYPGE TGITLATDLG IYHWPYNKPS LIRIEKTVKN
KFPKDMISAL TELKEQAEKV IEKKPKKNSH FDAQSFSSMD RMSRKSSMSS
LWYRTIRNER GNKIRYTFEL DGNDATPMII DGATKKIFKV ELMHNNEEPF
LIATDHATFS ESNSEFDHMQ YLSSNLLMLY NSSTIKFVDY ENGFTFLQQK
IPEGIKWVKN LSGTYFLVWT SNDEVQLFSY HVDDGSEDDD QESICGDIND
PDFYQLWRKV LFYKFFIDSP HSKELCVSDN PEESLDICAM KLRDLTVMWC
LRIFDKFQNY MVQLERSRNS RMIRSKCEEM IIKSIFDLFI KFWAPPQLVI
LKVFPSAISS LVLEITGQEH HCLLKEAEEV KETYDIPPHL LNRWCLPYLT
DTRRHLQNLL SKENDDESRI TWCYRDREIK QSFDFFLISN HDDVDLNTML
TLIDTVLFKC YLYYNPPMVG PFIRVENHCD SHVIVTELKI RHMFKDLIDF
YYKRGNHEEA LKFLTDLVDE LENDNTDQKQ RQKIDHGVKI LVIYYLKKLS
NPQLDVIFTY TDWLLNRHND SIKEILSSIF FYDSQACSSR DHLKVYGYIK
KFDKLLAIQY LEFAISTFRL EGNKLHTVLI KLYLENLDIP STRIKLKSLL
ETTSVYEPRT ILKLLNDAIE SGSDQLPTNQ LNFVKYLKIF PLSKLENHKE
AVHILLDEID DYKAATSYCN DVYQSDSTKG EELLLYLYSK LVSIYDSNRN
SKLILNFLQD HGSKLNSAEI YKNLPQDISL YDIGRVVSQL LKKHTSKMDE
TRLEKALLQV ELVATTYKLN ERMSSYGVLS DSHKCPICKK VISNFGTDSI
SWFTREGRNI ITHYNCGKVL QERFNAKNEK SSRIKQKTLG EVINELNNK
Legend
- X Monomethylation
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[35, Mono-CH3] | Wang, K., Zhou, Y.J., Liu, H., Cheng, K., Mao, J., Wang, F., Liu, W., Ye, M., Zhao, Z.K., Zou, H. (2015). Proteomic analysis of protein methylation in the yeast Saccharomyces cerevisiae. J Proteomics 114: 226-233. (Publication) (All modifications) |
[37, Mono-CH3] | Wang, K., Zhou, Y.J., Liu, H., Cheng, K., Mao, J., Wang, F., Liu, W., Ye, M., Zhao, Z.K., Zou, H. (2015). Proteomic analysis of protein methylation in the yeast Saccharomyces cerevisiae. J Proteomics 114: 226-233. (Publication) (All modifications) |
[92, 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) |
[92, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[235, 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) |
[235, 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) |
[235, 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) |
[235, 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) |
[235, Phos] | Holt, L.J., Tuch, B.B., Villén, J., Johnson, A.D., Gygi, S.P., Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications) |
[235, Phos] | 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) |
[235, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[237, 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) |
[237, 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) |
[237, 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) |
[237, 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] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[238, 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) |
[238, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[246, 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) |
[247, 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) |
[247, 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) |
[247, 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) |
[247, 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) |
[247, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[249, 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) |
[250, 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) |
[250, 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) |
[250, Phos] | Holt, L.J., Tuch, B.B., Villén, J., Johnson, A.D., Gygi, S.P., Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications) |
[250, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |