Basic Information

NameNucleoporin GLE1 (Nuclear pore protein GLE1) (RNA export factor GLE1)
Uniprot IDQ12315
Systematic gene nameYDL207W
Standard gene nameGLE1
Gene namesGLE1 BRR3 RSS1 YDL207W D1049
Description from SGDYDL207W GLE1 SGDID:S000002366, Chr IV from 88248-89864, Genome Release 64-3-1, Verified ORF, "Cytoplasmic nucleoporin required for polyadenylated mRNA export; contains a nuclear export signal; when bound to inositol hexakisphosphate (IP6), functions as an activator for the Dbp5p ATPase activity at the nuclear pore complex during mRNA export; mediates translation initiation; required for efficient translation termination"
Protein length538
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MRFVFDEVFN SDTDSPEFEE TCSTTSSTSS QCPTPEPSPA IKLPSFTKVG
TKKLVNESVV ILDPALENAL RDLNLQSKLI PINEPIVAAS SIIVPHSTNM
PLPRASHSSL LDNAKNSNAT APLLEAIEES FQRKMQNLVL ANQKEIQSIR
ENKRRVEEQR KRKEEEERKR KEAEEKAKRE QELLRQKKDE EERKRKEAEA
KLAQQKQEEE RKKIEEQNEK ERQLKKEHEA KLLQQKDKLG KAVTNFDKIS
KMFWHYKDKI AQIKQDIVLP IKKADVNVRN LLSRHKRKIN PKFGQLTNSN
QQLFKIQNEL TQLINDTKGD SLAYHWILNF IAKAVVHQAE TEVRVKPESA
LPLGKLTLYL LVQFPELQEL FMARLVKKCP FVIGFTCEID TEKGRQNMGW
KRNNENKWED NTSYDERMGG ILSLFAIITR LQLPQEFITT TSHPFPIALS
WHILARICNT PLNLITNTHF VILGSWWDAA AVQFLQAYGN QASKLLILIG
EELTSRMAEK KYVGAARLRI LLEAWQNNNM ESFPEMSP

Legend

  • 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

[106, 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)
[108, 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)
[108, Phos]Renvoisé M, Bonhomme L, Davanture M, et al (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. Journal of Proteomics 106:140–150. (Publication) (All modifications)
[108, 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)
[108, 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)
[108, 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)
[108, 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)
[108, Phos]Chen, S.H., Albuquerque, C.P., Liang, J., Suhandynata, R.T., Zhou, H. (2010). A proteome-wide analysis of kinase-substrate network in the DNA damage response. J Biol Chem 285: 12803-12812. (Publication) (All modifications)
[108, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[109, 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)