| UniProt ID | GLE1_YEAST | |
|---|---|---|
| UniProt AC | Q12315 | |
| Protein Name | Nucleoporin GLE1 | |
| Gene Name | GLE1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 538 | |
| Subcellular Localization |
Nucleus, nuclear pore complex . Nucleus membrane Peripheral membrane protein Cytoplasmic side . Nucleus membrane Peripheral membrane protein Nucleoplasmic side . Biased towards cytoplasmic side. |
|
| Protein Description | Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved in a terminal step of poly(A)+ mRNA transport through the NPC probably by binding the ATP-dependent RNA helicase DBP5 and GFD1 at the cytoplasmic side of the NPC. These interactions are thought to be important for the dissociation of transport proteins such as the heterogeneous nuclear ribonucleoprotein (hnRNP) NAB2 from exported mRNA.. | |
| Protein Sequence | MRFVFDEVFNSDTDSPEFEETCSTTSSTSSQCPTPEPSPAIKLPSFTKVGTKKLVNESVVILDPALENALRDLNLQSKLIPINEPIVAASSIIVPHSTNMPLPRASHSSLLDNAKNSNATAPLLEAIEESFQRKMQNLVLANQKEIQSIRENKRRVEEQRKRKEEEERKRKEAEEKAKREQELLRQKKDEEERKRKEAEAKLAQQKQEEERKKIEEQNEKERQLKKEHEAKLLQQKDKLGKAVTNFDKISKMFWHYKDKIAQIKQDIVLPIKKADVNVRNLLSRHKRKINPKFGQLTNSNQQLFKIQNELTQLINDTKGDSLAYHWILNFIAKAVVHQAETEVRVKPESALPLGKLTLYLLVQFPELQELFMARLVKKCPFVIGFTCEIDTEKGRQNMGWKRNNENKWEDNTSYDERMGGILSLFAIITRLQLPQEFITTTSHPFPIALSWHILARICNTPLNLITNTHFVILGSWWDAAAVQFLQAYGNQASKLLILIGEELTSRMAEKKYVGAARLRILLEAWQNNNMESFPEMSP | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 45 | Phosphorylation | SPAIKLPSFTKVGTK CCCCCCCCCCCCCCC | 56.86 | 27017623 | |
| 106 | Phosphorylation | NMPLPRASHSSLLDN CCCCCCCCCHHHHHH | 25.78 | 30377154 | |
| 108 | Phosphorylation | PLPRASHSSLLDNAK CCCCCCCHHHHHHHC | 21.86 | 17563356 | |
| 109 | Phosphorylation | LPRASHSSLLDNAKN CCCCCCHHHHHHHCC | 27.77 | 30377154 | |
| 264 | Acetylation | KDKIAQIKQDIVLPI HHHHHHHCCCEEEEE | 29.82 | 24489116 | |
| 505 | Phosphorylation | LIGEELTSRMAEKKY HHCHHHHHHHHHHHC | 32.46 | 30377154 |
| 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 GLE1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GLE1_YEAST !! | ||||||
* 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 GLE1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-108, 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-108, AND MASSSPECTROMETRY. | |
