| UniProt ID | NUP84_YEAST | |
|---|---|---|
| UniProt AC | P52891 | |
| Protein Name | Nucleoporin NUP84 | |
| Gene Name | NUP84 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 726 | |
| Subcellular Localization |
Nucleus, nuclear pore complex. Nucleus membrane Peripheral membrane protein Cytoplasmic side. Nucleus membrane Peripheral membrane protein Nucleoplasmic side. Symmetric distribution. |
|
| 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. NUP84 is involved in nuclear poly(A)+ RNA export, in NPC assembly and distribution, as well as in nuclear envelope organization.. | |
| Protein Sequence | MELSPTYQTERFTKFSDTLKEFKIEQNNEQNPIDPFNIIREFRSAAGQLALDLANSGDESNVISSKDWELEARFWHLVELLLVFRNADLDLDEMELHPYNSRGLFEKKLMQDNKQLYQIWIVMVWLKENTYVMERPKNVPTSKWLNSITSGGLKSCDLDFPLRENTNVLDVKDKEEDHIFFKYIYELILAGAIDEALEEAKLSDNISICMILCGIQEYLNPVIDTQIANEFNTQQGIKKHSLWRRTVYSLSQQAGLDPYERAIYSYLSGAIPNQEVLQYSDWESDLHIHLNQILQTEIENYLLENNQVGTDELILPLPSHALTVQEVLNRVASRHPSESEHPIRVLMASVILDSLPSVIHSSVEMLLDVVKGTEASNDIIDKPYLLRIVTHLAICLDIINPGSVEEVDKSKLITTYISLLKLQGLYENIPIYATFLNESDCLEACSFILSSLEDPQVRKKQIETINFLRLPASNILRRTTQRVFDETEQEYSPSNEISISFDVNNIDMHLIYGVEWLIEGKLYVDAVHSIIALSRRFLLNGRVKALEQFMERNNIGEICKNYELEKIADNISKDENEDQFLEEITQYEHLIKGIREYEEWQKSVSLLSSESNIPTLIEKLQGFSKDTFELIKTFLVDLTSSNFADSADYEILYEIRALYTPFLLMELHKKLVEAAKLLKIPKFISEALAFTSLVANENDKIYLLFQSSGKLKEYLDLVARTATLSN | |
| 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 |
|---|---|---|---|---|---|
| 4 | Phosphorylation | ----MELSPTYQTER ----CCCCCCCCHHH | 11.24 | 28152593 | |
| 6 | Phosphorylation | --MELSPTYQTERFT --CCCCCCCCHHHCH | 25.53 | 24961812 | |
| 7 | Phosphorylation | -MELSPTYQTERFTK -CCCCCCCCHHHCHH | 19.47 | 28889911 | |
| 16 | Phosphorylation | TERFTKFSDTLKEFK HHHCHHHHHHHHHCC | 31.10 | 28889911 | |
| 20 | Ubiquitination | TKFSDTLKEFKIEQN HHHHHHHHHCCCCCC | 64.30 | 23749301 | |
| 147 | Phosphorylation | PTSKWLNSITSGGLK CCHHHHHHCCCCCCC | 25.69 | 30377154 | |
| 154 | Ubiquitination | SITSGGLKSCDLDFP HCCCCCCCCCCCCCC | 52.92 | 24961812 | |
| 172 | Ubiquitination | NTNVLDVKDKEEDHI CCCEECCCCCCCCCH | 63.85 | 24961812 | |
| 382 | Ubiquitination | ASNDIIDKPYLLRIV CCCCCCCHHHHHHHH | 25.75 | 23749301 | |
| 521 | Ubiquitination | VEWLIEGKLYVDAVH EHHHHCCCCHHHHHH | 24.69 | 17644757 | |
| 572 | Phosphorylation | EKIADNISKDENEDQ HHHHHHCCCCCCHHH | 40.07 | 21440633 | |
| 603 | Phosphorylation | EYEEWQKSVSLLSSE HHHHHHHHHHHHHCC | 11.22 | 17563356 | |
| 615 | Phosphorylation | SSESNIPTLIEKLQG HCCCCHHHHHHHHCC | 36.25 | 17563356 | |
| 676 | Ubiquitination | KKLVEAAKLLKIPKF HHHHHHHHHCCCHHH | 62.49 | 23749301 | |
| 702 | Phosphorylation | ANENDKIYLLFQSSG CCCCCEEEEEEECCC | 11.77 | 28889911 | |
| 707 | Phosphorylation | KIYLLFQSSGKLKEY EEEEEEECCCCHHHH | 33.45 | 28889911 | |
| 708 | Phosphorylation | IYLLFQSSGKLKEYL EEEEEECCCCHHHHH | 29.21 | 28889911 |
| 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 NUP84_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NUP84_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 NUP84_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-603 AND THR-615, ANDMASS SPECTROMETRY. | |
