| UniProt ID | NUP42_YEAST | |
|---|---|---|
| UniProt AC | P49686 | |
| Protein Name | Nucleoporin NUP42 | |
| Gene Name | NUP42 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 430 | |
| Subcellular Localization |
Nucleus, nuclear pore complex. Nucleus membrane Peripheral membrane protein 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. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP42 is specifically important for nuclear protein and mRNA export.. | |
| Protein Sequence | MSAFGNPFTSGAKPNLSNTSGINPFTNNAASTNNMGGSAFGRPSFGTANTMTGGTTTSAFGMPQFGTNTGNTGNTSISAFGNTSNAAKPSAFGAPAFGSSAPINVNPPSTTSAFGAPSFGSTGFGAMAATSNPFGKSPGSMGSAFGQPAFGANKTAIPSSSVSNSNNSAFGAASNTPLTTTSPFGSLQQNASQNASSTSSAFGKPTFGAATNTQSPFGTIQNTSTSSGTGVSPFGTFGTNSNNKSPFSNLQSGAGAGSSPFGTTTSKANNNNNVGSSAFGTTNNQSPFSGGSGGTFGSASNLNKNTNGNFQSSFGNKGFSFGITPQNDANKVSQSNPSFGQTMPNTDPNISLKSNGNATSFGFGQQQMNATNVNANTATGKIRFVQGLSSEKDGILELADLAEETLKIFRANKFELGLVPDIPPPPALVA | |
| 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 |
|---|---|---|---|---|---|
| 50 | Phosphorylation | PSFGTANTMTGGTTT CCCCCCCCCCCCCEE | 17.41 | 30377154 | |
| 72 | Phosphorylation | FGTNTGNTGNTSISA CCCCCCCCCCCEEEC | 32.90 | 30377154 | |
| 83 | Phosphorylation | SISAFGNTSNAAKPS EEECCCCCCCCCCCC | 24.60 | 30377154 | |
| 137 | Phosphorylation | TSNPFGKSPGSMGSA CCCCCCCCCCCHHHH | 34.57 | 22369663 | |
| 140 | Phosphorylation | PFGKSPGSMGSAFGQ CCCCCCCCHHHHHCC | 24.29 | 25521595 | |
| 143 | Phosphorylation | KSPGSMGSAFGQPAF CCCCCHHHHHCCCCC | 16.28 | 25521595 | |
| 245 | Phosphorylation | GTNSNNKSPFSNLQS CCCCCCCCCCCCCCC | 33.04 | 21551504 | |
| 258 | Phosphorylation | QSGAGAGSSPFGTTT CCCCCCCCCCCCCCC | 34.01 | 28132839 | |
| 259 | Phosphorylation | SGAGAGSSPFGTTTS CCCCCCCCCCCCCCC | 24.27 | 28132839 | |
| 276 | Phosphorylation | NNNNNVGSSAFGTTN CCCCCCCCCCEECCC | 17.76 | 22369663 | |
| 277 | Phosphorylation | NNNNVGSSAFGTTNN CCCCCCCCCEECCCC | 22.99 | 22369663 | |
| 281 | Phosphorylation | VGSSAFGTTNNQSPF CCCCCEECCCCCCCC | 21.64 | 22369663 | |
| 282 | Phosphorylation | GSSAFGTTNNQSPFS CCCCEECCCCCCCCC | 32.33 | 22369663 | |
| 286 | Phosphorylation | FGTTNNQSPFSGGSG EECCCCCCCCCCCCC | 30.00 | 23749301 | |
| 289 | Phosphorylation | TNNQSPFSGGSGGTF CCCCCCCCCCCCCCC | 45.70 | 22369663 | |
| 292 | Phosphorylation | QSPFSGGSGGTFGSA CCCCCCCCCCCCCCC | 37.26 | 22369663 | |
| 295 | Phosphorylation | FSGGSGGTFGSASNL CCCCCCCCCCCCCCC | 28.48 | 25521595 | |
| 298 | Phosphorylation | GSGGTFGSASNLNKN CCCCCCCCCCCCCCC | 25.08 | 22369663 | |
| 300 | Phosphorylation | GGTFGSASNLNKNTN CCCCCCCCCCCCCCC | 43.47 | 22369663 | |
| 313 | Phosphorylation | TNGNFQSSFGNKGFS CCCCCCCCCCCCCEE | 26.79 | 30377154 | |
| 320 | Phosphorylation | SFGNKGFSFGITPQN CCCCCCEECEECCCC | 31.09 | 30377154 | |
| 324 | Phosphorylation | KGFSFGITPQNDANK CCEECEECCCCCHHC | 21.14 | 30377154 | |
| 338 | Phosphorylation | KVSQSNPSFGQTMPN CHHCCCCCCCCCCCC | 46.38 | 30377154 | |
| 342 | Phosphorylation | SNPSFGQTMPNTDPN CCCCCCCCCCCCCCC | 34.67 | 30377154 | |
| 351 | Phosphorylation | PNTDPNISLKSNGNA CCCCCCCEECCCCCC | 36.06 | 15665377 | |
| 359 | Phosphorylation | LKSNGNATSFGFGQQ ECCCCCCCCCCCCCC | 28.70 | 28889911 | |
| 360 | Phosphorylation | KSNGNATSFGFGQQQ CCCCCCCCCCCCCCC | 22.44 | 28889911 | |
| 371 | Phosphorylation | GQQQMNATNVNANTA CCCCCCCEECCCCCC | 34.39 | 28889911 | |
| 379 | Phosphorylation | NVNANTATGKIRFVQ ECCCCCCCCEEEEEE | 36.65 | 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 NUP42_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NUP42_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 NUP42_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-137 AND SER-298, ANDMASS SPECTROMETRY. | |
