| UniProt ID | NUP59_YEAST | |
|---|---|---|
| UniProt AC | Q05166 | |
| Protein Name | Nucleoporin ASM4 | |
| Gene Name | ASM4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 528 | |
| 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. 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). May have a mitosis control function (By similarity).. | |
| Protein Sequence | MFGIRSGNNNGGFTNLTSQAPQTTQMFQSQSQLQPQPQPQPQQQQQHLQFNGSSDASSLRFGNSLSNTVNANNYSSNIGNNSINNNNIKNGTNNISQHGQGNNPSWVNNPKKRFTPHTVIRRKTTKQNSSSDINQNDDSSSMNATMRNFSKQNQDSKHNERNKSAANNDINSLLSNFNDIPPSVTLQDWQREDEFGSIPSLTTQFVTDKYTAKKTNRSAYDSKNTPNVFDKDSYVRIANIEQNHLDNNYNTAETNNKVHETSSKSSSLSAIIVFGYPESISNELIEHFSHFGHIMEDFQVLRLGRGINPNTFRIFHNHDTGCDENDSTVNKSITLKGRNNESNNKKYPIFTGESWVKLTYNSPSSALRALQENGTIFRGSLIGCIPYSKNAVEQLAGCKIDNVDDIGEFNVSMYQNSSTSSTSNTPSPPNVIITDGTLLREDDNTPAGHAGNPTNISSPIVANSPNKRLDVIDGKLPFMQNAGPNSNIPNLLRNLESKMRQQEAKYRNNEPAGFTHKLSNWLFGWNDL | |
| 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 |
|---|---|---|---|---|---|
| 82 | Phosphorylation | SSNIGNNSINNNNIK CCCCCCCCCCCCCCC | 30.60 | 23749301 | |
| 115 | Phosphorylation | NNPKKRFTPHTVIRR CCCCCCCCCCHHEEC | 20.42 | 27738172 | |
| 129 | Phosphorylation | RKTTKQNSSSDINQN CCCCCCCCCCCCCCC | 28.82 | 21440633 | |
| 130 | Phosphorylation | KTTKQNSSSDINQND CCCCCCCCCCCCCCC | 39.31 | 28889911 | |
| 131 | Phosphorylation | TTKQNSSSDINQNDD CCCCCCCCCCCCCCC | 42.18 | 24961812 | |
| 141 | Phosphorylation | NQNDDSSSMNATMRN CCCCCCHHHHHHHHH | 21.73 | 28889911 | |
| 150 | Phosphorylation | NATMRNFSKQNQDSK HHHHHHHHHHCHHHH | 36.56 | 21440633 | |
| 231 | Acetylation | NTPNVFDKDSYVRIA CCCCCCCCCCEEEEE | 36.79 | 24489116 | |
| 279 | Phosphorylation | IVFGYPESISNELIE EEEECCHHHCHHHHH | 27.15 | 28889911 | |
| 445 | Phosphorylation | LLREDDNTPAGHAGN EEECCCCCCCCCCCC | 22.85 | 22890988 | |
| 454 | Phosphorylation | AGHAGNPTNISSPIV CCCCCCCCCCCCCCC | 49.54 | 22890988 | |
| 457 | Phosphorylation | AGNPTNISSPIVANS CCCCCCCCCCCCCCC | 31.93 | 25533186 | |
| 458 | Phosphorylation | GNPTNISSPIVANSP CCCCCCCCCCCCCCC | 18.17 | 17563356 | |
| 464 | Phosphorylation | SSPIVANSPNKRLDV CCCCCCCCCCCCCCE | 21.80 | 19795423 |
| 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 NUP59_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NUP59_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 NUP59_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-457 AND SER-458, ANDMASS SPECTROMETRY. | |
| "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-458, AND MASSSPECTROMETRY. | |
