UniProt ID | NUP57_YEAST | |
---|---|---|
UniProt AC | P48837 | |
Protein Name | Nucleoporin NUP57 | |
Gene Name | NUP57 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 541 | |
Subcellular Localization |
Nucleus, nuclear pore complex. Nucleus membrane Peripheral membrane protein Cytoplasmic side. Nucleus membrane Peripheral membrane protein Nucleoplasmic side. Symmetric distribution. |
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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). NUP57 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, and pre-ribosome transport.. | |
Protein Sequence | MFGFSGSNNGFGNKPAGSTGFSFGQNNNNTNTQPSASGFGFGGSQPNSGTATTGGFGANQATNTFGSNQQSSTGGGLFGNKPALGSLGSSSTTASGTTATGTGLFGQQTAQPQQSTIGGGLFGNKPTTTTGGLFGNSAQNNSTTSGGLFGNKVGSTGSLMGGNSTQNTSNMNAGGLFGAKPQNTTATTGGLFGSKPQGSTTNGGLFGSGTQNNNTLGGGGLFGQSQQPQTNTAPGLGNTVSTQPSFAWSKPSTGSNLQQQQQQQIQVPLQQTQAIAQQQQLSNYPQQIQEQVLKCKESWDPNTTKTKLRAFVYNKVNETEAILYTKPGHVLQEEWDQAMEKKPSPQTIPIQIYGFEGLNQRNQVQTENVAQARIILNHILEKSTQLQQKHELDTASRILKAQSRNVEIEKRILKLGTQLATLKNRGLPLGIAEEKMWSQFQTLLQRSEDPAGLGKTNELWARLAILKERAKNISSQLDSKLMVFNDDTKNQDSMSKGTGEESNDRINKIVEILTNQQRGITYLNEVLEKDAAIVKKYKNKT | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
86 | Phosphorylation | GNKPALGSLGSSSTT CCCCCCCCCCCCCCC | 30.33 | 20377248 | |
89 | Phosphorylation | PALGSLGSSSTTASG CCCCCCCCCCCCCCC | 26.80 | 20377248 | |
90 | Phosphorylation | ALGSLGSSSTTASGT CCCCCCCCCCCCCCC | 29.88 | 20377248 | |
95 | Phosphorylation | GSSSTTASGTTATGT CCCCCCCCCCEEECC | 34.28 | 20377248 | |
97 | Phosphorylation | SSTTASGTTATGTGL CCCCCCCCEEECCCC | 15.68 | 20377248 | |
98 | Phosphorylation | STTASGTTATGTGLF CCCCCCCEEECCCCC | 26.25 | 20377248 | |
155 | Phosphorylation | LFGNKVGSTGSLMGG CCCCCCCCCCCCCCC | 32.36 | 24909858 | |
156 | Phosphorylation | FGNKVGSTGSLMGGN CCCCCCCCCCCCCCC | 25.51 | 21551504 | |
158 | Phosphorylation | NKVGSTGSLMGGNST CCCCCCCCCCCCCCC | 18.44 | 28889911 | |
164 | Phosphorylation | GSLMGGNSTQNTSNM CCCCCCCCCCCCCCC | 34.34 | 29734811 | |
344 | Phosphorylation | QAMEKKPSPQTIPIQ HHHHHCCCCCCCCEE | 38.22 | 22369663 | |
347 | Phosphorylation | EKKPSPQTIPIQIYG HHCCCCCCCCEEEEC | 31.91 | 22369663 | |
353 | Phosphorylation | QTIPIQIYGFEGLNQ CCCCEEEECCCCCCC | 10.21 | 22369663 | |
382 | Ubiquitination | ILNHILEKSTQLQQK HHHHHHHHCHHHHHH | 56.19 | 24961812 | |
382 | Acetylation | ILNHILEKSTQLQQK HHHHHHHHCHHHHHH | 56.19 | 24489116 | |
394 | Phosphorylation | QQKHELDTASRILKA HHHHHHHHHHHHHHH | 38.87 | 27017623 | |
396 | Phosphorylation | KHELDTASRILKAQS HHHHHHHHHHHHHHH | 23.19 | 19684113 | |
435 | Ubiquitination | PLGIAEEKMWSQFQT CCCHHHHHHHHHHHH | 36.86 | 23749301 | |
471 | Ubiquitination | AILKERAKNISSQLD HHHHHHHHHHHHHHH | 62.12 | 23749301 | |
474 | Phosphorylation | KERAKNISSQLDSKL HHHHHHHHHHHHCEE | 22.79 | 22890988 | |
475 | Phosphorylation | ERAKNISSQLDSKLM HHHHHHHHHHHCEEE | 30.85 | 22890988 | |
479 | Phosphorylation | NISSQLDSKLMVFND HHHHHHHCEEEEEEC | 35.96 | 22890988 | |
488 | Phosphorylation | LMVFNDDTKNQDSMS EEEEECCCCCCCHHC | 34.46 | 22890988 | |
489 | Ubiquitination | MVFNDDTKNQDSMSK EEEECCCCCCCHHCC | 60.65 | 23749301 | |
493 | Phosphorylation | DDTKNQDSMSKGTGE CCCCCCCHHCCCCCC | 18.39 | 22890988 | |
495 | Phosphorylation | TKNQDSMSKGTGEES CCCCCHHCCCCCCCH | 31.70 | 22890988 | |
496 | Ubiquitination | KNQDSMSKGTGEESN CCCCHHCCCCCCCHH | 52.42 | 23749301 | |
502 | Phosphorylation | SKGTGEESNDRINKI CCCCCCCHHHHHHHH | 39.46 | 23749301 | |
529 | Acetylation | YLNEVLEKDAAIVKK HHHHHHHHHHHHHHH | 48.81 | 24489116 |
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 NUP57_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NUP57_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 NUP57_YEAST !! |
Kegg Drug | ||||||
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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-344, 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-344 AND THR-347, ANDMASS SPECTROMETRY. |