UniProt ID | NUP53_YEAST | |
---|---|---|
UniProt AC | Q03790 | |
Protein Name | Nucleoporin NUP53 | |
Gene Name | NUP53 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 475 | |
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). NUP53 may play an important role in cell cycle regulation by inhibiting PSE1 transport functions during mitosis and sequestration of MAD1-MAD2 in a cell cycle-dependent manner. It also seems to play an important role in de novo NPC assembly by associating with nuclear membranes and driving their proliferation.. | |
Protein Sequence | MADLQKQENSSRFTNVSVIAPESQGQHEQQKQQEQLEQQKQPTGLLKGLNGFPSAPQPLFMEDPPSTVSGELNDNPAWFNNPRKRAIPNSIIKRSNGQSLSPVRSDSADVPAFSNSNGFNNVTFGSKKDPRILKNVSPNDNNSANNNAHSSDLGTVVFDSNEAPPKTSLADWQKEDGIFSSKTDNIEDPNLSSNITFDGKPTATPSPFRPLEKTSRILNFFDKNTKTTPNTASSEASAGSKEGASTNWDDHAIIIFGYPETIANSIILHFANFGEILEDFRVIKDFKKLNSKNMSKSPSLTAQKYPIYTGDGWVKLTYKSELSKSRALQENGIIMNGTLIGCVSYSPAALKQLASLKKSEEIINNKTSSQTSLSSKDLSNYRKTEGIFEKAKAKAVTSKVRNAEFKVSKNSTSFKNPRRLEIKDGRSLFLRNRGKIHSGVLSSIESDLKKREQASKSKKSWLNRLNNWLFGWNDL | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MADLQKQEN ------CCCHHHHHH | 26.65 | 22814378 | |
6 | Acetylation | --MADLQKQENSSRF --CCCHHHHHHCCCC | 67.86 | 25381059 | |
43 | Phosphorylation | LEQQKQPTGLLKGLN HHHHHCCCHHCCCCC | 37.66 | 19795423 | |
90 | Phosphorylation | RKRAIPNSIIKRSNG CCCCCCCCCEECCCC | 21.97 | 21440633 | |
95 | Phosphorylation | PNSIIKRSNGQSLSP CCCCEECCCCCCCCC | 40.07 | 25521595 | |
99 | Phosphorylation | IKRSNGQSLSPVRSD EECCCCCCCCCCCCC | 32.01 | 19823750 | |
101 | Phosphorylation | RSNGQSLSPVRSDSA CCCCCCCCCCCCCCC | 26.96 | 25521595 | |
105 | Phosphorylation | QSLSPVRSDSADVPA CCCCCCCCCCCCCCC | 35.83 | 25521595 | |
107 | Phosphorylation | LSPVRSDSADVPAFS CCCCCCCCCCCCCCC | 27.84 | 25521595 | |
114 | Phosphorylation | SADVPAFSNSNGFNN CCCCCCCCCCCCCCC | 41.26 | 21440633 | |
116 | Phosphorylation | DVPAFSNSNGFNNVT CCCCCCCCCCCCCCC | 36.81 | 23749301 | |
123 | Phosphorylation | SNGFNNVTFGSKKDP CCCCCCCCCCCCCCC | 25.13 | 19823750 | |
126 | Phosphorylation | FNNVTFGSKKDPRIL CCCCCCCCCCCCCHH | 32.13 | 19823750 | |
137 | Phosphorylation | PRILKNVSPNDNNSA CCHHCCCCCCCCCCC | 27.64 | 21440633 | |
143 | Phosphorylation | VSPNDNNSANNNAHS CCCCCCCCCCCCCCC | 38.33 | 24961812 | |
150 | Phosphorylation | SANNNAHSSDLGTVV CCCCCCCCCCCCEEE | 24.12 | 21440633 | |
151 | Phosphorylation | ANNNAHSSDLGTVVF CCCCCCCCCCCEEEE | 27.30 | 24961812 | |
155 | Phosphorylation | AHSSDLGTVVFDSNE CCCCCCCEEEECCCC | 22.31 | 24961812 | |
192 | Phosphorylation | NIEDPNLSSNITFDG CCCCCCCCCCEEECC | 28.16 | 25521595 | |
193 | Phosphorylation | IEDPNLSSNITFDGK CCCCCCCCCEEECCC | 35.10 | 20377248 | |
196 | Phosphorylation | PNLSSNITFDGKPTA CCCCCCEEECCCCCC | 21.66 | 20377248 | |
202 | Phosphorylation | ITFDGKPTATPSPFR EEECCCCCCCCCCCC | 46.80 | 20377248 | |
204 | Phosphorylation | FDGKPTATPSPFRPL ECCCCCCCCCCCCCH | 27.12 | 21440633 | |
206 | Phosphorylation | GKPTATPSPFRPLEK CCCCCCCCCCCCHHH | 32.11 | 20377248 | |
215 | Phosphorylation | FRPLEKTSRILNFFD CCCHHHHHHHHHHHC | 28.52 | 21440633 | |
223 | Acetylation | RILNFFDKNTKTTPN HHHHHHCCCCCCCCC | 62.45 | 22865919 | |
227 | Phosphorylation | FFDKNTKTTPNTASS HHCCCCCCCCCCCCC | 45.51 | 20377248 | |
228 | Phosphorylation | FDKNTKTTPNTASSE HCCCCCCCCCCCCCC | 18.98 | 20377248 | |
231 | Phosphorylation | NTKTTPNTASSEASA CCCCCCCCCCCCCCC | 29.17 | 22369663 | |
233 | Phosphorylation | KTTPNTASSEASAGS CCCCCCCCCCCCCCC | 27.03 | 22369663 | |
234 | Phosphorylation | TTPNTASSEASAGSK CCCCCCCCCCCCCCC | 34.42 | 23749301 | |
237 | Phosphorylation | NTASSEASAGSKEGA CCCCCCCCCCCCCCC | 29.16 | 22369663 | |
240 | Phosphorylation | SSEASAGSKEGASTN CCCCCCCCCCCCCCC | 27.53 | 22369663 | |
295 | Phosphorylation | KLNSKNMSKSPSLTA HHCCCCCCCCCCCCC | 39.10 | 20377248 | |
297 | Phosphorylation | NSKNMSKSPSLTAQK CCCCCCCCCCCCCCC | 16.65 | 22369663 | |
299 | Phosphorylation | KNMSKSPSLTAQKYP CCCCCCCCCCCCCCC | 45.50 | 22369663 | |
301 | Phosphorylation | MSKSPSLTAQKYPIY CCCCCCCCCCCCCEE | 31.23 | 22369663 | |
338 | Phosphorylation | NGIIMNGTLIGCVSY CCEEECCEEEEEEEC | 15.36 | 28889911 | |
345 | Phosphorylation | TLIGCVSYSPAALKQ EEEEEEECCHHHHHH | 9.77 | 28889911 | |
346 | Phosphorylation | LIGCVSYSPAALKQL EEEEEECCHHHHHHH | 10.68 | 28889911 | |
355 | Phosphorylation | AALKQLASLKKSEEI HHHHHHHHCCCCHHH | 49.68 | 28889911 | |
366 | Ubiquitination | SEEIINNKTSSQTSL CHHHHHCCCCCCCCC | 45.34 | 23749301 | |
367 | Phosphorylation | EEIINNKTSSQTSLS HHHHHCCCCCCCCCC | 35.42 | 19823750 | |
368 | Phosphorylation | EIINNKTSSQTSLSS HHHHCCCCCCCCCCH | 23.27 | 19823750 | |
369 | Phosphorylation | IINNKTSSQTSLSSK HHHCCCCCCCCCCHH | 42.58 | 21440633 | |
371 | Phosphorylation | NNKTSSQTSLSSKDL HCCCCCCCCCCHHHH | 33.32 | 19823750 | |
372 | Phosphorylation | NKTSSQTSLSSKDLS CCCCCCCCCCHHHHH | 20.72 | 23749301 | |
374 | Phosphorylation | TSSQTSLSSKDLSNY CCCCCCCCHHHHHHH | 34.80 | 23749301 | |
375 | Phosphorylation | SSQTSLSSKDLSNYR CCCCCCCHHHHHHHH | 35.17 | 19823750 | |
376 | Acetylation | SQTSLSSKDLSNYRK CCCCCCHHHHHHHHH | 60.35 | 24489116 | |
392 | Acetylation | EGIFEKAKAKAVTSK HCHHHHHHHHHHHHH | 62.58 | 23572591 | |
394 | Acetylation | IFEKAKAKAVTSKVR HHHHHHHHHHHHHHH | 42.56 | 23572591 | |
399 | Acetylation | KAKAVTSKVRNAEFK HHHHHHHHHHCCEEE | 35.53 | 23572591 | |
415 | Acetylation | SKNSTSFKNPRRLEI CCCCCCCCCCCEEEE | 66.85 | 25381059 | |
438 | Phosphorylation | RNRGKIHSGVLSSIE CCCCCCCHHHHHHHH | 33.79 | 21440633 | |
442 | Phosphorylation | KIHSGVLSSIESDLK CCCHHHHHHHHHHHH | 27.19 | 21126336 | |
446 | Phosphorylation | GVLSSIESDLKKREQ HHHHHHHHHHHHHHH | 46.72 | 21551504 |
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 NUP53_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NUP53_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 NUP53_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-101 AND SER-438, 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-101, AND MASSSPECTROMETRY. |