UniProt ID | NUP1_ARATH | |
---|---|---|
UniProt AC | Q9CAF4 | |
Protein Name | Nuclear pore complex protein NUP1 {ECO:0000303|PubMed:19843313} | |
Gene Name | NUP1 {ECO:0000303|PubMed:19843313} | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 1309 | |
Subcellular Localization | Nucleus envelope . Nucleus, nuclear pore complex . Cytoplasm, cytosol . Interacts dynamically with the NPC and localizes to the cytosolic pool following nuclear envelope breakdown during mitosis. | |
Protein Description | Nucleoporin required for nuclear mRNA export. Functions as an adapter and/or regulator molecule in the periphery of the nuclear pore complex (NPC). May interact with importin proteins and mediate active nucleocytoplasmic transport through the NPC. Involved in regulation of nuclear morphology.. | |
Protein Sequence | MASAARGESSNPYGGGLGTGGKFRKPTARRSQKTPYDRPTTSVRNAGLGGGDVRGGGWLSKLVDPAQRLITYSAQRLFGSLSRKRLGSGETPLQSPEQQKQLPERGVNQETKVGHKEDVSNLSMKNGLIRMEDTNASVDPPKDGFTDLEKILQGKTFTRSEVDRLTTLLRSKAADSSTMNEEQRNEVGMVVRHPPSHERDRTHPDNGSMNTLVSTPPGSLRTLDECIASPAQLAKAYMGSRPSEVTPSMLGLRGQAGREDSVFLNRTPFPQKSPTMSLVTKPSGQRPLENGFVTPRSRGRSAVYSMARTPYSRPQSSVKIGSLFQASPSKWEESLPSGSRQGFQSGLKRRSSVLDNDIGSVGPVRRIRQKSNLSSRSLALPVSESPLSVRANGGEKTTHTSKDSAEDIPGSSFNLVPTKSSEMASKILQQLDKLVSTREKSPSKLSPSMLRGPALKSLQNVEAPKFLGNLPEKKANSPDSSYQKQEISRESVSREVLAQSEKTGDAVDGTSKTGSSKDQDMRGKGVYMPLTNSLEEHPPKKRSFRMSAHEDFLELDDDLGAASTPCEVAEKQNAFEVEKSHISMPIGEKPLTPSEAMPSTSYISNGDASQGTSNGSLETERNKFVAFPIEAVQQSNMASEPTSKFIQGTEKSSISSGKPTSEEKRIPLEEPKKPAAVFPNISFSPPATGLLNQNSGASADIKLEKTSSTAFGVSEAWAKPTESKKTFSNSASGAESSTSAAPTLNGSIFSAGANAVTPPPSNGSLTSSPSFPPSISNIPSDNSVGDMPSTVQSFAATHNSSSIFGKLPTSNDSNSQSTSASPLSSTSPFKFGQPAAPFSAPAVSESSGQISKETEVKNATFGNTSTFKFGGMASADQSTGIVFGAKSAENKSRPGFVFGSSSVVGGSTLNPSTAAASAPESSGSLIFGVTSSSTPGTETSKISASSAATNTGNSVFGTSSFAFTSSGSSMVGGVSASTGSSVFGFNAVSSASATSSQSQASNLFGAGNAQTGNTGSGTTTSTQSIPFQFGSSPSAPSFGLSGNSSLASNSSPFGFSKSEPAVFTSVSTPQLSSTNSSASSSSTMSSPLFGTSWQAPNSSPNSGPVFSSSFTTSSTPTTFSFGGSSAATVSSTTTPIFGASTNNTPSPSPIFGFGSTPPTTPQQPVFGNSGTPSQSLFGNSTPGFAFGAPNNGNGINNNQQVSMEDSMAEDTDQANRASMVAPMFGQAAVSMPQPNFAFGGGAATQPPSMANPFQFGGQPMASTLQNASPFQASQSLEFQGGGSFSLGSTGGGDKSGRRIFKAKKSTRKK | |
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 |
---|---|---|---|---|---|
88 | Phosphorylation | LSRKRLGSGETPLQS CCCCCCCCCCCCCCC | 30407730 | ||
91 | Phosphorylation | KRLGSGETPLQSPEQ CCCCCCCCCCCCHHH | 30407730 | ||
95 | Phosphorylation | SGETPLQSPEQQKQL CCCCCCCCHHHHHCC | 30407730 | ||
229 | Phosphorylation | TLDECIASPAQLAKA CHHHHHCCHHHHHHH | 30291188 | ||
261 | Phosphorylation | GQAGREDSVFLNRTP CCCCCCCCCEECCCC | 30407730 | ||
294 | Phosphorylation | PLENGFVTPRSRGRS CCCCCCCCCCCCCCC | 29654922 | ||
327 | Phosphorylation | IGSLFQASPSKWEES CCCCEECCHHHHHHC | 27288362 | ||
329 | Phosphorylation | SLFQASPSKWEESLP CCEECCHHHHHHCCC | 27288362 | ||
351 | Phosphorylation | QSGLKRRSSVLDNDI HHHHHHHHHCCCCCC | 30407730 | ||
352 | Phosphorylation | SGLKRRSSVLDNDIG HHHHHHHHCCCCCCC | 23111157 | ||
360 | Phosphorylation | VLDNDIGSVGPVRRI CCCCCCCCCHHHHHH | 30291188 | ||
371 | Phosphorylation | VRRIRQKSNLSSRSL HHHHHHCCCCCCCCE | 25561503 | ||
374 | Phosphorylation | IRQKSNLSSRSLALP HHHCCCCCCCCEEEE | 25561503 | ||
375 | Phosphorylation | RQKSNLSSRSLALPV HHCCCCCCCCEEEEC | 25561503 | ||
377 | Phosphorylation | KSNLSSRSLALPVSE CCCCCCCCEEEECCC | 29654922 | ||
383 | Phosphorylation | RSLALPVSESPLSVR CCEEEECCCCCCEEE | 27288362 | ||
385 | Phosphorylation | LALPVSESPLSVRAN EEEECCCCCCEEEEC | 27288362 | ||
388 | Phosphorylation | PVSESPLSVRANGGE ECCCCCCEEEECCCC | 27288362 | ||
397 | Phosphorylation | RANGGEKTTHTSKDS EECCCCCCCCCCCCC | 23776212 | ||
398 | Phosphorylation | ANGGEKTTHTSKDSA ECCCCCCCCCCCCCH | 23776212 | ||
400 | Phosphorylation | GGEKTTHTSKDSAED CCCCCCCCCCCCHHH | 23776212 | ||
401 | Phosphorylation | GEKTTHTSKDSAEDI CCCCCCCCCCCHHHC | 23776212 | ||
404 | Phosphorylation | TTHTSKDSAEDIPGS CCCCCCCCHHHCCCC | 23776212 | ||
411 | Phosphorylation | SAEDIPGSSFNLVPT CHHHCCCCCCCCCCC | 23776212 | ||
412 | Phosphorylation | AEDIPGSSFNLVPTK HHHCCCCCCCCCCCC | 23776212 | ||
418 | Phosphorylation | SSFNLVPTKSSEMAS CCCCCCCCCCHHHHH | 23776212 | ||
477 | Phosphorylation | LPEKKANSPDSSYQK CCHHHCCCCCCHHHH | 23776212 | ||
480 | Phosphorylation | KKANSPDSSYQKQEI HHCCCCCCHHHHHHH | 23776212 | ||
481 | Phosphorylation | KANSPDSSYQKQEIS HCCCCCCHHHHHHHH | 23776212 | ||
482 | Phosphorylation | ANSPDSSYQKQEISR CCCCCCHHHHHHHHH | 23776212 | ||
488 | Phosphorylation | SYQKQEISRESVSRE HHHHHHHHHHHHHHH | 25561503 | ||
491 | Phosphorylation | KQEISRESVSREVLA HHHHHHHHHHHHHHH | 30407730 | ||
493 | Phosphorylation | EISRESVSREVLAQS HHHHHHHHHHHHHHH | 25561503 | ||
510 | Phosphorylation | TGDAVDGTSKTGSSK CCCCCCCCCCCCCCC | 23572148 | ||
511 | Phosphorylation | GDAVDGTSKTGSSKD CCCCCCCCCCCCCCC | 23572148 | ||
661 | Phosphorylation | ISSGKPTSEEKRIPL CCCCCCCCHHHCCCC | 23111157 | ||
682 | Phosphorylation | AAVFPNISFSPPATG CCCCCCCCCCCCCCC | 23111157 | ||
706 | Phosphorylation | ADIKLEKTSSTAFGV CCEEEEECCCCCCCC | 27288362 | ||
707 | Phosphorylation | DIKLEKTSSTAFGVS CEEEEECCCCCCCCC | 27288362 | ||
708 | Phosphorylation | IKLEKTSSTAFGVSE EEEEECCCCCCCCCH | 27288362 | ||
709 | Phosphorylation | KLEKTSSTAFGVSEA EEEECCCCCCCCCHH | 27288362 |
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 NUP1_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NUP1_ARATH !! |
* 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 NUP1_ARATH !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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