UniProt ID | NUP50_MOUSE | |
---|---|---|
UniProt AC | Q9JIH2 | |
Protein Name | Nuclear pore complex protein Nup50 | |
Gene Name | Nup50 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 466 | |
Subcellular Localization |
Nucleus, nuclear pore complex. Nucleus membrane Peripheral membrane protein Nucleoplasmic side . Localizes to the nucleoplasmic fibrils of the nuclear pore complex. Dissociates from the NPC structure early during prophase of mitosis. Associates w |
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Protein Description | Component of the nuclear pore complex that has a direct role in nuclear protein import. [PubMed: 10811608 Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling] | |
Protein Sequence | MAKRVAEKELTDRNWDEEDEVEEMGTFSVASEEVMKNRAVKKAKRRNVGFESDSGGAFKGFKGLVVPSGGGGFSGFGGSGGKPLEGLTNGNSTDNATPFSNVKTAAEPKAAFGSFAVNGPTTLVDKKISSPKCNNSNQPPSSGPASSTACPGNAYHKQLAGLNCSVRDWIVKHVNTNPLCDLTPIFKDYERYLATIEKQLENGGGSSSESQTDRATAGMEPPSLFGSTKLQQESPFSFHGNKAEDTSEKVEFTAEKKSDAAQGATSASFSFGKKIESSALGSLSSGSLTGFSFSAGSSSLFGKDAAQSKAASSLFSAKASESPAGGGSSECRDGEEEENDEPPKVVVTEVKEEDAFYSKKCKLFYKKDNEFKEKGVGTLHLKPTATQKTQLLVRADTNLGNILLNVLIAPNMPCTRTGKNNVLIVCVPNPPLDEKQPTLPATMLIRVKTSEDADELHKILLEKKDA | |
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 |
---|---|---|---|---|---|
8 | Acetylation | MAKRVAEKELTDRNW CCCCHHHHHHCCCCC | 48.57 | 23806337 | |
52 | Phosphorylation | RRNVGFESDSGGAFK HCCCCCCCCCCCCCC | 34.51 | 26525534 | |
54 | Phosphorylation | NVGFESDSGGAFKGF CCCCCCCCCCCCCCC | 48.70 | 26643407 | |
59 | Ubiquitination | SDSGGAFKGFKGLVV CCCCCCCCCCCEEEE | 64.00 | 22790023 | |
59 | Acetylation | SDSGGAFKGFKGLVV CCCCCCCCCCCEEEE | 64.00 | 22826441 | |
82 | Acetylation | GFGGSGGKPLEGLTN CCCCCCCCCCCCCCC | 50.37 | - | |
104 | Phosphorylation | TPFSNVKTAAEPKAA CCCCCCCCCCCCCHH | 27.15 | 18779572 | |
114 | Phosphorylation | EPKAAFGSFAVNGPT CCCHHHCCCEECCCC | 11.99 | 17203969 | |
121 | Phosphorylation | SFAVNGPTTLVDKKI CCEECCCCEEEECCC | 33.87 | 17203969 | |
122 | Phosphorylation | FAVNGPTTLVDKKIS CEECCCCEEEECCCC | 28.11 | 17203969 | |
126 | Acetylation | GPTTLVDKKISSPKC CCCEEEECCCCCCCC | 44.52 | 23806337 | |
129 | Phosphorylation | TLVDKKISSPKCNNS EEEECCCCCCCCCCC | 49.85 | 26160508 | |
130 | Phosphorylation | LVDKKISSPKCNNSN EEECCCCCCCCCCCC | 31.67 | 26160508 | |
136 | Phosphorylation | SSPKCNNSNQPPSSG CCCCCCCCCCCCCCC | 23.89 | 26160508 | |
172 | Acetylation | SVRDWIVKHVNTNPL CHHHHHHHHCCCCCC | 32.47 | 22826441 | |
208 | Phosphorylation | ENGGGSSSESQTDRA HCCCCCCCHHHHHHH | 42.86 | - | |
216 | Phosphorylation | ESQTDRATAGMEPPS HHHHHHHCCCCCCCH | 25.33 | 29514104 | |
229 | Ubiquitination | PSLFGSTKLQQESPF CHHHCCCCCEECCCC | 46.10 | 22790023 | |
234 | Phosphorylation | STKLQQESPFSFHGN CCCCEECCCCCCCCC | 27.23 | 27087446 | |
237 | Phosphorylation | LQQESPFSFHGNKAE CEECCCCCCCCCCCC | 21.51 | 25159016 | |
246 | Phosphorylation | HGNKAEDTSEKVEFT CCCCCCCCCCCEEEE | 30.23 | - | |
257 | Acetylation | VEFTAEKKSDAAQGA EEEEEECCCHHHCCC | 45.10 | 22826441 | |
265 | Phosphorylation | SDAAQGATSASFSFG CHHHCCCCEEEEECC | 31.48 | 25338131 | |
268 | Phosphorylation | AQGATSASFSFGKKI HCCCCEEEEECCCCC | 22.61 | - | |
273 | Acetylation | SASFSFGKKIESSAL EEEEECCCCCCCCCC | 48.87 | 22826441 | |
273 | Ubiquitination | SASFSFGKKIESSAL EEEEECCCCCCCCCC | 48.87 | 22790023 | |
294 | Phosphorylation | SLTGFSFSAGSSSLF CCCCEEEECCCHHHC | 30.44 | - | |
312 | Phosphorylation | AAQSKAASSLFSAKA HHHHHHHHHHHHCCC | 32.22 | 27600695 | |
313 | Phosphorylation | AQSKAASSLFSAKAS HHHHHHHHHHHCCCC | 28.80 | 21183079 | |
320 | Phosphorylation | SLFSAKASESPAGGG HHHHCCCCCCCCCCC | 37.59 | 28066266 | |
322 | Phosphorylation | FSAKASESPAGGGSS HHCCCCCCCCCCCCC | 19.97 | 25263469 | |
328 | Phosphorylation | ESPAGGGSSECRDGE CCCCCCCCCCCCCCC | 26.66 | 26745281 | |
329 | Phosphorylation | SPAGGGSSECRDGEE CCCCCCCCCCCCCCC | 43.95 | 26745281 | |
382 | Ubiquitination | GVGTLHLKPTATQKT CCEEEEECCCCCCCE | 29.58 | 27667366 | |
397 | Phosphorylation | QLLVRADTNLGNILL EEEEECCCCHHHHHH | 31.21 | 25890499 | |
417 | Phosphorylation | PNMPCTRTGKNNVLI CCCCCCCCCCCCEEE | 34.06 | 25890499 | |
448 | Acetylation | ATMLIRVKTSEDADE EEEEEEEECCCCHHH | 36.16 | 23806337 |
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 NUP50_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NUP50_MOUSE !! |
* 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 NUP50_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CDN1B_MOUSE | Cdkn1b | physical | 10811608 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY. |