UniProt ID | NED1_SCHPO | |
---|---|---|
UniProt AC | Q9UUJ6 | |
Protein Name | Nuclear elongation and deformation protein 1 | |
Gene Name | ned1 | |
Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
Sequence Length | 656 | |
Subcellular Localization | ||
Protein Description | May have a role in the maintenance of the nuclear envelope structure and in minichromosome stability.. | |
Protein Sequence | MQYVGRAFDSVTKTWNAINPSTLSGAIDVIVVEQEDKTLACSPFHVRFGKFSLLLPSDKKVEFSVNGQLTGFNMKLGDGGEAFFVFATENAVPRELQTSPIVSPTTSPKQTPSINVTEPQDLELDKVSQDHEKDQSNTYLMEDGYEFPLTRDLIRRSKSDADQTPPTGFKHLRHSSCLEMAGSDRTPSMPATTLADLRLLQKAKELGKRLSGKELPTRVGDNGDVMLDMTGYKSSAANINIAELARETFKDEFPMIEKLLREDEEGNLWFHASEDAKKFAEVYGHSPPASPSRTPASPKSDSALMDEDSDLSRRHSLSEQSLSPVSESYPQYAKTLRLTSDQLRSLNLKPGKNELSFGVNGGKAICTANLFFWKHNDPVVISDIDGTITKSDALGHMFTLIGKDWTHAGVAKLYTDITNNGYKIMYLTSRSVGQADSTRHYLRNIEQNGYSLPDGPVILSPDRTMAALHREVILRKPEVFKMACLRDLCNIFALPVPRTPFYAGFGNRITDAISYNHVRVPPTRIFTINSAGEVHIELLQRSGHRSSYVYMNELVDHFFPPIEVSTRDEVSSFTDVNFWRSPLLELSDEEEDDTNKSTSKSPKTPKNTKFGYQEFEGIDEEDAQDYSPSPLIKSFNELMFEGEEDEEGEEDVENAV | |
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 |
---|---|---|---|---|---|
98 | Phosphorylation | AVPRELQTSPIVSPT CCCCHHCCCCCCCCC | 49.44 | 29996109 | |
99 | Phosphorylation | VPRELQTSPIVSPTT CCCHHCCCCCCCCCC | 10.32 | 28889911 | |
103 | Phosphorylation | LQTSPIVSPTTSPKQ HCCCCCCCCCCCCCC | 19.76 | 28889911 | |
105 | Phosphorylation | TSPIVSPTTSPKQTP CCCCCCCCCCCCCCC | 32.19 | 24763107 | |
106 | Phosphorylation | SPIVSPTTSPKQTPS CCCCCCCCCCCCCCC | 46.55 | 28889911 | |
107 | Phosphorylation | PIVSPTTSPKQTPSI CCCCCCCCCCCCCCC | 32.36 | 28889911 | |
113 | Phosphorylation | TSPKQTPSINVTEPQ CCCCCCCCCCCCCCC | 30.13 | 28889911 | |
157 | Phosphorylation | TRDLIRRSKSDADQT CHHHHHHCCCCCCCC | 27.02 | 29996109 | |
159 | Phosphorylation | DLIRRSKSDADQTPP HHHHHCCCCCCCCCC | 39.00 | 28889911 | |
164 | Phosphorylation | SKSDADQTPPTGFKH CCCCCCCCCCCCCHH | 31.61 | 29996109 | |
175 | Phosphorylation | GFKHLRHSSCLEMAG CCHHHCCCHHHHHCC | 19.13 | 29996109 | |
176 | Phosphorylation | FKHLRHSSCLEMAGS CHHHCCCHHHHHCCC | 19.32 | 25720772 | |
283 | Phosphorylation | AKKFAEVYGHSPPAS HHHHHHHHCCCCCCC | 10.71 | 25720772 | |
286 | Phosphorylation | FAEVYGHSPPASPSR HHHHHCCCCCCCCCC | 28.37 | 28889911 | |
290 | Phosphorylation | YGHSPPASPSRTPAS HCCCCCCCCCCCCCC | 29.22 | 28889911 | |
292 | Phosphorylation | HSPPASPSRTPASPK CCCCCCCCCCCCCCC | 46.41 | 21712547 | |
294 | Phosphorylation | PPASPSRTPASPKSD CCCCCCCCCCCCCCC | 27.78 | 21712547 | |
297 | Phosphorylation | SPSRTPASPKSDSAL CCCCCCCCCCCCCCC | 33.78 | 24763107 | |
300 | Phosphorylation | RTPASPKSDSALMDE CCCCCCCCCCCCCCC | 39.93 | 29996109 | |
302 | Phosphorylation | PASPKSDSALMDEDS CCCCCCCCCCCCCCC | 30.32 | 29996109 | |
312 | Phosphorylation | MDEDSDLSRRHSLSE CCCCCCHHHHHCCCH | 32.05 | 29996109 | |
316 | Phosphorylation | SDLSRRHSLSEQSLS CCHHHHHCCCHHCCC | 31.60 | 28889911 | |
318 | Phosphorylation | LSRRHSLSEQSLSPV HHHHHCCCHHCCCCC | 36.28 | 28889911 | |
321 | Phosphorylation | RHSLSEQSLSPVSES HHCCCHHCCCCCCCC | 27.11 | 28889911 | |
572 | Phosphorylation | STRDEVSSFTDVNFW ECCCCCCCCCCCCCC | 37.02 | 25720772 | |
587 | Phosphorylation | RSPLLELSDEEEDDT CCCCCCCCCCCCCCC | 33.33 | 12376568 | |
594 | Phosphorylation | SDEEEDDTNKSTSKS CCCCCCCCCCCCCCC | 57.79 | 25720772 | |
597 | Phosphorylation | EEDDTNKSTSKSPKT CCCCCCCCCCCCCCC | 39.73 | 25720772 | |
601 | Phosphorylation | TNKSTSKSPKTPKNT CCCCCCCCCCCCCCC | 31.25 | 25720772 | |
626 | Phosphorylation | DEEDAQDYSPSPLIK CHHHHCCCCCCHHHH | 15.48 | 21712547 | |
627 | Phosphorylation | EEDAQDYSPSPLIKS HHHHCCCCCCHHHHH | 27.47 | 21712547 | |
629 | Phosphorylation | DAQDYSPSPLIKSFN HHCCCCCCHHHHHHH | 26.80 | 21712547 |
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 NED1_SCHPO !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NED1_SCHPO !! |
* 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 NED1_SCHPO !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
RCC1_SCHPO | pim1 | genetic | 12376568 | |
SPI1_SCHPO | spi1 | genetic | 12376568 | |
DIS3_SCHPO | dis3 | physical | 12376568 | |
RCC1_SCHPO | pim1 | physical | 12376568 | |
NU189_SCHPO | nup189 | physical | 12376568 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Phosphoproteome analysis of fission yeast."; Wilson-Grady J.T., Villen J., Gygi S.P.; J. Proteome Res. 7:1088-1097(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-103; THR-106;SER-107; SER-159; SER-286; SER-318; SER-321 AND SER-587, AND MASSSPECTROMETRY. |