UniProt ID | NU155_RAT | |
---|---|---|
UniProt AC | P37199 | |
Protein Name | Nuclear pore complex protein Nup155 | |
Gene Name | Nup155 | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 1390 | |
Subcellular Localization |
Nucleus, nuclear pore complex . Nucleus membrane Peripheral membrane protein Cytoplasmic side . Nucleus membrane Peripheral membrane protein Nucleoplasmic side . In mitosis, assumes a diffuse cytoplasmic distribution probably as a monomer, be |
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Protein Description | Essential component of nuclear pore complex. Could be essessential for embryogenesis (By similarity). Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport.. | |
Protein Sequence | MPSMLGSMMVASTSAPSLQEALENAGRLIDRQLQEDRMYPDLSELLMVSAPNSPTVSGMSDMDYPLQGPGLLSVPSLPEISTIRRVPLRLSWLNSLDTCSVTAMMGVFPPISRAWLTIDSDIFMWNYEDGGDLAYFDGLSETILAVGLVKPKAGIFQPHVRHLLVLATPVDIVILGLSYANVQTGSGILNDSVCGGLQLLPDPLYSLPTDNTYLLTITSTDNGRIFLAGKDGCLYEVAYQAEAGWFSQRCRKINHSKSSLSFLVPSLLQFTFSEDDPIVQIEIDNSRNILYTRSEKGVIQVYDLGHDGQGMSRVASVSQNAIVCAAGNIARTIDRSVFKPIVQIAVIENSESLDCQLLAVTHAGVRLYFSTCPFRQPLARPNTLTLVHVRLPPGFSASSTVEKPSKVHKALYSKGILLMTASENEDNDILWCVNHDTFPFQKPMMETQMTTRVDGHSWALSAIDELKVDKIITPLNKDHIPITDSPVVVQQHMLPPKKFVLLSAQGSLMFHKLRPVDQLRHLLVSNVGGDGEEIERFFKLHQEDQACATCLILACSTAACDREVSAWATRAFFRYGGEAQMRFPATLPTPSNVGPILGSPMYSSSPVPTGSPYPNPSSLGTPSHGAQPPTMSTPMSAVGNPAMQAASLSGLTGPEIVYSGKHNGICIYFSRIMGNIWDASLVVERVFKSSNREITAIESSVPIQLLESVLQELKGLQEFLDRNSQFSGGPLGNPNTTAKVQQRLLGVMRPENGNTQQMQQELQRKFHEAQLSEKISLQAIQQLVRKSYQALALWKLLCEHQFTVIVGELQKEFQEQLKITTFKDLVIREKEVTGALIASLINCYIRDNAAVDGISLHLQDTCPLLYSTDDAVCSKANELLQRSRQVQSKSERERMLRESLKEYQKISNQVDLPSVCAQYRQVRFYEGVVELSLTAAEKKDPQGLGLHFYKHGEPEEDVVGLQTFQERLNSYKCITDTLQELVNQSKAAPQSPSVPKKPGPPVLSSDPNMLSNEEAGHHFEQMLKLAQRSKDELFSIALYNWLIQADLADKLLQIASPFLEPHLVRMAKVDQNRVRYMDLLWRYYEKNRSFSSAARVLSKLADMHSTEISLQQRLEYIARAILSAKSSTAISSIAADGEFLHELEEKMEVARIQLQIQETLQRQYSHHSSVQDAISQLDSELMDITKLYGEFADPFKLAECKLAIIHCAGYSDPILVHTLWQDIIEKELSDSVTLSSSDRMHALSLKLVLLGKIYAGTPRFFPLDFIVQFLEQQVCTLNWDVGFVIQTMNEIGVPLPRLLEVYDQLFKSRDPFWNRVKSPLHLLDCIHVLLTRYVENPSLVLNCERRRFTNLCLDAVCGYLVELQSMSSSVAVQAITGNFKSLQAKLERLH | |
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 |
---|---|---|---|---|---|
525 | O-linked_Glycosylation | QLRHLLVSNVGGDGE HHHHHHHHCCCCCHH | 26.26 | 12438562 | |
739 | Ubiquitination | GNPNTTAKVQQRLLG CCCCCHHHHHHHHHC | 38.18 | - | |
903 | Phosphorylation | LRESLKEYQKISNQV HHHHHHHHHHHHHCC | 17.33 | - | |
991 | Phosphorylation | QSKAAPQSPSVPKKP HHCCCCCCCCCCCCC | 20.34 | 29779826 | |
993 | Phosphorylation | KAAPQSPSVPKKPGP CCCCCCCCCCCCCCC | 57.19 | 27097102 | |
997 | Acetylation | QSPSVPKKPGPPVLS CCCCCCCCCCCCCCC | 49.49 | 22902405 | |
1056 | Phosphorylation | DKLLQIASPFLEPHL HHHHHHHHHHCCHHH | 20.15 | - | |
1105 | Phosphorylation | SKLADMHSTEISLQQ HHHHCCCCCCCCHHH | 22.54 | 25575281 | |
1106 | Phosphorylation | KLADMHSTEISLQQR HHHCCCCCCCCHHHH | 23.74 | 25575281 | |
1109 | Phosphorylation | DMHSTEISLQQRLEY CCCCCCCCHHHHHHH | 17.56 | 25575281 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of NU155_RAT !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NU155_RAT !! |
* 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 NU155_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of NU155_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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O-linked Glycosylation | |
Reference | PubMed |
"Mapping sites of O-GlcNAc modification using affinity tags for serineand threonine post-translational modifications."; Wells L., Vosseller K., Cole R.N., Cronshaw J.M., Matunis M.J.,Hart G.W.; Mol. Cell. Proteomics 1:791-804(2002). Cited for: GLYCOSYLATION AT SER-525. |