NU155_RAT - dbPTM
NU155_RAT - PTM Information in dbPTM
Basic Information of Protein
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
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
525O-linked_GlycosylationQLRHLLVSNVGGDGE
HHHHHHHHCCCCCHH
26.2612438562
739UbiquitinationGNPNTTAKVQQRLLG
CCCCCHHHHHHHHHC
38.18-
903PhosphorylationLRESLKEYQKISNQV
HHHHHHHHHHHHHCC
17.33-
991PhosphorylationQSKAAPQSPSVPKKP
HHCCCCCCCCCCCCC
20.3429779826
993PhosphorylationKAAPQSPSVPKKPGP
CCCCCCCCCCCCCCC
57.1927097102
997AcetylationQSPSVPKKPGPPVLS
CCCCCCCCCCCCCCC
49.4922902405
1056PhosphorylationDKLLQIASPFLEPHL
HHHHHHHHHHCCHHH
20.15-
1105PhosphorylationSKLADMHSTEISLQQ
HHHHCCCCCCCCHHH
22.5425575281
1106PhosphorylationKLADMHSTEISLQQR
HHHCCCCCCCCHHHH
23.7425575281
1109PhosphorylationDMHSTEISLQQRLEY
CCCCCCCCHHHHHHH
17.5625575281

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 NU155_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NU155_RAT !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NU155_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NU155_RAT

loading...

Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"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.

TOP