NU211_SCHPO - dbPTM
NU211_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NU211_SCHPO
UniProt AC O74424
Protein Name Nucleoporin nup211
Gene Name nup211
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1837
Subcellular Localization Cytoplasm . Nucleus . Nuclear rim.
Protein Description Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope..
Protein Sequence MHDSSWTEADILGVCSFLDIPKTKIDPLLQVDAFTSILIPLISKSKDYESIKNDRIVTEVNYEQQLRNSEKKLLQSNERYDLLEDERKLLENELSQIKEYLREKSSSYDTVLHDCSSLKSVNEALKQAQDQNLKQTAQLQNLLSDKEKEVEKKITIIKDLKDALASSTHQVLELQHTQQEKASLQTNYEFELQKLTQKNSILENNNTWLSRELQGVNDKLLSLHQEASLEKSQLSSQLSDAVLEKDALQRKVSSLSQQFTESNLRYQNIVAELSEMRKQYEFSQVSFEKEISSQKQISELWMEKCEDCSLRLKELQNSNGELEKLLEAAQSSFEEQLESHKEAEASLKSQINFLEKEVSSLESQLKLANERLRHYDEIEISDMSELKYSNLLNNSMKGFKGQSSVSDLYSERLYYKQKYEQTCQEVERLQRSYNHVMEEANLQHPLVKEQFKRFAHMQREIVAMSEQYQKSLEDCQKAKSRYEQLETLFKDKCTENKHYEQETKDLARQVQVLLHELDLCENGIVLGVDSRKKINSYVEKSLTEDETDTDQIISSRLVVFRNIRELQQQNQNLLSAVHELADRMEKDEKPDLDGAEIQEETLIKANETIDQLTKMLEEVSDQLRYSLKERDFFRSLVQENEKLLDMAPATPNSKLNTNLIEQTSYQRSLIRLEQLTNELESLKSISRNKEKKFEEAISSLQLEKSNIQLQLTSLTSERSLALEKLNDLEKSLVLSERSKDELDESYKSLQEQLASKKIEVQNVSSQLSICNSQLEQSNHIVDNLKSENLLLTSVKDKLKADLSNLESKLSSLQQDNFHMKAQIESSNQEYTATVDSMNSRILELSNDLRVANSKLSECSDDVRRLTLQNSFDLREHQTLVLQLQSNITELKQDITLQRTVRNQLEIQTTELKERLKFMEERQENLQSKLIAANKDTTQNPDNVEVEAISIELERTKEKLRMAELEKSNIQQKYLASEKTLEMMNETHEQFKHLVESEISTREEKITSLRSELLDLNKRVEVLKEEKESSSKELAKQLEDAVREKDSALSFKKDYEKIRSDADRVITSLKEDIEKERSLMKECHSNYESEIVSHGRTTQKLRDLRTEFDEVNTKYLKLKANFEQQHSGLSGAEKDWNIQRKAMEDEISSLKDYILGLENQNKLLHSQFDSLSQQITVLQQNSSENLNISANLEAVQDNDLRELVSYLRHEKEIMDNKYELTILDNRGLNQQVKSLQSTVDSLQLELNRLQSLPVSNDQTDTPIISGSQEVQLLYESNSVLRKDNDAKLGKIQELEKEVEKLNASLNPLQTEINELKAEIGAKTASLNLMKEYNSRWKLRFQSVLNKYERVDPTQLEELKKNCEALEKEKQELETKLQETAKETDTFKQQVNSLNEEVENLKKEVEQANTKNTRLAAAWNEKCENLKKSSLTRFAHLKQELTNKNKELTSKNAENEAMQKEIESLKDSNHQLQESASSDAEQITKEQFEQLKSEKERTEKELADSKNELEHLQSEAVDADGKTEISNLEKEIHELRSDKEGLVQQVQNLSAELAALREHSPTQGSLENADEIARLRSQLESTKQYYEKEKETEILAARSELVAEKEKTKEELENQLNEKSQRIKELEEQAQKNSSENTHDNIDDMIKQQVEEKLKENSANFDVKLKKVVAETEFRSKAKISVYEKKTRDLQNKITQLEETIENLNKQLSNPEKTDESTSSVTETKPVTSKPTASKADVGQNATEASSAKREPSGKSLSARLQGTGKQKGVQRPAVSRPVPMKPDSGKLSITGASKRIATSKNAAQNAKELSSTAKSGSLKRQRDDANKGGSSSNQKKAK
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
188PhosphorylationKASLQTNYEFELQKL
HHHCCCCHHHHHHHH
25.9427738172
650PhosphorylationLLDMAPATPNSKLNT
HHHCCCCCCCCHHCC
23.1928889911
653PhosphorylationMAPATPNSKLNTNLI
CCCCCCCCHHCCCHH
39.4629996109
1473PhosphorylationSNHQLQESASSDAEQ
CCHHHHHHHCCCHHH
22.0821712547
1475PhosphorylationHQLQESASSDAEQIT
HHHHHHHCCCHHHHC
37.7224763107
1476PhosphorylationQLQESASSDAEQITK
HHHHHHCCCHHHHCH
40.3221712547
1482PhosphorylationSSDAEQITKEQFEQL
CCCHHHHCHHHHHHH
28.3721712547
1521PhosphorylationAVDADGKTEISNLEK
CCCCCCCHHHHHHHH
44.0424763107
1535PhosphorylationKEIHELRSDKEGLVQ
HHHHHHHCCCCHHHH
66.7024763107
1548PhosphorylationVQQVQNLSAELAALR
HHHHHHHHHHHHHHH
27.5229996109
1558PhosphorylationLAALREHSPTQGSLE
HHHHHHHCCCCCCCC
25.5328889911
1560PhosphorylationALREHSPTQGSLENA
HHHHHCCCCCCCCCH
48.8828889911
1563PhosphorylationEHSPTQGSLENADEI
HHCCCCCCCCCHHHH
23.7728889911

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 NU211_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NU211_SCHPO !!

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 NU211_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BIS1_SCHPObis1physical
23695164
NU211_SCHPOnup211physical
26771498
PRP45_SCHPOprp45physical
26771498
BIS1_SCHPObis1physical
26771498

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NU211_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-650; SER-1558; THR-1560AND SER-1563, AND MASS SPECTROMETRY.

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