dbPTM

NUP45_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NUP45_SCHPO
UniProt AC	Q09793
Protein Name	Nucleoporin nup45
Gene Name	nup45
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	425
Subcellular Localization	Cytoplasm. Nucleus, nuclear pore complex.
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	MFGLNKTPSFGSTGTQNQNTGTSAGTGLFSSNTFGNNTQANTPASTGFGGVTGGAFGQTKPQTGGSLFGNKPNATSTTPGLNLFGQNPQAAPGGSLFGASTTKPQAPGGLFNQNQTQAQPAQAAPTGGLFGLSGQNQTQSQTQPAQANTSLFGQSNIGTTGGLFDQNRPNTSTFGQFSTQPASAGLFGQSTQPSGSTGFGLSNNTQTTPFFSAAQQQPSTTQLPSNPAINATTRYSSLNANTQKFLDDLDKEIFSQIQLAEELQTKLGTVSELVESVPNDVAEVQRRLSSVSTALLIDSDEIETTKRVVDEDTSNARISSRILDVFKTPGATYPFASNDPLMNYFEQFTENAKKRTDLYAATIGELEQHLEQVETTPQNNSPEALLKTIKEEHKLFMALSNRFAQVHDEVKRLQVNTSTSLPFIS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	PSFGSTGTQNQNTGT CCCCCCCCCCCCCCC	25.16	27738172
289	Phosphorylation	AEVQRRLSSVSTALL HHHHHHHHCCCCEEE	27.21	28889911
290	Phosphorylation	EVQRRLSSVSTALLI HHHHHHHCCCCEEEE	25.36	28889911
292	Phosphorylation	QRRLSSVSTALLIDS HHHHHCCCCEEEECC	15.20	29996109
293	Phosphorylation	RRLSSVSTALLIDSD HHHHCCCCEEEECCC	21.11	29996109
381	Phosphorylation	ETTPQNNSPEALLKT HCCCCCCCHHHHHHH	31.50	29996109
417	Phosphorylation	VKRLQVNTSTSLPFI HHHCCCCCCCCCCCC	34.23	21712547
418	Phosphorylation	KRLQVNTSTSLPFIS HHCCCCCCCCCCCCC	15.70	24763107
420	Phosphorylation	LQVNTSTSLPFIS-- CCCCCCCCCCCCC--	33.54	24763107

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 NUP45_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NUP45_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 NUP45_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
ALP7_SCHPO	alp7	physical	26771498
AFG2_SCHPO	SPBC56F2.07c	physical	26771498

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NUP45_SCHPO

Related Literatures of Post-Translational Modification

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-289 AND SER-290, ANDMASS SPECTROMETRY.	18257517 [Abstract]