NSP1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NSP1_SCHPO
• UniProt AC: Q10168
• Protein Name: Nucleoporin nsp1
• Gene Name: nsp1
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 598
• Subcellular Localization: Nucleus, nuclear pore complex . Nucleus membrane ; Peripheral membrane protein ; Cytoplasmic side . Nucleus membrane ; Peripheral membrane protein ; Nucleoplasmic side .
• 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. Appears to have a role in the formation of the septum..
• Protein Sequence: MSFNPGNNQNSGFSFGKPAQPNSAAQGAATPAATGLFGNTNNNTSSTAPSGGLFGSNNASNTSAPSTFSFGKAATTGNSTNASTSSPFSFGSTNTNNTAGAKPLFGGLGSTGSANSTGDKSKNTASSATGAATTNPSGSTFNFGSSNNSFNFGKPASTTNTTTPAAASTGSLFGKPAATGTTSNAPPASSTSTTPATGSGGFSFGKPASLGSTNNASTSTTANSGFSFGKPATTSAPGSNTTVTPSSSITGTNDSKPAASNTGSAPTTGFSFGKPAGQAASTATDKGTTTTSSAGTGFSFGKPATTEDTNKPTAPNSAFTKPATSTGDNKPTFSFGNTSKPTENTSTTATSAPPLSNNTKPAEGANQTSSGFSFGKPATDTTTSTSKTGPLFGNKPADPSAKPGATASTTPSEPPPSSIKHKTLQEILNKWSTDLTTQTEVFNKLCDQVSDWDRTLVDNGALISKLYTETVEAEQMSNRIDDGLEYVSSSQQELFKLLDSYETQLETFDGRATSALNVERERAFGVADDILSRLDRLGEDLGTVINQMNDFSKPDDSISEIVKVLNAQLASLGWVENRIFQMEEKLDTIKKKNSDVLF

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
2	Phosphorylation	------MSFNPGNNQ ------CCCCCCCCC	33.46	24763107
113	Phosphorylation	GGLGSTGSANSTGDK CCCCCCCCCCCCCCC	25.10	24763107
117	Phosphorylation	STGSANSTGDKSKNT CCCCCCCCCCCCCCC	49.56	27738172
168	Phosphorylation	TTTPAAASTGSLFGK CCCCCHHHCCCCCCC	28.68	24763107
169	Phosphorylation	TTPAAASTGSLFGKP CCCCHHHCCCCCCCC	26.51	24763107
244	Phosphorylation	PGSNTTVTPSSSITG CCCCCEECCCHHCCC	18.50	24763107
246	Phosphorylation	SNTTVTPSSSITGTN CCCEECCCHHCCCCC	27.61	24763107
264	Phosphorylation	PAASNTGSAPTTGFS CCCCCCCCCCCCCCC	29.09	27738172
320	Phosphorylation	TAPNSAFTKPATSTG CCCCCCCCCCCCCCC	35.52	24763107
408	Phosphorylation	AKPGATASTTPSEPP CCCCCCCCCCCCCCC	28.58	27738172
488	Phosphorylation	DDGLEYVSSSQQELF CHHHHHCCHHHHHHH	24.30	25720772
489	Phosphorylation	DGLEYVSSSQQELFK HHHHHCCHHHHHHHH	23.32	28889911
490	Phosphorylation	GLEYVSSSQQELFKL HHHHCCHHHHHHHHH	28.51	28889911
500	Phosphorylation	ELFKLLDSYETQLET HHHHHHHHHHHHHHH	25.49	25720772
557	Phosphorylation	DFSKPDDSISEIVKV CCCCCCCCHHHHHHH	35.08	29996109
559	Phosphorylation	SKPDDSISEIVKVLN CCCCCCHHHHHHHHH	25.81	29996109
594	Phosphorylation	DTIKKKNSDVLF--- HHHHHHCCCCCC---	37.67	25720772

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

Oops, there are no upstream regulatory protein records of NSP1_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NSP1_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NSP1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NUP44_SCHPO	nup44	physical	26771498

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-489 AND SER-490, ANDMASS SPECTROMETRY.
PubMed: 18257517