dbPTM

NBP1_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NBP1_YEAST
UniProt AC	P52919
Protein Name	NAP1-binding protein
Gene Name	NBP1
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	319
Subcellular Localization
Protein Description
Protein Sequence	MLKSVQGLWKDFFGIRDDGRKREYGSLDEVRKRSALRSRRKQMRPTGKSVLKRPRKVTDRKTEEKIRTNRRKTPKRRLTKIFQTIRDVFSNDNENMSKMQNVCGDMTRILKKRSQGRPSYMDTDTAKSRILRSDAFKRKISELKYNKQRISELRSGSSDGSSGKDRNQSLYLDREILLQRQIKKRDEKIKALESKLQSLQEALNYSNEKYRILEDLLDSSNIHPSYTKSRRTMSNLARENDEIKPLKIDLSPSPIRRTNSLFTSSPMKTYNRDGNIPEMQPLQENISPACPTPPYRSRETEKEDETLSPISVDFSSYLS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
34	Phosphorylation	LDEVRKRSALRSRRK HHHHHHHHHHHHHHH	34.39	21700874
38	Phosphorylation	RKRSALRSRRKQMRP HHHHHHHHHHHHCCC	36.97	21700874
46	Phosphorylation	RRKQMRPTGKSVLKR HHHHCCCCCHHHHCC	47.04	21700874
73	Phosphorylation	IRTNRRKTPKRRLTK HHHCCCCCCHHHHHH	32.03	28889911
90	Phosphorylation	QTIRDVFSNDNENMS HHHHHHHCCCCCCHH	43.02	27017623
97	Phosphorylation	SNDNENMSKMQNVCG CCCCCCHHHHHHHHH	36.24	27017623
119	Phosphorylation	KRSQGRPSYMDTDTA HHHCCCCCCCCCHHH	31.56	21700874
120	Phosphorylation	RSQGRPSYMDTDTAK HHCCCCCCCCCHHHH	11.16	21700874
123	Phosphorylation	GRPSYMDTDTAKSRI CCCCCCCCHHHHHHH	20.79	21700874
125	Phosphorylation	PSYMDTDTAKSRILR CCCCCCHHHHHHHHC	37.77	21700874
133	Phosphorylation	AKSRILRSDAFKRKI HHHHHHCCHHHHHHH	29.82	21700874
141	Phosphorylation	DAFKRKISELKYNKQ HHHHHHHHHHHHCHH	39.65	21700874
145	Phosphorylation	RKISELKYNKQRISE HHHHHHHHCHHHHHH	39.97	21700874
155	Phosphorylation	QRISELRSGSSDGSS HHHHHHHCCCCCCCC	56.50	21700874
162	Phosphorylation	SGSSDGSSGKDRNQS CCCCCCCCCCCCCCH	56.23	21700874
169	Phosphorylation	SGKDRNQSLYLDREI CCCCCCCHHHHCHHH	23.64	21700874
205	Phosphorylation	SLQEALNYSNEKYRI HHHHHHCCCHHHHHH	17.45	21700874
219	Phosphorylation	ILEDLLDSSNIHPSY HHHHHHHCCCCCCCH	25.84	21700874
220	Phosphorylation	LEDLLDSSNIHPSYT HHHHHHCCCCCCCHH	39.20	23749301
225	Phosphorylation	DSSNIHPSYTKSRRT HCCCCCCCHHHHHHH	31.13	21700874
226	Phosphorylation	SSNIHPSYTKSRRTM CCCCCCCHHHHHHHH	23.72	21700874
227	Phosphorylation	SNIHPSYTKSRRTMS CCCCCCHHHHHHHHH	27.21	27017623
234	Phosphorylation	TKSRRTMSNLAREND HHHHHHHHHHHHCCC	28.25	17287358
251	Phosphorylation	KPLKIDLSPSPIRRT CCCEEECCCCCCCCC	21.42	22369663
253	Phosphorylation	LKIDLSPSPIRRTNS CEEECCCCCCCCCCC	29.59	22369663
258	Phosphorylation	SPSPIRRTNSLFTSS CCCCCCCCCCCCCCC	21.22	22369663
260	Phosphorylation	SPIRRTNSLFTSSPM CCCCCCCCCCCCCCC	25.01	22369663
263	Phosphorylation	RRTNSLFTSSPMKTY CCCCCCCCCCCCCCC	33.32	22369663
264	Phosphorylation	RTNSLFTSSPMKTYN CCCCCCCCCCCCCCC	25.72	22369663
265	Phosphorylation	TNSLFTSSPMKTYNR CCCCCCCCCCCCCCC	26.42	22369663
287	Phosphorylation	QPLQENISPACPTPP CCCCCCCCCCCCCCC	20.30	21440633
292	Phosphorylation	NISPACPTPPYRSRE CCCCCCCCCCCCCCC	36.46	28152593
295	Phosphorylation	PACPTPPYRSRETEK CCCCCCCCCCCCCCC	23.56	21440633
308	Phosphorylation	EKEDETLSPISVDFS CCCCCCCCCCEECHH	27.83	21700874
315	Phosphorylation	SPISVDFSSYLS--- CCCEECHHHHCC---	17.38	21700874

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 NBP1_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NBP1_YEAST !!

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 NBP1_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NAP1_YEAST	NAP1	physical	10767562
NBP1_YEAST	NBP1	physical	16436507
MPS2_YEAST	MPS2	physical	16436507
BBP1_YEAST	BBP1	physical	16436507
SXM1_YEAST	SXM1	physical	21785410
IMB4_YEAST	KAP123	physical	21785410
GRP78_YEAST	KAR2	physical	21785410
MPS3_YEAST	MPS3	physical	21785410
NOG1_YEAST	NOG1	physical	21785410
NOP2_YEAST	NOP2	physical	21785410
NUG1_YEAST	NUG1	physical	21785410
PABP_YEAST	PAB1	physical	21785410
NBP1_YEAST	NBP1	physical	20139001

Drug and Disease Associations

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

Regulatory Network of NBP1_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251 AND SER-260, ANDMASS SPECTROMETRY.	18407956 [Abstract]
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND MASSSPECTROMETRY.	17287358 [Abstract]