SIP5_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SIP5_SCHPO
• UniProt AC: O74775
• Protein Name: Protein sip5
• Gene Name: sip5
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 554
• Subcellular Localization: Cytoplasm.
• Protein Description: May negatively regulate the snf1 kinase..
• Protein Sequence: MGNTIGKERQENDEELIQHLVQLVDGGFLDPQGVYSSAPAYKTNIVRKLMLERRLMPFYKGLDSYSKDWPADKVVEVVEKALGPHKSALLHCAIRQSRSLSVGNTRSLKRDSRGSSDHLLTRNRSNSTPGSISADYRTTAITTIYANAMECPICFLYYPSNFNYTRCCAQPICSECFVEIRRAEPHLPTVHANEPTPNEFDLISEPAKCPYCMTERFGVIYKPNPKLTPFSFNNNPDTLPSNIAPMGTLSKSSLPLHHIPWPPNQHIKFAHDDKNVVSTDFIHPDWQYKLERARRRALRRAANATLLNSHLLETGPANANANHNTDLSHDPTSHGGPRRTLSSRRQHYLANVEQLMLAEAIRQSLLDAQSNDSTNSLPSTEVSQPDSTNISNEQEIVQPQPTHTTNVALVEEINRPDSVESAITASSSIDTGNENETQEVNSDSLPQFVHQTMTQTNFQESSPSVAADETRVHNVDEYIEQQDLDELIHSPIASTNPFLADQFARSETVDLNAHICSPALSVSDDGVTATNKTQSSFPSVYEHQLKSNELERGH

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
101	Phosphorylation	IRQSRSLSVGNTRSL HHHCCCCCCCCCCCC	29.26	25720772
112	Phosphorylation	TRSLKRDSRGSSDHL CCCCCCCCCCCCCCC	42.44	29996109
115	Phosphorylation	LKRDSRGSSDHLLTR CCCCCCCCCCCCCCC	31.33	29996109
116	Phosphorylation	KRDSRGSSDHLLTRN CCCCCCCCCCCCCCC	31.69	25720772
125	Phosphorylation	HLLTRNRSNSTPGSI CCCCCCCCCCCCCCC	38.39	25720772
127	Phosphorylation	LTRNRSNSTPGSISA CCCCCCCCCCCCCCC	36.91	28889911
128	Phosphorylation	TRNRSNSTPGSISAD CCCCCCCCCCCCCCC	35.60	28889911
131	Phosphorylation	RSNSTPGSISADYRT CCCCCCCCCCCCCHH	17.99	25720772
133	Phosphorylation	NSTPGSISADYRTTA CCCCCCCCCCCHHCH	19.45	25720772
241	Phosphorylation	NNPDTLPSNIAPMGT CCCCCCCCCCCCCCC	43.94	21712547
248	Phosphorylation	SNIAPMGTLSKSSLP CCCCCCCCCCCCCCC	22.93	25720772
250	Phosphorylation	IAPMGTLSKSSLPLH CCCCCCCCCCCCCCC	30.26	21712547
478	Phosphorylation	RVHNVDEYIEQQDLD CCCCHHHHHHHCCHH	12.80	29996109
490	Phosphorylation	DLDELIHSPIASTNP CHHHHHCCCHHHCCH	15.82	29996109
517	Phosphorylation	DLNAHICSPALSVSD CCCCEECCCCCEECC	16.77	29996109
521	Phosphorylation	HICSPALSVSDDGVT EECCCCCEECCCCCC	22.98	25720772
523	Phosphorylation	CSPALSVSDDGVTAT CCCCCEECCCCCCCC	26.97	29996109
533	Phosphorylation	GVTATNKTQSSFPSV CCCCCCCCCCCCCHH	35.43	21712547
535	Phosphorylation	TATNKTQSSFPSVYE CCCCCCCCCCCHHHH	38.90	21712547
536	Phosphorylation	ATNKTQSSFPSVYEH CCCCCCCCCCHHHHH	31.21	21712547
539	Phosphorylation	KTQSSFPSVYEHQLK CCCCCCCHHHHHHHH	35.01	21712547
541	Phosphorylation	QSSFPSVYEHQLKSN CCCCCHHHHHHHHHC	16.42	25720772
547	Phosphorylation	VYEHQLKSNELERGH HHHHHHHHCCCCCCC	44.09	21712547

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

Oops, there are no upstream regulatory protein records of SIP5_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SIP5_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 SIP5_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of SIP5_SCHPO !!

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-127 AND THR-128, ANDMASS SPECTROMETRY.
PubMed: 18257517