CYC8_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CYC8_SCHPO
• UniProt AC: O60184
• Protein Name: General transcriptional corepressor ssn6
• Gene Name: ssn6
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 1102
• Subcellular Localization: Cytoplasm. Nucleus. Nuclear dots.
• Protein Description: Acts as component of the ssn6-tup corepressor complexes, which are involved in the repression of many genes in a wide variety of physiological processes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex (By similarity)..
• Protein Sequence: MPQSQVATASPSQNAQPNHGMGSKVLSSDPNASLPPQTAYYASPLHANSVSLPPSHLPRSTLHPLLSQQQQPAQQSPSLGPAQQNIQQPPSVSIASQPHYAEAIVPIQQVLQPQQYRQLPPNMVAATNAPQQHPQLQRMMPILSSNQPIQQLPLPNQASPYIPVPLQQQQQSQPQQQPQQQQHQQPQQPQPPQQPLQQQQQQRQLHSGIQQPVSTIVSQNGTYYSIPAVNHPMAGQPIAIAPVPAPNQAALPPIPPQALPANGTPNTLASPVTLPAANSAVQNAQPVPMTSSPAMAVVPQNKTAATSTLAAQQGANVLPPNAPESVRHLISLNEETWIQIGRLAELFDDQDKALSAYESALRQNPYSIPAMLQIATILRNREQFPLAIEYYQTILDCDPKQGEIWSALGHCYLMQDDLSRAYSAYRQALYHLKDPKDPKLWYGIGILYDRYGSHEHAEEAFMQCLRMDPNFEKVNEIYFRLGIIYKQQHKFAQSLELFRHILDNPPKPLTVLDIYFQIGHVYEQRKEYKLAKEAYERVLAETPNHAKVLQQLGWLCHQQSSSFTNQDLAIQYLTKSLEADDTDAQSWYLIGRCYVAQQKYNKAYEAYQQAVYRDGRNPTFWCSIGVLYYQINQYQDALDAYSRAIRLNPYISEVWYDLGTLYESCHNQISDALDAYQRAAELDPTNPHIKARLQLLRGPNNEQHKIVNAPPSNVPNVQTAKYINQPGVPYSNVPVAQLSGNWQPPHLPQAQLPSATGQSGVVQQPYQTQPSVTNNNVATQPVIASTVPVQTAAPSSQTAVPQTIHQSNAFTPRGKHASGSRNSISSTKSPQHKLSDQPRSRNNSISNVSHRERSNSVSSKSRETRTSASNESDPKKSTQRDSSKKLENSTVVSGSPSSSSKSDAAKSIKPQKPEPALKPVEGTADPKSTKRNHQETEKTADTDVSSTEPVKRQKTADVNDDVGEEEVKQSVSEQVDSAQLTSEPKSESLPKSPEEKSDDTSNDVTTENTNDINGDSNMDNVATVDKSTDAVDTSTATVAATTTTAEEELPQKESQERSSPSPENQDSTPLAPKSVSPKQAARTLDIDENYDDDEGEKETVSV

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
8	Phosphorylation	MPQSQVATASPSQNA CCHHHCCCCCCCCCC	28.89	24763107
10	Phosphorylation	QSQVATASPSQNAQP HHHCCCCCCCCCCCC	22.26	21712547
12	Phosphorylation	QVATASPSQNAQPNH HCCCCCCCCCCCCCC	33.30	21712547
41	Phosphorylation	LPPQTAYYASPLHAN CCCCCEECCCCCCCC	9.72	29996109
43	Phosphorylation	PQTAYYASPLHANSV CCCEECCCCCCCCCC	16.33	29996109
49	Phosphorylation	ASPLHANSVSLPPSH CCCCCCCCCCCCHHH	17.54	29996109
51	Phosphorylation	PLHANSVSLPPSHLP CCCCCCCCCCHHHCC	34.67	29996109
818	Phosphorylation	TPRGKHASGSRNSIS CCCCCCCCCCCCCCC	36.70	21712547
820	Phosphorylation	RGKHASGSRNSISST CCCCCCCCCCCCCCC	26.29	24763107
823	Phosphorylation	HASGSRNSISSTKSP CCCCCCCCCCCCCCC	23.80	21712547
825	Phosphorylation	SGSRNSISSTKSPQH CCCCCCCCCCCCCCC	31.60	21712547
826	Phosphorylation	GSRNSISSTKSPQHK CCCCCCCCCCCCCCC	37.88	21712547
827	Phosphorylation	SRNSISSTKSPQHKL CCCCCCCCCCCCCCC	28.84	21712547
829	Phosphorylation	NSISSTKSPQHKLSD CCCCCCCCCCCCCCC	29.85	25720772
835	Phosphorylation	KSPQHKLSDQPRSRN CCCCCCCCCCCCCCC	38.72	25720772
840	Phosphorylation	KLSDQPRSRNNSISN CCCCCCCCCCCCCCC	46.15	25720772
844	Phosphorylation	QPRSRNNSISNVSHR CCCCCCCCCCCCCHH	30.83	28889911
846	Phosphorylation	RSRNNSISNVSHRER CCCCCCCCCCCHHHH	30.88	29996109
849	Phosphorylation	NNSISNVSHRERSNS CCCCCCCCHHHHHCC	22.52	25720772
854	Phosphorylation	NVSHRERSNSVSSKS CCCHHHHHCCCCCCC	28.80	25720772
856	Phosphorylation	SHRERSNSVSSKSRE CHHHHHCCCCCCCHH	25.31	25720772
882	Phosphorylation	KKSTQRDSSKKLENS CCCCCCCHHHHHCCC	46.36	25720772
883	Phosphorylation	KSTQRDSSKKLENST CCCCCCHHHHHCCCE	37.79	25720772
889	Phosphorylation	SSKKLENSTVVSGSP HHHHHCCCEEECCCC	17.13	21712547
893	Phosphorylation	LENSTVVSGSPSSSS HCCCEEECCCCCCCC	29.26	28889911
895	Phosphorylation	NSTVVSGSPSSSSKS CCEEECCCCCCCCHH	17.69	28889911
897	Phosphorylation	TVVSGSPSSSSKSDA EEECCCCCCCCHHHH	44.54	28889911
898	Phosphorylation	VVSGSPSSSSKSDAA EECCCCCCCCHHHHH	41.85	28889911
899	Phosphorylation	VSGSPSSSSKSDAAK ECCCCCCCCHHHHHH	46.23	29996109
900	Phosphorylation	SGSPSSSSKSDAAKS CCCCCCCCHHHHHHH	37.82	29996109
955	Phosphorylation	EPVKRQKTADVNDDV CCCCCCCCCCCCCCC	21.54	24763107
986	Phosphorylation	QLTSEPKSESLPKSP HCCCCCCCCCCCCCC	43.03	21712547
988	Phosphorylation	TSEPKSESLPKSPEE CCCCCCCCCCCCCCC	58.00	24763107
992	Phosphorylation	KSESLPKSPEEKSDD CCCCCCCCCCCCCCC	35.29	28889911
1054	Phosphorylation	EELPQKESQERSSPS HHCCHHHHHCCCCCC	44.36	28889911
1058	Phosphorylation	QKESQERSSPSPENQ HHHHHCCCCCCCCCC	45.94	24763107
1059	Phosphorylation	KESQERSSPSPENQD HHHHCCCCCCCCCCC	35.30	28889911
1061	Phosphorylation	SQERSSPSPENQDST HHCCCCCCCCCCCCC	46.95	28889911
1067	Phosphorylation	PSPENQDSTPLAPKS CCCCCCCCCCCCCCC	23.35	21712547
1068	Phosphorylation	SPENQDSTPLAPKSV CCCCCCCCCCCCCCC	30.52	29996109

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

Oops, there are no upstream regulatory protein records of CYC8_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CYC8_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 CYC8_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TUP11_SCHPO	tup11	physical	15632072
TUP12_SCHPO	tup12	physical	15632072

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-893; SER-895; SER-897;SER-898; SER-992; SER-1059 AND SER-1061, AND MASS SPECTROMETRY.
PubMed: 18257517