CYC8_YEAST - dbPTM
CYC8_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CYC8_YEAST
UniProt AC P14922
Protein Name General transcriptional corepressor CYC8
Gene Name CYC8
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 966
Subcellular Localization Nucleus.
Protein Description Acts as component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. 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, like MATALPHA2, MIG1, RFX1 and SKO1. 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..
Protein Sequence MNPGGEQTIMEQPAQQQQQQQQQQQQQQQQAAVPQQPLDPLTQSTAETWLSIASLAETLGDGDRAAMAYDATLQFNPSSAKALTSLAHLYRSRDMFQRAAELYERALLVNPELSDVWATLGHCYLMLDDLQRAYNAYQQALYHLSNPNVPKLWHGIGILYDRYGSLDYAEEAFAKVLELDPHFEKANEIYFRLGIIYKHQGKWSQALECFRYILPQPPAPLQEWDIWFQLGSVLESMGEWQGAKEAYEHVLAQNQHHAKVLQQLGCLYGMSNVQFYDPQKALDYLLKSLEADPSDATTWYHLGRVHMIRTDYTAAYDAFQQAVNRDSRNPIFWCSIGVLYYQISQYRDALDAYTRAIRLNPYISEVWYDLGTLYETCNNQLSDALDAYKQAARLDVNNVHIRERLEALTKQLENPGNINKSNGAPTNASPAPPPVILQPTLQPNDQGNPLNTRISAQSANATASMVQQQHPAQQTPINSSATMYSNGASPQLQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAHAQAQAQAQAQAQAQAQAQAQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQLQPLPRQQLQQKGVSVQMLNPQQGQPYITQPTVIQAHQLQPFSTQAMEHPQSSQLPPQQQQLQSVQHPQQLQGQPQAQAPQPLIQHNVEQNVLPQKRYMEGAIHTLVDAAVSSSTHTENNTKSPRQPTHAIPTQAPATGITNAEPQVKKQKLNSPNSNINKLVNTATSIEENAKSEVSNQSPAVVESNTNNTSQEEKPVKANSIPSVIGAQEPPQEASPAEEATKAASVSPSTKPLNTEPESSSVQPTVSSESSTTKANDQSTAETIELSTATVPAEASPVEDEVRQHSKEENGTTEASAPSTEEAEPAASRDAEKQQDETAATTITVIKPTLETMETVKEEAKMREEEQTSQEKSPQENTLPRENVVRQVEEDENYDD
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 Orthologous
Protein Cluster
163PhosphorylationIGILYDRYGSLDYAE
CCCCHHCCCCCCHHH		14.2528889911
165PhosphorylationILYDRYGSLDYAEEA
CCHHCCCCCCHHHHH		14.7728889911
175UbiquitinationYAEEAFAKVLELDPH
HHHHHHHHHHHHCCC		40.6823749301
202AcetylationIIYKHQGKWSQALEC
EEEECCCCHHHHHHH		36.7825381059
410AcetylationERLEALTKQLENPGN
HHHHHHHHHHHCCCC		54.4524489116
421PhosphorylationNPGNINKSNGAPTNA
CCCCCCCCCCCCCCC		35.6922369663
426PhosphorylationNKSNGAPTNASPAPP
CCCCCCCCCCCCCCC		42.7722369663
429PhosphorylationNGAPTNASPAPPPVI
CCCCCCCCCCCCCEE		24.5422369663
440PhosphorylationPPVILQPTLQPNDQG
CCEEECCCCCCCCCC		25.6822369663
452PhosphorylationDQGNPLNTRISAQSA
CCCCCCHHHHHHHHH		36.7422369663
475PhosphorylationQQHPAQQTPINSSAT
HCCCCCCCCCCCCCC		17.6628889911
699PhosphorylationTLVDAAVSSSTHTEN
HHHHHHHHCCCCCCC		17.5323607784
700PhosphorylationLVDAAVSSSTHTENN
HHHHHHHCCCCCCCC		32.4323607784
701PhosphorylationVDAAVSSSTHTENNT
HHHHHHCCCCCCCCC		19.3919779198
702PhosphorylationDAAVSSSTHTENNTK
HHHHHCCCCCCCCCC		34.4623607784
704PhosphorylationAVSSSTHTENNTKSP
HHHCCCCCCCCCCCC		40.2623607784
708PhosphorylationSTHTENNTKSPRQPT
CCCCCCCCCCCCCCC		44.4723607784
710PhosphorylationHTENNTKSPRQPTHA
CCCCCCCCCCCCCCC		24.2322369663
715PhosphorylationTKSPRQPTHAIPTQA
CCCCCCCCCCCCCCC		18.6622369663
720PhosphorylationQPTHAIPTQAPATGI
CCCCCCCCCCCCCCC		31.1120377248
725PhosphorylationIPTQAPATGITNAEP
CCCCCCCCCCCCCCH		28.2325521595
728PhosphorylationQAPATGITNAEPQVK
CCCCCCCCCCCHHHH		29.7122369663
735AcetylationTNAEPQVKKQKLNSP
CCCCHHHHHHHCCCC		44.2124489116
738AcetylationEPQVKKQKLNSPNSN
CHHHHHHHCCCCCHH		59.5224489116
741PhosphorylationVKKQKLNSPNSNINK
HHHHHCCCCCHHHHH		35.5822369663
744PhosphorylationQKLNSPNSNINKLVN
HHCCCCCHHHHHHHH		42.3322890988
748AcetylationSPNSNINKLVNTATS
CCCHHHHHHHHHHHH		50.4424489116
754PhosphorylationNKLVNTATSIEENAK
HHHHHHHHHHHHHHH		28.3522369663
755PhosphorylationKLVNTATSIEENAKS
HHHHHHHHHHHHHHH		26.0722369663
762PhosphorylationSIEENAKSEVSNQSP
HHHHHHHHHHCCCCC		40.6022369663
765PhosphorylationENAKSEVSNQSPAVV
HHHHHHHCCCCCCEE		25.7122369663
768PhosphorylationKSEVSNQSPAVVESN
HHHHCCCCCCEEECC		21.0522369663
774PhosphorylationQSPAVVESNTNNTSQ
CCCCEEECCCCCCCC		37.0322369663
776PhosphorylationPAVVESNTNNTSQEE
CCEEECCCCCCCCCC		38.8422369663
779PhosphorylationVESNTNNTSQEEKPV
EECCCCCCCCCCCCC		33.5822369663
780PhosphorylationESNTNNTSQEEKPVK
ECCCCCCCCCCCCCC		37.4022369663
784AcetylationNNTSQEEKPVKANSI
CCCCCCCCCCCCCCC		55.1224489116
790PhosphorylationEKPVKANSIPSVIGA
CCCCCCCCCCCCCCC		40.5125752575
793PhosphorylationVKANSIPSVIGAQEP
CCCCCCCCCCCCCCC		25.3825752575
805PhosphorylationQEPPQEASPAEEATK
CCCCCCCCHHHHHHH		24.7222369663
811PhosphorylationASPAEEATKAASVSP
CCHHHHHHHHHCCCC		25.2120377248
815PhosphorylationEEATKAASVSPSTKP
HHHHHHHCCCCCCCC		28.1722369663
817PhosphorylationATKAASVSPSTKPLN
HHHHHCCCCCCCCCC		15.6122369663
819PhosphorylationKAASVSPSTKPLNTE
HHHCCCCCCCCCCCC		41.3722369663
820PhosphorylationAASVSPSTKPLNTEP
HHCCCCCCCCCCCCC		39.8122890988
825PhosphorylationPSTKPLNTEPESSSV
CCCCCCCCCCCCCCC		61.6822890988
829PhosphorylationPLNTEPESSSVQPTV
CCCCCCCCCCCCCCC		38.3322890988
830PhosphorylationLNTEPESSSVQPTVS
CCCCCCCCCCCCCCC		32.6322890988
831PhosphorylationNTEPESSSVQPTVSS
CCCCCCCCCCCCCCC		33.7722890988
835PhosphorylationESSSVQPTVSSESST
CCCCCCCCCCCCCCC		18.8722890988
837PhosphorylationSSVQPTVSSESSTTK
CCCCCCCCCCCCCCC		30.7622890988
838PhosphorylationSVQPTVSSESSTTKA
CCCCCCCCCCCCCCC		36.8422890988
840PhosphorylationQPTVSSESSTTKAND
CCCCCCCCCCCCCCC		34.6322890988
841PhosphorylationPTVSSESSTTKANDQ
CCCCCCCCCCCCCCC		35.7222890988
842PhosphorylationTVSSESSTTKANDQS
CCCCCCCCCCCCCCC		41.4122890988
843PhosphorylationVSSESSTTKANDQST
CCCCCCCCCCCCCCC		30.0622890988
866PhosphorylationATVPAEASPVEDEVR
CCCCCCCCCCHHHHH		22.4522369663
876PhosphorylationEDEVRQHSKEENGTT
HHHHHHHHHHHCCCC		33.1622369663
882PhosphorylationHSKEENGTTEASAPS
HHHHHCCCCCCCCCC		32.8022369663
883PhosphorylationSKEENGTTEASAPST
HHHHCCCCCCCCCCH		30.8422369663
886PhosphorylationENGTTEASAPSTEEA
HCCCCCCCCCCHHHC		34.1822369663
889PhosphorylationTTEASAPSTEEAEPA
CCCCCCCCHHHCCCC		48.4422369663
890PhosphorylationTEASAPSTEEAEPAA
CCCCCCCHHHCCCCC		36.4620377248
898PhosphorylationEEAEPAASRDAEKQQ
HHCCCCCCCCHHHHC		32.5722369663
927AcetylationLETMETVKEEAKMRE
HHHHHHHHHHHHHHH		58.2024489116
938PhosphorylationKMREEEQTSQEKSPQ
HHHHHHHHHCCCCCC		35.3429136822
939PhosphorylationMREEEQTSQEKSPQE
HHHHHHHHCCCCCCC		35.7222369663
942AcetylationEEQTSQEKSPQENTL
HHHHHCCCCCCCCCC		60.8524489116
943PhosphorylationEQTSQEKSPQENTLP
HHHHCCCCCCCCCCC		30.9422369663
948PhosphorylationEKSPQENTLPRENVV
CCCCCCCCCCHHHHC		37.0722369663
964PhosphorylationQVEEDENYDD-----
HHHCCCCCCC-----		21.3124961812
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
780SPhosphorylationKinaseATM/ATR-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CYC8_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 CYC8_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TUP1_YEASTTUP1physical
2038333
HOS2_YEASTHOS2physical
14525981
HOS2_YEASTHOS2physical
11069890
RPD3_YEASTRPD3physical
14525981
GCN5_YEASTGCN5physical
12086626
MED3_YEASTPGD1physical
10722672
MED2_YEASTMED2physical
10722672
MED4_YEASTMED4physical
10722672
RGT1_YEASTRGT1physical
12220226
RTG3_YEASTRTG3physical
9867831
AFT1_YEASTAFT1physical
14739928
TUP1_YEASTTUP1physical
8008070
MIG1_YEASTMIG1physical
15031717
TUP1_YEASTTUP1physical
8943325
RGT1_YEASTRGT1physical
15489524
TUP1_YEASTTUP1genetic
10821179
HXT2_YEASTHXT2genetic
8206851
SWI1_YEASTSWI1genetic
9321405
SET2_YEASTSET2physical
16329992
TUP1_YEASTTUP1physical
17634984
TUP1_YEASTTUP1physical
18467557
CYC8_YEASTCYC8physical
19345193
FMC1_YEASTFMC1genetic
20093466
RAV1_YEASTRAV1genetic
20093466
NHP10_YEASTNHP10genetic
20093466
INO2_YEASTINO2genetic
20093466
SWI5_YEASTSWI5genetic
20093466
RT103_YEASTRTT103genetic
20093466
ENV10_YEASTENV10genetic
20093466
SWI6_YEASTSWI6genetic
20093466
ROM2_YEASTROM2genetic
20093466
YL422_YEASTYLR422Wgenetic
20093466
MSC1_YEASTMSC1genetic
20093466
PKR1_YEASTPKR1genetic
20093466
ERG2_YEASTERG2genetic
20093466
IDH1_YEASTIDH1genetic
20093466
AIM44_YEASTAIM44genetic
20093466
HDA3_YEASTHDA3genetic
20093466
SIN3_YEASTSIN3genetic
21104417
SWI5_YEASTSWI5genetic
20959818
SODC_YEASTSOD1genetic
20959818
SAC3_YEASTSAC3genetic
20959818
GTS1_YEASTGTS1physical
21512249
TUP1_YEASTTUP1physical
21552514
YAP6_YEASTYAP6physical
21552514
SKN7_YEASTSKN7physical
21552514
PHD1_YEASTPHD1physical
21552514
SUT1_YEASTSUT1physical
21552514
NRG1_YEASTNRG1physical
21552514
SKO1_YEASTSKO1physical
21552514
YAP4_YEASTCIN5physical
21552514
RGT1_YEASTRGT1physical
23468525
TUP1_YEASTTUP1physical
26257283
HSP72_YEASTSSA2physical
26257283
SAR1_YEASTSAR1physical
26257283
PABP_YEASTPAB1physical
26257283
DED1_YEASTDED1physical
26257283
RS19A_YEASTRPS19Aphysical
26257283
RS19B_YEASTRPS19Bphysical
26257283
RL2A_YEASTRPL2Aphysical
26257283
RL2B_YEASTRPL2Aphysical
26257283
RL3_YEASTRPL3physical
26257283
HRP1_YEASTHRP1physical
26257283
NOP3_YEASTNPL3physical
26257283
FBRL_YEASTNOP1physical
26257283
MAS5_YEASTYDJ1physical
26257283
ACH1_YEASTACH1physical
26257283
PSP2_YEASTPSP2physical
26257283
PURA_YEASTADE12physical
26257283
TAT1_YEASTTAT1genetic
26546823
TAT2_YEASTTAT2genetic
26546823
TRPF_YEASTTRP1genetic
26546823
PDC2_YEASTPDC2genetic
27708008
PDS5_YEASTPDS5genetic
27708008
MTW1_YEASTMTW1genetic
27708008
CDC24_YEASTCDC24genetic
27708008
KPC1_YEASTPKC1genetic
27708008
CDC53_YEASTCDC53genetic
27708008
GLE1_YEASTGLE1genetic
27708008
UBC3_YEASTCDC34genetic
27708008
CDC37_YEASTCDC37genetic
27708008
GPI19_YEASTGPI19genetic
27708008
SEC20_YEASTSEC20genetic
27708008
RPN11_YEASTRPN11genetic
27708008
PSB7_YEASTPRE4genetic
27708008
STT3_YEASTSTT3genetic
27708008
BRL1_YEASTBRL1genetic
27708008
MED6_YEASTMED6genetic
27708008
DNA2_YEASTDNA2genetic
27708008
ARP4_YEASTARP4genetic
27708008
DPB11_YEASTDPB11genetic
27708008
CDC11_YEASTCDC11genetic
27708008
FIP1_YEASTFIP1genetic
27708008
RPF2_YEASTRPF2genetic
27708008
SEC22_YEASTSEC22genetic
27708008
SEC65_YEASTSEC65genetic
27708008
SGT1_YEASTSGT1genetic
27708008
PROF_YEASTPFY1genetic
27708008
SEC63_YEASTSEC63genetic
27708008
PSA7_YEASTPRE10genetic
27708008
GPI2_YEASTGPI2genetic
27708008
SEC62_YEASTSEC62genetic
27708008
SRP54_YEASTSRP54genetic
27708008
PSB5_YEASTPRE2genetic
27708008
RPN7_YEASTRPN7genetic
27708008
PGTB2_YEASTBET2genetic
27708008
NHP10_YEASTNHP10genetic
27708008
INO2_YEASTINO2genetic
27708008
SWI5_YEASTSWI5genetic
27708008
NUM1_YEASTNUM1genetic
27708008
RT103_YEASTRTT103genetic
27708008
HUR1_YEASTHUR1genetic
27708008
GTR2_YEASTGTR2genetic
27708008
FMC1_YEASTFMC1genetic
27708008
RCY1_YEASTRCY1genetic
27708008
CTK1_YEASTCTK1genetic
27708008
ENV10_YEASTENV10genetic
27708008
ROM2_YEASTROM2genetic
27708008
MSC1_YEASTMSC1genetic
27708008
PKR1_YEASTPKR1genetic
27708008
HDA1_YEASTHDA1genetic
27708008
IDH1_YEASTIDH1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
AIM44_YEASTAIM44genetic
27708008
HDA3_YEASTHDA3genetic
27708008
GCN5_YEASTGCN5genetic
28115623
SAS3_YEASTSAS3genetic
28115623
ADA2_YEASTADA2genetic
28115623
TUP1_YEASTTUP1physical
29053708
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CYC8_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-429; THR-475; SER-710;SER-741; SER-755; SER-768; THR-779; SER-780; SER-793; SER-805;SER-815; SER-817; SER-866; SER-939 AND SER-943, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741; SER-780 ANDSER-815, AND MASS SPECTROMETRY.
"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-710, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815; SER-817 ANDSER-943, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-805, AND MASSSPECTROMETRY.

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