TUP1_YEAST - dbPTM
TUP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TUP1_YEAST
UniProt AC P16649
Protein Name General transcriptional corepressor TUP1
Gene Name TUP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 713
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 MTASVSNTQNKLNELLDAIRQEFLQVSQEANTYRLQNQKDYDFKMNQQLAEMQQIRNTVYELELTHRKMKDAYEEEIKHLKLGLEQRDHQIASLTVQQQRQQQQQQQVQQHLQQQQQQLAAASASVPVAQQPPATTSATATPAANTTTGSPSAFPVQASRPNLVGSQLPTTTLPVVSSNAQQQLPQQQLQQQQLQQQQPPPQVSVAPLSNTAINGSPTSKETTTLPSVKAPESTLKETEPENNNTSKINDTGSATTATTTTATETEIKPKEEDATPASLHQDHYLVPYNQRANHSKPIPPFLLDLDSQSVPDALKKQTNDYYILYNPALPREIDVELHKSLDHTSVVCCVKFSNDGEYLATGCNKTTQVYRVSDGSLVARLSDDSAANNHRNSITENNTTTSTDNNTMTTTTTTTITTTAMTSAAELAKDVENLNTSSSPSSDLYIRSVCFSPDGKFLATGAEDRLIRIWDIENRKIVMILQGHEQDIYSLDYFPSGDKLVSGSGDRTVRIWDLRTGQCSLTLSIEDGVTTVAVSPGDGKYIAAGSLDRAVRVWDSETGFLVERLDSENESGTGHKDSVYSVVFTRDGQSVVSGSLDRSVKLWNLQNANNKSDSKTPNSGTCEVTYIGHKDFVLSVATTQNDEYILSGSKDRGVLFWDKKSGNPLLMLQGHRNSVISVAVANGSPLGPEYNVFATGSGDCKARIWKYKKIAPN
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
2Phosphorylation------MTASVSNTQ
------CCCCCHHHH		27.8630377154
4Phosphorylation----MTASVSNTQNK
----CCCCCHHHHHH		19.5330377154
6Phosphorylation--MTASVSNTQNKLN
--CCCCCHHHHHHHH		31.5030377154
8PhosphorylationMTASVSNTQNKLNEL
CCCCCHHHHHHHHHH		26.4730377154
39SuccinylationTYRLQNQKDYDFKMN
HHHCCCHHHCCHHHH		66.8423954790
39AcetylationTYRLQNQKDYDFKMN
HHHCCCHHHCCHHHH		66.8424489116
78AcetylationDAYEEEIKHLKLGLE
HHHHHHHHHHHHCHH		46.2824489116
81AcetylationEEEIKHLKLGLEQRD
HHHHHHHHHCHHHHC		39.9824489116
150PhosphorylationAANTTTGSPSAFPVQ
CCCCCCCCCCCCCEE		17.3728889911
216PhosphorylationSNTAINGSPTSKETT
CCCCCCCCCCCCCCC		22.1027214570
218PhosphorylationTAINGSPTSKETTTL
CCCCCCCCCCCCCCC		54.8728889911
229AcetylationTTTLPSVKAPESTLK
CCCCCCCCCCHHHCC		63.6624489116
233PhosphorylationPSVKAPESTLKETEP
CCCCCCHHHCCCCCC		37.6723749301
236AcetylationKAPESTLKETEPENN
CCCHHHCCCCCCCCC		63.7822865919
236UbiquitinationKAPESTLKETEPENN
CCCHHHCCCCCCCCC		63.7823749301
246PhosphorylationEPENNNTSKINDTGS
CCCCCCCCCCCCCCC		33.3928889911
247AcetylationPENNNTSKINDTGSA
CCCCCCCCCCCCCCC		43.4124489116
251PhosphorylationNTSKINDTGSATTAT
CCCCCCCCCCCEEEE		28.6622369663
253PhosphorylationSKINDTGSATTATTT
CCCCCCCCCEEEEEE		25.2422369663
255PhosphorylationINDTGSATTATTTTA
CCCCCCCEEEEEEEE		20.7519795423
256PhosphorylationNDTGSATTATTTTAT
CCCCCCEEEEEEEEE		23.0219795423
258PhosphorylationTGSATTATTTTATET
CCCCEEEEEEEEECE		23.6822369663
259PhosphorylationGSATTATTTTATETE
CCCEEEEEEEEECEE		21.4922369663
260PhosphorylationSATTATTTTATETEI
CCEEEEEEEEECEEE		15.3019795423
261PhosphorylationATTATTTTATETEIK
CEEEEEEEEECEEEC		29.5019795423
263PhosphorylationTATTTTATETEIKPK
EEEEEEEECEEECCC		41.1519795423
265PhosphorylationTTTTATETEIKPKEE
EEEEEECEEECCCCC		38.3619795423
270SumoylationTETEIKPKEEDATPA
ECEEECCCCCCCCCC		69.59-
275PhosphorylationKPKEEDATPASLHQD
CCCCCCCCCCCCCCC		31.5422369663
278PhosphorylationEEDATPASLHQDHYL
CCCCCCCCCCCCEEE		27.8222369663
284PhosphorylationASLHQDHYLVPYNQR
CCCCCCEEEECCCCC		20.0622369663
288PhosphorylationQDHYLVPYNQRANHS
CCEEEECCCCCCCCC		19.2222369663
315AcetylationQSVPDALKKQTNDYY
CCCCHHHHHHCCCEE		44.5524489116
340PhosphorylationIDVELHKSLDHTSVV
CCEEHHHCCCCCEEE		28.4321440633
344PhosphorylationLHKSLDHTSVVCCVK
HHHCCCCCEEEEEEE		23.9221440633
365UbiquitinationYLATGCNKTTQVYRV
EEEEEECCCCEEEEC		57.9623749301
436PhosphorylationKDVENLNTSSSPSSD
HHHHHCCCCCCCCCC		32.9022369663
437PhosphorylationDVENLNTSSSPSSDL
HHHHCCCCCCCCCCE		27.9622369663
438PhosphorylationVENLNTSSSPSSDLY
HHHCCCCCCCCCCEE		44.2025521595
439PhosphorylationENLNTSSSPSSDLYI
HHCCCCCCCCCCEEE		28.6822369663
441PhosphorylationLNTSSSPSSDLYIRS
CCCCCCCCCCEEEEE		38.1325521595
442PhosphorylationNTSSSPSSDLYIRSV
CCCCCCCCCEEEEEE		34.7122369663
445PhosphorylationSSPSSDLYIRSVCFS
CCCCCCEEEEEEEEC		10.1629136822
456AcetylationVCFSPDGKFLATGAE
EEECCCCCEECCCCC		44.5824489116
516PhosphorylationVRIWDLRTGQCSLTL
EEEEECCCCEEEEEE		38.6129688323
520PhosphorylationDLRTGQCSLTLSIED
ECCCCEEEEEEEEEC		19.2629688323
522PhosphorylationRTGQCSLTLSIEDGV
CCCEEEEEEEEECCC		11.3629688323
524PhosphorylationGQCSLTLSIEDGVTT
CEEEEEEEEECCCEE		20.7829688323
530PhosphorylationLSIEDGVTTVAVSPG
EEEECCCEEEEECCC		22.5329688323
531PhosphorylationSIEDGVTTVAVSPGD
EEECCCEEEEECCCC		12.2229688323
535PhosphorylationGVTTVAVSPGDGKYI
CCEEEEECCCCCCEE		17.2729688323
567PhosphorylationFLVERLDSENESGTG
EEEEECCCCCCCCCC		47.0828889911
576AcetylationNESGTGHKDSVYSVV
CCCCCCCCCCEEEEE		53.7124489116
593PhosphorylationRDGQSVVSGSLDRSV
CCCCEEEECCCCCEE		22.1024909858
595PhosphorylationGQSVVSGSLDRSVKL
CCEEEECCCCCEEEE		21.4224909858
601UbiquitinationGSLDRSVKLWNLQNA
CCCCCEEEEEECCCC		49.3723749301
611AcetylationNLQNANNKSDSKTPN
ECCCCCCCCCCCCCC		56.2824489116
616PhosphorylationNNKSDSKTPNSGTCE
CCCCCCCCCCCCEEE		31.4921440633
621PhosphorylationSKTPNSGTCEVTYIG
CCCCCCCEEEEEEEE		12.8128889911
659UbiquitinationRGVLFWDKKSGNPLL
CCEEEEECCCCCEEE		39.1623749301
659AcetylationRGVLFWDKKSGNPLL
CCEEEEECCCCCEEE		39.1624489116
674PhosphorylationMLQGHRNSVISVAVA
EEECCCCCEEEEEEE		22.3021440633
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 TUP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TUP1_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 TUP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLU_YEASTCLU1physical
11805837
CYC8_YEASTCYC8physical
11805837
SSY5_YEASTSSY5physical
11805837
HSP7E_YEASTECM10physical
11805837
SPH1_YEASTSPH1physical
11805837
CYC8_YEASTCYC8physical
2038333
SSN3_YEASTSSN3physical
11226276
RPD3_YEASTRPD3physical
14525981
SSN8_YEASTSSN8physical
11226276
RPD3_YEASTRPD3physical
11069890
CYC8_YEASTCYC8physical
11069890
MED3_YEASTPGD1physical
11470794
MED2_YEASTMED2physical
11470794
MED14_YEASTRGR1physical
11470794
MED16_YEASTSIN4physical
11470794
MED21_YEASTSRB7physical
11470794
CET1_YEASTCET1physical
12637515
HDA1_YEASTHDA1physical
11172717
CYC8_YEASTCYC8physical
10722750
CYC8_YEASTCYC8physical
10722672
MED3_YEASTPGD1physical
10722672
H4_YEASTHHF1physical
8675011
H3_YEASTHHT1physical
8675011
CYC8_YEASTCYC8physical
10802055
TUP1_YEASTTUP1physical
11967834
TUP1_YEASTTUP1physical
10722750
CYC8_YEASTCYC8physical
10821179
CYC8_YEASTCYC8physical
9111019
SWI1_YEASTSWI1genetic
9321405
MIG1_YEASTMIG1genetic
8828236
CDC48_YEASTCDC48physical
16554755
DOA1_YEASTDOA1physical
16554755
SSN3_YEASTSSN3physical
17689156
DHSO2_YEASTSOR2physical
18467557
NHP6B_YEASTNHP6Bphysical
11095729
CYC8_YEASTCYC8physical
11095729
KPR1_YEASTPRS1physical
11297736
CDC73_YEASTCDC73physical
11525400
NHP6B_YEASTNHP6Bphysical
11525400
CYC8_YEASTCYC8physical
11525400
CYC8_YEASTCYC8genetic
16354707
CYC8_YEASTCYC8physical
21552514
SKN7_YEASTSKN7physical
21552514
YAP6_YEASTYAP6physical
21552514
YAP4_YEASTCIN5physical
21552514
NRG1_YEASTNRG1physical
21552514
PHD1_YEASTPHD1physical
21552514
RAD16_YEASTRAD16genetic
21698136
GCN5_YEASTGCN5genetic
21698136
SNF2_YEASTSNF2genetic
22156212
STH1_YEASTSTH1genetic
22156212
GCN5_YEASTGCN5genetic
22156212
MED15_YEASTGAL11genetic
22156212
MED15_YEASTGAL11physical
22156212
TUP1_YEASTTUP1physical
22707714
CYC8_YEASTCYC8physical
22707714
NCA2_YEASTNCA2physical
22875988
KIN3_YEASTKIN3physical
22875988
TUP1_YEASTTUP1physical
22875988
YET3_YEASTYET3physical
22875988
KEL2_YEASTKEL2physical
22875988
KOG1_YEASTKOG1physical
22875988
NOT3_YEASTNOT3physical
22875988
LAA1_YEASTLAA1physical
22875988
YKT6_YEASTYKT6physical
22875988
DYHC_YEASTDYN1physical
22875988
MMR1_YEASTMMR1physical
22875988
AF9_YEASTYAF9physical
22875988
NUF2_YEASTNUF2physical
22875988
CTR9_YEASTCTR9physical
22875988
YO304_YEASTBIL1physical
22875988
CTF19_YEASTCTF19physical
22875988
TBP6_YEASTYTA6physical
22875988
IQG1_YEASTIQG1physical
22875988
GYP5_YEASTGYP5physical
22875988
YEF3_YEASTYEL043Wphysical
22875988
HOS1_YEASTHOS1genetic
21712029
SIZ1_YEASTSIZ1physical
23712011
PMP1_YEASTPMP1physical
26404137
CYC8_YEASTCYC8physical
29053708
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TUP1_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-150; SER-216; THR-218;SER-253; SER-437; SER-438; SER-439; SER-441 AND SER-442, AND MASSSPECTROMETRY.
"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-439, AND MASSSPECTROMETRY.

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