NOT5_YEAST - dbPTM
NOT5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOT5_YEAST
UniProt AC Q12514
Protein Name General negative regulator of transcription subunit 5
Gene Name NOT5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 560
Subcellular Localization Cytoplasm . Nucleus.
Protein Description Acts as component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT protein subcomplex negatively regulates the basal and activated transcription of many genes. Preferentially affects TC-type TATA element-dependent transcription. Could directly or indirectly inhibit component(s) of the general transcription machinery..
Protein Sequence MSQRKLQQDIDKLLKKVKEGIEDFDDIYEKFQSTDPSNSSHREKLESDLKREIKKLQKHRDQIKTWLSKEDVKDKQSVLMTNRRLIENGMERFKSVEKLMKTKQFSKEALTNPDIIKDPKELKKRDQVLFIHDCLDELQKQLEQYEAQENEEQTERHEFHIANLENILKKLQNNEMDPEPVEEFQDDIKYYVENNDDPDFIEYDTIYEDMGCEIQPSSSNNEAPKEGNNQTSLSSIRSSKKQERSPKKKAPQRDVSISDRATTPIAPGVESASQSISSTPTPVSTDTPLHTVKDDSIKFDNSTLGTPTTHVSMKKKESENDSEQQLNFPPDRTDEIRKTIQHDVETNAAFQNPLFNDELKYWLDSKRYLMQPLQEMSPKMVSQLESSLLNCPDSLDADSPCLYTKPLSLPHPTSIFFPNEPIRFVYPYDVPLNLTNNENDTDNKFGKDSKAKSKKDDDIYSRTSLARIFMKFDLDTLFFIFYHYQGSYEQFLAARELFKNRNWLFNKVDRCWYYKEIEKLPPGMGKSEEESWRYFDYKKSWLARRCGNDFVYNEEDFEKL
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
12AcetylationKLQQDIDKLLKKVKE
HHHHHHHHHHHHHHH		56.9324489116
18UbiquitinationDKLLKKVKEGIEDFD
HHHHHHHHHCCCCHH		60.1323749301
33PhosphorylationDIYEKFQSTDPSNSS
HHHHHHHCCCCCCHH		37.6029734811
37PhosphorylationKFQSTDPSNSSHREK
HHHCCCCCCHHHHHH		52.7529734811
64AcetylationQKHRDQIKTWLSKED
HHHHHHHHHHHCHHH		28.1924489116
102PhosphorylationSVEKLMKTKQFSKEA
HHHHHHHCCCCCHHH		18.9928889911
117AcetylationLTNPDIIKDPKELKK
HHCHHHCCCHHHHHH		69.2024489116
117UbiquitinationLTNPDIIKDPKELKK
HHCHHHCCCHHHHHH		69.2023749301
120AcetylationPDIIKDPKELKKRDQ
HHHCCCHHHHHHHHH		82.7424489116
170UbiquitinationNLENILKKLQNNEMD
HHHHHHHHHHCCCCC		52.4323749301
231PhosphorylationPKEGNNQTSLSSIRS
CCCCCCCCCHHHHHC		33.4820377248
232PhosphorylationKEGNNQTSLSSIRSS
CCCCCCCCHHHHHCH		19.2522369663
234PhosphorylationGNNQTSLSSIRSSKK
CCCCCCHHHHHCHHC		24.4022369663
235PhosphorylationNNQTSLSSIRSSKKQ
CCCCCHHHHHCHHCC		27.5822369663
238PhosphorylationTSLSSIRSSKKQERS
CCHHHHHCHHCCCCC		44.8521551504
239PhosphorylationSLSSIRSSKKQERSP
CHHHHHCHHCCCCCC		33.7419823750
245PhosphorylationSSKKQERSPKKKAPQ
CHHCCCCCCCCCCCC		40.0819795423
248UbiquitinationKQERSPKKKAPQRDV
CCCCCCCCCCCCCCC		58.5124961812
249UbiquitinationQERSPKKKAPQRDVS
CCCCCCCCCCCCCCC		72.0024961812
256PhosphorylationKAPQRDVSISDRATT
CCCCCCCCHHHCCCC		22.2119823750
258PhosphorylationPQRDVSISDRATTPI
CCCCCCHHHCCCCCC		17.3424909858
262PhosphorylationVSISDRATTPIAPGV
CCHHHCCCCCCCCCC		33.7222369663
263PhosphorylationSISDRATTPIAPGVE
CHHHCCCCCCCCCCC		16.2422369663
271PhosphorylationPIAPGVESASQSISS
CCCCCCCCCCCCCCC		30.7122369663
273PhosphorylationAPGVESASQSISSTP
CCCCCCCCCCCCCCC		33.4722890988
275PhosphorylationGVESASQSISSTPTP
CCCCCCCCCCCCCCC		23.1822369663
277PhosphorylationESASQSISSTPTPVS
CCCCCCCCCCCCCCC		33.1522369663
278PhosphorylationSASQSISSTPTPVST
CCCCCCCCCCCCCCC		36.4122890988
279PhosphorylationASQSISSTPTPVSTD
CCCCCCCCCCCCCCC		25.1322369663
281PhosphorylationQSISSTPTPVSTDTP
CCCCCCCCCCCCCCC		36.0922369663
284PhosphorylationSSTPTPVSTDTPLHT
CCCCCCCCCCCCCCC		23.0522890988
285PhosphorylationSTPTPVSTDTPLHTV
CCCCCCCCCCCCCCC		44.0922890988
287PhosphorylationPTPVSTDTPLHTVKD
CCCCCCCCCCCCCCC		28.0422890988
291PhosphorylationSTDTPLHTVKDDSIK
CCCCCCCCCCCCCCC		36.6122890988
293UbiquitinationDTPLHTVKDDSIKFD
CCCCCCCCCCCCCCC		57.9024961812
296PhosphorylationLHTVKDDSIKFDNST
CCCCCCCCCCCCCCC		37.5022369663
298UbiquitinationTVKDDSIKFDNSTLG
CCCCCCCCCCCCCCC		51.0923749301
302PhosphorylationDSIKFDNSTLGTPTT
CCCCCCCCCCCCCCH		27.1822369663
303PhosphorylationSIKFDNSTLGTPTTH
CCCCCCCCCCCCCHH		35.1522890988
306PhosphorylationFDNSTLGTPTTHVSM
CCCCCCCCCCHHEEC		22.1522369663
308PhosphorylationNSTLGTPTTHVSMKK
CCCCCCCCHHEECCC		29.4022369663
309PhosphorylationSTLGTPTTHVSMKKK
CCCCCCCHHEECCCC		22.8322890988
312PhosphorylationGTPTTHVSMKKKESE
CCCCHHEECCCCCCC		19.7822890988
314UbiquitinationPTTHVSMKKKESEND
CCHHEECCCCCCCCC		53.8623749301
314AcetylationPTTHVSMKKKESEND
CCHHEECCCCCCCCC		53.8625381059
318PhosphorylationVSMKKKESENDSEQQ
EECCCCCCCCCCHHH		51.0528889911
322PhosphorylationKKESENDSEQQLNFP
CCCCCCCCHHHHCCC		49.2219823750
333PhosphorylationLNFPPDRTDEIRKTI
HCCCCCCHHHHHHHH		45.4219823750
338UbiquitinationDRTDEIRKTIQHDVE
CCHHHHHHHHHHHHH		56.4923749301
365PhosphorylationELKYWLDSKRYLMQP
HHHHHHHHHHHHHHH		19.5027017623
368PhosphorylationYWLDSKRYLMQPLQE
HHHHHHHHHHHHHHH		15.4027017623
377PhosphorylationMQPLQEMSPKMVSQL
HHHHHHCCHHHHHHH		22.1822369663
394PhosphorylationSLLNCPDSLDADSPC
HHHCCCCCCCCCCCC		17.1921551504
399PhosphorylationPDSLDADSPCLYTKP
CCCCCCCCCCEECCC		21.1621551504
444AcetylationNENDTDNKFGKDSKA
CCCCCCCCCCCCCCC		59.3024489116
444UbiquitinationNENDTDNKFGKDSKA
CCCCCCCCCCCCCCC		59.3023749301
461PhosphorylationKKDDDIYSRTSLARI
CCCCCHHHHHHHHHH		29.4428889911
526UbiquitinationKLPPGMGKSEEESWR
CCCCCCCCCHHHHHH		45.8923749301
538UbiquitinationSWRYFDYKKSWLARR
HHHHHCHHHHHHHHH		42.0222817900
539UbiquitinationWRYFDYKKSWLARRC
HHHHCHHHHHHHHHH		40.4122817900
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 NOT5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOT5_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 NOT5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
POP2_YEASTPOP2physical
10490603
NOT2_YEASTCDC36physical
10490603
NOT1_YEASTCDC39physical
9511744
NOT3_YEASTNOT3physical
9511744
NOT4_YEASTMOT2physical
9511744
TBP_YEASTSPT15physical
10880468
TAF6_YEASTTAF6physical
10880468
TAF12_YEASTTAF12physical
10880468
TAF5_YEASTTAF5physical
10880468
NOT5_YEASTNOT5physical
11967834
TAF1_YEASTTAF1genetic
12215531
NOT3_YEASTNOT3genetic
9511744
NOT4_YEASTMOT2genetic
9511744
NOT1_YEASTCDC39genetic
11023781
NOT3_YEASTNOT3genetic
11023781
POP2_YEASTPOP2genetic
10490603
CCR4_YEASTCCR4genetic
10490603
NHP6A_YEASTNHP6Agenetic
16272410
NHP6B_YEASTNHP6Bgenetic
16272410
TF2B_YEASTSUA7genetic
16272410
NOT2_YEASTCDC36physical
16429126
SKN7_YEASTSKN7physical
17965252
RAD9_YEASTRAD9genetic
19197357
NOT5_YEASTNOT5physical
19707589
NOT1_YEASTCDC39physical
19707589
NOT3_YEASTNOT3physical
19707589
CAF40_YEASTCAF40physical
19707589
RRP41_YEASTSKI6physical
19707589
RPB1_YEASTRPO21physical
21406554
NAB2_YEASTNAB2physical
21464899
HRP1_YEASTHRP1physical
21464899
NOT4_YEASTMOT2physical
21321079
RNH1_YEASTRNH1genetic
22195970
NOT1_YEASTCDC39genetic
9511744
NOT2_YEASTCDC36genetic
9511744
STF1_YEASTSTF1physical
22875988
MED3_YEASTPGD1physical
22875988
KXD1_YEASTKXD1physical
22875988
HPH1_YEASTFRT1physical
22875988
NIP80_YEASTNIP100physical
22875988
ADA2_YEASTADA2physical
27899560
PAT1_YEASTPAT1physical
26952104
ADA2_YEASTADA2physical
28180299
SPT20_YEASTSPT20physical
28180299
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NOT5_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 THR-262; THR-263; SER-275;SER-277; THR-306; THR-308 AND SER-377, 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-377, 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 THR-306 AND SER-377, ANDMASS 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 THR-262 AND THR-263, ANDMASS SPECTROMETRY.

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