TAF4_YEAST - dbPTM
TAF4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAF4_YEAST
UniProt AC P50105
Protein Name Transcription initiation factor TFIID subunit 4
Gene Name TAF4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 388
Subcellular Localization Nucleus .
Protein Description Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription..
Protein Sequence MANSPKKPSDGTGVSASDTPKYQHTVPETKPAFNLSPGKASELSHSLPSPSQIKSTAHVSSTHNDAAGNTDDSVLPKNVSPTTNLRVESNGDTNNMFSSPAGLALPKKDDKKKNKGTSKADSKDGKASNSSGQNAQQQSDPNKMQDVLFSAGIDVREEEALLNSSINASKSQVQTNNVKIPNHLPFLHPEQVSNYMRKVGKEQNFNLTPTKNPEILDMMSSACENYMRDILTNAIVISRHRRKAVKINSGRRSEVSAALRAIALIQKKEEERRVKKRIALGLEKEDYENKIDSEETLHRASNVTAGLRAGSKKQYGWLTSSVNKPTSLGAKSSGKVASDITARGESGLKFREAREEPGIVMRDLLFALENRRNSVQTIISKGYAKIRD
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
4Phosphorylation----MANSPKKPSDG
----CCCCCCCCCCC		28.6722369663
9PhosphorylationANSPKKPSDGTGVSA
CCCCCCCCCCCCCCC		58.5122369663
12PhosphorylationPKKPSDGTGVSASDT
CCCCCCCCCCCCCCC		39.1322369663
15PhosphorylationPSDGTGVSASDTPKY
CCCCCCCCCCCCCCC		24.3322369663
17PhosphorylationDGTGVSASDTPKYQH
CCCCCCCCCCCCCCC		34.2122369663
19PhosphorylationTGVSASDTPKYQHTV
CCCCCCCCCCCCCCC		21.1322369663
21AcetylationVSASDTPKYQHTVPE
CCCCCCCCCCCCCCC		60.6824489116
29PhosphorylationYQHTVPETKPAFNLS
CCCCCCCCCCCCCCC		35.9429136822
36PhosphorylationTKPAFNLSPGKASEL
CCCCCCCCCCCHHHH		32.4825521595
41PhosphorylationNLSPGKASELSHSLP
CCCCCCHHHHHCCCC		42.4228889911
44PhosphorylationPGKASELSHSLPSPS
CCCHHHHHCCCCCHH		13.6422369663
46PhosphorylationKASELSHSLPSPSQI
CHHHHHCCCCCHHHC		38.3022369663
49PhosphorylationELSHSLPSPSQIKST
HHHCCCCCHHHCCCE		42.3422369663
51PhosphorylationSHSLPSPSQIKSTAH
HCCCCCHHHCCCEEE		49.2022369663
77AcetylationTDDSVLPKNVSPTTN
CCCCCCCCCCCCCCC		66.8624489116
80PhosphorylationSVLPKNVSPTTNLRV
CCCCCCCCCCCCEEE		26.3922369663
82PhosphorylationLPKNVSPTTNLRVES
CCCCCCCCCCEEEEC		22.3220377248
83PhosphorylationPKNVSPTTNLRVESN
CCCCCCCCCEEEECC		35.3222369663
89PhosphorylationTTNLRVESNGDTNNM
CCCEEEECCCCCCCC		43.1620377248
93PhosphorylationRVESNGDTNNMFSSP
EEECCCCCCCCCCCC		29.8622369663
98PhosphorylationGDTNNMFSSPAGLAL
CCCCCCCCCCCCCCC		25.3322369663
99PhosphorylationDTNNMFSSPAGLALP
CCCCCCCCCCCCCCC		13.9122369663
128PhosphorylationDSKDGKASNSSGQNA
CCCCCCCCCCCCCCH		40.5028889911
139PhosphorylationGQNAQQQSDPNKMQD
CCCHHHCCCCCHHHH		51.1828889911
169PhosphorylationLNSSINASKSQVQTN
HHHHHCCCHHHHHCC		28.4930377154
208PhosphorylationKEQNFNLTPTKNPEI
CCCCCCCCCCCCHHH		29.9825521595
210PhosphorylationQNFNLTPTKNPEILD
CCCCCCCCCCHHHHH		37.9124909858
284AcetylationRIALGLEKEDYENKI
HHHHCCCHHHHHCCC		62.0124489116
293PhosphorylationDYENKIDSEETLHRA
HHHCCCCCHHHHHHH		40.5828889911
296PhosphorylationNKIDSEETLHRASNV
CCCCCHHHHHHHHHC		24.6624961812
301PhosphorylationEETLHRASNVTAGLR
HHHHHHHHHCCCCCC		31.6124961812
304PhosphorylationLHRASNVTAGLRAGS
HHHHHHCCCCCCCCC		21.1824961812
311PhosphorylationTAGLRAGSKKQYGWL
CCCCCCCCCCHHEEE		35.3824961812
313AcetylationGLRAGSKKQYGWLTS
CCCCCCCCHHEEEEC		50.9125381059
320PhosphorylationKQYGWLTSSVNKPTS
CHHEEEECCCCCCCC		30.0721440633
321PhosphorylationQYGWLTSSVNKPTSL
HHEEEECCCCCCCCC		25.1925752575
335AcetylationLGAKSSGKVASDITA
CCCCCCCCCCCCCCC		36.2522865919
338PhosphorylationKSSGKVASDITARGE
CCCCCCCCCCCCCCC		32.3127214570
374PhosphorylationALENRRNSVQTIISK
HHHHCCHHHHHHHHH		17.5021440633
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 TAF4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAF4_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 TAF4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBP_YEASTSPT15physical
12052880
TBP_YEASTSPT15physical
10788514
TAF1_YEASTTAF1physical
12052880
TAF1_YEASTTAF1physical
10788514
TAF2_YEASTTAF2physical
12052880
TAF9_YEASTTAF9physical
12052880
TAF13_YEASTTAF13physical
12052880
TAF10_YEASTTAF10physical
12052880
TAF14_YEASTTAF14physical
12052880
TAF11_YEASTTAF11physical
12052880
TAF3_YEASTTAF3physical
12052880
ASK10_YEASTASK10physical
12052880
CCR4_YEASTCCR4physical
12052880
ELP4_YEASTELP4physical
12052880
HIR1_YEASTHIR1physical
12052880
HIR2_YEASTHIR2physical
12052880
HIR3_YEASTHIR3physical
12052880
HOS3_YEASTHOS3physical
12052880
HPC2_YEASTHPC2physical
12052880
MSL1_YEASTMSL1physical
12052880
PRP2_YEASTPRP2physical
12052880
RPD3_YEASTRPD3physical
12052880
SAP30_YEASTSAP30physical
12052880
SFL1_YEASTSFL1physical
12052880
SIN3_YEASTSIN3physical
12052880
SPP2_YEASTSPP2physical
12052880
STB4_YEASTSTB4physical
12052880
TAF6_YEASTTAF6physical
12052880
TAF12_YEASTTAF12physical
12052880
TAF8_YEASTTAF8physical
12052880
TAF7_YEASTTAF7physical
12052880
TAF5_YEASTTAF5physical
12052880
TAF13_YEASTTAF13physical
10788514
TAF3_YEASTTAF3physical
10788514
TAF12_YEASTTAF12physical
10788514
TAF5_YEASTTAF5physical
10788514
TAF6_YEASTTAF6physical
12582245
TAF12_YEASTTAF12physical
12237303
TBP_YEASTSPT15physical
15132995
SPT8_YEASTSPT8physical
15132995
T2AG_YEASTTOA2physical
15132995
TAF12_YEASTTAF12genetic
12237303
TAF1_YEASTTAF1physical
16554755
SNL1_YEASTSNL1physical
16554755
TAF11_YEASTTAF11physical
16554755
TAF9_YEASTTAF9physical
16554755
TAF3_YEASTTAF3physical
16554755
TAF11_YEASTTAF11physical
16429126
TAF12_YEASTTAF12physical
16429126
TAF3_YEASTTAF3physical
16429126
TAF5_YEASTTAF5physical
16429126
TAF9_YEASTTAF9physical
16429126
TAF1_YEASTTAF1physical
16429126
TAF10_YEASTTAF10physical
16429126
TAF6_YEASTTAF6physical
16429126
VPS71_YEASTVPS71genetic
17314980
SWC3_YEASTSWC3genetic
17314980
VPS72_YEASTVPS72genetic
17314980
SWC5_YEASTSWC5genetic
17314980
SWR1_YEASTSWR1genetic
17314980
MED31_YEASTSOH1genetic
17314980
ELP2_YEASTELP2genetic
17314980
SET2_YEASTSET2genetic
17314980
ARP6_YEASTARP6genetic
17314980
TSA1_YEASTTSA1genetic
17314980
TBP7_YEASTYTA7genetic
17314980
MET18_YEASTMET18genetic
17314980
RAD5_YEASTRAD5genetic
17314980
MNN11_YEASTMNN11genetic
17314980
CDC26_YEASTCDC26genetic
17314980
FEN1_YEASTRAD27genetic
17314980
DOT1_YEASTDOT1genetic
17314980
TBA3_YEASTTUB3genetic
17314980
SRC1_YEASTSRC1genetic
17314980
SWI3_YEASTSWI3genetic
17314980
CSK2B_YEASTCKB1genetic
17314980
NAP1_YEASTNAP1genetic
17314980
TAF9_YEASTTAF9physical
20189987
TAF10_YEASTTAF10physical
20189987
RAP1_YEASTRAP1physical
20189987
TAF4_YEASTTAF4physical
23814059
TAF5_YEASTTAF5physical
23814059
TAF12_YEASTTAF12physical
23814059
TAF11_YEASTTAF11physical
23814059
RAP1_YEASTRAP1physical
23814059
TOA1_YEASTTOA1physical
23814059
T2AG_YEASTTOA2physical
23814059
TOA1_YEASTTOA1genetic
23814059
T2AG_YEASTTOA2genetic
23814059
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TAF4_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-4; SER-36; SER-49;SER-51; SER-80 AND SER-89, 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-36, 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-36, 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-80, AND MASSSPECTROMETRY.

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