TAF2_YEAST - dbPTM
TAF2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAF2_YEAST
UniProt AC P23255
Protein Name Transcription initiation factor TFIID subunit 2
Gene Name TAF2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1407
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 MMSFSKNATPRAIVSESSTLHEMKFRNFRVAHEKISLDIDLATHCITGSATIIIIPLIQNLEYVTFDCKEMTIKDVLVENRRCDQFIHDDPLQTNLNGLTSQNVLYSDNSIEQSHFLRSKFASLNEYPETDSKSQLTIKIPSSIKISLEDANALSNYTPITPSIKTTPGFQESVFTPITLQIEYEIRNPKSGIKFDTVYADKPWLWNVYTSNGEICSSASYWVPCVDLLDEKSTWELEFSVPRLVKNIGTSKLIGQNGEESEKEKEDTPEHDEEEEGKPARVIKDEDKDSNLKNDEEGKNSKSKDAQDNDEEEEEGESDEEEEEGEEERRNIEESNNPSLRDVIVCCSEYSNIKELPHPIDLTKKKCIFQIINPVAPHHIGWAIGAFNSWSLPLISPPSVDAEDEVEEDKLRENVVDNVNDTMDDDIGSDIIPIQIFTLPTQETDELTVINSTVVCQKIIDFYSKEFGSYPFTCYSMVFLPTAPSKHMDFAALGICNTRLLYPLEVIDKAFSTTNELAWALANQWSCVNITPLDMNDYWCCLGIAGYMVFQVTKKLMGNNTYKYQLKRNSEAIVEQDFEKPPIGSTFTGSSRPISWSSKDLSFIQLKAPMILHILDRRMTKTERSFGMSRVLPKIFLQAMSGDLPNNSLTSSHFQHVCERVNKSKLENFFNEWVYGSGVPILRVTQRFNRKRMVIELGIRQVQDEELGHEKVVGEEGFFKSALDHLEHPDLNRTECFTGSMTIRIHEHDGTPYEHIVEIKDTFTKIDIQYNTKYRRLRKRGGGANDENGVENNNEEKPIVVDVNCLGNVYMSPEECSRFSLTEFNRTSESNELLKQNEAFEWIRIDSDLEWICQMHINQPDYMFSSQLRQDGDIEAQLEAIRYYEDVVVNGGVKSLVYSSILFRTAIDERYFFGIRLAACEALSKYVYDPDFTGGVKHLIQIFQILFCLEDSNIPKSNNFENPKLYFLQCNIPKYLAKVKNENGKCPKLVKQFLLDILVYNENGENKYSDDAYVRSLIENVVKVALNEYKDKAYMEKVKTQLLRYENLVNWLSSYESLIKTTIMYAKYKLHKVGAYDFTELTGMIMHTLTLGINNGDISRESFQNEFLMVLKIMLLEGGLKNKDALVLFTEILCFHEDSYIRDKSVDVLSECVNLVVMDGSLDTISDDIKSSVQSVHNEVKNIKSEDDIELFLSGHYVDDMKIKIEKIGRQNISGLIQICRDMFKGYSPLKILLWDVLNLPVLSLYQRKQIHDLVRVMYTLINSFVVRLETPRERRLVAKMNSNEEGKLDIVIKRESILKVHIKKEVTSTVEAPKKANKIKISLKGDKPVRKVEKQIVKPKVTSKQRKVKSHVNRMGSLPLRFVKIQQQPRVMVHLSSVPYSQFVQITKVTSRSFMVKIRTKNDAKN
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
3Phosphorylation-----MMSFSKNATP
-----CCCCCCCCCC		37.9219823750
5Phosphorylation---MMSFSKNATPRA
---CCCCCCCCCCCE		20.0719823750
6Acetylation--MMSFSKNATPRAI
--CCCCCCCCCCCEE		48.9025381059
9PhosphorylationMSFSKNATPRAIVSE
CCCCCCCCCCEEECC		23.7720377248
15PhosphorylationATPRAIVSESSTLHE
CCCCEEECCCCCHHH		26.1623749301
17PhosphorylationPRAIVSESSTLHEMK
CCEEECCCCCHHHHH		22.5519823750
18PhosphorylationRAIVSESSTLHEMKF
CEEECCCCCHHHHHC		30.8228152593
19PhosphorylationAIVSESSTLHEMKFR
EEECCCCCHHHHHCC		41.2217563356
120UbiquitinationQSHFLRSKFASLNEY
HHHHHHHHCCCCCCC		38.2223749301
147PhosphorylationIPSSIKISLEDANAL
CCCCEEEEHHHHHHH		22.2430377154
155PhosphorylationLEDANALSNYTPITP
HHHHHHHCCCCCCCC		25.9422369663
157PhosphorylationDANALSNYTPITPSI
HHHHHCCCCCCCCCC		15.5422369663
158PhosphorylationANALSNYTPITPSIK
HHHHCCCCCCCCCCC		16.6822369663
161PhosphorylationLSNYTPITPSIKTTP
HCCCCCCCCCCCCCC		16.5222369663
163PhosphorylationNYTPITPSIKTTPGF
CCCCCCCCCCCCCCC		28.2422369663
166PhosphorylationPITPSIKTTPGFQES
CCCCCCCCCCCCCCC		36.2328889911
261PhosphorylationIGQNGEESEKEKEDT
CCCCCCCCCCCCCCC		50.0622369663
268PhosphorylationSEKEKEDTPEHDEEE
CCCCCCCCCCCCHHH		31.5017330950
318PhosphorylationEEEEEGESDEEEEEG
HHHHCCCCHHHHHHH		62.2717330950
335PhosphorylationERRNIEESNNPSLRD
HHHHHHHHCCCCHHH		29.1727017623
351PhosphorylationIVCCSEYSNIKELPH
HHHCCCCCCCCCCCC		28.2027017623
663UbiquitinationHVCERVNKSKLENFF
HHHHHCCHHHHHHHH		46.2217644757
665UbiquitinationCERVNKSKLENFFNE
HHHCCHHHHHHHHHH		62.5217644757
773AcetylationIDIQYNTKYRRLRKR
EEEEHHHHHHHHHHC		32.8724489116
926PhosphorylationACEALSKYVYDPDFT
HHHHHHHHCCCCCCC		10.8125521595
928PhosphorylationEALSKYVYDPDFTGG
HHHHHHCCCCCCCCH		20.7625521595
1309PhosphorylationHIKKEVTSTVEAPKK
EEEEEEECCEECCCC		35.3130377154
1310PhosphorylationIKKEVTSTVEAPKKA
EEEEEECCEECCCCC		17.0130377154
1358PhosphorylationSHVNRMGSLPLRFVK
HHHHHCCCCCEEEEE		19.9230377154
1365UbiquitinationSLPLRFVKIQQQPRV
CCCEEEEEECCCCEE		31.8923749301
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 TAF2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAF2_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 TAF2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAF14_YEASTTAF14physical
11805826
TAF1_YEASTTAF1physical
11805826
TAF11_YEASTTAF11physical
11805826
TAF6_YEASTTAF6physical
11805826
TAF8_YEASTTAF8physical
11805826
TAF5_YEASTTAF5physical
11805826
EF1G2_YEASTTEF4physical
11805826
TBP_YEASTSPT15physical
12052880
TBP_YEASTSPT15physical
10788514
TAF1_YEASTTAF1physical
12052880
TAF1_YEASTTAF1physical
10788514
CFT1_YEASTCFT1physical
12052880
CFT2_YEASTCFT2physical
12052880
FIP1_YEASTFIP1physical
12052880
GCR1_YEASTGCR1physical
12052880
LEUR_YEASTLEU3physical
12052880
MPE1_YEASTMPE1physical
12052880
MSN2_YEASTMSN2physical
12052880
PAP_YEASTPAP1physical
12052880
PTA1_YEASTPTA1physical
12052880
REF2_YEASTREF2physical
12052880
SSU72_YEASTSSU72physical
12052880
TAF2_YEASTTAF2physical
12052880
TAF9_YEASTTAF9physical
12052880
TAF13_YEASTTAF13physical
12052880
TAF10_YEASTTAF10physical
12052880
TAF14_YEASTTAF14physical
12052880
TAF11_YEASTTAF11physical
12052880
TAF3_YEASTTAF3physical
12052880
TAF4_YEASTTAF4physical
12052880
TAF6_YEASTTAF6physical
12052880
TAF12_YEASTTAF12physical
12052880
TAF8_YEASTTAF8physical
12052880
TAF7_YEASTTAF7physical
12052880
TAF5_YEASTTAF5physical
12052880
YSH1_YEASTYSH1physical
12052880
TBP_YEASTSPT15physical
8340360
TBP_YEASTSPT15physical
8083216
TBP_YEASTSPT15physical
7667272
TAF6_YEASTTAF6physical
12582245
TAF11_YEASTTAF11physical
9083082
TAF10_YEASTTAF10physical
8662725
TAF14_YEASTTAF14physical
15896708
TAF1_YEASTTAF1physical
16429126
TAF14_YEASTTAF14physical
16429126
TAF5_YEASTTAF5physical
16429126
TAF6_YEASTTAF6physical
16429126
TAF8_YEASTTAF8physical
16429126
EF1G2_YEASTTEF4physical
16429126
TAF11_YEASTTAF11physical
16429126
TAF7_YEASTTAF7physical
27587401
TAF8_YEASTTAF8physical
27587401
TAF14_YEASTTAF14physical
27587401
TAF14_YEASTTAF14genetic
27587401
TAF4_YEASTTAF4physical
27587401
TAF9_YEASTTAF9physical
27587401
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TAF2_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-18; THR-19; THR-158;THR-161; SER-163; THR-166 AND SER-318, 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 THR-19 AND SER-318, 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-318, AND MASSSPECTROMETRY.
"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 THR-268, AND MASSSPECTROMETRY.

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