T2AG_YEAST - dbPTM
T2AG_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID T2AG_YEAST
UniProt AC P32774
Protein Name Transcription initiation factor IIA subunit 2
Gene Name TOA2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 122
Subcellular Localization Cytoplasm . Nucleus . Imported to nucleus via interaction with KAP122.
Protein Description TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity..
Protein Sequence MAVPGYYELYRRSTIGNSLVDALDTLISDGRIEASLAMRVLETFDKVVAETLKDNTQSKLTVKGNLDTYGFCDDVWTFIVKNCQVTVEDSHRDASQNGSGDSQSVISVDKLRIVACNSKKSE
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
6Phosphorylation--MAVPGYYELYRRS
--CCCCCCHHHHHCC
6.4130377154
7Phosphorylation-MAVPGYYELYRRST
-CCCCCCHHHHHCCC
12.8430377154
43PhosphorylationLAMRVLETFDKVVAE
HHHHHHHHHHHHHHH
32.7330377154
46AcetylationRVLETFDKVVAETLK
HHHHHHHHHHHHHHC
34.1224489116
53UbiquitinationKVVAETLKDNTQSKL
HHHHHHHCCCCCCCE
57.2523749301
86PhosphorylationIVKNCQVTVEDSHRD
EEECCEEEEEECCCC
7.7224961812
90PhosphorylationCQVTVEDSHRDASQN
CEEEEEECCCCHHHC
13.6028889911
95PhosphorylationEDSHRDASQNGSGDS
EECCCCHHHCCCCCC
28.5922369663
99PhosphorylationRDASQNGSGDSQSVI
CCHHHCCCCCCCCEE
47.1522369663
102PhosphorylationSQNGSGDSQSVISVD
HHCCCCCCCCEEEEE
28.0722369663
104PhosphorylationNGSGDSQSVISVDKL
CCCCCCCCEEEEEEE
25.9322369663
107PhosphorylationGDSQSVISVDKLRIV
CCCCCEEEEEEEEEE
23.3122369663

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 T2AG_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of T2AG_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 T2AG_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBP_YEASTSPT15physical
11223526
TF2B_YEASTSUA7physical
11223526
TAF11_YEASTTAF11physical
11238911
TOA1_YEASTTOA1physical
11238911
TBP_YEASTSPT15physical
12527429
SPT3_YEASTSPT3genetic
15132995
SPT8_YEASTSPT8genetic
15132995
GCN5_YEASTGCN5genetic
15340090
SNF2_YEASTSNF2genetic
15340090
RRT5_YEASTRRT5physical
16554755
RT18_YEASTMRPS18physical
16554755
YO093_YEASTYOR093Cphysical
16554755
TOA1_YEASTTOA1physical
16554755
AP1_YEASTYAP1physical
16835452
TBP_YEASTSPT15genetic
15340090
DBP5_YEASTDBP5genetic
22963203
TAF4_YEASTTAF4physical
23814059
TOA1_YEASTTOA1genetic
23814059
TAF11_YEASTTAF11genetic
23814059
TAF4_YEASTTAF4genetic
23814059

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of T2AG_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-95; SER-99; SER-102;SER-104 AND SER-107, 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-99 AND SER-102, AND MASSSPECTROMETRY.

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