TFB3_YEAST - dbPTM
TFB3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TFB3_YEAST
UniProt AC Q03290
Protein Name RNA polymerase II transcription factor B subunit 3
Gene Name TFB3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 321
Subcellular Localization Nucleus.
Protein Description Acts as component of the general transcription and DNA repair factor IIH (TFIIH or factor B), which is essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has CTD kinase and DNA-dependent ATPase activity, and is essential for polymerase II transcription in vitro..
Protein Sequence MLMDEYEENKDMCPICKTDRYLSPDVKFLVNPECYHRICESCVDRIFSLGPAQCPYKGCDKILRKNKFKTQIFDDVEVEKEVDIRKRVFNVFNKTIDDFNGDLVEYNKYLEEVEDIIYKLDHGIDVAKTEEKLRTYEELNKQLIMNNLERSRTEIESFEQRQKFEKEMKLKKRLLERQIEEEERMNKEWTKKEIVNRLSTTTQDINETIEGVKNTVKLKKSSARRKLEELNRVLKNNPYFNSNVNVQNSRLKDAVPFTPFNGDREAHPRFTLKGSVYNDPFIKDLEHRKEFIASGFNTNYAYERVLTEAFMGLGCVISEEL
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
151PhosphorylationIMNNLERSRTEIESF
HHHHHHHHHHHHHHH		33.8928889911
153PhosphorylationNNLERSRTEIESFEQ
HHHHHHHHHHHHHHH		42.4330377154
157PhosphorylationRSRTEIESFEQRQKF
HHHHHHHHHHHHHHH		39.4828889911
199PhosphorylationKEIVNRLSTTTQDIN
HHHHHHHHHCCHHHH		22.0719823750
200PhosphorylationEIVNRLSTTTQDINE
HHHHHHHHCCHHHHH		38.1519823750
201PhosphorylationIVNRLSTTTQDINET
HHHHHHHCCHHHHHH		21.0519823750
202PhosphorylationVNRLSTTTQDINETI
HHHHHHCCHHHHHHH		25.0819823750
208PhosphorylationTTQDINETIEGVKNT
CCHHHHHHHHHHHHH		21.6019795423
215PhosphorylationTIEGVKNTVKLKKSS
HHHHHHHHHHHCHHH		17.1919795423
239PhosphorylationRVLKNNPYFNSNVNV
HHHHHCCCCCCCCCC		19.9522369663
242PhosphorylationKNNPYFNSNVNVQNS
HHCCCCCCCCCCCCC		32.0522369663
258PhosphorylationLKDAVPFTPFNGDRE
CCCCCCCCCCCCCCC		22.3922369663
275PhosphorylationPRFTLKGSVYNDPFI
CCEEECCEECCCCCC		21.6021551504
307PhosphorylationYAYERVLTEAFMGLG
HHHHHHHHHHHHCCC		23.5525005228
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 TFB3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TFB3_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 TFB3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAD3_YEASTRAD3physical
11805837
RAD3_YEASTRAD3physical
10681587
KIN28_YEASTKIN28physical
9235928
KIN28_YEASTKIN28physical
14500720
CCL1_YEASTCCL1physical
14500720
CCL1_YEASTCCL1genetic
9294030
KIN28_YEASTKIN28genetic
9294030
RAD3_YEASTRAD3physical
16554755
SSL1_YEASTSSL1physical
16554755
TFB4_YEASTTFB4physical
16554755
HSP71_YEASTSSA1physical
19536198
SSB1_YEASTSSB1physical
19536198
RAD25_YEASTSSL2physical
19818408
RAD3_YEASTRAD3physical
19818408
TFB1_YEASTTFB1physical
19818408
TFB2_YEASTTFB2physical
19818408
SSL1_YEASTSSL1physical
19818408
CCL1_YEASTCCL1physical
19818408
TFB4_YEASTTFB4physical
19818408
KIN28_YEASTKIN28physical
19818408
RAD25_YEASTSSL2physical
22308316
RAD3_YEASTRAD3physical
22308316
TFB2_YEASTTFB2physical
22308316
SSL1_YEASTSSL1physical
22308316
TFB1_YEASTTFB1physical
22308316
CCL1_YEASTCCL1physical
22308316
TFB4_YEASTTFB4physical
22308316
KIN28_YEASTKIN28physical
22308316
TFB5_YEASTTFB5physical
22308316
RAD3_YEASTRAD3physical
22411836
TFB1_YEASTTFB1physical
22411836
TFB2_YEASTTFB2physical
22411836
SSL1_YEASTSSL1physical
22411836
CCL1_YEASTCCL1physical
22411836
TFB4_YEASTTFB4physical
22411836
KIN28_YEASTKIN28physical
22411836
RAD25_YEASTSSL2physical
22411836
YO352_YEASTTFB6physical
22411836
URA7_YEASTURA7genetic
27708008
SNF6_YEASTSNF6genetic
27708008
ERG3_YEASTERG3genetic
27708008
RAD3_YEASTRAD3physical
26340423
SSL1_YEASTSSL1physical
26340423
KIN28_YEASTKIN28physical
26340423
TFB1_YEASTTFB1physical
26340423
XRN1_YEASTXRN1genetic
27453043
CDC42_YEASTCDC42genetic
27453043
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TFB3_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-157 AND THR-258, 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-258, 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-258, 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 THR-258, AND MASSSPECTROMETRY.

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