TAF7_HUMAN - dbPTM
TAF7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAF7_HUMAN
UniProt AC Q15545
Protein Name Transcription initiation factor TFIID subunit 7
Gene Name TAF7
Organism Homo sapiens (Human).
Sequence Length 349
Subcellular Localization Nucleus .
Protein Description Functions as a component of the DNA-binding general transcription factor complex TFIID, a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Present in both of the previously described TFIID species which either lack or contain TAFII30 (TFIID alpha and TFIID beta respectively)..
Protein Sequence MSKSKDDAPHELESQFILRLPPEYASTVRRAVQSGHVNLKDRLTIELHPDGRHGIVRVDRVPLASKLVDLPCVMESLKTIDKKTFYKTADICQMLVSTVDGDLYPPVEEPVASTDPKASKKKDKDKEKKFIWNHGITLPLKNVRKRRFRKTAKKKYIESPDVEKEVKRLLSTDAEAVSTRWEIIAEDETKEAENQGLDISSPGMSGHRQGHDSLEHDELREIFNDLSSSSEDEDETQHQDEEDINIIDTEEDLERQLQDKLNESDEQHQENEGTNQLVMGIQKQIDNMKGKLQETQDRAKRQEDLIMKVENLALKNRFQAVLDELKQKEDREKEQLSSLQEELESLLEK
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
2Phosphorylation------MSKSKDDAP
------CCCCCCCCC		45.7130108239
3Acetylation-----MSKSKDDAPH
-----CCCCCCCCCC		61.2925953088
4Phosphorylation----MSKSKDDAPHE
----CCCCCCCCCCC		33.7330108239
5Methylation---MSKSKDDAPHEL
---CCCCCCCCCCCH		64.4616415881
5Acetylation---MSKSKDDAPHEL
---CCCCCCCCCCCH		64.4625953088
5Ubiquitination---MSKSKDDAPHEL
---CCCCCCCCCCCH		64.4629967540
24PhosphorylationILRLPPEYASTVRRA
HHHCCHHHHHHHHHH		16.1827642862
34PhosphorylationTVRRAVQSGHVNLKD
HHHHHHHHCCCCCHH		25.0325159151
40UbiquitinationQSGHVNLKDRLTIEL
HHCCCCCHHCEEEEE		35.2832015554
66UbiquitinationDRVPLASKLVDLPCV
CCCCCCHHHCCCHHH		47.0932015554
78UbiquitinationPCVMESLKTIDKKTF
HHHHHHHCCCCHHHH		53.3532015554
129SumoylationKDKDKEKKFIWNHGI
CCCHHCHHHHHCCCC		43.08-
129SumoylationKDKDKEKKFIWNHGI
CCCHHCHHHHHCCCC		43.08-
141UbiquitinationHGITLPLKNVRKRRF
CCCCCCCCHHHHHHH		52.0023000965
145UbiquitinationLPLKNVRKRRFRKTA
CCCCHHHHHHHHHHH		43.5823000965
155UbiquitinationFRKTAKKKYIESPDV
HHHHHHHHHCCCCCH		51.2429967540
156PhosphorylationRKTAKKKYIESPDVE
HHHHHHHHCCCCCHH		20.8521406692
159PhosphorylationAKKKYIESPDVEKEV
HHHHHCCCCCHHHHH		19.4925159151
171PhosphorylationKEVKRLLSTDAEAVS
HHHHHHHHCCHHHHH		28.9129255136
172PhosphorylationEVKRLLSTDAEAVST
HHHHHHHCCHHHHHH		38.9230266825
178PhosphorylationSTDAEAVSTRWEIIA
HCCHHHHHHHEEEEE		21.2124670416
179PhosphorylationTDAEAVSTRWEIIAE
CCHHHHHHHEEEEEE		32.9524670416
200PhosphorylationENQGLDISSPGMSGH
HHCCCCCCCCCCCCC		30.1029255136
201PhosphorylationNQGLDISSPGMSGHR
HCCCCCCCCCCCCCC		26.3029255136
205PhosphorylationDISSPGMSGHRQGHD
CCCCCCCCCCCCCCC		37.0430266825
213PhosphorylationGHRQGHDSLEHDELR
CCCCCCCCCCHHHHH		29.9525159151
227PhosphorylationREIFNDLSSSSEDED
HHHHHHHCCCCCCCH		30.9126552605
228PhosphorylationEIFNDLSSSSEDEDE
HHHHHHCCCCCCCHH		45.2226552605
229PhosphorylationIFNDLSSSSEDEDET
HHHHHCCCCCCCHHH		34.0826552605
230PhosphorylationFNDLSSSSEDEDETQ
HHHHCCCCCCCHHHC		51.5226552605
236PhosphorylationSSEDEDETQHQDEED
CCCCCHHHCCCCHHH		43.6126552605
249PhosphorylationEDINIIDTEEDLERQ
HHCCEECCHHHHHHH		30.7621406692
264PhosphorylationLQDKLNESDEQHQEN
HHHHCHHHHHHHHHC		45.4329255136
274PhosphorylationQHQENEGTNQLVMGI
HHHHCCHHHHHHHHH		17.3929255136
291AcetylationQIDNMKGKLQETQDR
HHHHHHHHHHHHHHH		41.2923749302
326UbiquitinationQAVLDELKQKEDREK
HHHHHHHHHHHHHHH		58.2224816145
337PhosphorylationDREKEQLSSLQEELE
HHHHHHHHHHHHHHH		28.7922199227
338PhosphorylationREKEQLSSLQEELES
HHHHHHHHHHHHHHH		42.5422199227
345PhosphorylationSLQEELESLLEK---
HHHHHHHHHHHC---		51.3724719451
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
264SPhosphorylationKinaseTAF1P21675
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
264SPhosphorylation

18669648
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 TAF7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAF1_HUMANTAF1physical
11592977
NEMO_HUMANIKBKGphysical
20211142
TRI22_HUMANTRIM22physical
20211142
ZSCA1_HUMANZSCAN1physical
20211142
THA_HUMANTHRAphysical
10409738
VDR_HUMANVDRphysical
10409738
CDK7_HUMANCDK7physical
18391197
CDK9_HUMANCDK9physical
18391197
CPSF1_HUMANCPSF1physical
9311784
TAF9_HUMANTAF9physical
22939629
TRRAP_HUMANTRRAPphysical
22939629
TAF13_HUMANTAF13physical
29111974
TAF11_HUMANTAF11physical
29111974
TAF1_HUMANTAF1physical
29111974
TAF2_HUMANTAF2physical
29111974
TAF3_HUMANTAF3physical
29111974
TAF4_HUMANTAF4physical
29111974
TAF4B_HUMANTAF4Bphysical
29111974
TAF5_HUMANTAF5physical
29111974
TAF6_HUMANTAF6physical
29111974
TAF8_HUMANTAF8physical
29111974
TAF9_HUMANTAF9physical
29111974
TAF9B_HUMANTAF9Bphysical
29111974
TAF10_HUMANTAF10physical
29111974
TAF12_HUMANTAF12physical
29111974
TBP_HUMANTBPphysical
29111974
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TAF7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND SER-264, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND SER-264, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201 AND SER-264, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; SER-227; SER-228;SER-229 AND SER-230, AND MASS SPECTROMETRY.

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