TAF8_HUMAN - dbPTM
TAF8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAF8_HUMAN
UniProt AC Q7Z7C8
Protein Name Transcription initiation factor TFIID subunit 8
Gene Name TAF8
Organism Homo sapiens (Human).
Sequence Length 310
Subcellular Localization Nucleus . Cytoplasm. Localized in the cytoplasm and transported from the cytoplasm to the nucleus in some cells, possibly depending on the functional or developmental state of the cell..
Protein Description Transcription factor TFIID is one of the general factors required for accurate and regulated initiation by RNA polymerase II. Mediates both basal and activator-dependent transcription. Plays a role in the differentiation of preadipocyte fibroblasts to adipocytes, however, does not seem to play a role in differentiation of myoblasts. Required for the integration of TAF10 in the TAF complex. May be important for survival of cells of the inner cell mass which constitute the pluripotent cell population of the early embryo (By similarity)..
Protein Sequence MADAAATAGAGGSGTRSGSKQSTNPADNYHLARRRTLQVVVSSLLTEAGFESAEKASVETLTEMLQSYISEIGRSAKSYCEHTARTQPTLSDIVVTLVEMGFNVDTLPAYAKRSQRMVITAPPVTNQPVTPKALTAGQNRPHPPHIPSHFPEFPDPHTYIKTPTYREPVSDYQVLREKAASQRRDVERALTRFMAKTGETQSLFKDDVSTFPLIAARPFTIPYLTALLPSELEMQQMEETDSSEQDEQTDTENLALHISMEDSGAEKENTSVLQQNPSLSGSRNGEENIIDNPYLRPVKKPKIRRKKSLS
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
2Acetylation------MADAAATAG
------CCCHHHHCC		18.3622814378
7Phosphorylation-MADAAATAGAGGSG
-CCCHHHHCCCCCCC		22.3923186163
13PhosphorylationATAGAGGSGTRSGSK
HHCCCCCCCCCCCCC		35.7522199227
15PhosphorylationAGAGGSGTRSGSKQS
CCCCCCCCCCCCCCC		24.2925159151
17PhosphorylationAGGSGTRSGSKQSTN
CCCCCCCCCCCCCCC		47.4525627689
19PhosphorylationGSGTRSGSKQSTNPA
CCCCCCCCCCCCCCC		28.8625627689
36PhosphorylationYHLARRRTLQVVVSS
HHHCHHHHHHHHHHH		21.52-
42PhosphorylationRTLQVVVSSLLTEAG
HHHHHHHHHHHHHHC		12.0322210691
43PhosphorylationTLQVVVSSLLTEAGF
HHHHHHHHHHHHHCH		18.7822210691
46PhosphorylationVVVSSLLTEAGFESA
HHHHHHHHHHCHHHH		29.1422210691
52PhosphorylationLTEAGFESAEKASVE
HHHHCHHHHHHHCHH		39.1922210691
62PhosphorylationKASVETLTEMLQSYI
HHCHHHHHHHHHHHH		27.11-
78PhosphorylationEIGRSAKSYCEHTAR
HHHHHHHHHHHHHHC		34.43-
117SulfoxidationYAKRSQRMVITAPPV
HHHHCCCEEEECCCC		1.6621406390
120PhosphorylationRSQRMVITAPPVTNQ
HCCCEEEECCCCCCC		23.0022199227
125PhosphorylationVITAPPVTNQPVTPK
EEECCCCCCCCCCHH		33.6322199227
130PhosphorylationPVTNQPVTPKALTAG
CCCCCCCCHHHCCCC		26.2525159151
158PhosphorylationPEFPDPHTYIKTPTY
CCCCCCCCCCCCCCC		32.1228796482
159PhosphorylationEFPDPHTYIKTPTYR
CCCCCCCCCCCCCCC		9.4428796482
162PhosphorylationDPHTYIKTPTYREPV
CCCCCCCCCCCCCCC		16.0025159151
165PhosphorylationTYIKTPTYREPVSDY
CCCCCCCCCCCCCHH		17.7418083107
172PhosphorylationYREPVSDYQVLREKA
CCCCCCHHHHHHHHH		7.9428796482
202PhosphorylationAKTGETQSLFKDDVS
HHHCCCHHHHCCCCC		43.1024719451
270PhosphorylationSGAEKENTSVLQQNP
CCCCCCCCCHHHCCC		22.7025159151
271PhosphorylationGAEKENTSVLQQNPS
CCCCCCCCHHHCCCC		32.2021815630
278PhosphorylationSVLQQNPSLSGSRNG
CHHHCCCCCCCCCCC		42.5930266825
280PhosphorylationLQQNPSLSGSRNGEE
HHCCCCCCCCCCCCC		38.7729255136
282PhosphorylationQNPSLSGSRNGEENI
CCCCCCCCCCCCCCC		21.1329255136
308PhosphorylationPKIRRKKSLS-----
CCCCCCCCCC-----		36.56-
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 TAF8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAF8_HUMAN !!
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 TAF8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAF6_HUMANTAF6physical
17375202
TAF10_HUMANTAF10physical
17375202
TAF13_HUMANTAF13physical
17375202
TAF5_HUMANTAF5physical
17375202
TBP_HUMANTBPphysical
17375202
ST65G_HUMANSUPT7Lphysical
17375202
TAF8_HUMANTAF8physical
17375202
TAF10_HUMANTAF10physical
14580349
TAF6_HUMANTAF6physical
14580349
TAF11_HUMANTAF11physical
14580349
TBP_HUMANTBPphysical
14580349
TAF1_HUMANTAF1physical
14580349
TAF2_HUMANTAF2physical
14580349
TAF4_HUMANTAF4physical
14580349
TAF5_HUMANTAF5physical
14580349
TAF7_HUMANTAF7physical
14580349
TAF8_HUMANTAF8physical
14580349
TAF9_HUMANTAF9physical
14580349
IMA1_HUMANKPNA2physical
15870280
IMB1_HUMANKPNB1physical
15870280
MEF2A_HUMANMEF2Aphysical
23326349
GBB2_HUMANGNB2physical
23326349
TAF6_HUMANTAF6physical
26186194
TAF5_HUMANTAF5physical
26186194
TAF4B_HUMANTAF4Bphysical
26186194
TAF4_HUMANTAF4physical
26186194
TAF9B_HUMANTAF9Bphysical
26186194
TAF9_HUMANTAF9physical
26186194
TAF10_HUMANTAF10physical
26186194
ZDH17_HUMANZDHHC17physical
26186194
TAF12_HUMANTAF12physical
26186194
TAF1_HUMANTAF1physical
26186194
TAF2_HUMANTAF2physical
26186194
TAF7_HUMANTAF7physical
26186194
TAF3_HUMANTAF3physical
28514442
TAF2_HUMANTAF2physical
28514442
TAF1_HUMANTAF1physical
28514442
TAF4B_HUMANTAF4Bphysical
28514442
TAF9B_HUMANTAF9Bphysical
28514442
TAF5_HUMANTAF5physical
28514442
TAF6_HUMANTAF6physical
28514442
TAF11_HUMANTAF11physical
28514442
TAF4_HUMANTAF4physical
28514442
TAF7_HUMANTAF7physical
28514442
TAF9_HUMANTAF9physical
28514442
TAF12_HUMANTAF12physical
28514442
TAF13_HUMANTAF13physical
28514442
TAF10_HUMANTAF10physical
28514442
DCC1_HUMANDSCC1physical
28514442
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 TAF8_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 THR-130, AND MASSSPECTROMETRY.

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