TAF9B_HUMAN - dbPTM
TAF9B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAF9B_HUMAN
UniProt AC Q9HBM6
Protein Name Transcription initiation factor TFIID subunit 9B
Gene Name TAF9B
Organism Homo sapiens (Human).
Sequence Length 251
Subcellular Localization Nucleus.
Protein Description Essential for cell viability. TAF9 and TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes. May have a role in gene regulation associated with apoptosis. TAFs are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription..
Protein Sequence MESGKMAPPKNAPRDALVMAQILKDMGITEYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPNVDADDVRLAIQCRADQSFTSPPPRDFLLDIARQKNQTPLPLIKPYAGPRLPPDRYCLTAPNYRLKSLIKKGPNQGRLVPRLSVGAVSSKPTTPTIATPQTVSVPNKVATPMSVTSQRFTVQIPPSQSTPVKPVPATTAVQNVLINPSMIGPKNILITTNMVSSQNTANEANPLKRKHEDDDDNDIM
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
1Acetylation-------MESGKMAP
-------CCCCCCCC		9.2622814378
3Phosphorylation-----MESGKMAPPK
-----CCCCCCCCCC		42.2720860994
5Ubiquitination---MESGKMAPPKNA
---CCCCCCCCCCCC		40.9622505724
5Acetylation---MESGKMAPPKNA
---CCCCCCCCCCCC		40.9625953088
10UbiquitinationSGKMAPPKNAPRDAL
CCCCCCCCCCCHHHH		65.76-
24UbiquitinationLVMAQILKDMGITEY
HHHHHHHHHCCCCCC		47.5022817900
46PhosphorylationMLEFAFRYVTTILDD
HHHHHHHHHHHHHHH		8.8329083192
48PhosphorylationEFAFRYVTTILDDAK
HHHHHHHHHHHHHHH		10.1329083192
49PhosphorylationFAFRYVTTILDDAKI
HHHHHHHHHHHHHHH		14.9729083192
55UbiquitinationTTILDDAKIYSSHAK
HHHHHHHHHHHCCCC		49.52-
57PhosphorylationILDDAKIYSSHAKKP
HHHHHHHHHCCCCCC		11.92-
62UbiquitinationKIYSSHAKKPNVDAD
HHHHCCCCCCCCCHH		64.4429967540
63AcetylationIYSSHAKKPNVDADD
HHHCCCCCCCCCHHH		42.4826051181
63UbiquitinationIYSSHAKKPNVDADD
HHHCCCCCCCCCHHH		42.4829967540
82PhosphorylationIQCRADQSFTSPPPR
HCCCCCCCCCCCCCC		30.9229396449
84PhosphorylationCRADQSFTSPPPRDF
CCCCCCCCCCCCCHH		45.6421815630
85PhosphorylationRADQSFTSPPPRDFL
CCCCCCCCCCCCHHH		33.1425159151
99UbiquitinationLLDIARQKNQTPLPL
HHHHHHHCCCCCCCC		45.53-
102PhosphorylationIARQKNQTPLPLIKP
HHHHCCCCCCCCCCC		35.8725159151
108UbiquitinationQTPLPLIKPYAGPRL
CCCCCCCCCCCCCCC		39.3929967540
108AcetylationQTPLPLIKPYAGPRL
CCCCCCCCCCCCCCC		39.3926051181
119MethylationGPRLPPDRYCLTAPN
CCCCCCCCCEECCCC		29.82-
128MethylationCLTAPNYRLKSLIKK
EECCCCHHHHHHHHH		42.1326494477
131PhosphorylationAPNYRLKSLIKKGPN
CCCHHHHHHHHHCCC		39.6624719451
147PhosphorylationGRLVPRLSVGAVSSK
CCCCCCEEECCCCCC		21.5626055452
152PhosphorylationRLSVGAVSSKPTTPT
CEEECCCCCCCCCCC		31.9130278072
152O-linked_GlycosylationRLSVGAVSSKPTTPT
CEEECCCCCCCCCCC		31.9130059200
153O-linked_GlycosylationLSVGAVSSKPTTPTI
EEECCCCCCCCCCCC		35.7430059200
153PhosphorylationLSVGAVSSKPTTPTI
EEECCCCCCCCCCCC		35.7428355574
154AcetylationSVGAVSSKPTTPTIA
EECCCCCCCCCCCCC		38.5926051181
156PhosphorylationGAVSSKPTTPTIATP
CCCCCCCCCCCCCCC		49.5026055452
156O-linked_GlycosylationGAVSSKPTTPTIATP
CCCCCCCCCCCCCCC		49.5030059200
157O-linked_GlycosylationAVSSKPTTPTIATPQ
CCCCCCCCCCCCCCC		27.2830059200
157PhosphorylationAVSSKPTTPTIATPQ
CCCCCCCCCCCCCCC		27.2828355574
159O-linked_GlycosylationSSKPTTPTIATPQTV
CCCCCCCCCCCCCEE		22.5830059200
159PhosphorylationSSKPTTPTIATPQTV
CCCCCCCCCCCCCEE		22.5822617229
162O-linked_GlycosylationPTTPTIATPQTVSVP
CCCCCCCCCCEEECC		16.4530059200
162PhosphorylationPTTPTIATPQTVSVP
CCCCCCCCCCEEECC		16.4526055452
165PhosphorylationPTIATPQTVSVPNKV
CCCCCCCEEECCCCE		18.8926074081
167O-linked_GlycosylationIATPQTVSVPNKVAT
CCCCCEEECCCCEEC		34.9330059200
167PhosphorylationIATPQTVSVPNKVAT
CCCCCEEECCCCEEC		34.9326074081
174PhosphorylationSVPNKVATPMSVTSQ
ECCCCEECCCEEECC		23.6325159151
177O-linked_GlycosylationNKVATPMSVTSQRFT
CCEECCCEEECCEEE		24.3630059200
177PhosphorylationNKVATPMSVTSQRFT
CCEECCCEEECCEEE		24.3625159151
179PhosphorylationVATPMSVTSQRFTVQ
EECCCEEECCEEEEE		16.3120068231
180PhosphorylationATPMSVTSQRFTVQI
ECCCEEECCEEEEEC		19.7320068231
190PhosphorylationFTVQIPPSQSTPVKP
EEEECCCCCCCCCCC		31.26-
192PhosphorylationVQIPPSQSTPVKPVP
EECCCCCCCCCCCCC		38.73-
193PhosphorylationQIPPSQSTPVKPVPA
ECCCCCCCCCCCCCC		25.19-
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 TAF9B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAF9B_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 TAF9B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI15_HUMANTRIM15physical
20211142
A4_HUMANAPPphysical
21832049
TRRAP_HUMANTRRAPphysical
15899866
TAF9B_HUMANTAF9Bphysical
15899866
TAF1_HUMANTAF1physical
15899866
TAF5_HUMANTAF5physical
15899866
KAT2A_HUMANKAT2Aphysical
15899866
TAF6_HUMANTAF6physical
15899866
TAF7_HUMANTAF7physical
15899866
TBP_HUMANTBPphysical
15899866
TAF9_HUMANTAF9physical
15899866
TAF4_HUMANTAF4physical
26344197
TAF5_HUMANTAF5physical
26344197
TAF6_HUMANTAF6physical
26344197
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 TAF9B_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 THR-159, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-157, AND MASSSPECTROMETRY.

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