TAF3_HUMAN - dbPTM
TAF3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAF3_HUMAN
UniProt AC Q5VWG9
Protein Name Transcription initiation factor TFIID subunit 3
Gene Name TAF3
Organism Homo sapiens (Human).
Sequence Length 929
Subcellular Localization Nucleus .
Protein Description Transcription factor TFIID is one of the general factors required for accurate and regulated initiation by RNA polymerase II. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Required in complex with TBPL2 for the differentiation of myoblasts into myocytes. The complex replaces TFIID at specific promoters at an early stage in the differentiation process..
Protein Sequence MCESYSRSLLRVSVAQICQALGWDSVQLSACHLLTDVLQRYLQQLGRGCHRYSELYGRTDPILDDVGEAFQLMGVSLHELEDYIHNIEPVTFPHQIPSFPVSKNNVLQFPQPGSKDAEERKEYIPDYLPPIVSSQEEEEEEQVPTDGGTSAEAMQVPLEEDDELEEEEIINDENFLGKRPLDSPEAEELPAMKRPRLLSTKGDTLDVVLLEAREPLSSINTQKIPPMLSPVHVQDSTDLAPPSPEPPMLAPVAKSQMPTAKPLETKSFTPKTKTKTSSPGQKTKSPKTAQSPAMVGSPIRSPKTVSKEKKSPGRSKSPKSPKSPKVTTHIPQTPVRPETPNRTPSATLSEKISKETIQVKQIQTPPDAGKLNSENQPKKAVVADKTIEASIDAVIARACAEREPDPFEFSSGSESEGDIFTSPKRISGPECTTPKASTSANNFTKSGSTPLPLSGGTSSSDNSWTMDASIDEVVRKAKLGTPSNMPPNFPYISSPSVSPPTPEPLHKVYEEKTKLPSSVEVKKKLKKELKTKMKKKEKQRDREREKDKNKDKSKEKDKVKEKEKDKETGRETKYPWKEFLKEEEADPYKFKIKEFEDVDPKVKLKDGLVRKEKEKHKDKKKDREKGKKDKDKREKEKVKDKGREDKMKAPAPPLVLPPKELALPLFSPATASRVPAMLPSLLPVLPEKLFEEKEKVKEKEKKKDKKEKKKKKEKEKEKKEKEREKEKREREKREKEKEKHKHEKIKVEPVALAPSPVIPRLTLRVGAGQDKIVISKVVPAPEAKPAPSQNRPKTPPPAPAPAPGPMLVSPAPVPLPLLAQAAAGPALLPSPGPAASGASAKAPVRSVVTETVSTYVIRDEWGNQIWICPGCNKPDDGSPMIGCDDCDDWYHWPCVGIMTAPPEEMQWFCPKCANKKKDKKHKKRKHRAH
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
52PhosphorylationLGRGCHRYSELYGRT
HCCHHHHHHHHHCCC		5.26-
56PhosphorylationCHRYSELYGRTDPIL
HHHHHHHHCCCCCCH		10.66-
114PhosphorylationLQFPQPGSKDAEERK
ECCCCCCCCCHHHHH		33.7625159151
183PhosphorylationLGKRPLDSPEAEELP
CCCCCCCCCCHHHCC		32.1129255136
199PhosphorylationMKRPRLLSTKGDTLD
CCCCCCCCCCCCCEE		32.4422617229
200PhosphorylationKRPRLLSTKGDTLDV
CCCCCCCCCCCCEEE		38.7327273156
204PhosphorylationLLSTKGDTLDVVLLE
CCCCCCCCEEEEEEE		33.2622617229
221PhosphorylationEPLSSINTQKIPPML
CCHHHCCCCCCCCCC		29.5726074081
229PhosphorylationQKIPPMLSPVHVQDS
CCCCCCCCCCEECCC		20.7225159151
236PhosphorylationSPVHVQDSTDLAPPS
CCCEECCCCCCCCCC		13.5130278072
237PhosphorylationPVHVQDSTDLAPPSP
CCEECCCCCCCCCCC		43.2330278072
243PhosphorylationSTDLAPPSPEPPMLA
CCCCCCCCCCCCCCC		40.6225159151
255PhosphorylationMLAPVAKSQMPTAKP
CCCCHHHCCCCCCCC		23.2126074081
256PhosphorylationLAPVAKSQMPTAKPL
CCCHHHCCCCCCCCC		40.9620736484
257PhosphorylationAPVAKSQMPTAKPLE
CCHHHCCCCCCCCCC		4.0420736484
259PhosphorylationVAKSQMPTAKPLETK
HHHCCCCCCCCCCCC		41.8126074081
261AcetylationKSQMPTAKPLETKSF
HCCCCCCCCCCCCCC		53.2525953088
265PhosphorylationPTAKPLETKSFTPKT
CCCCCCCCCCCCCCC		39.4029083192
266AcetylationTAKPLETKSFTPKTK
CCCCCCCCCCCCCCC		33.9119608861
267PhosphorylationAKPLETKSFTPKTKT
CCCCCCCCCCCCCCC		41.6022817900
269PhosphorylationPLETKSFTPKTKTKT
CCCCCCCCCCCCCCC		30.8524719451
272PhosphorylationTKSFTPKTKTKTSSP
CCCCCCCCCCCCCCC		45.1929083192
276PhosphorylationTPKTKTKTSSPGQKT
CCCCCCCCCCCCCCC		39.4028176443
277PhosphorylationPKTKTKTSSPGQKTK
CCCCCCCCCCCCCCC		35.7728176443
278PhosphorylationKTKTKTSSPGQKTKS
CCCCCCCCCCCCCCC		37.9828176443
288PhosphorylationQKTKSPKTAQSPAMV
CCCCCCCCCCCCCCC		33.0623927012
291PhosphorylationKSPKTAQSPAMVGSP
CCCCCCCCCCCCCCC		16.5023927012
294SulfoxidationKTAQSPAMVGSPIRS
CCCCCCCCCCCCCCC		3.8921406390
297PhosphorylationQSPAMVGSPIRSPKT
CCCCCCCCCCCCCCC		13.0225159151
301PhosphorylationMVGSPIRSPKTVSKE
CCCCCCCCCCCCCCC		31.3123927012
304PhosphorylationSPIRSPKTVSKEKKS
CCCCCCCCCCCCCCC		33.1426074081
315PhosphorylationEKKSPGRSKSPKSPK
CCCCCCCCCCCCCCC		43.3223911959
317PhosphorylationKSPGRSKSPKSPKSP
CCCCCCCCCCCCCCC		38.5124275569
320PhosphorylationGRSKSPKSPKSPKVT
CCCCCCCCCCCCCCC		40.7323911959
323PhosphorylationKSPKSPKSPKVTTHI
CCCCCCCCCCCCCCC		33.0823911959
327PhosphorylationSPKSPKVTTHIPQTP
CCCCCCCCCCCCCCC		20.8429978859
328PhosphorylationPKSPKVTTHIPQTPV
CCCCCCCCCCCCCCC		22.3129978859
333PhosphorylationVTTHIPQTPVRPETP
CCCCCCCCCCCCCCC		20.5630266825
339PhosphorylationQTPVRPETPNRTPSA
CCCCCCCCCCCCCCC		28.6630266825
343PhosphorylationRPETPNRTPSATLSE
CCCCCCCCCCCCCCH		28.3825159151
345PhosphorylationETPNRTPSATLSEKI
CCCCCCCCCCCCHHH		33.0229978859
347PhosphorylationPNRTPSATLSEKISK
CCCCCCCCCCHHHCC		34.8429978859
349PhosphorylationRTPSATLSEKISKET
CCCCCCCCHHHCCCC		32.2729978859
360AcetylationSKETIQVKQIQTPPD
CCCCEEEEECCCCCC		25.8826051181
364PhosphorylationIQVKQIQTPPDAGKL
EEEEECCCCCCCCCC		38.1230266825
370UbiquitinationQTPPDAGKLNSENQP
CCCCCCCCCCCCCCC		46.3329967540
370AcetylationQTPPDAGKLNSENQP
CCCCCCCCCCCCCCC		46.3325953088
373PhosphorylationPDAGKLNSENQPKKA
CCCCCCCCCCCCCCE		48.6530266825
410PhosphorylationEPDPFEFSSGSESEG
CCCCCCCCCCCCCCC		26.9621082442
411PhosphorylationPDPFEFSSGSESEGD
CCCCCCCCCCCCCCC		52.2220873877
413PhosphorylationPFEFSSGSESEGDIF
CCCCCCCCCCCCCCC		39.6420873877
415PhosphorylationEFSSGSESEGDIFTS
CCCCCCCCCCCCCCC		48.8820873877
421PhosphorylationESEGDIFTSPKRISG
CCCCCCCCCCCCCCC		44.4426552605
422PhosphorylationSEGDIFTSPKRISGP
CCCCCCCCCCCCCCC		20.0626552605
427PhosphorylationFTSPKRISGPECTTP
CCCCCCCCCCCCCCC		52.9428450419
432PhosphorylationRISGPECTTPKASTS
CCCCCCCCCCCCCCC		44.4629255136
433PhosphorylationISGPECTTPKASTSA
CCCCCCCCCCCCCCC		34.1629255136
437PhosphorylationECTTPKASTSANNFT
CCCCCCCCCCCCCCC		29.0823312004
438PhosphorylationCTTPKASTSANNFTK
CCCCCCCCCCCCCCC		36.4023312004
439PhosphorylationTTPKASTSANNFTKS
CCCCCCCCCCCCCCC		26.8928674419
444PhosphorylationSTSANNFTKSGSTPL
CCCCCCCCCCCCCCC		26.8223312004
481PhosphorylationVRKAKLGTPSNMPPN
HHHHCCCCCCCCCCC		33.7026074081
483PhosphorylationKAKLGTPSNMPPNFP
HHCCCCCCCCCCCCC		45.6726074081
491PhosphorylationNMPPNFPYISSPSVS
CCCCCCCCCCCCCCC		14.8626074081
493PhosphorylationPPNFPYISSPSVSPP
CCCCCCCCCCCCCCC		30.2826074081
494PhosphorylationPNFPYISSPSVSPPT
CCCCCCCCCCCCCCC		16.1926074081
496PhosphorylationFPYISSPSVSPPTPE
CCCCCCCCCCCCCCC		36.8626074081
498PhosphorylationYISSPSVSPPTPEPL
CCCCCCCCCCCCCCH		29.5126074081
501PhosphorylationSPSVSPPTPEPLHKV
CCCCCCCCCCCHHHH		43.6026074081
517PhosphorylationEEKTKLPSSVEVKKK
HHHCCCCCHHHHHHH		58.4125159151
518PhosphorylationEKTKLPSSVEVKKKL
HHCCCCCHHHHHHHH		21.9821815630
522AcetylationLPSSVEVKKKLKKEL
CCCHHHHHHHHHHHH		30.5925953088
568PhosphorylationEKEKDKETGRETKYP
HHHHHHHCCCCCCCC		47.48-
572PhosphorylationDKETGRETKYPWKEF
HHHCCCCCCCCHHHH		34.22-
581SumoylationYPWKEFLKEEEADPY
CCHHHHHHHHCCCCC		69.2928112733
601AcetylationEFEDVDPKVKLKDGL
ECCCCCCCCCCCCCH		47.7624848833
621AcetylationEKHKDKKKDREKGKK
HHCCCHHHHHHHCCC		68.6988967
625AcetylationDKKKDREKGKKDKDK
CHHHHHHHCCCCHHH		76.5488969
628AcetylationKDREKGKKDKDKREK
HHHHHCCCCHHHHHH		77.8888965
667PhosphorylationELALPLFSPATASRV
HHCCCCCCCCHHHCC		22.7029255136
670PhosphorylationLPLFSPATASRVPAM
CCCCCCCHHHCCCCH		28.6629255136
672PhosphorylationLFSPATASRVPAMLP
CCCCCHHHCCCCHHH		29.4729255136
677SulfoxidationTASRVPAMLPSLLPV
HHHCCCCHHHHHHHH		4.6521406390
746SumoylationKHKHEKIKVEPVALA
HHHCCCCCCEECEEC		52.17-
746SumoylationKHKHEKIKVEPVALA
HHHCCCCCCEECEEC		52.1728112733
755PhosphorylationEPVALAPSPVIPRLT
EECEECCCCCCCCEE		26.6230266825
762PhosphorylationSPVIPRLTLRVGAGQ
CCCCCCEEEEECCCC		17.50-
771AcetylationRVGAGQDKIVISKVV
EECCCCCEEEEEEEE		30.8725953088
776AcetylationQDKIVISKVVPAPEA
CCEEEEEEEEECCCC		35.8119608861
784AcetylationVVPAPEAKPAPSQNR
EEECCCCCCCCCCCC		39.8023236377
794PhosphorylationPSQNRPKTPPPAPAP
CCCCCCCCCCCCCCC		43.6525159151
809PhosphorylationAPGPMLVSPAPVPLP
CCCCEEEECCCCCHH		16.0425159151
830PhosphorylationAGPALLPSPGPAASG
HCCCCCCCCCCCCCC		42.3225627689
846PhosphorylationSAKAPVRSVVTETVS
CCCCCHHHEEECEEE		22.6025627689
849PhosphorylationAPVRSVVTETVSTYV
CCHHHEEECEEEEEE		24.6325627689
851PhosphorylationVRSVVTETVSTYVIR
HHHEEECEEEEEEEE		15.4725627689
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 TAF3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAF3_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 TAF3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBPL2_HUMANTBPL2physical
17704303
TBP_HUMANTBPphysical
11438666
KAT2A_HUMANKAT2Aphysical
11438666
TAF10_HUMANTAF10physical
11438666
TAF12_HUMANTAF12physical
11438666
TAF13_HUMANTAF13physical
11438666
SP130_HUMANSAP130physical
11438666
TAF7_HUMANTAF7physical
11438666
TBP_HUMANTBPphysical
21884934
CTCF_HUMANCTCFphysical
21884934
TAF5_HUMANTAF5physical
22939629
TAF4_HUMANTAF4physical
22939629
TAF6_HUMANTAF6physical
22939629
IMA1_HUMANKPNA2physical
15870280
IMB1_HUMANKPNB1physical
15870280
H31T_HUMANHIST3H3physical
17884155
CDC23_HUMANCDC23physical
26344197
NP1L4_HUMANNAP1L4physical
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 TAF3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-266 AND LYS-776, AND MASSSPECTROMETRY.
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-199; SER-229; SER-243;SER-297; SER-301 AND THR-501, AND MASS SPECTROMETRY.
"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 SER-229; SER-243; SER-291;SER-297 AND THR-364, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND MASSSPECTROMETRY.
"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-183; SER-410; SER-411;SER-413 AND SER-415, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229; SER-236; SER-243;SER-297 AND SER-410, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory