TAF2_HUMAN - dbPTM
TAF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAF2_HUMAN
UniProt AC Q6P1X5
Protein Name Transcription initiation factor TFIID subunit 2
Gene Name TAF2
Organism Homo sapiens (Human).
Sequence Length 1199
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. It requires core promoter-specific cofactors for productive transcription stimulation. TAF2 stabilizes TFIID binding to core promoter..
Protein Sequence MPLTGVEPARMNRKKGDKGFESPRPYKLTHQVVCINNINFQRKSVVGFVELTIFPTVANLNRIKLNSKQCRIYRVRINDLEAAFIYNDPTLEVCHSESKQRNLNYFSNAYAAAVSAVDPDAGNGELCIKVPSELWKHVDELKVLKIHINFSLDQPKGGLHFVVPSVEGSMAERGAHVFSCGYQNSTRFWFPCVDSYSELCTWKLEFTVDAAMVAVSNGDLVETVYTHDMRKKTFHYMLTIPTAASNISLAIGPFEILVDPYMHEVTHFCLPQLLPLLKHTTSYLHEVFEFYEEILTCRYPYSCFKTVFIDEAYVEVAAYASMSIFSTNLLHSAMIIDETPLTRRCLAQSLAQQFFGCFISRMSWSDEWVLKGISGYIYGLWMKKTFGVNEYRHWIKEELDKIVAYELKTGGVLLHPIFGGGKEKDNPASHLHFSIKHPHTLSWEYYSMFQCKAHLVMRLIENRISMEFMLQVFNKLLSLASTASSQKFQSHMWSQMLVSTSGFLKSISNVSGKDIQPLIKQWVDQSGVVKFYGSFAFNRKRNVLELEIKQDYTSPGTQKYVGPLKVTVQELDGSFNHTLQIEENSLKHDIPCHSKSRRNKKKKIPLMNGEEVDMDLSAMDADSPLLWIRIDPDMSVLRKVEFEQADFMWQYQLRYERDVVAQQESILALEKFPTPASRLALTDILEQEQCFYRVRMSACFCLAKIANSMVSTWTGPPAMKSLFTRMFCCKSCPNIVKTNNFMSFQSYFLQKTMPVAMALLRDVHNLCPKEVLTFILDLIKYNDNRKNKFSDNYYRAEMIDALANSVTPAVSVNNEVRTLDNLNPDVRLILEEITRFLNMEKLLPSYRHTITVSCLRAIRVLQKNGHVPSDPALFKSYAEYGHFVDIRIAALEAVVDYTKVDRSYEELQWLLNMIQNDPVPYVRHKILNMLTKNPPFTKNMESPLCNEALVDQLWKLMNSGTSHDWRLRCGAVDLYFTLFGLSRPSCLPLPELGLVLNLKEKKAVLNPTIIPESVAGNQEAANNPSSHPQLVGFQNPFSSSQDEEEIDMDTVHDSQAFISHHLNMLERPSTPGLSKYRPASSRSALIPQHSAGCDSTPTTKPQWSLELARKGTGKEQAPLEMSMHPAASAPLSVFTKESTASKHSDHHHHHHHEHKKKKKKHKHKHKHKHKHDSKEKDKEPFTFSSPASGRSIRSPSLSD
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
22PhosphorylationKGDKGFESPRPYKLT
CCCCCCCCCCCCCCC		24.7720873877
73PhosphorylationNSKQCRIYRVRINDL
CCCCCEEEEEEECCE		5.4526657352
99UbiquitinationEVCHSESKQRNLNYF
EECCCHHHHHCHHHH		49.58-
132PhosphorylationELCIKVPSELWKHVD
CEEEECCHHHHHCHH		48.5923898821
136UbiquitinationKVPSELWKHVDELKV
ECCHHHHHCHHCCEE		46.50-
142UbiquitinationWKHVDELKVLKIHIN
HHCHHCCEEEEEEEE		43.40-
151PhosphorylationLKIHINFSLDQPKGG
EEEEEEEEECCCCCC		26.9224043423
169PhosphorylationVVPSVEGSMAERGAH
EEEECCCCHHHCCCE		11.00-
223PhosphorylationSNGDLVETVYTHDMR
CCCCEEEEEEECCCC		16.01-
225PhosphorylationGDLVETVYTHDMRKK
CCEEEEEEECCCCCC		13.04-
226PhosphorylationDLVETVYTHDMRKKT
CEEEEEEECCCCCCE		13.68-
401UbiquitinationWIKEELDKIVAYELK
HHHHHHHHHHHHCCC		52.27-
422AcetylationHPIFGGGKEKDNPAS
EECCCCCCCCCCCCC		65.9423954790
478PhosphorylationQVFNKLLSLASTASS
HHHHHHHHHHHHHCC		32.1228634298
481PhosphorylationNKLLSLASTASSQKF
HHHHHHHHHHCCHHH		29.7828634298
482PhosphorylationKLLSLASTASSQKFQ
HHHHHHHHHCCHHHH		25.5928634298
484PhosphorylationLSLASTASSQKFQSH
HHHHHHHCCHHHHHH		33.1328634298
485PhosphorylationSLASTASSQKFQSHM
HHHHHHCCHHHHHHH		34.6228634298
513UbiquitinationSISNVSGKDIQPLIK
HHHCCCCCCCHHHHH		44.12-
532PhosphorylationQSGVVKFYGSFAFNR
CCCCEEEEEEEHHCC		13.2222210691
534PhosphorylationGVVKFYGSFAFNRKR
CCEEEEEEEHHCCCC		11.3022210691
553PhosphorylationLEIKQDYTSPGTQKY
EEEEECCCCCCCEEE		36.4128270605
554PhosphorylationEIKQDYTSPGTQKYV
EEEECCCCCCCEEEE		18.3328270605
557PhosphorylationQDYTSPGTQKYVGPL
ECCCCCCCEEEEEEE		25.8528270605
559UbiquitinationYTSPGTQKYVGPLKV
CCCCCCEEEEEEEEE		41.56-
585PhosphorylationTLQIEENSLKHDIPC
EEEEECCCCCCCCCC		41.9121815630
617PhosphorylationEEVDMDLSAMDADSP
CEECCCHHHCCCCCC		19.7920068231
623PhosphorylationLSAMDADSPLLWIRI
HHHCCCCCCEEEEEE		21.1120068231
697PhosphorylationCFYRVRMSACFCLAK
HHHHHHHHHHHHHHH		16.01-
708PhosphorylationCLAKIANSMVSTWTG
HHHHHHHCHHHHCCC		16.1321712546
711PhosphorylationKIANSMVSTWTGPPA
HHHHCHHHHCCCCHH		15.0221712546
714PhosphorylationNSMVSTWTGPPAMKS
HCHHHHCCCCHHHHH		39.6421712546
730UbiquitinationFTRMFCCKSCPNIVK
HHHHHCCCCCCCCHH		57.16-
747PhosphorylationNFMSFQSYFLQKTMP
CCCCHHHHHHHHHHH		9.4922210691
752PhosphorylationQSYFLQKTMPVAMAL
HHHHHHHHHHHHHHH		17.4722210691
788UbiquitinationYNDNRKNKFSDNYYR
CCCCCCCCCCCCHHH		49.64-
790PhosphorylationDNRKNKFSDNYYRAE
CCCCCCCCCCHHHHH		26.9320363803
793PhosphorylationKNKFSDNYYRAEMID
CCCCCCCHHHHHHHH		10.1822167270
794PhosphorylationNKFSDNYYRAEMIDA
CCCCCCHHHHHHHHH		15.0324702127
805PhosphorylationMIDALANSVTPAVSV
HHHHHHHCCCCCCCC		23.04-
834PhosphorylationRLILEEITRFLNMEK
HHHHHHHHHHHCHHH		20.7428857561
841UbiquitinationTRFLNMEKLLPSYRH
HHHHCHHHHCCCCCC		44.55-
845PhosphorylationNMEKLLPSYRHTITV
CHHHHCCCCCCCHHH		34.4724719451
899UbiquitinationEAVVDYTKVDRSYEE
HHHCCHHCCCCCHHH		35.5921906983
931PhosphorylationHKILNMLTKNPPFTK
HHHHHHHHCCCCCCC		20.2927251275
938UbiquitinationTKNPPFTKNMESPLC
HCCCCCCCCCCCCCC		55.46-
975PhosphorylationRCGAVDLYFTLFGLS
HHCCCEEEHHHHCCC		7.0525002506
977PhosphorylationGAVDLYFTLFGLSRP
CCCEEEHHHHCCCCC		13.9725002506
982PhosphorylationYFTLFGLSRPSCLPL
EHHHHCCCCCHHCCC		42.3925002506
985PhosphorylationLFGLSRPSCLPLPEL
HHCCCCCHHCCCCHH		27.4625002506
1069PhosphorylationLNMLERPSTPGLSKY
CCCCCCCCCCCCCCC		54.1523312004
1070PhosphorylationNMLERPSTPGLSKYR
CCCCCCCCCCCCCCC		24.8629255136
1075AcetylationPSTPGLSKYRPASSR
CCCCCCCCCCCCCCC		50.7725953088
1083PhosphorylationYRPASSRSALIPQHS
CCCCCCCCCCCCCCC		29.4020873877
1090PhosphorylationSALIPQHSAGCDSTP
CCCCCCCCCCCCCCC		22.5520873877
1095PhosphorylationQHSAGCDSTPTTKPQ
CCCCCCCCCCCCCCC		40.1220873877
1096PhosphorylationHSAGCDSTPTTKPQW
CCCCCCCCCCCCCCH		16.0525159151
1098PhosphorylationAGCDSTPTTKPQWSL
CCCCCCCCCCCCHHH		47.7629978859
1099PhosphorylationGCDSTPTTKPQWSLE
CCCCCCCCCCCHHHH		41.7629978859
1100AcetylationCDSTPTTKPQWSLEL
CCCCCCCCCCHHHHH		37.3823749302
1104PhosphorylationPTTKPQWSLELARKG
CCCCCCHHHHHHHCC		13.5029978859
1122PhosphorylationEQAPLEMSMHPAASA
CCCCCCCCCCCCCCC		12.4529507054
1128PhosphorylationMSMHPAASAPLSVFT
CCCCCCCCCCEEEEE		32.3129507054
1135PhosphorylationSAPLSVFTKESTASK
CCCEEEEECCCCCCC		31.5729507054
1139PhosphorylationSVFTKESTASKHSDH
EEEECCCCCCCCCCC		35.7230576142
1144PhosphorylationESTASKHSDHHHHHH
CCCCCCCCCCCCCCC		42.2330576142
1182PhosphorylationEKDKEPFTFSSPASG
CCCCCCCCCCCCCCC		33.0729255136
1184PhosphorylationDKEPFTFSSPASGRS
CCCCCCCCCCCCCCC		32.1423401153
1185PhosphorylationKEPFTFSSPASGRSI
CCCCCCCCCCCCCCC		21.9429255136
1188PhosphorylationFTFSSPASGRSIRSP
CCCCCCCCCCCCCCC		37.8230266825
1191PhosphorylationSSPASGRSIRSPSLS
CCCCCCCCCCCCCCC		26.3623403867
1194PhosphorylationASGRSIRSPSLSD--
CCCCCCCCCCCCC--		19.7125159151
1196PhosphorylationGRSIRSPSLSD----
CCCCCCCCCCC----		41.5725159151
1198PhosphorylationSIRSPSLSD------
CCCCCCCCC------		45.6825159151
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 TAF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAF2_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 TAF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAF6_HUMANTAF6physical
22939629
TAF9_HUMANTAF9physical
22939629
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615599Mental retardation, autosomal recessive 40 (MRT40)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TAF2_HUMAN

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Related Literatures of Post-Translational Modification
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 SER-1194; SER-1196 ANDSER-1198, 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-1196, 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-1194; SER-1196 ANDSER-1198, AND MASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1194; SER-1196 ANDSER-1198, AND MASS SPECTROMETRY.

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