TAF6_HUMAN - dbPTM
TAF6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAF6_HUMAN
UniProt AC P49848
Protein Name Transcription initiation factor TFIID subunit 6
Gene Name TAF6
Organism Homo sapiens (Human).
Sequence Length 677
Subcellular Localization Nucleus.
Protein Description TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TIIFD is multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors..
Protein Sequence MAEEKKLKLSNTVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALKLKNVEPLYGFHAQEFIPFRFASGGGRELYFYEEKEVDLSDIINTPLPRVPLDVCLKAHWLSIEGCQPAIPENPPPAPKEQQKAEATEPLKSAKPGQEEDGPLKGKGQGATTADGKGKEKKAPPLLEGAPLRLKPRSIHELSVEQQLYYKEITEACVGSCEAKRAEALQSIATDPGLYQMLPRFSTFISEGVRVNVVQNNLALLIYLMRMVKALMDNPTLYLEKYVHELIPAVMTCIVSRQLCLRPDVDNHWALRDFAARLVAQICKHFSTTTNNIQSRITKTFTKSWVDEKTPWTTRYGSIAGLAELGHDVIKTLILPRLQQEGERIRSVLDGPVLSNIDRIGADHVQSLLLKHCAPVLAKLRPPPDNQDAYRAEFGSLGPLLCSQVVKARAQAALQAQQVNRTTLTITQPRPTLTLSQAPQPGPRTPGLLKVPGSIALPVQTLVSARAAAPPQPSPPPTKFIVMSSSSSAPSTQQVLSLSTSAPGSGSTTTSPVTTTVPSVQPIVKLVSTATTAPPSTAPSGPGSVQKYIVVSLPPTGEGKGGPTSHPSPVPPPASSPSPLSGSALCGGKQEAGDSPPPAPGTPKANGSQPNSGSPQPAP
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
6Acetylation--MAEEKKLKLSNTV
--CCCCCCCCCCCCC		54.8825953088
8AcetylationMAEEKKLKLSNTVLP
CCCCCCCCCCCCCCC		59.7625953088
8 (in isoform 3)Phosphorylation-59.76-
19SulfoxidationTVLPSESMKVVAESM
CCCCHHHHHHHHHHH		3.1621406390
48UbiquitinationDEVSYRIKEIAQDAL
HHHHHHHHHHHHHHH		33.79-
56UbiquitinationEIAQDALKFMHMGKR
HHHHHHHHHHHCCCC		42.22-
65UbiquitinationMHMGKRQKLTTSDID
HHCCCCCCCCHHHHH		52.40-
76UbiquitinationSDIDYALKLKNVEPL
HHHHHHHHCCCCCCC		49.60-
78UbiquitinationIDYALKLKNVEPLYG
HHHHHHCCCCCCCCC		58.31-
85 (in isoform 3)Ubiquitination-18.62-
113 (in isoform 3)Ubiquitination-41.36-
115 (in isoform 3)Ubiquitination-23.46-
120PhosphorylationDLSDIINTPLPRVPL
CHHHHCCCCCCCCCH		18.7830266825
137PhosphorylationCLKAHWLSIEGCQPA
HHHHHEEEECCCCCC		17.2528348404
193AcetylationTTADGKGKEKKAPPL
CCCCCCCCCCCCCCC		70.6011921105
196SumoylationDGKGKEKKAPPLLEG
CCCCCCCCCCCCCCC		68.19-
196SumoylationDGKGKEKKAPPLLEG
CCCCCCCCCCCCCCC		68.1928112733
212PhosphorylationPLRLKPRSIHELSVE
CCCCCCCCHHCCCHH		36.5027174698
217PhosphorylationPRSIHELSVEQQLYY
CCCHHCCCHHHHHHH		22.1827174698
223PhosphorylationLSVEQQLYYKEITEA
CCHHHHHHHHHHHHH		14.2527174698
224PhosphorylationSVEQQLYYKEITEAC
CHHHHHHHHHHHHHH		15.6727174698
238AcetylationCVGSCEAKRAEALQS
HHHCHHHHHHHHHHH		29.8223749302
238UbiquitinationCVGSCEAKRAEALQS
HHHCHHHHHHHHHHH		29.82-
248PhosphorylationEALQSIATDPGLYQM
HHHHHHCCCHHHHHH		40.85-
253PhosphorylationIATDPGLYQMLPRFS
HCCCHHHHHHHHHHH		9.5917360941
264PhosphorylationPRFSTFISEGVRVNV
HHHHHHHCCCCCCEE		24.89-
275 (in isoform 3)Ubiquitination-15.03-
287"N6,N6-dimethyllysine"IYLMRMVKALMDNPT
HHHHHHHHHHHHCCH		26.85-
287MethylationIYLMRMVKALMDNPT
HHHHHHHHHHHHCCH		26.8523644510
287AcetylationIYLMRMVKALMDNPT
HHHHHHHHHHHHCCH		26.8526051181
342AcetylationRLVAQICKHFSTTTN
HHHHHHHHHHHCCCC		49.6826051181
357UbiquitinationNIQSRITKTFTKSWV
CHHHHHHHHHCHHHH		38.99-
361UbiquitinationRITKTFTKSWVDEKT
HHHHHHCHHHHCCCC		37.82-
367UbiquitinationTKSWVDEKTPWTTRY
CHHHHCCCCCCCCCC		56.26-
367AcetylationTKSWVDEKTPWTTRY
CHHHHCCCCCCCCCC		56.2626051181
372PhosphorylationDEKTPWTTRYGSIAG
CCCCCCCCCCCCHHH		20.30-
389UbiquitinationELGHDVIKTLILPRL
HHCHHHHHHHHHHHH		36.81-
398 (in isoform 3)Ubiquitination-66.31-
405PhosphorylationQEGERIRSVLDGPVL
HCCHHHHHHHCCCHH		25.35-
413PhosphorylationVLDGPVLSNIDRIGA
HHCCCHHCCCCCCCH		31.79-
425PhosphorylationIGADHVQSLLLKHCA
CCHHHHHHHHHHHHH		21.64-
429UbiquitinationHVQSLLLKHCAPVLA
HHHHHHHHHHHHHHH		36.29-
437UbiquitinationHCAPVLAKLRPPPDN
HHHHHHHHCCCCCCC		40.65-
465UbiquitinationLLCSQVVKARAQAAL
HHHHHHHHHHHHHHH		33.04-
466 (in isoform 3)Ubiquitination-10.63-
480O-linked_GlycosylationQAQQVNRTTLTITQP
HHHHCCCCEEEEEEC		22.4330059200
481O-linked_GlycosylationAQQVNRTTLTITQPR
HHHCCCCEEEEEECC		20.7530059200
483O-linked_GlycosylationQVNRTTLTITQPRPT
HCCCCEEEEEECCCE		21.6430059200
483PhosphorylationQVNRTTLTITQPRPT
HCCCCEEEEEECCCE		21.64-
485O-linked_GlycosylationNRTTLTITQPRPTLT
CCCEEEEEECCCEEE		27.5630059200
490O-linked_GlycosylationTITQPRPTLTLSQAP
EEEECCCEEEECCCC		33.3830059200
490PhosphorylationTITQPRPTLTLSQAP
EEEECCCEEEECCCC		33.3825002506
492PhosphorylationTQPRPTLTLSQAPQP
EECCCEEEECCCCCC		27.1725002506
492O-linked_GlycosylationTQPRPTLTLSQAPQP
EECCCEEEECCCCCC		27.1730059200
494PhosphorylationPRPTLTLSQAPQPGP
CCCEEEECCCCCCCC		21.0425002506
494O-linked_GlycosylationPRPTLTLSQAPQPGP
CCCEEEECCCCCCCC		21.0430059200
502 (in isoform 3)Ubiquitination-60.51-
502MethylationQAPQPGPRTPGLLKV
CCCCCCCCCCCCEEC		60.51115385781
503PhosphorylationAPQPGPRTPGLLKVP
CCCCCCCCCCCEECC		25.4923312004
524MethylationVQTLVSARAAAPPQP
HHHHHHHHHCCCCCC		19.7724129315
524DimethylationVQTLVSARAAAPPQP
HHHHHHHHHCCCCCC		19.77-
532PhosphorylationAAAPPQPSPPPTKFI
HCCCCCCCCCCCEEE		44.8030266825
536PhosphorylationPQPSPPPTKFIVMSS
CCCCCCCCEEEEEEC		44.3429255136
537MethylationQPSPPPTKFIVMSSS
CCCCCCCEEEEEECC		38.58116264843
586PhosphorylationQPIVKLVSTATTAPP
HHCEEHHHCCCCCCC		23.8229116813
586O-linked_GlycosylationQPIVKLVSTATTAPP
HHCEEHHHCCCCCCC		23.8230059200
589PhosphorylationVKLVSTATTAPPSTA
EEHHHCCCCCCCCCC		24.4729116813
589O-linked_GlycosylationVKLVSTATTAPPSTA
EEHHHCCCCCCCCCC		24.4730059200
590PhosphorylationKLVSTATTAPPSTAP
EHHHCCCCCCCCCCC		34.4029116813
590O-linked_GlycosylationKLVSTATTAPPSTAP
EHHHCCCCCCCCCCC		34.4030059200
594PhosphorylationTATTAPPSTAPSGPG
CCCCCCCCCCCCCCC		35.8229116813
594O-linked_GlycosylationTATTAPPSTAPSGPG
CCCCCCCCCCCCCCC		35.8230059200
595O-linked_GlycosylationATTAPPSTAPSGPGS
CCCCCCCCCCCCCCC		48.6530059200
598PhosphorylationAPPSTAPSGPGSVQK
CCCCCCCCCCCCCCE		55.9725627689
598O-linked_GlycosylationAPPSTAPSGPGSVQK
CCCCCCCCCCCCCCE		55.9730059200
602PhosphorylationTAPSGPGSVQKYIVV
CCCCCCCCCCEEEEE		25.2227050516
602O-linked_GlycosylationTAPSGPGSVQKYIVV
CCCCCCCCCCEEEEE		25.2230059200
606PhosphorylationGPGSVQKYIVVSLPP
CCCCCCEEEEEECCC		5.0519413330
614O-linked_GlycosylationIVVSLPPTGEGKGGP
EEEECCCCCCCCCCC		46.0230059200
614PhosphorylationIVVSLPPTGEGKGGP
EEEECCCCCCCCCCC		46.0220068231
622PhosphorylationGEGKGGPTSHPSPVP
CCCCCCCCCCCCCCC		42.8323401153
623PhosphorylationEGKGGPTSHPSPVPP
CCCCCCCCCCCCCCC		36.2130266825
626PhosphorylationGGPTSHPSPVPPPAS
CCCCCCCCCCCCCCC		32.8623401153
633PhosphorylationSPVPPPASSPSPLSG
CCCCCCCCCCCCCCC		48.8623401153
634PhosphorylationPVPPPASSPSPLSGS
CCCCCCCCCCCCCCC		31.3530266825
636PhosphorylationPPPASSPSPLSGSAL
CCCCCCCCCCCCCCC		40.1823401153
639PhosphorylationASSPSPLSGSALCGG
CCCCCCCCCCCCCCC		33.8030266825
641PhosphorylationSPSPLSGSALCGGKQ
CCCCCCCCCCCCCCC		18.0730278072
647AcetylationGSALCGGKQEAGDSP
CCCCCCCCCCCCCCC		30.1926051181
653PhosphorylationGKQEAGDSPPPAPGT
CCCCCCCCCCCCCCC		38.0929255136
660PhosphorylationSPPPAPGTPKANGSQ
CCCCCCCCCCCCCCC		22.1319664994
666PhosphorylationGTPKANGSQPNSGSP
CCCCCCCCCCCCCCC		42.1223403867
670PhosphorylationANGSQPNSGSPQPAP
CCCCCCCCCCCCCCC		47.5330266825
672PhosphorylationGSQPNSGSPQPAP--
CCCCCCCCCCCCC--		21.8630266825
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 TAF6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAF6_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 TAF6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAF5_HUMANTAF5physical
10523658
TAF1_HUMANTAF1physical
7667268
T2EA_HUMANGTF2E1physical
7667268
P53_HUMANTP53physical
20096117
TAF12_HUMANTAF12physical
9133630
TAF1_HUMANTAF1physical
12453419
CHD3_HUMANCHD3physical
12453419
SIN3A_HUMANSIN3Aphysical
12453419
SMRC2_HUMANSMARCC2physical
12453419
SMRC1_HUMANSMARCC1physical
12453419
SMCA2_HUMANSMARCA2physical
12453419
HDAC1_HUMANHDAC1physical
12453419
HDAC2_HUMANHDAC2physical
12453419
RBBP4_HUMANRBBP4physical
12453419
RBBP7_HUMANRBBP7physical
12453419
SNF5_HUMANSMARCB1physical
12453419
TBP_HUMANTBPphysical
12453419
MBD3_HUMANMBD3physical
12453419
TAF9_HUMANTAF9physical
12453419
SAP30_HUMANSAP30physical
12453419
RAN_HUMANRANphysical
12453419
TAF9_HUMANTAF9physical
7597030
ERCC1_HUMANERCC1physical
22323595
TAF9_HUMANTAF9physical
15601843
A4_HUMANAPPphysical
21832049
TBP_HUMANTBPphysical
22939629
TAF9_HUMANTAF9physical
22939629
TAF7_HUMANTAF7physical
22939629
TAF9B_HUMANTAF9Bphysical
22939629
CDC26_HUMANCDC26physical
26344197
SPT5H_HUMANSUPT5Hphysical
26344197
TAF1_HUMANTAF1physical
26344197
TAF10_HUMANTAF10physical
26344197
TAF3_HUMANTAF3physical
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 TAF6_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-653 AND THR-660, ANDMASS 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-653; THR-660; SER-670AND SER-672, AND MASS 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-626; SER-634; SER-636;SER-653 AND THR-660, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653 AND THR-660, ANDMASS 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-653, AND MASSSPECTROMETRY.

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