TF3B_HUMAN - dbPTM
TF3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TF3B_HUMAN
UniProt AC Q92994
Protein Name Transcription factor IIIB 90 kDa subunit
Gene Name BRF1
Organism Homo sapiens (Human).
Sequence Length 677
Subcellular Localization Nucleus.
Protein Description General activator of RNA polymerase which utilizes different TFIIIB complexes at structurally distinct promoters. The isoform 1 is involved in the transcription of tRNA, adenovirus VA1, 7SL and 5S RNA. Isoform 2 is required for transcription of the U6 promoter..
Protein Sequence MTGRVCRGCGGTDIELDAARGDAVCTACGSVLEDNIIVSEVQFVESSGGGSSAVGQFVSLDGAGKTPTLGGGFHVNLGKESRAQTLQNGRRHIHHLGNQLQLNQHCLDTAFNFFKMAVSRHLTRGRKMAHVIAACLYLVCRTEGTPHMLLDLSDLLQVNVYVLGKTFLLLARELCINAPAIDPCLYIPRFAHLLEFGEKNHEVSMTALRLLQRMKRDWMHTGRRPSGLCGAALLVAARMHDFRRTVKEVISVVKVCESTLRKRLTEFEDTPTSQLTIDEFMKIDLEEECDPPSYTAGQRKLRMKQLEQVLSKKLEEVEGEISSYQDAIEIELENSRPKAKGGLASLAKDGSTEDTASSLCGEEDTEDEELEAAASHLNKDLYRELLGGAPGSSEAAGSPEWGGRPPALGSLLDPLPTAASLGISDSIRECISSQSSDPKDASGDGELDLSGIDDLEIDRYILNESEARVKAELWMRENAEYLREQREKEARIAKEKELGIYKEHKPKKSCKRREPIQASTAREAIEKMLEQKKISSKINYSVLRGLSSAGGGSPHREDAQPEHSASARKLSRRRTPASRSGADPVTSVGKRLRPLVSTQPAKKVATGEALLPSSPTLGAEPARPQAVLVESGPVSYHADEEADEEEPDEEDGEPCVSALQMMGSNDYGCDGDEDDGY
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
66PhosphorylationSLDGAGKTPTLGGGF
EECCCCCCCCCCCCE		22.1625159151
68PhosphorylationDGAGKTPTLGGGFHV
CCCCCCCCCCCCEEE		43.1828555341
79UbiquitinationGFHVNLGKESRAQTL
CEEEECCCHHHHHHH		56.54-
79AcetylationGFHVNLGKESRAQTL
CEEEECCCHHHHHHH		56.5425953088
199UbiquitinationHLLEFGEKNHEVSMT
HHHHHHHHCHHHHHH		65.07-
226PhosphorylationMHTGRRPSGLCGAAL
HHCCCCCCCHHHHHH		42.4524719451
247UbiquitinationHDFRRTVKEVISVVK
HHHHHHHHHHHHHHH		45.72-
254UbiquitinationKEVISVVKVCESTLR
HHHHHHHHHHHHHHH		38.73-
270PhosphorylationRLTEFEDTPTSQLTI
HHHCCCCCCCCCCCH		22.6722281053
293PhosphorylationEEECDPPSYTAGQRK
CCCCCCCCCCHHHHH		40.2726552605
294PhosphorylationEECDPPSYTAGQRKL
CCCCCCCCCHHHHHH		13.3426552605
295PhosphorylationECDPPSYTAGQRKLR
CCCCCCCCHHHHHHH		28.7526552605
304UbiquitinationGQRKLRMKQLEQVLS
HHHHHHHHHHHHHHH		45.34-
311PhosphorylationKQLEQVLSKKLEEVE
HHHHHHHHHHHHHHH		28.9624972180
312UbiquitinationQLEQVLSKKLEEVEG
HHHHHHHHHHHHHHH		58.16-
313UbiquitinationLEQVLSKKLEEVEGE
HHHHHHHHHHHHHHC		58.73-
324PhosphorylationVEGEISSYQDAIEIE
HHHCHHCHHHHHHHE		12.0122817900
333 (in isoform 3)Ubiquitination-40.1321890473
333UbiquitinationDAIEIELENSRPKAK
HHHHHEEECCCCCCC		40.1321890473
340UbiquitinationENSRPKAKGGLASLA
ECCCCCCCCCHHHHC		60.69-
345PhosphorylationKAKGGLASLAKDGST
CCCCCHHHHCCCCCC		33.6229457462
351PhosphorylationASLAKDGSTEDTASS
HHHCCCCCCHHHHHH		38.4630278072
352PhosphorylationSLAKDGSTEDTASSL
HHCCCCCCHHHHHHH		43.3321712546
355PhosphorylationKDGSTEDTASSLCGE
CCCCCHHHHHHHCCC		23.3930278072
357PhosphorylationGSTEDTASSLCGEED
CCCHHHHHHHCCCCC		26.4030278072
357 (in isoform 8)Phosphorylation-26.4027174698
358PhosphorylationSTEDTASSLCGEEDT
CCHHHHHHHCCCCCC		25.8030278072
365PhosphorylationSLCGEEDTEDEELEA
HHCCCCCCCHHHHHH		48.9223401153
367 (in isoform 8)Phosphorylation-57.6827174698
372 (in isoform 8)Phosphorylation-22.4327174698
375PhosphorylationEELEAAASHLNKDLY
HHHHHHHHHHCHHHH		24.6323403867
382PhosphorylationSHLNKDLYRELLGGA
HHHCHHHHHHHHCCC		16.5128122231
392PhosphorylationLLGGAPGSSEAAGSP
HHCCCCCCHHCCCCC		24.7727080861
393PhosphorylationLGGAPGSSEAAGSPE
HCCCCCCHHCCCCCC		36.8527080861
398PhosphorylationGSSEAAGSPEWGGRP
CCHHCCCCCCCCCCC		18.2125159151
410PhosphorylationGRPPALGSLLDPLPT
CCCCCCHHHCCCCCC		26.9827080861
417PhosphorylationSLLDPLPTAASLGIS
HHCCCCCCHHHCCCC		42.4027080861
432PhosphorylationDSIRECISSQSSDPK
HHHHHHHHCCCCCCC		33.7029449344
433PhosphorylationSIRECISSQSSDPKD
HHHHHHHCCCCCCCC		17.7317525332
435PhosphorylationRECISSQSSDPKDAS
HHHHHCCCCCCCCCC		38.3625159151
436PhosphorylationECISSQSSDPKDASG
HHHHCCCCCCCCCCC		50.7421815630
442PhosphorylationSSDPKDASGDGELDL
CCCCCCCCCCCCCCC		47.7727732954
450PhosphorylationGDGELDLSGIDDLEI
CCCCCCCCCCCHHHC		33.1130278072
465PhosphorylationDRYILNESEARVKAE
CEEECCHHHHHHHHH		35.1721815630
494UbiquitinationEKEARIAKEKELGIY
HHHHHHHHHHHHCCC		67.93-
496UbiquitinationEARIAKEKELGIYKE
HHHHHHHHHHCCCCC		58.49-
502AcetylationEKELGIYKEHKPKKS
HHHHCCCCCCCCCCC		51.9625953088
509PhosphorylationKEHKPKKSCKRREPI
CCCCCCCCCCCCCCC		30.88-
510 (in isoform 5)Ubiquitination-5.6621890473
510UbiquitinationEHKPKKSCKRREPIQ
CCCCCCCCCCCCCCC		5.6621890473
510UbiquitinationEHKPKKSCKRREPIQ
CCCCCCCCCCCCCCC		5.6621890473
537 (in isoform 1)Ubiquitination-28.3421890473
537UbiquitinationEQKKISSKINYSVLR
HHCCHHHHHCHHHHH		28.3421890473
541PhosphorylationISSKINYSVLRGLSS
HHHHHCHHHHHHHHC		15.3628555341
547PhosphorylationYSVLRGLSSAGGGSP
HHHHHHHHCCCCCCC		22.4423927012
548PhosphorylationSVLRGLSSAGGGSPH
HHHHHHHCCCCCCCC		35.6630266825
553PhosphorylationLSSAGGGSPHREDAQ
HHCCCCCCCCCCCCC		22.3229255136
564PhosphorylationEDAQPEHSASARKLS
CCCCCCCCHHHHHHH		23.4323401153
566PhosphorylationAQPEHSASARKLSRR
CCCCCCHHHHHHHCC		31.4625159151
586PhosphorylationRSGADPVTSVGKRLR
HCCCCCCCCHHHHHH		24.0829396449
587PhosphorylationSGADPVTSVGKRLRP
CCCCCCCCHHHHHHC		29.1629396449
590AcetylationDPVTSVGKRLRPLVS
CCCCCHHHHHHCCCC		46.2123749302
602AcetylationLVSTQPAKKVATGEA
CCCCCCCCCCCCCCC		55.2325953088
606PhosphorylationQPAKKVATGEALLPS
CCCCCCCCCCCCCCC		38.2423312004
613PhosphorylationTGEALLPSSPTLGAE
CCCCCCCCCCCCCCC		49.2526074081
614PhosphorylationGEALLPSSPTLGAEP
CCCCCCCCCCCCCCC		21.6929255136
616PhosphorylationALLPSSPTLGAEPAR
CCCCCCCCCCCCCCC		39.5129255136
631PhosphorylationPQAVLVESGPVSYHA
CCEEEEECCCCCEEC		40.7026074081
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
270TPhosphorylationKinasePLK1P53350
PSP
450SPhosphorylationKinasePLK1P53350
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TF3B_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 TF3B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF3C5_HUMANGTF3C5physical
10373544
PHS2_HUMANPCBD2physical
20211142
TBP_HUMANTBPphysical
11809839
A4_HUMANAPPphysical
21832049
TBP_HUMANTBPphysical
18391023
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616202Cerebellofaciodental syndrome (CFDS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TF3B_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 THR-365 AND SER-450, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, 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-553, AND MASSSPECTROMETRY.
"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-365, AND MASSSPECTROMETRY.

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