BRF2_HUMAN - dbPTM
BRF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRF2_HUMAN
UniProt AC Q9HAW0
Protein Name Transcription factor IIIB 50 kDa subunit
Gene Name BRF2
Organism Homo sapiens (Human).
Sequence Length 419
Subcellular Localization Nucleus .
Protein Description General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites. [PubMed: 11040218]
Protein Sequence MPGRGRCPDCGSTELVEDSHYSQSQLVCSDCGCVVTEGVLTTTFSDEGNLREVTYSRSTGENEQVSRSQQRGLRRVRDLCRVLQLPPTFEDTAVAYYQQAYRHSGIRAARLQKKEVLVGCCVLITCRQHNWPLTMGAICTLLYADLDVFSSTYMQIVKLLGLDVPSLCLAELVKTYCSSFKLFQASPSVPAKYVEDKEKMLSRTMQLVELANETWLVTGRHPLPVITAATFLAWQSLQPADRLSCSLARFCKLANVDLPYPASSRLQELLAVLLRMAEQLAWLRVLRLDKRSVVKHIGDLLQHRQSLVRSAFRDGTAEVETREKEPPGWGQGQGEGEVGNNSLGLPQGKRPASPALLLPPCMLKSPKRICPVPPVSTVTGDENISDSEIEQYLRTPQEVRDFQRAQAARQAATSVPNPP
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
140PhosphorylationLTMGAICTLLYADLD
CHHHHHHHHHHHCHH		17.43-
150PhosphorylationYADLDVFSSTYMQIV
HHCHHHHCHHHHHHH		22.94-
176PhosphorylationLAELVKTYCSSFKLF
HHHHHHHHHHHCCCC		5.6630631047
178PhosphorylationELVKTYCSSFKLFQA
HHHHHHHHHCCCCCC		28.5330631047
179PhosphorylationLVKTYCSSFKLFQAS
HHHHHHHHCCCCCCC		23.8830631047
186PhosphorylationSFKLFQASPSVPAKY
HCCCCCCCCCCCHHH		13.6125627689
188PhosphorylationKLFQASPSVPAKYVE
CCCCCCCCCCHHHHC		37.9325627689
188O-linked_GlycosylationKLFQASPSVPAKYVE
CCCCCCCCCCHHHHC		37.9330379171
192UbiquitinationASPSVPAKYVEDKEK
CCCCCCHHHHCCHHH		43.7021906983
193PhosphorylationSPSVPAKYVEDKEKM
CCCCCHHHHCCHHHH		15.92-
197UbiquitinationPAKYVEDKEKMLSRT
CHHHHCCHHHHHHHH		45.8122817900
199UbiquitinationKYVEDKEKMLSRTMQ
HHHCCHHHHHHHHHH		51.38-
202PhosphorylationEDKEKMLSRTMQLVE
CCHHHHHHHHHHHHH		23.3924719451
218PhosphorylationANETWLVTGRHPLPV
HHCCEEECCCCCCCH		26.7424719451
260PhosphorylationLANVDLPYPASSRLQ
HCCCCCCCCCHHHHH		20.8022817900
295UbiquitinationLDKRSVVKHIGDLLQ
CCHHHHHHHHHHHHH		27.6129967540
306PhosphorylationDLLQHRQSLVRSAFR
HHHHHHHHHHHHHHH		28.8724719451
324UbiquitinationAEVETREKEPPGWGQ
CEEEEECCCCCCCCC		72.7021906983
353PhosphorylationPQGKRPASPALLLPP
CCCCCCCCCHHHCCC		17.2529255136
361SulfationPALLLPPCMLKSPKR
CHHHCCCCCCCCCCC		4.7526638071
361OxidationPALLLPPCMLKSPKR
CHHHCCCCCCCCCCC		4.7526638071
361Cysteine sulfenic acid (-SOH)PALLLPPCMLKSPKR
CHHHCCCCCCCCCCC		4.75-
365PhosphorylationLPPCMLKSPKRICPV
CCCCCCCCCCCCCCC		31.5228464451
376PhosphorylationICPVPPVSTVTGDEN
CCCCCCCCCCCCCCC		23.9630108239
377PhosphorylationCPVPPVSTVTGDENI
CCCCCCCCCCCCCCC		23.4828464451
379PhosphorylationVPPVSTVTGDENISD
CCCCCCCCCCCCCCH		38.7230108239
385PhosphorylationVTGDENISDSEIEQY
CCCCCCCCHHHHHHH		46.8230278072
387PhosphorylationGDENISDSEIEQYLR
CCCCCCHHHHHHHHC		33.4130278072
392PhosphorylationSDSEIEQYLRTPQEV
CHHHHHHHHCCHHHH		5.8325850435
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 BRF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
361COxidation

26638071
361COxidation

26638071
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 BRF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XPO7_HUMANXPO7physical
17353931
DAAF5_HUMANDNAAF5physical
17353931
IPO4_HUMANIPO4physical
17353931
COPG1_HUMANCOPG1physical
17353931
ATD3A_HUMANATAD3Aphysical
17353931
XPO4_HUMANXPO4physical
17353931
SYMC_HUMANMARSphysical
17353931
AIFM1_HUMANAIFM1physical
17353931
GCN1_HUMANGCN1L1physical
17353931
GEMI4_HUMANGEMIN4physical
17353931
OTUD4_HUMANOTUD4physical
17353931
TNPO3_HUMANTNPO3physical
17353931
FANCI_HUMANFANCIphysical
17353931
NOC2L_HUMANNOC2Lphysical
17353931
TMM33_HUMANTMEM33physical
17353931
DPM1_HUMANDPM1physical
17353931
ABCD3_HUMANABCD3physical
17353931
4F2_HUMANSLC3A2physical
17353931
HACD3_HUMANPTPLAD1physical
17353931
NUP93_HUMANNUP93physical
17353931
XPO6_HUMANXPO6physical
17353931
NSMA3_HUMANSMPD4physical
17353931
MYO1B_HUMANMYO1Bphysical
17353931
RN219_HUMANRNF219physical
17353931
SMAP1_HUMANSMAP1physical
17353931
SF3B1_HUMANSF3B1physical
17353931
TBP_HUMANTBPphysical
11564744
NCAM1_HUMANNCAM1physical
28514442
PLAK_HUMANJUPphysical
28514442
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 BRF2_HUMAN

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Related Literatures of Post-Translational Modification

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