TAF1B_HUMAN - dbPTM
TAF1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAF1B_HUMAN
UniProt AC Q53T94
Protein Name TATA box-binding protein-associated factor RNA polymerase I subunit B
Gene Name TAF1B
Organism Homo sapiens (Human).
Sequence Length 588
Subcellular Localization Nucleus, nucleolus.
Protein Description Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment as a component of the SL1/TIF-IB complex and, possibly, directly through its interaction with RRN3..
Protein Sequence MDLEEAEEFKERCTQCAAVSWGLTDEGKYYCTSCHNVTERYQEVTNTDLIPNTQIKALNRGLKKKNNTEKGWDWYVCEGFQYILYQQAEALKNLGVGPELKNDVLHNFWKRYLQKSKQAYCKNPVYTTGRKPTVLEDNLSHSDWASEPELLSDVSCPPFLESGAESQSDIHTRKPFPVSKASQSETSVCSGSLDGVEYSQRKEKGIVKMTMPQTLAFCYLSLLWQREAITLSDLLRFVEEDHIPYINAFQHFPEQMKLYGRDRGIFGIESWPDYEDIYKKTVEVGTFLDLPRFPDITEDCYLHPNILCMKYLMEVNLPDEMHSLTCHVVKMTGMGEVDFLTFDPIAKMAKTVKYDVQAVAIIVVVLKLLFLLDDSFEWSLSNLAEKHNEKNKKDKPWFDFRKWYQIMKKAFDEKKQKWEEARAKYLWKSEKPLYYSFVDKPVAYKKREMVVNLQKQFSTLVESTATAGKKSPSSFQFNWTEEDTDRTCFHGHSLQGVLKEKGQSLLTKNSLYWLSTQKFCRCYCTHVTTYEESNYSLSYQFILNLFSFLLRIKTSLLHEEVSLVEKKLFEKKYSVKRKKSRSKKVRRH
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
1Acetylation-------MDLEEAEE
-------CCHHHHHH		13.8122814378
45PhosphorylationTERYQEVTNTDLIPN
HHHHHHHCCCCCCCH		31.4820860994
53PhosphorylationNTDLIPNTQIKALNR
CCCCCCHHHHHHHHH		26.7328555341
56UbiquitinationLIPNTQIKALNRGLK
CCCHHHHHHHHHCHH		36.6822817900
56 (in isoform 2)Ubiquitination-36.6821890473
56 (in isoform 1)Ubiquitination-36.6821890473
56UbiquitinationLIPNTQIKALNRGLK
CCCHHHHHHHHHCHH		36.6821890473
112PhosphorylationLHNFWKRYLQKSKQA
HHHHHHHHHHHHHHH		15.1230242111
122UbiquitinationKSKQAYCKNPVYTTG
HHHHHHCCCCCCCCC		52.1627667366
140UbiquitinationTVLEDNLSHSDWASE
CCCCCCCCCCCCCCC		27.4829967540
173UbiquitinationSQSDIHTRKPFPVSK
CCCCCCCCCCCCCCC		30.4122817900
174UbiquitinationQSDIHTRKPFPVSKA
CCCCCCCCCCCCCCC		52.7633845483
176UbiquitinationDIHTRKPFPVSKASQ
CCCCCCCCCCCCCCC		11.9321890473
180UbiquitinationRKPFPVSKASQSETS
CCCCCCCCCCCCCCC		52.9029967540
185UbiquitinationVSKASQSETSVCSGS
CCCCCCCCCCCCCCC		37.1523000965
190UbiquitinationQSETSVCSGSLDGVE
CCCCCCCCCCCCCCC		29.3023000965
191UbiquitinationSETSVCSGSLDGVEY
CCCCCCCCCCCCCCH		27.4023000965
220UbiquitinationQTLAFCYLSLLWQRE
HHHHHHHHHHHHHHH		2.8222817900
223UbiquitinationAFCYLSLLWQREAIT
HHHHHHHHHHHHCCC		3.0821890473
232UbiquitinationQREAITLSDLLRFVE
HHHCCCHHHHHHHHH		19.9823000965
237UbiquitinationTLSDLLRFVEEDHIP
CHHHHHHHHHHCCCC		9.0523000965
238UbiquitinationLSDLLRFVEEDHIPY
HHHHHHHHHHCCCCC		6.7823000965
246UbiquitinationEEDHIPYINAFQHFP
HHCCCCCCCCHHHCH		2.2229967540
253UbiquitinationINAFQHFPEQMKLYG
CCCHHHCHHHHHHHC		28.8721890473
300UbiquitinationFPDITEDCYLHPNIL
CCCCCCCCCCCCCCH		2.9521890473
395UbiquitinationNEKNKKDKPWFDFRK
HHHCCCCCCCHHHHH		53.6929967540
404PhosphorylationWFDFRKWYQIMKKAF
CHHHHHHHHHHHHHH		7.3824260401
425PhosphorylationWEEARAKYLWKSEKP
HHHHHHHHHHHCCCC		19.46-
428UbiquitinationARAKYLWKSEKPLYY
HHHHHHHHCCCCCEE		46.2522817900
431UbiquitinationKYLWKSEKPLYYSFV
HHHHHCCCCCEEEEC		47.6221890473
431 (in isoform 2)Ubiquitination-47.6221890473
431UbiquitinationKYLWKSEKPLYYSFV
HHHHHCCCCCEEEEC		47.6222817900
431 (in isoform 1)Ubiquitination-47.6221890473
434PhosphorylationWKSEKPLYYSFVDKP
HHCCCCCEEEECCCC		12.9425159151
435PhosphorylationKSEKPLYYSFVDKPV
HCCCCCEEEECCCCC		11.8725159151
440AcetylationLYYSFVDKPVAYKKR
CEEEECCCCCHHCCH		35.7719608861
440UbiquitinationLYYSFVDKPVAYKKR
CEEEECCCCCHHCCH		35.7723000965
445UbiquitinationVDKPVAYKKREMVVN
CCCCCHHCCHHHHHH		35.3023000965
446UbiquitinationDKPVAYKKREMVVNL
CCCCHHCCHHHHHHH		40.7023000965
463PhosphorylationQFSTLVESTATAGKK
HHHHHHHHHCCCCCC		18.8324043423
464PhosphorylationFSTLVESTATAGKKS
HHHHHHHHCCCCCCC		17.9624043423
466PhosphorylationTLVESTATAGKKSPS
HHHHHHCCCCCCCCC		35.7124043423
501UbiquitinationLQGVLKEKGQSLLTK
HHHHHHHHCCCCCCC		61.7429967540
504PhosphorylationVLKEKGQSLLTKNSL
HHHHHCCCCCCCCCE		33.7324719451
508UbiquitinationKGQSLLTKNSLYWLS
HCCCCCCCCCEEEHH		44.5021890473
508 (in isoform 1)Ubiquitination-44.5021890473
508UbiquitinationKGQSLLTKNSLYWLS
HCCCCCCCCCEEEHH		44.5022817900
508 (in isoform 2)Ubiquitination-44.5021890473
547PhosphorylationQFILNLFSFLLRIKT
HHHHHHHHHHHHHHH		20.3924719451
562PhosphorylationSLLHEEVSLVEKKLF
HHHHHHHHHHHHHHH		29.9428258704
574PhosphorylationKLFEKKYSVKRKKSR
HHHHCHHCCCCCHHH		30.0028258704
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 TAF1B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAF1B_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 TAF1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBP_HUMANTBPphysical
7801123
TAF1C_HUMANTAF1Cphysical
7801123
UBF1_HUMANUBTFphysical
10913176
H2B2E_HUMANHIST2H2BEphysical
17179179
H2A2C_HUMANHIST2H2ACphysical
17179179
H32_HUMANHIST2H3Cphysical
17179179
THAP7_HUMANTHAP7physical
16195249
RXRA_HUMANRXRAphysical
12511607
PRGR_HUMANPGRphysical
12511607
THAP7_HUMANTHAP7physical
15561719
TAF1D_HUMANTAF1Dphysical
17318177
A4_HUMANAPPphysical
21832049
KAT2B_HUMANKAT2Bphysical
23667505
TAF1D_HUMANTAF1Dphysical
26186194
TAF1A_HUMANTAF1Aphysical
26186194
TAF1C_HUMANTAF1Cphysical
26186194
TAF1D_HUMANTAF1Dphysical
28514442
TAF1C_HUMANTAF1Cphysical
28514442
TAF1A_HUMANTAF1Aphysical
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 TAF1B_HUMAN

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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-440, AND MASS SPECTROMETRY.

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