TAF1C_HUMAN - dbPTM
TAF1C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAF1C_HUMAN
UniProt AC Q15572
Protein Name TATA box-binding protein-associated factor RNA polymerase I subunit C
Gene Name TAF1C
Organism Homo sapiens (Human).
Sequence Length 869
Subcellular Localization Nucleus.
Protein Description Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. Formation of SL1/TIF-IB excludes the association of TBP with TFIID subunits. Recruits RNA polymerase I to the rRNA gene promoter via interaction with RRN3..
Protein Sequence MDFPSSLRPALFLTGPLGLSDVPDLSFMCSWRDALTLPEAQPQNSENGALHVTKDLLWEPATPGPLPMLPPLIDPWDPGLTARDLLFRGGCRYRKRPRVVLDVTEQISRFLLDHGDVAFAPLGKLMLENFKLEGAGSRTKKKTVVSVKKLLQDLGGHQPWGCPWAYLSNRQRRFSILGGPILGTSVASHLAELLHEELVLRWEQLLLDEACTGGALAWVPGRTPQFGQLVYPAGGAQDRLHFQEVVLTPGDNPQFLGKPGRIQLQGPVRQVVTCTVQGESKALIYTFLPHWLTCYLTPGPFHPSSALLAVRSDYHCAVWKFGKQWQPTLLQAMQVEKGATGISLSPHLPGELAICSRSGAVCLWSPEDGLRQIYRDPETLVFRDSSSWRWADFTAHPRVLTVGDRTGVKMLDTQGPPGCGLLLFRLGAEASCQKGERVLLTQYLGHSSPKCLPPTLHLVCTQFSLYLVDERLPLVPMLKWNHGLPSPLLLARLLPPPRPSCVQPLLLGGQGGQLQLLHLAGEGASVPRLAGPPQSLPSRIDSLPAFPLLEPKIQWRLQERLKAPTIGLAAVVPPLPSAPTPGLVLFQLSAAGDVFYQQLRPQVDSSLRRDAGPPGDTQPDCHAPTASWTSQDTAGCSQWLKALLKVPLAPPVWTAPTFTHRQMLGSTELRREEEEGQRLGVLRKAMARGQLLLQRDLGSLPAAEPPPAPESGLEDKLSERLGEAWAGRGAAWWERQQGRTSEPGRQTRRPKRRTQLSSSFSLSGHVDPSEDTSSPHSPEWPPADALPLPPTTPPSQELTPDACAQGVPSEQRQMLRDYMAKLPPQRDTPGCATTPPHSQASSVRATRSQQHTPVLSSSQPLRKKPRMGF
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
5Phosphorylation---MDFPSSLRPALF
---CCCCCCCCCHHH		41.8322210691
6Phosphorylation--MDFPSSLRPALFL
--CCCCCCCCCHHHH		28.7422210691
14PhosphorylationLRPALFLTGPLGLSD
CCCHHHHCCCCCCCC		29.4422210691
20PhosphorylationLTGPLGLSDVPDLSF
HCCCCCCCCCCCHHH		34.4622210691
64 (in isoform 2)Ubiquitination-31.8321906983
108PhosphorylationLDVTEQISRFLLDHG
EEHHHHHHHHHHHCC		19.37-
124UbiquitinationVAFAPLGKLMLENFK
EEEEEHHHHHHHCCC		38.10-
131 (in isoform 1)Ubiquitination-58.1521906983
131UbiquitinationKLMLENFKLEGAGSR
HHHHHCCCCCCCCCC		58.1521906983
139O-linked_GlycosylationLEGAGSRTKKKTVVS
CCCCCCCCCCCEEEE		49.2430379171
191 (in isoform 2)Ubiquitination-10.4421906983
230 (in isoform 2)Ubiquitination-4.0721906983
258 (in isoform 1)Ubiquitination-46.5821906983
258UbiquitinationDNPQFLGKPGRIQLQ
CCCHHCCCCCEEEEC		46.5821906983
323 (in isoform 1)Ubiquitination-52.0421906983
323UbiquitinationCAVWKFGKQWQPTLL
EEHHHCCCCCCCHHH		52.0421906983
341 (in isoform 2)Ubiquitination-13.6221906983
409UbiquitinationVGDRTGVKMLDTQGP
ECCCCCCEECCCCCC		34.78-
434 (in isoform 1)Ubiquitination-68.0421906983
434UbiquitinationGAEASCQKGERVLLT
CHHHCCCCCCEEEEE		68.0421906983
458 (in isoform 2)Ubiquitination-3.68-
459 (in isoform 2)Ubiquitination-2.0121906983
479UbiquitinationLPLVPMLKWNHGLPS
CCCCCCCCCCCCCCC		39.43-
525PhosphorylationHLAGEGASVPRLAGP
ECCCCCCCCCHHCCC		43.4424719451
542PhosphorylationSLPSRIDSLPAFPLL
CCCCCCCCCCCCCCC		33.60-
552 (in isoform 1)Ubiquitination-37.8521906983
552UbiquitinationAFPLLEPKIQWRLQE
CCCCCCHHHHHHHHH		37.852190698
617PhosphorylationDAGPPGDTQPDCHAP
CCCCCCCCCCCCCCC		48.17-
641UbiquitinationAGCSQWLKALLKVPL
CCHHHHHHHHHCCCC		33.75-
645UbiquitinationQWLKALLKVPLAPPV
HHHHHHHCCCCCCCC		42.53-
654PhosphorylationPLAPPVWTAPTFTHR
CCCCCCCCCCCCCCH		24.00-
667PhosphorylationHRQMLGSTELRREEE
CHHHHCCHHHHCHHH		36.9228842319
716UbiquitinationPESGLEDKLSERLGE
CCCCHHHHHHHHHHH		44.53-
728MethylationLGEAWAGRGAAWWER
HHHHHCCCCHHHHHH		24.6797825357
740PhosphorylationWERQQGRTSEPGRQT
HHHHCCCCCCCCCCC		44.2419664995
763PhosphorylationLSSSFSLSGHVDPSE
CCCCEECCCCCCCCC		26.1718077418
828PhosphorylationKLPPQRDTPGCATTP
HCCCCCCCCCCCCCC		24.6230266825
833PhosphorylationRDTPGCATTPPHSQA
CCCCCCCCCCCCCHH		43.8630266825
834PhosphorylationDTPGCATTPPHSQAS
CCCCCCCCCCCCHHH		19.1223401153
838PhosphorylationCATTPPHSQASSVRA
CCCCCCCCHHHHHHC		32.9630266825
838O-linked_GlycosylationCATTPPHSQASSVRA
CCCCCCCCHHHHHHC		32.9630379171
841PhosphorylationTPPHSQASSVRATRS
CCCCCHHHHHHCCCC		23.0223403867
842PhosphorylationPPHSQASSVRATRSQ
CCCCHHHHHHCCCCC		20.7323403867
846PhosphorylationQASSVRATRSQQHTP
HHHHHHCCCCCCCCC		21.9321712546
848PhosphorylationSSVRATRSQQHTPVL
HHHHCCCCCCCCCCC		29.8217525332
852PhosphorylationATRSQQHTPVLSSSQ
CCCCCCCCCCCCCCC		15.6825159151
856PhosphorylationQQHTPVLSSSQPLRK
CCCCCCCCCCCCCCC		28.3327732954
857PhosphorylationQHTPVLSSSQPLRKK
CCCCCCCCCCCCCCC		28.9125159151
858PhosphorylationHTPVLSSSQPLRKKP
CCCCCCCCCCCCCCC		32.2317525332
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 TAF1C_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAF1C_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
434Ubiquitination429 (5)G ⇒ Rrs4150167
  • Autism
22843504
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBP_HUMANTBPphysical
7801123
UBF1_HUMANUBTFphysical
10913176
TAF1D_HUMANTAF1Dphysical
17318177
TBP_HUMANTBPphysical
17268553
TAF12_HUMANTAF12physical
17268553
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 TAF1C_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-848 AND SER-858, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-834, AND MASSSPECTROMETRY.

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