TF3C5_HUMAN - dbPTM
TF3C5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TF3C5_HUMAN
UniProt AC Q9Y5Q8
Protein Name General transcription factor 3C polypeptide 5
Gene Name GTF3C5
Organism Homo sapiens (Human).
Sequence Length 519
Subcellular Localization Nucleus.
Protein Description Involved in RNA polymerase III-mediated transcription. Integral, tightly associated component of the DNA-binding TFIIIC2 subcomplex that directly binds tRNA and virus-associated RNA promoters..
Protein Sequence MAAEAADLGLGAAVPVELRRERRMVCVEYPGVVRDVAKMLPTLGGEEGVSRIYADPTKRLELYFRPKDPYCHPVCANRFSTSSLLLRIRKRTRRQKGVLGTEAHSEVTFDMEILGIISTIYKFQGMSDFQYLAVHTEAGGKHTSMYDKVLMLRPEKEAFFHQELPLYIPPPIFSRLDAPVDYFYRPETQHREGYNNPPISGENLIGLSRARRPHNAIFVNFEDEEVPKQPLEAAAQTWRRVCTNPVDRKVEEELRKLFDIRPIWSRNAVKANISVHPDKLKVLLPFIAYYMITGPWRSLWIRFGYDPRKNPDAKIYQVLDFRIRCGMKHGYAPSDLPVKAKRSTYNYSLPITVKKTSSQLVTMHDLKQGLGPSGTSGARKPASSKYKLKDSVYIFREGALPPYRQMFYQLCDLNVEELQKIIHRNDGAENSCTERDGWCLPKTSDELRDTMSLMIRQTIRSKRPALFSSSAKADGGKEQLTYESGEDEEDEEEEEEEEEDFKPSDGSENEMETEILDYV
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
2Acetylation------MAAEAADLG
------CCHHHHHCC		17.6322814378
38 (in isoform 1)Ubiquitination-40.6021890473
38UbiquitinationGVVRDVAKMLPTLGG
CHHHHHHHHCCCCCC		40.6021890473
38 (in isoform 2)Ubiquitination-40.6021890473
38 (in isoform 3)Ubiquitination-40.6021890473
53PhosphorylationEEGVSRIYADPTKRL
CCCCCEEEECCCCEE		12.1126552605
53 (in isoform 3)Phosphorylation-12.1127642862
57PhosphorylationSRIYADPTKRLELYF
CEEEECCCCEEEEEE		29.3726552605
58 (in isoform 1)Ubiquitination-61.4421890473
58UbiquitinationRIYADPTKRLELYFR
EEEECCCCEEEEEEC		61.4421906983
58 (in isoform 3)Ubiquitination-61.4421890473
67UbiquitinationLELYFRPKDPYCHPV
EEEEECCCCCCCCCC		68.06-
67 (in isoform 3)Ubiquitination-68.06-
70 (in isoform 3)Phosphorylation-17.3327642862
131 (in isoform 3)Phosphorylation-9.1627642862
141UbiquitinationVHTEAGGKHTSMYDK
EEECCCCCCCCCCCE		42.67-
146PhosphorylationGGKHTSMYDKVLMLR
CCCCCCCCCEEEECC		16.63-
148UbiquitinationKHTSMYDKVLMLRPE
CCCCCCCEEEECCCC		21.56-
167 (in isoform 3)Phosphorylation-14.9427642862
167PhosphorylationFHQELPLYIPPPIFS
HCCCCCCCCCCCCHH		14.94-
182 (in isoform 3)Phosphorylation-11.6227642862
182PhosphorylationRLDAPVDYFYRPETQ
CCCCCCCEECCCCCC		11.6229496907
184PhosphorylationDAPVDYFYRPETQHR
CCCCCEECCCCCCCC		21.0122461510
188PhosphorylationDYFYRPETQHREGYN
CEECCCCCCCCCCCC		32.1529496907
194PhosphorylationETQHREGYNNPPISG
CCCCCCCCCCCCCCH		13.6528796482
200PhosphorylationGYNNPPISGENLIGL
CCCCCCCCHHCHHCC		45.9221712546
200 (in isoform 3)Phosphorylation-45.9227251275
208PhosphorylationGENLIGLSRARRPHN
HHCHHCCCCCCCCCC		20.76-
246 (in isoform 2)Ubiquitination-13.9221890473
256UbiquitinationKVEEELRKLFDIRPI
HHHHHHHHHHCCCCC		67.1621890473
256 (in isoform 1)Ubiquitination-67.1621890473
256 (in isoform 3)Ubiquitination-67.1621890473
260 (in isoform 2)Ubiquitination-4.4021890473
270 (in isoform 1)Ubiquitination-33.0521890473
270UbiquitinationIWSRNAVKANISVHP
CCCCCCHHCCEEECH		33.0521906983
270 (in isoform 3)Ubiquitination-33.0521890473
279UbiquitinationNISVHPDKLKVLLPF
CEEECHHHHHHHHHH		55.44-
290PhosphorylationLLPFIAYYMITGPWR
HHHHHHHHHHHCCCH		3.50-
316PhosphorylationKNPDAKIYQVLDFRI
CCCCCCEEEEEEEEH		7.5820393185
316 (in isoform 3)Phosphorylation-7.5827642862
328AcetylationFRIRCGMKHGYAPSD
EEHHCCCCCCCCCCC		21.1125953088
328MethylationFRIRCGMKHGYAPSD
EEHHCCCCCCCCCCC		21.11-
329 (in isoform 2)Ubiquitination-26.1321890473
331 (in isoform 3)Phosphorylation-18.3027642862
331PhosphorylationRCGMKHGYAPSDLPV
HCCCCCCCCCCCCCC		18.3029496907
334PhosphorylationMKHGYAPSDLPVKAK
CCCCCCCCCCCCCCC		43.5429214152
339UbiquitinationAPSDLPVKAKRSTYN
CCCCCCCCCCCCCCC		46.3721906983
339 (in isoform 1)Ubiquitination-46.3721890473
339 (in isoform 3)Ubiquitination-46.3721890473
339SumoylationAPSDLPVKAKRSTYN
CCCCCCCCCCCCCCC		46.37-
339SumoylationAPSDLPVKAKRSTYN
CCCCCCCCCCCCCCC		46.37-
339MethylationAPSDLPVKAKRSTYN
CCCCCCCCCCCCCCC		46.37-
341MethylationSDLPVKAKRSTYNYS
CCCCCCCCCCCCCEE		40.96-
343PhosphorylationLPVKAKRSTYNYSLP
CCCCCCCCCCCEECC		34.2428796482
344 (in isoform 2)Ubiquitination-21.5921890473
344PhosphorylationPVKAKRSTYNYSLPI
CCCCCCCCCCEECCE		21.5930206219
345PhosphorylationVKAKRSTYNYSLPIT
CCCCCCCCCEECCEE		17.2230206219
345 (in isoform 3)Phosphorylation-17.2227642862
347 (in isoform 3)Phosphorylation-10.9427642862
347PhosphorylationAKRSTYNYSLPITVK
CCCCCCCEECCEEEE		10.9430206219
348PhosphorylationKRSTYNYSLPITVKK
CCCCCCEECCEEEEE		24.8328796482
352PhosphorylationYNYSLPITVKKTSSQ
CCEECCEEEEECCCC		25.0823186163
354 (in isoform 3)Ubiquitination-41.5021890473
354 (in isoform 1)Ubiquitination-41.5021890473
354AcetylationYSLPITVKKTSSQLV
EECCEEEEECCCCEE		41.5025953088
354UbiquitinationYSLPITVKKTSSQLV
EECCEEEEECCCCEE		41.5021906983
355 (in isoform 3)Ubiquitination-49.67-
355MethylationSLPITVKKTSSQLVT
ECCEEEEECCCCEEE		49.67-
355UbiquitinationSLPITVKKTSSQLVT
ECCEEEEECCCCEEE		49.67-
356PhosphorylationLPITVKKTSSQLVTM
CCEEEEECCCCEEEH		28.0828555341
357PhosphorylationPITVKKTSSQLVTMH
CEEEEECCCCEEEHH		25.6028555341
357 (in isoform 2)Ubiquitination-25.6021890473
358PhosphorylationITVKKTSSQLVTMHD
EEEEECCCCEEEHHH		32.5328555341
367MethylationLVTMHDLKQGLGPSG
EEEHHHHCCCCCCCC		48.67-
367 (in isoform 1)Ubiquitination-48.6721890473
367 (in isoform 3)Ubiquitination-48.6721890473
367UbiquitinationLVTMHDLKQGLGPSG
EEEHHHHCCCCCCCC		48.6721890473
373PhosphorylationLKQGLGPSGTSGARK
HCCCCCCCCCCCCCC		53.5626074081
375PhosphorylationQGLGPSGTSGARKPA
CCCCCCCCCCCCCCC		28.4625159151
376PhosphorylationGLGPSGTSGARKPAS
CCCCCCCCCCCCCCC		33.7025159151
383PhosphorylationSGARKPASSKYKLKD
CCCCCCCCCCCCCCC		35.5726074081
384PhosphorylationGARKPASSKYKLKDS
CCCCCCCCCCCCCCC		41.9526074081
386PhosphorylationRKPASSKYKLKDSVY
CCCCCCCCCCCCCEE		24.4126074081
391PhosphorylationSKYKLKDSVYIFREG
CCCCCCCCEEEECCC		18.42-
393PhosphorylationYKLKDSVYIFREGAL
CCCCCCEEEECCCCC		9.78-
403PhosphorylationREGALPPYRQMFYQL
CCCCCCHHHHHHHHH		16.13-
452PhosphorylationDELRDTMSLMIRQTI
HHHHHHHHHHHHHHH		19.5122210691
462UbiquitinationIRQTIRSKRPALFSS
HHHHHHHCCCCEECC		53.18-
462AcetylationIRQTIRSKRPALFSS
HHHHHHHCCCCEECC		53.1824431753
468PhosphorylationSKRPALFSSSAKADG
HCCCCEECCCCCCCC		25.0024173317
469PhosphorylationKRPALFSSSAKADGG
CCCCEECCCCCCCCC		27.2923186163
470PhosphorylationRPALFSSSAKADGGK
CCCEECCCCCCCCCC		32.3730576142
472UbiquitinationALFSSSAKADGGKEQ
CEECCCCCCCCCCCC		49.29-
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 TF3C5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TF3C5_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 TF3C5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF3C2_HUMANGTF3C2physical
10373544
TF3C6_HUMANGTF3C6physical
22939629
SRA1_HUMANSRA1physical
20398657
K1C40_HUMANKRT40physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
BRD7_HUMANBRD7physical
26344197
PB1_HUMANPBRM1physical
26344197
PLK1_HUMANPLK1physical
27173435
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 TF3C5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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