TF3C3_HUMAN - dbPTM
TF3C3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TF3C3_HUMAN
UniProt AC Q9Y5Q9
Protein Name General transcription factor 3C polypeptide 3
Gene Name GTF3C3
Organism Homo sapiens (Human).
Sequence Length 886
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 MSGFSPELIDYLEGKISFEEFERRREERKTREKKSLQEKGKLSAEENPDDSEVPSSSGINSTKSQDKDVNEGETSDGVRKSVHKVFASMLGENEDDEEEEEEEEEEEEEEETPEQPTAGDVFVLEMVLNRETKKMMKEKRPRSKLPRALRGLMGEANIRFARGEREEAILMCMEIIRQAPLAYEPFSTLAMIYEDQGDMEKSLQFELIAAHLNPSDTEEWVRLAEMSLEQDNIKQAIFCYTKALKYEPTNVRYLWERSSLYEQMGDHKMAMDGYRRILNLLSPSDGERFMQLARDMAKSYYEANDVTSAINIIDEAFSKHQGLVSMEDVNIAAELYISNKQYDKALEIITDFSGIVLEKKTSEEGTSEENKAPENVTCTIPDGVPIDITVKLMVCLVHLNILEPLNPLLTTLVEQNPEDMGDLYLDVAEAFLDVGEYNSALPLLSALVCSERYNLAVVWLRHAECLKALGYMERAAESYGKVVDLAPLHLDARISLSTLQQQLGQPEKALEALEPMYDPDTLAQDANAAQQELKLLLHRSTLLFSQGKMYGYVDTLLTMLAMLLKVAMNRAQVCLISSSKSGERHLYLIKVSRDKISDSNDQESANCDAKAIFAVLTSVLTKDDWWNLLLKAIYSLCDLSRFQEAELLVDSSLEYYSFYDDRQKRKELEYFGLSAAILDKNFRKAYNYIRIMVMENVNKPQLWNIFNQVTMHSQDVRHHRFCLRLMLKNPENHALCVLNGHNAFVSGSFKHALGQYVQAFRTHPDEPLYSFCIGLTFIHMASQKYVLRRHALIVQGFSFLNRYLSLRGPCQESFYNLGRGLHQLGLIHLAIHYYQKALELPPLVVEGIELDQLDLRRDIAYNLSLIYQSSGNTGMAQTLLYTYCSI
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------MSGFSPELI
------CCCCCHHHH		48.8522223895
2Phosphorylation------MSGFSPELI
------CCCCCHHHH		48.8522199227
5Phosphorylation---MSGFSPELIDYL
---CCCCCHHHHHHH		22.4625849741
17PhosphorylationDYLEGKISFEEFERR
HHHCCCCCHHHHHHH		30.0521815630
39UbiquitinationEKKSLQEKGKLSAEE
HHHHHHHHCCCCCCC		48.6722817900
41UbiquitinationKSLQEKGKLSAEENP
HHHHHHCCCCCCCCC		50.7921906983
41 (in isoform 1)Ubiquitination-50.7921906983
41 (in isoform 2)Ubiquitination-50.7921906983
41AcetylationKSLQEKGKLSAEENP
HHHHHHCCCCCCCCC		50.7923236377
43PhosphorylationLQEKGKLSAEENPDD
HHHHCCCCCCCCCCC		36.8029255136
51PhosphorylationAEENPDDSEVPSSSG
CCCCCCCCCCCCCCC		48.1230266825
55PhosphorylationPDDSEVPSSSGINST
CCCCCCCCCCCCCCC		42.1623927012
56PhosphorylationDDSEVPSSSGINSTK
CCCCCCCCCCCCCCC		26.8923927012
57PhosphorylationDSEVPSSSGINSTKS
CCCCCCCCCCCCCCC		48.2925159151
61PhosphorylationPSSSGINSTKSQDKD
CCCCCCCCCCCCCCC		34.9823927012
62PhosphorylationSSSGINSTKSQDKDV
CCCCCCCCCCCCCCC		30.1723927012
63 (in isoform 2)Ubiquitination-46.0421906983
63 (in isoform 1)Ubiquitination-46.0421906983
63UbiquitinationSSGINSTKSQDKDVN
CCCCCCCCCCCCCCC		46.0421906983
64PhosphorylationSGINSTKSQDKDVNE
CCCCCCCCCCCCCCC		43.6423663014
67UbiquitinationNSTKSQDKDVNEGET
CCCCCCCCCCCCCCC		56.8122817900
67AcetylationNSTKSQDKDVNEGET
CCCCCCCCCCCCCCC		56.8126051181
74PhosphorylationKDVNEGETSDGVRKS
CCCCCCCCCHHHHHH		42.8723663014
75PhosphorylationDVNEGETSDGVRKSV
CCCCCCCCHHHHHHH		28.2323663014
80UbiquitinationETSDGVRKSVHKVFA
CCCHHHHHHHHHHHH		55.1929967540
81PhosphorylationTSDGVRKSVHKVFAS
CCHHHHHHHHHHHHH		20.9129214152
89UbiquitinationVHKVFASMLGENEDD
HHHHHHHHHCCCCCC		5.1022817900
116UbiquitinationEEETPEQPTAGDVFV
HHCCCCCCCCHHHHH		23.6622817900
137UbiquitinationRETKKMMKEKRPRSK
HHHHHHHHHHCCHHH		57.49-
142UbiquitinationMMKEKRPRSKLPRAL
HHHHHCCHHHHCHHH		50.9223503661
150MethylationSKLPRALRGLMGEAN
HHHCHHHHHHHHHHH		34.90-
187PhosphorylationPLAYEPFSTLAMIYE
CCCCCCCCCEEEHHC		32.97-
188PhosphorylationLAYEPFSTLAMIYED
CCCCCCCCEEEHHCC		20.93-
188UbiquitinationLAYEPFSTLAMIYED
CCCCCCCCEEEHHCC		20.9321963094
198UbiquitinationMIYEDQGDMEKSLQF
EHHCCCCCHHHHHHH		36.1122817900
203UbiquitinationQGDMEKSLQFELIAA
CCCHHHHHHHEEHHH		11.3622817900
226SulfoxidationEWVRLAEMSLEQDNI
HHHHHHHHHCCCCCH		4.6321406390
234SumoylationSLEQDNIKQAIFCYT
HCCCCCHHHHHHHHH		39.67-
234UbiquitinationSLEQDNIKQAIFCYT
HCCCCCHHHHHHHHH		39.67-
242UbiquitinationQAIFCYTKALKYEPT
HHHHHHHHHHCCCCC		25.83-
242AcetylationQAIFCYTKALKYEPT
HHHHHHHHHHCCCCC		25.8325953088
245AcetylationFCYTKALKYEPTNVR
HHHHHHHCCCCCCHH		53.0525953088
245UbiquitinationFCYTKALKYEPTNVR
HHHHHHHCCCCCCHH		53.0527667366
246PhosphorylationCYTKALKYEPTNVRY
HHHHHHCCCCCCHHH		28.1722461510
253PhosphorylationYEPTNVRYLWERSSL
CCCCCHHHHHHHHHH		16.3430576142
259PhosphorylationRYLWERSSLYEQMGD
HHHHHHHHHHHHHCC		40.9930576142
261PhosphorylationLWERSSLYEQMGDHK
HHHHHHHHHHHCCHH		13.1827642862
268UbiquitinationYEQMGDHKMAMDGYR
HHHHCCHHHHHHHHH		32.8521906983
268 (in isoform 2)Ubiquitination-32.8521906983
268 (in isoform 1)Ubiquitination-32.8521906983
275MethylationKMAMDGYRRILNLLS
HHHHHHHHHHHHHCC		25.37-
282PhosphorylationRRILNLLSPSDGERF
HHHHHHCCCCCHHHH		26.0630266825
284PhosphorylationILNLLSPSDGERFMQ
HHHHCCCCCHHHHHH		55.6730266825
298UbiquitinationQLARDMAKSYYEAND
HHHHHHHHHHHHHHC		32.1423503661
307UbiquitinationYYEANDVTSAINIID
HHHHHCHHHHHHHHH		18.4623503661
344UbiquitinationISNKQYDKALEIITD
ECCHHHHHHHHHHHC		50.35-
359 (in isoform 1)Ubiquitination-58.1321906983
359 (in isoform 2)Ubiquitination-58.1321906983
359UbiquitinationFSGIVLEKKTSEEGT
CCCEEEEEECCCCCC		58.1321906983
360UbiquitinationSGIVLEKKTSEEGTS
CCEEEEEECCCCCCC		48.1622817900
362PhosphorylationIVLEKKTSEEGTSEE
EEEEEECCCCCCCCC		42.4025849741
366PhosphorylationKKTSEEGTSEENKAP
EECCCCCCCCCCCCC		35.92-
377PhosphorylationNKAPENVTCTIPDGV
CCCCCCCEEECCCCC		18.6028509920
453PhosphorylationALVCSERYNLAVVWL
HHHHHCCCCCHHHHH		15.5221406692
467UbiquitinationLRHAECLKALGYMER
HHHHHHHHHHCCHHH		53.90-
471PhosphorylationECLKALGYMERAAES
HHHHHHCCHHHHHHH		9.1728102081
481 (in isoform 1)Ubiquitination-30.7421906983
481UbiquitinationRAAESYGKVVDLAPL
HHHHHHCCEEEEHHH		30.7421906983
495PhosphorylationLHLDARISLSTLQQQ
HCCCCCCHHHHHHHH		15.6625159151
497PhosphorylationLDARISLSTLQQQLG
CCCCCHHHHHHHHHC		21.9322617229
498PhosphorylationDARISLSTLQQQLGQ
CCCCHHHHHHHHHCC		33.6022617229
508UbiquitinationQQLGQPEKALEALEP
HHHCCHHHHHHHHCC		66.0221906983
508 (in isoform 1)Ubiquitination-66.0221906983
534UbiquitinationNAAQQELKLLLHRST
HHHHHHHHHHHHHHH		36.0123503661
558PhosphorylationGYVDTLLTMLAMLLK
HHHHHHHHHHHHHHH		17.1622210691
580UbiquitinationVCLISSSKSGERHLY
EEEEECCCCCCCEEE		65.5127667366
590UbiquitinationERHLYLIKVSRDKIS
CCEEEEEEEEHHHCC		31.4022817900
592PhosphorylationHLYLIKVSRDKISDS
EEEEEEEEHHHCCCC		29.74-
595 (in isoform 1)Ubiquitination-42.8921906983
595UbiquitinationLIKVSRDKISDSNDQ
EEEEEHHHCCCCCCH		42.8927667366
686PhosphorylationDKNFRKAYNYIRIMV
CCCHHHHHHHHHEEE		16.13-
699SumoylationMVMENVNKPQLWNIF
EEEECCCCHHHHHHH		29.83-
699UbiquitinationMVMENVNKPQLWNIF
EEEECCCCHHHHHHH		29.8323503661
728UbiquitinationFCLRLMLKNPENHAL
HHHHHHHHCCCCCEE		57.39-
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 TF3C3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TF3C3_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 TF3C3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF3C2_HUMANGTF3C2physical
10373544
TF3B_HUMANBRF1physical
10373544
TF3C5_HUMANGTF3C5physical
22939629
TF3C4_HUMANGTF3C4physical
22939629
TF3C6_HUMANGTF3C6physical
22939629
BRD7_HUMANBRD7physical
26344197
TF3C5_HUMANGTF3C5physical
26344197
RPB1_HUMANPOLR2Aphysical
26344197
SMCA4_HUMANSMARCA4physical
26344197
SMRC2_HUMANSMARCC2physical
26344197
RPC4_HUMANPOLR3Dphysical
28514442
RPC5_HUMANPOLR3Ephysical
28514442
TF3C2_HUMANGTF3C2physical
28514442
TF3C1_HUMANGTF3C1physical
28514442
ZN629_HUMANZNF629physical
28514442
TF3C5_HUMANGTF3C5physical
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 TF3C3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-43, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASSSPECTROMETRY.
"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 SER-43, AND MASSSPECTROMETRY.

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