TF3C4_HUMAN - dbPTM
TF3C4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TF3C4_HUMAN
UniProt AC Q9UKN8
Protein Name General transcription factor 3C polypeptide 4
Gene Name GTF3C4
Organism Homo sapiens (Human).
Sequence Length 822
Subcellular Localization Nucleus.
Protein Description Essential for RNA polymerase III to make a number of small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin. Has histone acetyltransferase activity (HAT) with unique specificity for free and nucleosomal H3. May cooperate with GTF3C5 in facilitating the recruitment of TFIIIB and RNA polymerase through direct interactions with BRF1, POLR3C and POLR3F. May be localized close to the A box..
Protein Sequence MNTADQARVGPADDGPAPSGEEEGEGGGEAGGKEPAADAAPGPSAAFRLMVTRREPAVKLQYAVSGLEPLAWSEDHRVSVSTARSIAVLELICDVHNPGQDLVIHRTSVPAPLNSCLLKVGSKTEVAECKEKFAASKDPTVSQTFMLDRVFNPEGKALPPMRGFKYTSWSPMGCDANGRCLLAALTMDNRLTIQANLNRLQWVQLVDLTEIYGERLYETSYRLSKNEAPEGNLGDFAEFQRRHSMQTPVRMEWSGICTTQQVKHNNECRDVGSVLLAVLFENGNIAVWQFQLPFVGKESISSCNTIESGITSPSVLFWWEYEHNNRKMSGLIVGSAFGPIKILPVNLKAVKGYFTLRQPVILWKEMDQLPVHSIKCVPLYHPYQKCSCSLVVAARGSYVFWCLLLISKAGLNVHNSHVTGLHSLPIVSMTADKQNGTVYTCSSDGKVRQLIPIFTDVALKFEHQLIKLSDVFGSVRTHGIAVSPCGAYLAIITTEGMINGLHPVNKNYQVQFVTLKTFEEAAAQLLESSVQNLFKQVDLIDLVRWKILKDKHIPQFLQEALEKKIESSGVTYFWRFKLFLLRILYQSMQKTPSEALWKPTHEDSKILLVDSPGMGNADDEQQEEGTSSKQVVKQGLQERSKEGDVEEPTDDSLPTTGDAGGREPMEEKLLEIQGKIEAVEMHLTREHMKRVLGEVYLHTWITENTSIPTRGLCNFLMSDEEYDDRTARVLIGHISKKMNKQTFPEHCSLCKEILPFTDRKQAVCSNGHIWLRCFLTYQSCQSLIYRRCLLHDSIARHPAPEDPDWIKRLLQSPCPFCDSPVF
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-------MNTADQAR
-------CCHHHHCC		10.1719413330
3Phosphorylation-----MNTADQARVG
-----CCHHHHCCCC		30.2520068231
19PhosphorylationADDGPAPSGEEEGEG
CCCCCCCCCCCCCCC		62.0330266825
33AcetylationGGGEAGGKEPAADAA
CCCCCCCCCCCCCCC		60.6526051181
33UbiquitinationGGGEAGGKEPAADAA
CCCCCCCCCCCCCCC		60.6521906983
44PhosphorylationADAAPGPSAAFRLMV
CCCCCCCCHHHHHHH		37.8426074081
59UbiquitinationTRREPAVKLQYAVSG
CCCCCCHHHEEEECC		31.79-
115PhosphorylationSVPAPLNSCLLKVGS
CCCCCCCCCEEEECC		17.5228555341
119AcetylationPLNSCLLKVGSKTEV
CCCCCEEEECCCCCH		31.4425953088
119UbiquitinationPLNSCLLKVGSKTEV
CCCCCEEEECCCCCH		31.44-
122PhosphorylationSCLLKVGSKTEVAEC
CCEEEECCCCCHHHH		39.1223312004
123AcetylationCLLKVGSKTEVAECK
CEEEECCCCCHHHHH		42.6626051181
123UbiquitinationCLLKVGSKTEVAECK
CEEEECCCCCHHHHH		42.66-
124PhosphorylationLLKVGSKTEVAECKE
EEEECCCCCHHHHHH		37.0723312004
132AcetylationEVAECKEKFAASKDP
CHHHHHHHHHHCCCC		26.2926051181
137UbiquitinationKEKFAASKDPTVSQT
HHHHHHCCCCCHHCE		64.1021906983
149MethylationSQTFMLDRVFNPEGK
HCEEECCEECCCCCC		30.85-
156UbiquitinationRVFNPEGKALPPMRG
EECCCCCCCCCCCCC		45.12-
156AcetylationRVFNPEGKALPPMRG
EECCCCCCCCCCCCC		45.1226051181
165MethylationLPPMRGFKYTSWSPM
CCCCCCCEECCCCCC		50.90-
165UbiquitinationLPPMRGFKYTSWSPM
CCCCCCCEECCCCCC		50.90-
217PhosphorylationEIYGERLYETSYRLS
HHHHHHHHHHHCCCC		24.3128796482
224PhosphorylationYETSYRLSKNEAPEG
HHHHCCCCCCCCCCC		25.1628555341
225UbiquitinationETSYRLSKNEAPEGN
HHHCCCCCCCCCCCC		64.5021906983
225AcetylationETSYRLSKNEAPEGN
HHHCCCCCCCCCCCC		64.5026051181
225SumoylationETSYRLSKNEAPEGN
HHHCCCCCCCCCCCC		64.5028112733
348UbiquitinationKILPVNLKAVKGYFT
EEEECCHHEEECEEE		46.0221890473
348AcetylationKILPVNLKAVKGYFT
EEEECCHHEEECEEE		46.0225953088
351UbiquitinationPVNLKAVKGYFTLRQ
ECCHHEEECEEEECC		53.40-
355PhosphorylationKAVKGYFTLRQPVIL
HEEECEEEECCCEEE		16.7324719451
364UbiquitinationRQPVILWKEMDQLPV
CCCEEEEEECCCCCC		39.4521906983
366SulfoxidationPVILWKEMDQLPVHS
CEEEEEECCCCCCCE		3.3621406390
375UbiquitinationQLPVHSIKCVPLYHP
CCCCCEEEEEECCCC		31.99-
380PhosphorylationSIKCVPLYHPYQKCS
EEEEEECCCCCCCCC		8.4822817900
383PhosphorylationCVPLYHPYQKCSCSL
EEECCCCCCCCCCEE		13.8022817900
398PhosphorylationVVAARGSYVFWCLLL
EEEECCHHHHHHHHH		11.5122817900
446AcetylationYTCSSDGKVRQLIPI
EEECCCCCEEEEEEE		38.9526051181
446UbiquitinationYTCSSDGKVRQLIPI
EEECCCCCEEEEEEE		38.95-
460UbiquitinationIFTDVALKFEHQLIK
EEHHHHHHHHHHHHH		38.68-
467UbiquitinationKFEHQLIKLSDVFGS
HHHHHHHHHHHCCCC		51.0021906983
508PhosphorylationLHPVNKNYQVQFVTL
CCCCCCCCEEEEEEE		16.2128152594
551UbiquitinationRWKILKDKHIPQFLQ
HHHHHCCCCHHHHHH		41.67-
5512-HydroxyisobutyrylationRWKILKDKHIPQFLQ
HHHHHCCCCHHHHHH		41.67-
563UbiquitinationFLQEALEKKIESSGV
HHHHHHHHHHHHCCC		60.96-
567PhosphorylationALEKKIESSGVTYFW
HHHHHHHHCCCCHHH		35.5520068231
568PhosphorylationLEKKIESSGVTYFWR
HHHHHHHCCCCHHHH		25.2120068231
571PhosphorylationKIESSGVTYFWRFKL
HHHHCCCCHHHHHHH		19.2720068231
572PhosphorylationIESSGVTYFWRFKLF
HHHCCCCHHHHHHHH		9.9520068231
598UbiquitinationTPSEALWKPTHEDSK
CHHHHHCCCCCCCCC		40.67-
598AcetylationTPSEALWKPTHEDSK
CHHHHHCCCCCCCCC		40.6725953088
600PhosphorylationSEALWKPTHEDSKIL
HHHHCCCCCCCCCEE		33.8827422710
604PhosphorylationWKPTHEDSKILLVDS
CCCCCCCCCEEEECC		20.7225159151
611PhosphorylationSKILLVDSPGMGNAD
CCEEEECCCCCCCCC		18.8419664994
626PhosphorylationDEQQEEGTSSKQVVK
HHHHHCCCCHHHHHH		32.8623403867
627PhosphorylationEQQEEGTSSKQVVKQ
HHHHCCCCHHHHHHH		46.5223403867
628PhosphorylationQQEEGTSSKQVVKQG
HHHCCCCHHHHHHHH		27.2623403867
629UbiquitinationQEEGTSSKQVVKQGL
HHCCCCHHHHHHHHH		47.0521906983
629SumoylationQEEGTSSKQVVKQGL
HHCCCCHHHHHHHHH		47.0528112733
633UbiquitinationTSSKQVVKQGLQERS
CCHHHHHHHHHHHHH		39.53-
633AcetylationTSSKQVVKQGLQERS
CCHHHHHHHHHHHHH		39.5325953088
640PhosphorylationKQGLQERSKEGDVEE
HHHHHHHHCCCCCCC		34.0224732914
641AcetylationQGLQERSKEGDVEEP
HHHHHHHCCCCCCCC		72.4526051181
641UbiquitinationQGLQERSKEGDVEEP
HHHHHHHCCCCCCCC		72.45-
649PhosphorylationEGDVEEPTDDSLPTT
CCCCCCCCCCCCCCC		56.5723401153
652PhosphorylationVEEPTDDSLPTTGDA
CCCCCCCCCCCCCCC		38.7723401153
655PhosphorylationPTDDSLPTTGDAGGR
CCCCCCCCCCCCCCC		49.0223663014
656PhosphorylationTDDSLPTTGDAGGRE
CCCCCCCCCCCCCCC		30.9929255136
668UbiquitinationGREPMEEKLLEIQGK
CCCCHHHHHHHHHHH		45.10-
718PhosphorylationGLCNFLMSDEEYDDR
CHHHHHCCCCCCCHH		43.9829449344
736AcetylationVLIGHISKKMNKQTF
HHHHHHHHHCCCCCC		56.2825953088
740UbiquitinationHISKKMNKQTFPEHC
HHHHHCCCCCCHHHH		47.41-
760UbiquitinationILPFTDRKQAVCSNG
HCCCCCHHHEECCCC		45.48-
807UbiquitinationPEDPDWIKRLLQSPC
CCCCHHHHHHHCCCC		32.5121906983
807AcetylationPEDPDWIKRLLQSPC
CCCCHHHHHHHCCCC		32.5125953088
812PhosphorylationWIKRLLQSPCPFCDS
HHHHHHCCCCCCCCC		28.5627050516
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 TF3C4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TF3C4_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 TF3C4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF3C1_HUMANGTF3C1physical
10523658
TF3C2_HUMANGTF3C2physical
10523658
TF3C5_HUMANGTF3C5physical
10523658
TF3C3_HUMANGTF3C3physical
10523658
TF3C5_HUMANGTF3C5physical
22939629
TF3C6_HUMANGTF3C6physical
22939629
XPP1_HUMANXPNPEP1physical
22939629
API5_HUMANAPI5physical
22863883
EHD4_HUMANEHD4physical
22863883
EZRI_HUMANEZRphysical
22863883
LIMD1_HUMANLIMD1physical
22863883
NOL3_HUMANNOL3physical
22863883
PAPS2_HUMANPAPSS2physical
22863883
PLPHP_HUMANPROSCphysical
22863883
RL22_HUMANRPL22physical
22863883
EFTU_HUMANTUFMphysical
22863883
SYWC_HUMANWARSphysical
22863883
UBP15_HUMANUSP15physical
27173435
JIP4_HUMANSPAG9physical
27173435
MCM2_HUMANMCM2physical
27173435
MCM4_HUMANMCM4physical
27173435
MCM6_HUMANMCM6physical
27173435
EP15R_HUMANEPS15L1physical
27173435
NS1BP_HUMANIVNS1ABPphysical
27173435
SMC1A_HUMANSMC1Aphysical
27173435
GAPD1_HUMANGAPVD1physical
27173435
ANK3_HUMANANK3physical
27173435
SBNO1_HUMANSBNO1physical
27173435
SMC3_HUMANSMC3physical
27173435
HSF1_HUMANHSF1physical
27173435
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 TF3C4_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-611, AND MASS SPECTROMETRY.
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-611, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-611, AND MASS SPECTROMETRY.
"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-611, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, AND MASSSPECTROMETRY.

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