Q9UKN8 (TF3C4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
General transcription factor 3C polypeptide 4
EC=2.3.1.48

Alternative name(s):
TF3C-delta
Transcription factor IIIC 90 kDa subunit
Short name=TFIIIC 90 kDa subunit
Short name=TFIIIC90
Transcription factor IIIC subunit delta

Gene names

Name:

GTF3C4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	822 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Part of the TFIIIC subcomplex TFIIIC2, consisting of six subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6. Interacts with BRF1, GTF3C1, GTF3C2, GTF3C5, GTF3C6, POLR3C and POLR3F. Ref.1 Ref.5
Subcellular location	Nucleus.
Sequence similarities	Belongs to the TFIIIC subunit 4 family.
Sequence caution	The sequence AAH11619.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	Transcription
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	5S class rRNA transcription from RNA polymerase III type 1 promoter Inferred by curator Ref.5. Source: HGNC tRNA transcription from RNA polymerase III promoter Inferred by curator Ref.5. Source: HGNC transcription initiation from RNA polymerase III promoter Traceable author statement Ref.1. Source: ProtInc
Cellular_component	transcription factor TFIIIC complex Inferred from direct assay Ref.5. Source: HGNC
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW enzyme activator activity Traceable author statement Ref.1. Source: ProtInc histone acetyltransferase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 822	822	General transcription factor 3C polypeptide 4		PRO_0000209713
Amino acid modifications
	Modified residue	611	1	Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.11
Natural variations
	Natural variant	243	1	H → R. Corresponds to variant rs1044697 [ dbSNP | Ensembl ].		VAR_047098
Experimental info
	Sequence conflict	268	1	C → S in AAF05087. Ref.1
	Sequence conflict	402	1	C → R in AAF05087. Ref.1
	Sequence conflict	413	1	V → L in AAF05087. Ref.1
	Sequence conflict	450	1	L → V in AAF05087. Ref.1
	Sequence conflict	483	1	S → K in AAF05087. Ref.1
	Sequence conflict	690	1	R → P in AAF05087. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9UKN8 [UniParc]. Last modified November 4, 2008. Version 2. Checksum: 2546A1E7D87F563C	FASTA	822	91,982
	10 20 30 40 50 60 MNTADQARVG PADDGPAPSG EEEGEGGGEA GGKEPAADAA PGPSAAFRLM VTRREPAVKL 70 80 90 100 110 120 QYAVSGLEPL AWSEDHRVSV STARSIAVLE LICDVHNPGQ DLVIHRTSVP APLNSCLLKV 130 140 150 160 170 180 GSKTEVAECK EKFAASKDPT VSQTFMLDRV FNPEGKALPP MRGFKYTSWS PMGCDANGRC 190 200 210 220 230 240 LLAALTMDNR LTIQANLNRL QWVQLVDLTE IYGERLYETS YRLSKNEAPE GNLGDFAEFQ 250 260 270 280 290 300 RRHSMQTPVR MEWSGICTTQ QVKHNNECRD VGSVLLAVLF ENGNIAVWQF QLPFVGKESI 310 320 330 340 350 360 SSCNTIESGI TSPSVLFWWE YEHNNRKMSG LIVGSAFGPI KILPVNLKAV KGYFTLRQPV 370 380 390 400 410 420 ILWKEMDQLP VHSIKCVPLY HPYQKCSCSL VVAARGSYVF WCLLLISKAG LNVHNSHVTG 430 440 450 460 470 480 LHSLPIVSMT ADKQNGTVYT CSSDGKVRQL IPIFTDVALK FEHQLIKLSD VFGSVRTHGI 490 500 510 520 530 540 AVSPCGAYLA IITTEGMING LHPVNKNYQV QFVTLKTFEE AAAQLLESSV QNLFKQVDLI 550 560 570 580 590 600 DLVRWKILKD KHIPQFLQEA LEKKIESSGV TYFWRFKLFL LRILYQSMQK TPSEALWKPT 610 620 630 640 650 660 HEDSKILLVD SPGMGNADDE QQEEGTSSKQ VVKQGLQERS KEGDVEEPTD DSLPTTGDAG 670 680 690 700 710 720 GREPMEEKLL EIQGKIEAVE MHLTREHMKR VLGEVYLHTW ITENTSIPTR GLCNFLMSDE 730 740 750 760 770 780 EYDDRTARVL IGHISKKMNK QTFPEHCSLC KEILPFTDRK QAVCSNGHIW LRCFLTYQSC 790 800 810 820 QSLIYRRCLL HDSIARHPAP EDPDWIKRLL QSPCPFCDSP VF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone-specific acetyltransferase activity." Hsieh Y.-J., Kundu T.K., Wang Z., Kovelman R., Roeder R.G. Mol. Cell. Biol. 19:7697-7704(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 139-156; 170-179; 614-626 AND 643-659, INTERACTION WITH GTF3C1; GTF3C2; GTF3C5; BRF1; POLR3C AND POLR3F.
[2]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Placenta and Testis.
[5]	"Identification, molecular cloning, and characterization of the sixth subunit of human transcription factor TFIIIC." Dumay-Odelot H., Marck C., Durrieu-Gaillard S., Lefebvre O., Jourdain S., Prochazkova M., Pflieger A., Teichmann M. J. Biol. Chem. 282:17179-17189(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN TFIIIC COMPLEX, INTERACTION WITH GTF3C6.
[6]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF142328 mRNA. Translation: AAF05087.1. AL160165 Genomic DNA. Translation: CAH70534.1. CH471090 Genomic DNA. Translation: EAW88011.1. BC011619 mRNA. Translation: AAH11619.1. Sequence problems. BC094774 mRNA. Translation: AAH94774.1. BC104755 mRNA. Translation: AAI04756.1. BC112245 mRNA. Translation: AAI12246.1.
IPI	IPI00016725.
RefSeq	NP_036336.2. NM_012204.2.
UniGene	Hs.656646.
3D structure databases
ProteinModelPortal	Q9UKN8.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UKN8. 3 interactions.
STRING	9606.ENSP00000361219.
PTM databases
PhosphoSite	Q9UKN8.
Polymorphism databases
DMDM	212276467.
Proteomic databases
PaxDb	Q9UKN8.
PRIDE	Q9UKN8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000372146; ENSP00000361219; ENSG00000125484.
GeneID	9329.
KEGG	hsa:9329.
UCSC	uc010mzv.3. human.
Organism-specific databases
CTD	9329.
GeneCards	GC09P135545.
HGNC	HGNC:4667. GTF3C4.
MIM	604892. gene.
neXtProt	NX_Q9UKN8.
PharmGKB	PA29055.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG79304.
HOGENOM	HOG000121774.
HOVERGEN	HBG059337.
InParanoid	Q9UKN8.
KO	K11310.
OMA	AVWQFQL.
OrthoDB	EOG40CHG9.
PhylomeDB	Q9UKN8.
Enzyme and pathway databases
Reactome	REACT_1788. Transcription. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q9UKN8.
Bgee	Q9UKN8.
CleanEx	HS_GTF3C4.
Genevestigator	Q9UKN8.
GermOnline	ENSG00000125484. Homo sapiens.
Family and domain databases
InterPro	IPR024761. TFIIIC_delta_N. IPR024764. TFIIIC_Znf. [Graphical view]
Pfam	PF12657. TFIIIC_delta. 1 hit. PF12660. zf-TFIIIC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	9329.
NextBio	34943.
SOURCE	Search...

Entry information

Entry name

TF3C4_HUMAN

Accession

Primary (citable) accession number: Q9UKN8
Secondary accession number(s): Q5VZJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	November 4, 2008
Last modified:	April 3, 2013
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.