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Q9UKN8 (TF3C4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length822 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 822822General transcription factor 3C polypeptide 4
PRO_0000209713

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8
Modified residue6111Phosphoserine Ref.6 Ref.7 Ref.9 Ref.10 Ref.12

Natural variations

Natural variant2431H → R.
Corresponds to variant rs1044697 [ dbSNP | Ensembl ].
VAR_047098

Experimental info

Sequence conflict2681C → S in AAF05087. Ref.1
Sequence conflict4021C → R in AAF05087. Ref.1
Sequence conflict4131V → L in AAF05087. Ref.1
Sequence conflict4501L → V in AAF05087. Ref.1
Sequence conflict4831S → K in AAF05087. Ref.1
Sequence conflict6901R → P in AAF05087. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9UKN8 [UniParc].

Last modified November 4, 2008. Version 2.
Checksum: 2546A1E7D87F563C

FASTA82291,982
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
RefSeqNP_036336.2. NM_012204.2.
UniGeneHs.656646.

3D structure databases

ProteinModelPortalQ9UKN8.
SMRQ9UKN8. Positions 420-451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114738. 44 interactions.
IntActQ9UKN8. 6 interactions.
STRING9606.ENSP00000361219.

PTM databases

PhosphoSiteQ9UKN8.

Polymorphism databases

DMDM212276467.

Proteomic databases

PaxDbQ9UKN8.
PRIDEQ9UKN8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372146; ENSP00000361219; ENSG00000125484.
GeneID9329.
KEGGhsa:9329.
UCSCuc010mzv.3. human.

Organism-specific databases

CTD9329.
GeneCardsGC09P135545.
HGNCHGNC:4667. GTF3C4.
MIM604892. gene.
neXtProtNX_Q9UKN8.
PharmGKBPA29055.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG79304.
HOGENOMHOG000121774.
HOVERGENHBG059337.
InParanoidQ9UKN8.
KOK11310.
OMAAVWQFQL.
OrthoDBEOG7WQ7RS.
PhylomeDBQ9UKN8.
TreeFamTF328412.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9UKN8.
BgeeQ9UKN8.
CleanExHS_GTF3C4.
GenevestigatorQ9UKN8.

Family and domain databases

InterProIPR024761. TFIIIC_delta_N.
IPR024764. TFIIIC_Znf.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF12657. TFIIIC_delta. 1 hit.
PF12660. zf-TFIIIC. 1 hit.
[Graphical view]
SUPFAMSSF50978. SSF50978. 2 hits.
ProtoNetSearch...

Other

GeneWikiGTF3C4.
GenomeRNAi9329.
NextBio34943.
PROQ9UKN8.
SOURCESearch...

Entry information

Entry nameTF3C4_HUMAN
AccessionPrimary (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 16, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM