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Q9UKN8

- TF3C4_HUMAN

UniProt

Q9UKN8 - TF3C4_HUMAN

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Protein

General transcription factor 3C polypeptide 4

Gene

GTF3C4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. enzyme activator activity Source: ProtInc
  3. histone acetyltransferase activity Source: ProtInc

GO - Biological processi

  1. 5S class rRNA transcription from RNA polymerase III type 1 promoter Source: HGNC
  2. gene expression Source: Reactome
  3. histone acetylation Source: GOC
  4. positive regulation of catalytic activity Source: GOC
  5. transcription, DNA-templated Source: HGNC
  6. transcription from RNA polymerase III promoter Source: HGNC
  7. transcription initiation from RNA polymerase III promoter Source: ProtInc
  8. tRNA transcription from RNA polymerase III promoter Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Transcription

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_1036. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
REACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_347. RNA Polymerase III Transcription Initiation From Type 1 Promoter.

Names & Taxonomyi

Protein namesi
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 namesi
Name:GTF3C4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:4667. GTF3C4.

Subcellular locationi

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. transcription factor TFIIIC complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29055.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 822822General transcription factor 3C polypeptide 4PRO_0000209713Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei611 – 6111Phosphoserine5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UKN8.
PaxDbiQ9UKN8.
PRIDEiQ9UKN8.

PTM databases

PhosphoSiteiQ9UKN8.

Expressioni

Gene expression databases

BgeeiQ9UKN8.
CleanExiHS_GTF3C4.
ExpressionAtlasiQ9UKN8. baseline and differential.
GenevestigatoriQ9UKN8.

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

BioGridi114738. 47 interactions.
IntActiQ9UKN8. 6 interactions.
STRINGi9606.ENSP00000361219.

Structurei

3D structure databases

ProteinModelPortaliQ9UKN8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TFIIIC subunit 4 family.Curated

Phylogenomic databases

eggNOGiNOG79304.
GeneTreeiENSGT00390000011873.
HOGENOMiHOG000121774.
HOVERGENiHBG059337.
InParanoidiQ9UKN8.
KOiK11310.
OMAiWQFQLPF.
OrthoDBiEOG7WQ7RS.
PhylomeDBiQ9UKN8.
TreeFamiTF328412.

Family and domain databases

InterProiIPR024761. TFIIIC_delta_N.
IPR024764. TFIIIC_Znf.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12657. TFIIIC_delta. 1 hit.
PF12660. zf-TFIIIC. 1 hit.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9UKN8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNTADQARVG PADDGPAPSG EEEGEGGGEA GGKEPAADAA PGPSAAFRLM
60 70 80 90 100
VTRREPAVKL QYAVSGLEPL AWSEDHRVSV STARSIAVLE LICDVHNPGQ
110 120 130 140 150
DLVIHRTSVP APLNSCLLKV GSKTEVAECK EKFAASKDPT VSQTFMLDRV
160 170 180 190 200
FNPEGKALPP MRGFKYTSWS PMGCDANGRC LLAALTMDNR LTIQANLNRL
210 220 230 240 250
QWVQLVDLTE IYGERLYETS YRLSKNEAPE GNLGDFAEFQ RRHSMQTPVR
260 270 280 290 300
MEWSGICTTQ QVKHNNECRD VGSVLLAVLF ENGNIAVWQF QLPFVGKESI
310 320 330 340 350
SSCNTIESGI TSPSVLFWWE YEHNNRKMSG LIVGSAFGPI KILPVNLKAV
360 370 380 390 400
KGYFTLRQPV ILWKEMDQLP VHSIKCVPLY HPYQKCSCSL VVAARGSYVF
410 420 430 440 450
WCLLLISKAG LNVHNSHVTG LHSLPIVSMT ADKQNGTVYT CSSDGKVRQL
460 470 480 490 500
IPIFTDVALK FEHQLIKLSD VFGSVRTHGI AVSPCGAYLA IITTEGMING
510 520 530 540 550
LHPVNKNYQV QFVTLKTFEE AAAQLLESSV QNLFKQVDLI DLVRWKILKD
560 570 580 590 600
KHIPQFLQEA LEKKIESSGV TYFWRFKLFL LRILYQSMQK TPSEALWKPT
610 620 630 640 650
HEDSKILLVD SPGMGNADDE QQEEGTSSKQ VVKQGLQERS KEGDVEEPTD
660 670 680 690 700
DSLPTTGDAG GREPMEEKLL EIQGKIEAVE MHLTREHMKR VLGEVYLHTW
710 720 730 740 750
ITENTSIPTR GLCNFLMSDE EYDDRTARVL IGHISKKMNK QTFPEHCSLC
760 770 780 790 800
KEILPFTDRK QAVCSNGHIW LRCFLTYQSC QSLIYRRCLL HDSIARHPAP
810 820
EDPDWIKRLL QSPCPFCDSP VF
Length:822
Mass (Da):91,982
Last modified:November 4, 2008 - v2
Checksum:i2546A1E7D87F563C
GO

Sequence cautioni

The sequence AAH11619.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti268 – 2681C → S in AAF05087. (PubMed:10523658)Curated
Sequence conflicti402 – 4021C → R in AAF05087. (PubMed:10523658)Curated
Sequence conflicti413 – 4131V → L in AAF05087. (PubMed:10523658)Curated
Sequence conflicti450 – 4501L → V in AAF05087. (PubMed:10523658)Curated
Sequence conflicti483 – 4831S → K in AAF05087. (PubMed:10523658)Curated
Sequence conflicti690 – 6901R → P in AAF05087. (PubMed:10523658)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti243 – 2431H → R.
Corresponds to variant rs1044697 [ dbSNP | Ensembl ].
VAR_047098

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6953.1.
RefSeqiNP_036336.2. NM_012204.2.
UniGeneiHs.656646.

Genome annotation databases

EnsembliENST00000372146; ENSP00000361219; ENSG00000125484.
GeneIDi9329.
KEGGihsa:9329.
UCSCiuc010mzv.3. human.

Polymorphism databases

DMDMi212276467.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS6953.1.
RefSeqi NP_036336.2. NM_012204.2.
UniGenei Hs.656646.

3D structure databases

ProteinModelPortali Q9UKN8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114738. 47 interactions.
IntActi Q9UKN8. 6 interactions.
STRINGi 9606.ENSP00000361219.

PTM databases

PhosphoSitei Q9UKN8.

Polymorphism databases

DMDMi 212276467.

Proteomic databases

MaxQBi Q9UKN8.
PaxDbi Q9UKN8.
PRIDEi Q9UKN8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000372146 ; ENSP00000361219 ; ENSG00000125484 .
GeneIDi 9329.
KEGGi hsa:9329.
UCSCi uc010mzv.3. human.

Organism-specific databases

CTDi 9329.
GeneCardsi GC09P135545.
HGNCi HGNC:4667. GTF3C4.
MIMi 604892. gene.
neXtProti NX_Q9UKN8.
PharmGKBi PA29055.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG79304.
GeneTreei ENSGT00390000011873.
HOGENOMi HOG000121774.
HOVERGENi HBG059337.
InParanoidi Q9UKN8.
KOi K11310.
OMAi WQFQLPF.
OrthoDBi EOG7WQ7RS.
PhylomeDBi Q9UKN8.
TreeFami TF328412.

Enzyme and pathway databases

Reactomei REACT_1036. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
REACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_347. RNA Polymerase III Transcription Initiation From Type 1 Promoter.

Miscellaneous databases

ChiTaRSi GTF3C4. human.
GeneWikii GTF3C4.
GenomeRNAii 9329.
NextBioi 34943.
PROi Q9UKN8.
SOURCEi Search...

Gene expression databases

Bgeei Q9UKN8.
CleanExi HS_GTF3C4.
ExpressionAtlasi Q9UKN8. baseline and differential.
Genevestigatori Q9UKN8.

Family and domain databases

InterProi IPR024761. TFIIIC_delta_N.
IPR024764. TFIIIC_Znf.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF12657. TFIIIC_delta. 1 hit.
PF12660. zf-TFIIIC. 1 hit.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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].

Entry informationi

Entry nameiTF3C4_HUMAN
AccessioniPrimary (citable) accession number: Q9UKN8
Secondary accession number(s): Q5VZJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: November 4, 2008
Last modified: November 26, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3