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Q9UKN8

- TF3C4_HUMAN

UniProt

Q9UKN8 - TF3C4_HUMAN

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
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (04 Nov 2008)
      Previous versions | rss
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    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
    4. protein binding Source: HGNC

    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

    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

    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

    ArrayExpressiQ9UKN8.
    BgeeiQ9UKN8.
    CleanExiHS_GTF3C4.
    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. 46 interactions.
    IntActiQ9UKN8. 6 interactions.
    STRINGi9606.ENSP00000361219.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UKN8.
    SMRiQ9UKN8. Positions 422-451.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TFIIIC subunit 4 family.Curated

    Phylogenomic databases

    eggNOGiNOG79304.
    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

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    MNTADQARVG PADDGPAPSG EEEGEGGGEA GGKEPAADAA PGPSAAFRLM    50
    VTRREPAVKL QYAVSGLEPL AWSEDHRVSV STARSIAVLE LICDVHNPGQ 100
    DLVIHRTSVP APLNSCLLKV GSKTEVAECK EKFAASKDPT VSQTFMLDRV 150
    FNPEGKALPP MRGFKYTSWS PMGCDANGRC LLAALTMDNR LTIQANLNRL 200
    QWVQLVDLTE IYGERLYETS YRLSKNEAPE GNLGDFAEFQ RRHSMQTPVR 250
    MEWSGICTTQ QVKHNNECRD VGSVLLAVLF ENGNIAVWQF QLPFVGKESI 300
    SSCNTIESGI TSPSVLFWWE YEHNNRKMSG LIVGSAFGPI KILPVNLKAV 350
    KGYFTLRQPV ILWKEMDQLP VHSIKCVPLY HPYQKCSCSL VVAARGSYVF 400
    WCLLLISKAG LNVHNSHVTG LHSLPIVSMT ADKQNGTVYT CSSDGKVRQL 450
    IPIFTDVALK FEHQLIKLSD VFGSVRTHGI AVSPCGAYLA IITTEGMING 500
    LHPVNKNYQV QFVTLKTFEE AAAQLLESSV QNLFKQVDLI DLVRWKILKD 550
    KHIPQFLQEA LEKKIESSGV TYFWRFKLFL LRILYQSMQK TPSEALWKPT 600
    HEDSKILLVD SPGMGNADDE QQEEGTSSKQ VVKQGLQERS KEGDVEEPTD 650
    DSLPTTGDAG GREPMEEKLL EIQGKIEAVE MHLTREHMKR VLGEVYLHTW 700
    ITENTSIPTR GLCNFLMSDE EYDDRTARVL IGHISKKMNK QTFPEHCSLC 750
    KEILPFTDRK QAVCSNGHIW LRCFLTYQSC QSLIYRRCLL HDSIARHPAP 800
    EDPDWIKRLL QSPCPFCDSP VF 822
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    SMRi Q9UKN8. Positions 422-451.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114738. 46 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.
    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

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

    Gene expression databases

    ArrayExpressi Q9UKN8.
    Bgeei Q9UKN8.
    CleanExi HS_GTF3C4.
    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

    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: October 1, 2014
    This is version 105 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