TF3A_HUMAN
ID TF3A_HUMAN Reviewed; 365 AA.
AC Q92664; B7ZBK5; Q12963; Q13097;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Transcription factor IIIA;
DE Short=TFIIIA;
GN Name=GTF3A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=7789179; DOI=10.1159/000134041;
RA Arakawa H., Nagase H., Hayashi N., Ogawa M., Nagata M., Fujiwara T.,
RA Takahashi E., Shin S., Nakamura Y.;
RT "Molecular cloning, characterization, and chromosomal mapping of a novel
RT human gene (GTF3A) that is highly homologous to Xenopus transcription
RT factor IIIA.";
RL Cytogenet. Cell Genet. 70:235-238(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-365 (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=7622052; DOI=10.1016/0378-1119(95)00145-v;
RA Drew P.D., Nagle J.W., Canning R.D., Ozato K., Biddison W.E., Becker K.G.;
RT "Cloning and expression analysis of a human cDNA homologous to Xenopus
RT TFIIIA.";
RL Gene 159:215-218(1995).
RN [4]
RP CHARACTERIZATION.
RX PubMed=8063702; DOI=10.1016/s0021-9258(17)31901-4;
RA Moorefield B., Roeder R.G.;
RT "Purification and characterization of human transcription factor IIIA.";
RL J. Biol. Chem. 269:20857-20865(1994).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP FUNCTION.
RX PubMed=24120868; DOI=10.1016/j.celrep.2013.08.049;
RA Sloan K.E., Bohnsack M.T., Watkins N.J.;
RT "The 5S RNP couples p53 homeostasis to ribosome biogenesis and nucleolar
RT stress.";
RL Cell Rep. 5:237-247(2013).
CC -!- FUNCTION: Involved in ribosomal large subunit biogenesis. Binds the
CC approximately 50 base pairs internal control region (ICR) of 5S
CC ribosomal RNA genes. It is required for their RNA polymerase III-
CC dependent transcription and may also maintain the transcription of
CC other genes (PubMed:24120868). Also binds the transcribed 5S RNA's (By
CC similarity). {ECO:0000250|UniProtKB:P17842,
CC ECO:0000269|PubMed:24120868}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92664-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92664-2; Sequence=VSP_031525, VSP_031526;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- CAUTION: It is uncertain whether Met-1 is the initiator. Based on the
CC lack of an in-frame AUG codon, mammalian TFIIIA may be translated from
CC this non-AUG initiation site, which has a good Kozak context and which
CC is well conserved among mammals. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06988.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA06988.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D32257; BAA06988.1; ALT_SEQ; mRNA.
DR EMBL; AL137059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U20272; AAA75623.1; -; mRNA.
DR EMBL; U14134; AAA21873.1; -; mRNA.
DR CCDS; CCDS45019.1; -. [Q92664-1]
DR PIR; I38937; I38937.
DR RefSeq; NP_002088.2; NM_002097.2. [Q92664-1]
DR AlphaFoldDB; Q92664; -.
DR SMR; Q92664; -.
DR BioGRID; 109226; 7.
DR CORUM; Q92664; -.
DR IntAct; Q92664; 8.
DR STRING; 9606.ENSP00000370532; -.
DR iPTMnet; Q92664; -.
DR PhosphoSitePlus; Q92664; -.
DR BioMuta; GTF3A; -.
DR DMDM; 172045838; -.
DR EPD; Q92664; -.
DR jPOST; Q92664; -.
DR MassIVE; Q92664; -.
DR MaxQB; Q92664; -.
DR PaxDb; Q92664; -.
DR PeptideAtlas; Q92664; -.
DR PRIDE; Q92664; -.
DR ProteomicsDB; 75396; -. [Q92664-1]
DR ProteomicsDB; 75397; -. [Q92664-2]
DR Antibodypedia; 5062; 248 antibodies from 25 providers.
DR DNASU; 2971; -.
DR Ensembl; ENST00000381140.10; ENSP00000370532.5; ENSG00000122034.17. [Q92664-1]
DR GeneID; 2971; -.
DR KEGG; hsa:2971; -.
DR MANE-Select; ENST00000381140.10; ENSP00000370532.5; NM_002097.3; NP_002088.2.
DR UCSC; uc058wav.1; human. [Q92664-1]
DR CTD; 2971; -.
DR DisGeNET; 2971; -.
DR GeneCards; GTF3A; -.
DR HGNC; HGNC:4662; GTF3A.
DR HPA; ENSG00000122034; Low tissue specificity.
DR MIM; 600860; gene.
DR neXtProt; NX_Q92664; -.
DR OpenTargets; ENSG00000122034; -.
DR PharmGKB; PA29048; -.
DR VEuPathDB; HostDB:ENSG00000122034; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000155647; -.
DR HOGENOM; CLU_002678_91_0_1; -.
DR InParanoid; Q92664; -.
DR OMA; HRKEQHR; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q92664; -.
DR TreeFam; TF333011; -.
DR PathwayCommons; Q92664; -.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR SignaLink; Q92664; -.
DR SIGNOR; Q92664; -.
DR BioGRID-ORCS; 2971; 633 hits in 1044 CRISPR screens.
DR ChiTaRS; GTF3A; human.
DR GeneWiki; GTF3A; -.
DR GenomeRNAi; 2971; -.
DR Pharos; Q92664; Tbio.
DR PRO; PR:Q92664; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q92664; protein.
DR Bgee; ENSG00000122034; Expressed in parotid gland and 211 other tissues.
DR ExpressionAtlas; Q92664; baseline and differential.
DR Genevisible; Q92664; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008097; F:5S rRNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0009303; P:rRNA transcription; TAS:ProtInc.
DR GO; GO:0006383; P:transcription by RNA polymerase III; TAS:ProtInc.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Ribosome biogenesis; RNA-binding;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..365
FT /note="Transcription factor IIIA"
FT /id="PRO_0000047080"
FT ZN_FING 40..64
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 70..94
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 100..125
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 132..154
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 162..186
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 189..213
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 217..239
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 246..271
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 277..301
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VAR_SEQ 164..188
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7622052"
FT /id="VSP_031525"
FT VAR_SEQ 189..190
FT /note="YV -> LC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7622052"
FT /id="VSP_031526"
FT VARIANT 245
FT /note="V -> L (in dbSNP:rs7323)"
FT /id="VAR_014824"
FT CONFLICT 156
FT /note="H -> N (in Ref. 1; BAA06988)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="R -> G (in Ref. 1; BAA06988)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 41515 MW; 261EBDCC550130B9 CRC64;
MDPPAVVAES VSSLTIADAF IAAGESSAPT PPRPALPRRF ICSFPDCSAN YSKAWKLDAH
LCKHTGERPF VCDYEGCGKA FIRDYHLSRH ILTHTGEKPF VCAANGCDQK FNTKSNLKKH
FERKHENQQK QYICSFEDCK KTFKKHQQLK IHQCQHTNEP LFKCTQEGCG KHFASPSKLK
RHAKAHEGYV CQKGCSFVAK TWTELLKHVR ETHKEEILCE VCRKTFKRKD YLKQHMKTHA
PERDVCRCPR EGCGRTYTTV FNLQSHILSF HEESRPFVCE HAGCGKTFAM KQSLTRHAVV
HDPDKKKMKL KVKKSREKRS LASHLSGYIP PKRKQGQGLS LCQNGESPNC VEDKMLSTVA
VLTLG
