Full text data of GTF3C5
GTF3C5
[Confidence: low (only semi-automatic identification from reviews)]
General transcription factor 3C polypeptide 5 (TF3C-epsilon; Transcription factor IIIC 63 kDa subunit; TFIIIC 63 kDa subunit; TFIIIC63; Transcription factor IIIC subunit epsilon)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
General transcription factor 3C polypeptide 5 (TF3C-epsilon; Transcription factor IIIC 63 kDa subunit; TFIIIC 63 kDa subunit; TFIIIC63; Transcription factor IIIC subunit epsilon)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y5Q8
ID TF3C5_HUMAN Reviewed; 519 AA.
AC Q9Y5Q8; A6NI44; A6NJB9; Q5T7U2; Q5T7U3; Q8N2U7; Q8N857; Q96GD9;
read moreAC Q9H4P2;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=General transcription factor 3C polypeptide 5;
DE AltName: Full=TF3C-epsilon;
DE AltName: Full=Transcription factor IIIC 63 kDa subunit;
DE Short=TFIIIC 63 kDa subunit;
DE Short=TFIIIC63;
DE AltName: Full=Transcription factor IIIC subunit epsilon;
GN Name=GTF3C5; ORFNames=CDABP0017;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH BRF1 AND TBP,
RP AND IDENTIFICATION OF SUBUNITS OF TFIIIC2 COMPLEX.
RX PubMed=10373544;
RA Hsieh Y.-J., Wang Z., Kovelman R., Roeder R.G.;
RT "Cloning and characterization of two evolutionarily conserved subunits
RT (TFIIIC102 and TFIIIC63) of human TFIIIC and their involvement in
RT functional interactions with TFIIIB and RNA polymerase III.";
RL Mol. Cell. Biol. 19:4944-4952(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Leukemia;
RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A.,
RA Margolin J.F.;
RT "Pediatric leukemia cDNA sequencing project.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain, and Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Kidney, Ovary, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION IN TFIIIC COMPLEX, AND INTERACTION WITH GTF3C6.
RX PubMed=17409385; DOI=10.1074/jbc.M611542200;
RA Dumay-Odelot H., Marck C., Durrieu-Gaillard S., Lefebvre O.,
RA Jourdain S., Prochazkova M., Pflieger A., Teichmann M.;
RT "Identification, molecular cloning, and characterization of the sixth
RT subunit of human transcription factor TFIIIC.";
RL J. Biol. Chem. 282:17179-17189(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in RNA polymerase III-mediated transcription.
CC Integral, tightly associated component of the DNA-binding TFIIIC2
CC subcomplex that directly binds tRNA and virus-associated RNA
CC promoters.
CC -!- SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six
CC subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6.
CC Interacts with BRF1, GTF3C6 and TBP.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y5Q8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y5Q8-2; Sequence=VSP_010355;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9Y5Q8-3; Sequence=VSP_035196;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the TFIIIC subunit 5 family.
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DR EMBL; AF133124; AAD41476.1; -; mRNA.
DR EMBL; AY007123; AAG01991.1; -; mRNA.
DR EMBL; AK055092; BAG51466.1; -; mRNA.
DR EMBL; AK097295; BAC04993.1; -; mRNA.
DR EMBL; AL162417; CAI13406.1; -; Genomic_DNA.
DR EMBL; AL162417; CAI13407.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88026.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88029.1; -; Genomic_DNA.
DR EMBL; BC009741; AAH09741.2; -; mRNA.
DR EMBL; BC011355; AAH11355.1; -; mRNA.
DR EMBL; BC017337; AAH17337.1; -; mRNA.
DR EMBL; BC030157; AAH30157.2; -; mRNA.
DR RefSeq; NP_001116295.1; NM_001122823.1.
DR RefSeq; NP_036219.2; NM_012087.3.
DR UniGene; Hs.495417; -.
DR ProteinModelPortal; Q9Y5Q8; -.
DR DIP; DIP-50823N; -.
DR IntAct; Q9Y5Q8; 4.
DR MINT; MINT-4777347; -.
DR PhosphoSite; Q9Y5Q8; -.
DR DMDM; 47606222; -.
DR PaxDb; Q9Y5Q8; -.
DR PRIDE; Q9Y5Q8; -.
DR DNASU; 9328; -.
DR Ensembl; ENST00000372097; ENSP00000361169; ENSG00000148308.
DR Ensembl; ENST00000372108; ENSP00000361180; ENSG00000148308.
DR GeneID; 9328; -.
DR KEGG; hsa:9328; -.
DR UCSC; uc004cci.4; human.
DR CTD; 9328; -.
DR GeneCards; GC09P135906; -.
DR HGNC; HGNC:4668; GTF3C5.
DR MIM; 604890; gene.
DR neXtProt; NX_Q9Y5Q8; -.
DR PharmGKB; PA29056; -.
DR eggNOG; NOG311463; -.
DR HOVERGEN; HBG058445; -.
DR KO; K15202; -.
DR OMA; RDTMSLM; -.
DR OrthoDB; EOG780RMW; -.
DR PhylomeDB; Q9Y5Q8; -.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; GTF3C5; human.
DR GeneWiki; GTF3C5; -.
DR GenomeRNAi; 9328; -.
DR NextBio; 34939; -.
DR PRO; PR:Q9Y5Q8; -.
DR ArrayExpress; Q9Y5Q8; -.
DR Bgee; Q9Y5Q8; -.
DR Genevestigator; Q9Y5Q8; -.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000127; C:transcription factor TFIIIC complex; IDA:HGNC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042791; P:5S class rRNA transcription from RNA polymerase III type 1 promoter; IC:HGNC.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0042797; P:tRNA transcription from RNA polymerase III promoter; IC:HGNC.
DR InterPro; IPR019136; TF_IIIC_su-5.
DR Pfam; PF09734; Tau95; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; DNA-binding;
KW Nucleus; Polymorphism; Reference proteome; Transcription.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 519 General transcription factor 3C
FT polypeptide 5.
FT /FTId=PRO_0000209715.
FT COMPBIAS 478 514 Glu-rich.
FT COMPBIAS 486 499 Poly-Glu.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 56 65 Missing (in isoform 2).
FT /FTId=VSP_010355.
FT VAR_SEQ 389 389 K -> KVSLQTLR (in isoform 3).
FT /FTId=VSP_035196.
FT VARIANT 445 445 D -> N (in dbSNP:rs637435).
FT /FTId=VAR_053727.
FT CONFLICT 372 372 P -> R (in Ref. 1; AAD41476).
FT CONFLICT 375 375 T -> A (in Ref. 3; BAC04993).
SQ SEQUENCE 519 AA; 59571 MW; 088B8B6125CEEF36 CRC64;
MAAEAADLGL GAAVPVELRR ERRMVCVEYP GVVRDVAKML PTLGGEEGVS RIYADPTKRL
ELYFRPKDPY CHPVCANRFS TSSLLLRIRK RTRRQKGVLG TEAHSEVTFD MEILGIISTI
YKFQGMSDFQ YLAVHTEAGG KHTSMYDKVL MLRPEKEAFF HQELPLYIPP PIFSRLDAPV
DYFYRPETQH REGYNNPPIS GENLIGLSRA RRPHNAIFVN FEDEEVPKQP LEAAAQTWRR
VCTNPVDRKV EEELRKLFDI RPIWSRNAVK ANISVHPDKL KVLLPFIAYY MITGPWRSLW
IRFGYDPRKN PDAKIYQVLD FRIRCGMKHG YAPSDLPVKA KRSTYNYSLP ITVKKTSSQL
VTMHDLKQGL GPSGTSGARK PASSKYKLKD SVYIFREGAL PPYRQMFYQL CDLNVEELQK
IIHRNDGAEN SCTERDGWCL PKTSDELRDT MSLMIRQTIR SKRPALFSSS AKADGGKEQL
TYESGEDEED EEEEEEEEED FKPSDGSENE METEILDYV
//
ID TF3C5_HUMAN Reviewed; 519 AA.
AC Q9Y5Q8; A6NI44; A6NJB9; Q5T7U2; Q5T7U3; Q8N2U7; Q8N857; Q96GD9;
read moreAC Q9H4P2;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=General transcription factor 3C polypeptide 5;
DE AltName: Full=TF3C-epsilon;
DE AltName: Full=Transcription factor IIIC 63 kDa subunit;
DE Short=TFIIIC 63 kDa subunit;
DE Short=TFIIIC63;
DE AltName: Full=Transcription factor IIIC subunit epsilon;
GN Name=GTF3C5; ORFNames=CDABP0017;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH BRF1 AND TBP,
RP AND IDENTIFICATION OF SUBUNITS OF TFIIIC2 COMPLEX.
RX PubMed=10373544;
RA Hsieh Y.-J., Wang Z., Kovelman R., Roeder R.G.;
RT "Cloning and characterization of two evolutionarily conserved subunits
RT (TFIIIC102 and TFIIIC63) of human TFIIIC and their involvement in
RT functional interactions with TFIIIB and RNA polymerase III.";
RL Mol. Cell. Biol. 19:4944-4952(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Leukemia;
RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A.,
RA Margolin J.F.;
RT "Pediatric leukemia cDNA sequencing project.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain, and Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Kidney, Ovary, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION IN TFIIIC COMPLEX, AND INTERACTION WITH GTF3C6.
RX PubMed=17409385; DOI=10.1074/jbc.M611542200;
RA Dumay-Odelot H., Marck C., Durrieu-Gaillard S., Lefebvre O.,
RA Jourdain S., Prochazkova M., Pflieger A., Teichmann M.;
RT "Identification, molecular cloning, and characterization of the sixth
RT subunit of human transcription factor TFIIIC.";
RL J. Biol. Chem. 282:17179-17189(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in RNA polymerase III-mediated transcription.
CC Integral, tightly associated component of the DNA-binding TFIIIC2
CC subcomplex that directly binds tRNA and virus-associated RNA
CC promoters.
CC -!- SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six
CC subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6.
CC Interacts with BRF1, GTF3C6 and TBP.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y5Q8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y5Q8-2; Sequence=VSP_010355;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9Y5Q8-3; Sequence=VSP_035196;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the TFIIIC subunit 5 family.
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DR EMBL; AF133124; AAD41476.1; -; mRNA.
DR EMBL; AY007123; AAG01991.1; -; mRNA.
DR EMBL; AK055092; BAG51466.1; -; mRNA.
DR EMBL; AK097295; BAC04993.1; -; mRNA.
DR EMBL; AL162417; CAI13406.1; -; Genomic_DNA.
DR EMBL; AL162417; CAI13407.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88026.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88029.1; -; Genomic_DNA.
DR EMBL; BC009741; AAH09741.2; -; mRNA.
DR EMBL; BC011355; AAH11355.1; -; mRNA.
DR EMBL; BC017337; AAH17337.1; -; mRNA.
DR EMBL; BC030157; AAH30157.2; -; mRNA.
DR RefSeq; NP_001116295.1; NM_001122823.1.
DR RefSeq; NP_036219.2; NM_012087.3.
DR UniGene; Hs.495417; -.
DR ProteinModelPortal; Q9Y5Q8; -.
DR DIP; DIP-50823N; -.
DR IntAct; Q9Y5Q8; 4.
DR MINT; MINT-4777347; -.
DR PhosphoSite; Q9Y5Q8; -.
DR DMDM; 47606222; -.
DR PaxDb; Q9Y5Q8; -.
DR PRIDE; Q9Y5Q8; -.
DR DNASU; 9328; -.
DR Ensembl; ENST00000372097; ENSP00000361169; ENSG00000148308.
DR Ensembl; ENST00000372108; ENSP00000361180; ENSG00000148308.
DR GeneID; 9328; -.
DR KEGG; hsa:9328; -.
DR UCSC; uc004cci.4; human.
DR CTD; 9328; -.
DR GeneCards; GC09P135906; -.
DR HGNC; HGNC:4668; GTF3C5.
DR MIM; 604890; gene.
DR neXtProt; NX_Q9Y5Q8; -.
DR PharmGKB; PA29056; -.
DR eggNOG; NOG311463; -.
DR HOVERGEN; HBG058445; -.
DR KO; K15202; -.
DR OMA; RDTMSLM; -.
DR OrthoDB; EOG780RMW; -.
DR PhylomeDB; Q9Y5Q8; -.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; GTF3C5; human.
DR GeneWiki; GTF3C5; -.
DR GenomeRNAi; 9328; -.
DR NextBio; 34939; -.
DR PRO; PR:Q9Y5Q8; -.
DR ArrayExpress; Q9Y5Q8; -.
DR Bgee; Q9Y5Q8; -.
DR Genevestigator; Q9Y5Q8; -.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000127; C:transcription factor TFIIIC complex; IDA:HGNC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042791; P:5S class rRNA transcription from RNA polymerase III type 1 promoter; IC:HGNC.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0042797; P:tRNA transcription from RNA polymerase III promoter; IC:HGNC.
DR InterPro; IPR019136; TF_IIIC_su-5.
DR Pfam; PF09734; Tau95; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; DNA-binding;
KW Nucleus; Polymorphism; Reference proteome; Transcription.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 519 General transcription factor 3C
FT polypeptide 5.
FT /FTId=PRO_0000209715.
FT COMPBIAS 478 514 Glu-rich.
FT COMPBIAS 486 499 Poly-Glu.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 56 65 Missing (in isoform 2).
FT /FTId=VSP_010355.
FT VAR_SEQ 389 389 K -> KVSLQTLR (in isoform 3).
FT /FTId=VSP_035196.
FT VARIANT 445 445 D -> N (in dbSNP:rs637435).
FT /FTId=VAR_053727.
FT CONFLICT 372 372 P -> R (in Ref. 1; AAD41476).
FT CONFLICT 375 375 T -> A (in Ref. 3; BAC04993).
SQ SEQUENCE 519 AA; 59571 MW; 088B8B6125CEEF36 CRC64;
MAAEAADLGL GAAVPVELRR ERRMVCVEYP GVVRDVAKML PTLGGEEGVS RIYADPTKRL
ELYFRPKDPY CHPVCANRFS TSSLLLRIRK RTRRQKGVLG TEAHSEVTFD MEILGIISTI
YKFQGMSDFQ YLAVHTEAGG KHTSMYDKVL MLRPEKEAFF HQELPLYIPP PIFSRLDAPV
DYFYRPETQH REGYNNPPIS GENLIGLSRA RRPHNAIFVN FEDEEVPKQP LEAAAQTWRR
VCTNPVDRKV EEELRKLFDI RPIWSRNAVK ANISVHPDKL KVLLPFIAYY MITGPWRSLW
IRFGYDPRKN PDAKIYQVLD FRIRCGMKHG YAPSDLPVKA KRSTYNYSLP ITVKKTSSQL
VTMHDLKQGL GPSGTSGARK PASSKYKLKD SVYIFREGAL PPYRQMFYQL CDLNVEELQK
IIHRNDGAEN SCTERDGWCL PKTSDELRDT MSLMIRQTIR SKRPALFSSS AKADGGKEQL
TYESGEDEED EEEEEEEEED FKPSDGSENE METEILDYV
//
MIM
604890
*RECORD*
*FIELD* NO
604890
*FIELD* TI
*604890 GENERAL TRANSCRIPTION FACTOR 3C, POLYPEPTIDE 5; GTF3C5
;;TRANSCRIPTION FACTOR IIIC, 63-KD SUBUNIT; TFIIIC63
read more*FIELD* TX
RNA polymerases are unable to initiate RNA synthesis in the absence of
additional proteins called general transcription factors (GTFs). GTFs
assemble in a complex on the DNA promoter and recruit the RNA
polymerase. GTF3C family proteins (e.g., GTF3C1; 603246) are essential
for RNA polymerase III to make a number of small nuclear and cytoplasmic
RNAs, including 5S RNA (180420), tRNA, and adenovirus-associated (VA)
RNA of both cellular and viral origin. Transcription by RNA polymerase
III is enhanced during viral infection by the expression of immediate
early proteins of adenovirus and pseudorabies virus.
By screening human cDNA cell libraries using degenerate PCR primers
corresponding to internal peptide sequences of the 63-kD subunit of
GTF3C, Hsieh et al. (1999) obtained a cDNA encoding GTF3C5, which they
called TFIIIC63. Sequence analysis showed that the deduced 519-amino
acid GTF3C5 protein contains a central helix-turn-helix motif and a
C-terminal acidic region. Immunoblot analyses indicated that the
expressed cDNA encodes a 63-kD protein that copurifies with the
remainder of the GTF3C complex. In addition, the authors showed that the
GTF3C complex interacts with GTF3B (see TAF3C; 604902) in the
recruitment of RNA polymerase III.
*FIELD* RF
1. Hsieh, Y.-J.; Wang, Z.; Kovelman, R.; Roeder, R. G.: Cloning and
characterization of two evolutionarily conserved subunits (TFIIIC102
and TFIIIC63) of human TFIIIC and their involvement in functional
interactions with TFIIIB and RNA polymerase III. Mol. Cell. Biol. 19:
4944-4952, 1999.
*FIELD* CD
Paul J. Converse: 4/28/2000
*FIELD* ED
mgross: 05/01/2000
mgross: 4/28/2000
*RECORD*
*FIELD* NO
604890
*FIELD* TI
*604890 GENERAL TRANSCRIPTION FACTOR 3C, POLYPEPTIDE 5; GTF3C5
;;TRANSCRIPTION FACTOR IIIC, 63-KD SUBUNIT; TFIIIC63
read more*FIELD* TX
RNA polymerases are unable to initiate RNA synthesis in the absence of
additional proteins called general transcription factors (GTFs). GTFs
assemble in a complex on the DNA promoter and recruit the RNA
polymerase. GTF3C family proteins (e.g., GTF3C1; 603246) are essential
for RNA polymerase III to make a number of small nuclear and cytoplasmic
RNAs, including 5S RNA (180420), tRNA, and adenovirus-associated (VA)
RNA of both cellular and viral origin. Transcription by RNA polymerase
III is enhanced during viral infection by the expression of immediate
early proteins of adenovirus and pseudorabies virus.
By screening human cDNA cell libraries using degenerate PCR primers
corresponding to internal peptide sequences of the 63-kD subunit of
GTF3C, Hsieh et al. (1999) obtained a cDNA encoding GTF3C5, which they
called TFIIIC63. Sequence analysis showed that the deduced 519-amino
acid GTF3C5 protein contains a central helix-turn-helix motif and a
C-terminal acidic region. Immunoblot analyses indicated that the
expressed cDNA encodes a 63-kD protein that copurifies with the
remainder of the GTF3C complex. In addition, the authors showed that the
GTF3C complex interacts with GTF3B (see TAF3C; 604902) in the
recruitment of RNA polymerase III.
*FIELD* RF
1. Hsieh, Y.-J.; Wang, Z.; Kovelman, R.; Roeder, R. G.: Cloning and
characterization of two evolutionarily conserved subunits (TFIIIC102
and TFIIIC63) of human TFIIIC and their involvement in functional
interactions with TFIIIB and RNA polymerase III. Mol. Cell. Biol. 19:
4944-4952, 1999.
*FIELD* CD
Paul J. Converse: 4/28/2000
*FIELD* ED
mgross: 05/01/2000
mgross: 4/28/2000