Full text data of BTF3
BTF3
(NACB)
[Confidence: low (only semi-automatic identification from reviews)]
Transcription factor BTF3 (RNA polymerase B transcription factor 3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Transcription factor BTF3 (RNA polymerase B transcription factor 3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P20290
ID BTF3_HUMAN Reviewed; 206 AA.
AC P20290; A8K510; Q13893; Q76M56;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1991, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Transcription factor BTF3;
DE AltName: Full=RNA polymerase B transcription factor 3;
GN Name=BTF3; Synonyms=NACB; ORFNames=OK/SW-cl.8;
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] (ISOFORMS 1 AND 2).
RX PubMed=2320128; DOI=10.1038/344556a0;
RA Zheng X.M., Black D., Chambon P., Egly J.-M.;
RT "Sequencing and expression of complementary DNA for the general
RT transcription factor BTF3.";
RL Nature 344:556-559(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leukocyte;
RX PubMed=1386332; DOI=10.1016/0378-1119(92)90732-5;
RA Kanno M., Chalut C., Egly J.-M.;
RT "Genomic structure of the putative BTF3 transcription factor.";
RL Gene 117:219-228(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Leffers H., Honore B., Madsen A., Nielsen M.S., Anderson A.H.,
RA Celis J.E.;
RT "cDNA expression and human 2D-gel data bases: towards integrating
RT protein and DNA information.";
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
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).
CC -!- FUNCTION: General transcription factor. BTF3 can form a stable
CC complex with RNA polymerase II. Required for the initiation of
CC transcription.
CC -!- INTERACTION:
CC P03372:ESR1; NbExp=5; IntAct=EBI-1054703, EBI-78473;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=BTF3a;
CC IsoId=P20290-1; Sequence=Displayed;
CC Name=2; Synonyms=BTF3b;
CC IsoId=P20290-2; Sequence=VSP_013587;
CC -!- SIMILARITY: Belongs to the NAC-beta family.
CC -!- SIMILARITY: Contains 1 NAC-A/B (NAC-alpha/beta) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X53280; CAA37375.1; -; mRNA.
DR EMBL; X53281; CAA37376.1; -; mRNA.
DR EMBL; M90357; AAA58398.1; -; Genomic_DNA.
DR EMBL; M90352; AAA58398.1; JOINED; Genomic_DNA.
DR EMBL; X74070; CAA52200.1; -; mRNA.
DR EMBL; AB062126; BAB93458.1; -; mRNA.
DR EMBL; BT007120; AAP35784.1; -; mRNA.
DR EMBL; AK291125; BAF83814.1; -; mRNA.
DR EMBL; CH471084; EAW95727.1; -; Genomic_DNA.
DR EMBL; BC008062; AAH08062.1; -; mRNA.
DR PIR; JC1235; JC1235.
DR RefSeq; NP_001032726.1; NM_001037637.1.
DR RefSeq; NP_001198.2; NM_001207.4.
DR UniGene; Hs.591768; -.
DR PDB; 3LKX; X-ray; 2.50 A; A=97-162.
DR PDB; 3MCB; X-ray; 1.90 A; B=97-154.
DR PDBsum; 3LKX; -.
DR PDBsum; 3MCB; -.
DR ProteinModelPortal; P20290; -.
DR SMR; P20290; 97-154.
DR IntAct; P20290; 5.
DR MINT; MINT-5002480; -.
DR STRING; 9606.ENSP00000369965; -.
DR PhosphoSite; P20290; -.
DR DMDM; 115143; -.
DR PaxDb; P20290; -.
DR PRIDE; P20290; -.
DR DNASU; 689; -.
DR Ensembl; ENST00000335895; ENSP00000338516; ENSG00000145741.
DR Ensembl; ENST00000380591; ENSP00000369965; ENSG00000145741.
DR GeneID; 689; -.
DR KEGG; hsa:689; -.
DR UCSC; uc003kcq.1; human.
DR CTD; 689; -.
DR GeneCards; GC05P072794; -.
DR HGNC; HGNC:1125; BTF3.
DR HPA; CAB013007; -.
DR MIM; 602542; gene.
DR neXtProt; NX_P20290; -.
DR PharmGKB; PA25445; -.
DR eggNOG; NOG283773; -.
DR HOGENOM; HOG000261245; -.
DR HOVERGEN; HBG004906; -.
DR InParanoid; P20290; -.
DR KO; K01527; -.
DR OMA; DGKAPIA; -.
DR OrthoDB; EOG7CVPXQ; -.
DR PhylomeDB; P20290; -.
DR ChiTaRS; BTF3; human.
DR EvolutionaryTrace; P20290; -.
DR GeneWiki; BTF3; -.
DR GenomeRNAi; 689; -.
DR NextBio; 2836; -.
DR PRO; PR:P20290; -.
DR ArrayExpress; P20290; -.
DR Bgee; P20290; -.
DR CleanEx; HS_BTF3; -.
DR Genevestigator; P20290; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR Pfam; PF01849; NAC; 1.
DR PROSITE; PS51151; NAC_AB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1 206 Transcription factor BTF3.
FT /FTId=PRO_0000213548.
FT DOMAIN 82 147 NAC-A/B.
FT COMPBIAS 185 188 Poly-Asp.
FT MOD_RES 30 30 Phosphoserine.
FT VAR_SEQ 1 44 Missing (in isoform 2).
FT /FTId=VSP_013587.
FT CONFLICT 41 41 Q -> E (in Ref. 2; AAA58398).
FT CONFLICT 68 105 Missing (in Ref. 2; AAA58398).
FT CONFLICT 192 196 DLVEN -> GG (in Ref. 2).
FT CONFLICT 198 198 D -> Q (in Ref. 2).
FT STRAND 105 110
FT STRAND 113 120
FT STRAND 122 126
FT TURN 127 130
FT STRAND 131 136
FT STRAND 138 142
FT HELIX 143 146
FT HELIX 149 153
FT HELIX 158 161
SQ SEQUENCE 206 AA; 22168 MW; 9653AC480EAF64C6 CRC64;
MRRTGAPAQA DSRGRGRARG GCPGGEATLS QPPPRGGTRG QEPQMKETIM NQEKLAKLQA
QVRIGGKGTA RRKKKVVHRT ATADDKKLQF SLKKLGVNNI SGIEEVNMFT NQGTVIHFNN
PKVQASLAAN TFTITGHAET KQLTEMLPSI LNQLGADSLT SLRRLAEALP KQSVDGKAPL
ATGEDDDDEV PDLVENFDEA SKNEAN
//
ID BTF3_HUMAN Reviewed; 206 AA.
AC P20290; A8K510; Q13893; Q76M56;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1991, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Transcription factor BTF3;
DE AltName: Full=RNA polymerase B transcription factor 3;
GN Name=BTF3; Synonyms=NACB; ORFNames=OK/SW-cl.8;
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] (ISOFORMS 1 AND 2).
RX PubMed=2320128; DOI=10.1038/344556a0;
RA Zheng X.M., Black D., Chambon P., Egly J.-M.;
RT "Sequencing and expression of complementary DNA for the general
RT transcription factor BTF3.";
RL Nature 344:556-559(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leukocyte;
RX PubMed=1386332; DOI=10.1016/0378-1119(92)90732-5;
RA Kanno M., Chalut C., Egly J.-M.;
RT "Genomic structure of the putative BTF3 transcription factor.";
RL Gene 117:219-228(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Leffers H., Honore B., Madsen A., Nielsen M.S., Anderson A.H.,
RA Celis J.E.;
RT "cDNA expression and human 2D-gel data bases: towards integrating
RT protein and DNA information.";
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
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).
CC -!- FUNCTION: General transcription factor. BTF3 can form a stable
CC complex with RNA polymerase II. Required for the initiation of
CC transcription.
CC -!- INTERACTION:
CC P03372:ESR1; NbExp=5; IntAct=EBI-1054703, EBI-78473;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=BTF3a;
CC IsoId=P20290-1; Sequence=Displayed;
CC Name=2; Synonyms=BTF3b;
CC IsoId=P20290-2; Sequence=VSP_013587;
CC -!- SIMILARITY: Belongs to the NAC-beta family.
CC -!- SIMILARITY: Contains 1 NAC-A/B (NAC-alpha/beta) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X53280; CAA37375.1; -; mRNA.
DR EMBL; X53281; CAA37376.1; -; mRNA.
DR EMBL; M90357; AAA58398.1; -; Genomic_DNA.
DR EMBL; M90352; AAA58398.1; JOINED; Genomic_DNA.
DR EMBL; X74070; CAA52200.1; -; mRNA.
DR EMBL; AB062126; BAB93458.1; -; mRNA.
DR EMBL; BT007120; AAP35784.1; -; mRNA.
DR EMBL; AK291125; BAF83814.1; -; mRNA.
DR EMBL; CH471084; EAW95727.1; -; Genomic_DNA.
DR EMBL; BC008062; AAH08062.1; -; mRNA.
DR PIR; JC1235; JC1235.
DR RefSeq; NP_001032726.1; NM_001037637.1.
DR RefSeq; NP_001198.2; NM_001207.4.
DR UniGene; Hs.591768; -.
DR PDB; 3LKX; X-ray; 2.50 A; A=97-162.
DR PDB; 3MCB; X-ray; 1.90 A; B=97-154.
DR PDBsum; 3LKX; -.
DR PDBsum; 3MCB; -.
DR ProteinModelPortal; P20290; -.
DR SMR; P20290; 97-154.
DR IntAct; P20290; 5.
DR MINT; MINT-5002480; -.
DR STRING; 9606.ENSP00000369965; -.
DR PhosphoSite; P20290; -.
DR DMDM; 115143; -.
DR PaxDb; P20290; -.
DR PRIDE; P20290; -.
DR DNASU; 689; -.
DR Ensembl; ENST00000335895; ENSP00000338516; ENSG00000145741.
DR Ensembl; ENST00000380591; ENSP00000369965; ENSG00000145741.
DR GeneID; 689; -.
DR KEGG; hsa:689; -.
DR UCSC; uc003kcq.1; human.
DR CTD; 689; -.
DR GeneCards; GC05P072794; -.
DR HGNC; HGNC:1125; BTF3.
DR HPA; CAB013007; -.
DR MIM; 602542; gene.
DR neXtProt; NX_P20290; -.
DR PharmGKB; PA25445; -.
DR eggNOG; NOG283773; -.
DR HOGENOM; HOG000261245; -.
DR HOVERGEN; HBG004906; -.
DR InParanoid; P20290; -.
DR KO; K01527; -.
DR OMA; DGKAPIA; -.
DR OrthoDB; EOG7CVPXQ; -.
DR PhylomeDB; P20290; -.
DR ChiTaRS; BTF3; human.
DR EvolutionaryTrace; P20290; -.
DR GeneWiki; BTF3; -.
DR GenomeRNAi; 689; -.
DR NextBio; 2836; -.
DR PRO; PR:P20290; -.
DR ArrayExpress; P20290; -.
DR Bgee; P20290; -.
DR CleanEx; HS_BTF3; -.
DR Genevestigator; P20290; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR Pfam; PF01849; NAC; 1.
DR PROSITE; PS51151; NAC_AB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1 206 Transcription factor BTF3.
FT /FTId=PRO_0000213548.
FT DOMAIN 82 147 NAC-A/B.
FT COMPBIAS 185 188 Poly-Asp.
FT MOD_RES 30 30 Phosphoserine.
FT VAR_SEQ 1 44 Missing (in isoform 2).
FT /FTId=VSP_013587.
FT CONFLICT 41 41 Q -> E (in Ref. 2; AAA58398).
FT CONFLICT 68 105 Missing (in Ref. 2; AAA58398).
FT CONFLICT 192 196 DLVEN -> GG (in Ref. 2).
FT CONFLICT 198 198 D -> Q (in Ref. 2).
FT STRAND 105 110
FT STRAND 113 120
FT STRAND 122 126
FT TURN 127 130
FT STRAND 131 136
FT STRAND 138 142
FT HELIX 143 146
FT HELIX 149 153
FT HELIX 158 161
SQ SEQUENCE 206 AA; 22168 MW; 9653AC480EAF64C6 CRC64;
MRRTGAPAQA DSRGRGRARG GCPGGEATLS QPPPRGGTRG QEPQMKETIM NQEKLAKLQA
QVRIGGKGTA RRKKKVVHRT ATADDKKLQF SLKKLGVNNI SGIEEVNMFT NQGTVIHFNN
PKVQASLAAN TFTITGHAET KQLTEMLPSI LNQLGADSLT SLRRLAEALP KQSVDGKAPL
ATGEDDDDEV PDLVENFDEA SKNEAN
//
MIM
602542
*RECORD*
*FIELD* NO
602542
*FIELD* TI
*602542 BASIC TRANSCRIPTION FACTOR 3; BTF3
;;NASCENT POLYPEPTIDE-ASSOCIATED COMPLEX, BETA POLYPEPTIDE; NACB;;
read moreBETA-NAC
BTF3A, INCLUDED;;
BTF3B, INCLUDED
*FIELD* TX
CLONING
Several transcription factors are involved in the initiation of
transcription from proximal promoter elements such as the TATA box. One
such transcription factor is BTF3. Zheng et al. (1990) cloned the human
BTF3 gene from a HeLa cell cDNA library. They identified 2 distinct
cDNAs, presumed to be alternatively spliced products of a single gene.
The 2 cDNAs, termed BTF3a and BTF3a, encode polypeptides of 206 and 162
amino acids with observed masses of 27 and 22 kD, respectively. BTF3b is
shorter by 44 amino acids at the N terminus. Zheng et al. (1990)
demonstrated that cells transfected with BTF3A, but not BTF3B, express
BTF3-mediated transcriptional activity. They also showed that both BTF3a
and BTF3b form complexes with RNA polymerase IIB (180661).
By Southern blotting, Kanno et al. (1992) found that BTF3 has at least 3
homologous sequences in the human genome, termed BTF3L1 (602543), BTF3L2
(603738), and BTF3L3 (603739).
Wiedmann et al. (1994) purified the heterodimeric nascent
polypeptide-associ ated complex (NAC) from bovine cytosol and determined
that it contains Naca (602542), which migrated at an apparent molecular
mass of about 33 kD, and Btf3b, which migrated at an apparent molecular
mass of about 21 kD. Using peptide sequences from the purified proteins,
they cloned human NACA and BTF3B.
GENE FUNCTION
Wiedmann et al. (1994) determined that NAC bound ubiquitously to nascent
polypeptides emerging from ribosomes unless a signal peptide was fully
exposed. NAC did not bind to fully emerged signal peptides. In the
absence of NAC, the signal recognition particle (SRP; see 604857)
interacted with polypeptides even in the absence of a signal peptide and
allowed mistargeting of the protein to the SRP receptor (see 600867) at
the endoplasmic reticulum membrane. Readdition of purified NAC prevented
mistranslocation.
Bloss et al. (2003) reported that the C. elegans inhibitor of cell
death-1 (ICD1) is necessary and sufficient to prevent apoptosis. Loss of
ICD1 leads to inappropriate apoptosis in developing and differentiated
cells in various tissues. Although this apoptosis requires CED4, it
occurs independently of CED3, the caspase essential for developmental
apoptosis, showing that these core proapoptotic proteins have separable
roles. Overexpression of ICD1 inhibited the apoptosis of cells that are
normally programmed to die. ICD1 is the beta-subunit of the nascent
polypeptide-associated complex (beta-NAC) and contains a putative
caspase cleavage site and caspase recruitment domain. It localizes
primarily to mitochondria, underscoring the role of mitochondria in
coordinating apoptosis. Human beta-NAC is a caspase substrate that is
rapidly eliminated in dying cells (Brockstedt et al., 1999; Thiede et
al., 2001), suggesting that ICD1 apoptosis-suppressing activity may be
inactivated by caspases.
GENE STRUCTURE
Kanno et al. (1992) examined the genomic structure of the BTF3 gene.
They confirmed that BTF3a and BTF3b are the products of alternative
splicing. The gene consists of 7 exons spanning approximately 7 kb of
the genome. Exon 1 is the 3-prime noncoding region; the start codons for
BTF3a and BTF3b are on exons 2 and 3, respectively.
*FIELD* RF
1. Bloss, T. A.; Witze, E. S.; Rothman, J. H.: Suppression of CED-3-independent
apoptosis by mitochondrial beta-NAC in Caenorhabditis elegans. Nature 424:
1066-1071, 2003.
2. Brockstedt, E.; Otto, A.; Rickers, A.; Bommert, K.; Wittmann-Liebold,
B.: Preparative high-resolution two-dimensional electrophoresis enables
the identification of RNA polymerase B transcription factor 3 as an
apoptosis-associated protein in the human BL60-2 Burkitt lymphoma
cell line. J. Protein Chem. 18: 225-231, 1999.
3. Kanno, M.; Chalut, C.; Egly, J.-M.: Genomic structure of the putative
BTF3 transcription factor. Gene 117: 219-228, 1992.
4. Thiede, B.; Dimmler, C.; Siejak, F.; Rudel, T.: Predominant identification
of RNA-binding proteins in Fas-induced apoptosis by proteome analysis. J.
Biol. Chem. 276: 26044-26050, 2001.
5. Wiedmann, B.; Sakai, H.; Davis, T. A.; Wiedmann, M.: A protein
complex required for signal-sequence-specific sorting and translocation. Nature 370:
434-440, 1994.
6. Zheng, X. M.; Black, D.; Chambon, P.; Egly, J. M.: Sequencing
and expression of complementary DNA for the general transcription
factor BTF3. Nature 344: 556-559, 1990.
*FIELD* CN
Patricia A. Hartz - updated: 10/27/2003
Ada Hamosh - updated: 9/15/2003
*FIELD* CD
Jennifer P. Macke: 4/22/1998
*FIELD* ED
mgross: 11/04/2003
terry: 10/27/2003
alopez: 9/15/2003
alopez: 4/16/1999
carol: 6/22/1998
dholmes: 6/16/1998
*RECORD*
*FIELD* NO
602542
*FIELD* TI
*602542 BASIC TRANSCRIPTION FACTOR 3; BTF3
;;NASCENT POLYPEPTIDE-ASSOCIATED COMPLEX, BETA POLYPEPTIDE; NACB;;
read moreBETA-NAC
BTF3A, INCLUDED;;
BTF3B, INCLUDED
*FIELD* TX
CLONING
Several transcription factors are involved in the initiation of
transcription from proximal promoter elements such as the TATA box. One
such transcription factor is BTF3. Zheng et al. (1990) cloned the human
BTF3 gene from a HeLa cell cDNA library. They identified 2 distinct
cDNAs, presumed to be alternatively spliced products of a single gene.
The 2 cDNAs, termed BTF3a and BTF3a, encode polypeptides of 206 and 162
amino acids with observed masses of 27 and 22 kD, respectively. BTF3b is
shorter by 44 amino acids at the N terminus. Zheng et al. (1990)
demonstrated that cells transfected with BTF3A, but not BTF3B, express
BTF3-mediated transcriptional activity. They also showed that both BTF3a
and BTF3b form complexes with RNA polymerase IIB (180661).
By Southern blotting, Kanno et al. (1992) found that BTF3 has at least 3
homologous sequences in the human genome, termed BTF3L1 (602543), BTF3L2
(603738), and BTF3L3 (603739).
Wiedmann et al. (1994) purified the heterodimeric nascent
polypeptide-associ ated complex (NAC) from bovine cytosol and determined
that it contains Naca (602542), which migrated at an apparent molecular
mass of about 33 kD, and Btf3b, which migrated at an apparent molecular
mass of about 21 kD. Using peptide sequences from the purified proteins,
they cloned human NACA and BTF3B.
GENE FUNCTION
Wiedmann et al. (1994) determined that NAC bound ubiquitously to nascent
polypeptides emerging from ribosomes unless a signal peptide was fully
exposed. NAC did not bind to fully emerged signal peptides. In the
absence of NAC, the signal recognition particle (SRP; see 604857)
interacted with polypeptides even in the absence of a signal peptide and
allowed mistargeting of the protein to the SRP receptor (see 600867) at
the endoplasmic reticulum membrane. Readdition of purified NAC prevented
mistranslocation.
Bloss et al. (2003) reported that the C. elegans inhibitor of cell
death-1 (ICD1) is necessary and sufficient to prevent apoptosis. Loss of
ICD1 leads to inappropriate apoptosis in developing and differentiated
cells in various tissues. Although this apoptosis requires CED4, it
occurs independently of CED3, the caspase essential for developmental
apoptosis, showing that these core proapoptotic proteins have separable
roles. Overexpression of ICD1 inhibited the apoptosis of cells that are
normally programmed to die. ICD1 is the beta-subunit of the nascent
polypeptide-associated complex (beta-NAC) and contains a putative
caspase cleavage site and caspase recruitment domain. It localizes
primarily to mitochondria, underscoring the role of mitochondria in
coordinating apoptosis. Human beta-NAC is a caspase substrate that is
rapidly eliminated in dying cells (Brockstedt et al., 1999; Thiede et
al., 2001), suggesting that ICD1 apoptosis-suppressing activity may be
inactivated by caspases.
GENE STRUCTURE
Kanno et al. (1992) examined the genomic structure of the BTF3 gene.
They confirmed that BTF3a and BTF3b are the products of alternative
splicing. The gene consists of 7 exons spanning approximately 7 kb of
the genome. Exon 1 is the 3-prime noncoding region; the start codons for
BTF3a and BTF3b are on exons 2 and 3, respectively.
*FIELD* RF
1. Bloss, T. A.; Witze, E. S.; Rothman, J. H.: Suppression of CED-3-independent
apoptosis by mitochondrial beta-NAC in Caenorhabditis elegans. Nature 424:
1066-1071, 2003.
2. Brockstedt, E.; Otto, A.; Rickers, A.; Bommert, K.; Wittmann-Liebold,
B.: Preparative high-resolution two-dimensional electrophoresis enables
the identification of RNA polymerase B transcription factor 3 as an
apoptosis-associated protein in the human BL60-2 Burkitt lymphoma
cell line. J. Protein Chem. 18: 225-231, 1999.
3. Kanno, M.; Chalut, C.; Egly, J.-M.: Genomic structure of the putative
BTF3 transcription factor. Gene 117: 219-228, 1992.
4. Thiede, B.; Dimmler, C.; Siejak, F.; Rudel, T.: Predominant identification
of RNA-binding proteins in Fas-induced apoptosis by proteome analysis. J.
Biol. Chem. 276: 26044-26050, 2001.
5. Wiedmann, B.; Sakai, H.; Davis, T. A.; Wiedmann, M.: A protein
complex required for signal-sequence-specific sorting and translocation. Nature 370:
434-440, 1994.
6. Zheng, X. M.; Black, D.; Chambon, P.; Egly, J. M.: Sequencing
and expression of complementary DNA for the general transcription
factor BTF3. Nature 344: 556-559, 1990.
*FIELD* CN
Patricia A. Hartz - updated: 10/27/2003
Ada Hamosh - updated: 9/15/2003
*FIELD* CD
Jennifer P. Macke: 4/22/1998
*FIELD* ED
mgross: 11/04/2003
terry: 10/27/2003
alopez: 9/15/2003
alopez: 4/16/1999
carol: 6/22/1998
dholmes: 6/16/1998