BTF3_HUMAN
ID BTF3_HUMAN Reviewed; 206 AA.
AC P20290; A8K510; Q13893; Q76M56;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Transcription factor BTF3;
DE AltName: Full=Nascent polypeptide-associated complex subunit beta;
DE Short=NAC-beta;
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Celis J.E.;
RT "cDNA expression and human 2D-gel data bases: towards integrating protein
RT 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-reactive
RT 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 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, INTERACTION WITH NACA, ASSOCIATION WITH RIBOSOMES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10982809; DOI=10.1074/jbc.m006368200;
RA Beatrix B., Sakai H., Wiedmann M.;
RT "The alpha and beta subunit of the nascent polypeptide-associated complex
RT have distinct functions.";
RL J. Biol. Chem. 275:37838-37845(2000).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA 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 [11]
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., Buerckstuemmer T.,
RA 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-173, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-160, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-19; LYS-46 AND LYS-54, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 97-154, AND SUBUNIT.
RX PubMed=21203952; DOI=10.1007/s13238-010-0049-3;
RA Wang L., Zhang W., Wang L., Zhang X.C., Li X., Rao Z.;
RT "Crystal structures of NAC domains of human nascent polypeptide-associated
RT complex (NAC) and its alphaNAC subunit.";
RL Protein Cell 1:406-416(2010).
CC -!- FUNCTION: When associated with NACA, prevents inappropriate targeting
CC of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds
CC to nascent polypeptide chains as they emerge from the ribosome and
CC blocks their interaction with the signal recognition particle (SRP),
CC which normally targets nascent secretory peptides to the ER. BTF3 is
CC also a general transcription factor that can form a stable complex with
CC RNA polymerase II. Required for the initiation of transcription.
CC {ECO:0000269|PubMed:10982809}.
CC -!- SUBUNIT: Part of the nascent polypeptide-associated complex (NAC),
CC which is a heterodimer of NACA and BTF3 (via NAC-A/B domains). NAC
CC associates with ribosomes through the BTF3/NACB subunit. Both subunits
CC can contact nascent polypeptide chains. {ECO:0000269|PubMed:21203952}.
CC -!- INTERACTION:
CC P20290; Q86VG3: IFTAP; NbExp=4; IntAct=EBI-1054687, EBI-3923037;
CC P20290; P40222: TXLNA; NbExp=3; IntAct=EBI-1054687, EBI-359793;
CC P20290; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-1054687, EBI-6116822;
CC P20290-2; P03372: ESR1; NbExp=5; IntAct=EBI-1054703, EBI-78473;
CC P20290-2; Q86UY6: NAA40; NbExp=3; IntAct=EBI-1054703, EBI-16356946;
CC P20290-2; O60551: NMT2; NbExp=3; IntAct=EBI-1054703, EBI-3920273;
CC P20290-2; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-1054703, EBI-17490746;
CC P20290-2; Q9NRG4: SMYD2; NbExp=3; IntAct=EBI-1054703, EBI-1055671;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10982809}. Nucleus
CC {ECO:0000269|PubMed:10982809}. Note=The heterodimer with NACA is
CC cytoplasmic.
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. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) 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 CCDS; CCDS34185.1; -. [P20290-1]
DR CCDS; CCDS4019.1; -. [P20290-2]
DR PIR; JC1235; JC1235.
DR RefSeq; NP_001032726.1; NM_001037637.1. [P20290-1]
DR RefSeq; NP_001198.2; NM_001207.4. [P20290-2]
DR PDB; 3LKX; X-ray; 2.50 A; A=97-162.
DR PDB; 3MCB; X-ray; 1.90 A; B=97-154.
DR PDB; 7QWQ; EM; 2.83 A; u=45-206.
DR PDB; 7QWR; EM; 2.90 A; u=45-206.
DR PDBsum; 3LKX; -.
DR PDBsum; 3MCB; -.
DR PDBsum; 7QWQ; -.
DR PDBsum; 7QWR; -.
DR AlphaFoldDB; P20290; -.
DR SMR; P20290; -.
DR BioGRID; 107154; 766.
DR ComplexPortal; CPX-676; Nascent polypeptide-associated complex.
DR IntAct; P20290; 46.
DR MINT; P20290; -.
DR STRING; 9606.ENSP00000369965; -.
DR GlyGen; P20290; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P20290; -.
DR MetOSite; P20290; -.
DR PhosphoSitePlus; P20290; -.
DR SwissPalm; P20290; -.
DR BioMuta; BTF3; -.
DR DMDM; 115143; -.
DR EPD; P20290; -.
DR jPOST; P20290; -.
DR MassIVE; P20290; -.
DR MaxQB; P20290; -.
DR PaxDb; P20290; -.
DR PeptideAtlas; P20290; -.
DR PRIDE; P20290; -.
DR ProteomicsDB; 53742; -. [P20290-1]
DR ProteomicsDB; 53743; -. [P20290-2]
DR TopDownProteomics; P20290-1; -. [P20290-1]
DR TopDownProteomics; P20290-2; -. [P20290-2]
DR Antibodypedia; 4573; 211 antibodies from 29 providers.
DR DNASU; 689; -.
DR Ensembl; ENST00000335895.12; ENSP00000338516.8; ENSG00000145741.17. [P20290-2]
DR Ensembl; ENST00000380591.8; ENSP00000369965.3; ENSG00000145741.17. [P20290-1]
DR GeneID; 689; -.
DR KEGG; hsa:689; -.
DR MANE-Select; ENST00000380591.8; ENSP00000369965.3; NM_001037637.2; NP_001032726.1.
DR UCSC; uc003kcq.2; human. [P20290-1]
DR CTD; 689; -.
DR DisGeNET; 689; -.
DR GeneCards; BTF3; -.
DR HGNC; HGNC:1125; BTF3.
DR HPA; ENSG00000145741; Low tissue specificity.
DR MIM; 602542; gene.
DR neXtProt; NX_P20290; -.
DR OpenTargets; ENSG00000145741; -.
DR PharmGKB; PA25445; -.
DR VEuPathDB; HostDB:ENSG00000145741; -.
DR eggNOG; KOG2240; Eukaryota.
DR GeneTree; ENSGT00940000153288; -.
DR HOGENOM; CLU_098726_3_0_1; -.
DR InParanoid; P20290; -.
DR OMA; KVHKNSM; -.
DR OrthoDB; 1435264at2759; -.
DR PhylomeDB; P20290; -.
DR TreeFam; TF317546; -.
DR PathwayCommons; P20290; -.
DR SignaLink; P20290; -.
DR SIGNOR; P20290; -.
DR BioGRID-ORCS; 689; 272 hits in 1063 CRISPR screens.
DR ChiTaRS; BTF3; human.
DR EvolutionaryTrace; P20290; -.
DR GeneWiki; BTF3; -.
DR GenomeRNAi; 689; -.
DR Pharos; P20290; Tbio.
DR PRO; PR:P20290; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P20290; protein.
DR Bgee; ENSG00000145741; Expressed in mucosa of sigmoid colon and 209 other tissues.
DR ExpressionAtlas; P20290; baseline and differential.
DR Genevisible; P20290; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005854; C:nascent polypeptide-associated complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:1905551; P:negative regulation of protein localization to endoplasmic reticulum; IDA:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.20.70.30; -; 1.
DR IDEAL; IID00444; -.
DR InterPro; IPR039370; BTF3.
DR InterPro; IPR038187; NAC_A/B_dom_sf.
DR InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR PANTHER; PTHR10351; PTHR10351; 1.
DR Pfam; PF01849; NAC; 1.
DR SMART; SM01407; NAC; 1.
DR PROSITE; PS51151; NAC_AB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chaperone; Cytoplasm; Methylation;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW Transcription; Transcription regulation; Transport.
FT CHAIN 1..206
FT /note="Transcription factor BTF3"
FT /id="PRO_0000213548"
FT DOMAIN 82..147
FT /note="NAC-A/B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 46
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 54
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 160
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..44
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:2320128,
FT ECO:0000303|Ref.3, ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT /id="VSP_013587"
FT CONFLICT 41
FT /note="Q -> E (in Ref. 2; AAA58398)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..105
FT /note="Missing (in Ref. 2; AAA58398)"
FT /evidence="ECO:0000305"
FT CONFLICT 192..196
FT /note="DLVEN -> GG (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="D -> Q (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3MCB"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:3MCB"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:3MCB"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:3MCB"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:3MCB"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:3MCB"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:3MCB"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:3MCB"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:3LKX"
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
