ID GABP1_HUMAN Reviewed; 395 AA. AC Q06547; A8IE52; Q06545; Q12940; Q12941; Q12942; Q8IYD0; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2002, sequence version 2. DT 27-MAR-2024, entry version 220. DE RecName: Full=GA-binding protein subunit beta-1; DE Short=GABP subunit beta-1; DE Short=GABPB-1; DE AltName: Full=GABP subunit beta-2; DE Short=GABPB-2; DE AltName: Full=Nuclear respiratory factor 2; DE AltName: Full=Transcription factor E4TF1-47 {ECO:0000303|PubMed:8441384}; DE AltName: Full=Transcription factor E4TF1-53 {ECO:0000303|PubMed:8441384}; GN Name=GABPB1; GN Synonyms=E4TF1B {ECO:0000303|PubMed:8441384}, GABPB, GABPB2; 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 2), FUNCTION, FUNCTION (MICROBIAL RP INFECTION), AND SUBCELLULAR LOCATION. RX PubMed=8441384; DOI=10.1128/mcb.13.3.1385-1391.1993; RA Watanabe H., Sawada J., Yano K., Yamaguchi K., Goto M., Handa H.; RT "cDNA cloning of transcription factor E4TF1 subunits with Ets and notch RT motifs."; RL Mol. Cell. Biol. 13:1385-1391(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), SUBUNIT, AND RP SUBCELLULAR LOCATION. RC TISSUE=Testis; RX PubMed=7799916; DOI=10.1128/mcb.15.1.102; RA Gugneja S., Virbasius J.V., Scarpulla R.C.; RT "Four structurally distinct, non-DNA-binding subunits of human nuclear RT respiratory factor 2 share a conserved transcriptional activation domain."; RL Mol. Cell. Biol. 15:102-111(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Hepatoma; RA Yang S.J., Li K.N., Zhang Y.Q.; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Prostate, Testis, and Uterus; 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 [7] RP PROTEIN SEQUENCE OF 74-81. RX PubMed=7918435; DOI=10.1021/bi00206a017; RA Cardot P., Pastier D., Lacorte J.-M., Mangeney M., Zannis V.I., Chambaz J.; RT "Purification and characterization of nuclear factors binding to the RT negative regulatory element D of human apolipoprotein A-II promoter: a RT negative regulatory effect is reversed by GABP, an Ets-related protein."; RL Biochemistry 33:12139-12148(1994). RN [8] RP PROTEIN SEQUENCE OF 105-125 AND 339-385. RX PubMed=8383622; DOI=10.1101/gad.7.3.380; RA Virbasius J.V., Virbasius C.A., Scarpulla R.C.; RT "Identity of GABP with NRF-2, a multisubunit activator of cytochrome RT oxidase expression, reveals a cellular role for an ETS domain activator of RT viral promoters."; RL Genes Dev. 7:380-392(1993). RN [9] RP FUNCTION, AND MUTAGENESIS OF 262-GLN-GLN-263; 264-VAL-VAL-265; RP 270-GLN-GLN-271; 273-ILE--ILE-275; GLN-295; 297-ILE--VAL-299; RP 305-GLN-GLN-306 AND 307-VAL--VAL-310. RX PubMed=8816484; DOI=10.1128/mcb.16.10.5708; RA Gugneja S., Virbasius C.M., Scarpulla R.C.; RT "Nuclear respiratory factors 1 and 2 utilize similar glutamine-containing RT clusters of hydrophobic residues to activate transcription."; RL Mol. Cell. Biol. 16:5708-5716(1996). RN [10] RP FUNCTION, INTERACTION WITH HCFC1, AND MUTAGENESIS OF 264-VAL-VAL-265; RP 273-ILE--ILE-275; 297-ILE--VAL-299 AND 307-VAL--VAL-310. RX PubMed=10675337; DOI=10.1093/emboj/19.4.683; RA Vogel J.L., Kristie T.M.; RT "The novel coactivator C1 (HCF) coordinates multiprotein enhancer formation RT and mediates transcription activation by GABP."; RL EMBO J. 19:683-690(2000). 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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. 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., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [13] RP VARIANT [LARGE SCALE ANALYSIS] ALA-31. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Transcription factor capable of interacting with purine rich CC repeats (GA repeats) (PubMed:8441384, PubMed:10675337, PubMed:8816484). CC Acts as a master regulator of nuclear-encoded mitochondrial genes (By CC similarity). {ECO:0000250|UniProtKB:Q00420, CC ECO:0000269|PubMed:10675337, ECO:0000269|PubMed:8441384, CC ECO:0000269|PubMed:8816484}. CC -!- FUNCTION: (Microbial infection) Necessary for the expression of the CC Adenovirus E4 gene. {ECO:0000269|PubMed:8441384}. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits CC (PubMed:7799916). Interacts with HCFC1, causing repression of CC transcriptional activity (PubMed:10675337). CC {ECO:0000269|PubMed:10675337, ECO:0000269|PubMed:7799916}. CC -!- INTERACTION: CC Q06547; O95994: AGR2; NbExp=3; IntAct=EBI-618165, EBI-712648; CC Q06547; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-618165, EBI-6658203; CC Q06547; Q06546: GABPA; NbExp=3; IntAct=EBI-618165, EBI-638925; CC Q06547; P51610: HCFC1; NbExp=3; IntAct=EBI-618165, EBI-396176; CC Q06547; Q14005-2: IL16; NbExp=3; IntAct=EBI-618165, EBI-17178971; CC Q06547; P25800: LMO1; NbExp=4; IntAct=EBI-618165, EBI-8639312; CC Q06547; P61968: LMO4; NbExp=6; IntAct=EBI-618165, EBI-2798728; CC Q06547; Q96M61: MAGEB18; NbExp=3; IntAct=EBI-618165, EBI-741835; CC Q06547; Q9H944: MED20; NbExp=3; IntAct=EBI-618165, EBI-394644; CC Q06547; Q7Z3K3: POGZ; NbExp=5; IntAct=EBI-618165, EBI-1389308; CC Q06547; P57052: RBM11; NbExp=3; IntAct=EBI-618165, EBI-741332; CC Q06547; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-618165, EBI-748350; CC Q06547; P09012: SNRPA; NbExp=3; IntAct=EBI-618165, EBI-607085; CC Q06547; P08579: SNRPB2; NbExp=3; IntAct=EBI-618165, EBI-1053651; CC Q06547; Q13573: SNW1; NbExp=3; IntAct=EBI-618165, EBI-632715; CC Q06547; Q8NHU6: TDRD7; NbExp=4; IntAct=EBI-618165, EBI-624505; CC Q06547; Q12933: TRAF2; NbExp=7; IntAct=EBI-618165, EBI-355744; CC Q06547; Q8CGM1: Adgrb2; Xeno; NbExp=3; IntAct=EBI-618165, EBI-8014984; CC Q06547-2; P54253: ATXN1; NbExp=6; IntAct=EBI-618189, EBI-930964; CC Q06547-2; P02489: CRYAA; NbExp=3; IntAct=EBI-618189, EBI-6875961; CC Q06547-2; P25685: DNAJB1; NbExp=3; IntAct=EBI-618189, EBI-357034; CC Q06547-2; P41091: EIF2S3; NbExp=3; IntAct=EBI-618189, EBI-1054228; CC Q06547-2; O75460-2: ERN1; NbExp=3; IntAct=EBI-618189, EBI-25852368; CC Q06547-2; P22607: FGFR3; NbExp=3; IntAct=EBI-618189, EBI-348399; CC Q06547-2; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-618189, EBI-10226858; CC Q06547-2; O14908-2: GIPC1; NbExp=3; IntAct=EBI-618189, EBI-25913156; CC Q06547-2; Q14957: GRIN2C; NbExp=3; IntAct=EBI-618189, EBI-8285963; CC Q06547-2; P51610: HCFC1; NbExp=6; IntAct=EBI-618189, EBI-396176; CC Q06547-2; P54652: HSPA2; NbExp=3; IntAct=EBI-618189, EBI-356991; CC Q06547-2; Q92993: KAT5; NbExp=3; IntAct=EBI-618189, EBI-399080; CC Q06547-2; O14901: KLF11; NbExp=3; IntAct=EBI-618189, EBI-948266; CC Q06547-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-618189, EBI-11742507; CC Q06547-2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-618189, EBI-2811583; CC Q06547-2; Q96HC4-3: PDLIM5; NbExp=3; IntAct=EBI-618189, EBI-25913059; CC Q06547-2; Q16512: PKN1; NbExp=3; IntAct=EBI-618189, EBI-602382; CC Q06547-2; P62937-2: PPIA; NbExp=3; IntAct=EBI-618189, EBI-25884072; CC Q06547-2; P23284: PPIB; NbExp=3; IntAct=EBI-618189, EBI-359252; CC Q06547-2; P63000: RAC1; NbExp=3; IntAct=EBI-618189, EBI-413628; CC Q06547-2; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-618189, EBI-9090795; CC Q06547-2; Q13148: TARDBP; NbExp=6; IntAct=EBI-618189, EBI-372899; CC Q06547-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-618189, EBI-741480; CC Q06547-2; P31930: UQCRC1; NbExp=3; IntAct=EBI-618189, EBI-1052596; CC Q06547-2; P61758: VBP1; NbExp=3; IntAct=EBI-618189, EBI-357430; CC Q06547-2; P61981: YWHAG; NbExp=3; IntAct=EBI-618189, EBI-359832; CC Q06547-2; Q9Y649; NbExp=3; IntAct=EBI-618189, EBI-25900580; CC Q06547-3; P55212: CASP6; NbExp=3; IntAct=EBI-9088619, EBI-718729; CC Q06547-3; P06307: CCK; NbExp=3; IntAct=EBI-9088619, EBI-6624398; CC Q06547-3; P28329-3: CHAT; NbExp=3; IntAct=EBI-9088619, EBI-25837549; CC Q06547-3; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-9088619, EBI-21553822; CC Q06547-3; P25685: DNAJB1; NbExp=3; IntAct=EBI-9088619, EBI-357034; CC Q06547-3; O14645: DNALI1; NbExp=3; IntAct=EBI-9088619, EBI-395638; CC Q06547-3; P41091: EIF2S3; NbExp=3; IntAct=EBI-9088619, EBI-1054228; CC Q06547-3; O75460-2: ERN1; NbExp=3; IntAct=EBI-9088619, EBI-25852368; CC Q06547-3; P22607: FGFR3; NbExp=3; IntAct=EBI-9088619, EBI-348399; CC Q06547-3; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-9088619, EBI-10226858; CC Q06547-3; P06396: GSN; NbExp=3; IntAct=EBI-9088619, EBI-351506; CC Q06547-3; O00291: HIP1; NbExp=3; IntAct=EBI-9088619, EBI-473886; CC Q06547-3; P54652: HSPA2; NbExp=3; IntAct=EBI-9088619, EBI-356991; CC Q06547-3; Q92993: KAT5; NbExp=3; IntAct=EBI-9088619, EBI-399080; CC Q06547-3; O14901: KLF11; NbExp=3; IntAct=EBI-9088619, EBI-948266; CC Q06547-3; P13473-2: LAMP2; NbExp=3; IntAct=EBI-9088619, EBI-21591415; CC Q06547-3; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-9088619, EBI-11742507; CC Q06547-3; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-9088619, EBI-2811583; CC Q06547-3; Q96HC4-3: PDLIM5; NbExp=3; IntAct=EBI-9088619, EBI-25913059; CC Q06547-3; P62937-2: PPIA; NbExp=3; IntAct=EBI-9088619, EBI-25884072; CC Q06547-3; P17252: PRKCA; NbExp=3; IntAct=EBI-9088619, EBI-1383528; CC Q06547-3; P62826: RAN; NbExp=3; IntAct=EBI-9088619, EBI-286642; CC Q06547-3; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-9088619, EBI-9090795; CC Q06547-3; P62308: SNRPG; NbExp=3; IntAct=EBI-9088619, EBI-624585; CC Q06547-3; P31948: STIP1; NbExp=3; IntAct=EBI-9088619, EBI-1054052; CC Q06547-3; P61981: YWHAG; NbExp=3; IntAct=EBI-9088619, EBI-359832; CC Q06547-3; Q9Y649; NbExp=3; IntAct=EBI-9088619, EBI-25900580; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:7799916, CC ECO:0000305|PubMed:8441384}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=GABPB-1, Beta-1 {ECO:0000303|PubMed:7799916}; CC IsoId=Q06547-1; Sequence=Displayed; CC Name=2; Synonyms=Beta-2 {ECO:0000303|PubMed:7799916}; CC IsoId=Q06547-2; Sequence=VSP_000275; CC Name=3; Synonyms=GABPB-2, Gamma-1 {ECO:0000303|PubMed:7799916}; CC IsoId=Q06547-3; Sequence=VSP_009337; CC Name=4; Synonyms=Gamma-2 {ECO:0000303|PubMed:7799916}; CC IsoId=Q06547-4; Sequence=VSP_000275, VSP_009337; CC -!- PTM: Acetylated by EP300/p300. Deacetylated by SIRT7, promoting CC heterotetramerization and activity. {ECO:0000250|UniProtKB:Q00420}. 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; D13316; BAA02573.1; -; mRNA. DR EMBL; D13317; BAA02574.1; -; mRNA. DR EMBL; U13045; AAA65707.1; -; mRNA. DR EMBL; U13046; AAA65708.1; -; mRNA. DR EMBL; U13047; AAA65709.1; -; mRNA. DR EMBL; U13048; AAA65710.1; -; mRNA. DR EMBL; EU159454; ABV90874.1; -; mRNA. DR EMBL; BT006652; AAP35298.1; -; mRNA. DR EMBL; CH471082; EAW77395.1; -; Genomic_DNA. DR EMBL; BC016910; AAH16910.1; -; mRNA. DR EMBL; BC036080; AAH36080.1; -; mRNA. DR EMBL; BC050702; AAH50702.1; -; mRNA. DR CCDS; CCDS10135.1; -. [Q06547-2] DR CCDS; CCDS10136.1; -. [Q06547-4] DR CCDS; CCDS32239.1; -. [Q06547-1] DR CCDS; CCDS45258.1; -. [Q06547-3] DR PIR; C48146; C48146. DR PIR; I38741; I38741. DR PIR; I38743; I38743. DR PIR; I38744; I38744. DR RefSeq; NP_001307839.1; NM_001320910.1. [Q06547-1] DR RefSeq; NP_002032.2; NM_002041.4. [Q06547-3] DR RefSeq; NP_005245.2; NM_005254.5. [Q06547-1] DR RefSeq; NP_057738.1; NM_016654.4. [Q06547-2] DR RefSeq; NP_057739.1; NM_016655.4. [Q06547-4] DR RefSeq; NP_852092.1; NM_181427.3. [Q06547-4] DR RefSeq; XP_005254331.1; XM_005254274.3. [Q06547-1] DR RefSeq; XP_016877542.1; XM_017022053.1. [Q06547-2] DR AlphaFoldDB; Q06547; -. DR EMDB; EMD-27750; -. DR SMR; Q06547; -. DR BioGRID; 108827; 44. DR DIP; DIP-33979N; -. DR IntAct; Q06547; 69. DR MINT; Q06547; -. DR STRING; 9606.ENSP00000220429; -. DR GlyCosmos; Q06547; 3 sites, 2 glycans. DR GlyGen; Q06547; 3 sites, 2 O-linked glycans (3 sites). DR iPTMnet; Q06547; -. DR PhosphoSitePlus; Q06547; -. DR BioMuta; GABPB1; -. DR DMDM; 23503070; -. DR EPD; Q06547; -. DR jPOST; Q06547; -. DR MassIVE; Q06547; -. DR MaxQB; Q06547; -. DR PaxDb; 9606-ENSP00000220429; -. DR PeptideAtlas; Q06547; -. DR ProteomicsDB; 58458; -. [Q06547-1] DR ProteomicsDB; 58459; -. [Q06547-2] DR ProteomicsDB; 58460; -. [Q06547-3] DR ProteomicsDB; 58461; -. [Q06547-4] DR Pumba; Q06547; -. DR Antibodypedia; 1425; 389 antibodies from 34 providers. DR DNASU; 2553; -. DR Ensembl; ENST00000220429.12; ENSP00000220429.8; ENSG00000104064.18. [Q06547-1] DR Ensembl; ENST00000359031.8; ENSP00000351923.4; ENSG00000104064.18. [Q06547-4] DR Ensembl; ENST00000380877.8; ENSP00000370259.3; ENSG00000104064.18. [Q06547-2] DR Ensembl; ENST00000396464.7; ENSP00000379728.3; ENSG00000104064.18. [Q06547-4] DR Ensembl; ENST00000429662.6; ENSP00000395771.2; ENSG00000104064.18. [Q06547-3] DR GeneID; 2553; -. DR KEGG; hsa:2553; -. DR MANE-Select; ENST00000380877.8; ENSP00000370259.3; NM_016654.5; NP_057738.1. [Q06547-2] DR UCSC; uc001zya.4; human. [Q06547-1] DR AGR; HGNC:4074; -. DR CTD; 2553; -. DR DisGeNET; 2553; -. DR GeneCards; GABPB1; -. DR HGNC; HGNC:4074; GABPB1. DR HPA; ENSG00000104064; Low tissue specificity. DR MIM; 600610; gene. DR neXtProt; NX_Q06547; -. DR OpenTargets; ENSG00000104064; -. DR PharmGKB; PA162389163; -. DR VEuPathDB; HostDB:ENSG00000104064; -. DR eggNOG; ENOG502QRTX; Eukaryota. DR GeneTree; ENSGT00940000157875; -. DR HOGENOM; CLU_000134_12_0_1; -. DR InParanoid; Q06547; -. DR OMA; ACRQKLE; -. DR OrthoDB; 2918558at2759; -. DR PhylomeDB; Q06547; -. DR TreeFam; TF326036; -. DR PathwayCommons; Q06547; -. DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis. DR SignaLink; Q06547; -. DR SIGNOR; Q06547; -. DR BioGRID-ORCS; 2553; 365 hits in 1170 CRISPR screens. DR ChiTaRS; GABPB1; human. DR GeneWiki; GABPB2; -. DR GenomeRNAi; 2553; -. DR Pharos; Q06547; Tbio. DR PRO; PR:Q06547; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q06547; Protein. DR Bgee; ENSG00000104064; Expressed in secondary oocyte and 181 other cell types or tissues. DR ExpressionAtlas; Q06547; baseline and differential. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI. DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR PANTHER; PTHR24193; ANKYRIN REPEAT PROTEIN; 1. DR PANTHER; PTHR24193:SF76; GA-BINDING PROTEIN SUBUNIT BETA-1; 1. DR Pfam; PF12796; Ank_2; 1. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 4. DR SUPFAM; SSF48403; Ankyrin repeat; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 3. DR Genevisible; Q06547; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; ANK repeat; Direct protein sequencing; KW Nucleus; Reference proteome; Repeat; Transcription; KW Transcription regulation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..395 FT /note="GA-binding protein subunit beta-1" FT /id="PRO_0000066993" FT REPEAT 5..34 FT /note="ANK 1" FT REPEAT 37..66 FT /note="ANK 2" FT REPEAT 70..99 FT /note="ANK 3" FT REPEAT 103..132 FT /note="ANK 4" FT REPEAT 136..166 FT /note="ANK 5" FT REGION 258..327 FT /note="Transcription activation and HCFC1 interaction" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 69 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q00420" FT MOD_RES 352 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q00420" FT MOD_RES 381 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q00420" FT VAR_SEQ 195..206 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7799916, ECO:0000303|PubMed:8441384" FT /id="VSP_000275" FT VAR_SEQ 346..395 FT /note="EREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMTRLQTNKEAV FT -> VRSLLPGVLCRSHPK (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7799916, ECO:0000303|Ref.4" FT /id="VSP_009337" FT VARIANT 31 FT /note="P -> A (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035613" FT MUTAGEN 262..263 FT /note="QQ->AA: Minor reduction in transcriptional FT activation; when associated with A-295 or A-305 and A-306." FT /evidence="ECO:0000269|PubMed:8816484" FT MUTAGEN 264..265 FT /note="VV->AA: Minor effect upon interaction with HCFC1 and FT transcriptional activation. Loss of activity; when FT associated with A-297; A-298 and A-299, or with A-307 and FT A-310." FT /evidence="ECO:0000269|PubMed:10675337, FT ECO:0000269|PubMed:8816484" FT MUTAGEN 270..271 FT /note="QQ->AA: Minor reduction in transcriptional FT activation. Moderate reduction in activity; when associated FT with A-305 and A-306." FT /evidence="ECO:0000269|PubMed:8816484" FT MUTAGEN 273..275 FT /note="ITI->ATA: Strongly reduces interaction with HCFC1 FT and transcriptional activation. Loss of activity; when FT associated with A-297; A-298 and A-299, or with A-307 and FT A-310." FT /evidence="ECO:0000269|PubMed:10675337, FT ECO:0000269|PubMed:8816484" FT MUTAGEN 295 FT /note="Q->A: No effect on transcriptional activation. Minor FT reduction in activity; when associated with A-270 and FT A-271." FT /evidence="ECO:0000269|PubMed:8816484" FT MUTAGEN 297..299 FT /note="IIV->AAA: Strongly reduces interaction with HCFC1 FT and transcriptional activation. Loss of activity; when FT associated with A-264 and A-265, or A-273 and A-275." FT /evidence="ECO:0000269|PubMed:10675337, FT ECO:0000269|PubMed:8816484" FT MUTAGEN 305..306 FT /note="QQ->AA: Minor reduction in transcriptional FT activation. Moderate reduction in activity; when associated FT with A-270 and A-271." FT /evidence="ECO:0000269|PubMed:8816484" FT MUTAGEN 307..310 FT /note="VLTV->ALTA: Moderately reduces interaction with FT HCFC1 and transcriptional activation. Loss of activity; FT when associated with A-273 and A-275." FT /evidence="ECO:0000269|PubMed:10675337, FT ECO:0000269|PubMed:8816484" FT CONFLICT 76 FT /note="H -> L (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 246 FT /note="Missing (in Ref. 1; BAA02573)" FT /evidence="ECO:0000305" FT CONFLICT 274 FT /note="T -> A (in Ref. 6; AAH36080)" FT /evidence="ECO:0000305" FT CONFLICT 341 FT /note="S -> C (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 395 AA; 42483 MW; 723D63962FB29BD9 CRC64; MSLVDLGKKL LEAARAGQDD EVRILMANGA PFTTDWLGTS PLHLAAQYGH YSTTEVLLRA GVSRDARTKV DRTPLHMAAS EGHASIVEVL LKHGADVNAK DMLKMTALHW ATEHNHQEVV ELLIKYGADV HTQSKFCKTA FDISIDNGNE DLAEILQIAM QNQINTNPES PDTVTIHAAT PQFIIGPGGV VNLTGLVSSE NSSKATDETG VSAVQFGNSS TSVLATLAAL AEASAPLSNS SETPVVATEE VVTAESVDGA IQQVVSSGGQ QVITIVTDGI QLGNLHSIPT SGIGQPIIVT MPDGQQVLTV PATDIAEETV ISEEPPAKRQ CIEIIENRVE SAEIEEREAL QKQLDEANRE AQKYRQQLLK KEQEAEAYRQ KLEAMTRLQT NKEAV //