GABP1_HUMAN
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 03-AUG-2022, entry version 212.
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; 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 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}.
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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 SMR; Q06547; -.
DR BioGRID; 108827; 41.
DR DIP; DIP-33979N; -.
DR IntAct; Q06547; 69.
DR MINT; Q06547; -.
DR STRING; 9606.ENSP00000220429; -.
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; Q06547; -.
DR PeptideAtlas; Q06547; -.
DR PRIDE; Q06547; -.
DR ProteomicsDB; 58458; -. [Q06547-1]
DR ProteomicsDB; 58459; -. [Q06547-2]
DR ProteomicsDB; 58460; -. [Q06547-3]
DR ProteomicsDB; 58461; -. [Q06547-4]
DR Antibodypedia; 1425; 340 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 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; 1514706at2759; -.
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; 350 hits in 1091 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 tissues.
DR ExpressionAtlas; Q06547; baseline and differential.
DR Genevisible; Q06547; HS.
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; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
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 A-
FT 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
