GABP1_MOUSE
ID GABP1_MOUSE Reviewed; 383 AA.
AC Q00420; A2AQ68; A2AQ70; Q00421; Q8BS31; Q91YZ0; Q9QVV2;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 203.
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;
GN Name=Gabpb1; Synonyms=Gabpb, Gabpb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RX PubMed=1876836; DOI=10.1126/science.1876836;
RA Lamarco K., Thompson C.C., Byers B.P., Walton E.M., McKnight S.L.;
RT "Identification of Ets- and notch-related subunits in GA binding protein.";
RL Science 253:789-792(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Aorta, Mammary gland, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 5-157.
RX PubMed=9461436; DOI=10.1126/science.279.5353.1037;
RA Batchelor A.H., Piper D.E., de la Brousse F.C., McKnight S.L.,
RA Wolberger C.;
RT "The structure of GABPalpha/beta: an ETS domain-ankyrin repeat heterodimer
RT bound to DNA.";
RL Science 279:1037-1041(1998).
RN [6]
RP FUNCTION, SUBUNIT, ACETYLATION AT LYS-69; LYS-340 AND LYS-369, AND
RP MUTAGENESIS OF LYS-69; LYS-340 AND LYS-369.
RX PubMed=25200183; DOI=10.1016/j.cmet.2014.08.001;
RA Ryu D., Jo Y.S., Lo Sasso G., Stein S., Zhang H., Perino A., Lee J.U.,
RA Zeviani M., Romand R., Hottiger M.O., Schoonjans K., Auwerx J.;
RT "A SIRT7-dependent acetylation switch of GABPbeta1 controls mitochondrial
RT function.";
RL Cell Metab. 20:856-869(2014).
CC -!- FUNCTION: Transcription factor capable of interacting with purine rich
CC repeats (GA repeats) (PubMed:25200183). Acts as a a master regulator of
CC nuclear-encoded mitochondrial genes (PubMed:25200183).
CC {ECO:0000269|PubMed:25200183}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits
CC (PubMed:25200183). Interacts with HCFC1, causing repression of
CC transcriptional activity (By similarity).
CC {ECO:0000250|UniProtKB:Q06547, ECO:0000269|PubMed:25200183}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06547}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q00420-1; Sequence=Displayed;
CC Name=2; Synonyms=GABP-beta-2 subunit, GABBP2;
CC IsoId=Q00420-2; Sequence=VSP_009336;
CC Name=3; Synonyms=GABP-beta-1;
CC IsoId=Q00420-3; Sequence=VSP_009333;
CC Name=4;
CC IsoId=Q00420-4; Sequence=VSP_009334, VSP_009335;
CC -!- PTM: Acetylated by EP300/p300 (PubMed:25200183). Deacetylated by SIRT7,
CC promoting heterotetramerization and activity (PubMed:25200183).
CC {ECO:0000269|PubMed:25200183}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to competing acceptor splice
CC sites. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to an intron retention.
CC {ECO:0000305}.
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DR EMBL; M74516; AAA53031.1; -; mRNA.
DR EMBL; M74517; AAA53032.1; -; mRNA.
DR EMBL; AK040722; BAC30682.1; -; mRNA.
DR EMBL; AK052828; BAC35165.1; -; mRNA.
DR EMBL; AL844555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013558; AAH13558.1; -; mRNA.
DR CCDS; CCDS16685.1; -. [Q00420-3]
DR CCDS; CCDS16686.1; -. [Q00420-2]
DR CCDS; CCDS71135.1; -. [Q00420-4]
DR CCDS; CCDS71137.1; -. [Q00420-1]
DR PIR; B40858; B40858.
DR PIR; C40858; C40858.
DR RefSeq; NP_001258396.1; NM_001271467.1. [Q00420-3]
DR RefSeq; NP_001258397.1; NM_001271468.1. [Q00420-1]
DR RefSeq; NP_001258421.1; NM_001271492.1. [Q00420-4]
DR RefSeq; NP_034379.1; NM_010249.2. [Q00420-2]
DR RefSeq; NP_997552.1; NM_207669.2. [Q00420-3]
DR RefSeq; XP_006498820.1; XM_006498757.3. [Q00420-1]
DR RefSeq; XP_006498821.1; XM_006498758.3.
DR RefSeq; XP_006498822.1; XM_006498759.3. [Q00420-1]
DR RefSeq; XP_006498823.1; XM_006498760.3. [Q00420-1]
DR RefSeq; XP_006498824.1; XM_006498761.3. [Q00420-3]
DR PDB; 1AWC; X-ray; 2.15 A; B=5-157.
DR PDBsum; 1AWC; -.
DR AlphaFoldDB; Q00420; -.
DR SMR; Q00420; -.
DR DIP; DIP-321N; -.
DR MINT; Q00420; -.
DR STRING; 10090.ENSMUSP00000106055; -.
DR iPTMnet; Q00420; -.
DR PhosphoSitePlus; Q00420; -.
DR EPD; Q00420; -.
DR MaxQB; Q00420; -.
DR PaxDb; Q00420; -.
DR PeptideAtlas; Q00420; -.
DR PRIDE; Q00420; -.
DR ProteomicsDB; 273405; -. [Q00420-1]
DR ProteomicsDB; 273406; -. [Q00420-2]
DR ProteomicsDB; 273407; -. [Q00420-3]
DR ProteomicsDB; 273408; -. [Q00420-4]
DR Antibodypedia; 1425; 340 antibodies from 34 providers.
DR DNASU; 14391; -.
DR Ensembl; ENSMUST00000089745; ENSMUSP00000087177; ENSMUSG00000027361. [Q00420-4]
DR Ensembl; ENSMUST00000103226; ENSMUSP00000099516; ENSMUSG00000027361. [Q00420-2]
DR Ensembl; ENSMUST00000103227; ENSMUSP00000099517; ENSMUSG00000027361. [Q00420-3]
DR Ensembl; ENSMUST00000110424; ENSMUSP00000106054; ENSMUSG00000027361. [Q00420-3]
DR Ensembl; ENSMUST00000110425; ENSMUSP00000106055; ENSMUSG00000027361. [Q00420-1]
DR GeneID; 14391; -.
DR KEGG; mmu:14391; -.
DR UCSC; uc008mdv.2; mouse. [Q00420-1]
DR UCSC; uc008mdx.2; mouse. [Q00420-2]
DR UCSC; uc008mdz.2; mouse. [Q00420-4]
DR CTD; 2553; -.
DR MGI; MGI:95611; Gabpb1.
DR VEuPathDB; HostDB:ENSMUSG00000027361; -.
DR eggNOG; ENOG502QRTX; Eukaryota.
DR GeneTree; ENSGT00940000157875; -.
DR HOGENOM; CLU_000134_12_0_1; -.
DR InParanoid; Q00420; -.
DR OMA; ACRQKLE; -.
DR OrthoDB; 1514706at2759; -.
DR PhylomeDB; Q00420; -.
DR TreeFam; TF326036; -.
DR Reactome; R-MMU-2151201; Transcriptional activation of mitochondrial biogenesis.
DR BioGRID-ORCS; 14391; 15 hits in 77 CRISPR screens.
DR ChiTaRS; Gabpb1; mouse.
DR EvolutionaryTrace; Q00420; -.
DR PRO; PR:Q00420; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q00420; protein.
DR Bgee; ENSMUSG00000027361; Expressed in embryonic post-anal tail and 251 other tissues.
DR ExpressionAtlas; Q00420; baseline and differential.
DR Genevisible; Q00420; MM.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO: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 3D-structure; Acetylation; Alternative splicing; ANK repeat; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q06547"
FT CHAIN 2..383
FT /note="GA-binding protein subunit beta-1"
FT /id="PRO_0000066994"
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 MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q06547"
FT MOD_RES 69
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:25200183"
FT MOD_RES 340
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:25200183"
FT MOD_RES 369
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:25200183"
FT VAR_SEQ 233
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1876836"
FT /id="VSP_009333"
FT VAR_SEQ 233
FT /note="V -> G (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009334"
FT VAR_SEQ 234..383
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009335"
FT VAR_SEQ 334..383
FT /note="EREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMTRIQTNKEAV
FT -> VRSLIPGVFCCSHPK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1876836"
FT /id="VSP_009336"
FT MUTAGEN 69
FT /note="K->R: Decreased acetylation; when associated with R-
FT 340 and Lys-369."
FT /evidence="ECO:0000269|PubMed:25200183"
FT MUTAGEN 340
FT /note="K->R: Decreased acetylation; when associated with R-
FT 69 and Lys-369."
FT /evidence="ECO:0000269|PubMed:25200183"
FT MUTAGEN 369
FT /note="K->R: Decreased acetylation; when associated with R-
FT 69 and Lys-340."
FT /evidence="ECO:0000269|PubMed:25200183"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:1AWC"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:1AWC"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:1AWC"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:1AWC"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1AWC"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:1AWC"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:1AWC"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1AWC"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:1AWC"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:1AWC"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:1AWC"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:1AWC"
SQ SEQUENCE 383 AA; 41358 MW; E3BCE5A05B1AF5A9 CRC64;
MSLVDLGKKL LEAARAGQDD EVRILMANGA PFTTDWLGTS PLHLAAQYGH FSTTEVLLRA
GVSRDARTKV DRTPLHMAAS EGHANIVEVL LKHGADVNAK DMLKMTALHW ATEHNHQEVV
ELLIKYGADV HTQSKFCKTA FDISIDNGNE DLAEILQIAM QNQINTNPES PDTVTIHAAT
PQFIIGPGGV VNLTDETGVS AVQFGNSSTS VLATLAALAE ASAPLSNSSE TPVVATEEVV
TAESVDGAIQ QVVSSGGQQV ITIVTDGIQL GNLHSIPTSG MGQPIIVTMP DGQQVLTVPA
TDIAEETVIS EEPPAKRQCM EIIESRVECA EIEEREALQK QLDEANREAQ KYRQQLLKKE
QEAEAYRQKL EAMTRIQTNK EAV
