ABT1_MOUSE
ID ABT1_MOUSE Reviewed; 269 AA.
AC Q9QYL7; Q0VGU7; Q9D762;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Activator of basal transcription 1;
GN Name=Abt1;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Fibroblast;
RX PubMed=10648625; DOI=10.1128/mcb.20.4.1407-1418.2000;
RA Oda T., Kayukawa K., Hagiwara H., Yudate H.T., Masuho Y., Murakami Y.,
RA Tamura T.-A., Muramatsu M.-A.;
RT "A novel TATA-binding protein-binding protein, ABT1, activates basal
RT transcription and has a yeast homolog that is essential for growth.";
RL Mol. Cell. Biol. 20:1407-1418(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Tongue;
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].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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).
CC -!- FUNCTION: Could be a novel TATA-binding protein (TBP) which can
CC function as a basal transcription activator. Can act as a regulator of
CC basal transcription for class II genes.
CC -!- SUBUNIT: Interacts with ESF1/ABTAP. Interacts with IGHMBP2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10648625}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:10648625}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10648625}.
CC -!- SIMILARITY: Belongs to the ESF2/ABP1 family. {ECO:0000305}.
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DR EMBL; AB021860; BAA87912.1; -; mRNA.
DR EMBL; AK009557; BAB26356.1; -; mRNA.
DR EMBL; AK029222; BAC26353.1; -; mRNA.
DR EMBL; AL714025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC082609; AAH82609.1; -; mRNA.
DR CCDS; CCDS26338.1; -.
DR RefSeq; NP_038952.1; NM_013924.3.
DR AlphaFoldDB; Q9QYL7; -.
DR BioGRID; 206023; 47.
DR STRING; 10090.ENSMUSP00000045888; -.
DR iPTMnet; Q9QYL7; -.
DR PhosphoSitePlus; Q9QYL7; -.
DR EPD; Q9QYL7; -.
DR MaxQB; Q9QYL7; -.
DR PaxDb; Q9QYL7; -.
DR PeptideAtlas; Q9QYL7; -.
DR PRIDE; Q9QYL7; -.
DR ProteomicsDB; 285968; -.
DR Antibodypedia; 11097; 194 antibodies from 28 providers.
DR DNASU; 30946; -.
DR Ensembl; ENSMUST00000041782; ENSMUSP00000045888; ENSMUSG00000036376.
DR GeneID; 30946; -.
DR KEGG; mmu:30946; -.
DR UCSC; uc007pto.1; mouse.
DR CTD; 29777; -.
DR MGI; MGI:1353636; Abt1.
DR VEuPathDB; HostDB:ENSMUSG00000036376; -.
DR eggNOG; KOG3152; Eukaryota.
DR GeneTree; ENSGT00390000002062; -.
DR HOGENOM; CLU_054086_3_1_1; -.
DR InParanoid; Q9QYL7; -.
DR OMA; TRPNSSW; -.
DR OrthoDB; 1377351at2759; -.
DR PhylomeDB; Q9QYL7; -.
DR TreeFam; TF314506; -.
DR BioGRID-ORCS; 30946; 28 hits in 73 CRISPR screens.
DR ChiTaRS; Abt1; mouse.
DR PRO; PR:Q9QYL7; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9QYL7; protein.
DR Bgee; ENSMUSG00000036376; Expressed in cleaving embryo and 270 other tissues.
DR Genevisible; Q9QYL7; MM.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0034462; P:small-subunit processome assembly; IBA:GO_Central.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IGI:MGI.
DR CDD; cd12263; RRM_ABT1_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR039119; ABT1/Esf2.
DR InterPro; IPR034353; ABT1/ESF2_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR PANTHER; PTHR12311; PTHR12311; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; DNA-binding; Nucleus; Reference proteome; RNA-binding;
KW Transcription; Transcription regulation.
FT CHAIN 1..269
FT /note="Activator of basal transcription 1"
FT /id="PRO_0000233169"
FT DOMAIN 48..145
FT /note="RRM"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..29
FT /evidence="ECO:0000255"
FT COILED 164..194
FT /evidence="ECO:0000255"
FT COMPBIAS 220..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 73
FT /note="E -> R (in Ref. 2; BAB26356)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="G -> D (in Ref. 2; BAB26356)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 30659 MW; 1C52B1E55C0B0DD8 CRC64;
MVKAGELVEQ QKAAMEEEAN AEAAEDQEEP EDTACSSSSK KKKKVVPGIV YLGHVPPRFR
PLHVRNLLSA YGEVGRVFFQ AEDHFVKRKK KAAAAAGGKK GAKYSKDYTE GWVEFRDKRV
AKRVAASLHN TPMGARKRSP FRYDLWNLKY LHRFTWSHLS EHLAFERQVR RQRLRAEVAQ
AKRETDFYLR NVEQGQHFLA ADGDATRPNS SWTFTQRPTE QEFRARKAAR PGGRERARLA
NVEDQARSNR GLLAKIFGAP LPAESKEKP
