ABT1_HUMAN
ID ABT1_HUMAN Reviewed; 272 AA.
AC Q9ULW3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Activator of basal transcription 1;
DE Short=hABT1;
DE AltName: Full=Basal transcriptional activator;
GN Name=ABT1;
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].
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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Duodenum, and Testis;
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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [5]
RP INTERACTION WITH IGHMBP2.
RX PubMed=19299493; DOI=10.1093/hmg/ddp134;
RA de Planell-Saguer M., Schroeder D.G., Rodicio M.C., Cox G.A.,
RA Mourelatos Z.;
RT "Biochemical and genetic evidence for a role of IGHMBP2 in the
RT translational machinery.";
RL Hum. Mol. Genet. 18:2115-2126(2009).
RN [6]
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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ESF1/ABTAP (By similarity). Interacts with
CC IGHMBP2. {ECO:0000250, ECO:0000269|PubMed:19299493}.
CC -!- INTERACTION:
CC Q9ULW3; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-2602396, EBI-10171416;
CC Q9ULW3; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-2602396, EBI-5278764;
CC Q9ULW3; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-2602396, EBI-739624;
CC Q9ULW3; Q92997: DVL3; NbExp=5; IntAct=EBI-2602396, EBI-739789;
CC Q9ULW3; P50402: EMD; NbExp=6; IntAct=EBI-2602396, EBI-489887;
CC Q9ULW3; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-2602396, EBI-10175124;
CC Q9ULW3; P42858: HTT; NbExp=9; IntAct=EBI-2602396, EBI-466029;
CC Q9ULW3; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-2602396, EBI-2556193;
CC Q9ULW3; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-2602396, EBI-741037;
CC Q9ULW3; Q8N8X9: MAB21L3; NbExp=3; IntAct=EBI-2602396, EBI-10268010;
CC Q9ULW3; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2602396, EBI-79165;
CC Q9ULW3; Q2KHN1: RNF151; NbExp=3; IntAct=EBI-2602396, EBI-12002474;
CC Q9ULW3; Q8N205: SYNE4; NbExp=3; IntAct=EBI-2602396, EBI-7131783;
CC Q9ULW3; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-2602396, EBI-947459;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ESF2/ABP1 family. {ECO:0000305}.
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DR EMBL; AB027258; BAA86886.1; -; mRNA.
DR EMBL; AL513548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048812; AAH48812.1; -; mRNA.
DR EMBL; BC066313; AAH66313.1; -; mRNA.
DR CCDS; CCDS4616.1; -.
DR RefSeq; NP_037507.1; NM_013375.3.
DR AlphaFoldDB; Q9ULW3; -.
DR BioGRID; 118909; 406.
DR IntAct; Q9ULW3; 38.
DR STRING; 9606.ENSP00000274849; -.
DR iPTMnet; Q9ULW3; -.
DR PhosphoSitePlus; Q9ULW3; -.
DR BioMuta; ABT1; -.
DR DMDM; 74753396; -.
DR EPD; Q9ULW3; -.
DR jPOST; Q9ULW3; -.
DR MassIVE; Q9ULW3; -.
DR MaxQB; Q9ULW3; -.
DR PaxDb; Q9ULW3; -.
DR PeptideAtlas; Q9ULW3; -.
DR PRIDE; Q9ULW3; -.
DR ProteomicsDB; 85141; -.
DR Antibodypedia; 11097; 194 antibodies from 28 providers.
DR DNASU; 29777; -.
DR Ensembl; ENST00000274849.3; ENSP00000274849.1; ENSG00000146109.5.
DR GeneID; 29777; -.
DR KEGG; hsa:29777; -.
DR MANE-Select; ENST00000274849.3; ENSP00000274849.1; NM_013375.4; NP_037507.1.
DR UCSC; uc003nii.4; human.
DR CTD; 29777; -.
DR DisGeNET; 29777; -.
DR GeneCards; ABT1; -.
DR HGNC; HGNC:17369; ABT1.
DR HPA; ENSG00000146109; Low tissue specificity.
DR MIM; 618750; gene.
DR neXtProt; NX_Q9ULW3; -.
DR OpenTargets; ENSG00000146109; -.
DR PharmGKB; PA38451; -.
DR VEuPathDB; HostDB:ENSG00000146109; -.
DR eggNOG; KOG3152; Eukaryota.
DR GeneTree; ENSGT00390000002062; -.
DR HOGENOM; CLU_054086_3_1_1; -.
DR InParanoid; Q9ULW3; -.
DR OMA; TRPNSSW; -.
DR OrthoDB; 1377351at2759; -.
DR PhylomeDB; Q9ULW3; -.
DR TreeFam; TF314506; -.
DR PathwayCommons; Q9ULW3; -.
DR SignaLink; Q9ULW3; -.
DR BioGRID-ORCS; 29777; 508 hits in 1078 CRISPR screens.
DR ChiTaRS; ABT1; human.
DR GenomeRNAi; 29777; -.
DR Pharos; Q9ULW3; Tbio.
DR PRO; PR:Q9ULW3; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9ULW3; protein.
DR Bgee; ENSG00000146109; Expressed in granulocyte and 168 other tissues.
DR ExpressionAtlas; Q9ULW3; baseline and differential.
DR Genevisible; Q9ULW3; HS.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
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; IEA:Ensembl.
DR GO; GO:0034462; P:small-subunit processome assembly; IBA:GO_Central.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
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 1: Evidence at protein level;
KW Acetylation; Coiled coil; DNA-binding; Nucleus; Reference proteome;
KW RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..272
FT /note="Activator of basal transcription 1"
FT /id="PRO_0000233168"
FT DOMAIN 46..142
FT /note="RRM"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 161..191
FT /evidence="ECO:0000255"
FT COMPBIAS 19..33
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
SQ SEQUENCE 272 AA; 31079 MW; FB9B44192C16BD8A CRC64;
MEAEESEKAA TEQEPLEGTE QTLDAEEEQE ESEEAACGSK KRVVPGIVYL GHIPPRFRPL
HVRNLLSAYG EVGRVFFQAE DRFVRRKKKA AAAAGGKKRS YTKDYTEGWV EFRDKRIAKR
VAASLHNTPM GARRRSPFRY DLWNLKYLHR FTWSHLSEHL AFERQVRRQR LRAEVAQAKR
ETDFYLQSVE RGQRFLAADG DPARPDGSWT FAQRPTEQEL RARKAARPGG RERARLATAQ
DKARSNKGLL ARIFGAPPPS ESMEGPSLVR DS
